data_7HCD
# 
_entry.id   7HCD 
# 
_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   7HCD         pdb_00007hcd 10.2210/pdb7hcd/pdb 
WWPDB D_1001407295 ?            ?                   
# 
_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                        7HCD 
_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 '(3R,6S)-6-methyl-1-(3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-carbonyl)piperidine-3-carboxylic acid' 318.325   1   
?                      ? ? ?                                                                                    
3 water       nat water                                                                                              18.015    437 
?                      ? ? ?                                                                                    
# 
_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 '(3R,6S)-6-methyl-1-(3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-carbonyl)piperidine-3-carboxylic acid' A1A42 
3 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 
A1A42 non-polymer         . '(3R,6S)-6-methyl-1-(3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-carbonyl)piperidine-3-carboxylic acid' ? 
'C16 H18 N2 O5'  318.325 
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 
CYS   'L-peptide linking' y CYSTEINE                                                                                           ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                          ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                    ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                            ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                          ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                              ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                         ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                            ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                             ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                         ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                      ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                            ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                             ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                          ? 
'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                                                           ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                             ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1A42 1   201 201  A1A42 LA1 A . 
D 3 HOH   1   301 625  HOH   HOH A . 
D 3 HOH   2   302 74   HOH   HOH A . 
D 3 HOH   3   303 196  HOH   HOH A . 
D 3 HOH   4   304 93   HOH   HOH A . 
D 3 HOH   5   305 292  HOH   HOH A . 
D 3 HOH   6   306 105  HOH   HOH A . 
D 3 HOH   7   307 661  HOH   HOH A . 
D 3 HOH   8   308 78   HOH   HOH A . 
D 3 HOH   9   309 493  HOH   HOH A . 
D 3 HOH   10  310 153  HOH   HOH A . 
D 3 HOH   11  311 18   HOH   HOH A . 
D 3 HOH   12  312 192  HOH   HOH A . 
D 3 HOH   13  313 209  HOH   HOH A . 
D 3 HOH   14  314 109  HOH   HOH A . 
D 3 HOH   15  315 393  HOH   HOH A . 
D 3 HOH   16  316 76   HOH   HOH A . 
D 3 HOH   17  317 1309 HOH   HOH A . 
D 3 HOH   18  318 1301 HOH   HOH A . 
D 3 HOH   19  319 1283 HOH   HOH A . 
D 3 HOH   20  320 136  HOH   HOH A . 
D 3 HOH   21  321 964  HOH   HOH A . 
D 3 HOH   22  322 1295 HOH   HOH A . 
D 3 HOH   23  323 337  HOH   HOH A . 
D 3 HOH   24  324 39   HOH   HOH A . 
D 3 HOH   25  325 236  HOH   HOH A . 
D 3 HOH   26  326 247  HOH   HOH A . 
D 3 HOH   27  327 29   HOH   HOH A . 
D 3 HOH   28  328 229  HOH   HOH A . 
D 3 HOH   29  329 1289 HOH   HOH A . 
D 3 HOH   30  330 151  HOH   HOH A . 
D 3 HOH   31  331 124  HOH   HOH A . 
D 3 HOH   32  332 15   HOH   HOH A . 
D 3 HOH   33  333 1300 HOH   HOH A . 
D 3 HOH   34  334 140  HOH   HOH A . 
D 3 HOH   35  335 469  HOH   HOH A . 
D 3 HOH   36  336 225  HOH   HOH A . 
D 3 HOH   37  337 1308 HOH   HOH A . 
D 3 HOH   38  338 24   HOH   HOH A . 
D 3 HOH   39  339 409  HOH   HOH A . 
D 3 HOH   40  340 164  HOH   HOH A . 
D 3 HOH   41  341 57   HOH   HOH A . 
D 3 HOH   42  342 20   HOH   HOH A . 
D 3 HOH   43  343 3    HOH   HOH A . 
D 3 HOH   44  344 155  HOH   HOH A . 
D 3 HOH   45  345 381  HOH   HOH A . 
D 3 HOH   46  346 1290 HOH   HOH A . 
D 3 HOH   47  347 12   HOH   HOH A . 
D 3 HOH   48  348 662  HOH   HOH A . 
D 3 HOH   49  349 630  HOH   HOH A . 
D 3 HOH   50  350 241  HOH   HOH A . 
D 3 HOH   51  351 139  HOH   HOH A . 
D 3 HOH   52  352 42   HOH   HOH A . 
D 3 HOH   53  353 23   HOH   HOH A . 
D 3 HOH   54  354 195  HOH   HOH A . 
D 3 HOH   55  355 92   HOH   HOH A . 
D 3 HOH   56  356 320  HOH   HOH A . 
D 3 HOH   57  357 102  HOH   HOH A . 
D 3 HOH   58  358 21   HOH   HOH A . 
D 3 HOH   59  359 303  HOH   HOH A . 
D 3 HOH   60  360 2    HOH   HOH A . 
D 3 HOH   61  361 165  HOH   HOH A . 
D 3 HOH   62  362 939  HOH   HOH A . 
D 3 HOH   63  363 33   HOH   HOH A . 
D 3 HOH   64  364 396  HOH   HOH A . 
D 3 HOH   65  365 66   HOH   HOH A . 
D 3 HOH   66  366 36   HOH   HOH A . 
D 3 HOH   67  367 19   HOH   HOH A . 
D 3 HOH   68  368 296  HOH   HOH A . 
D 3 HOH   69  369 354  HOH   HOH A . 
D 3 HOH   70  370 148  HOH   HOH A . 
D 3 HOH   71  371 56   HOH   HOH A . 
D 3 HOH   72  372 162  HOH   HOH A . 
D 3 HOH   73  373 81   HOH   HOH A . 
D 3 HOH   74  374 5    HOH   HOH A . 
D 3 HOH   75  375 49   HOH   HOH A . 
D 3 HOH   76  376 138  HOH   HOH A . 
D 3 HOH   77  377 1    HOH   HOH A . 
D 3 HOH   78  378 45   HOH   HOH A . 
D 3 HOH   79  379 46   HOH   HOH A . 
D 3 HOH   80  380 24   HOH   HOH A . 
D 3 HOH   81  381 169  HOH   HOH A . 
D 3 HOH   82  382 218  HOH   HOH A . 
D 3 HOH   83  383 159  HOH   HOH A . 
D 3 HOH   84  384 17   HOH   HOH A . 
D 3 HOH   85  385 86   HOH   HOH A . 
D 3 HOH   86  386 134  HOH   HOH A . 
D 3 HOH   87  387 26   HOH   HOH A . 
D 3 HOH   88  388 27   HOH   HOH A . 
D 3 HOH   89  389 16   HOH   HOH A . 
D 3 HOH   90  390 62   HOH   HOH A . 
D 3 HOH   91  391 405  HOH   HOH A . 
D 3 HOH   92  392 186  HOH   HOH A . 
D 3 HOH   93  393 85   HOH   HOH A . 
D 3 HOH   94  394 35   HOH   HOH A . 
D 3 HOH   95  395 154  HOH   HOH A . 
D 3 HOH   96  396 13   HOH   HOH A . 
D 3 HOH   97  397 26   HOH   HOH A . 
D 3 HOH   98  398 461  HOH   HOH A . 
D 3 HOH   99  399 96   HOH   HOH A . 
D 3 HOH   100 400 30   HOH   HOH A . 
D 3 HOH   101 401 4    HOH   HOH A . 
D 3 HOH   102 402 1315 HOH   HOH A . 
D 3 HOH   103 403 366  HOH   HOH A . 
D 3 HOH   104 404 116  HOH   HOH A . 
D 3 HOH   105 405 58   HOH   HOH A . 
D 3 HOH   106 406 83   HOH   HOH A . 
D 3 HOH   107 407 1310 HOH   HOH A . 
D 3 HOH   108 408 1275 HOH   HOH A . 
D 3 HOH   109 409 67   HOH   HOH A . 
D 3 HOH   110 410 6    HOH   HOH A . 
D 3 HOH   111 411 132  HOH   HOH A . 
D 3 HOH   112 412 281  HOH   HOH A . 
D 3 HOH   113 413 4    HOH   HOH A . 
D 3 HOH   114 414 351  HOH   HOH A . 
D 3 HOH   115 415 3    HOH   HOH A . 
D 3 HOH   116 416 1313 HOH   HOH A . 
D 3 HOH   117 417 333  HOH   HOH A . 
D 3 HOH   118 418 199  HOH   HOH A . 
D 3 HOH   119 419 397  HOH   HOH A . 
D 3 HOH   120 420 6    HOH   HOH A . 
D 3 HOH   121 421 25   HOH   HOH A . 
D 3 HOH   122 422 34   HOH   HOH A . 
D 3 HOH   123 423 121  HOH   HOH A . 
D 3 HOH   124 424 68   HOH   HOH A . 
D 3 HOH   125 425 1068 HOH   HOH A . 
D 3 HOH   126 426 5    HOH   HOH A . 
D 3 HOH   127 427 51   HOH   HOH A . 
D 3 HOH   128 428 8    HOH   HOH A . 
D 3 HOH   129 429 1279 HOH   HOH A . 
D 3 HOH   130 430 123  HOH   HOH A . 
D 3 HOH   131 431 278  HOH   HOH A . 
D 3 HOH   132 432 582  HOH   HOH A . 
D 3 HOH   133 433 125  HOH   HOH A . 
D 3 HOH   134 434 95   HOH   HOH A . 
D 3 HOH   135 435 53   HOH   HOH A . 
D 3 HOH   136 436 122  HOH   HOH A . 
D 3 HOH   137 437 7    HOH   HOH A . 
D 3 HOH   138 438 1222 HOH   HOH A . 
D 3 HOH   139 439 70   HOH   HOH A . 
D 3 HOH   140 440 156  HOH   HOH A . 
D 3 HOH   141 441 212  HOH   HOH A . 
D 3 HOH   142 442 1286 HOH   HOH A . 
D 3 HOH   143 443 952  HOH   HOH A . 
D 3 HOH   144 444 115  HOH   HOH A . 
D 3 HOH   145 445 1189 HOH   HOH A . 
D 3 HOH   146 446 73   HOH   HOH A . 
D 3 HOH   147 447 16   HOH   HOH A . 
D 3 HOH   148 448 40   HOH   HOH A . 
D 3 HOH   149 449 1296 HOH   HOH A . 
D 3 HOH   150 450 27   HOH   HOH A . 
D 3 HOH   151 451 1238 HOH   HOH A . 
D 3 HOH   152 452 71   HOH   HOH A . 
D 3 HOH   153 453 80   HOH   HOH A . 
D 3 HOH   154 454 576  HOH   HOH A . 
D 3 HOH   155 455 94   HOH   HOH A . 
D 3 HOH   156 456 944  HOH   HOH A . 
D 3 HOH   157 457 19   HOH   HOH A . 
D 3 HOH   158 458 97   HOH   HOH A . 
D 3 HOH   159 459 1094 HOH   HOH A . 
D 3 HOH   160 460 104  HOH   HOH A . 
D 3 HOH   161 461 188  HOH   HOH A . 
D 3 HOH   162 462 330  HOH   HOH A . 
D 3 HOH   163 463 28   HOH   HOH A . 
D 3 HOH   164 464 79   HOH   HOH A . 
D 3 HOH   165 465 1119 HOH   HOH A . 
D 3 HOH   166 466 1134 HOH   HOH A . 
D 3 HOH   167 467 107  HOH   HOH A . 
D 3 HOH   168 468 509  HOH   HOH A . 
D 3 HOH   169 469 8    HOH   HOH A . 
D 3 HOH   170 470 163  HOH   HOH A . 
D 3 HOH   171 471 18   HOH   HOH A . 
D 3 HOH   172 472 2    HOH   HOH A . 
D 3 HOH   173 473 726  HOH   HOH A . 
D 3 HOH   174 474 408  HOH   HOH A . 
D 3 HOH   175 475 756  HOH   HOH A . 
D 3 HOH   176 476 556  HOH   HOH A . 
D 3 HOH   177 477 280  HOH   HOH A . 
D 3 HOH   178 478 1276 HOH   HOH A . 
D 3 HOH   179 479 801  HOH   HOH A . 
D 3 HOH   180 480 7    HOH   HOH A . 
D 3 HOH   181 481 319  HOH   HOH A . 
D 3 HOH   182 482 361  HOH   HOH A . 
D 3 HOH   183 483 126  HOH   HOH A . 
D 3 HOH   184 484 63   HOH   HOH A . 
D 3 HOH   185 485 342  HOH   HOH A . 
D 3 HOH   186 486 12   HOH   HOH A . 
D 3 HOH   187 487 1307 HOH   HOH A . 
D 3 HOH   188 488 10   HOH   HOH A . 
D 3 HOH   189 489 224  HOH   HOH A . 
D 3 HOH   190 490 267  HOH   HOH A . 
D 3 HOH   191 491 250  HOH   HOH A . 
D 3 HOH   192 492 370  HOH   HOH A . 
D 3 HOH   193 493 14   HOH   HOH A . 
D 3 HOH   194 494 1306 HOH   HOH A . 
D 3 HOH   195 495 1287 HOH   HOH A . 
D 3 HOH   196 496 9    HOH   HOH A . 
D 3 HOH   197 497 202  HOH   HOH A . 
D 3 HOH   198 498 135  HOH   HOH A . 
D 3 HOH   199 499 695  HOH   HOH A . 
D 3 HOH   200 500 919  HOH   HOH A . 
D 3 HOH   201 501 674  HOH   HOH A . 
D 3 HOH   202 502 318  HOH   HOH A . 
D 3 HOH   203 503 1314 HOH   HOH A . 
D 3 HOH   204 504 521  HOH   HOH A . 
D 3 HOH   205 505 17   HOH   HOH A . 
D 3 HOH   206 506 309  HOH   HOH A . 
D 3 HOH   207 507 11   HOH   HOH A . 
D 3 HOH   208 508 1299 HOH   HOH A . 
D 3 HOH   209 509 315  HOH   HOH A . 
D 3 HOH   210 510 711  HOH   HOH A . 
D 3 HOH   211 511 263  HOH   HOH A . 
D 3 HOH   212 512 331  HOH   HOH A . 
D 3 HOH   213 513 805  HOH   HOH A . 
D 3 HOH   214 514 152  HOH   HOH A . 
D 3 HOH   215 515 941  HOH   HOH A . 
D 3 HOH   216 516 22   HOH   HOH A . 
D 3 HOH   217 517 1284 HOH   HOH A . 
D 3 HOH   218 518 208  HOH   HOH A . 
D 3 HOH   219 519 1071 HOH   HOH A . 
D 3 HOH   220 520 180  HOH   HOH A . 
D 3 HOH   221 521 350  HOH   HOH A . 
D 3 HOH   222 522 356  HOH   HOH A . 
D 3 HOH   223 523 363  HOH   HOH A . 
D 3 HOH   224 524 326  HOH   HOH A . 
D 3 HOH   225 525 371  HOH   HOH A . 
D 3 HOH   226 526 313  HOH   HOH A . 
D 3 HOH   227 527 25   HOH   HOH A . 
D 3 HOH   228 528 21   HOH   HOH A . 
D 3 HOH   229 529 429  HOH   HOH A . 
D 3 HOH   230 530 185  HOH   HOH A . 
D 3 HOH   231 531 15   HOH   HOH A . 
D 3 HOH   232 532 376  HOH   HOH A . 
D 3 HOH   233 533 772  HOH   HOH A . 
D 3 HOH   234 534 1074 HOH   HOH A . 
D 3 HOH   235 535 346  HOH   HOH A . 
D 3 HOH   236 536 1292 HOH   HOH A . 
D 3 HOH   237 537 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 654  HOH   HOH B . 
E 3 HOH   3   203 358  HOH   HOH B . 
E 3 HOH   4   204 900  HOH   HOH B . 
E 3 HOH   5   205 549  HOH   HOH B . 
E 3 HOH   6   206 758  HOH   HOH B . 
E 3 HOH   7   207 398  HOH   HOH B . 
E 3 HOH   8   208 1249 HOH   HOH B . 
E 3 HOH   9   209 264  HOH   HOH B . 
E 3 HOH   10  210 364  HOH   HOH B . 
E 3 HOH   11  211 240  HOH   HOH B . 
E 3 HOH   12  212 353  HOH   HOH B . 
E 3 HOH   13  213 743  HOH   HOH B . 
E 3 HOH   14  214 531  HOH   HOH B . 
E 3 HOH   15  215 343  HOH   HOH B . 
E 3 HOH   16  216 282  HOH   HOH B . 
E 3 HOH   17  217 50   HOH   HOH B . 
E 3 HOH   18  218 1278 HOH   HOH B . 
E 3 HOH   19  219 120  HOH   HOH B . 
E 3 HOH   20  220 232  HOH   HOH B . 
E 3 HOH   21  221 444  HOH   HOH B . 
E 3 HOH   22  222 452  HOH   HOH B . 
E 3 HOH   23  223 332  HOH   HOH B . 
E 3 HOH   24  224 272  HOH   HOH B . 
E 3 HOH   25  225 723  HOH   HOH B . 
E 3 HOH   26  226 75   HOH   HOH B . 
E 3 HOH   27  227 131  HOH   HOH B . 
E 3 HOH   28  228 276  HOH   HOH B . 
E 3 HOH   29  229 82   HOH   HOH B . 
E 3 HOH   30  230 205  HOH   HOH B . 
E 3 HOH   31  231 1140 HOH   HOH B . 
E 3 HOH   32  232 54   HOH   HOH B . 
E 3 HOH   33  233 69   HOH   HOH B . 
E 3 HOH   34  234 133  HOH   HOH B . 
E 3 HOH   35  235 166  HOH   HOH B . 
E 3 HOH   36  236 128  HOH   HOH B . 
E 3 HOH   37  237 110  HOH   HOH B . 
E 3 HOH   38  238 1    HOH   HOH B . 
E 3 HOH   39  239 127  HOH   HOH B . 
E 3 HOH   40  240 9    HOH   HOH B . 
E 3 HOH   41  241 325  HOH   HOH B . 
E 3 HOH   42  242 231  HOH   HOH B . 
E 3 HOH   43  243 300  HOH   HOH B . 
E 3 HOH   44  244 14   HOH   HOH B . 
E 3 HOH   45  245 181  HOH   HOH B . 
E 3 HOH   46  246 60   HOH   HOH B . 
E 3 HOH   47  247 129  HOH   HOH B . 
E 3 HOH   48  248 302  HOH   HOH B . 
E 3 HOH   49  249 30   HOH   HOH B . 
E 3 HOH   50  250 1312 HOH   HOH B . 
E 3 HOH   51  251 172  HOH   HOH B . 
E 3 HOH   52  252 144  HOH   HOH B . 
E 3 HOH   53  253 391  HOH   HOH B . 
E 3 HOH   54  254 10   HOH   HOH B . 
E 3 HOH   55  255 31   HOH   HOH B . 
E 3 HOH   56  256 52   HOH   HOH B . 
E 3 HOH   57  257 347  HOH   HOH B . 
E 3 HOH   58  258 143  HOH   HOH B . 
E 3 HOH   59  259 61   HOH   HOH B . 
E 3 HOH   60  260 47   HOH   HOH B . 
E 3 HOH   61  261 72   HOH   HOH B . 
E 3 HOH   62  262 11   HOH   HOH B . 
E 3 HOH   63  263 103  HOH   HOH B . 
E 3 HOH   64  264 252  HOH   HOH B . 
E 3 HOH   65  265 41   HOH   HOH B . 
E 3 HOH   66  266 1277 HOH   HOH B . 
E 3 HOH   67  267 77   HOH   HOH B . 
E 3 HOH   68  268 59   HOH   HOH B . 
E 3 HOH   69  269 243  HOH   HOH B . 
E 3 HOH   70  270 20   HOH   HOH B . 
E 3 HOH   71  271 150  HOH   HOH B . 
E 3 HOH   72  272 43   HOH   HOH B . 
E 3 HOH   73  273 175  HOH   HOH B . 
E 3 HOH   74  274 84   HOH   HOH B . 
E 3 HOH   75  275 117  HOH   HOH B . 
E 3 HOH   76  276 242  HOH   HOH B . 
E 3 HOH   77  277 1305 HOH   HOH B . 
E 3 HOH   78  278 221  HOH   HOH B . 
E 3 HOH   79  279 220  HOH   HOH B . 
E 3 HOH   80  280 216  HOH   HOH B . 
E 3 HOH   81  281 114  HOH   HOH B . 
E 3 HOH   82  282 22   HOH   HOH B . 
E 3 HOH   83  283 106  HOH   HOH B . 
E 3 HOH   84  284 271  HOH   HOH B . 
E 3 HOH   85  285 287  HOH   HOH B . 
E 3 HOH   86  286 13   HOH   HOH B . 
E 3 HOH   87  287 147  HOH   HOH B . 
E 3 HOH   88  288 1066 HOH   HOH B . 
E 3 HOH   89  289 89   HOH   HOH B . 
E 3 HOH   90  290 235  HOH   HOH B . 
E 3 HOH   91  291 137  HOH   HOH B . 
E 3 HOH   92  292 88   HOH   HOH B . 
E 3 HOH   93  293 99   HOH   HOH B . 
E 3 HOH   94  294 387  HOH   HOH B . 
E 3 HOH   95  295 635  HOH   HOH B . 
E 3 HOH   96  296 299  HOH   HOH B . 
E 3 HOH   97  297 141  HOH   HOH B . 
E 3 HOH   98  298 112  HOH   HOH B . 
E 3 HOH   99  299 416  HOH   HOH B . 
E 3 HOH   100 300 142  HOH   HOH B . 
E 3 HOH   101 301 316  HOH   HOH B . 
E 3 HOH   102 302 48   HOH   HOH B . 
E 3 HOH   103 303 215  HOH   HOH B . 
E 3 HOH   104 304 1106 HOH   HOH B . 
E 3 HOH   105 305 311  HOH   HOH B . 
E 3 HOH   106 306 160  HOH   HOH B . 
E 3 HOH   107 307 341  HOH   HOH B . 
E 3 HOH   108 308 297  HOH   HOH B . 
E 3 HOH   109 309 37   HOH   HOH B . 
E 3 HOH   110 310 38   HOH   HOH B . 
E 3 HOH   111 311 1126 HOH   HOH B . 
E 3 HOH   112 312 101  HOH   HOH B . 
E 3 HOH   113 313 32   HOH   HOH B . 
E 3 HOH   114 314 118  HOH   HOH B . 
E 3 HOH   115 315 704  HOH   HOH B . 
E 3 HOH   116 316 161  HOH   HOH B . 
E 3 HOH   117 317 170  HOH   HOH B . 
E 3 HOH   118 318 1291 HOH   HOH B . 
E 3 HOH   119 319 91   HOH   HOH B . 
E 3 HOH   120 320 23   HOH   HOH B . 
E 3 HOH   121 321 100  HOH   HOH B . 
E 3 HOH   122 322 44   HOH   HOH B . 
E 3 HOH   123 323 1274 HOH   HOH B . 
E 3 HOH   124 324 28   HOH   HOH B . 
E 3 HOH   125 325 177  HOH   HOH B . 
E 3 HOH   126 326 197  HOH   HOH B . 
E 3 HOH   127 327 29   HOH   HOH B . 
E 3 HOH   128 328 334  HOH   HOH B . 
E 3 HOH   129 329 717  HOH   HOH B . 
E 3 HOH   130 330 98   HOH   HOH B . 
E 3 HOH   131 331 182  HOH   HOH B . 
E 3 HOH   132 332 1294 HOH   HOH B . 
E 3 HOH   133 333 1285 HOH   HOH B . 
E 3 HOH   134 334 339  HOH   HOH B . 
E 3 HOH   135 335 55   HOH   HOH B . 
E 3 HOH   136 336 65   HOH   HOH B . 
E 3 HOH   137 337 445  HOH   HOH B . 
E 3 HOH   138 338 207  HOH   HOH B . 
E 3 HOH   139 339 619  HOH   HOH B . 
E 3 HOH   140 340 234  HOH   HOH B . 
E 3 HOH   141 341 1293 HOH   HOH B . 
E 3 HOH   142 342 178  HOH   HOH B . 
E 3 HOH   143 343 362  HOH   HOH B . 
E 3 HOH   144 344 90   HOH   HOH B . 
E 3 HOH   145 345 960  HOH   HOH B . 
E 3 HOH   146 346 463  HOH   HOH B . 
E 3 HOH   147 347 623  HOH   HOH B . 
E 3 HOH   148 348 191  HOH   HOH B . 
E 3 HOH   149 349 1046 HOH   HOH B . 
E 3 HOH   150 350 335  HOH   HOH B . 
E 3 HOH   151 351 1304 HOH   HOH B . 
E 3 HOH   152 352 1280 HOH   HOH B . 
E 3 HOH   153 353 304  HOH   HOH B . 
E 3 HOH   154 354 541  HOH   HOH B . 
E 3 HOH   155 355 203  HOH   HOH B . 
E 3 HOH   156 356 290  HOH   HOH B . 
E 3 HOH   157 357 87   HOH   HOH B . 
E 3 HOH   158 358 479  HOH   HOH B . 
E 3 HOH   159 359 389  HOH   HOH B . 
E 3 HOH   160 360 1077 HOH   HOH B . 
E 3 HOH   161 361 718  HOH   HOH B . 
E 3 HOH   162 362 283  HOH   HOH B . 
E 3 HOH   163 363 1072 HOH   HOH B . 
E 3 HOH   164 364 898  HOH   HOH B . 
E 3 HOH   165 365 1316 HOH   HOH B . 
E 3 HOH   166 366 615  HOH   HOH B . 
E 3 HOH   167 367 373  HOH   HOH B . 
E 3 HOH   168 368 340  HOH   HOH B . 
E 3 HOH   169 369 190  HOH   HOH B . 
E 3 HOH   170 370 667  HOH   HOH B . 
E 3 HOH   171 371 291  HOH   HOH B . 
E 3 HOH   172 372 431  HOH   HOH B . 
E 3 HOH   173 373 1303 HOH   HOH B . 
E 3 HOH   174 374 310  HOH   HOH B . 
E 3 HOH   175 375 1173 HOH   HOH B . 
E 3 HOH   176 376 149  HOH   HOH B . 
E 3 HOH   177 377 183  HOH   HOH B . 
E 3 HOH   178 378 1163 HOH   HOH B . 
E 3 HOH   179 379 1000 HOH   HOH B . 
E 3 HOH   180 380 418  HOH   HOH B . 
E 3 HOH   181 381 1311 HOH   HOH B . 
E 3 HOH   182 382 176  HOH   HOH B . 
E 3 HOH   183 383 424  HOH   HOH B . 
E 3 HOH   184 384 1298 HOH   HOH B . 
E 3 HOH   185 385 981  HOH   HOH B . 
E 3 HOH   186 386 265  HOH   HOH B . 
E 3 HOH   187 387 248  HOH   HOH B . 
E 3 HOH   188 388 491  HOH   HOH B . 
E 3 HOH   189 389 470  HOH   HOH B . 
E 3 HOH   190 390 184  HOH   HOH B . 
E 3 HOH   191 391 360  HOH   HOH B . 
E 3 HOH   192 392 355  HOH   HOH B . 
E 3 HOH   193 393 410  HOH   HOH B . 
E 3 HOH   194 394 274  HOH   HOH B . 
E 3 HOH   195 395 566  HOH   HOH B . 
E 3 HOH   196 396 157  HOH   HOH B . 
E 3 HOH   197 397 314  HOH   HOH B . 
E 3 HOH   198 398 792  HOH   HOH B . 
E 3 HOH   199 399 321  HOH   HOH B . 
E 3 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HCD 
_cell.length_a           88.818 
_cell.length_b           88.818 
_cell.length_c           39.594 
_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                         7HCD 
_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          7HCD 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.83 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_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.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2022-06-29 
_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                     7HCD 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.410 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165310 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.300 
_reflns.pdbx_Rmerge_I_obs            0.041 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.900 
_reflns.B_iso_Wilson_estimate        11.390 
_reflns.pdbx_redundancy              6.400 
_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     1051639 
_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                      ? 
_reflns.pdbx_CC_star                 ? 
# 
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 
_reflns_shell.pdbx_CC_star 
1 1 1.000 1.020  ? 33662 7288 ? 0.959 ? ? ? 4.600 ? 1.100  ? ? ? ? ? ? 88.400 1.080 0.483 0.681 ? 
1 2 5.480 44.410 ? 7521  1098 ? 0.025 ? ? ? 6.800 ? 53.600 ? ? ? ? ? ? 99.800 0.027 0.010 0.999 ? 
# 
_refine.entry_id                                 7HCD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             39.7200 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.1700 
_refine.ls_number_reflns_obs                     165207 
_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                          0.1410 
_refine.ls_R_factor_R_work                       0.1403 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1543 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7959 
_refine.ls_number_reflns_R_work                  157248 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.2015 
_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                            0.0900 
_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                                62.060 
_refine.B_iso_min                                8.550 
_refine.pdbx_overall_phase_error                 16.3400 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        39.7200 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             437 
_refine_hist.number_atoms_total               3019 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           11.70 
_refine_hist.pdbx_B_iso_mean_solvent          29.56 
_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 
_refine_ls_shell.R_factor_obs 
1.0000 1.0100  30 85.0000  4510 . 0.3704 0.3211 . 230 0.0000 4740 . 'X-RAY DIFFRACTION' . 
1.0100 1.0200  30 94.0000  4991 . 0.2940 0.3047 . 232 0.0000 5223 . 'X-RAY DIFFRACTION' . 
1.0200 1.0400  30 100.0000 5239 . 0.2501 0.2622 . 232 0.0000 5471 . 'X-RAY DIFFRACTION' . 
1.0400 1.0500  30 100.0000 5235 . 0.2145 0.2352 . 285 0.0000 5520 . 'X-RAY DIFFRACTION' . 
1.0500 1.0600  30 100.0000 5187 . 0.1951 0.2111 . 312 0.0000 5499 . 'X-RAY DIFFRACTION' . 
1.0600 1.0800  30 100.0000 5236 . 0.1901 0.2173 . 263 0.0000 5499 . 'X-RAY DIFFRACTION' . 
1.0800 1.0900  30 100.0000 5329 . 0.1785 0.2113 . 261 0.0000 5590 . 'X-RAY DIFFRACTION' . 
1.0900 1.1100  30 100.0000 5243 . 0.1613 0.1861 . 262 0.0000 5505 . 'X-RAY DIFFRACTION' . 
1.1100 1.1300  30 100.0000 5251 . 0.1517 0.1767 . 280 0.0000 5531 . 'X-RAY DIFFRACTION' . 
1.1300 1.1400  30 100.0000 5275 . 0.1404 0.1488 . 242 0.0000 5517 . 'X-RAY DIFFRACTION' . 
1.1400 1.1600  30 100.0000 5281 . 0.1308 0.1611 . 248 0.0000 5529 . 'X-RAY DIFFRACTION' . 
1.1600 1.1900  30 100.0000 5283 . 0.1231 0.1460 . 268 0.0000 5551 . 'X-RAY DIFFRACTION' . 
1.1900 1.2100  30 100.0000 5203 . 0.1187 0.1403 . 290 0.0000 5493 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 5275 . 0.1161 0.1394 . 245 0.0000 5520 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 5263 . 0.1186 0.1318 . 266 0.0000 5529 . 'X-RAY DIFFRACTION' . 
1.2600 1.2900  30 100.0000 5273 . 0.1216 0.1392 . 271 0.0000 5544 . 'X-RAY DIFFRACTION' . 
1.2900 1.3200  30 100.0000 5269 . 0.1227 0.1427 . 281 0.0000 5550 . 'X-RAY DIFFRACTION' . 
1.3200 1.3600  30 100.0000 5233 . 0.1291 0.1451 . 279 0.0000 5512 . 'X-RAY DIFFRACTION' . 
1.3600 1.4000  30 100.0000 5293 . 0.1259 0.1575 . 251 0.0000 5544 . 'X-RAY DIFFRACTION' . 
1.4000 1.4400  30 100.0000 5249 . 0.1219 0.1530 . 262 0.0000 5511 . 'X-RAY DIFFRACTION' . 
1.4400 1.4900  30 100.0000 5320 . 0.1174 0.1208 . 255 0.0000 5575 . 'X-RAY DIFFRACTION' . 
1.4900 1.5500  30 100.0000 5258 . 0.1146 0.1169 . 277 0.0000 5535 . 'X-RAY DIFFRACTION' . 
1.5500 1.6200  30 100.0000 5271 . 0.1150 0.1312 . 262 0.0000 5533 . 'X-RAY DIFFRACTION' . 
1.6200 1.7100  30 100.0000 5338 . 0.1231 0.1405 . 267 0.0000 5605 . 'X-RAY DIFFRACTION' . 
1.7100 1.8200  30 100.0000 5264 . 0.1326 0.1495 . 255 0.0000 5519 . 'X-RAY DIFFRACTION' . 
1.8200 1.9600  30 100.0000 5272 . 0.1327 0.1298 . 282 0.0000 5554 . 'X-RAY DIFFRACTION' . 
1.9600 2.1500  30 99.0000  5281 . 0.1365 0.1413 . 278 0.0000 5559 . 'X-RAY DIFFRACTION' . 
2.1500 2.4700  30 99.0000  5303 . 0.1367 0.1455 . 295 0.0000 5598 . 'X-RAY DIFFRACTION' . 
2.4700 3.1100  30 100.0000 5338 . 0.1484 0.1611 . 259 0.0000 5597 . 'X-RAY DIFFRACTION' . 
3.1100 39.7200 30 100.0000 5485 . 0.1481 0.1695 . 269 0.0000 5754 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCD 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000303' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCD 
_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 3 ? 
# 
_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 7HCD A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCD 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 7HCD SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCD MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCD SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCD 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 
2 1 B,E   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HCD 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HD1 A HIS 91  ? ? O A HOH 301 ? ? 1.59 
2 1 O   B HOH 214 ? ? O B HOH 326 ? ? 2.19 
# 
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  ? ? 55.62 -133.42 
2 1 SER A 128 ? B 71.11 -7.30   
3 1 HIS B 86  ? ? 57.16 -128.38 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 535 ? 5.98 . 
2 1 O ? A HOH 536 ? 6.16 . 
3 1 O ? A HOH 537 ? 7.62 . 
4 1 O ? B HOH 400 ? 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 
A1A42 N2   N N N 1   
A1A42 C3   C N N 2   
A1A42 C6   C N N 3   
A1A42 C9   C Y N 4   
A1A42 C12  C Y N 5   
A1A42 C14  C N N 6   
A1A42 C1   C N N 7   
A1A42 C10  C Y N 8   
A1A42 C11  C Y N 9   
A1A42 C13  C N N 10  
A1A42 C15  C Y N 11  
A1A42 C16  C Y N 12  
A1A42 C2   C N S 13  
A1A42 C4   C N N 14  
A1A42 C5   C N R 15  
A1A42 C7   C N N 16  
A1A42 C8   C N N 17  
A1A42 N1   N N N 18  
A1A42 O1   O N N 19  
A1A42 O2   O N N 20  
A1A42 O3   O N N 21  
A1A42 O4   O N N 22  
A1A42 O5   O N N 23  
A1A42 H14  H N N 24  
A1A42 H7   H N N 25  
A1A42 H6   H N N 26  
A1A42 H16  H N N 27  
A1A42 H15  H N N 28  
A1A42 H4   H N N 29  
A1A42 H5   H N N 30  
A1A42 H3   H N N 31  
A1A42 H12  H N N 32  
A1A42 H13  H N N 33  
A1A42 H17  H N N 34  
A1A42 H1   H N N 35  
A1A42 H8   H N N 36  
A1A42 H9   H N N 37  
A1A42 H2   H N N 38  
A1A42 H11  H N N 39  
A1A42 H10  H N N 40  
A1A42 H18  H N N 41  
ALA   N    N N N 42  
ALA   CA   C N S 43  
ALA   C    C N N 44  
ALA   O    O N N 45  
ALA   CB   C N N 46  
ALA   OXT  O N N 47  
ALA   H    H N N 48  
ALA   H2   H N N 49  
ALA   HA   H N N 50  
ALA   HB1  H N N 51  
ALA   HB2  H N N 52  
ALA   HB3  H N N 53  
ALA   HXT  H N N 54  
ARG   N    N N N 55  
ARG   CA   C N S 56  
ARG   C    C N N 57  
ARG   O    O N N 58  
ARG   CB   C N N 59  
ARG   CG   C N N 60  
ARG   CD   C N N 61  
ARG   NE   N N N 62  
ARG   CZ   C N N 63  
ARG   NH1  N N N 64  
ARG   NH2  N N N 65  
ARG   OXT  O N N 66  
ARG   H    H N N 67  
ARG   H2   H N N 68  
ARG   HA   H N N 69  
ARG   HB2  H N N 70  
ARG   HB3  H N N 71  
ARG   HG2  H N N 72  
ARG   HG3  H N N 73  
ARG   HD2  H N N 74  
ARG   HD3  H N N 75  
ARG   HE   H N N 76  
ARG   HH11 H N N 77  
ARG   HH12 H N N 78  
ARG   HH21 H N N 79  
ARG   HH22 H N N 80  
ARG   HXT  H N N 81  
ASN   N    N N N 82  
ASN   CA   C N S 83  
ASN   C    C N N 84  
ASN   O    O N N 85  
ASN   CB   C N N 86  
ASN   CG   C N N 87  
ASN   OD1  O N N 88  
ASN   ND2  N N N 89  
ASN   OXT  O N N 90  
ASN   H    H N N 91  
ASN   H2   H N N 92  
ASN   HA   H N N 93  
ASN   HB2  H N N 94  
ASN   HB3  H N N 95  
ASN   HD21 H N N 96  
ASN   HD22 H N N 97  
ASN   HXT  H N N 98  
ASP   N    N N N 99  
ASP   CA   C N S 100 
ASP   C    C N N 101 
ASP   O    O N N 102 
ASP   CB   C N N 103 
ASP   CG   C N N 104 
ASP   OD1  O N N 105 
ASP   OD2  O N N 106 
ASP   OXT  O N N 107 
ASP   H    H N N 108 
ASP   H2   H N N 109 
ASP   HA   H N N 110 
ASP   HB2  H N N 111 
ASP   HB3  H N N 112 
ASP   HD2  H N N 113 
ASP   HXT  H N N 114 
CYS   N    N N N 115 
CYS   CA   C N R 116 
CYS   C    C N N 117 
CYS   O    O N N 118 
CYS   CB   C N N 119 
CYS   SG   S N N 120 
CYS   OXT  O N N 121 
CYS   H    H N N 122 
CYS   H2   H N N 123 
CYS   HA   H N N 124 
CYS   HB2  H N N 125 
CYS   HB3  H N N 126 
CYS   HG   H N N 127 
CYS   HXT  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 
THR   N    N N N 345 
THR   CA   C N S 346 
THR   C    C N N 347 
THR   O    O N N 348 
THR   CB   C N R 349 
THR   OG1  O N N 350 
THR   CG2  C N N 351 
THR   OXT  O N N 352 
THR   H    H N N 353 
THR   H2   H N N 354 
THR   HA   H N N 355 
THR   HB   H N N 356 
THR   HG1  H N N 357 
THR   HG21 H N N 358 
THR   HG22 H N N 359 
THR   HG23 H N N 360 
THR   HXT  H N N 361 
TYR   N    N N N 362 
TYR   CA   C N S 363 
TYR   C    C N N 364 
TYR   O    O N N 365 
TYR   CB   C N N 366 
TYR   CG   C Y N 367 
TYR   CD1  C Y N 368 
TYR   CD2  C Y N 369 
TYR   CE1  C Y N 370 
TYR   CE2  C Y N 371 
TYR   CZ   C Y N 372 
TYR   OH   O N N 373 
TYR   OXT  O N N 374 
TYR   H    H N N 375 
TYR   H2   H N N 376 
TYR   HA   H N N 377 
TYR   HB2  H N N 378 
TYR   HB3  H N N 379 
TYR   HD1  H N N 380 
TYR   HD2  H N N 381 
TYR   HE1  H N N 382 
TYR   HE2  H N N 383 
TYR   HH   H N N 384 
TYR   HXT  H N N 385 
VAL   N    N N N 386 
VAL   CA   C N S 387 
VAL   C    C N N 388 
VAL   O    O N N 389 
VAL   CB   C N N 390 
VAL   CG1  C N N 391 
VAL   CG2  C N N 392 
VAL   OXT  O N N 393 
VAL   H    H N N 394 
VAL   H2   H N N 395 
VAL   HA   H N N 396 
VAL   HB   H N N 397 
VAL   HG11 H N N 398 
VAL   HG12 H N N 399 
VAL   HG13 H N N 400 
VAL   HG21 H N N 401 
VAL   HG22 H N N 402 
VAL   HG23 H N N 403 
VAL   HXT  H N N 404 
# 
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 
A1A42 C3  C2   sing N N 1   
A1A42 C3  C4   sing N N 2   
A1A42 C2  C1   sing N N 3   
A1A42 C2  N1   sing N N 4   
A1A42 C4  C5   sing N N 5   
A1A42 O2  C8   doub N N 6   
A1A42 N1  C8   sing N N 7   
A1A42 N1  C7   sing N N 8   
A1A42 C5  C7   sing N N 9   
A1A42 C5  C6   sing N N 10  
A1A42 C8  C9   sing N N 11  
A1A42 O5  C6   doub N N 12  
A1A42 C6  O1   sing N N 13  
A1A42 C16 C9   doub Y N 14  
A1A42 C16 C15  sing Y N 15  
A1A42 C9  C10  sing Y N 16  
A1A42 O4  C15  sing N N 17  
A1A42 O4  C14  sing N N 18  
A1A42 C15 C12  doub Y N 19  
A1A42 C10 C11  doub Y N 20  
A1A42 C14 C13  sing N N 21  
A1A42 C12 C11  sing Y N 22  
A1A42 C12 N2   sing N N 23  
A1A42 C13 N2   sing N N 24  
A1A42 C13 O3   doub N N 25  
A1A42 N2  H14  sing N N 26  
A1A42 C3  H7   sing N N 27  
A1A42 C3  H6   sing N N 28  
A1A42 C14 H16  sing N N 29  
A1A42 C14 H15  sing N N 30  
A1A42 C1  H4   sing N N 31  
A1A42 C1  H5   sing N N 32  
A1A42 C1  H3   sing N N 33  
A1A42 C10 H12  sing N N 34  
A1A42 C11 H13  sing N N 35  
A1A42 C16 H17  sing N N 36  
A1A42 C2  H1   sing N N 37  
A1A42 C4  H8   sing N N 38  
A1A42 C4  H9   sing N N 39  
A1A42 C5  H2   sing N N 40  
A1A42 C7  H11  sing N N 41  
A1A42 C7  H10  sing N N 42  
A1A42 O1  H18  sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TYR   N   CA   sing N N 349 
TYR   N   H    sing N N 350 
TYR   N   H2   sing N N 351 
TYR   CA  C    sing N N 352 
TYR   CA  CB   sing N N 353 
TYR   CA  HA   sing N N 354 
TYR   C   O    doub N N 355 
TYR   C   OXT  sing N N 356 
TYR   CB  CG   sing N N 357 
TYR   CB  HB2  sing N N 358 
TYR   CB  HB3  sing N N 359 
TYR   CG  CD1  doub Y N 360 
TYR   CG  CD2  sing Y N 361 
TYR   CD1 CE1  sing Y N 362 
TYR   CD1 HD1  sing N N 363 
TYR   CD2 CE2  doub Y N 364 
TYR   CD2 HD2  sing N N 365 
TYR   CE1 CZ   doub Y N 366 
TYR   CE1 HE1  sing N N 367 
TYR   CE2 CZ   sing Y N 368 
TYR   CE2 HE2  sing N N 369 
TYR   CZ  OH   sing N N 370 
TYR   OH  HH   sing N N 371 
TYR   OXT HXT  sing N N 372 
VAL   N   CA   sing N N 373 
VAL   N   H    sing N N 374 
VAL   N   H2   sing N N 375 
VAL   CA  C    sing N N 376 
VAL   CA  CB   sing N N 377 
VAL   CA  HA   sing N N 378 
VAL   C   O    doub N N 379 
VAL   C   OXT  sing N N 380 
VAL   CB  CG1  sing N N 381 
VAL   CB  CG2  sing N N 382 
VAL   CB  HB   sing N N 383 
VAL   CG1 HG11 sing N N 384 
VAL   CG1 HG12 sing N N 385 
VAL   CG1 HG13 sing N N 386 
VAL   CG2 HG21 sing N N 387 
VAL   CG2 HG22 sing N N 388 
VAL   CG2 HG23 sing N N 389 
VAL   OXT HXT  sing N N 390 
# 
_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                    7HCD 
_atom_sites.fract_transf_matrix[1][1]   0.011259 
_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]   0.011259 
_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]   0.025256 
_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 
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   ? 19.706 -16.279 22.294  0.74 49.34 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.650 -16.277 22.314  0.26 48.15 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.739 -15.199 22.451  0.74 48.92 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.723 -15.169 22.508  0.26 47.88 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.398 -13.854 22.168  0.74 47.50 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.400 -13.848 22.171  0.26 46.94 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.496 -13.575 22.650  0.74 47.84 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.515 -13.579 22.620  0.26 47.25 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.093 -15.226 23.851  0.74 49.57 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.163 -15.152 23.943  0.26 48.34 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.086 -14.093 23.997  0.74 49.75 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.177 -14.004 24.116  0.26 48.48 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.428 -16.572 24.101  0.74 49.77 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.503 -16.482 24.270  0.26 48.48 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.029 -15.315 21.804  0.74 58.70 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.973 -15.275 21.904  0.26 57.46 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.782 -15.104 24.522  0.74 59.49 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.893 -15.017 24.567  0.26 58.01 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.563 -14.239 24.801  0.74 59.70 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.708 -14.117 24.958  0.26 58.17 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.561 -13.250 24.062  0.74 59.70 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.663 -13.165 24.120  0.26 58.17 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.502 -14.087 23.222  0.74 59.70 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.544 -14.019 23.381  0.26 58.17 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.970 -16.544 24.955  0.74 59.73 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.091 -16.423 25.146  0.26 58.18 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.792 -16.746 23.389  0.74 59.73 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.829 -16.672 23.599  0.26 58.18 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.108 -17.264 24.112  0.74 59.73 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.177 -17.179 24.268  0.26 58.18 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.721 -13.027 21.374  1.00 45.37 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.191 -11.690 21.040  1.00 41.42 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.055 -10.699 21.263  1.00 38.04 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.919 -11.080 21.562  1.00 37.82 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.753 -11.616 19.610  1.00 40.64 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.729 -11.971 18.553  1.00 39.73 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.631 -11.416 18.523  1.00 39.18 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.087 -12.902 17.675  1.00 39.49 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.968 -13.226 21.007  0.74 54.45 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.966 -13.227 21.010  0.26 54.45 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.913 -11.457 21.639  1.00 49.71 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 20.062 -10.713 19.437  1.00 48.76 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.494 -12.239 19.531  1.00 48.76 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.543 -13.139 17.052  1.00 47.38 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.864 -13.269 17.727  1.00 47.38 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.369 -9.412  21.119  1.00 34.42 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.458 -8.342  21.509  1.00 30.86 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.540 -7.878  20.384  1.00 26.35 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.777 -6.928  20.583  1.00 26.71 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.241 -7.150  22.072  1.00 31.88 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.152 -6.641  21.116  1.00 32.59 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 19.110 -9.130  20.787  1.00 41.30 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.890 -8.666  22.221  1.00 37.03 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.620 -6.445  22.319  1.00 38.26 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.739 -7.437  22.856  1.00 38.26 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.576 -5.987  21.438  1.00 39.10 ?  5   SER   A HG   1 
ATOM   57   N N    A PHE   A 1 6   ? 16.564 -8.524  19.222  0.74 23.07 ?  6   PHE   A N    1 
ATOM   58   N N    B PHE   A 1 6   ? 16.619 -8.503  19.211  0.26 24.53 ?  6   PHE   A N    1 
ATOM   59   C CA   A PHE   A 1 6   ? 15.659 -8.130  18.146  0.74 20.49 ?  6   PHE   A CA   1 
ATOM   60   C CA   B PHE   A 1 6   ? 15.688 -8.203  18.133  0.26 22.68 ?  6   PHE   A CA   1 
ATOM   61   C C    A PHE   A 1 6   ? 14.221 -8.474  18.524  0.74 20.82 ?  6   PHE   A C    1 
ATOM   62   C C    B PHE   A 1 6   ? 14.305 -8.696  18.528  0.26 22.06 ?  6   PHE   A C    1 
ATOM   63   O O    A PHE   A 1 6   ? 13.944 -9.577  19.001  0.74 21.92 ?  6   PHE   A O    1 
ATOM   64   O O    B PHE   A 1 6   ? 14.128 -9.878  18.843  0.26 22.39 ?  6   PHE   A O    1 
ATOM   65   C CB   A PHE   A 1 6   ? 16.046 -8.832  16.848  0.74 18.62 ?  6   PHE   A CB   1 
ATOM   66   C CB   B PHE   A 1 6   ? 16.132 -8.896  16.850  0.26 21.61 ?  6   PHE   A CB   1 
ATOM   67   C CG   A PHE   A 1 6   ? 17.314 -8.308  16.230  0.74 17.28 ?  6   PHE   A CG   1 
ATOM   68   C CG   B PHE   A 1 6   ? 17.370 -8.312  16.236  0.26 20.65 ?  6   PHE   A CG   1 
ATOM   69   C CD1  A PHE   A 1 6   ? 17.314 -7.122  15.516  0.74 17.08 ?  6   PHE   A CD1  1 
ATOM   70   C CD1  B PHE   A 1 6   ? 17.341 -7.061  15.644  0.26 20.29 ?  6   PHE   A CD1  1 
ATOM   71   C CD2  A PHE   A 1 6   ? 18.503 -9.006  16.356  0.74 17.85 ?  6   PHE   A CD2  1 
ATOM   72   C CD2  B PHE   A 1 6   ? 18.558 -9.024  16.231  0.26 20.46 ?  6   PHE   A CD2  1 
ATOM   73   C CE1  A PHE   A 1 6   ? 18.477 -6.638  14.943  0.74 17.17 ?  6   PHE   A CE1  1 
ATOM   74   C CE1  B PHE   A 1 6   ? 18.478 -6.524  15.072  0.26 20.16 ?  6   PHE   A CE1  1 
ATOM   75   C CE2  A PHE   A 1 6   ? 19.666 -8.531  15.784  0.74 18.07 ?  6   PHE   A CE2  1 
ATOM   76   C CE2  B PHE   A 1 6   ? 19.696 -8.493  15.658  0.26 20.34 ?  6   PHE   A CE2  1 
ATOM   77   C CZ   A PHE   A 1 6   ? 19.652 -7.345  15.074  0.74 17.54 ?  6   PHE   A CZ   1 
ATOM   78   C CZ   B PHE   A 1 6   ? 19.656 -7.242  15.077  0.26 20.19 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 17.082 -9.184  19.036  0.74 27.69 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 17.202 -9.106  19.018  0.26 29.44 ?  6   PHE   A H    1 
ATOM   81   H HA   A PHE   A 1 6   ? 15.717 -7.176  18.012  0.74 24.59 ?  6   PHE   A HA   1 
ATOM   82   H HA   B PHE   A 1 6   ? 15.653 -7.245  17.985  0.26 27.22 ?  6   PHE   A HA   1 
ATOM   83   H HB2  A PHE   A 1 6   ? 16.172 -9.778  17.028  0.74 22.35 ?  6   PHE   A HB2  1 
ATOM   84   H HB2  B PHE   A 1 6   ? 16.309 -9.830  17.046  0.26 25.93 ?  6   PHE   A HB2  1 
ATOM   85   H HB3  A PHE   A 1 6   ? 15.330 -8.715  16.205  0.74 22.35 ?  6   PHE   A HB3  1 
ATOM   86   H HB3  B PHE   A 1 6   ? 15.418 -8.828  16.198  0.26 25.93 ?  6   PHE   A HB3  1 
ATOM   87   H HD1  A PHE   A 1 6   ? 16.521 -6.645  15.423  0.74 20.50 ?  6   PHE   A HD1  1 
ATOM   88   H HD1  B PHE   A 1 6   ? 16.549 -6.575  15.639  0.26 24.34 ?  6   PHE   A HD1  1 
ATOM   89   H HD2  A PHE   A 1 6   ? 18.516 -9.805  16.833  0.74 21.42 ?  6   PHE   A HD2  1 
ATOM   90   H HD2  B PHE   A 1 6   ? 18.589 -9.867  16.622  0.26 24.56 ?  6   PHE   A HD2  1 
ATOM   91   H HE1  A PHE   A 1 6   ? 18.463 -5.839  14.465  0.74 20.60 ?  6   PHE   A HE1  1 
ATOM   92   H HE1  B PHE   A 1 6   ? 18.447 -5.680  14.680  0.26 24.19 ?  6   PHE   A HE1  1 
ATOM   93   H HE2  A PHE   A 1 6   ? 20.460 -9.005  15.879  0.74 21.68 ?  6   PHE   A HE2  1 
ATOM   94   H HE2  B PHE   A 1 6   ? 20.489 -8.979  15.664  0.26 24.41 ?  6   PHE   A HE2  1 
ATOM   95   H HZ   A PHE   A 1 6   ? 20.435 -7.017  14.692  0.74 21.05 ?  6   PHE   A HZ   1 
ATOM   96   H HZ   B PHE   A 1 6   ? 20.422 -6.882  14.692  0.26 24.23 ?  6   PHE   A HZ   1 
ATOM   97   N N    A SER   A 1 7   ? 13.299 -7.533  18.307  0.74 20.10 ?  7   SER   A N    1 
ATOM   98   N N    B SER   A 1 7   ? 13.323 -7.801  18.506  0.26 21.08 ?  7   SER   A N    1 
ATOM   99   C CA   A SER   A 1 7   ? 11.930 -7.664  18.793  0.74 20.51 ?  7   SER   A CA   1 
ATOM   100  C CA   B SER   A 1 7   ? 11.975 -8.138  18.933  0.26 20.36 ?  7   SER   A CA   1 
ATOM   101  C C    A SER   A 1 7   ? 10.926 -7.427  17.670  0.74 19.34 ?  7   SER   A C    1 
ATOM   102  C C    B SER   A 1 7   ? 10.965 -7.651  17.905  0.26 19.11 ?  7   SER   A C    1 
ATOM   103  O O    A SER   A 1 7   ? 11.134 -6.574  16.805  0.74 19.18 ?  7   SER   A O    1 
ATOM   104  O O    B SER   A 1 7   ? 11.169 -6.633  17.239  0.26 19.08 ?  7   SER   A O    1 
ATOM   105  C CB   A SER   A 1 7   ? 11.674 -6.672  19.939  0.74 22.12 ?  7   SER   A CB   1 
ATOM   106  C CB   B SER   A 1 7   ? 11.655 -7.522  20.298  0.26 21.01 ?  7   SER   A CB   1 
ATOM   107  O OG   A SER   A 1 7   ? 10.333 -6.743  20.387  0.74 23.82 ?  7   SER   A OG   1 
ATOM   108  O OG   B SER   A 1 7   ? 10.534 -8.149  20.891  0.26 21.65 ?  7   SER   A OG   1 
ATOM   109  H H    A SER   A 1 7   ? 13.449 -6.802  17.874  0.74 24.13 ?  7   SER   A H    1 
ATOM   110  H H    B SER   A 1 7   ? 13.422 -6.986  18.244  0.26 25.29 ?  7   SER   A H    1 
ATOM   111  H HA   A SER   A 1 7   ? 11.793 -8.559  19.135  0.74 24.61 ?  7   SER   A HA   1 
ATOM   112  H HA   B SER   A 1 7   ? 11.898 -9.100  19.005  0.26 24.44 ?  7   SER   A HA   1 
ATOM   113  H HB2  A SER   A 1 7   ? 12.262 -6.889  20.682  0.74 26.54 ?  7   SER   A HB2  1 
ATOM   114  H HB2  B SER   A 1 7   ? 12.423 -7.630  20.879  0.26 25.21 ?  7   SER   A HB2  1 
ATOM   115  H HB3  A SER   A 1 7   ? 11.858 -5.773  19.627  0.74 26.54 ?  7   SER   A HB3  1 
ATOM   116  H HB3  B SER   A 1 7   ? 11.458 -6.581  20.179  0.26 25.21 ?  7   SER   A HB3  1 
ATOM   117  H HG   A SER   A 1 7   ? 10.208 -6.192  21.010  0.74 28.58 ?  7   SER   A HG   1 
ATOM   118  H HG   B SER   A 1 7   ? 9.863  -8.073  20.393  0.26 25.98 ?  7   SER   A HG   1 
ATOM   119  N N    A GLY   A 1 8   ? 9.833  -8.189  17.687  0.74 18.94 ?  8   GLY   A N    1 
ATOM   120  N N    B GLY   A 1 8   ? 9.869  -8.395  17.784  0.26 18.07 ?  8   GLY   A N    1 
ATOM   121  C CA   A GLY   A 1 8   ? 8.742  -7.944  16.765  0.74 18.46 ?  8   GLY   A CA   1 
ATOM   122  C CA   B GLY   A 1 8   ? 8.798  -8.033  16.883  0.26 17.14 ?  8   GLY   A CA   1 
ATOM   123  C C    A GLY   A 1 8   ? 8.936  -8.452  15.355  0.74 17.46 ?  8   GLY   A C    1 
ATOM   124  C C    B GLY   A 1 8   ? 8.951  -8.513  15.461  0.26 16.06 ?  8   GLY   A C    1 
ATOM   125  O O    A GLY   A 1 8   ? 8.201  -8.031  14.455  0.74 17.96 ?  8   GLY   A O    1 
ATOM   126  O O    B GLY   A 1 8   ? 8.152  -8.113  14.605  0.26 16.29 ?  8   GLY   A O    1 
ATOM   127  H H    A GLY   A 1 8   ? 9.708  -8.845  18.226  0.74 22.73 ?  8   GLY   A H    1 
ATOM   128  H H    B GLY   A 1 8   ? 9.725  -9.120  18.224  0.26 21.69 ?  8   GLY   A H    1 
ATOM   129  H HA2  A GLY   A 1 8   ? 7.940  -8.354  17.124  0.74 22.16 ?  8   GLY   A HA2  1 
ATOM   130  H HA2  B GLY   A 1 8   ? 7.967  -8.392  17.222  0.26 20.57 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  A GLY   A 1 8   ? 8.587  -6.986  16.717  0.74 22.16 ?  8   GLY   A HA3  1 
ATOM   132  H HA3  B GLY   A 1 8   ? 8.724  -7.068  16.858  0.26 20.57 ?  8   GLY   A HA3  1 
ATOM   133  N N    A TYR   A 1 9   ? 9.901  -9.336  15.123  0.74 15.88 ?  9   TYR   A N    1 
ATOM   134  N N    B TYR   A 1 9   ? 9.938  -9.355  15.174  0.26 14.80 ?  9   TYR   A N    1 
ATOM   135  C CA   A TYR   A 1 9   ? 10.135 -9.879  13.792  0.74 14.47 ?  9   TYR   A CA   1 
ATOM   136  C CA   B TYR   A 1 9   ? 10.183 -9.807  13.814  0.26 13.63 ?  9   TYR   A CA   1 
ATOM   137  C C    A TYR   A 1 9   ? 9.247  -11.089 13.531  0.74 13.93 ?  9   TYR   A C    1 
ATOM   138  C C    B TYR   A 1 9   ? 9.344  -11.039 13.500  0.26 12.95 ?  9   TYR   A C    1 
ATOM   139  O O    A TYR   A 1 9   ? 8.920  -11.861 14.439  0.74 14.72 ?  9   TYR   A O    1 
ATOM   140  O O    B TYR   A 1 9   ? 9.359  -12.018 14.254  0.26 13.34 ?  9   TYR   A O    1 
ATOM   141  C CB   A TYR   A 1 9   ? 11.607 -10.287 13.618  0.74 14.65 ?  9   TYR   A CB   1 
ATOM   142  C CB   B TYR   A 1 9   ? 11.665 -10.125 13.619  0.26 13.54 ?  9   TYR   A CB   1 
ATOM   143  C CG   A TYR   A 1 9   ? 12.541 -9.108  13.478  0.74 14.37 ?  9   TYR   A CG   1 
ATOM   144  C CG   B TYR   A 1 9   ? 12.521 -8.893  13.437  0.26 13.37 ?  9   TYR   A CG   1 
ATOM   145  C CD1  A TYR   A 1 9   ? 12.889 -8.341  14.579  0.74 14.55 ?  9   TYR   A CD1  1 
ATOM   146  C CD1  B TYR   A 1 9   ? 12.772 -8.038  14.499  0.26 13.41 ?  9   TYR   A CD1  1 
ATOM   147  C CD2  A TYR   A 1 9   ? 13.055 -8.747  12.239  0.74 14.09 ?  9   TYR   A CD2  1 
ATOM   148  C CD2  B TYR   A 1 9   ? 13.059 -8.575  12.197  0.26 12.94 ?  9   TYR   A CD2  1 
ATOM   149  C CE1  A TYR   A 1 9   ? 13.723 -7.246  14.456  0.74 14.70 ?  9   TYR   A CE1  1 
ATOM   150  C CE1  B TYR   A 1 9   ? 13.542 -6.905  14.337  0.26 13.11 ?  9   TYR   A CE1  1 
ATOM   151  C CE2  A TYR   A 1 9   ? 13.886 -7.656  12.103  0.74 14.30 ?  9   TYR   A CE2  1 
ATOM   152  C CE2  B TYR   A 1 9   ? 13.830 -7.443  12.023  0.26 12.62 ?  9   TYR   A CE2  1 
ATOM   153  C CZ   A TYR   A 1 9   ? 14.215 -6.909  13.214  0.74 14.97 ?  9   TYR   A CZ   1 
ATOM   154  C CZ   B TYR   A 1 9   ? 14.064 -6.612  13.095  0.26 12.51 ?  9   TYR   A CZ   1 
ATOM   155  O OH   A TYR   A 1 9   ? 15.040 -5.828  13.074  0.74 16.21 ?  9   TYR   A OH   1 
ATOM   156  O OH   B TYR   A 1 9   ? 14.826 -5.481  12.928  0.26 12.30 ?  9   TYR   A OH   1 
ATOM   157  H H    A TYR   A 1 9   ? 10.441 -9.633  15.724  0.74 19.06 ?  9   TYR   A H    1 
ATOM   158  H H    B TYR   A 1 9   ? 10.490 -9.681  15.754  0.26 17.76 ?  9   TYR   A H    1 
ATOM   159  H HA   A TYR   A 1 9   ? 9.936  -9.195  13.130  0.74 17.36 ?  9   TYR   A HA   1 
ATOM   160  H HA   B TYR   A 1 9   ? 9.942  -9.107  13.190  0.26 16.35 ?  9   TYR   A HA   1 
ATOM   161  H HB2  A TYR   A 1 9   ? 11.890 -10.799 14.388  0.74 17.58 ?  9   TYR   A HB2  1 
ATOM   162  H HB2  B TYR   A 1 9   ? 12.003 -10.636 14.376  0.26 16.25 ?  9   TYR   A HB2  1 
ATOM   163  H HB3  A TYR   A 1 9   ? 11.686 -10.822 12.813  0.74 17.58 ?  9   TYR   A HB3  1 
ATOM   164  H HB3  B TYR   A 1 9   ? 11.725 -10.642 12.810  0.26 16.25 ?  9   TYR   A HB3  1 
ATOM   165  H HD1  A TYR   A 1 9   ? 12.544 -8.561  15.414  0.74 17.46 ?  9   TYR   A HD1  1 
ATOM   166  H HD1  B TYR   A 1 9   ? 12.416 -8.235  15.336  0.26 16.09 ?  9   TYR   A HD1  1 
ATOM   167  H HD2  A TYR   A 1 9   ? 12.838 -9.244  11.484  0.74 16.90 ?  9   TYR   A HD2  1 
ATOM   168  H HD2  B TYR   A 1 9   ? 12.904 -9.135  11.470  0.26 15.53 ?  9   TYR   A HD2  1 
ATOM   169  H HE1  A TYR   A 1 9   ? 13.947 -6.742  15.205  0.74 17.64 ?  9   TYR   A HE1  1 
ATOM   170  H HE1  B TYR   A 1 9   ? 13.699 -6.339  15.059  0.26 15.73 ?  9   TYR   A HE1  1 
ATOM   171  H HE2  A TYR   A 1 9   ? 14.240 -7.428  11.269  0.74 17.16 ?  9   TYR   A HE2  1 
ATOM   172  H HE2  B TYR   A 1 9   ? 14.190 -7.236  11.189  0.26 15.15 ?  9   TYR   A HE2  1 
ATOM   173  H HH   A TYR   A 1 9   ? 15.179 -5.469  13.823  0.74 19.46 ?  9   TYR   A HH   1 
ATOM   174  H HH   B TYR   A 1 9   ? 15.081 -5.413  12.131  0.26 14.76 ?  9   TYR   A HH   1 
ATOM   175  N N    A LEU   A 1 10  ? 8.879  -11.256 12.263  0.74 13.27 ?  10  LEU   A N    1 
ATOM   176  N N    B LEU   A 1 10  ? 8.616  -10.987 12.386  0.26 12.07 ?  10  LEU   A N    1 
ATOM   177  C CA   A LEU   A 1 10  ? 8.267  -12.483 11.777  0.74 13.17 ?  10  LEU   A CA   1 
ATOM   178  C CA   B LEU   A 1 10  ? 7.979  -12.188 11.869  0.26 11.30 ?  10  LEU   A CA   1 
ATOM   179  C C    A LEU   A 1 10  ? 9.379  -13.415 11.306  0.74 12.43 ?  10  LEU   A C    1 
ATOM   180  C C    B LEU   A 1 10  ? 9.043  -13.147 11.351  0.26 11.67 ?  10  LEU   A C    1 
ATOM   181  O O    A LEU   A 1 10  ? 10.344 -12.978 10.669  0.74 12.84 ?  10  LEU   A O    1 
ATOM   182  O O    B LEU   A 1 10  ? 10.008 -12.741 10.695  0.26 12.10 ?  10  LEU   A O    1 
ATOM   183  C CB   A LEU   A 1 10  ? 7.339  -12.165 10.606  0.74 14.75 ?  10  LEU   A CB   1 
ATOM   184  C CB   B LEU   A 1 10  ? 7.006  -11.838 10.744  0.26 10.50 ?  10  LEU   A CB   1 
ATOM   185  C CG   A LEU   A 1 10  ? 6.640  -13.363 9.957   0.74 17.37 ?  10  LEU   A CG   1 
ATOM   186  C CG   B LEU   A 1 10  ? 6.266  -13.042 10.148  0.26 9.63  ?  10  LEU   A CG   1 
ATOM   187  C CD1  A LEU   A 1 10  ? 5.549  -13.905 10.864  0.74 19.17 ?  10  LEU   A CD1  1 
ATOM   188  C CD1  B LEU   A 1 10  ? 4.837  -12.660 9.808   0.26 10.09 ?  10  LEU   A CD1  1 
ATOM   189  C CD2  A LEU   A 1 10  ? 6.095  -13.011 8.579   0.74 19.22 ?  10  LEU   A CD2  1 
ATOM   190  C CD2  B LEU   A 1 10  ? 6.965  -13.604 8.911   0.26 9.34  ?  10  LEU   A CD2  1 
ATOM   191  H H    A LEU   A 1 10  ? 8.992  -10.657 11.649  0.74 15.92 ?  10  LEU   A H    1 
ATOM   192  H H    B LEU   A 1 10  ? 8.473  -10.268 11.922  0.26 14.48 ?  10  LEU   A H    1 
ATOM   193  H HA   A LEU   A 1 10  ? 7.763  -12.907 12.492  0.74 15.80 ?  10  LEU   A HA   1 
ATOM   194  H HA   B LEU   A 1 10  ? 7.482  -12.618 12.584  0.26 13.56 ?  10  LEU   A HA   1 
ATOM   195  H HB2  A LEU   A 1 10  ? 6.652  -11.560 10.921  0.74 17.71 ?  10  LEU   A HB2  1 
ATOM   196  H HB2  B LEU   A 1 10  ? 6.337  -11.219 11.089  0.26 12.60 ?  10  LEU   A HB2  1 
ATOM   197  H HB3  A LEU   A 1 10  ? 7.865  -11.726 9.919   0.74 17.71 ?  10  LEU   A HB3  1 
ATOM   198  H HB3  B LEU   A 1 10  ? 7.499  -11.413 10.028  0.26 12.60 ?  10  LEU   A HB3  1 
ATOM   199  H HG   A LEU   A 1 10  ? 7.291  -14.071 9.835   0.74 20.84 ?  10  LEU   A HG   1 
ATOM   200  H HG   B LEU   A 1 10  ? 6.226  -13.741 10.817  0.26 11.56 ?  10  LEU   A HG   1 
ATOM   201  H HD11 A LEU   A 1 10  ? 5.152  -14.686 10.446  0.74 23.00 ?  10  LEU   A HD11 1 
ATOM   202  H HD11 B LEU   A 1 10  ? 4.389  -13.425 9.413   0.26 12.11 ?  10  LEU   A HD11 1 
ATOM   203  H HD12 A LEU   A 1 10  ? 5.940  -14.152 11.718  0.74 23.00 ?  10  LEU   A HD12 1 
ATOM   204  H HD12 B LEU   A 1 10  ? 4.373  -12.391 10.620  0.26 12.11 ?  10  LEU   A HD12 1 
ATOM   205  H HD13 A LEU   A 1 10  ? 4.875  -13.221 10.995  0.74 23.00 ?  10  LEU   A HD13 1 
ATOM   206  H HD13 B LEU   A 1 10  ? 4.845  -11.922 9.177   0.26 12.11 ?  10  LEU   A HD13 1 
ATOM   207  H HD21 A LEU   A 1 10  ? 5.662  -13.795 8.206   0.74 23.07 ?  10  LEU   A HD21 1 
ATOM   208  H HD21 B LEU   A 1 10  ? 6.417  -14.316 8.542   0.26 11.21 ?  10  LEU   A HD21 1 
ATOM   209  H HD22 A LEU   A 1 10  ? 5.458  -12.288 8.667   0.74 23.07 ?  10  LEU   A HD22 1 
ATOM   210  H HD22 B LEU   A 1 10  ? 7.065  -12.894 8.258   0.26 11.21 ?  10  LEU   A HD22 1 
ATOM   211  H HD23 A LEU   A 1 10  ? 6.833  -12.740 8.010   0.74 23.07 ?  10  LEU   A HD23 1 
ATOM   212  H HD23 B LEU   A 1 10  ? 7.830  -13.949 9.164   0.26 11.21 ?  10  LEU   A HD23 1 
ATOM   213  N N    A LYS   A 1 11  ? 9.247  -14.697 11.629  0.74 12.25 ?  11  LYS   A N    1 
ATOM   214  N N    B LYS   A 1 11  ? 8.862  -14.425 11.648  0.26 11.48 ?  11  LYS   A N    1 
ATOM   215  C CA   A LYS   A 1 11  ? 10.252 -15.692 11.274  0.74 12.55 ?  11  LYS   A CA   1 
ATOM   216  C CA   B LYS   A 1 11  ? 9.825  -15.454 11.286  0.26 11.36 ?  11  LYS   A CA   1 
ATOM   217  C C    A LYS   A 1 11  ? 9.893  -16.283 9.915   0.74 12.13 ?  11  LYS   A C    1 
ATOM   218  C C    B LYS   A 1 11  ? 9.500  -15.966 9.889   0.26 11.39 ?  11  LYS   A C    1 
ATOM   219  O O    A LYS   A 1 11  ? 8.835  -16.902 9.774   0.74 13.68 ?  11  LYS   A O    1 
ATOM   220  O O    B LYS   A 1 11  ? 8.411  -16.501 9.660   0.26 11.34 ?  11  LYS   A O    1 
ATOM   221  C CB   A LYS   A 1 11  ? 10.300 -16.772 12.358  0.74 11.93 ?  11  LYS   A CB   1 
ATOM   222  C CB   B LYS   A 1 11  ? 9.756  -16.593 12.300  0.26 11.02 ?  11  LYS   A CB   1 
ATOM   223  C CG   A LYS   A 1 11  ? 11.335 -17.870 12.162  0.74 12.21 ?  11  LYS   A CG   1 
ATOM   224  C CG   B LYS   A 1 11  ? 10.814 -17.657 12.100  0.26 10.91 ?  11  LYS   A CG   1 
ATOM   225  C CD   A LYS   A 1 11  ? 11.398 -18.739 13.422  0.74 12.50 ?  11  LYS   A CD   1 
ATOM   226  C CD   B LYS   A 1 11  ? 10.783 -18.683 13.220  0.26 11.32 ?  11  LYS   A CD   1 
ATOM   227  C CE   A LYS   A 1 11  ? 12.401 -19.888 13.322  0.74 12.58 ?  11  LYS   A CE   1 
ATOM   228  C CE   B LYS   A 1 11  ? 11.832 -19.765 13.012  0.26 11.28 ?  11  LYS   A CE   1 
ATOM   229  N NZ   A LYS   A 1 11  ? 13.769 -19.427 12.995  0.74 12.65 ?  11  LYS   A NZ   1 
ATOM   230  N NZ   B LYS   A 1 11  ? 13.223 -19.227 13.023  0.26 11.36 ?  11  LYS   A NZ   1 
ATOM   231  H H    A LYS   A 1 11  ? 8.571  -15.023 12.054  0.74 14.70 ?  11  LYS   A H    1 
ATOM   232  H H    B LYS   A 1 11  ? 8.173  -14.722 12.065  0.26 13.78 ?  11  LYS   A H    1 
ATOM   233  H HA   A LYS   A 1 11  ? 11.123 -15.268 11.212  0.74 15.06 ?  11  LYS   A HA   1 
ATOM   234  H HA   B LYS   A 1 11  ? 10.721 -15.078 11.288  0.26 13.63 ?  11  LYS   A HA   1 
ATOM   235  H HB2  A LYS   A 1 11  ? 10.500 -16.340 13.205  0.74 14.32 ?  11  LYS   A HB2  1 
ATOM   236  H HB2  B LYS   A 1 11  ? 9.865  -16.222 13.190  0.26 13.22 ?  11  LYS   A HB2  1 
ATOM   237  H HB3  A LYS   A 1 11  ? 9.435  -17.195 12.407  0.74 14.32 ?  11  LYS   A HB3  1 
ATOM   238  H HB3  B LYS   A 1 11  ? 8.885  -17.015 12.227  0.26 13.22 ?  11  LYS   A HB3  1 
ATOM   239  H HG2  A LYS   A 1 11  ? 11.080 -18.430 11.412  0.74 14.65 ?  11  LYS   A HG2  1 
ATOM   240  H HG2  B LYS   A 1 11  ? 10.653 -18.116 11.262  0.26 13.09 ?  11  LYS   A HG2  1 
ATOM   241  H HG3  A LYS   A 1 11  ? 12.210 -17.478 12.014  0.74 14.65 ?  11  LYS   A HG3  1 
ATOM   242  H HG3  B LYS   A 1 11  ? 11.689 -17.240 12.094  0.26 13.09 ?  11  LYS   A HG3  1 
ATOM   243  H HD2  A LYS   A 1 11  ? 11.653 -18.188 14.176  0.74 15.01 ?  11  LYS   A HD2  1 
ATOM   244  H HD2  B LYS   A 1 11  ? 10.962 -18.243 14.066  0.26 13.58 ?  11  LYS   A HD2  1 
ATOM   245  H HD3  A LYS   A 1 11  ? 10.522 -19.130 13.580  0.74 15.01 ?  11  LYS   A HD3  1 
ATOM   246  H HD3  B LYS   A 1 11  ? 9.908  -19.106 13.242  0.26 13.58 ?  11  LYS   A HD3  1 
ATOM   247  H HE2  A LYS   A 1 11  ? 12.442 -20.352 14.178  0.74 15.10 ?  11  LYS   A HE2  1 
ATOM   248  H HE2  B LYS   A 1 11  ? 11.754 -20.419 13.724  0.26 13.53 ?  11  LYS   A HE2  1 
ATOM   249  H HE3  A LYS   A 1 11  ? 12.119 -20.503 12.629  0.74 15.10 ?  11  LYS   A HE3  1 
ATOM   250  H HE3  B LYS   A 1 11  ? 11.678 -20.189 12.153  0.26 13.53 ?  11  LYS   A HE3  1 
ATOM   251  H HZ1  A LYS   A 1 11  ? 14.324 -20.125 12.947  0.74 15.18 ?  11  LYS   A HZ1  1 
ATOM   252  H HZ1  B LYS   A 1 11  ? 13.803 -19.884 12.869  0.26 13.63 ?  11  LYS   A HZ1  1 
ATOM   253  H HZ2  A LYS   A 1 11  ? 13.768 -19.007 12.211  0.74 15.18 ?  11  LYS   A HZ2  1 
ATOM   254  H HZ2  B LYS   A 1 11  ? 13.315 -18.606 12.392  0.26 13.63 ?  11  LYS   A HZ2  1 
ATOM   255  H HZ3  A LYS   A 1 11  ? 14.063 -18.870 13.623  0.74 15.18 ?  11  LYS   A HZ3  1 
ATOM   256  H HZ3  B LYS   A 1 11  ? 13.402 -18.863 13.815  0.26 13.63 ?  11  LYS   A HZ3  1 
ATOM   257  N N    A LEU   A 1 12  ? 10.761 -16.097 8.915   0.74 11.17 ?  12  LEU   A N    1 
ATOM   258  N N    B LEU   A 1 12  ? 10.431 -15.785 8.951   0.26 11.92 ?  12  LEU   A N    1 
ATOM   259  C CA   A LEU   A 1 12  ? 10.493 -16.672 7.598   0.74 11.69 ?  12  LEU   A CA   1 
ATOM   260  C CA   B LEU   A 1 12  ? 10.239 -16.298 7.598   0.26 11.98 ?  12  LEU   A CA   1 
ATOM   261  C C    A LEU   A 1 12  ? 11.072 -18.075 7.444   0.74 11.50 ?  12  LEU   A C    1 
ATOM   262  C C    B LEU   A 1 12  ? 10.796 -17.708 7.434   0.26 11.86 ?  12  LEU   A C    1 
ATOM   263  O O    A LEU   A 1 12  ? 10.442 -18.946 6.831   0.74 12.06 ?  12  LEU   A O    1 
ATOM   264  O O    B LEU   A 1 12  ? 10.131 -18.581 6.867   0.26 11.95 ?  12  LEU   A O    1 
ATOM   265  C CB   A LEU   A 1 12  ? 11.047 -15.773 6.488   0.74 12.54 ?  12  LEU   A CB   1 
ATOM   266  C CB   B LEU   A 1 12  ? 10.885 -15.361 6.574   0.26 12.53 ?  12  LEU   A CB   1 
ATOM   267  C CG   A LEU   A 1 12  ? 10.415 -14.386 6.341   0.74 13.52 ?  12  LEU   A CG   1 
ATOM   268  C CG   B LEU   A 1 12  ? 10.055 -14.158 6.124   0.26 13.09 ?  12  LEU   A CG   1 
ATOM   269  C CD1  A LEU   A 1 12  ? 11.155 -13.604 5.268   0.74 14.29 ?  12  LEU   A CD1  1 
ATOM   270  C CD1  B LEU   A 1 12  ? 10.853 -13.294 5.163   0.26 13.22 ?  12  LEU   A CD1  1 
ATOM   271  C CD2  A LEU   A 1 12  ? 8.932  -14.481 6.006   0.74 14.12 ?  12  LEU   A CD2  1 
ATOM   272  C CD2  B LEU   A 1 12  ? 8.754  -14.608 5.478   0.26 13.50 ?  12  LEU   A CD2  1 
ATOM   273  H H    A LEU   A 1 12  ? 11.494 -15.638 8.968   0.74 13.41 ?  12  LEU   A H    1 
ATOM   274  H H    B LEU   A 1 12  ? 11.168 -15.353 9.069   0.26 14.31 ?  12  LEU   A H    1 
ATOM   275  H HA   A LEU   A 1 12  ? 9.535  -16.735 7.476   0.74 14.03 ?  12  LEU   A HA   1 
ATOM   276  H HA   B LEU   A 1 12  ? 9.286  -16.329 7.416   0.26 14.37 ?  12  LEU   A HA   1 
ATOM   277  H HB2  A LEU   A 1 12  ? 11.993 -15.641 6.646   0.74 15.05 ?  12  LEU   A HB2  1 
ATOM   278  H HB2  B LEU   A 1 12  ? 11.706 -15.016 6.954   0.26 15.04 ?  12  LEU   A HB2  1 
ATOM   279  H HB3  A LEU   A 1 12  ? 10.925 -16.232 5.640   0.74 15.05 ?  12  LEU   A HB3  1 
ATOM   280  H HB3  B LEU   A 1 12  ? 11.089 -15.880 5.781   0.26 15.04 ?  12  LEU   A HB3  1 
ATOM   281  H HG   A LEU   A 1 12  ? 10.506 -13.903 7.176   0.74 16.23 ?  12  LEU   A HG   1 
ATOM   282  H HG   B LEU   A 1 12  ? 9.835  -13.617 6.898   0.26 15.71 ?  12  LEU   A HG   1 
ATOM   283  H HD11 A LEU   A 1 12  ? 10.751 -12.726 5.181   0.74 17.14 ?  12  LEU   A HD11 1 
ATOM   284  H HD11 B LEU   A 1 12  ? 10.313 -12.532 4.901   0.26 15.86 ?  12  LEU   A HD11 1 
ATOM   285  H HD12 A LEU   A 1 12  ? 12.086 -13.514 5.529   0.74 17.14 ?  12  LEU   A HD12 1 
ATOM   286  H HD12 B LEU   A 1 12  ? 11.660 -12.991 5.607   0.26 15.86 ?  12  LEU   A HD12 1 
ATOM   287  H HD13 A LEU   A 1 12  ? 11.092 -14.083 4.427   0.74 17.14 ?  12  LEU   A HD13 1 
ATOM   288  H HD13 B LEU   A 1 12  ? 11.083 -13.821 4.382   0.26 15.86 ?  12  LEU   A HD13 1 
ATOM   289  H HD21 A LEU   A 1 12  ? 8.593  -13.593 5.814   0.74 16.94 ?  12  LEU   A HD21 1 
ATOM   290  H HD21 B LEU   A 1 12  ? 8.377  -13.869 4.977   0.26 16.20 ?  12  LEU   A HD21 1 
ATOM   291  H HD22 A LEU   A 1 12  ? 8.820  -15.053 5.231   0.74 16.94 ?  12  LEU   A HD22 1 
ATOM   292  H HD22 B LEU   A 1 12  ? 8.939  -15.351 4.882   0.26 16.20 ?  12  LEU   A HD22 1 
ATOM   293  H HD23 A LEU   A 1 12  ? 8.462  -14.858 6.766   0.74 16.94 ?  12  LEU   A HD23 1 
ATOM   294  H HD23 B LEU   A 1 12  ? 8.136  -14.888 6.171   0.26 16.20 ?  12  LEU   A HD23 1 
ATOM   295  N N    A THR   A 1 13  ? 12.280 -18.287 7.957   0.74 11.37 ?  13  THR   A N    1 
ATOM   296  N N    B THR   A 1 13  ? 12.019 -17.938 7.903   0.26 11.85 ?  13  THR   A N    1 
ATOM   297  C CA   A THR   A 1 13  ? 12.975 -19.562 7.857   0.74 11.63 ?  13  THR   A CA   1 
ATOM   298  C CA   B THR   A 1 13  ? 12.656 -19.245 7.832   0.26 12.09 ?  13  THR   A CA   1 
ATOM   299  C C    A THR   A 1 13  ? 13.743 -19.781 9.150   0.74 11.33 ?  13  THR   A C    1 
ATOM   300  C C    B THR   A 1 13  ? 13.394 -19.485 9.146   0.26 12.13 ?  13  THR   A C    1 
ATOM   301  O O    A THR   A 1 13  ? 13.658 -18.994 10.098  0.74 11.34 ?  13  THR   A O    1 
ATOM   302  O O    B THR   A 1 13  ? 13.228 -18.751 10.125  0.26 12.45 ?  13  THR   A O    1 
ATOM   303  C CB   A THR   A 1 13  ? 13.953 -19.604 6.671   0.74 12.47 ?  13  THR   A CB   1 
ATOM   304  C CB   B THR   A 1 13  ? 13.623 -19.326 6.643   0.26 12.18 ?  13  THR   A CB   1 
ATOM   305  O OG1  A THR   A 1 13  ? 15.035 -18.706 6.924   0.74 12.71 ?  13  THR   A OG1  1 
ATOM   306  O OG1  B THR   A 1 13  ? 14.689 -18.390 6.836   0.26 11.93 ?  13  THR   A OG1  1 
ATOM   307  C CG2  A THR   A 1 13  ? 13.281 -19.226 5.365   0.74 13.73 ?  13  THR   A CG2  1 
ATOM   308  C CG2  B THR   A 1 13  ? 12.917 -19.032 5.320   0.26 12.76 ?  13  THR   A CG2  1 
ATOM   309  H H    A THR   A 1 13  ? 12.738 -17.684 8.370   0.74 13.65 ?  13  THR   A H    1 
ATOM   310  H H    B THR   A 1 13  ? 12.510 -17.332 8.262   0.26 14.22 ?  13  THR   A H    1 
ATOM   311  H HA   A THR   A 1 13  ? 12.333 -20.280 7.755   0.74 13.95 ?  13  THR   A HA   1 
ATOM   312  H HA   B THR   A 1 13  ? 11.975 -19.929 7.722   0.26 14.51 ?  13  THR   A HA   1 
ATOM   313  H HB   A THR   A 1 13  ? 14.304 -20.506 6.579   0.74 14.97 ?  13  THR   A HB   1 
ATOM   314  H HB   B THR   A 1 13  ? 13.992 -20.221 6.591   0.26 14.62 ?  13  THR   A HB   1 
ATOM   315  H HG1  A THR   A 1 13  ? 15.581 -18.726 6.275   0.74 15.25 ?  13  THR   A HG1  1 
ATOM   316  H HG1  B THR   A 1 13  ? 15.221 -18.425 6.185   0.26 14.32 ?  13  THR   A HG1  1 
ATOM   317  H HG21 A THR   A 1 13  ? 13.895 -19.359 4.626   0.74 16.47 ?  13  THR   A HG21 1 
ATOM   318  H HG21 B THR   A 1 13  ? 13.536 -19.155 4.580   0.26 15.32 ?  13  THR   A HG21 1 
ATOM   319  H HG22 A THR   A 1 13  ? 12.497 -19.782 5.225   0.74 16.47 ?  13  THR   A HG22 1 
ATOM   320  H HG22 B THR   A 1 13  ? 12.167 -19.637 5.202   0.26 15.32 ?  13  THR   A HG22 1 
ATOM   321  H HG23 A THR   A 1 13  ? 13.009 -18.297 5.388   0.74 16.47 ?  13  THR   A HG23 1 
ATOM   322  H HG23 B THR   A 1 13  ? 12.592 -18.120 5.310   0.26 15.32 ?  13  THR   A HG23 1 
ATOM   323  N N    A ASP   A 1 14  ? 14.547 -20.843 9.158   0.74 11.87 ?  14  ASP   A N    1 
ATOM   324  N N    B ASP   A 1 14  ? 14.233 -20.521 9.151   0.26 12.66 ?  14  ASP   A N    1 
ATOM   325  C CA   A ASP   A 1 14  ? 15.394 -21.126 10.306  0.74 12.47 ?  14  ASP   A CA   1 
ATOM   326  C CA   B ASP   A 1 14  ? 15.033 -20.837 10.329  0.26 13.42 ?  14  ASP   A CA   1 
ATOM   327  C C    A ASP   A 1 14  ? 16.244 -19.924 10.698  0.74 12.16 ?  14  ASP   A C    1 
ATOM   328  C C    B ASP   A 1 14  ? 15.899 -19.656 10.754  0.26 12.41 ?  14  ASP   A C    1 
ATOM   329  O O    A ASP   A 1 14  ? 16.507 -19.711 11.886  0.74 13.07 ?  14  ASP   A O    1 
ATOM   330  O O    B ASP   A 1 14  ? 16.067 -19.404 11.954  0.26 12.27 ?  14  ASP   A O    1 
ATOM   331  C CB   A ASP   A 1 14  ? 16.313 -22.302 9.997   0.74 14.97 ?  14  ASP   A CB   1 
ATOM   332  C CB   B ASP   A 1 14  ? 15.895 -22.065 10.035  0.26 15.29 ?  14  ASP   A CB   1 
ATOM   333  C CG   A ASP   A 1 14  ? 17.238 -22.608 11.144  0.74 18.92 ?  14  ASP   A CG   1 
ATOM   334  C CG   B ASP   A 1 14  ? 16.923 -22.342 11.120  0.26 17.38 ?  14  ASP   A CG   1 
ATOM   335  O OD1  A ASP   A 1 14  ? 16.732 -23.083 12.183  0.74 20.11 ?  14  ASP   A OD1  1 
ATOM   336  O OD1  B ASP   A 1 14  ? 16.591 -22.218 12.319  0.26 18.31 ?  14  ASP   A OD1  1 
ATOM   337  O OD2  A ASP   A 1 14  ? 18.450 -22.333 11.017  0.74 21.75 -1 14  ASP   A OD2  1 
ATOM   338  O OD2  B ASP   A 1 14  ? 18.064 -22.707 10.769  0.26 18.23 -1 14  ASP   A OD2  1 
ATOM   339  H H    A ASP   A 1 14  ? 14.630 -21.412 8.514   0.74 14.25 ?  14  ASP   A H    1 
ATOM   340  H H    B ASP   A 1 14  ? 14.349 -21.049 8.489   0.26 15.19 ?  14  ASP   A H    1 
ATOM   341  H HA   A ASP   A 1 14  ? 14.843 -21.370 11.066  0.74 14.97 ?  14  ASP   A HA   1 
ATOM   342  H HA   B ASP   A 1 14  ? 14.437 -21.053 11.064  0.26 16.10 ?  14  ASP   A HA   1 
ATOM   343  H HB2  A ASP   A 1 14  ? 15.775 -23.098 9.821   0.74 17.96 ?  14  ASP   A HB2  1 
ATOM   344  H HB2  B ASP   A 1 14  ? 15.317 -22.839 9.955   0.26 18.35 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  A ASP   A 1 14  ? 16.857 -22.098 9.221   0.74 17.96 ?  14  ASP   A HB3  1 
ATOM   346  H HB3  B ASP   A 1 14  ? 16.369 -21.919 9.200   0.26 18.35 ?  14  ASP   A HB3  1 
ATOM   347  N N    A ASN   A 1 15  ? 16.709 -19.144 9.713   0.74 11.62 ?  15  ASN   A N    1 
ATOM   348  N N    B ASN   A 1 15  ? 16.440 -18.904 9.789   0.26 11.73 ?  15  ASN   A N    1 
ATOM   349  C CA   A ASN   A 1 15  ? 17.705 -18.111 9.974   0.74 11.88 ?  15  ASN   A CA   1 
ATOM   350  C CA   B ASN   A 1 15  ? 17.414 -17.863 10.090  0.26 11.46 ?  15  ASN   A CA   1 
ATOM   351  C C    A ASN   A 1 15  ? 17.336 -16.714 9.495   0.74 12.28 ?  15  ASN   A C    1 
ATOM   352  C C    B ASN   A 1 15  ? 17.066 -16.481 9.551   0.26 11.72 ?  15  ASN   A C    1 
ATOM   353  O O    A ASN   A 1 15  ? 18.109 -15.788 9.750   0.74 13.86 ?  15  ASN   A O    1 
ATOM   354  O O    B ASN   A 1 15  ? 17.853 -15.552 9.754   0.26 12.94 ?  15  ASN   A O    1 
ATOM   355  C CB   A ASN   A 1 15  ? 19.070 -18.499 9.368   0.74 11.88 ?  15  ASN   A CB   1 
ATOM   356  C CB   B ASN   A 1 15  ? 18.807 -18.256 9.568   0.26 11.59 ?  15  ASN   A CB   1 
ATOM   357  C CG   A ASN   A 1 15  ? 19.033 -18.580 7.855   0.74 12.43 ?  15  ASN   A CG   1 
ATOM   358  C CG   B ASN   A 1 15  ? 18.837 -18.451 8.063   0.26 11.81 ?  15  ASN   A CG   1 
ATOM   359  O OD1  A ASN   A 1 15  ? 18.331 -19.418 7.284   0.74 12.85 ?  15  ASN   A OD1  1 
ATOM   360  O OD1  B ASN   A 1 15  ? 17.997 -19.153 7.500   0.26 11.92 ?  15  ASN   A OD1  1 
ATOM   361  N ND2  A ASN   A 1 15  ? 19.788 -17.706 7.194   0.74 12.71 ?  15  ASN   A ND2  1 
ATOM   362  N ND2  B ASN   A 1 15  ? 19.801 -17.817 7.402   0.26 11.81 ?  15  ASN   A ND2  1 
ATOM   363  H H    A ASN   A 1 15  ? 16.469 -19.206 8.893   0.74 13.95 ?  15  ASN   A H    1 
ATOM   364  H H    B ASN   A 1 15  ? 16.249 -18.978 8.956   0.26 14.07 ?  15  ASN   A H    1 
ATOM   365  H HA   A ASN   A 1 15  ? 17.840 -18.056 10.932  0.74 14.26 ?  15  ASN   A HA   1 
ATOM   366  H HA   B ASN   A 1 15  ? 17.482 -17.772 11.052  0.26 13.75 ?  15  ASN   A HA   1 
ATOM   367  H HB2  A ASN   A 1 15  ? 19.732 -17.826 9.618   0.74 14.26 ?  15  ASN   A HB2  1 
ATOM   368  H HB2  B ASN   A 1 15  ? 19.436 -17.552 9.793   0.26 13.91 ?  15  ASN   A HB2  1 
ATOM   369  H HB3  A ASN   A 1 15  ? 19.344 -19.366 9.712   0.74 14.26 ?  15  ASN   A HB3  1 
ATOM   370  H HB3  B ASN   A 1 15  ? 19.071 -19.087 9.983   0.26 13.91 ?  15  ASN   A HB3  1 
ATOM   371  H HD21 A ASN   A 1 15  ? 19.798 -17.716 6.334   0.74 15.26 ?  15  ASN   A HD21 1 
ATOM   372  H HD21 B ASN   A 1 15  ? 19.859 -17.891 6.546   0.26 14.17 ?  15  ASN   A HD21 1 
ATOM   373  H HD22 A ASN   A 1 15  ? 20.266 -17.134 7.623   0.74 15.26 ?  15  ASN   A HD22 1 
ATOM   374  H HD22 B ASN   A 1 15  ? 20.370 -17.332 7.829   0.26 14.17 ?  15  ASN   A HD22 1 
ATOM   375  N N    A VAL   A 1 16  ? 16.205 -16.527 8.815   0.74 12.10 ?  16  VAL   A N    1 
ATOM   376  N N    B VAL   A 1 16  ? 15.920 -16.304 8.898   0.26 11.19 ?  16  VAL   A N    1 
ATOM   377  C CA   A VAL   A 1 16  ? 15.820 -15.231 8.269   0.74 12.05 ?  16  VAL   A CA   1 
ATOM   378  C CA   B VAL   A 1 16  ? 15.558 -15.034 8.276   0.26 11.33 ?  16  VAL   A CA   1 
ATOM   379  C C    A VAL   A 1 16  ? 14.548 -14.741 8.950   0.74 11.81 ?  16  VAL   A C    1 
ATOM   380  C C    B VAL   A 1 16  ? 14.295 -14.509 8.945   0.26 11.25 ?  16  VAL   A C    1 
ATOM   381  O O    A VAL   A 1 16  ? 13.546 -15.469 9.029   0.74 11.75 ?  16  VAL   A O    1 
ATOM   382  O O    B VAL   A 1 16  ? 13.269 -15.202 8.985   0.26 11.06 ?  16  VAL   A O    1 
ATOM   383  C CB   A VAL   A 1 16  ? 15.653 -15.269 6.740   0.74 12.67 ?  16  VAL   A CB   1 
ATOM   384  C CB   B VAL   A 1 16  ? 15.378 -15.171 6.755   0.26 11.96 ?  16  VAL   A CB   1 
ATOM   385  C CG1  A VAL   A 1 16  ? 15.250 -13.887 6.217   0.74 13.49 ?  16  VAL   A CG1  1 
ATOM   386  C CG1  B VAL   A 1 16  ? 14.957 -13.839 6.136   0.26 12.16 ?  16  VAL   A CG1  1 
ATOM   387  C CG2  A VAL   A 1 16  ? 16.928 -15.755 6.063   0.74 13.91 ?  16  VAL   A CG2  1 
ATOM   388  C CG2  B VAL   A 1 16  ? 16.663 -15.679 6.111   0.26 12.38 ?  16  VAL   A CG2  1 
ATOM   389  H H    A VAL   A 1 16  ? 15.641 -17.157 8.653   0.74 14.52 ?  16  VAL   A H    1 
ATOM   390  H H    B VAL   A 1 16  ? 15.315 -16.911 8.808   0.26 13.43 ?  16  VAL   A H    1 
ATOM   391  H HA   A VAL   A 1 16  ? 16.526 -14.594 8.467   0.74 14.46 ?  16  VAL   A HA   1 
ATOM   392  H HA   B VAL   A 1 16  ? 16.261 -14.386 8.434   0.26 13.60 ?  16  VAL   A HA   1 
ATOM   393  H HB   A VAL   A 1 16  ? 14.941 -15.887 6.521   0.74 15.20 ?  16  VAL   A HB   1 
ATOM   394  H HB   B VAL   A 1 16  ? 14.678 -15.815 6.577   0.26 14.35 ?  16  VAL   A HB   1 
ATOM   395  H HG11 A VAL   A 1 16  ? 15.332 -13.884 5.251   0.74 16.19 ?  16  VAL   A HG11 1 
ATOM   396  H HG11 B VAL   A 1 16  ? 15.037 -13.903 5.170   0.26 14.60 ?  16  VAL   A HG11 1 
ATOM   397  H HG12 A VAL   A 1 16  ? 14.331 -13.706 6.470   0.74 16.19 ?  16  VAL   A HG12 1 
ATOM   398  H HG12 B VAL   A 1 16  ? 14.037 -13.652 6.377   0.26 14.60 ?  16  VAL   A HG12 1 
ATOM   399  H HG13 A VAL   A 1 16  ? 15.839 -13.220 6.601   0.74 16.19 ?  16  VAL   A HG13 1 
ATOM   400  H HG13 B VAL   A 1 16  ? 15.538 -13.138 6.468   0.26 14.60 ?  16  VAL   A HG13 1 
ATOM   401  H HG21 A VAL   A 1 16  ? 16.824 -15.675 5.102   0.74 16.69 ?  16  VAL   A HG21 1 
ATOM   402  H HG21 B VAL   A 1 16  ? 16.549 -15.702 5.148   0.26 14.86 ?  16  VAL   A HG21 1 
ATOM   403  H HG22 A VAL   A 1 16  ? 17.673 -15.212 6.361   0.74 16.69 ?  16  VAL   A HG22 1 
ATOM   404  H HG22 B VAL   A 1 16  ? 17.392 -15.081 6.342   0.26 14.86 ?  16  VAL   A HG22 1 
ATOM   405  H HG23 A VAL   A 1 16  ? 17.078 -16.682 6.304   0.74 16.69 ?  16  VAL   A HG23 1 
ATOM   406  H HG23 B VAL   A 1 16  ? 16.852 -16.571 6.444   0.26 14.86 ?  16  VAL   A HG23 1 
ATOM   407  N N    A TYR   A 1 17  ? 14.591 -13.481 9.390   0.74 11.92 ?  17  TYR   A N    1 
ATOM   408  N N    B TYR   A 1 17  ? 14.376 -13.280 9.465   0.26 11.47 ?  17  TYR   A N    1 
ATOM   409  C CA   A TYR   A 1 17  ? 13.534 -12.798 10.122  0.74 11.71 ?  17  TYR   A CA   1 
ATOM   410  C CA   B TYR   A 1 17  ? 13.283 -12.595 10.140  0.26 11.31 ?  17  TYR   A CA   1 
ATOM   411  C C    A TYR   A 1 17  ? 13.253 -11.468 9.431   0.74 12.11 ?  17  TYR   A C    1 
ATOM   412  C C    B TYR   A 1 17  ? 13.057 -11.251 9.465   0.26 11.30 ?  17  TYR   A C    1 
ATOM   413  O O    A TYR   A 1 17  ? 14.121 -10.928 8.743   0.74 11.87 ?  17  TYR   A O    1 
ATOM   414  O O    B TYR   A 1 17  ? 14.017 -10.582 9.075   0.26 11.23 ?  17  TYR   A O    1 
ATOM   415  C CB   A TYR   A 1 17  ? 13.994 -12.551 11.567  0.74 11.94 ?  17  TYR   A CB   1 
ATOM   416  C CB   B TYR   A 1 17  ? 13.633 -12.359 11.610  0.26 11.32 ?  17  TYR   A CB   1 
ATOM   417  C CG   A TYR   A 1 17  ? 14.197 -13.827 12.354  0.74 12.84 ?  17  TYR   A CG   1 
ATOM   418  C CG   B TYR   A 1 17  ? 13.750 -13.629 12.409  0.26 11.68 ?  17  TYR   A CG   1 
ATOM   419  C CD1  A TYR   A 1 17  ? 15.366 -14.578 12.241  0.74 13.37 ?  17  TYR   A CD1  1 
ATOM   420  C CD1  B TYR   A 1 17  ? 14.894 -14.413 12.341  0.26 12.04 ?  17  TYR   A CD1  1 
ATOM   421  C CD2  A TYR   A 1 17  ? 13.205 -14.298 13.201  0.74 12.90 ?  17  TYR   A CD2  1 
ATOM   422  C CD2  B TYR   A 1 17  ? 12.712 -14.050 13.229  0.26 11.66 ?  17  TYR   A CD2  1 
ATOM   423  C CE1  A TYR   A 1 17  ? 15.533 -15.759 12.957  0.74 13.64 ?  17  TYR   A CE1  1 
ATOM   424  C CE1  B TYR   A 1 17  ? 15.005 -15.585 13.067  0.26 12.06 ?  17  TYR   A CE1  1 
ATOM   425  C CE2  A TYR   A 1 17  ? 13.359 -15.473 13.917  0.74 13.31 ?  17  TYR   A CE2  1 
ATOM   426  C CE2  B TYR   A 1 17  ? 12.813 -15.223 13.960  0.26 11.43 ?  17  TYR   A CE2  1 
ATOM   427  C CZ   A TYR   A 1 17  ? 14.524 -16.201 13.794  0.74 13.22 ?  17  TYR   A CZ   1 
ATOM   428  C CZ   B TYR   A 1 17  ? 13.961 -15.986 13.877  0.26 11.72 ?  17  TYR   A CZ   1 
ATOM   429  O OH   A TYR   A 1 17  ? 14.681 -17.365 14.514  0.74 13.69 ?  17  TYR   A OH   1 
ATOM   430  O OH   B TYR   A 1 17  ? 14.055 -17.149 14.607  0.26 11.83 ?  17  TYR   A OH   1 
ATOM   431  H H    A TYR   A 1 17  ? 15.271 -12.969 9.248   0.74 14.30 ?  17  TYR   A H    1 
ATOM   432  H H    B TYR   A 1 17  ? 15.089 -12.799 9.436   0.26 13.76 ?  17  TYR   A H    1 
ATOM   433  H HA   A TYR   A 1 17  ? 12.730 -13.339 10.124  0.74 14.05 ?  17  TYR   A HA   1 
ATOM   434  H HA   B TYR   A 1 17  ? 12.464 -13.110 10.089  0.26 13.57 ?  17  TYR   A HA   1 
ATOM   435  H HB2  A TYR   A 1 17  ? 14.836 -12.075 11.552  0.74 14.33 ?  17  TYR   A HB2  1 
ATOM   436  H HB2  B TYR   A 1 17  ? 14.475 -11.884 11.672  0.26 13.59 ?  17  TYR   A HB2  1 
ATOM   437  H HB3  A TYR   A 1 17  ? 13.321 -12.028 12.022  0.74 14.33 ?  17  TYR   A HB3  1 
ATOM   438  H HB3  B TYR   A 1 17  ? 12.934 -11.834 12.012  0.26 13.59 ?  17  TYR   A HB3  1 
ATOM   439  H HD1  A TYR   A 1 17  ? 16.046 -14.291 11.676  0.74 16.04 ?  17  TYR   A HD1  1 
ATOM   440  H HD1  B TYR   A 1 17  ? 15.596 -14.143 11.795  0.26 14.45 ?  17  TYR   A HD1  1 
ATOM   441  H HD2  A TYR   A 1 17  ? 12.418 -13.820 13.289  0.74 15.48 ?  17  TYR   A HD2  1 
ATOM   442  H HD2  B TYR   A 1 17  ? 11.934 -13.538 13.288  0.26 14.00 ?  17  TYR   A HD2  1 
ATOM   443  H HE1  A TYR   A 1 17  ? 16.320 -16.255 12.875  0.74 16.37 ?  17  TYR   A HE1  1 
ATOM   444  H HE1  B TYR   A 1 17  ? 15.777 -16.101 13.007  0.26 14.48 ?  17  TYR   A HE1  1 
ATOM   445  H HE2  A TYR   A 1 17  ? 12.681 -15.769 14.484  0.74 15.97 ?  17  TYR   A HE2  1 
ATOM   446  H HE2  B TYR   A 1 17  ? 12.111 -15.498 14.505  0.26 13.72 ?  17  TYR   A HE2  1 
ATOM   447  H HH   A TYR   A 1 17  ? 15.445 -17.691 14.382  0.74 16.43 ?  17  TYR   A HH   1 
ATOM   448  H HH   B TYR   A 1 17  ? 13.318 -17.316 14.974  0.26 14.20 ?  17  TYR   A HH   1 
ATOM   449  N N    A ILE   A 1 18  ? 12.043 -10.920 9.609   0.74 12.40 ?  18  ILE   A N    1 
ATOM   450  N N    B ILE   A 1 18  ? 11.791 -10.850 9.338   0.26 10.98 ?  18  ILE   A N    1 
ATOM   451  C CA   A ILE   A 1 18  ? 11.645 -9.724  8.863   0.74 12.60 ?  18  ILE   A CA   1 
ATOM   452  C CA   B ILE   A 1 18  ? 11.417 -9.625  8.639   0.26 11.43 ?  18  ILE   A CA   1 
ATOM   453  C C    A ILE   A 1 18  ? 10.687 -8.859  9.678   0.74 13.08 ?  18  ILE   A C    1 
ATOM   454  C C    B ILE   A 1 18  ? 10.488 -8.802  9.522   0.26 12.21 ?  18  ILE   A C    1 
ATOM   455  O O    A ILE   A 1 18  ? 9.887  -9.362  10.477  0.74 13.17 ?  18  ILE   A O    1 
ATOM   456  O O    B ILE   A 1 18  ? 9.559  -9.343  10.132  0.26 12.48 ?  18  ILE   A O    1 
ATOM   457  C CB   A ILE   A 1 18  ? 11.068 -10.115 7.480   0.74 12.49 ?  18  ILE   A CB   1 
ATOM   458  C CB   B ILE   A 1 18  ? 10.765 -9.951  7.277   0.26 11.50 ?  18  ILE   A CB   1 
ATOM   459  C CG1  A ILE   A 1 18  ? 11.004 -8.908  6.538   0.74 12.93 ?  18  ILE   A CG1  1 
ATOM   460  C CG1  B ILE   A 1 18  ? 10.520 -8.680  6.464   0.26 11.81 ?  18  ILE   A CG1  1 
ATOM   461  C CG2  A ILE   A 1 18  ? 9.720  -10.813 7.633   0.74 13.54 ?  18  ILE   A CG2  1 
ATOM   462  C CG2  B ILE   A 1 18  ? 9.471  -10.745 7.460   0.26 12.10 ?  18  ILE   A CG2  1 
ATOM   463  C CD1  A ILE   A 1 18  ? 10.717 -9.290  5.111   0.74 14.45 ?  18  ILE   A CD1  1 
ATOM   464  C CD1  B ILE   A 1 18  ? 10.183 -8.963  5.014   0.26 12.51 ?  18  ILE   A CD1  1 
ATOM   465  H H    A ILE   A 1 18  ? 11.448 -11.232 10.144  0.74 14.88 ?  18  ILE   A H    1 
ATOM   466  H H    B ILE   A 1 18  ? 11.116 -11.288 9.642   0.26 13.18 ?  18  ILE   A H    1 
ATOM   467  H HA   A ILE   A 1 18  ? 12.450 -9.199  8.707   0.74 15.12 ?  18  ILE   A HA   1 
ATOM   468  H HA   B ILE   A 1 18  ? 12.213 -9.098  8.468   0.26 13.72 ?  18  ILE   A HA   1 
ATOM   469  H HB   A ILE   A 1 18  ? 11.686 -10.751 7.088   0.74 14.98 ?  18  ILE   A HB   1 
ATOM   470  H HB   B ILE   A 1 18  ? 11.381 -10.503 6.782   0.26 13.80 ?  18  ILE   A HB   1 
ATOM   471  H HG12 A ILE   A 1 18  ? 10.308 -8.310  6.833   0.74 15.51 ?  18  ILE   A HG12 1 
ATOM   472  H HG12 B ILE   A 1 18  ? 9.777  -8.191  6.852   0.26 14.17 ?  18  ILE   A HG12 1 
ATOM   473  H HG13 A ILE   A 1 18  ? 11.864 -8.448  6.550   0.74 15.51 ?  18  ILE   A HG13 1 
ATOM   474  H HG13 B ILE   A 1 18  ? 11.321 -8.135  6.484   0.26 14.17 ?  18  ILE   A HG13 1 
ATOM   475  H HG21 A ILE   A 1 18  ? 9.461  -11.185 6.776   0.74 16.25 ?  18  ILE   A HG21 1 
ATOM   476  H HG21 B ILE   A 1 18  ? 9.167  -11.052 6.590   0.26 14.52 ?  18  ILE   A HG21 1 
ATOM   477  H HG22 A ILE   A 1 18  ? 9.801  -11.519 8.291   0.74 16.25 ?  18  ILE   A HG22 1 
ATOM   478  H HG22 B ILE   A 1 18  ? 9.646  -11.506 8.034   0.26 14.52 ?  18  ILE   A HG22 1 
ATOM   479  H HG23 A ILE   A 1 18  ? 9.058  -10.164 7.925   0.74 16.25 ?  18  ILE   A HG23 1 
ATOM   480  H HG23 B ILE   A 1 18  ? 8.799  -10.174 7.861   0.26 14.52 ?  18  ILE   A HG23 1 
ATOM   481  H HD11 A ILE   A 1 18  ? 10.757 -8.492  4.557   0.74 17.34 ?  18  ILE   A HD11 1 
ATOM   482  H HD11 B ILE   A 1 18  ? 10.096 -8.123  4.539   0.26 15.01 ?  18  ILE   A HD11 1 
ATOM   483  H HD12 A ILE   A 1 18  ? 11.379 -9.931  4.813   0.74 17.34 ?  18  ILE   A HD12 1 
ATOM   484  H HD12 B ILE   A 1 18  ? 10.898 -9.491  4.623   0.26 15.01 ?  18  ILE   A HD12 1 
ATOM   485  H HD13 A ILE   A 1 18  ? 9.831  -9.680  5.063   0.74 17.34 ?  18  ILE   A HD13 1 
ATOM   486  H HD13 B ILE   A 1 18  ? 9.349  -9.456  4.972   0.26 15.01 ?  18  ILE   A HD13 1 
ATOM   487  N N    A LYS   A 1 19  ? 10.751 -7.543  9.436   0.74 13.80 ?  19  LYS   A N    1 
ATOM   488  N N    B LYS   A 1 19  ? 10.736 -7.490  9.590   0.26 12.36 ?  19  LYS   A N    1 
ATOM   489  C CA   A LYS   A 1 19  ? 9.947  -6.567  10.167  0.74 14.94 ?  19  LYS   A CA   1 
ATOM   490  C CA   B LYS   A 1 19  ? 9.931  -6.593  10.410  0.26 12.92 ?  19  LYS   A CA   1 
ATOM   491  C C    A LYS   A 1 19  ? 9.729  -5.327  9.306   0.74 14.74 ?  19  LYS   A C    1 
ATOM   492  C C    B LYS   A 1 19  ? 9.807  -5.250  9.710   0.26 12.23 ?  19  LYS   A C    1 
ATOM   493  O O    A LYS   A 1 19  ? 10.600 -4.939  8.527   0.74 14.29 ?  19  LYS   A O    1 
ATOM   494  O O    B LYS   A 1 19  ? 10.747 -4.797  9.053   0.26 12.33 ?  19  LYS   A O    1 
ATOM   495  C CB   A LYS   A 1 19  ? 10.680 -6.181  11.459  0.74 16.09 ?  19  LYS   A CB   1 
ATOM   496  C CB   B LYS   A 1 19  ? 10.560 -6.406  11.801  0.26 14.10 ?  19  LYS   A CB   1 
ATOM   497  C CG   A LYS   A 1 19  ? 9.938  -5.266  12.418  0.74 18.09 ?  19  LYS   A CG   1 
ATOM   498  C CG   B LYS   A 1 19  ? 9.884  -5.371  12.690  0.26 15.37 ?  19  LYS   A CG   1 
ATOM   499  C CD   A LYS   A 1 19  ? 10.862 -4.927  13.586  0.74 19.22 ?  19  LYS   A CD   1 
ATOM   500  C CD   B LYS   A 1 19  ? 10.560 -5.338  14.046  0.26 16.45 ?  19  LYS   A CD   1 
ATOM   501  C CE   A LYS   A 1 19  ? 10.191 -4.086  14.655  0.74 20.64 ?  19  LYS   A CE   1 
ATOM   502  C CE   B LYS   A 1 19  ? 10.226 -4.089  14.835  0.26 17.40 ?  19  LYS   A CE   1 
ATOM   503  N NZ   A LYS   A 1 19  ? 11.123 -3.849  15.795  0.74 21.09 ?  19  LYS   A NZ   1 
ATOM   504  N NZ   B LYS   A 1 19  ? 11.109 -3.970  16.030  0.26 17.90 ?  19  LYS   A NZ   1 
ATOM   505  H H    A LYS   A 1 19  ? 11.267 -7.198  8.841   0.74 16.56 ?  19  LYS   A H    1 
ATOM   506  H H    B LYS   A 1 19  ? 11.371 -7.085  9.161   0.26 14.84 ?  19  LYS   A H    1 
ATOM   507  H HA   A LYS   A 1 19  ? 9.092  -6.965  10.390  0.74 17.93 ?  19  LYS   A HA   1 
ATOM   508  H HA   B LYS   A 1 19  ? 9.045  -6.955  10.525  0.26 15.51 ?  19  LYS   A HA   1 
ATOM   509  H HB2  A LYS   A 1 19  ? 10.888 -6.998  11.943  0.74 19.31 ?  19  LYS   A HB2  1 
ATOM   510  H HB2  B LYS   A 1 19  ? 10.528 -7.255  12.270  0.26 16.92 ?  19  LYS   A HB2  1 
ATOM   511  H HB3  A LYS   A 1 19  ? 11.506 -5.738  11.213  0.74 19.31 ?  19  LYS   A HB3  1 
ATOM   512  H HB3  B LYS   A 1 19  ? 11.480 -6.131  11.690  0.26 16.92 ?  19  LYS   A HB3  1 
ATOM   513  H HG2  A LYS   A 1 19  ? 9.695  -4.446  11.963  0.74 21.71 ?  19  LYS   A HG2  1 
ATOM   514  H HG2  B LYS   A 1 19  ? 9.968  -4.492  12.289  0.26 18.44 ?  19  LYS   A HG2  1 
ATOM   515  H HG3  A LYS   A 1 19  ? 9.152  -5.719  12.760  0.74 21.71 ?  19  LYS   A HG3  1 
ATOM   516  H HG3  B LYS   A 1 19  ? 8.953  -5.604  12.814  0.26 18.44 ?  19  LYS   A HG3  1 
ATOM   517  H HD2  A LYS   A 1 19  ? 11.159 -5.755  13.999  0.74 23.06 ?  19  LYS   A HD2  1 
ATOM   518  H HD2  B LYS   A 1 19  ? 10.283 -6.112  14.563  0.26 19.74 ?  19  LYS   A HD2  1 
ATOM   519  H HD3  A LYS   A 1 19  ? 11.626 -4.435  13.249  0.74 23.06 ?  19  LYS   A HD3  1 
ATOM   520  H HD3  B LYS   A 1 19  ? 11.517 -5.348  13.912  0.26 19.74 ?  19  LYS   A HD3  1 
ATOM   521  H HE2  A LYS   A 1 19  ? 9.943  -3.226  14.280  0.74 24.77 ?  19  LYS   A HE2  1 
ATOM   522  H HE2  B LYS   A 1 19  ? 10.362 -3.309  14.273  0.26 20.88 ?  19  LYS   A HE2  1 
ATOM   523  H HE3  A LYS   A 1 19  ? 9.408  -4.549  14.989  0.74 24.77 ?  19  LYS   A HE3  1 
ATOM   524  H HE3  B LYS   A 1 19  ? 9.305  -4.133  15.135  0.26 20.88 ?  19  LYS   A HE3  1 
ATOM   525  H HZ1  A LYS   A 1 19  ? 10.693 -3.442  16.459  0.74 25.31 ?  19  LYS   A HZ1  1 
ATOM   526  H HZ1  B LYS   A 1 19  ? 10.906 -3.233  16.485  0.26 21.48 ?  19  LYS   A HZ1  1 
ATOM   527  H HZ2  A LYS   A 1 19  ? 11.443 -4.626  16.091  0.74 25.31 ?  19  LYS   A HZ2  1 
ATOM   528  H HZ2  B LYS   A 1 19  ? 11.000 -4.677  16.559  0.26 21.48 ?  19  LYS   A HZ2  1 
ATOM   529  H HZ3  A LYS   A 1 19  ? 11.801 -3.339  15.533  0.74 25.31 ?  19  LYS   A HZ3  1 
ATOM   530  H HZ3  B LYS   A 1 19  ? 11.961 -3.927  15.775  0.26 21.48 ?  19  LYS   A HZ3  1 
ATOM   531  N N    A ASN   A 1 20  ? 8.552  -4.717  9.433   0.74 15.62 ?  20  ASN   A N    1 
ATOM   532  N N    B ASN   A 1 20  ? 8.639  -4.623  9.838   0.26 12.16 ?  20  ASN   A N    1 
ATOM   533  C CA   A ASN   A 1 20  ? 8.304  -3.397  8.850   0.74 16.96 ?  20  ASN   A CA   1 
ATOM   534  C CA   B ASN   A 1 20  ? 8.441  -3.277  9.315   0.26 12.15 ?  20  ASN   A CA   1 
ATOM   535  C C    A ASN   A 1 20  ? 8.914  -2.369  9.792   0.74 17.77 ?  20  ASN   A C    1 
ATOM   536  C C    B ASN   A 1 20  ? 9.094  -2.305  10.286  0.26 11.93 ?  20  ASN   A C    1 
ATOM   537  O O    A ASN   A 1 20  ? 8.344  -2.059  10.841  0.74 19.03 ?  20  ASN   A O    1 
ATOM   538  O O    B ASN   A 1 20  ? 8.627  -2.132  11.415  0.26 11.99 ?  20  ASN   A O    1 
ATOM   539  C CB   A ASN   A 1 20  ? 6.807  -3.174  8.656   0.74 17.95 ?  20  ASN   A CB   1 
ATOM   540  C CB   B ASN   A 1 20  ? 6.954  -2.982  9.132   0.26 12.69 ?  20  ASN   A CB   1 
ATOM   541  C CG   A ASN   A 1 20  ? 6.461  -1.742  8.239   0.74 18.50 ?  20  ASN   A CG   1 
ATOM   542  C CG   B ASN   A 1 20  ? 6.669  -1.507  8.873   0.26 13.32 ?  20  ASN   A CG   1 
ATOM   543  O OD1  A ASN   A 1 20  ? 5.483  -1.162  8.724   0.74 19.53 ?  20  ASN   A OD1  1 
ATOM   544  O OD1  B ASN   A 1 20  ? 5.803  -0.912  9.514   0.26 14.17 ?  20  ASN   A OD1  1 
ATOM   545  N ND2  A ASN   A 1 20  ? 7.254  -1.175  7.340   0.74 19.13 ?  20  ASN   A ND2  1 
ATOM   546  N ND2  B ASN   A 1 20  ? 7.399  -0.912  7.939   0.26 13.15 ?  20  ASN   A ND2  1 
ATOM   547  H H    A ASN   A 1 20  ? 7.879  -5.070  9.840   0.74 18.74 ?  20  ASN   A H    1 
ATOM   548  H H    B ASN   A 1 20  ? 7.950  -4.952  10.229  0.26 14.59 ?  20  ASN   A H    1 
ATOM   549  H HA   A ASN   A 1 20  ? 8.745  -3.342  7.991   0.74 20.35 ?  20  ASN   A HA   1 
ATOM   550  H HA   B ASN   A 1 20  ? 8.877  -3.197  8.454   0.26 14.58 ?  20  ASN   A HA   1 
ATOM   551  H HB2  A ASN   A 1 20  ? 6.487  -3.775  7.964   0.74 21.54 ?  20  ASN   A HB2  1 
ATOM   552  H HB2  B ASN   A 1 20  ? 6.626  -3.489  8.369   0.26 15.23 ?  20  ASN   A HB2  1 
ATOM   553  H HB3  A ASN   A 1 20  ? 6.353  -3.370  9.493   0.74 21.54 ?  20  ASN   A HB3  1 
ATOM   554  H HB3  B ASN   A 1 20  ? 6.477  -3.247  9.932   0.26 15.23 ?  20  ASN   A HB3  1 
ATOM   555  H HD21 A ASN   A 1 20  ? 7.093  -0.377  7.081   0.74 22.96 ?  20  ASN   A HD21 1 
ATOM   556  H HD21 B ASN   A 1 20  ? 7.267  -0.082  7.759   0.26 15.78 ?  20  ASN   A HD21 1 
ATOM   557  H HD22 A ASN   A 1 20  ? 7.920  -1.613  7.017   0.74 22.96 ?  20  ASN   A HD22 1 
ATOM   558  H HD22 B ASN   A 1 20  ? 7.998  -1.356  7.512   0.26 15.78 ?  20  ASN   A HD22 1 
ATOM   559  N N    A ALA   A 1 21  ? 10.084 -1.841  9.426   0.74 17.61 ?  21  ALA   A N    1 
ATOM   560  N N    B ALA   A 1 21  ? 10.202 -1.707  9.864   0.26 12.82 ?  21  ALA   A N    1 
ATOM   561  C CA   A ALA   A 1 21  ? 10.813 -0.948  10.319  0.74 17.52 ?  21  ALA   A CA   1 
ATOM   562  C CA   B ALA   A 1 21  ? 10.891 -0.734  10.695  0.26 13.65 ?  21  ALA   A CA   1 
ATOM   563  C C    A ALA   A 1 21  ? 11.766 -0.069  9.524   0.74 16.47 ?  21  ALA   A C    1 
ATOM   564  C C    B ALA   A 1 21  ? 11.931 -0.027  9.845   0.26 13.71 ?  21  ALA   A C    1 
ATOM   565  O O    A ALA   A 1 21  ? 12.193 -0.423  8.422   0.74 16.08 ?  21  ALA   A O    1 
ATOM   566  O O    B ALA   A 1 21  ? 12.470 -0.605  8.897   0.26 13.50 ?  21  ALA   A O    1 
ATOM   567  C CB   A ALA   A 1 21  ? 11.582 -1.729  11.390  0.74 18.63 ?  21  ALA   A CB   1 
ATOM   568  C CB   B ALA   A 1 21  ? 11.553 -1.408  11.901  0.26 14.44 ?  21  ALA   A CB   1 
ATOM   569  H H    A ALA   A 1 21  ? 10.465 -1.978  8.665   0.74 21.13 ?  21  ALA   A H    1 
ATOM   570  H H    B ALA   A 1 21  ? 10.583 -1.857  9.107   0.26 15.39 ?  21  ALA   A H    1 
ATOM   571  H HA   A ALA   A 1 21  ? 10.174 -0.375  10.767  0.74 21.03 ?  21  ALA   A HA   1 
ATOM   572  H HA   B ALA   A 1 21  ? 10.260 -0.073  11.017  0.26 16.38 ?  21  ALA   A HA   1 
ATOM   573  H HB1  A ALA   A 1 21  ? 11.999 -1.099  11.993  0.74 22.35 ?  21  ALA   A HB1  1 
ATOM   574  H HB1  B ALA   A 1 21  ? 11.996 -0.733  12.434  0.26 17.32 ?  21  ALA   A HB1  1 
ATOM   575  H HB2  A ALA   A 1 21  ? 10.952 -2.287  11.885  0.74 22.35 ?  21  ALA   A HB2  1 
ATOM   576  H HB2  B ALA   A 1 21  ? 10.866 -1.850  12.428  0.26 17.32 ?  21  ALA   A HB2  1 
ATOM   577  H HB3  A ALA   A 1 21  ? 12.247 -2.286  10.965  0.74 22.35 ?  21  ALA   A HB3  1 
ATOM   578  H HB3  B ALA   A 1 21  ? 12.195 -2.061  11.583  0.26 17.32 ?  21  ALA   A HB3  1 
ATOM   579  N N    A ASP   A 1 22  ? 12.083 1.087   10.115  0.74 16.52 ?  22  ASP   A N    1 
ATOM   580  N N    B ASP   A 1 22  ? 12.168 1.240   10.170  0.26 14.16 ?  22  ASP   A N    1 
ATOM   581  C CA   A ASP   A 1 22  ? 13.117 1.988   9.621   0.74 16.45 ?  22  ASP   A CA   1 
ATOM   582  C CA   B ASP   A 1 22  ? 13.294 1.968   9.605   0.26 14.70 ?  22  ASP   A CA   1 
ATOM   583  C C    A ASP   A 1 22  ? 14.452 1.507   10.177  0.74 15.08 ?  22  ASP   A C    1 
ATOM   584  C C    B ASP   A 1 22  ? 14.579 1.387   10.178  0.26 14.36 ?  22  ASP   A C    1 
ATOM   585  O O    A ASP   A 1 22  ? 14.651 1.508   11.396  0.74 16.37 ?  22  ASP   A O    1 
ATOM   586  O O    B ASP   A 1 22  ? 14.785 1.404   11.396  0.26 14.87 ?  22  ASP   A O    1 
ATOM   587  C CB   A ASP   A 1 22  ? 12.807 3.404   10.111  0.74 18.41 ?  22  ASP   A CB   1 
ATOM   588  C CB   B ASP   A 1 22  ? 13.177 3.445   9.971   0.26 15.79 ?  22  ASP   A CB   1 
ATOM   589  C CG   A ASP   A 1 22  ? 13.824 4.445   9.642   0.74 20.22 ?  22  ASP   A CG   1 
ATOM   590  C CG   B ASP   A 1 22  ? 14.333 4.274   9.452   0.26 16.82 ?  22  ASP   A CG   1 
ATOM   591  O OD1  A ASP   A 1 22  ? 14.897 4.081   9.123   0.74 20.35 ?  22  ASP   A OD1  1 
ATOM   592  O OD1  B ASP   A 1 22  ? 15.047 3.802   8.542   0.26 16.88 ?  22  ASP   A OD1  1 
ATOM   593  O OD2  A ASP   A 1 22  ? 13.544 5.651   9.805   0.74 21.93 -1 22  ASP   A OD2  1 
ATOM   594  O OD2  B ASP   A 1 22  ? 14.530 5.396   9.965   0.26 17.71 -1 22  ASP   A OD2  1 
ATOM   595  H H    A ASP   A 1 22  ? 11.692 1.368   10.830  0.74 19.83 ?  22  ASP   A H    1 
ATOM   596  H H    B ASP   A 1 22  ? 11.676 1.704   10.703  0.26 16.99 ?  22  ASP   A H    1 
ATOM   597  H HA   A ASP   A 1 22  ? 13.144 1.968   8.655   0.74 19.74 ?  22  ASP   A HA   1 
ATOM   598  H HA   B ASP   A 1 22  ? 13.300 1.872   8.636   0.26 17.64 ?  22  ASP   A HA   1 
ATOM   599  H HB2  A ASP   A 1 22  ? 11.926 3.654   9.789   0.74 22.09 ?  22  ASP   A HB2  1 
ATOM   600  H HB2  B ASP   A 1 22  ? 12.352 3.797   9.602   0.26 18.95 ?  22  ASP   A HB2  1 
ATOM   601  H HB3  A ASP   A 1 22  ? 12.813 3.402   11.082  0.74 22.09 ?  22  ASP   A HB3  1 
ATOM   602  H HB3  B ASP   A 1 22  ? 13.174 3.528   10.935  0.26 18.95 ?  22  ASP   A HB3  1 
ATOM   603  N N    A ILE   A 1 23  ? 15.355 1.080   9.288   0.74 14.39 ?  23  ILE   A N    1 
ATOM   604  N N    B ILE   A 1 23  ? 15.437 0.857   9.304   0.26 14.18 ?  23  ILE   A N    1 
ATOM   605  C CA   A ILE   A 1 23  ? 16.613 0.476   9.721   0.74 13.84 ?  23  ILE   A CA   1 
ATOM   606  C CA   B ILE   A 1 23  ? 16.685 0.258   9.768   0.26 14.47 ?  23  ILE   A CA   1 
ATOM   607  C C    A ILE   A 1 23  ? 17.415 1.426   10.603  0.74 13.66 ?  23  ILE   A C    1 
ATOM   608  C C    B ILE   A 1 23  ? 17.508 1.270   10.551  0.26 14.79 ?  23  ILE   A C    1 
ATOM   609  O O    A ILE   A 1 23  ? 18.130 0.980   11.508  0.74 14.38 ?  23  ILE   A O    1 
ATOM   610  O O    B ILE   A 1 23  ? 18.276 0.899   11.447  0.26 14.94 ?  23  ILE   A O    1 
ATOM   611  C CB   A ILE   A 1 23  ? 17.411 -0.045  8.503   0.74 13.18 ?  23  ILE   A CB   1 
ATOM   612  C CB   B ILE   A 1 23  ? 17.464 -0.338  8.578   0.26 14.26 ?  23  ILE   A CB   1 
ATOM   613  C CG1  A ILE   A 1 23  ? 18.551 -0.962  8.952   0.74 13.45 ?  23  ILE   A CG1  1 
ATOM   614  C CG1  B ILE   A 1 23  ? 18.716 -1.069  9.070   0.26 14.12 ?  23  ILE   A CG1  1 
ATOM   615  C CG2  A ILE   A 1 23  ? 17.908 1.105   7.635   0.74 13.05 ?  23  ILE   A CG2  1 
ATOM   616  C CG2  B ILE   A 1 23  ? 17.813 0.747   7.570   0.26 14.30 ?  23  ILE   A CG2  1 
ATOM   617  C CD1  A ILE   A 1 23  ? 19.272 -1.650  7.805   0.74 13.67 ?  23  ILE   A CD1  1 
ATOM   618  C CD1  B ILE   A 1 23  ? 19.459 -1.807  7.983   0.26 14.00 ?  23  ILE   A CD1  1 
ATOM   619  H H    A ILE   A 1 23  ? 15.256 1.126   8.442   0.74 17.27 ?  23  ILE   A H    1 
ATOM   620  H H    B ILE   A 1 23  ? 15.322 0.838   8.454   0.26 17.02 ?  23  ILE   A H    1 
ATOM   621  H HA   A ILE   A 1 23  ? 16.404 -0.294  10.270  0.74 16.61 ?  23  ILE   A HA   1 
ATOM   622  H HA   B ILE   A 1 23  ? 16.472 -0.471  10.369  0.26 17.37 ?  23  ILE   A HA   1 
ATOM   623  H HB   A ILE   A 1 23  ? 16.802 -0.575  7.967   0.74 15.82 ?  23  ILE   A HB   1 
ATOM   624  H HB   B ILE   A 1 23  ? 16.893 -0.983  8.137   0.26 17.12 ?  23  ILE   A HB   1 
ATOM   625  H HG12 A ILE   A 1 23  ? 19.205 -0.438  9.438   0.74 16.14 ?  23  ILE   A HG12 1 
ATOM   626  H HG12 B ILE   A 1 23  ? 19.328 -0.425  9.456   0.26 16.95 ?  23  ILE   A HG12 1 
ATOM   627  H HG13 A ILE   A 1 23  ? 18.190 -1.654  9.528   0.74 16.14 ?  23  ILE   A HG13 1 
ATOM   628  H HG13 B ILE   A 1 23  ? 18.455 -1.719  9.741   0.26 16.95 ?  23  ILE   A HG13 1 
ATOM   629  H HG21 A ILE   A 1 23  ? 18.258 0.745   6.804   0.74 15.67 ?  23  ILE   A HG21 1 
ATOM   630  H HG21 B ILE   A 1 23  ? 18.206 0.331   6.788   0.26 17.16 ?  23  ILE   A HG21 1 
ATOM   631  H HG22 A ILE   A 1 23  ? 17.167 1.703   7.447   0.74 15.67 ?  23  ILE   A HG22 1 
ATOM   632  H HG22 B ILE   A 1 23  ? 17.003 1.218   7.319   0.26 17.16 ?  23  ILE   A HG22 1 
ATOM   633  H HG23 A ILE   A 1 23  ? 18.606 1.583   8.109   0.74 15.67 ?  23  ILE   A HG23 1 
ATOM   634  H HG23 B ILE   A 1 23  ? 18.443 1.362   7.973   0.26 17.16 ?  23  ILE   A HG23 1 
ATOM   635  H HD11 A ILE   A 1 23  ? 19.919 -2.275  8.168   0.74 16.40 ?  23  ILE   A HD11 1 
ATOM   636  H HD11 B ILE   A 1 23  ? 20.164 -2.336  8.388   0.26 16.80 ?  23  ILE   A HD11 1 
ATOM   637  H HD12 A ILE   A 1 23  ? 18.622 -2.124  7.263   0.74 16.40 ?  23  ILE   A HD12 1 
ATOM   638  H HD12 B ILE   A 1 23  ? 18.838 -2.386  7.515   0.26 16.80 ?  23  ILE   A HD12 1 
ATOM   639  H HD13 A ILE   A 1 23  ? 19.724 -0.980  7.269   0.74 16.40 ?  23  ILE   A HD13 1 
ATOM   640  H HD13 B ILE   A 1 23  ? 19.841 -1.162  7.368   0.26 16.80 ?  23  ILE   A HD13 1 
ATOM   641  N N    A VAL   A 1 24  ? 17.296 2.740   10.380  0.74 14.26 ?  24  VAL   A N    1 
ATOM   642  N N    B VAL   A 1 24  ? 17.363 2.557   10.232  0.26 15.37 ?  24  VAL   A N    1 
ATOM   643  C CA   A VAL   A 1 24  ? 17.984 3.710   11.234  0.74 15.91 ?  24  VAL   A CA   1 
ATOM   644  C CA   B VAL   A 1 24  ? 18.067 3.604   10.969  0.26 15.98 ?  24  VAL   A CA   1 
ATOM   645  C C    A VAL   A 1 24  ? 17.479 3.604   12.668  0.74 17.05 ?  24  VAL   A C    1 
ATOM   646  C C    B VAL   A 1 24  ? 17.598 3.638   12.419  0.26 16.84 ?  24  VAL   A C    1 
ATOM   647  O O    A VAL   A 1 24  ? 18.263 3.533   13.624  0.74 17.27 ?  24  VAL   A O    1 
ATOM   648  O O    B VAL   A 1 24  ? 18.397 3.522   13.356  0.26 17.13 ?  24  VAL   A O    1 
ATOM   649  C CB   A VAL   A 1 24  ? 17.810 5.136   10.678  0.74 16.89 ?  24  VAL   A CB   1 
ATOM   650  C CB   B VAL   A 1 24  ? 17.877 4.965   10.275  0.26 16.02 ?  24  VAL   A CB   1 
ATOM   651  C CG1  A VAL   A 1 24  ? 18.326 6.175   11.672  0.74 17.66 ?  24  VAL   A CG1  1 
ATOM   652  C CG1  B VAL   A 1 24  ? 18.584 6.057   11.050  0.26 16.38 ?  24  VAL   A CG1  1 
ATOM   653  C CG2  A VAL   A 1 24  ? 18.513 5.270   9.336   0.74 17.70 ?  24  VAL   A CG2  1 
ATOM   654  C CG2  B VAL   A 1 24  ? 18.379 4.904   8.836   0.26 15.70 ?  24  VAL   A CG2  1 
ATOM   655  H H    A VAL   A 1 24  ? 16.834 3.091   9.747   0.74 17.11 ?  24  VAL   A H    1 
ATOM   656  H H    B VAL   A 1 24  ? 16.872 2.848   9.591   0.26 18.44 ?  24  VAL   A H    1 
ATOM   657  H HA   A VAL   A 1 24  ? 18.934 3.511   11.239  0.74 19.10 ?  24  VAL   A HA   1 
ATOM   658  H HA   B VAL   A 1 24  ? 19.015 3.405   10.972  0.26 19.18 ?  24  VAL   A HA   1 
ATOM   659  H HB   A VAL   A 1 24  ? 16.865 5.305   10.533  0.74 20.27 ?  24  VAL   A HB   1 
ATOM   660  H HB   B VAL   A 1 24  ? 16.931 5.178   10.250  0.26 19.22 ?  24  VAL   A HB   1 
ATOM   661  H HG11 A VAL   A 1 24  ? 18.453 7.016   11.206  0.74 21.19 ?  24  VAL   A HG11 1 
ATOM   662  H HG11 B VAL   A 1 24  ? 18.632 6.850   10.496  0.26 19.66 ?  24  VAL   A HG11 1 
ATOM   663  H HG12 A VAL   A 1 24  ? 17.676 6.284   12.380  0.74 21.19 ?  24  VAL   A HG12 1 
ATOM   664  H HG12 B VAL   A 1 24  ? 18.079 6.247   11.856  0.26 19.66 ?  24  VAL   A HG12 1 
ATOM   665  H HG13 A VAL   A 1 24  ? 19.171 5.867   12.034  0.74 21.19 ?  24  VAL   A HG13 1 
ATOM   666  H HG13 B VAL   A 1 24  ? 19.475 5.754   11.276  0.26 19.66 ?  24  VAL   A HG13 1 
ATOM   667  H HG21 A VAL   A 1 24  ? 18.396 6.174   9.004   0.74 21.23 ?  24  VAL   A HG21 1 
ATOM   668  H HG21 B VAL   A 1 24  ? 18.201 5.754   8.406   0.26 18.84 ?  24  VAL   A HG21 1 
ATOM   669  H HG22 A VAL   A 1 24  ? 19.459 5.083   9.454   0.74 21.23 ?  24  VAL   A HG22 1 
ATOM   670  H HG22 B VAL   A 1 24  ? 19.332 4.732   8.842   0.26 18.84 ?  24  VAL   A HG22 1 
ATOM   671  H HG23 A VAL   A 1 24  ? 18.128 4.636   8.710   0.74 21.23 ?  24  VAL   A HG23 1 
ATOM   672  H HG23 B VAL   A 1 24  ? 17.916 4.193   8.364   0.26 18.84 ?  24  VAL   A HG23 1 
ATOM   673  N N    A GLU   A 1 25  ? 16.156 3.586   12.837  0.74 18.43 ?  25  GLU   A N    1 
ATOM   674  N N    B GLU   A 1 25  ? 16.287 3.800   12.624  0.26 17.72 ?  25  GLU   A N    1 
ATOM   675  C CA   A GLU   A 1 25  ? 15.582 3.505   14.176  0.74 20.25 ?  25  GLU   A CA   1 
ATOM   676  C CA   B GLU   A 1 25  ? 15.748 3.831   13.980  0.26 18.92 ?  25  GLU   A CA   1 
ATOM   677  C C    A GLU   A 1 25  ? 15.817 2.132   14.797  0.74 19.45 ?  25  GLU   A C    1 
ATOM   678  C C    B GLU   A 1 25  ? 15.919 2.491   14.683  0.26 18.38 ?  25  GLU   A C    1 
ATOM   679  O O    A GLU   A 1 25  ? 16.072 2.027   16.003  0.74 19.80 ?  25  GLU   A O    1 
ATOM   680  O O    B GLU   A 1 25  ? 16.130 2.455   15.901  0.26 18.48 ?  25  GLU   A O    1 
ATOM   681  C CB   A GLU   A 1 25  ? 14.092 3.855   14.132  0.74 23.08 ?  25  GLU   A CB   1 
ATOM   682  C CB   B GLU   A 1 25  ? 14.272 4.232   13.951  0.26 20.91 ?  25  GLU   A CB   1 
ATOM   683  C CG   A GLU   A 1 25  ? 13.820 5.293   13.704  0.74 26.15 ?  25  GLU   A CG   1 
ATOM   684  C CG   B GLU   A 1 25  ? 14.027 5.683   13.564  0.26 22.80 ?  25  GLU   A CG   1 
ATOM   685  C CD   A GLU   A 1 25  ? 14.573 6.303   14.549  0.74 28.94 ?  25  GLU   A CD   1 
ATOM   686  C CD   B GLU   A 1 25  ? 14.411 6.661   14.660  0.26 24.48 ?  25  GLU   A CD   1 
ATOM   687  O OE1  A GLU   A 1 25  ? 14.564 6.164   15.791  0.74 30.00 ?  25  GLU   A OE1  1 
ATOM   688  O OE1  B GLU   A 1 25  ? 14.815 6.208   15.752  0.26 25.23 ?  25  GLU   A OE1  1 
ATOM   689  O OE2  A GLU   A 1 25  ? 15.185 7.226   13.971  0.74 29.98 -1 25  GLU   A OE2  1 
ATOM   690  O OE2  B GLU   A 1 25  ? 14.308 7.884   14.428  0.26 25.00 -1 25  GLU   A OE2  1 
ATOM   691  H H    A GLU   A 1 25  ? 15.579 3.622   12.201  0.74 22.12 ?  25  GLU   A H    1 
ATOM   692  H H    B GLU   A 1 25  ? 15.698 3.891   12.005  0.26 21.26 ?  25  GLU   A H    1 
ATOM   693  H HA   A GLU   A 1 25  ? 16.021 4.155   14.743  0.74 24.30 ?  25  GLU   A HA   1 
ATOM   694  H HA   B GLU   A 1 25  ? 16.227 4.493   14.497  0.26 22.71 ?  25  GLU   A HA   1 
ATOM   695  H HB2  A GLU   A 1 25  ? 13.645 3.273   13.498  0.74 27.70 ?  25  GLU   A HB2  1 
ATOM   696  H HB2  B GLU   A 1 25  ? 13.810 3.673   13.306  0.26 25.09 ?  25  GLU   A HB2  1 
ATOM   697  H HB3  A GLU   A 1 25  ? 13.710 3.736   15.016  0.74 27.70 ?  25  GLU   A HB3  1 
ATOM   698  H HB3  B GLU   A 1 25  ? 13.892 4.092   14.833  0.26 25.09 ?  25  GLU   A HB3  1 
ATOM   699  H HG2  A GLU   A 1 25  ? 14.099 5.410   12.783  0.74 31.38 ?  25  GLU   A HG2  1 
ATOM   700  H HG2  B GLU   A 1 25  ? 14.562 5.895   12.785  0.26 27.36 ?  25  GLU   A HG2  1 
ATOM   701  H HG3  A GLU   A 1 25  ? 12.870 5.478   13.790  0.74 31.38 ?  25  GLU   A HG3  1 
ATOM   702  H HG3  B GLU   A 1 25  ? 13.085 5.799   13.362  0.26 27.36 ?  25  GLU   A HG3  1 
ATOM   703  N N    A GLU   A 1 26  ? 15.752 1.070   13.992  0.74 18.79 ?  26  GLU   A N    1 
ATOM   704  N N    B GLU   A 1 26  ? 15.833 1.386   13.938  0.26 17.92 ?  26  GLU   A N    1 
ATOM   705  C CA   A GLU   A 1 26  ? 16.076 -0.258  14.506  0.74 18.42 ?  26  GLU   A CA   1 
ATOM   706  C CA   B GLU   A 1 26  ? 16.039 0.068   14.531  0.26 17.75 ?  26  GLU   A CA   1 
ATOM   707  C C    A GLU   A 1 26  ? 17.510 -0.309  15.014  0.74 16.84 ?  26  GLU   A C    1 
ATOM   708  C C    B GLU   A 1 26  ? 17.452 -0.061  15.086  0.26 16.64 ?  26  GLU   A C    1 
ATOM   709  O O    A GLU   A 1 26  ? 17.778 -0.872  16.081  0.74 16.87 ?  26  GLU   A O    1 
ATOM   710  O O    B GLU   A 1 26  ? 17.649 -0.465  16.238  0.26 16.52 ?  26  GLU   A O    1 
ATOM   711  C CB   A GLU   A 1 26  ? 15.884 -1.312  13.417  0.74 19.96 ?  26  GLU   A CB   1 
ATOM   712  C CB   B GLU   A 1 26  ? 15.786 -1.012  13.478  0.26 18.99 ?  26  GLU   A CB   1 
ATOM   713  C CG   A GLU   A 1 26  ? 14.485 -1.868  13.283  0.74 21.93 ?  26  GLU   A CG   1 
ATOM   714  C CG   B GLU   A 1 26  ? 14.467 -1.741  13.626  0.26 20.83 ?  26  GLU   A CG   1 
ATOM   715  C CD   A GLU   A 1 26  ? 14.028 -2.643  14.511  0.74 22.66 ?  26  GLU   A CD   1 
ATOM   716  C CD   B GLU   A 1 26  ? 14.484 -2.761  14.750  0.26 22.23 ?  26  GLU   A CD   1 
ATOM   717  O OE1  A GLU   A 1 26  ? 14.457 -3.802  14.753  0.74 22.79 ?  26  GLU   A OE1  1 
ATOM   718  O OE1  B GLU   A 1 26  ? 15.573 -3.035  15.293  0.26 22.85 ?  26  GLU   A OE1  1 
ATOM   719  O OE2  A GLU   A 1 26  ? 13.215 -2.073  15.242  0.74 23.43 -1 26  GLU   A OE2  1 
ATOM   720  O OE2  B GLU   A 1 26  ? 13.403 -3.283  15.095  0.26 22.95 -1 26  GLU   A OE2  1 
ATOM   721  H H    A GLU   A 1 26  ? 15.531 1.093   13.163  0.74 22.55 ?  26  GLU   A H    1 
ATOM   722  H H    B GLU   A 1 26  ? 15.664 1.375   13.094  0.26 21.51 ?  26  GLU   A H    1 
ATOM   723  H HA   A GLU   A 1 26  ? 15.488 -0.465  15.246  0.74 22.10 ?  26  GLU   A HA   1 
ATOM   724  H HA   B GLU   A 1 26  ? 15.410 -0.063  15.256  0.26 21.30 ?  26  GLU   A HA   1 
ATOM   725  H HB2  A GLU   A 1 26  ? 16.123 -0.920  12.563  0.74 23.95 ?  26  GLU   A HB2  1 
ATOM   726  H HB2  B GLU   A 1 26  ? 15.792 -0.602  12.599  0.26 22.79 ?  26  GLU   A HB2  1 
ATOM   727  H HB3  A GLU   A 1 26  ? 16.473 -2.059  13.608  0.74 23.95 ?  26  GLU   A HB3  1 
ATOM   728  H HB3  B GLU   A 1 26  ? 16.495 -1.672  13.531  0.26 22.79 ?  26  GLU   A HB3  1 
ATOM   729  H HG2  A GLU   A 1 26  ? 13.871 -1.125  13.128  0.74 26.32 ?  26  GLU   A HG2  1 
ATOM   730  H HG2  B GLU   A 1 26  ? 13.775 -1.099  13.834  0.26 25.00 ?  26  GLU   A HG2  1 
ATOM   731  H HG3  A GLU   A 1 26  ? 14.450 -2.482  12.540  0.74 26.32 ?  26  GLU   A HG3  1 
ATOM   732  H HG3  B GLU   A 1 26  ? 14.263 -2.191  12.789  0.26 25.00 ?  26  GLU   A HG3  1 
ATOM   733  N N    . ALA   A 1 27  ? 18.449 0.275   14.266  1.00 15.58 ?  27  ALA   A N    1 
ATOM   734  C CA   . ALA   A 1 27  ? 19.844 0.224   14.698  1.00 15.45 ?  27  ALA   A CA   1 
ATOM   735  C C    . ALA   A 1 27  ? 20.061 1.039   15.967  1.00 17.10 ?  27  ALA   A C    1 
ATOM   736  O O    . ALA   A 1 27  ? 20.737 0.585   16.897  1.00 16.97 ?  27  ALA   A O    1 
ATOM   737  C CB   . ALA   A 1 27  ? 20.761 0.716   13.576  1.00 15.00 ?  27  ALA   A CB   1 
ATOM   738  H H    A ALA   A 1 27  ? 18.309 0.696   13.527  0.74 18.69 ?  27  ALA   A H    1 
ATOM   739  H H    B ALA   A 1 27  ? 18.342 0.549   13.457  0.26 18.69 ?  27  ALA   A H    1 
ATOM   740  H HA   . ALA   A 1 27  ? 20.074 -0.693  14.895  1.00 18.55 ?  27  ALA   A HA   1 
ATOM   741  H HB1  . ALA   A 1 27  ? 21.681 0.674   13.884  1.00 18.00 ?  27  ALA   A HB1  1 
ATOM   742  H HB2  . ALA   A 1 27  ? 20.645 0.143   12.803  1.00 18.00 ?  27  ALA   A HB2  1 
ATOM   743  H HB3  . ALA   A 1 27  ? 20.529 1.629   13.353  1.00 18.00 ?  27  ALA   A HB3  1 
ATOM   744  N N    . LYS   A 1 28  ? 19.484 2.242   16.034  1.00 19.66 ?  28  LYS   A N    1 
ATOM   745  C CA   . LYS   A 1 28  ? 19.635 3.061   17.233  1.00 23.43 ?  28  LYS   A CA   1 
ATOM   746  C C    . LYS   A 1 28  ? 19.096 2.356   18.472  1.00 24.92 ?  28  LYS   A C    1 
ATOM   747  O O    . LYS   A 1 28  ? 19.648 2.518   19.566  1.00 26.18 ?  28  LYS   A O    1 
ATOM   748  C CB   . LYS   A 1 28  ? 18.961 4.423   17.041  1.00 25.96 ?  28  LYS   A CB   1 
ATOM   749  C CG   . LYS   A 1 28  ? 19.732 5.350   16.115  1.00 28.46 ?  28  LYS   A CG   1 
ATOM   750  C CD   . LYS   A 1 28  ? 19.280 6.796   16.240  1.00 31.39 ?  28  LYS   A CD   1 
ATOM   751  C CE   . LYS   A 1 28  ? 17.957 7.032   15.540  1.00 33.71 ?  28  LYS   A CE   1 
ATOM   752  N NZ   . LYS   A 1 28  ? 17.621 8.483   15.492  1.00 35.26 ?  28  LYS   A NZ   1 
ATOM   753  H H    . LYS   A 1 28  ? 19.013 2.601   15.413  1.00 23.60 ?  28  LYS   A H    1 
ATOM   754  H HA   . LYS   A 1 28  ? 20.576 3.226   17.387  1.00 28.11 ?  28  LYS   A HA   1 
ATOM   755  H HB2  . LYS   A 1 28  ? 18.080 4.292   16.660  1.00 31.15 ?  28  LYS   A HB2  1 
ATOM   756  H HB3  . LYS   A 1 28  ? 18.885 4.866   17.903  1.00 31.15 ?  28  LYS   A HB3  1 
ATOM   757  H HG2  . LYS   A 1 28  ? 20.675 5.311   16.336  1.00 34.15 ?  28  LYS   A HG2  1 
ATOM   758  H HG3  . LYS   A 1 28  ? 19.591 5.071   15.197  1.00 34.15 ?  28  LYS   A HG3  1 
ATOM   759  H HD2  . LYS   A 1 28  ? 19.170 7.019   17.179  1.00 37.67 ?  28  LYS   A HD2  1 
ATOM   760  H HD3  . LYS   A 1 28  ? 19.945 7.375   15.836  1.00 37.67 ?  28  LYS   A HD3  1 
ATOM   761  H HE2  . LYS   A 1 28  ? 18.014 6.702   14.630  1.00 40.46 ?  28  LYS   A HE2  1 
ATOM   762  H HE3  . LYS   A 1 28  ? 17.253 6.572   16.022  1.00 40.46 ?  28  LYS   A HE3  1 
ATOM   763  H HZ1  . LYS   A 1 28  ? 16.843 8.601   15.077  1.00 42.32 ?  28  LYS   A HZ1  1 
ATOM   764  H HZ2  . LYS   A 1 28  ? 17.562 8.809   16.318  1.00 42.32 ?  28  LYS   A HZ2  1 
ATOM   765  H HZ3  . LYS   A 1 28  ? 18.255 8.927   15.051  1.00 42.32 ?  28  LYS   A HZ3  1 
ATOM   766  N N    A LYS   A 1 29  ? 18.031 1.569   18.322  0.74 24.92 ?  29  LYS   A N    1 
ATOM   767  N N    B LYS   A 1 29  ? 18.033 1.565   18.321  0.26 25.91 ?  29  LYS   A N    1 
ATOM   768  C CA   A LYS   A 1 29  ? 17.435 0.880   19.463  0.74 26.43 ?  29  LYS   A CA   1 
ATOM   769  C CA   B LYS   A 1 29  ? 17.432 0.880   19.461  0.26 27.16 ?  29  LYS   A CA   1 
ATOM   770  C C    A LYS   A 1 29  ? 18.240 -0.356  19.851  0.74 25.73 ?  29  LYS   A C    1 
ATOM   771  C C    B LYS   A 1 29  ? 18.231 -0.359  19.851  0.26 26.10 ?  29  LYS   A C    1 
ATOM   772  O O    A LYS   A 1 29  ? 18.543 -0.566  21.032  0.74 26.49 ?  29  LYS   A O    1 
ATOM   773  O O    B LYS   A 1 29  ? 18.530 -0.570  21.032  0.26 26.49 ?  29  LYS   A O    1 
ATOM   774  C CB   A LYS   A 1 29  ? 15.994 0.485   19.128  0.74 29.11 ?  29  LYS   A CB   1 
ATOM   775  C CB   B LYS   A 1 29  ? 15.990 0.493   19.125  0.26 29.30 ?  29  LYS   A CB   1 
ATOM   776  C CG   A LYS   A 1 29  ? 15.252 -0.220  20.254  0.74 31.97 ?  29  LYS   A CG   1 
ATOM   777  C CG   B LYS   A 1 29  ? 15.219 -0.144  20.273  0.26 31.23 ?  29  LYS   A CG   1 
ATOM   778  C CD   A LYS   A 1 29  ? 14.842 0.754   21.346  0.74 34.65 ?  29  LYS   A CD   1 
ATOM   779  C CD   B LYS   A 1 29  ? 14.841 0.883   21.326  0.26 32.87 ?  29  LYS   A CD   1 
ATOM   780  C CE   A LYS   A 1 29  ? 13.977 0.076   22.397  0.74 36.48 ?  29  LYS   A CE   1 
ATOM   781  C CE   B LYS   A 1 29  ? 13.944 0.275   22.393  0.26 33.99 ?  29  LYS   A CE   1 
ATOM   782  N NZ   A LYS   A 1 29  ? 13.526 1.031   23.445  0.74 37.52 ?  29  LYS   A NZ   1 
ATOM   783  N NZ   B LYS   A 1 29  ? 13.525 1.278   23.410  0.26 34.57 ?  29  LYS   A NZ   1 
ATOM   784  H H    A LYS   A 1 29  ? 17.637 1.420   17.573  0.74 29.90 ?  29  LYS   A H    1 
ATOM   785  H H    B LYS   A 1 29  ? 17.645 1.410   17.570  0.26 31.10 ?  29  LYS   A H    1 
ATOM   786  H HA   A LYS   A 1 29  ? 17.412 1.479   20.224  0.74 31.71 ?  29  LYS   A HA   1 
ATOM   787  H HA   B LYS   A 1 29  ? 17.414 1.481   20.222  0.26 32.59 ?  29  LYS   A HA   1 
ATOM   788  H HB2  A LYS   A 1 29  ? 15.495 1.286   18.906  0.74 34.93 ?  29  LYS   A HB2  1 
ATOM   789  H HB2  B LYS   A 1 29  ? 15.507 1.291   18.858  0.26 35.16 ?  29  LYS   A HB2  1 
ATOM   790  H HB3  A LYS   A 1 29  ? 16.005 -0.114  18.365  0.74 34.93 ?  29  LYS   A HB3  1 
ATOM   791  H HB3  B LYS   A 1 29  ? 16.000 -0.143  18.393  0.26 35.16 ?  29  LYS   A HB3  1 
ATOM   792  H HG2  A LYS   A 1 29  ? 14.449 -0.629  19.897  0.74 38.37 ?  29  LYS   A HG2  1 
ATOM   793  H HG2  B LYS   A 1 29  ? 14.403 -0.539  19.928  0.26 37.48 ?  29  LYS   A HG2  1 
ATOM   794  H HG3  A LYS   A 1 29  ? 15.822 -0.899  20.650  0.74 38.37 ?  29  LYS   A HG3  1 
ATOM   795  H HG3  B LYS   A 1 29  ? 15.766 -0.826  20.695  0.26 37.48 ?  29  LYS   A HG3  1 
ATOM   796  H HD2  A LYS   A 1 29  ? 15.637 1.101   21.782  0.74 41.58 ?  29  LYS   A HD2  1 
ATOM   797  H HD2  B LYS   A 1 29  ? 15.645 1.213   21.756  0.26 39.45 ?  29  LYS   A HD2  1 
ATOM   798  H HD3  A LYS   A 1 29  ? 14.332 1.480   20.952  0.74 41.58 ?  29  LYS   A HD3  1 
ATOM   799  H HD3  B LYS   A 1 29  ? 14.361 1.613   20.904  0.26 39.45 ?  29  LYS   A HD3  1 
ATOM   800  H HE2  A LYS   A 1 29  ? 13.191 -0.299  21.968  0.74 43.78 ?  29  LYS   A HE2  1 
ATOM   801  H HE2  B LYS   A 1 29  ? 13.145 -0.081  21.973  0.26 40.79 ?  29  LYS   A HE2  1 
ATOM   802  H HE3  A LYS   A 1 29  ? 14.490 -0.627  22.827  0.74 43.78 ?  29  LYS   A HE3  1 
ATOM   803  H HE3  B LYS   A 1 29  ? 14.426 -0.433  22.848  0.26 40.79 ?  29  LYS   A HE3  1 
ATOM   804  H HZ1  A LYS   A 1 29  ? 13.022 0.608   24.045  0.74 45.02 ?  29  LYS   A HZ1  1 
ATOM   805  H HZ1  B LYS   A 1 29  ? 13.003 0.893   24.019  0.26 41.49 ?  29  LYS   A HZ1  1 
ATOM   806  H HZ2  A LYS   A 1 29  ? 14.230 1.386   23.857  0.74 45.02 ?  29  LYS   A HZ2  1 
ATOM   807  H HZ2  B LYS   A 1 29  ? 14.241 1.617   23.816  0.26 41.49 ?  29  LYS   A HZ2  1 
ATOM   808  H HZ3  A LYS   A 1 29  ? 13.047 1.684   23.075  0.74 45.02 ?  29  LYS   A HZ3  1 
ATOM   809  H HZ3  B LYS   A 1 29  ? 13.075 1.938   23.018  0.26 41.49 ?  29  LYS   A HZ3  1 
ATOM   810  N N    . VAL   A 1 30  ? 18.581 -1.191  18.870  1.00 24.59 ?  30  VAL   A N    1 
ATOM   811  C CA   . VAL   A 1 30  ? 19.219 -2.469  19.166  1.00 22.75 ?  30  VAL   A CA   1 
ATOM   812  C C    . VAL   A 1 30  ? 20.725 -2.329  19.385  1.00 20.98 ?  30  VAL   A C    1 
ATOM   813  O O    . VAL   A 1 30  ? 21.306 -3.055  20.198  1.00 21.15 ?  30  VAL   A O    1 
ATOM   814  C CB   . VAL   A 1 30  ? 18.891 -3.461  18.036  1.00 23.37 ?  30  VAL   A CB   1 
ATOM   815  C CG1  . VAL   A 1 30  ? 19.600 -4.792  18.255  1.00 24.08 ?  30  VAL   A CG1  1 
ATOM   816  C CG2  . VAL   A 1 30  ? 17.381 -3.661  17.927  1.00 23.95 ?  30  VAL   A CG2  1 
ATOM   817  H H    A VAL   A 1 30  ? 18.447 -1.045  18.032  0.74 29.50 ?  30  VAL   A H    1 
ATOM   818  H H    B VAL   A 1 30  ? 18.455 -1.042  18.031  0.26 29.50 ?  30  VAL   A H    1 
ATOM   819  H HA   . VAL   A 1 30  ? 18.834 -2.823  19.980  1.00 27.30 ?  30  VAL   A HA   1 
ATOM   820  H HB   . VAL   A 1 30  ? 19.202 -3.095  17.193  1.00 28.04 ?  30  VAL   A HB   1 
ATOM   821  H HG11 . VAL   A 1 30  ? 19.216 -5.454  17.657  1.00 28.90 ?  30  VAL   A HG11 1 
ATOM   822  H HG12 . VAL   A 1 30  ? 20.543 -4.684  18.067  1.00 28.90 ?  30  VAL   A HG12 1 
ATOM   823  H HG13 . VAL   A 1 30  ? 19.471 -5.068  19.176  1.00 28.90 ?  30  VAL   A HG13 1 
ATOM   824  H HG21 . VAL   A 1 30  ? 17.200 -4.346  17.265  1.00 28.74 ?  30  VAL   A HG21 1 
ATOM   825  H HG22 . VAL   A 1 30  ? 17.037 -3.937  18.791  1.00 28.74 ?  30  VAL   A HG22 1 
ATOM   826  H HG23 . VAL   A 1 30  ? 16.969 -2.825  17.658  1.00 28.74 ?  30  VAL   A HG23 1 
ATOM   827  N N    . LYS   A 1 31  ? 21.374 -1.402  18.690  1.00 19.59 ?  31  LYS   A N    1 
ATOM   828  C CA   . LYS   A 1 31  ? 22.830 -1.320  18.639  1.00 20.40 ?  31  LYS   A CA   1 
ATOM   829  C C    . LYS   A 1 31  ? 23.420 -2.688  18.284  1.00 18.46 ?  31  LYS   A C    1 
ATOM   830  O O    . LYS   A 1 31  ? 24.204 -3.254  19.051  1.00 19.36 ?  31  LYS   A O    1 
ATOM   831  C CB   . LYS   A 1 31  ? 23.419 -0.784  19.936  1.00 25.03 ?  31  LYS   A CB   1 
ATOM   832  C CG   . LYS   A 1 31  ? 22.773 0.510   20.410  1.00 30.60 ?  31  LYS   A CG   1 
ATOM   833  C CD   . LYS   A 1 31  ? 23.813 1.542   20.821  1.00 34.87 ?  31  LYS   A CD   1 
ATOM   834  C CE   . LYS   A 1 31  ? 23.203 2.627   21.696  1.00 37.68 ?  31  LYS   A CE   1 
ATOM   835  N NZ   . LYS   A 1 31  ? 22.055 3.314   21.043  1.00 39.10 ?  31  LYS   A NZ   1 
ATOM   836  H H    . LYS   A 1 31  ? 20.982 -0.793  18.231  1.00 23.50 ?  31  LYS   A H    1 
ATOM   837  H HA   . LYS   A 1 31  ? 23.070 -0.705  17.931  1.00 24.49 ?  31  LYS   A HA   1 
ATOM   838  H HB2  . LYS   A 1 31  ? 23.305 -1.448  20.631  1.00 30.04 ?  31  LYS   A HB2  1 
ATOM   839  H HB3  . LYS   A 1 31  ? 24.366 -0.610  19.798  1.00 30.04 ?  31  LYS   A HB3  1 
ATOM   840  H HG2  . LYS   A 1 31  ? 22.242 0.885   19.689  1.00 36.72 ?  31  LYS   A HG2  1 
ATOM   841  H HG3  . LYS   A 1 31  ? 22.211 0.323   21.178  1.00 36.72 ?  31  LYS   A HG3  1 
ATOM   842  H HD2  . LYS   A 1 31  ? 24.518 1.105   21.323  1.00 41.84 ?  31  LYS   A HD2  1 
ATOM   843  H HD3  . LYS   A 1 31  ? 24.178 1.962   20.025  1.00 41.84 ?  31  LYS   A HD3  1 
ATOM   844  H HE2  . LYS   A 1 31  ? 22.884 2.226   22.520  1.00 45.22 ?  31  LYS   A HE2  1 
ATOM   845  H HE3  . LYS   A 1 31  ? 23.880 3.294   21.891  1.00 45.22 ?  31  LYS   A HE3  1 
ATOM   846  H HZ1  . LYS   A 1 31  ? 21.737 3.949   21.580  1.00 46.92 ?  31  LYS   A HZ1  1 
ATOM   847  H HZ2  . LYS   A 1 31  ? 22.318 3.686   20.279  1.00 46.92 ?  31  LYS   A HZ2  1 
ATOM   848  H HZ3  . LYS   A 1 31  ? 21.407 2.728   20.873  1.00 46.92 ?  31  LYS   A HZ3  1 
ATOM   849  N N    . PRO   A 1 32  ? 23.053 -3.240  17.133  1.00 16.47 ?  32  PRO   A N    1 
ATOM   850  C CA   . PRO   A 1 32  ? 23.519 -4.578  16.773  1.00 16.66 ?  32  PRO   A CA   1 
ATOM   851  C C    . PRO   A 1 32  ? 25.018 -4.598  16.548  1.00 16.49 ?  32  PRO   A C    1 
ATOM   852  O O    . PRO   A 1 32  ? 25.661 -3.570  16.329  1.00 16.33 ?  32  PRO   A O    1 
ATOM   853  C CB   . PRO   A 1 32  ? 22.770 -4.864  15.467  1.00 16.98 ?  32  PRO   A CB   1 
ATOM   854  C CG   . PRO   A 1 32  ? 22.584 -3.503  14.862  1.00 15.78 ?  32  PRO   A CG   1 
ATOM   855  C CD   . PRO   A 1 32  ? 22.313 -2.602  16.032  1.00 15.72 ?  32  PRO   A CD   1 
ATOM   856  H HA   . PRO   A 1 32  ? 23.278 -5.227  17.450  1.00 19.99 ?  32  PRO   A HA   1 
ATOM   857  H HB2  . PRO   A 1 32  ? 23.309 -5.435  14.893  1.00 20.38 ?  32  PRO   A HB2  1 
ATOM   858  H HB3  . PRO   A 1 32  ? 21.916 -5.284  15.664  1.00 20.38 ?  32  PRO   A HB3  1 
ATOM   859  H HG2  . PRO   A 1 32  ? 23.390 -3.246  14.394  1.00 18.94 ?  32  PRO   A HG2  1 
ATOM   860  H HG3  . PRO   A 1 32  ? 21.824 -3.527  14.255  1.00 18.94 ?  32  PRO   A HG3  1 
ATOM   861  H HD2  . PRO   A 1 32  ? 22.663 -1.717  15.845  1.00 18.87 ?  32  PRO   A HD2  1 
ATOM   862  H HD3  . PRO   A 1 32  ? 21.368 -2.583  16.225  1.00 18.87 ?  32  PRO   A HD3  1 
ATOM   863  N N    . THR   A 1 33  ? 25.573 -5.807  16.585  1.00 16.47 ?  33  THR   A N    1 
ATOM   864  C CA   . THR   A 1 33  ? 26.981 -5.972  16.253  1.00 16.59 ?  33  THR   A CA   1 
ATOM   865  C C    . THR   A 1 33  ? 27.265 -5.506  14.831  1.00 15.07 ?  33  THR   A C    1 
ATOM   866  O O    . THR   A 1 33  ? 28.295 -4.869  14.576  1.00 15.27 ?  33  THR   A O    1 
ATOM   867  C CB   . THR   A 1 33  ? 27.380 -7.434  16.445  1.00 18.05 ?  33  THR   A CB   1 
ATOM   868  O OG1  . THR   A 1 33  ? 27.063 -7.828  17.784  1.00 19.87 ?  33  THR   A OG1  1 
ATOM   869  C CG2  . THR   A 1 33  ? 28.871 -7.631  16.201  1.00 19.23 ?  33  THR   A CG2  1 
ATOM   870  H H    . THR   A 1 33  ? 25.166 -6.536  16.786  1.00 19.77 ?  33  THR   A H    1 
ATOM   871  H HA   . THR   A 1 33  ? 27.518 -5.438  16.855  1.00 19.91 ?  33  THR   A HA   1 
ATOM   872  H HB   . THR   A 1 33  ? 26.894 -7.998  15.820  1.00 21.66 ?  33  THR   A HB   1 
ATOM   873  H HG1  . THR   A 1 33  ? 27.493 -7.356  18.334  1.00 23.85 ?  33  THR   A HG1  1 
ATOM   874  H HG21 . THR   A 1 33  ? 29.136 -8.528  16.465  1.00 23.07 ?  33  THR   A HG21 1 
ATOM   875  H HG22 . THR   A 1 33  ? 29.074 -7.510  15.261  1.00 23.07 ?  33  THR   A HG22 1 
ATOM   876  H HG23 . THR   A 1 33  ? 29.378 -6.990  16.721  1.00 23.07 ?  33  THR   A HG23 1 
ATOM   877  N N    . VAL   A 1 34  ? 26.361 -5.805  13.897  1.00 13.51 ?  34  VAL   A N    1 
ATOM   878  C CA   . VAL   A 1 34  ? 26.541 -5.467  12.488  1.00 12.27 ?  34  VAL   A CA   1 
ATOM   879  C C    . VAL   A 1 34  ? 25.238 -4.904  11.929  1.00 11.49 ?  34  VAL   A C    1 
ATOM   880  O O    . VAL   A 1 34  ? 24.195 -5.571  11.980  1.00 12.26 ?  34  VAL   A O    1 
ATOM   881  C CB   . VAL   A 1 34  ? 26.980 -6.677  11.643  1.00 12.98 ?  34  VAL   A CB   1 
ATOM   882  C CG1  . VAL   A 1 34  ? 27.141 -6.262  10.185  1.00 12.98 ?  34  VAL   A CG1  1 
ATOM   883  C CG2  . VAL   A 1 34  ? 28.269 -7.302  12.188  1.00 14.39 ?  34  VAL   A CG2  1 
ATOM   884  H H    . VAL   A 1 34  ? 25.620 -6.210  14.059  1.00 16.21 ?  34  VAL   A H    1 
ATOM   885  H HA   . VAL   A 1 34  ? 27.220 -4.777  12.406  1.00 14.73 ?  34  VAL   A HA   1 
ATOM   886  H HB   . VAL   A 1 34  ? 26.283 -7.348  11.682  1.00 15.58 ?  34  VAL   A HB   1 
ATOM   887  H HG11 . VAL   A 1 34  ? 27.646 -6.946  9.719   1.00 15.58 ?  34  VAL   A HG11 1 
ATOM   888  H HG12 . VAL   A 1 34  ? 26.266 -6.164  9.780   1.00 15.58 ?  34  VAL   A HG12 1 
ATOM   889  H HG13 . VAL   A 1 34  ? 27.621 -5.417  10.148  1.00 15.58 ?  34  VAL   A HG13 1 
ATOM   890  H HG21 . VAL   A 1 34  ? 28.529 -8.041  11.614  1.00 17.27 ?  34  VAL   A HG21 1 
ATOM   891  H HG22 . VAL   A 1 34  ? 28.970 -6.631  12.197  1.00 17.27 ?  34  VAL   A HG22 1 
ATOM   892  H HG23 . VAL   A 1 34  ? 28.110 -7.625  13.089  1.00 17.27 ?  34  VAL   A HG23 1 
ATOM   893  N N    . VAL   A 1 35  ? 25.300 -3.690  11.376  1.00 10.88 ?  35  VAL   A N    1 
ATOM   894  C CA   . VAL   A 1 35  ? 24.264 -3.169  10.492  1.00 10.63 ?  35  VAL   A CA   1 
ATOM   895  C C    . VAL   A 1 35  ? 24.814 -3.164  9.072   1.00 9.95  ?  35  VAL   A C    1 
ATOM   896  O O    . VAL   A 1 35  ? 25.965 -2.775  8.843   1.00 10.67 ?  35  VAL   A O    1 
ATOM   897  C CB   . VAL   A 1 35  ? 23.743 -1.775  10.912  1.00 11.32 ?  35  VAL   A CB   1 
ATOM   898  C CG1  . VAL   A 1 35  ? 24.817 -0.685  10.771  1.00 11.76 ?  35  VAL   A CG1  1 
ATOM   899  C CG2  . VAL   A 1 35  ? 22.496 -1.418  10.104  1.00 12.05 ?  35  VAL   A CG2  1 
ATOM   900  H H    . VAL   A 1 35  ? 25.944 -3.135  11.503  1.00 13.05 ?  35  VAL   A H    1 
ATOM   901  H HA   . VAL   A 1 35  ? 23.504 -3.776  10.511  1.00 12.76 ?  35  VAL   A HA   1 
ATOM   902  H HB   . VAL   A 1 35  ? 23.477 -1.807  11.841  1.00 13.59 ?  35  VAL   A HB   1 
ATOM   903  H HG11 . VAL   A 1 35  ? 24.479 0.146   11.150  1.00 14.12 ?  35  VAL   A HG11 1 
ATOM   904  H HG12 . VAL   A 1 35  ? 25.613 -0.963  11.244  1.00 14.12 ?  35  VAL   A HG12 1 
ATOM   905  H HG13 . VAL   A 1 35  ? 25.019 -0.552  9.829   1.00 14.12 ?  35  VAL   A HG13 1 
ATOM   906  H HG21 . VAL   A 1 35  ? 22.144 -0.571  10.412  1.00 14.46 ?  35  VAL   A HG21 1 
ATOM   907  H HG22 . VAL   A 1 35  ? 22.733 -1.353  9.161   1.00 14.46 ?  35  VAL   A HG22 1 
ATOM   908  H HG23 . VAL   A 1 35  ? 21.829 -2.116  10.223  1.00 14.46 ?  35  VAL   A HG23 1 
ATOM   909  N N    . VAL   A 1 36  ? 23.995 -3.606  8.124   1.00 9.76  ?  36  VAL   A N    1 
ATOM   910  C CA   . VAL   A 1 36  ? 24.371 -3.618  6.717   1.00 9.14  ?  36  VAL   A CA   1 
ATOM   911  C C    . VAL   A 1 36  ? 23.914 -2.324  6.058   1.00 9.26  ?  36  VAL   A C    1 
ATOM   912  O O    . VAL   A 1 36  ? 22.758 -1.909  6.206   1.00 10.11 ?  36  VAL   A O    1 
ATOM   913  C CB   . VAL   A 1 36  ? 23.760 -4.832  5.998   1.00 9.35  ?  36  VAL   A CB   1 
ATOM   914  C CG1  . VAL   A 1 36  ? 24.013 -4.754  4.509   1.00 10.07 ?  36  VAL   A CG1  1 
ATOM   915  C CG2  . VAL   A 1 36  ? 24.303 -6.130  6.580   1.00 10.14 ?  36  VAL   A CG2  1 
ATOM   916  H H    . VAL   A 1 36  ? 23.204 -3.917  8.273   1.00 11.71 ?  36  VAL   A H    1 
ATOM   917  H HA   . VAL   A 1 36  ? 25.339 -3.678  6.643   1.00 10.97 ?  36  VAL   A HA   1 
ATOM   918  H HB   . VAL   A 1 36  ? 22.802 -4.824  6.132   1.00 11.22 ?  36  VAL   A HB   1 
ATOM   919  H HG11 . VAL   A 1 36  ? 23.874 -5.628  4.116   1.00 12.09 ?  36  VAL   A HG11 1 
ATOM   920  H HG12 . VAL   A 1 36  ? 23.398 -4.114  4.112   1.00 12.09 ?  36  VAL   A HG12 1 
ATOM   921  H HG13 . VAL   A 1 36  ? 24.929 -4.467  4.356   1.00 12.09 ?  36  VAL   A HG13 1 
ATOM   922  H HG21 . VAL   A 1 36  ? 23.918 -6.880  6.100   1.00 12.17 ?  36  VAL   A HG21 1 
ATOM   923  H HG22 . VAL   A 1 36  ? 25.270 -6.141  6.489   1.00 12.17 ?  36  VAL   A HG22 1 
ATOM   924  H HG23 . VAL   A 1 36  ? 24.061 -6.182  7.520   1.00 12.17 ?  36  VAL   A HG23 1 
ATOM   925  N N    . ASN   A 1 37  ? 24.827 -1.702  5.312   1.00 9.15  ?  37  ASN   A N    1 
ATOM   926  C CA   . ASN   A 1 37  ? 24.507 -0.573  4.454   1.00 8.90  ?  37  ASN   A CA   1 
ATOM   927  C C    . ASN   A 1 37  ? 24.382 -1.037  3.013   1.00 9.03  ?  37  ASN   A C    1 
ATOM   928  O O    . ASN   A 1 37  ? 25.165 -1.868  2.542   1.00 9.86  ?  37  ASN   A O    1 
ATOM   929  C CB   . ASN   A 1 37  ? 25.580 0.507   4.554   1.00 9.35  ?  37  ASN   A CB   1 
ATOM   930  C CG   . ASN   A 1 37  ? 25.260 1.710   3.704   1.00 9.34  ?  37  ASN   A CG   1 
ATOM   931  O OD1  . ASN   A 1 37  ? 24.086 2.059   3.519   1.00 10.09 ?  37  ASN   A OD1  1 
ATOM   932  N ND2  . ASN   A 1 37  ? 26.299 2.351   3.181   1.00 10.07 ?  37  ASN   A ND2  1 
ATOM   933  H H    . ASN   A 1 37  ? 25.662 -1.921  5.295   1.00 10.98 ?  37  ASN   A H    1 
ATOM   934  H HA   . ASN   A 1 37  ? 23.664 -0.188  4.734   1.00 10.68 ?  37  ASN   A HA   1 
ATOM   935  H HB2  . ASN   A 1 37  ? 25.653 0.805   5.477   1.00 11.22 ?  37  ASN   A HB2  1 
ATOM   936  H HB3  . ASN   A 1 37  ? 26.432 0.144   4.258   1.00 11.22 ?  37  ASN   A HB3  1 
ATOM   937  H HD21 . ASN   A 1 37  ? 26.167 3.041   2.683   1.00 12.08 ?  37  ASN   A HD21 1 
ATOM   938  H HD22 . ASN   A 1 37  ? 27.094 2.080   3.329   1.00 12.08 ?  37  ASN   A HD22 1 
ATOM   939  N N    A ALA   A 1 38  ? 23.374 -0.482  2.329   0.74 9.26  ?  38  ALA   A N    1 
ATOM   940  N N    B ALA   A 1 38  ? 23.396 -0.498  2.294   0.26 9.65  ?  38  ALA   A N    1 
ATOM   941  C CA   A ALA   A 1 38  ? 23.173 -0.608  0.886   0.74 9.50  ?  38  ALA   A CA   1 
ATOM   942  C CA   B ALA   A 1 38  ? 23.280 -0.773  0.860   0.26 10.37 ?  38  ALA   A CA   1 
ATOM   943  C C    A ALA   A 1 38  ? 24.104 0.378   0.182   0.74 9.23  ?  38  ALA   A C    1 
ATOM   944  C C    B ALA   A 1 38  ? 24.068 0.295   0.103   0.26 10.28 ?  38  ALA   A C    1 
ATOM   945  O O    A ALA   A 1 38  ? 23.713 1.478   -0.223  0.74 9.64  ?  38  ALA   A O    1 
ATOM   946  O O    B ALA   A 1 38  ? 23.533 1.302   -0.368  0.26 10.35 ?  38  ALA   A O    1 
ATOM   947  C CB   A ALA   A 1 38  ? 21.710 -0.338  0.535   0.74 10.29 ?  38  ALA   A CB   1 
ATOM   948  C CB   B ALA   A 1 38  ? 21.822 -0.829  0.426   0.26 10.99 ?  38  ALA   A CB   1 
ATOM   949  H H    A ALA   A 1 38  ? 22.773 0.005   2.705   0.74 11.11 ?  38  ALA   A H    1 
ATOM   950  H H    B ALA   A 1 38  ? 22.788 0.025   2.613   0.26 11.58 ?  38  ALA   A H    1 
ATOM   951  H HA   A ALA   A 1 38  ? 23.400 -1.503  0.601   0.74 11.41 ?  38  ALA   A HA   1 
ATOM   952  H HA   B ALA   A 1 38  ? 23.680 -1.637  0.672   0.26 12.45 ?  38  ALA   A HA   1 
ATOM   953  H HB1  A ALA   A 1 38  ? 21.588 -0.442  -0.422  0.74 12.35 ?  38  ALA   A HB1  1 
ATOM   954  H HB1  B ALA   A 1 38  ? 21.786 -1.076  -0.513  0.26 13.18 ?  38  ALA   A HB1  1 
ATOM   955  H HB2  A ALA   A 1 38  ? 21.150 -0.978  1.008   0.74 12.35 ?  38  ALA   A HB2  1 
ATOM   956  H HB2  B ALA   A 1 38  ? 21.354 -1.490  0.959   0.26 13.18 ?  38  ALA   A HB2  1 
ATOM   957  H HB3  A ALA   A 1 38  ? 21.477 0.563   0.803   0.74 12.35 ?  38  ALA   A HB3  1 
ATOM   958  H HB3  B ALA   A 1 38  ? 21.422 0.043   0.551   0.26 13.18 ?  38  ALA   A HB3  1 
ATOM   959  N N    A ALA   A 1 39  ? 25.365 -0.023  0.047   0.74 9.38  ?  39  ALA   A N    1 
ATOM   960  N N    B ALA   A 1 39  ? 25.370 0.058   -0.015  0.26 10.37 ?  39  ALA   A N    1 
ATOM   961  C CA   A ALA   A 1 39  ? 26.420 0.849   -0.443  0.74 9.22  ?  39  ALA   A CA   1 
ATOM   962  C CA   B ALA   A 1 39  ? 26.308 1.047   -0.522  0.26 10.62 ?  39  ALA   A CA   1 
ATOM   963  C C    A ALA   A 1 39  ? 26.525 0.811   -1.967  0.74 9.35  ?  39  ALA   A C    1 
ATOM   964  C C    B ALA   A 1 39  ? 26.573 0.850   -2.009  0.26 10.18 ?  39  ALA   A C    1 
ATOM   965  O O    A ALA   A 1 39  ? 26.001 -0.083  -2.637  0.74 9.61  ?  39  ALA   A O    1 
ATOM   966  O O    B ALA   A 1 39  ? 26.281 -0.199  -2.589  0.26 9.79  ?  39  ALA   A O    1 
ATOM   967  C CB   A ALA   A 1 39  ? 27.754 0.445   0.184   0.74 9.50  ?  39  ALA   A CB   1 
ATOM   968  C CB   B ALA   A 1 39  ? 27.629 0.958   0.245   0.26 11.30 ?  39  ALA   A CB   1 
ATOM   969  H H    A ALA   A 1 39  ? 25.635 -0.819  0.244   0.74 11.26 ?  39  ALA   A H    1 
ATOM   970  H H    B ALA   A 1 39  ? 25.742 -0.691  0.194   0.26 12.44 ?  39  ALA   A H    1 
ATOM   971  H HA   A ALA   A 1 39  ? 26.220 1.760   -0.178  0.74 11.07 ?  39  ALA   A HA   1 
ATOM   972  H HA   B ALA   A 1 39  ? 25.938 1.932   -0.394  0.26 12.75 ?  39  ALA   A HA   1 
ATOM   973  H HB1  A ALA   A 1 39  ? 28.446 1.038   -0.151  0.74 11.40 ?  39  ALA   A HB1  1 
ATOM   974  H HB1  B ALA   A 1 39  ? 28.239 1.627   -0.102  0.26 13.56 ?  39  ALA   A HB1  1 
ATOM   975  H HB2  A ALA   A 1 39  ? 27.686 0.532   1.149   0.74 11.40 ?  39  ALA   A HB2  1 
ATOM   976  H HB2  B ALA   A 1 39  ? 27.459 1.121   1.186   0.26 13.56 ?  39  ALA   A HB2  1 
ATOM   977  H HB3  A ALA   A 1 39  ? 27.952 -0.469  -0.055  0.74 11.40 ?  39  ALA   A HB3  1 
ATOM   978  H HB3  B ALA   A 1 39  ? 28.006 0.072   0.126   0.26 13.56 ?  39  ALA   A HB3  1 
ATOM   979  N N    A ASN   A 1 40  ? 27.220 1.810   -2.511  0.74 10.01 ?  40  ASN   A N    1 
ATOM   980  N N    B ASN   A 1 40  ? 27.132 1.889   -2.623  0.26 10.12 ?  40  ASN   A N    1 
ATOM   981  C CA   A ASN   A 1 40  ? 27.736 1.765   -3.872  0.74 10.20 ?  40  ASN   A CA   1 
ATOM   982  C CA   B ASN   A 1 40  ? 27.715 1.787   -3.951  0.26 10.26 ?  40  ASN   A CA   1 
ATOM   983  C C    A ASN   A 1 40  ? 29.260 1.659   -3.827  0.74 9.88  ?  40  ASN   A C    1 
ATOM   984  C C    B ASN   A 1 40  ? 29.230 1.627   -3.838  0.26 10.03 ?  40  ASN   A C    1 
ATOM   985  O O    A ASN   A 1 40  ? 29.879 1.763   -2.763  0.74 10.18 ?  40  ASN   A O    1 
ATOM   986  O O    B ASN   A 1 40  ? 29.812 1.689   -2.752  0.26 9.92  ?  40  ASN   A O    1 
ATOM   987  C CB   A ASN   A 1 40  ? 27.242 2.950   -4.719  0.74 11.11 ?  40  ASN   A CB   1 
ATOM   988  C CB   B ASN   A 1 40  ? 27.346 2.998   -4.817  0.26 10.67 ?  40  ASN   A CB   1 
ATOM   989  C CG   A ASN   A 1 40  ? 27.615 4.301   -4.137  0.74 12.00 ?  40  ASN   A CG   1 
ATOM   990  C CG   B ASN   A 1 40  ? 27.720 4.318   -4.173  0.26 10.75 ?  40  ASN   A CG   1 
ATOM   991  O OD1  A ASN   A 1 40  ? 28.777 4.548   -3.800  0.74 13.09 ?  40  ASN   A OD1  1 
ATOM   992  O OD1  B ASN   A 1 40  ? 28.897 4.602   -3.952  0.26 10.47 ?  40  ASN   A OD1  1 
ATOM   993  N ND2  A ASN   A 1 40  ? 26.627 5.186   -4.022  0.74 13.00 ?  40  ASN   A ND2  1 
ATOM   994  N ND2  B ASN   A 1 40  ? 26.718 5.140   -3.881  0.26 11.43 ?  40  ASN   A ND2  1 
ATOM   995  H H    A ASN   A 1 40  ? 27.414 2.532   -2.098  0.74 12.01 ?  40  ASN   A H    1 
ATOM   996  H H    B ASN   A 1 40  ? 27.181 2.676   -2.282  0.26 12.15 ?  40  ASN   A H    1 
ATOM   997  H HA   A ASN   A 1 40  ? 27.408 0.956   -4.299  0.74 12.24 ?  40  ASN   A HA   1 
ATOM   998  H HA   B ASN   A 1 40  ? 27.365 0.994   -4.389  0.26 12.31 ?  40  ASN   A HA   1 
ATOM   999  H HB2  A ASN   A 1 40  ? 27.632 2.881   -5.612  0.74 13.34 ?  40  ASN   A HB2  1 
ATOM   1000 H HB2  B ASN   A 1 40  ? 27.812 2.931   -5.667  0.26 12.80 ?  40  ASN   A HB2  1 
ATOM   1001 H HB3  A ASN   A 1 40  ? 26.276 2.908   -4.786  0.74 13.34 ?  40  ASN   A HB3  1 
ATOM   1002 H HB3  B ASN   A 1 40  ? 26.388 2.998   -4.967  0.26 12.80 ?  40  ASN   A HB3  1 
ATOM   1003 H HD21 A ASN   A 1 40  ? 26.791 5.971   -3.709  0.74 15.60 ?  40  ASN   A HD21 1 
ATOM   1004 H HD21 B ASN   A 1 40  ? 26.884 5.905   -3.523  0.26 13.71 ?  40  ASN   A HD21 1 
ATOM   1005 H HD22 A ASN   A 1 40  ? 25.831 4.974   -4.261  0.74 15.60 ?  40  ASN   A HD22 1 
ATOM   1006 H HD22 B ASN   A 1 40  ? 25.910 4.911   -4.053  0.26 13.71 ?  40  ASN   A HD22 1 
ATOM   1007 N N    . VAL   A 1 41  ? 29.869 1.403   -4.989  1.00 10.38 ?  41  VAL   A N    1 
ATOM   1008 C CA   . VAL   A 1 41  ? 31.299 1.092   -5.010  1.00 11.13 ?  41  VAL   A CA   1 
ATOM   1009 C C    . VAL   A 1 41  ? 32.169 2.238   -4.534  1.00 10.88 ?  41  VAL   A C    1 
ATOM   1010 O O    . VAL   A 1 41  ? 33.314 2.007   -4.128  1.00 11.63 ?  41  VAL   A O    1 
ATOM   1011 C CB   . VAL   A 1 41  ? 31.789 0.603   -6.390  1.00 12.19 ?  41  VAL   A CB   1 
ATOM   1012 C CG1  . VAL   A 1 41  ? 31.108 -0.706  -6.774  1.00 12.81 ?  41  VAL   A CG1  1 
ATOM   1013 C CG2  . VAL   A 1 41  ? 31.619 1.674   -7.472  1.00 13.07 ?  41  VAL   A CG2  1 
ATOM   1014 H H    A VAL   A 1 41  ? 29.485 1.395   -5.760  0.74 12.46 ?  41  VAL   A H    1 
ATOM   1015 H H    B VAL   A 1 41  ? 29.497 1.413   -5.766  0.26 12.46 ?  41  VAL   A H    1 
ATOM   1016 H HA   . VAL   A 1 41  ? 31.451 0.359   -4.391  1.00 13.36 ?  41  VAL   A HA   1 
ATOM   1017 H HB   . VAL   A 1 41  ? 32.738 0.406   -6.322  1.00 14.63 ?  41  VAL   A HB   1 
ATOM   1018 H HG11 . VAL   A 1 41  ? 31.454 -1.014  -7.625  1.00 15.37 ?  41  VAL   A HG11 1 
ATOM   1019 H HG12 . VAL   A 1 41  ? 31.286 -1.376  -6.087  1.00 15.37 ?  41  VAL   A HG12 1 
ATOM   1020 H HG13 . VAL   A 1 41  ? 30.150 -0.560  -6.841  1.00 15.37 ?  41  VAL   A HG13 1 
ATOM   1021 H HG21 . VAL   A 1 41  ? 31.865 1.294   -8.333  1.00 15.69 ?  41  VAL   A HG21 1 
ATOM   1022 H HG22 . VAL   A 1 41  ? 30.695 1.960   -7.489  1.00 15.69 ?  41  VAL   A HG22 1 
ATOM   1023 H HG23 . VAL   A 1 41  ? 32.199 2.422   -7.266  1.00 15.69 ?  41  VAL   A HG23 1 
ATOM   1024 N N    . TYR   A 1 42  ? 31.663 3.472   -4.599  1.00 11.00 ?  42  TYR   A N    1 
ATOM   1025 C CA   . TYR   A 1 42  ? 32.403 4.652   -4.180  1.00 10.78 ?  42  TYR   A CA   1 
ATOM   1026 C C    . TYR   A 1 42  ? 32.145 5.026   -2.729  1.00 10.70 ?  42  TYR   A C    1 
ATOM   1027 O O    . TYR   A 1 42  ? 32.712 6.014   -2.241  1.00 11.16 ?  42  TYR   A O    1 
ATOM   1028 C CB   . TYR   A 1 42  ? 32.055 5.842   -5.095  1.00 11.60 ?  42  TYR   A CB   1 
ATOM   1029 C CG   . TYR   A 1 42  ? 32.244 5.538   -6.564  1.00 12.25 ?  42  TYR   A CG   1 
ATOM   1030 C CD1  . TYR   A 1 42  ? 33.505 5.336   -7.097  1.00 13.12 ?  42  TYR   A CD1  1 
ATOM   1031 C CD2  . TYR   A 1 42  ? 31.151 5.418   -7.416  1.00 13.58 ?  42  TYR   A CD2  1 
ATOM   1032 C CE1  . TYR   A 1 42  ? 33.675 5.030   -8.441  1.00 14.00 ?  42  TYR   A CE1  1 
ATOM   1033 C CE2  . TYR   A 1 42  ? 31.314 5.124   -8.756  1.00 14.68 ?  42  TYR   A CE2  1 
ATOM   1034 C CZ   . TYR   A 1 42  ? 32.578 4.927   -9.264  1.00 14.91 ?  42  TYR   A CZ   1 
ATOM   1035 O OH   . TYR   A 1 42  ? 32.741 4.626   -10.598 1.00 16.59 ?  42  TYR   A OH   1 
ATOM   1036 H H    . TYR   A 1 42  ? 30.876 3.647   -4.897  1.00 13.20 ?  42  TYR   A H    1 
ATOM   1037 H HA   . TYR   A 1 42  ? 33.351 4.486   -4.280  1.00 12.93 ?  42  TYR   A HA   1 
ATOM   1038 H HB2  . TYR   A 1 42  ? 31.121 6.086   -4.961  1.00 13.92 ?  42  TYR   A HB2  1 
ATOM   1039 H HB3  . TYR   A 1 42  ? 32.624 6.596   -4.874  1.00 13.92 ?  42  TYR   A HB3  1 
ATOM   1040 H HD1  . TYR   A 1 42  ? 34.252 5.394   -6.544  1.00 15.74 ?  42  TYR   A HD1  1 
ATOM   1041 H HD2  . TYR   A 1 42  ? 30.295 5.553   -7.081  1.00 16.29 ?  42  TYR   A HD2  1 
ATOM   1042 H HE1  . TYR   A 1 42  ? 34.531 4.895   -8.783  1.00 16.80 ?  42  TYR   A HE1  1 
ATOM   1043 H HE2  . TYR   A 1 42  ? 30.573 5.055   -9.316  1.00 17.62 ?  42  TYR   A HE2  1 
ATOM   1044 H HH   . TYR   A 1 42  ? 33.561 4.528   -10.775 1.00 19.91 ?  42  TYR   A HH   1 
ATOM   1045 N N    . LEU   A 1 43  ? 31.287 4.267   -2.043  1.00 10.21 ?  43  LEU   A N    1 
ATOM   1046 C CA   . LEU   A 1 43  ? 30.840 4.600   -0.691  1.00 10.14 ?  43  LEU   A CA   1 
ATOM   1047 C C    . LEU   A 1 43  ? 30.359 6.048   -0.596  1.00 10.19 ?  43  LEU   A C    1 
ATOM   1048 O O    . LEU   A 1 43  ? 30.619 6.749   0.383   1.00 11.25 ?  43  LEU   A O    1 
ATOM   1049 C CB   . LEU   A 1 43  ? 31.895 4.293   0.371   1.00 10.39 ?  43  LEU   A CB   1 
ATOM   1050 C CG   . LEU   A 1 43  ? 32.389 2.844   0.459   1.00 10.98 ?  43  LEU   A CG   1 
ATOM   1051 C CD1  . LEU   A 1 43  ? 33.455 2.727   1.548   1.00 11.95 ?  43  LEU   A CD1  1 
ATOM   1052 C CD2  . LEU   A 1 43  ? 31.249 1.856   0.706   1.00 11.40 ?  43  LEU   A CD2  1 
ATOM   1053 H H    . LEU   A 1 43  ? 30.941 3.533   -2.344  1.00 12.25 ?  43  LEU   A H    1 
ATOM   1054 H HA   . LEU   A 1 43  ? 30.075 4.040   -0.489  1.00 12.17 ?  43  LEU   A HA   1 
ATOM   1055 H HB2  . LEU   A 1 43  ? 32.669 4.851   0.210   1.00 12.47 ?  43  LEU   A HB2  1 
ATOM   1056 H HB3  . LEU   A 1 43  ? 31.518 4.512   1.241   1.00 12.47 ?  43  LEU   A HB3  1 
ATOM   1057 H HG   . LEU   A 1 43  ? 32.808 2.607   -0.384  1.00 13.18 ?  43  LEU   A HG   1 
ATOM   1058 H HD11 . LEU   A 1 43  ? 33.766 1.806   1.594   1.00 14.35 ?  43  LEU   A HD11 1 
ATOM   1059 H HD12 . LEU   A 1 43  ? 34.200 3.311   1.330   1.00 14.35 ?  43  LEU   A HD12 1 
ATOM   1060 H HD13 . LEU   A 1 43  ? 33.071 2.986   2.400   1.00 14.35 ?  43  LEU   A HD13 1 
ATOM   1061 H HD21 . LEU   A 1 43  ? 31.621 0.970   0.840   1.00 13.68 ?  43  LEU   A HD21 1 
ATOM   1062 H HD22 . LEU   A 1 43  ? 30.761 2.132   1.498   1.00 13.68 ?  43  LEU   A HD22 1 
ATOM   1063 H HD23 . LEU   A 1 43  ? 30.661 1.856   -0.064  1.00 13.68 ?  43  LEU   A HD23 1 
ATOM   1064 N N    A LYS   A 1 44  ? 29.651 6.493   -1.631  0.74 10.12 ?  44  LYS   A N    1 
ATOM   1065 N N    B LYS   A 1 44  ? 29.614 6.485   -1.608  0.26 11.09 ?  44  LYS   A N    1 
ATOM   1066 C CA   A LYS   A 1 44  ? 29.018 7.812   -1.638  0.74 10.42 ?  44  LYS   A CA   1 
ATOM   1067 C CA   B LYS   A 1 44  ? 28.971 7.796   -1.588  0.26 12.25 ?  44  LYS   A CA   1 
ATOM   1068 C C    A LYS   A 1 44  ? 27.586 7.629   -1.156  0.74 10.14 ?  44  LYS   A C    1 
ATOM   1069 C C    B LYS   A 1 44  ? 27.570 7.623   -1.016  0.26 11.51 ?  44  LYS   A C    1 
ATOM   1070 O O    A LYS   A 1 44  ? 26.725 7.125   -1.886  0.74 10.99 ?  44  LYS   A O    1 
ATOM   1071 O O    B LYS   A 1 44  ? 26.673 7.100   -1.687  0.26 11.46 ?  44  LYS   A O    1 
ATOM   1072 C CB   A LYS   A 1 44  ? 29.063 8.428   -3.028  0.74 12.67 ?  44  LYS   A CB   1 
ATOM   1073 C CB   B LYS   A 1 44  ? 28.935 8.400   -2.991  0.26 14.37 ?  44  LYS   A CB   1 
ATOM   1074 C CG   A LYS   A 1 44  ? 30.437 8.929   -3.442  0.74 16.62 ?  44  LYS   A CG   1 
ATOM   1075 C CG   B LYS   A 1 44  ? 30.291 8.866   -3.506  0.26 16.80 ?  44  LYS   A CG   1 
ATOM   1076 C CD   A LYS   A 1 44  ? 31.065 9.853   -2.401  0.74 21.94 ?  44  LYS   A CD   1 
ATOM   1077 C CD   B LYS   A 1 44  ? 31.025 9.721   -2.479  0.26 19.44 ?  44  LYS   A CD   1 
ATOM   1078 C CE   A LYS   A 1 44  ? 32.398 10.399  -2.882  0.74 25.12 ?  44  LYS   A CE   1 
ATOM   1079 C CE   B LYS   A 1 44  ? 32.382 10.158  -2.987  0.26 21.02 ?  44  LYS   A CE   1 
ATOM   1080 N NZ   A LYS   A 1 44  ? 33.208 10.967  -1.771  0.74 26.78 ?  44  LYS   A NZ   1 
ATOM   1081 N NZ   B LYS   A 1 44  ? 33.212 10.754  -1.904  0.26 21.62 ?  44  LYS   A NZ   1 
ATOM   1082 H H    A LYS   A 1 44  ? 29.518 6.041   -2.348  0.74 12.15 ?  44  LYS   A H    1 
ATOM   1083 H H    B LYS   A 1 44  ? 29.455 6.031   -2.321  0.26 13.31 ?  44  LYS   A H    1 
ATOM   1084 H HA   A LYS   A 1 44  ? 29.464 8.391   -1.001  0.74 12.51 ?  44  LYS   A HA   1 
ATOM   1085 H HA   B LYS   A 1 44  ? 29.449 8.390   -0.990  0.26 14.69 ?  44  LYS   A HA   1 
ATOM   1086 H HB2  A LYS   A 1 44  ? 28.785 7.761   -3.673  0.74 15.20 ?  44  LYS   A HB2  1 
ATOM   1087 H HB2  B LYS   A 1 44  ? 28.602 7.732   -3.611  0.26 17.25 ?  44  LYS   A HB2  1 
ATOM   1088 H HB3  A LYS   A 1 44  ? 28.455 9.183   -3.052  0.74 15.20 ?  44  LYS   A HB3  1 
ATOM   1089 H HB3  B LYS   A 1 44  ? 28.345 9.169   -2.990  0.26 17.25 ?  44  LYS   A HB3  1 
ATOM   1090 H HG2  A LYS   A 1 44  ? 31.025 8.170   -3.568  0.74 19.95 ?  44  LYS   A HG2  1 
ATOM   1091 H HG2  B LYS   A 1 44  ? 30.840 8.092   -3.706  0.26 20.16 ?  44  LYS   A HG2  1 
ATOM   1092 H HG3  A LYS   A 1 44  ? 30.353 9.427   -4.271  0.74 19.95 ?  44  LYS   A HG3  1 
ATOM   1093 H HG3  B LYS   A 1 44  ? 30.162 9.400   -4.308  0.26 20.16 ?  44  LYS   A HG3  1 
ATOM   1094 H HD2  A LYS   A 1 44  ? 30.463 10.592  -2.226  0.74 26.33 ?  44  LYS   A HD2  1 
ATOM   1095 H HD2  B LYS   A 1 44  ? 30.490 10.507  -2.277  0.26 23.33 ?  44  LYS   A HD2  1 
ATOM   1096 H HD3  A LYS   A 1 44  ? 31.229 9.350   -1.586  0.74 26.33 ?  44  LYS   A HD3  1 
ATOM   1097 H HD3  B LYS   A 1 44  ? 31.180 9.203   -1.674  0.26 23.33 ?  44  LYS   A HD3  1 
ATOM   1098 H HE2  A LYS   A 1 44  ? 32.906 9.678   -3.289  0.74 30.14 ?  44  LYS   A HE2  1 
ATOM   1099 H HE2  B LYS   A 1 44  ? 32.853 9.387   -3.337  0.26 25.22 ?  44  LYS   A HE2  1 
ATOM   1100 H HE3  A LYS   A 1 44  ? 32.235 11.099  -3.530  0.74 30.14 ?  44  LYS   A HE3  1 
ATOM   1101 H HE3  B LYS   A 1 44  ? 32.263 10.823  -3.680  0.26 25.22 ?  44  LYS   A HE3  1 
ATOM   1102 H HZ1  A LYS   A 1 44  ? 33.979 11.279  -2.087  0.74 32.14 ?  44  LYS   A HZ1  1 
ATOM   1103 H HZ1  B LYS   A 1 44  ? 34.002 11.003  -2.229  0.26 25.95 ?  44  LYS   A HZ1  1 
ATOM   1104 H HZ2  A LYS   A 1 44  ? 32.764 11.635  -1.383  0.74 32.14 ?  44  LYS   A HZ2  1 
ATOM   1105 H HZ2  B LYS   A 1 44  ? 32.801 11.470  -1.566  0.26 25.95 ?  44  LYS   A HZ2  1 
ATOM   1106 H HZ3  A LYS   A 1 44  ? 33.375 10.340  -1.163  0.74 32.14 ?  44  LYS   A HZ3  1 
ATOM   1107 H HZ3  B LYS   A 1 44  ? 33.339 10.161  -1.254  0.26 25.95 ?  44  LYS   A HZ3  1 
ATOM   1108 N N    A HIS   A 1 45  ? 27.336 8.012   0.091   0.74 9.74  ?  45  HIS   A N    1 
ATOM   1109 N N    B HIS   A 1 45  ? 27.385 8.046   0.233   0.26 11.45 ?  45  HIS   A N    1 
ATOM   1110 C CA   A HIS   A 1 45  ? 26.094 7.656   0.778   0.74 9.77  ?  45  HIS   A CA   1 
ATOM   1111 C CA   B HIS   A 1 45  ? 26.135 7.813   0.954   0.26 11.49 ?  45  HIS   A CA   1 
ATOM   1112 C C    A HIS   A 1 45  ? 25.060 8.772   0.607   0.74 10.46 ?  45  HIS   A C    1 
ATOM   1113 C C    B HIS   A 1 45  ? 25.264 9.062   0.850   0.26 11.94 ?  45  HIS   A C    1 
ATOM   1114 O O    A HIS   A 1 45  ? 24.732 9.512   1.534   0.74 11.41 ?  45  HIS   A O    1 
ATOM   1115 O O    B HIS   A 1 45  ? 25.119 9.836   1.795   0.26 12.66 ?  45  HIS   A O    1 
ATOM   1116 C CB   A HIS   A 1 45  ? 26.377 7.398   2.248   0.74 9.95  ?  45  HIS   A CB   1 
ATOM   1117 C CB   B HIS   A 1 45  ? 26.420 7.455   2.405   0.26 11.31 ?  45  HIS   A CB   1 
ATOM   1118 C CG   A HIS   A 1 45  ? 27.492 6.430   2.488   0.74 9.53  ?  45  HIS   A CG   1 
ATOM   1119 C CG   B HIS   A 1 45  ? 27.526 6.463   2.577   0.26 11.09 ?  45  HIS   A CG   1 
ATOM   1120 N ND1  A HIS   A 1 45  ? 27.491 5.142   1.987   0.74 9.72  ?  45  HIS   A ND1  1 
ATOM   1121 N ND1  B HIS   A 1 45  ? 27.471 5.185   2.061   0.26 11.36 ?  45  HIS   A ND1  1 
ATOM   1122 C CD2  A HIS   A 1 45  ? 28.654 6.581   3.169   0.74 9.85  ?  45  HIS   A CD2  1 
ATOM   1123 C CD2  B HIS   A 1 45  ? 28.717 6.565   3.212   0.26 11.06 ?  45  HIS   A CD2  1 
ATOM   1124 C CE1  A HIS   A 1 45  ? 28.608 4.545   2.364   0.74 9.46  ?  45  HIS   A CE1  1 
ATOM   1125 C CE1  B HIS   A 1 45  ? 28.584 4.544   2.372   0.26 11.03 ?  45  HIS   A CE1  1 
ATOM   1126 N NE2  A HIS   A 1 45  ? 29.329 5.391   3.084   0.74 9.81  ?  45  HIS   A NE2  1 
ATOM   1127 N NE2  B HIS   A 1 45  ? 29.356 5.358   3.072   0.26 11.04 ?  45  HIS   A NE2  1 
ATOM   1128 H H    A HIS   A 1 45  ? 27.866 8.487   0.573   0.74 11.69 ?  45  HIS   A H    1 
ATOM   1129 H H    B HIS   A 1 45  ? 27.979 8.474   0.691   0.26 13.74 ?  45  HIS   A H    1 
ATOM   1130 H HA   A HIS   A 1 45  ? 25.725 6.843   0.394   0.74 11.72 ?  45  HIS   A HA   1 
ATOM   1131 H HA   B HIS   A 1 45  ? 25.660 7.077   0.540   0.26 13.78 ?  45  HIS   A HA   1 
ATOM   1132 H HB2  A HIS   A 1 45  ? 26.607 8.237   2.677   0.74 11.94 ?  45  HIS   A HB2  1 
ATOM   1133 H HB2  B HIS   A 1 45  ? 26.664 8.262   2.882   0.26 13.57 ?  45  HIS   A HB2  1 
ATOM   1134 H HB3  A HIS   A 1 45  ? 25.573 7.033   2.665   0.74 11.94 ?  45  HIS   A HB3  1 
ATOM   1135 H HB3  B HIS   A 1 45  ? 25.615 7.075   2.790   0.26 13.57 ?  45  HIS   A HB3  1 
ATOM   1136 H HD2  A HIS   A 1 45  ? 28.939 7.350   3.615   0.74 11.82 ?  45  HIS   A HD2  1 
ATOM   1137 H HD2  B HIS   A 1 45  ? 29.040 7.314   3.659   0.26 13.27 ?  45  HIS   A HD2  1 
ATOM   1138 H HE1  A HIS   A 1 45  ? 28.844 3.669   2.170   0.74 11.35 ?  45  HIS   A HE1  1 
ATOM   1139 H HE1  B HIS   A 1 45  ? 28.788 3.667   2.142   0.26 13.24 ?  45  HIS   A HE1  1 
ATOM   1140 H HE2  A HIS   A 1 45  ? 30.098 5.226   3.434   0.74 11.77 ?  45  HIS   A HE2  1 
ATOM   1141 H HE2  B HIS   A 1 45  ? 30.132 5.164   3.386   0.26 13.25 ?  45  HIS   A HE2  1 
ATOM   1142 N N    A GLY   A 1 46  ? 24.517 8.859   -0.603  0.74 11.61 ?  46  GLY   A N    1 
ATOM   1143 N N    B GLY   A 1 46  ? 24.665 9.248   -0.321  0.26 11.91 ?  46  GLY   A N    1 
ATOM   1144 C CA   A GLY   A 1 46  ? 23.700 9.999   -0.974  0.74 12.13 ?  46  GLY   A CA   1 
ATOM   1145 C CA   B GLY   A 1 46  ? 23.833 10.414  -0.546  0.26 11.46 ?  46  GLY   A CA   1 
ATOM   1146 C C    A GLY   A 1 46  ? 22.222 9.895   -0.666  0.74 12.31 ?  46  GLY   A C    1 
ATOM   1147 C C    B GLY   A 1 46  ? 22.346 10.126  -0.468  0.26 11.06 ?  46  GLY   A C    1 
ATOM   1148 O O    A GLY   A 1 46  ? 21.570 10.911  -0.397  0.74 13.54 ?  46  GLY   A O    1 
ATOM   1149 O O    B GLY   A 1 46  ? 21.574 10.957  0.020   0.26 11.44 ?  46  GLY   A O    1 
ATOM   1150 H H    A GLY   A 1 46  ? 24.591 8.263   -1.213  0.74 13.93 ?  46  GLY   A H    1 
ATOM   1151 H H    B GLY   A 1 46  ? 24.721 8.713   -0.996  0.26 14.29 ?  46  GLY   A H    1 
ATOM   1152 H HA2  A GLY   A 1 46  ? 24.022 10.783  -0.514  0.74 14.56 ?  46  GLY   A HA2  1 
ATOM   1153 H HA2  B GLY   A 1 46  ? 24.051 11.095  0.112   0.26 13.75 ?  46  GLY   A HA2  1 
ATOM   1154 H HA3  A GLY   A 1 46  ? 23.781 10.144  -1.925  0.74 14.56 ?  46  GLY   A HA3  1 
ATOM   1155 H HA3  B GLY   A 1 46  ? 24.026 10.775  -1.424  0.26 13.75 ?  46  GLY   A HA3  1 
ATOM   1156 N N    A GLY   A 1 47  ? 21.667 8.690   -0.736  0.74 11.88 ?  47  GLY   A N    1 
ATOM   1157 N N    B GLY   A 1 47  ? 21.931 8.950   -0.948  0.26 10.89 ?  47  GLY   A N    1 
ATOM   1158 C CA   A GLY   A 1 47  ? 20.232 8.517   -0.623  0.74 12.37 ?  47  GLY   A CA   1 
ATOM   1159 C CA   B GLY   A 1 47  ? 20.525 8.623   -1.047  0.26 10.72 ?  47  GLY   A CA   1 
ATOM   1160 C C    A GLY   A 1 47  ? 19.897 7.074   -0.318  0.74 11.52 ?  47  GLY   A C    1 
ATOM   1161 C C    B GLY   A 1 47  ? 20.249 7.206   -0.580  0.26 10.96 ?  47  GLY   A C    1 
ATOM   1162 O O    A GLY   A 1 47  ? 20.778 6.234   -0.122  0.74 11.35 ?  47  GLY   A O    1 
ATOM   1163 O O    B GLY   A 1 47  ? 21.164 6.433   -0.294  0.26 11.49 ?  47  GLY   A O    1 
ATOM   1164 H H    A GLY   A 1 47  ? 22.096 7.955   -0.844  0.74 14.26 ?  47  GLY   A H    1 
ATOM   1165 H H    B GLY   A 1 47  ? 22.459 8.336   -1.221  0.26 13.07 ?  47  GLY   A H    1 
ATOM   1166 H HA2  A GLY   A 1 47  ? 19.882 9.070   0.092   0.74 14.85 ?  47  GLY   A HA2  1 
ATOM   1167 H HA2  B GLY   A 1 47  ? 20.005 9.232   -0.501  0.26 12.87 ?  47  GLY   A HA2  1 
ATOM   1168 H HA3  A GLY   A 1 47  ? 19.799 8.765   -1.455  0.74 14.85 ?  47  GLY   A HA3  1 
ATOM   1169 H HA3  B GLY   A 1 47  ? 20.243 8.718   -1.972  0.26 12.87 ?  47  GLY   A HA3  1 
ATOM   1170 N N    A GLY   A 1 48  ? 18.598 6.789   -0.294  0.74 11.83 ?  48  GLY   A N    1 
ATOM   1171 N N    B GLY   A 1 48  ? 18.963 6.878   -0.512  0.26 11.06 ?  48  GLY   A N    1 
ATOM   1172 C CA   A GLY   A 1 48  ? 18.154 5.469   0.092   0.74 11.58 ?  48  GLY   A CA   1 
ATOM   1173 C CA   B GLY   A 1 48  ? 18.571 5.561   -0.041  0.26 11.01 ?  48  GLY   A CA   1 
ATOM   1174 C C    A GLY   A 1 48  ? 18.617 5.131   1.498   0.74 11.26 ?  48  GLY   A C    1 
ATOM   1175 C C    B GLY   A 1 48  ? 18.958 5.336   1.418   0.26 10.59 ?  48  GLY   A C    1 
ATOM   1176 O O    A GLY   A 1 48  ? 18.765 6.003   2.368   0.74 11.59 ?  48  GLY   A O    1 
ATOM   1177 O O    B GLY   A 1 48  ? 19.192 6.269   2.191   0.26 10.33 ?  48  GLY   A O    1 
ATOM   1178 H H    A GLY   A 1 48  ? 17.966 7.333   -0.492  0.74 14.19 ?  48  GLY   A H    1 
ATOM   1179 H H    B GLY   A 1 48  ? 18.312 7.390   -0.733  0.26 13.27 ?  48  GLY   A H    1 
ATOM   1180 H HA2  A GLY   A 1 48  ? 17.187 5.416   0.054   0.74 13.89 ?  48  GLY   A HA2  1 
ATOM   1181 H HA2  B GLY   A 1 48  ? 17.610 5.461   -0.127  0.26 13.21 ?  48  GLY   A HA2  1 
ATOM   1182 H HA3  A GLY   A 1 48  ? 18.521 4.802   -0.522  0.74 13.89 ?  48  GLY   A HA3  1 
ATOM   1183 H HA3  B GLY   A 1 48  ? 18.999 4.878   -0.585  0.26 13.21 ?  48  GLY   A HA3  1 
ATOM   1184 N N    A VAL   A 1 49  ? 18.854 3.837   1.725   0.74 11.08 ?  49  VAL   A N    1 
ATOM   1185 N N    B VAL   A 1 49  ? 19.022 4.054   1.789   0.26 10.50 ?  49  VAL   A N    1 
ATOM   1186 C CA   A VAL   A 1 49  ? 19.349 3.384   3.022   0.74 11.18 ?  49  VAL   A CA   1 
ATOM   1187 C CA   B VAL   A 1 49  ? 19.402 3.699   3.156   0.26 10.82 ?  49  VAL   A CA   1 
ATOM   1188 C C    A VAL   A 1 49  ? 20.645 4.098   3.379   0.74 10.06 ?  49  VAL   A C    1 
ATOM   1189 C C    B VAL   A 1 49  ? 20.807 4.191   3.485   0.26 9.87  ?  49  VAL   A C    1 
ATOM   1190 O O    A VAL   A 1 49  ? 20.828 4.542   4.516   0.74 10.16 ?  49  VAL   A O    1 
ATOM   1191 O O    B VAL   A 1 49  ? 21.111 4.478   4.650   0.26 9.73  ?  49  VAL   A O    1 
ATOM   1192 C CB   A VAL   A 1 49  ? 19.530 1.853   3.027   0.74 12.07 ?  49  VAL   A CB   1 
ATOM   1193 C CB   B VAL   A 1 49  ? 19.252 2.182   3.387   0.26 12.22 ?  49  VAL   A CB   1 
ATOM   1194 C CG1  A VAL   A 1 49  ? 20.347 1.410   4.251   0.74 12.00 ?  49  VAL   A CG1  1 
ATOM   1195 C CG1  B VAL   A 1 49  ? 20.095 1.421   2.402   0.26 12.62 ?  49  VAL   A CG1  1 
ATOM   1196 C CG2  A VAL   A 1 49  ? 18.180 1.159   2.994   0.74 13.58 ?  49  VAL   A CG2  1 
ATOM   1197 C CG2  B VAL   A 1 49  ? 19.646 1.810   4.809   0.26 13.20 ?  49  VAL   A CG2  1 
ATOM   1198 H H    A VAL   A 1 49  ? 18.742 3.205   1.147   0.74 13.30 ?  49  VAL   A H    1 
ATOM   1199 H H    B VAL   A 1 49  ? 18.851 3.381   1.278   0.26 12.59 ?  49  VAL   A H    1 
ATOM   1200 H HA   A VAL   A 1 49  ? 18.691 3.602   3.701   0.74 13.42 ?  49  VAL   A HA   1 
ATOM   1201 H HA   B VAL   A 1 49  ? 18.799 4.143   3.766   0.26 12.98 ?  49  VAL   A HA   1 
ATOM   1202 H HB   A VAL   A 1 49  ? 20.022 1.590   2.234   0.74 14.49 ?  49  VAL   A HB   1 
ATOM   1203 H HB   B VAL   A 1 49  ? 18.325 1.929   3.258   0.26 14.66 ?  49  VAL   A HB   1 
ATOM   1204 H HG11 A VAL   A 1 49  ? 20.208 0.463   4.397   0.74 14.40 ?  49  VAL   A HG11 1 
ATOM   1205 H HG11 B VAL   A 1 49  ? 20.038 0.477   2.614   0.26 15.14 ?  49  VAL   A HG11 1 
ATOM   1206 H HG12 A VAL   A 1 49  ? 21.288 1.584   4.087   0.74 14.40 ?  49  VAL   A HG12 1 
ATOM   1207 H HG12 B VAL   A 1 49  ? 19.757 1.581   1.510   0.26 15.14 ?  49  VAL   A HG12 1 
ATOM   1208 H HG13 A VAL   A 1 49  ? 20.048 1.911   5.028   0.74 14.40 ?  49  VAL   A HG13 1 
ATOM   1209 H HG13 B VAL   A 1 49  ? 21.012 1.721   2.474   0.26 15.14 ?  49  VAL   A HG13 1 
ATOM   1210 H HG21 A VAL   A 1 49  ? 18.319 0.196   2.996   0.74 16.29 ?  49  VAL   A HG21 1 
ATOM   1211 H HG21 B VAL   A 1 49  ? 19.417 0.881   4.965   0.26 15.84 ?  49  VAL   A HG21 1 
ATOM   1212 H HG22 A VAL   A 1 49  ? 17.671 1.418   3.778   0.74 16.29 ?  49  VAL   A HG22 1 
ATOM   1213 H HG22 B VAL   A 1 49  ? 20.605 1.932   4.916   0.26 15.84 ?  49  VAL   A HG22 1 
ATOM   1214 H HG23 A VAL   A 1 49  ? 17.709 1.422   2.190   0.74 16.29 ?  49  VAL   A HG23 1 
ATOM   1215 H HG23 B VAL   A 1 49  ? 19.169 2.379   5.431   0.26 15.84 ?  49  VAL   A HG23 1 
ATOM   1216 N N    A ALA   A 1 50  ? 21.580 4.173   2.428   0.74 9.72  ?  50  ALA   A N    1 
ATOM   1217 N N    B ALA   A 1 50  ? 21.691 4.273   2.486   0.26 9.73  ?  50  ALA   A N    1 
ATOM   1218 C CA   A ALA   A 1 50  ? 22.894 4.734   2.732   0.74 9.37  ?  50  ALA   A CA   1 
ATOM   1219 C CA   B ALA   A 1 50  ? 23.035 4.785   2.736   0.26 9.65  ?  50  ALA   A CA   1 
ATOM   1220 C C    A ALA   A 1 50  ? 22.787 6.188   3.169   0.74 9.45  ?  50  ALA   A C    1 
ATOM   1221 C C    B ALA   A 1 50  ? 22.989 6.249   3.151   0.26 9.30  ?  50  ALA   A C    1 
ATOM   1222 O O    A ALA   A 1 50  ? 23.431 6.606   4.139   0.74 9.96  ?  50  ALA   A O    1 
ATOM   1223 O O    B ALA   A 1 50  ? 23.600 6.646   4.151   0.26 9.34  ?  50  ALA   A O    1 
ATOM   1224 C CB   A ALA   A 1 50  ? 23.808 4.617   1.516   0.74 9.61  ?  50  ALA   A CB   1 
ATOM   1225 C CB   B ALA   A 1 50  ? 23.910 4.604   1.494   0.26 9.78  ?  50  ALA   A CB   1 
ATOM   1226 H H    A ALA   A 1 50  ? 21.478 3.908   1.615   0.74 11.66 ?  50  ALA   A H    1 
ATOM   1227 H H    B ALA   A 1 50  ? 21.542 4.045   1.671   0.26 11.67 ?  50  ALA   A H    1 
ATOM   1228 H HA   A ALA   A 1 50  ? 23.292 4.231   3.461   0.74 11.24 ?  50  ALA   A HA   1 
ATOM   1229 H HA   B ALA   A 1 50  ? 23.440 4.287   3.462   0.26 11.58 ?  50  ALA   A HA   1 
ATOM   1230 H HB1  A ALA   A 1 50  ? 24.675 4.994   1.737   0.74 11.53 ?  50  ALA   A HB1  1 
ATOM   1231 H HB1  B ALA   A 1 50  ? 24.800 4.949   1.677   0.26 11.74 ?  50  ALA   A HB1  1 
ATOM   1232 H HB2  A ALA   A 1 50  ? 23.905 3.681   1.280   0.74 11.53 ?  50  ALA   A HB2  1 
ATOM   1233 H HB2  B ALA   A 1 50  ? 23.963 3.659   1.278   0.26 11.74 ?  50  ALA   A HB2  1 
ATOM   1234 H HB3  A ALA   A 1 50  ? 23.414 5.106   0.777   0.74 11.53 ?  50  ALA   A HB3  1 
ATOM   1235 H HB3  B ALA   A 1 50  ? 23.516 5.091   0.753   0.26 11.74 ?  50  ALA   A HB3  1 
ATOM   1236 N N    A GLY   A 1 51  ? 22.001 6.984   2.445   0.74 9.50  ?  51  GLY   A N    1 
ATOM   1237 N N    B GLY   A 1 51  ? 22.275 7.073   2.385   0.26 9.04  ?  51  GLY   A N    1 
ATOM   1238 C CA   A GLY   A 1 51  ? 21.830 8.371   2.836   0.74 10.14 ?  51  GLY   A CA   1 
ATOM   1239 C CA   B GLY   A 1 51  ? 22.138 8.469   2.760   0.26 8.83  ?  51  GLY   A CA   1 
ATOM   1240 C C    A GLY   A 1 51  ? 21.253 8.503   4.232   0.74 10.17 ?  51  GLY   A C    1 
ATOM   1241 C C    B GLY   A 1 51  ? 21.405 8.641   4.075   0.26 8.78  ?  51  GLY   A C    1 
ATOM   1242 O O    A GLY   A 1 51  ? 21.670 9.367   5.008   0.74 10.90 ?  51  GLY   A O    1 
ATOM   1243 O O    B GLY   A 1 51  ? 21.711 9.548   4.853   0.26 9.07  ?  51  GLY   A O    1 
ATOM   1244 H H    A GLY   A 1 51  ? 21.579 6.746   1.732   0.74 11.40 ?  51  GLY   A H    1 
ATOM   1245 H H    B GLY   A 1 51  ? 21.878 6.851   1.657   0.26 10.85 ?  51  GLY   A H    1 
ATOM   1246 H HA2  A GLY   A 1 51  ? 22.692 8.821   2.808   0.74 12.17 ?  51  GLY   A HA2  1 
ATOM   1247 H HA2  B GLY   A 1 51  ? 23.019 8.871   2.843   0.26 10.59 ?  51  GLY   A HA2  1 
ATOM   1248 H HA3  A GLY   A 1 51  ? 21.238 8.809   2.203   0.74 12.17 ?  51  GLY   A HA3  1 
ATOM   1249 H HA3  B GLY   A 1 51  ? 21.648 8.941   2.072   0.26 10.59 ?  51  GLY   A HA3  1 
ATOM   1250 N N    A ALA   A 1 52  ? 20.285 7.642   4.571   0.74 10.15 ?  52  ALA   A N    1 
ATOM   1251 N N    B ALA   A 1 52  ? 20.421 7.776   4.339   0.26 9.30  ?  52  ALA   A N    1 
ATOM   1252 C CA   A ALA   A 1 52  ? 19.655 7.704   5.887   0.74 10.60 ?  52  ALA   A CA   1 
ATOM   1253 C CA   B ALA   A 1 52  ? 19.691 7.844   5.601   0.26 9.58  ?  52  ALA   A CA   1 
ATOM   1254 C C    A ALA   A 1 52  ? 20.610 7.265   6.996   0.74 9.70  ?  52  ALA   A C    1 
ATOM   1255 C C    B ALA   A 1 52  ? 20.587 7.468   6.778   0.26 9.38  ?  52  ALA   A C    1 
ATOM   1256 O O    A ALA   A 1 52  ? 20.683 7.908   8.050   0.74 10.48 ?  52  ALA   A O    1 
ATOM   1257 O O    B ALA   A 1 52  ? 20.629 8.178   7.789   0.26 9.37  ?  52  ALA   A O    1 
ATOM   1258 C CB   A ALA   A 1 52  ? 18.376 6.865   5.889   0.74 11.75 ?  52  ALA   A CB   1 
ATOM   1259 C CB   B ALA   A 1 52  ? 18.457 6.941   5.543   0.26 9.87  ?  52  ALA   A CB   1 
ATOM   1260 H H    A ALA   A 1 52  ? 19.992 7.012   4.056   0.74 12.18 ?  52  ALA   A H    1 
ATOM   1261 H H    B ALA   A 1 52  ? 20.161 7.151   3.809   0.26 11.16 ?  52  ALA   A H    1 
ATOM   1262 H HA   A ALA   A 1 52  ? 19.407 8.621   6.055   0.74 12.72 ?  52  ALA   A HA   1 
ATOM   1263 H HA   B ALA   A 1 52  ? 19.386 8.752   5.738   0.26 11.50 ?  52  ALA   A HA   1 
ATOM   1264 H HB1  A ALA   A 1 52  ? 17.970 6.921   6.768   0.74 14.10 ?  52  ALA   A HB1  1 
ATOM   1265 H HB1  B ALA   A 1 52  ? 17.983 6.998   6.389   0.26 11.85 ?  52  ALA   A HB1  1 
ATOM   1266 H HB2  A ALA   A 1 52  ? 17.765 7.216   5.220   0.74 14.10 ?  52  ALA   A HB2  1 
ATOM   1267 H HB2  B ALA   A 1 52  ? 17.881 7.239   4.822   0.26 11.85 ?  52  ALA   A HB2  1 
ATOM   1268 H HB3  A ALA   A 1 52  ? 18.597 5.944   5.683   0.74 14.10 ?  52  ALA   A HB3  1 
ATOM   1269 H HB3  B ALA   A 1 52  ? 18.740 6.026   5.385   0.26 11.85 ?  52  ALA   A HB3  1 
ATOM   1270 N N    A LEU   A 1 53  ? 21.350 6.171   6.788   0.74 9.67  ?  53  LEU   A N    1 
ATOM   1271 N N    B LEU   A 1 53  ? 21.314 6.353   6.667   0.26 9.18  ?  53  LEU   A N    1 
ATOM   1272 C CA   A LEU   A 1 53  ? 22.328 5.753   7.791   0.74 10.01 ?  53  LEU   A CA   1 
ATOM   1273 C CA   B LEU   A 1 53  ? 22.215 5.949   7.744   0.26 9.51  ?  53  LEU   A CA   1 
ATOM   1274 C C    A LEU   A 1 53  ? 23.380 6.833   7.992   0.74 9.74  ?  53  LEU   A C    1 
ATOM   1275 C C    B LEU   A 1 53  ? 23.295 7.002   7.968   0.26 9.23  ?  53  LEU   A C    1 
ATOM   1276 O O    A LEU   A 1 53  ? 23.736 7.170   9.124   0.74 10.78 ?  53  LEU   A O    1 
ATOM   1277 O O    B LEU   A 1 53  ? 23.548 7.417   9.104   0.26 9.18  ?  53  LEU   A O    1 
ATOM   1278 C CB   A LEU   A 1 53  ? 23.001 4.438   7.389   0.74 10.39 ?  53  LEU   A CB   1 
ATOM   1279 C CB   B LEU   A 1 53  ? 22.842 4.585   7.433   0.26 9.93  ?  53  LEU   A CB   1 
ATOM   1280 C CG   A LEU   A 1 53  ? 22.148 3.165   7.453   0.74 11.16 ?  53  LEU   A CG   1 
ATOM   1281 C CG   B LEU   A 1 53  ? 21.937 3.345   7.481   0.26 10.40 ?  53  LEU   A CG   1 
ATOM   1282 C CD1  A LEU   A 1 53  ? 22.895 2.007   6.815   0.74 12.15 ?  53  LEU   A CD1  1 
ATOM   1283 C CD1  B LEU   A 1 53  ? 22.684 2.135   6.941   0.26 10.73 ?  53  LEU   A CD1  1 
ATOM   1284 C CD2  A LEU   A 1 53  ? 21.769 2.811   8.886   0.74 12.15 ?  53  LEU   A CD2  1 
ATOM   1285 C CD2  B LEU   A 1 53  ? 21.437 3.064   8.891   0.26 11.05 ?  53  LEU   A CD2  1 
ATOM   1286 H H    A LEU   A 1 53  ? 21.304 5.660   6.089   0.74 11.61 ?  53  LEU   A H    1 
ATOM   1287 H H    B LEU   A 1 53  ? 21.305 5.824   5.991   0.26 11.02 ?  53  LEU   A H    1 
ATOM   1288 H HA   A LEU   A 1 53  ? 21.871 5.614   8.634   0.74 12.01 ?  53  LEU   A HA   1 
ATOM   1289 H HA   B LEU   A 1 53  ? 21.710 5.867   8.565   0.26 11.42 ?  53  LEU   A HA   1 
ATOM   1290 H HB2  A LEU   A 1 53  ? 23.312 4.527   6.475   0.74 12.47 ?  53  LEU   A HB2  1 
ATOM   1291 H HB2  B LEU   A 1 53  ? 23.213 4.623   6.538   0.26 11.92 ?  53  LEU   A HB2  1 
ATOM   1292 H HB3  A LEU   A 1 53  ? 23.761 4.301   7.974   0.74 12.47 ?  53  LEU   A HB3  1 
ATOM   1293 H HB3  B LEU   A 1 53  ? 23.558 4.430   8.067   0.26 11.92 ?  53  LEU   A HB3  1 
ATOM   1294 H HG   A LEU   A 1 53  ? 21.331 3.307   6.950   0.74 13.40 ?  53  LEU   A HG   1 
ATOM   1295 H HG   B LEU   A 1 53  ? 21.164 3.490   6.913   0.26 12.48 ?  53  LEU   A HG   1 
ATOM   1296 H HD11 A LEU   A 1 53  ? 22.345 1.210   6.866   0.74 14.58 ?  53  LEU   A HD11 1 
ATOM   1297 H HD11 B LEU   A 1 53  ? 22.104 1.358   6.983   0.26 12.88 ?  53  LEU   A HD11 1 
ATOM   1298 H HD12 A LEU   A 1 53  ? 23.081 2.223   5.888   0.74 14.58 ?  53  LEU   A HD12 1 
ATOM   1299 H HD12 B LEU   A 1 53  ? 22.942 2.307   6.022   0.26 12.88 ?  53  LEU   A HD12 1 
ATOM   1300 H HD13 A LEU   A 1 53  ? 23.727 1.866   7.295   0.74 14.58 ?  53  LEU   A HD13 1 
ATOM   1301 H HD13 B LEU   A 1 53  ? 23.475 1.985   7.483   0.26 12.88 ?  53  LEU   A HD13 1 
ATOM   1302 H HD21 A LEU   A 1 53  ? 21.264 1.982   8.884   0.74 14.58 ?  53  LEU   A HD21 1 
ATOM   1303 H HD21 B LEU   A 1 53  ? 20.589 2.597   8.838   0.26 13.26 ?  53  LEU   A HD21 1 
ATOM   1304 H HD22 A LEU   A 1 53  ? 22.578 2.703   9.410   0.74 14.58 ?  53  LEU   A HD22 1 
ATOM   1305 H HD22 B LEU   A 1 53  ? 22.089 2.512   9.351   0.26 13.26 ?  53  LEU   A HD22 1 
ATOM   1306 H HD23 A LEU   A 1 53  ? 21.227 3.526   9.257   0.74 14.58 ?  53  LEU   A HD23 1 
ATOM   1307 H HD23 B LEU   A 1 53  ? 21.324 3.901   9.364   0.26 13.26 ?  53  LEU   A HD23 1 
ATOM   1308 N N    A ASN   A 1 54  ? 23.891 7.391   6.896   0.74 9.37  ?  54  ASN   A N    1 
ATOM   1309 N N    B ASN   A 1 54  ? 23.931 7.461   6.888   0.26 9.48  ?  54  ASN   A N    1 
ATOM   1310 C CA   A ASN   A 1 54  ? 24.942 8.389   7.029   0.74 9.39  ?  54  ASN   A CA   1 
ATOM   1311 C CA   B ASN   A 1 54  ? 24.996 8.448   7.030   0.26 9.86  ?  54  ASN   A CA   1 
ATOM   1312 C C    A ASN   A 1 54  ? 24.435 9.631   7.762   0.74 9.75  ?  54  ASN   A C    1 
ATOM   1313 C C    B ASN   A 1 54  ? 24.485 9.723   7.689   0.26 10.04 ?  54  ASN   A C    1 
ATOM   1314 O O    A ASN   A 1 54  ? 25.111 10.156  8.657   0.74 9.86  ?  54  ASN   A O    1 
ATOM   1315 O O    B ASN   A 1 54  ? 25.210 10.366  8.458   0.26 10.23 ?  54  ASN   A O    1 
ATOM   1316 C CB   A ASN   A 1 54  ? 25.498 8.760   5.664   0.74 9.80  ?  54  ASN   A CB   1 
ATOM   1317 C CB   B ASN   A 1 54  ? 25.617 8.764   5.672   0.26 10.35 ?  54  ASN   A CB   1 
ATOM   1318 C CG   A ASN   A 1 54  ? 26.548 9.837   5.774   0.74 9.98  ?  54  ASN   A CG   1 
ATOM   1319 C CG   B ASN   A 1 54  ? 26.572 9.936   5.744   0.26 10.53 ?  54  ASN   A CG   1 
ATOM   1320 O OD1  A ASN   A 1 54  ? 27.533 9.684   6.509   0.74 9.61  ?  54  ASN   A OD1  1 
ATOM   1321 O OD1  B ASN   A 1 54  ? 27.627 9.848   6.374   0.26 10.64 ?  54  ASN   A OD1  1 
ATOM   1322 N ND2  A ASN   A 1 54  ? 26.334 10.951  5.095   0.74 11.29 ?  54  ASN   A ND2  1 
ATOM   1323 N ND2  B ASN   A 1 54  ? 26.201 11.047  5.120   0.26 10.94 ?  54  ASN   A ND2  1 
ATOM   1324 H H    A ASN   A 1 54  ? 23.648 7.211   6.090   0.74 11.24 ?  54  ASN   A H    1 
ATOM   1325 H H    B ASN   A 1 54  ? 23.764 7.220   6.083   0.26 11.38 ?  54  ASN   A H    1 
ATOM   1326 H HA   A ASN   A 1 54  ? 25.660 8.009   7.553   0.74 11.27 ?  54  ASN   A HA   1 
ATOM   1327 H HA   B ASN   A 1 54  ? 25.689 8.086   7.599   0.26 11.83 ?  54  ASN   A HA   1 
ATOM   1328 H HB2  A ASN   A 1 54  ? 25.906 7.968   5.265   0.74 11.76 ?  54  ASN   A HB2  1 
ATOM   1329 H HB2  B ASN   A 1 54  ? 26.113 7.987   5.366   0.26 12.42 ?  54  ASN   A HB2  1 
ATOM   1330 H HB3  A ASN   A 1 54  ? 24.781 9.083   5.101   0.74 11.76 ?  54  ASN   A HB3  1 
ATOM   1331 H HB3  B ASN   A 1 54  ? 24.914 8.982   5.043   0.26 12.42 ?  54  ASN   A HB3  1 
ATOM   1332 H HD21 A ASN   A 1 54  ? 26.905 11.592  5.137   0.74 13.55 ?  54  ASN   A HD21 1 
ATOM   1333 H HD21 B ASN   A 1 54  ? 26.710 11.741  5.137   0.26 13.13 ?  54  ASN   A HD21 1 
ATOM   1334 H HD22 A ASN   A 1 54  ? 25.632 11.027  4.608   0.74 13.55 ?  54  ASN   A HD22 1 
ATOM   1335 H HD22 B ASN   A 1 54  ? 25.457 11.071  4.691   0.26 13.13 ?  54  ASN   A HD22 1 
ATOM   1336 N N    . LYS   A 1 55  ? 23.240 10.109  7.400   1.00 10.10 ?  55  LYS   A N    1 
ATOM   1337 C CA   . LYS   A 1 55  ? 22.661 11.269  8.065   1.00 10.82 ?  55  LYS   A CA   1 
ATOM   1338 C C    . LYS   A 1 55  ? 22.561 11.037  9.568   1.00 10.99 ?  55  LYS   A C    1 
ATOM   1339 O O    . LYS   A 1 55  ? 22.845 11.940  10.365  1.00 11.77 ?  55  LYS   A O    1 
ATOM   1340 C CB   . LYS   A 1 55  ? 21.289 11.568  7.450   1.00 11.62 ?  55  LYS   A CB   1 
ATOM   1341 C CG   . LYS   A 1 55  ? 20.530 12.726  8.085   1.00 13.05 ?  55  LYS   A CG   1 
ATOM   1342 C CD   . LYS   A 1 55  ? 19.208 12.964  7.357   1.00 14.57 ?  55  LYS   A CD   1 
ATOM   1343 C CE   . LYS   A 1 55  ? 18.383 14.067  7.998   1.00 16.73 ?  55  LYS   A CE   1 
ATOM   1344 N NZ   . LYS   A 1 55  ? 17.048 14.210  7.350   1.00 17.13 ?  55  LYS   A NZ   1 
ATOM   1345 H H    A LYS   A 1 55  ? 22.741 9.771   6.784   0.74 12.12 ?  55  LYS   A H    1 
ATOM   1346 H H    B LYS   A 1 55  ? 22.712 9.712   6.845   0.26 12.12 ?  55  LYS   A H    1 
ATOM   1347 H HA   . LYS   A 1 55  ? 23.232 12.036  7.919   1.00 12.98 ?  55  LYS   A HA   1 
ATOM   1348 H HB2  . LYS   A 1 55  ? 21.416 11.786  6.513   1.00 13.95 ?  55  LYS   A HB2  1 
ATOM   1349 H HB3  . LYS   A 1 55  ? 20.735 10.778  7.528   1.00 13.95 ?  55  LYS   A HB3  1 
ATOM   1350 H HG2  . LYS   A 1 55  ? 20.331 12.511  9.012   1.00 15.66 ?  55  LYS   A HG2  1 
ATOM   1351 H HG3  . LYS   A 1 55  ? 21.062 13.532  8.030   1.00 15.66 ?  55  LYS   A HG3  1 
ATOM   1352 H HD2  . LYS   A 1 55  ? 19.398 13.217  6.440   1.00 17.48 ?  55  LYS   A HD2  1 
ATOM   1353 H HD3  . LYS   A 1 55  ? 18.687 12.145  7.374   1.00 17.48 ?  55  LYS   A HD3  1 
ATOM   1354 H HE2  . LYS   A 1 55  ? 18.245 13.859  8.935   1.00 20.08 ?  55  LYS   A HE2  1 
ATOM   1355 H HE3  . LYS   A 1 55  ? 18.855 14.910  7.909   1.00 20.08 ?  55  LYS   A HE3  1 
ATOM   1356 H HZ1  . LYS   A 1 55  ? 16.531 14.753  7.832   1.00 20.56 ?  55  LYS   A HZ1  1 
ATOM   1357 H HZ2  . LYS   A 1 55  ? 17.139 14.551  6.533   1.00 20.56 ?  55  LYS   A HZ2  1 
ATOM   1358 H HZ3  . LYS   A 1 55  ? 16.650 13.415  7.289   1.00 20.56 ?  55  LYS   A HZ3  1 
ATOM   1359 N N    . ALA   A 1 56  ? 22.166 9.827   9.974   1.00 11.40 ?  56  ALA   A N    1 
ATOM   1360 C CA   . ALA   A 1 56  ? 22.045 9.506   11.390  1.00 12.35 ?  56  ALA   A CA   1 
ATOM   1361 C C    . ALA   A 1 56  ? 23.386 9.532   12.114  1.00 12.19 ?  56  ALA   A C    1 
ATOM   1362 O O    . ALA   A 1 56  ? 23.404 9.719   13.334  1.00 13.55 ?  56  ALA   A O    1 
ATOM   1363 C CB   . ALA   A 1 56  ? 21.362 8.147   11.566  1.00 13.36 ?  56  ALA   A CB   1 
ATOM   1364 H H    . ALA   A 1 56  ? 21.961 9.184   9.445   1.00 13.68 ?  56  ALA   A H    1 
ATOM   1365 H HA   . ALA   A 1 56  ? 21.480 10.164  11.810  1.00 14.82 ?  56  ALA   A HA   1 
ATOM   1366 H HB1  . ALA   A 1 56  ? 21.295 7.947   12.515  1.00 16.03 ?  56  ALA   A HB1  1 
ATOM   1367 H HB2  . ALA   A 1 56  ? 20.476 8.184   11.174  1.00 16.03 ?  56  ALA   A HB2  1 
ATOM   1368 H HB3  . ALA   A 1 56  ? 21.891 7.462   11.125  1.00 16.03 ?  56  ALA   A HB3  1 
ATOM   1369 N N    . THR   A 1 57  ? 24.501 9.338   11.401  1.00 11.02 ?  57  THR   A N    1 
ATOM   1370 C CA   . THR   A 1 57  ? 25.841 9.458   11.980  1.00 11.18 ?  57  THR   A CA   1 
ATOM   1371 C C    . THR   A 1 57  ? 26.400 10.873  11.908  1.00 11.54 ?  57  THR   A C    1 
ATOM   1372 O O    . THR   A 1 57  ? 27.584 11.073  12.205  1.00 12.06 ?  57  THR   A O    1 
ATOM   1373 C CB   . THR   A 1 57  ? 26.847 8.503   11.306  1.00 11.16 ?  57  THR   A CB   1 
ATOM   1374 O OG1  . THR   A 1 57  ? 27.243 9.003   10.013  1.00 10.85 ?  57  THR   A OG1  1 
ATOM   1375 C CG2  . THR   A 1 57  ? 26.303 7.093   11.206  1.00 11.15 ?  57  THR   A CG2  1 
ATOM   1376 H H    . THR   A 1 57  ? 24.506 9.112   10.568  1.00 13.22 ?  57  THR   A H    1 
ATOM   1377 H HA   . THR   A 1 57  ? 25.792 9.196   12.917  1.00 13.41 ?  57  THR   A HA   1 
ATOM   1378 H HB   . THR   A 1 57  ? 27.644 8.453   11.868  1.00 13.40 ?  57  THR   A HB   1 
ATOM   1379 H HG1  . THR   A 1 57  ? 26.567 9.067   9.518   1.00 13.02 ?  57  THR   A HG1  1 
ATOM   1380 H HG21 . THR   A 1 57  ? 26.984 6.490   10.872  1.00 13.38 ?  57  THR   A HG21 1 
ATOM   1381 H HG22 . THR   A 1 57  ? 26.011 6.784   12.080  1.00 13.38 ?  57  THR   A HG22 1 
ATOM   1382 H HG23 . THR   A 1 57  ? 25.544 7.074   10.601  1.00 13.38 ?  57  THR   A HG23 1 
ATOM   1383 N N    . ASN   A 1 58  ? 25.592 11.853  11.504  1.00 11.82 ?  58  ASN   A N    1 
ATOM   1384 C CA   . ASN   A 1 58  ? 26.070 13.229  11.413  1.00 12.70 ?  58  ASN   A CA   1 
ATOM   1385 C C    . ASN   A 1 58  ? 27.215 13.351  10.398  1.00 11.84 ?  58  ASN   A C    1 
ATOM   1386 O O    . ASN   A 1 58  ? 28.116 14.178  10.556  1.00 12.35 ?  58  ASN   A O    1 
ATOM   1387 C CB   . ASN   A 1 58  ? 26.465 13.746  12.812  1.00 15.46 ?  58  ASN   A CB   1 
ATOM   1388 C CG   . ASN   A 1 58  ? 26.878 15.201  12.827  1.00 18.98 ?  58  ASN   A CG   1 
ATOM   1389 O OD1  . ASN   A 1 58  ? 26.257 16.032  12.179  1.00 20.47 ?  58  ASN   A OD1  1 
ATOM   1390 N ND2  . ASN   A 1 58  ? 27.924 15.521  13.596  1.00 20.25 ?  58  ASN   A ND2  1 
ATOM   1391 H H    . ASN   A 1 58  ? 24.767 11.737  11.272  1.00 14.19 ?  58  ASN   A H    1 
ATOM   1392 H HA   . ASN   A 1 58  ? 25.338 13.775  11.098  1.00 15.24 ?  58  ASN   A HA   1 
ATOM   1393 H HB2  . ASN   A 1 58  ? 25.704 13.641  13.412  1.00 18.55 ?  58  ASN   A HB2  1 
ATOM   1394 H HB3  . ASN   A 1 58  ? 27.213 13.228  13.145  1.00 18.55 ?  58  ASN   A HB3  1 
ATOM   1395 H HD21 . ASN   A 1 58  ? 28.189 16.339  13.645  1.00 24.30 ?  58  ASN   A HD21 1 
ATOM   1396 H HD22 . ASN   A 1 58  ? 28.329 14.911  14.041  1.00 24.30 ?  58  ASN   A HD22 1 
ATOM   1397 N N    . ASN   A 1 59  ? 27.187 12.529  9.344   1.00 10.93 ?  59  ASN   A N    1 
ATOM   1398 C CA   . ASN   A 1 59  ? 28.164 12.503  8.245   1.00 10.73 ?  59  ASN   A CA   1 
ATOM   1399 C C    . ASN   A 1 59  ? 29.478 11.818  8.635   1.00 10.66 ?  59  ASN   A C    1 
ATOM   1400 O O    . ASN   A 1 59  ? 30.397 11.769  7.809   1.00 10.82 ?  59  ASN   A O    1 
ATOM   1401 C CB   . ASN   A 1 59  ? 28.452 13.890  7.637   1.00 11.24 ?  59  ASN   A CB   1 
ATOM   1402 C CG   . ASN   A 1 59  ? 28.806 13.823  6.169   1.00 11.24 ?  59  ASN   A CG   1 
ATOM   1403 O OD1  . ASN   A 1 59  ? 28.097 13.204  5.376   1.00 11.73 ?  59  ASN   A OD1  1 
ATOM   1404 N ND2  . ASN   A 1 59  ? 29.897 14.472  5.791   1.00 11.90 ?  59  ASN   A ND2  1 
ATOM   1405 H H    . ASN   A 1 59  ? 26.562 11.945  9.228   1.00 13.12 ?  59  ASN   A H    1 
ATOM   1406 H HA   . ASN   A 1 59  ? 27.781 11.974  7.533   1.00 12.88 ?  59  ASN   A HA   1 
ATOM   1407 H HB2  . ASN   A 1 59  ? 27.663 14.449  7.724   1.00 13.49 ?  59  ASN   A HB2  1 
ATOM   1408 H HB3  . ASN   A 1 59  ? 29.199 14.297  8.102   1.00 13.49 ?  59  ASN   A HB3  1 
ATOM   1409 H HD21 . ASN   A 1 59  ? 30.141 14.466  4.966   1.00 14.27 ?  59  ASN   A HD21 1 
ATOM   1410 H HD22 . ASN   A 1 59  ? 30.374 14.895  6.373   1.00 14.27 ?  59  ASN   A HD22 1 
ATOM   1411 N N    . ALA   A 1 60  ? 29.601 11.271  9.848   1.00 10.53 ?  60  ALA   A N    1 
ATOM   1412 C CA   . ALA   A 1 60  ? 30.834 10.578  10.211  1.00 10.86 ?  60  ALA   A CA   1 
ATOM   1413 C C    . ALA   A 1 60  ? 31.060 9.343   9.348   1.00 10.58 ?  60  ALA   A C    1 
ATOM   1414 O O    . ALA   A 1 60  ? 32.205 9.023   9.015   1.00 11.04 ?  60  ALA   A O    1 
ATOM   1415 C CB   . ALA   A 1 60  ? 30.827 10.207  11.693  1.00 11.62 ?  60  ALA   A CB   1 
ATOM   1416 H H    . ALA   A 1 60  ? 28.999 11.280  10.461  1.00 12.64 ?  60  ALA   A H    1 
ATOM   1417 H HA   . ALA   A 1 60  ? 31.583 11.177  10.061  1.00 13.04 ?  60  ALA   A HA   1 
ATOM   1418 H HB1  . ALA   A 1 60  ? 31.656 9.753   11.910  1.00 13.94 ?  60  ALA   A HB1  1 
ATOM   1419 H HB2  . ALA   A 1 60  ? 30.750 11.021  12.219  1.00 13.94 ?  60  ALA   A HB2  1 
ATOM   1420 H HB3  . ALA   A 1 60  ? 30.073 9.626   11.871  1.00 13.94 ?  60  ALA   A HB3  1 
ATOM   1421 N N    . MET   A 1 61  ? 29.985 8.655   8.956   1.00 10.39 ?  61  MET   A N    1 
ATOM   1422 C CA   . MET   A 1 61  ? 30.123 7.518   8.049   1.00 10.16 ?  61  MET   A CA   1 
ATOM   1423 C C    . MET   A 1 61  ? 30.763 7.940   6.731   1.00 9.92  ?  61  MET   A C    1 
ATOM   1424 O O    . MET   A 1 61  ? 31.655 7.258   6.216   1.00 10.40 ?  61  MET   A O    1 
ATOM   1425 C CB   . MET   A 1 61  ? 28.759 6.856   7.829   1.00 10.04 ?  61  MET   A CB   1 
ATOM   1426 C CG   . MET   A 1 61  ? 28.767 5.696   6.846   1.00 10.81 ?  61  MET   A CG   1 
ATOM   1427 S SD   . MET   A 1 61  ? 27.148 4.970   6.613   1.00 11.84 ?  61  MET   A SD   1 
ATOM   1428 C CE   . MET   A 1 61  ? 26.973 4.088   8.167   1.00 13.59 ?  61  MET   A CE   1 
ATOM   1429 H H    . MET   A 1 61  ? 29.176 8.829   9.191   1.00 12.46 ?  61  MET   A H    1 
ATOM   1430 H HA   . MET   A 1 61  ? 30.697 6.859   8.473   1.00 12.20 ?  61  MET   A HA   1 
ATOM   1431 H HB2  . MET   A 1 61  ? 28.442 6.516   8.680   1.00 12.05 ?  61  MET   A HB2  1 
ATOM   1432 H HB3  . MET   A 1 61  ? 28.143 7.522   7.493   1.00 12.05 ?  61  MET   A HB3  1 
ATOM   1433 H HG2  . MET   A 1 61  ? 29.075 6.012   5.983   1.00 12.97 ?  61  MET   A HG2  1 
ATOM   1434 H HG3  . MET   A 1 61  ? 29.357 5.004   7.178   1.00 12.97 ?  61  MET   A HG3  1 
ATOM   1435 H HE1  . MET   A 1 61  ? 26.130 3.608   8.166   1.00 16.31 ?  61  MET   A HE1  1 
ATOM   1436 H HE2  . MET   A 1 61  ? 27.710 3.466   8.259   1.00 16.31 ?  61  MET   A HE2  1 
ATOM   1437 H HE3  . MET   A 1 61  ? 26.987 4.728   8.898   1.00 16.31 ?  61  MET   A HE3  1 
ATOM   1438 N N    . GLN   A 1 62  ? 30.326 9.070   6.171   1.00 9.91  ?  62  GLN   A N    1 
ATOM   1439 C CA   . GLN   A 1 62  ? 30.896 9.550   4.915   1.00 10.13 ?  62  GLN   A CA   1 
ATOM   1440 C C    . GLN   A 1 62  ? 32.365 9.923   5.067   1.00 10.28 ?  62  GLN   A C    1 
ATOM   1441 O O    . GLN   A 1 62  ? 33.173 9.616   4.186   1.00 10.77 ?  62  GLN   A O    1 
ATOM   1442 C CB   . GLN   A 1 62  ? 30.093 10.736  4.381   1.00 10.39 ?  62  GLN   A CB   1 
ATOM   1443 C CG   . GLN   A 1 62  ? 30.478 11.104  2.964   1.00 10.52 ?  62  GLN   A CG   1 
ATOM   1444 C CD   . GLN   A 1 62  ? 30.158 9.983   2.007   1.00 10.76 ?  62  GLN   A CD   1 
ATOM   1445 O OE1  . GLN   A 1 62  ? 28.980 9.681   1.788   1.00 11.33 ?  62  GLN   A OE1  1 
ATOM   1446 N NE2  . GLN   A 1 62  ? 31.177 9.305   1.492   1.00 11.16 ?  62  GLN   A NE2  1 
ATOM   1447 H H    . GLN   A 1 62  ? 29.702 9.562   6.495   1.00 11.90 ?  62  GLN   A H    1 
ATOM   1448 H HA   . GLN   A 1 62  ? 30.844 8.834   4.264   1.00 12.16 ?  62  GLN   A HA   1 
ATOM   1449 H HB2  . GLN   A 1 62  ? 29.149 10.511  4.387   1.00 12.47 ?  62  GLN   A HB2  1 
ATOM   1450 H HB3  . GLN   A 1 62  ? 30.253 11.509  4.945   1.00 12.47 ?  62  GLN   A HB3  1 
ATOM   1451 H HG2  . GLN   A 1 62  ? 29.975 11.888  2.689   1.00 12.62 ?  62  GLN   A HG2  1 
ATOM   1452 H HG3  . GLN   A 1 62  ? 31.429 11.281  2.920   1.00 12.62 ?  62  GLN   A HG3  1 
ATOM   1453 H HE21 . GLN   A 1 62  ? 31.983 9.529   1.685   1.00 13.40 ?  62  GLN   A HE21 1 
ATOM   1454 H HE22 . GLN   A 1 62  ? 31.027 8.654   0.951   1.00 13.40 ?  62  GLN   A HE22 1 
ATOM   1455 N N    . VAL   A 1 63  ? 32.726 10.603  6.160   1.00 10.66 ?  63  VAL   A N    1 
ATOM   1456 C CA   . VAL   A 1 63  ? 34.121 10.988  6.382   1.00 11.61 ?  63  VAL   A CA   1 
ATOM   1457 C C    . VAL   A 1 63  ? 35.013 9.748   6.439   1.00 10.88 ?  63  VAL   A C    1 
ATOM   1458 O O    . VAL   A 1 63  ? 36.068 9.682   5.793   1.00 11.46 ?  63  VAL   A O    1 
ATOM   1459 C CB   . VAL   A 1 63  ? 34.229 11.855  7.650   1.00 12.92 ?  63  VAL   A CB   1 
ATOM   1460 C CG1  . VAL   A 1 63  ? 35.678 12.090  8.029   1.00 14.63 ?  63  VAL   A CG1  1 
ATOM   1461 C CG2  . VAL   A 1 63  ? 33.507 13.185  7.428   1.00 13.56 ?  63  VAL   A CG2  1 
ATOM   1462 H H    . VAL   A 1 63  ? 32.180 10.849  6.786   1.00 12.79 ?  63  VAL   A H    1 
ATOM   1463 H HA   . VAL   A 1 63  ? 34.407 11.530  5.633   1.00 13.93 ?  63  VAL   A HA   1 
ATOM   1464 H HB   . VAL   A 1 63  ? 33.796 11.400  8.389   1.00 15.50 ?  63  VAL   A HB   1 
ATOM   1465 H HG11 . VAL   A 1 63  ? 35.723 12.815  8.671   1.00 17.56 ?  63  VAL   A HG11 1 
ATOM   1466 H HG12 . VAL   A 1 63  ? 36.042 11.281  8.418   1.00 17.56 ?  63  VAL   A HG12 1 
ATOM   1467 H HG13 . VAL   A 1 63  ? 36.177 12.328  7.229   1.00 17.56 ?  63  VAL   A HG13 1 
ATOM   1468 H HG21 . VAL   A 1 63  ? 33.599 13.734  8.223   1.00 16.27 ?  63  VAL   A HG21 1 
ATOM   1469 H HG22 . VAL   A 1 63  ? 33.906 13.638  6.667   1.00 16.27 ?  63  VAL   A HG22 1 
ATOM   1470 H HG23 . VAL   A 1 63  ? 32.569 13.012  7.253   1.00 16.27 ?  63  VAL   A HG23 1 
ATOM   1471 N N    . GLU   A 1 64  ? 34.592 8.738   7.202   1.00 10.87 ?  64  GLU   A N    1 
ATOM   1472 C CA   . GLU   A 1 64  ? 35.356 7.499   7.293   1.00 11.10 ?  64  GLU   A CA   1 
ATOM   1473 C C    . GLU   A 1 64  ? 35.439 6.808   5.935   1.00 10.86 ?  64  GLU   A C    1 
ATOM   1474 O O    . GLU   A 1 64  ? 36.489 6.268   5.553   1.00 11.21 ?  64  GLU   A O    1 
ATOM   1475 C CB   . GLU   A 1 64  ? 34.674 6.593   8.316   1.00 11.81 ?  64  GLU   A CB   1 
ATOM   1476 C CG   . GLU   A 1 64  ? 35.328 5.244   8.474   1.00 12.23 ?  64  GLU   A CG   1 
ATOM   1477 C CD   . GLU   A 1 64  ? 34.444 4.246   9.200   1.00 13.13 ?  64  GLU   A CD   1 
ATOM   1478 O OE1  . GLU   A 1 64  ? 33.206 4.344   9.069   1.00 14.05 ?  64  GLU   A OE1  1 
ATOM   1479 O OE2  . GLU   A 1 64  ? 34.992 3.346   9.883   1.00 13.58 -1 64  GLU   A OE2  1 
ATOM   1480 H H    . GLU   A 1 64  ? 33.864 8.745   7.663   1.00 13.04 ?  64  GLU   A H    1 
ATOM   1481 H HA   . GLU   A 1 64  ? 36.254 7.700   7.600   1.00 13.32 ?  64  GLU   A HA   1 
ATOM   1482 H HB2  . GLU   A 1 64  ? 34.696 7.035   9.186   1.00 14.17 ?  64  GLU   A HB2  1 
ATOM   1483 H HB3  . GLU   A 1 64  ? 33.756 6.456   8.046   1.00 14.17 ?  64  GLU   A HB3  1 
ATOM   1484 H HG2  . GLU   A 1 64  ? 35.533 4.873   7.599   1.00 14.67 ?  64  GLU   A HG2  1 
ATOM   1485 H HG3  . GLU   A 1 64  ? 36.146 5.344   8.985   1.00 14.67 ?  64  GLU   A HG3  1 
ATOM   1486 N N    . SER   A 1 65  ? 34.323 6.810   5.200   1.00 10.42 ?  65  SER   A N    1 
ATOM   1487 C CA   . SER   A 1 65  ? 34.272 6.159   3.895   1.00 10.47 ?  65  SER   A CA   1 
ATOM   1488 C C    . SER   A 1 65  ? 35.196 6.832   2.892   1.00 10.76 ?  65  SER   A C    1 
ATOM   1489 O O    . SER   A 1 65  ? 35.843 6.158   2.085   1.00 11.47 ?  65  SER   A O    1 
ATOM   1490 C CB   . SER   A 1 65  ? 32.842 6.174   3.359   1.00 10.42 ?  65  SER   A CB   1 
ATOM   1491 O OG   . SER   A 1 65  ? 31.986 5.352   4.143   1.00 10.92 ?  65  SER   A OG   1 
ATOM   1492 H H    . SER   A 1 65  ? 33.587 7.187   5.435   1.00 12.50 ?  65  SER   A H    1 
ATOM   1493 H HA   . SER   A 1 65  ? 34.555 5.238   3.990   1.00 12.56 ?  65  SER   A HA   1 
ATOM   1494 H HB2  . SER   A 1 65  ? 32.505 7.081   3.377   1.00 12.51 ?  65  SER   A HB2  1 
ATOM   1495 H HB3  . SER   A 1 65  ? 32.846 5.839   2.449   1.00 12.51 ?  65  SER   A HB3  1 
ATOM   1496 H HG   . SER   A 1 65  ? 31.972 5.633   4.936   1.00 13.10 ?  65  SER   A HG   1 
ATOM   1497 N N    . ASP   A 1 66  ? 35.277 8.164   2.921   1.00 10.76 ?  66  ASP   A N    1 
ATOM   1498 C CA   . ASP   A 1 66  ? 36.139 8.864   1.974   1.00 11.67 ?  66  ASP   A CA   1 
ATOM   1499 C C    . ASP   A 1 66  ? 37.602 8.507   2.209   1.00 11.71 ?  66  ASP   A C    1 
ATOM   1500 O O    . ASP   A 1 66  ? 38.371 8.340   1.257   1.00 12.61 ?  66  ASP   A O    1 
ATOM   1501 C CB   . ASP   A 1 66  ? 35.922 10.373  2.084   1.00 12.88 ?  66  ASP   A CB   1 
ATOM   1502 C CG   . ASP   A 1 66  ? 34.590 10.836  1.480   1.00 14.87 ?  66  ASP   A CG   1 
ATOM   1503 O OD1  . ASP   A 1 66  ? 33.876 10.044  0.827   1.00 15.24 ?  66  ASP   A OD1  1 
ATOM   1504 O OD2  . ASP   A 1 66  ? 34.282 12.033  1.640   1.00 17.93 -1 66  ASP   A OD2  1 
ATOM   1505 H H    . ASP   A 1 66  ? 34.848 8.675   3.465   1.00 12.91 ?  66  ASP   A H    1 
ATOM   1506 H HA   . ASP   A 1 66  ? 35.905 8.593   1.074   1.00 14.01 ?  66  ASP   A HA   1 
ATOM   1507 H HB2  . ASP   A 1 66  ? 35.923 10.625  3.020   1.00 15.46 ?  66  ASP   A HB2  1 
ATOM   1508 H HB3  . ASP   A 1 66  ? 36.641 10.829  1.617   1.00 15.46 ?  66  ASP   A HB3  1 
ATOM   1509 N N    . ASP   A 1 67  ? 38.002 8.371   3.474   1.00 11.55 ?  67  ASP   A N    1 
ATOM   1510 C CA   . ASP   A 1 67  ? 39.356 7.924   3.774   1.00 12.52 ?  67  ASP   A CA   1 
ATOM   1511 C C    . ASP   A 1 67  ? 39.579 6.491   3.306   1.00 12.54 ?  67  ASP   A C    1 
ATOM   1512 O O    . ASP   A 1 67  ? 40.639 6.171   2.760   1.00 13.09 ?  67  ASP   A O    1 
ATOM   1513 C CB   . ASP   A 1 67  ? 39.623 8.054   5.271   1.00 14.02 ?  67  ASP   A CB   1 
ATOM   1514 C CG   . ASP   A 1 67  ? 40.917 7.398   5.691   1.00 15.26 ?  67  ASP   A CG   1 
ATOM   1515 O OD1  . ASP   A 1 67  ? 41.989 8.034   5.565   1.00 17.89 ?  67  ASP   A OD1  1 
ATOM   1516 O OD2  . ASP   A 1 67  ? 40.865 6.232   6.144   1.00 15.07 -1 67  ASP   A OD2  1 
ATOM   1517 H H    . ASP   A 1 67  ? 37.516 8.532   4.161   1.00 13.87 ?  67  ASP   A H    1 
ATOM   1518 H HA   . ASP   A 1 67  ? 39.987 8.487   3.303   1.00 15.03 ?  67  ASP   A HA   1 
ATOM   1519 H HB2  . ASP   A 1 67  ? 39.676 8.991   5.496   1.00 16.83 ?  67  ASP   A HB2  1 
ATOM   1520 H HB3  . ASP   A 1 67  ? 38.900 7.628   5.756   1.00 16.83 ?  67  ASP   A HB3  1 
ATOM   1521 N N    . TYR   A 1 68  ? 38.584 5.615   3.496   1.00 11.78 ?  68  TYR   A N    1 
ATOM   1522 C CA   . TYR   A 1 68  ? 38.704 4.237   3.017   1.00 12.24 ?  68  TYR   A CA   1 
ATOM   1523 C C    . TYR   A 1 68  ? 38.945 4.193   1.507   1.00 11.83 ?  68  TYR   A C    1 
ATOM   1524 O O    . TYR   A 1 68  ? 39.822 3.463   1.028   1.00 12.44 ?  68  TYR   A O    1 
ATOM   1525 C CB   . TYR   A 1 68  ? 37.454 3.413   3.398   1.00 12.65 ?  68  TYR   A CB   1 
ATOM   1526 C CG   . TYR   A 1 68  ? 37.479 2.021   2.769   1.00 14.12 ?  68  TYR   A CG   1 
ATOM   1527 C CD1  . TYR   A 1 68  ? 37.016 1.822   1.470   1.00 15.75 ?  68  TYR   A CD1  1 
ATOM   1528 C CD2  . TYR   A 1 68  ? 38.021 0.933   3.438   1.00 15.92 ?  68  TYR   A CD2  1 
ATOM   1529 C CE1  . TYR   A 1 68  ? 37.081 0.603   0.856   1.00 17.37 ?  68  TYR   A CE1  1 
ATOM   1530 C CE2  . TYR   A 1 68  ? 38.081 -0.331  2.821   1.00 16.77 ?  68  TYR   A CE2  1 
ATOM   1531 C CZ   . TYR   A 1 68  ? 37.612 -0.465  1.532   1.00 17.62 ?  68  TYR   A CZ   1 
ATOM   1532 O OH   . TYR   A 1 68  ? 37.684 -1.674  0.899   1.00 19.09 ?  68  TYR   A OH   1 
ATOM   1533 H H    . TYR   A 1 68  ? 37.839 5.788   3.890   1.00 14.14 ?  68  TYR   A H    1 
ATOM   1534 H HA   . TYR   A 1 68  ? 39.464 3.821   3.448   1.00 14.69 ?  68  TYR   A HA   1 
ATOM   1535 H HB2  . TYR   A 1 68  ? 37.424 3.299   4.363   1.00 15.18 ?  68  TYR   A HB2  1 
ATOM   1536 H HB3  . TYR   A 1 68  ? 36.657 3.866   3.089   1.00 15.18 ?  68  TYR   A HB3  1 
ATOM   1537 H HD1  . TYR   A 1 68  ? 36.666 2.550   1.001   1.00 18.90 ?  68  TYR   A HD1  1 
ATOM   1538 H HD2  . TYR   A 1 68  ? 38.353 1.038   4.297   1.00 19.10 ?  68  TYR   A HD2  1 
ATOM   1539 H HE1  . TYR   A 1 68  ? 36.756 0.503   -0.011  1.00 20.85 ?  68  TYR   A HE1  1 
ATOM   1540 H HE2  . TYR   A 1 68  ? 38.445 -1.061  3.262   1.00 20.13 ?  68  TYR   A HE2  1 
ATOM   1541 H HH   . TYR   A 1 68  ? 38.011 -2.252  1.415   1.00 22.91 ?  68  TYR   A HH   1 
ATOM   1542 N N    . ILE   A 1 69  ? 38.156 4.952   0.737   1.00 11.63 ?  69  ILE   A N    1 
ATOM   1543 C CA   . ILE   A 1 69  ? 38.288 4.941   -0.719  1.00 11.74 ?  69  ILE   A CA   1 
ATOM   1544 C C    . ILE   A 1 69  ? 39.615 5.553   -1.152  1.00 11.44 ?  69  ILE   A C    1 
ATOM   1545 O O    . ILE   A 1 69  ? 40.260 5.067   -2.088  1.00 12.00 ?  69  ILE   A O    1 
ATOM   1546 C CB   . ILE   A 1 69  ? 37.091 5.650   -1.384  1.00 12.38 ?  69  ILE   A CB   1 
ATOM   1547 C CG1  . ILE   A 1 69  ? 35.783 4.907   -1.115  1.00 12.99 ?  69  ILE   A CG1  1 
ATOM   1548 C CG2  . ILE   A 1 69  ? 37.336 5.836   -2.888  1.00 13.93 ?  69  ILE   A CG2  1 
ATOM   1549 C CD1  . ILE   A 1 69  ? 35.620 3.620   -1.896  1.00 13.67 ?  69  ILE   A CD1  1 
ATOM   1550 H H    . ILE   A 1 69  ? 37.549 5.480   1.036   1.00 13.96 ?  69  ILE   A H    1 
ATOM   1551 H HA   . ILE   A 1 69  ? 38.283 4.018   -1.017  1.00 14.09 ?  69  ILE   A HA   1 
ATOM   1552 H HB   . ILE   A 1 69  ? 37.016 6.530   -0.988  1.00 14.85 ?  69  ILE   A HB   1 
ATOM   1553 H HG12 . ILE   A 1 69  ? 35.740 4.688   -0.171  1.00 15.58 ?  69  ILE   A HG12 1 
ATOM   1554 H HG13 . ILE   A 1 69  ? 35.044 5.491   -1.348  1.00 15.58 ?  69  ILE   A HG13 1 
ATOM   1555 H HG21 . ILE   A 1 69  ? 36.490 6.036   -3.322  1.00 16.71 ?  69  ILE   A HG21 1 
ATOM   1556 H HG22 . ILE   A 1 69  ? 37.951 6.580   -3.021  1.00 16.71 ?  69  ILE   A HG22 1 
ATOM   1557 H HG23 . ILE   A 1 69  ? 37.712 5.025   -3.255  1.00 16.71 ?  69  ILE   A HG23 1 
ATOM   1558 H HD11 . ILE   A 1 69  ? 34.830 3.162   -1.578  1.00 16.40 ?  69  ILE   A HD11 1 
ATOM   1559 H HD12 . ILE   A 1 69  ? 35.524 3.835   -2.838  1.00 16.40 ?  69  ILE   A HD12 1 
ATOM   1560 H HD13 . ILE   A 1 69  ? 36.404 3.067   -1.759  1.00 16.40 ?  69  ILE   A HD13 1 
ATOM   1561 N N    . ALA   A 1 70  ? 40.038 6.631   -0.493  1.00 12.06 ?  70  ALA   A N    1 
ATOM   1562 C CA   . ALA   A 1 70  ? 41.315 7.240   -0.851  1.00 13.11 ?  70  ALA   A CA   1 
ATOM   1563 C C    . ALA   A 1 70  ? 42.466 6.256   -0.685  1.00 13.22 ?  70  ALA   A C    1 
ATOM   1564 O O    . ALA   A 1 70  ? 43.432 6.294   -1.452  1.00 15.21 ?  70  ALA   A O    1 
ATOM   1565 C CB   . ALA   A 1 70  ? 41.563 8.491   -0.007  1.00 13.49 ?  70  ALA   A CB   1 
ATOM   1566 H H    . ALA   A 1 70  ? 39.617 7.018   0.143   1.00 14.47 ?  70  ALA   A H    1 
ATOM   1567 H HA   . ALA   A 1 70  ? 41.287 7.511   -1.783  1.00 15.74 ?  70  ALA   A HA   1 
ATOM   1568 H HB1  . ALA   A 1 70  ? 42.421 8.876   -0.262  1.00 16.18 ?  70  ALA   A HB1  1 
ATOM   1569 H HB2  . ALA   A 1 70  ? 40.855 9.127   -0.168  1.00 16.18 ?  70  ALA   A HB2  1 
ATOM   1570 H HB3  . ALA   A 1 70  ? 41.584 8.239   0.929   1.00 16.18 ?  70  ALA   A HB3  1 
ATOM   1571 N N    . THR   A 1 71  ? 42.368 5.355   0.290   1.00 12.62 ?  71  THR   A N    1 
ATOM   1572 C CA   . THR   A 1 71  ? 43.423 4.380   0.539   1.00 14.22 ?  71  THR   A CA   1 
ATOM   1573 C C    . THR   A 1 71  ? 43.303 3.155   -0.359  1.00 14.07 ?  71  THR   A C    1 
ATOM   1574 O O    . THR   A 1 71  ? 44.313 2.646   -0.862  1.00 16.14 ?  71  THR   A O    1 
ATOM   1575 C CB   . THR   A 1 71  ? 43.349 3.928   1.993   1.00 16.19 ?  71  THR   A CB   1 
ATOM   1576 O OG1  . THR   A 1 71  ? 43.588 5.052   2.847   1.00 17.48 ?  71  THR   A OG1  1 
ATOM   1577 C CG2  . THR   A 1 71  ? 44.367 2.828   2.278   1.00 17.44 ?  71  THR   A CG2  1 
ATOM   1578 H H    . THR   A 1 71  ? 41.690 5.273   0.812   1.00 15.15 ?  71  THR   A H    1 
ATOM   1579 H HA   . THR   A 1 71  ? 44.288 4.788   0.381   1.00 17.06 ?  71  THR   A HA   1 
ATOM   1580 H HB   . THR   A 1 71  ? 42.464 3.562   2.164   1.00 19.43 ?  71  THR   A HB   1 
ATOM   1581 H HG1  . THR   A 1 71  ? 43.540 4.802   3.649   1.00 20.97 ?  71  THR   A HG1  1 
ATOM   1582 H HG21 . THR   A 1 71  ? 44.504 2.746   3.235   1.00 20.93 ?  71  THR   A HG21 1 
ATOM   1583 H HG22 . THR   A 1 71  ? 44.057 1.975   1.934   1.00 20.93 ?  71  THR   A HG22 1 
ATOM   1584 H HG23 . THR   A 1 71  ? 45.218 3.045   1.860   1.00 20.93 ?  71  THR   A HG23 1 
ATOM   1585 N N    . ASN   A 1 72  ? 42.080 2.647   -0.542  1.00 13.26 ?  72  ASN   A N    1 
ATOM   1586 C CA   . ASN   A 1 72  ? 41.860 1.322   -1.107  1.00 13.58 ?  72  ASN   A CA   1 
ATOM   1587 C C    . ASN   A 1 72  ? 41.241 1.312   -2.492  1.00 13.70 ?  72  ASN   A C    1 
ATOM   1588 O O    . ASN   A 1 72  ? 41.250 0.256   -3.142  1.00 14.87 ?  72  ASN   A O    1 
ATOM   1589 C CB   . ASN   A 1 72  ? 40.973 0.501   -0.165  1.00 14.09 ?  72  ASN   A CB   1 
ATOM   1590 C CG   . ASN   A 1 72  ? 41.589 0.347   1.198   1.00 15.13 ?  72  ASN   A CG   1 
ATOM   1591 O OD1  . ASN   A 1 72  ? 41.138 0.951   2.172   1.00 17.14 ?  72  ASN   A OD1  1 
ATOM   1592 N ND2  . ASN   A 1 72  ? 42.640 -0.442  1.275   1.00 15.73 ?  72  ASN   A ND2  1 
ATOM   1593 H H    . ASN   A 1 72  ? 41.351 3.063   -0.343  1.00 15.91 ?  72  ASN   A H    1 
ATOM   1594 H HA   . ASN   A 1 72  ? 42.712 0.871   -1.176  1.00 16.30 ?  72  ASN   A HA   1 
ATOM   1595 H HB2  . ASN   A 1 72  ? 40.119 0.944   -0.063  1.00 16.91 ?  72  ASN   A HB2  1 
ATOM   1596 H HB3  . ASN   A 1 72  ? 40.849 -0.386  -0.541  1.00 16.91 ?  72  ASN   A HB3  1 
ATOM   1597 H HD21 . ASN   A 1 72  ? 43.036 -0.560  2.030   1.00 18.87 ?  72  ASN   A HD21 1 
ATOM   1598 H HD22 . ASN   A 1 72  ? 42.934 -0.843  0.571   1.00 18.87 ?  72  ASN   A HD22 1 
ATOM   1599 N N    . GLY   A 1 73  ? 40.692 2.427   -2.952  1.00 13.16 ?  73  GLY   A N    1 
ATOM   1600 C CA   . GLY   A 1 73  ? 39.952 2.446   -4.188  1.00 12.93 ?  73  GLY   A CA   1 
ATOM   1601 C C    . GLY   A 1 73  ? 38.560 1.862   -4.030  1.00 12.23 ?  73  GLY   A C    1 
ATOM   1602 O O    . GLY   A 1 73  ? 38.167 1.410   -2.949  1.00 12.77 ?  73  GLY   A O    1 
ATOM   1603 H H    . GLY   A 1 73  ? 40.740 3.202   -2.563  1.00 15.80 ?  73  GLY   A H    1 
ATOM   1604 H HA2  . GLY   A 1 73  ? 39.872 3.363   -4.504  1.00 15.52 ?  73  GLY   A HA2  1 
ATOM   1605 H HA3  . GLY   A 1 73  ? 40.428 1.932   -4.858  1.00 15.52 ?  73  GLY   A HA3  1 
ATOM   1606 N N    . PRO   A 1 74  ? 37.789 1.879   -5.116  1.00 12.70 ?  74  PRO   A N    1 
ATOM   1607 C CA   . PRO   A 1 74  ? 36.388 1.458   -5.039  1.00 12.78 ?  74  PRO   A CA   1 
ATOM   1608 C C    . PRO   A 1 74  ? 36.238 -0.025  -4.724  1.00 12.02 ?  74  PRO   A C    1 
ATOM   1609 O O    . PRO   A 1 74  ? 37.104 -0.859  -5.013  1.00 13.02 ?  74  PRO   A O    1 
ATOM   1610 C CB   . PRO   A 1 74  ? 35.844 1.772   -6.440  1.00 14.67 ?  74  PRO   A CB   1 
ATOM   1611 C CG   . PRO   A 1 74  ? 36.812 2.745   -7.042  1.00 16.98 ?  74  PRO   A CG   1 
ATOM   1612 C CD   . PRO   A 1 74  ? 38.142 2.399   -6.448  1.00 14.51 ?  74  PRO   A CD   1 
ATOM   1613 H HA   . PRO   A 1 74  ? 35.907 1.986   -4.378  1.00 15.34 ?  74  PRO   A HA   1 
ATOM   1614 H HB2  . PRO   A 1 74  ? 35.804 0.959   -6.963  1.00 17.61 ?  74  PRO   A HB2  1 
ATOM   1615 H HB3  . PRO   A 1 74  ? 34.963 2.176   -6.365  1.00 17.61 ?  74  PRO   A HB3  1 
ATOM   1616 H HG2  . PRO   A 1 74  ? 36.832 2.634   -8.005  1.00 20.38 ?  74  PRO   A HG2  1 
ATOM   1617 H HG3  . PRO   A 1 74  ? 36.562 3.649   -6.805  1.00 20.38 ?  74  PRO   A HG3  1 
ATOM   1618 H HD2  . PRO   A 1 74  ? 38.583 1.708   -6.974  1.00 17.41 ?  74  PRO   A HD2  1 
ATOM   1619 H HD3  . PRO   A 1 74  ? 38.696 3.196   -6.382  1.00 17.41 ?  74  PRO   A HD3  1 
ATOM   1620 N N    . LEU   A 1 75  ? 35.095 -0.348  -4.131  1.00 11.17 ?  75  LEU   A N    1 
ATOM   1621 C CA   . LEU   A 1 75  ? 34.696 -1.737  -3.983  1.00 10.92 ?  75  LEU   A CA   1 
ATOM   1622 C C    . LEU   A 1 75  ? 34.308 -2.314  -5.344  1.00 11.71 ?  75  LEU   A C    1 
ATOM   1623 O O    . LEU   A 1 75  ? 34.198 -1.599  -6.342  1.00 12.90 ?  75  LEU   A O    1 
ATOM   1624 C CB   . LEU   A 1 75  ? 33.508 -1.856  -3.031  1.00 11.26 ?  75  LEU   A CB   1 
ATOM   1625 C CG   . LEU   A 1 75  ? 33.717 -1.457  -1.572  1.00 13.06 ?  75  LEU   A CG   1 
ATOM   1626 C CD1  . LEU   A 1 75  ? 32.427 -1.661  -0.781  1.00 15.04 ?  75  LEU   A CD1  1 
ATOM   1627 C CD2  . LEU   A 1 75  ? 34.858 -2.184  -0.916  1.00 16.11 ?  75  LEU   A CD2  1 
ATOM   1628 H H    . LEU   A 1 75  ? 34.537 0.222   -3.806  1.00 13.40 ?  75  LEU   A H    1 
ATOM   1629 H HA   . LEU   A 1 75  ? 35.442 -2.246  -3.632  1.00 13.11 ?  75  LEU   A HA   1 
ATOM   1630 H HB2  . LEU   A 1 75  ? 32.794 -1.307  -3.379  1.00 13.52 ?  75  LEU   A HB2  1 
ATOM   1631 H HB3  . LEU   A 1 75  ? 33.228 -2.786  -3.034  1.00 13.52 ?  75  LEU   A HB3  1 
ATOM   1632 H HG   . LEU   A 1 75  ? 33.932 -0.510  -1.547  1.00 15.67 ?  75  LEU   A HG   1 
ATOM   1633 H HD11 . LEU   A 1 75  ? 32.579 -1.397  0.139   1.00 18.05 ?  75  LEU   A HD11 1 
ATOM   1634 H HD12 . LEU   A 1 75  ? 31.732 -1.108  -1.173  1.00 18.05 ?  75  LEU   A HD12 1 
ATOM   1635 H HD13 . LEU   A 1 75  ? 32.175 -2.593  -0.826  1.00 18.05 ?  75  LEU   A HD13 1 
ATOM   1636 H HD21 . LEU   A 1 75  ? 34.913 -1.914  0.015   1.00 19.33 ?  75  LEU   A HD21 1 
ATOM   1637 H HD22 . LEU   A 1 75  ? 34.705 -3.138  -0.977  1.00 19.33 ?  75  LEU   A HD22 1 
ATOM   1638 H HD23 . LEU   A 1 75  ? 35.690 -1.954  -1.371  1.00 19.33 ?  75  LEU   A HD23 1 
ATOM   1639 N N    . LYS   A 1 76  ? 34.111 -3.634  -5.367  1.00 12.12 ?  76  LYS   A N    1 
ATOM   1640 C CA   . LYS   A 1 76  ? 33.511 -4.347  -6.490  1.00 12.67 ?  76  LYS   A CA   1 
ATOM   1641 C C    . LYS   A 1 76  ? 31.999 -4.428  -6.289  1.00 11.48 ?  76  LYS   A C    1 
ATOM   1642 O O    . LYS   A 1 76  ? 31.523 -4.557  -5.161  1.00 11.22 ?  76  LYS   A O    1 
ATOM   1643 C CB   . LYS   A 1 76  ? 34.056 -5.786  -6.558  1.00 14.37 ?  76  LYS   A CB   1 
ATOM   1644 C CG   . LYS   A 1 76  ? 35.565 -5.898  -6.742  1.00 15.96 ?  76  LYS   A CG   1 
ATOM   1645 C CD   . LYS   A 1 76  ? 36.073 -7.311  -6.569  1.00 17.42 ?  76  LYS   A CD   1 
ATOM   1646 C CE   . LYS   A 1 76  ? 37.573 -7.377  -6.737  1.00 19.85 ?  76  LYS   A CE   1 
ATOM   1647 N NZ   . LYS   A 1 76  ? 38.074 -8.746  -6.532  1.00 20.75 ?  76  LYS   A NZ   1 
ATOM   1648 H H    . LYS   A 1 76  ? 34.319 -4.151  -4.714  1.00 14.55 ?  76  LYS   A H    1 
ATOM   1649 H HA   . LYS   A 1 76  ? 33.702 -3.886  -7.325  1.00 15.21 ?  76  LYS   A HA   1 
ATOM   1650 H HB2  . LYS   A 1 76  ? 33.826 -6.236  -5.732  1.00 17.24 ?  76  LYS   A HB2  1 
ATOM   1651 H HB3  . LYS   A 1 76  ? 33.634 -6.235  -7.306  1.00 17.24 ?  76  LYS   A HB3  1 
ATOM   1652 H HG2  . LYS   A 1 76  ? 35.796 -5.597  -7.636  1.00 19.16 ?  76  LYS   A HG2  1 
ATOM   1653 H HG3  . LYS   A 1 76  ? 36.005 -5.334  -6.083  1.00 19.16 ?  76  LYS   A HG3  1 
ATOM   1654 H HD2  . LYS   A 1 76  ? 35.849 -7.626  -5.680  1.00 20.90 ?  76  LYS   A HD2  1 
ATOM   1655 H HD3  . LYS   A 1 76  ? 35.664 -7.881  -7.241  1.00 20.90 ?  76  LYS   A HD3  1 
ATOM   1656 H HE2  . LYS   A 1 76  ? 37.806 -7.096  -7.635  1.00 23.82 ?  76  LYS   A HE2  1 
ATOM   1657 H HE3  . LYS   A 1 76  ? 37.992 -6.797  -6.083  1.00 23.82 ?  76  LYS   A HE3  1 
ATOM   1658 H HZ1  . LYS   A 1 76  ? 38.957 -8.771  -6.634  1.00 24.90 ?  76  LYS   A HZ1  1 
ATOM   1659 H HZ2  . LYS   A 1 76  ? 37.870 -9.030  -5.711  1.00 24.90 ?  76  LYS   A HZ2  1 
ATOM   1660 H HZ3  . LYS   A 1 76  ? 37.701 -9.303  -7.124  1.00 24.90 ?  76  LYS   A HZ3  1 
ATOM   1661 N N    . VAL   A 1 77  ? 31.242 -4.393  -7.390  1.00 11.87 ?  77  VAL   A N    1 
ATOM   1662 C CA   . VAL   A 1 77  ? 29.834 -4.775  -7.302  1.00 11.67 ?  77  VAL   A CA   1 
ATOM   1663 C C    . VAL   A 1 77  ? 29.765 -6.229  -6.863  1.00 11.14 ?  77  VAL   A C    1 
ATOM   1664 O O    . VAL   A 1 77  ? 30.427 -7.100  -7.438  1.00 11.51 ?  77  VAL   A O    1 
ATOM   1665 C CB   . VAL   A 1 77  ? 29.104 -4.545  -8.632  1.00 12.86 ?  77  VAL   A CB   1 
ATOM   1666 C CG1  . VAL   A 1 77  ? 27.650 -4.987  -8.512  1.00 13.58 ?  77  VAL   A CG1  1 
ATOM   1667 C CG2  . VAL   A 1 77  ? 29.179 -3.082  -9.041  1.00 14.66 ?  77  VAL   A CG2  1 
ATOM   1668 H H    . VAL   A 1 77  ? 31.516 -4.150  -8.170  1.00 14.24 ?  77  VAL   A H    1 
ATOM   1669 H HA   . VAL   A 1 77  ? 29.406 -4.233  -6.623  1.00 14.01 ?  77  VAL   A HA   1 
ATOM   1670 H HB   . VAL   A 1 77  ? 29.529 -5.072  -9.324  1.00 15.43 ?  77  VAL   A HB   1 
ATOM   1671 H HG11 . VAL   A 1 77  ? 27.161 -4.673  -9.285  1.00 16.30 ?  77  VAL   A HG11 1 
ATOM   1672 H HG12 . VAL   A 1 77  ? 27.615 -5.955  -8.467  1.00 16.30 ?  77  VAL   A HG12 1 
ATOM   1673 H HG13 . VAL   A 1 77  ? 27.271 -4.605  -7.703  1.00 16.30 ?  77  VAL   A HG13 1 
ATOM   1674 H HG21 . VAL   A 1 77  ? 28.672 -2.957  -9.857  1.00 17.60 ?  77  VAL   A HG21 1 
ATOM   1675 H HG22 . VAL   A 1 77  ? 28.802 -2.536  -8.330  1.00 17.60 ?  77  VAL   A HG22 1 
ATOM   1676 H HG23 . VAL   A 1 77  ? 30.107 -2.839  -9.185  1.00 17.60 ?  77  VAL   A HG23 1 
ATOM   1677 N N    . GLY   A 1 78  ? 28.974 -6.496  -5.821  1.00 10.80 ?  78  GLY   A N    1 
ATOM   1678 C CA   . GLY   A 1 78  ? 28.948 -7.785  -5.164  1.00 11.17 ?  78  GLY   A CA   1 
ATOM   1679 C C    . GLY   A 1 78  ? 29.862 -7.886  -3.963  1.00 10.46 ?  78  GLY   A C    1 
ATOM   1680 O O    . GLY   A 1 78  ? 29.803 -8.898  -3.245  1.00 11.34 ?  78  GLY   A O    1 
ATOM   1681 H H    . GLY   A 1 78  ? 28.426 -5.922  -5.479  1.00 12.96 ?  78  GLY   A H    1 
ATOM   1682 H HA2  . GLY   A 1 78  ? 28.045 -7.969  -4.868  1.00 13.40 ?  78  GLY   A HA2  1 
ATOM   1683 H HA3  . GLY   A 1 78  ? 29.206 -8.467  -5.801  1.00 13.40 ?  78  GLY   A HA3  1 
ATOM   1684 N N    . GLY   A 1 79  ? 30.721 -6.886  -3.737  1.00 10.69 ?  79  GLY   A N    1 
ATOM   1685 C CA   . GLY   A 1 79  ? 31.683 -6.911  -2.658  1.00 10.96 ?  79  GLY   A CA   1 
ATOM   1686 C C    . GLY   A 1 79  ? 31.233 -6.113  -1.443  1.00 10.32 ?  79  GLY   A C    1 
ATOM   1687 O O    . GLY   A 1 79  ? 30.117 -5.602  -1.366  1.00 10.89 ?  79  GLY   A O    1 
ATOM   1688 H H    . GLY   A 1 79  ? 30.764 -6.167  -4.209  1.00 12.82 ?  79  GLY   A H    1 
ATOM   1689 H HA2  . GLY   A 1 79  ? 31.831 -7.838  -2.385  1.00 13.15 ?  79  GLY   A HA2  1 
ATOM   1690 H HA3  . GLY   A 1 79  ? 32.528 -6.554  -2.967  1.00 13.15 ?  79  GLY   A HA3  1 
ATOM   1691 N N    . SER   A 1 80  ? 32.138 -6.025  -0.470  1.00 11.04 ?  80  SER   A N    1 
ATOM   1692 C CA   . SER   A 1 80  ? 31.821 -5.395  0.801   1.00 10.71 ?  80  SER   A CA   1 
ATOM   1693 C C    . SER   A 1 80  ? 33.093 -4.948  1.501   1.00 10.42 ?  80  SER   A C    1 
ATOM   1694 O O    . SER   A 1 80  ? 34.204 -5.378  1.170   1.00 11.97 ?  80  SER   A O    1 
ATOM   1695 C CB   . SER   A 1 80  ? 31.061 -6.355  1.726   1.00 11.74 ?  80  SER   A CB   1 
ATOM   1696 O OG   . SER   A 1 80  ? 31.895 -7.407  2.193   1.00 13.40 ?  80  SER   A OG   1 
ATOM   1697 H H    . SER   A 1 80  ? 32.946 -6.316  -0.524  1.00 13.25 ?  80  SER   A H    1 
ATOM   1698 H HA   . SER   A 1 80  ? 31.266 -4.618  0.630   1.00 12.85 ?  80  SER   A HA   1 
ATOM   1699 H HB2  . SER   A 1 80  ? 30.729 -5.858  2.489   1.00 14.09 ?  80  SER   A HB2  1 
ATOM   1700 H HB3  . SER   A 1 80  ? 30.317 -6.740  1.235   1.00 14.09 ?  80  SER   A HB3  1 
ATOM   1701 H HG   . SER   A 1 80  ? 32.189 -7.849  1.539   1.00 16.08 ?  80  SER   A HG   1 
ATOM   1702 N N    . CYS   A 1 81  ? 32.905 -4.100  2.511   1.00 10.41 ?  81  CYS   A N    1 
ATOM   1703 C CA   . CYS   A 1 81  ? 33.958 -3.816  3.471   1.00 10.57 ?  81  CYS   A CA   1 
ATOM   1704 C C    . CYS   A 1 81  ? 33.315 -3.577  4.827   1.00 10.32 ?  81  CYS   A C    1 
ATOM   1705 O O    . CYS   A 1 81  ? 32.152 -3.172  4.914   1.00 11.40 ?  81  CYS   A O    1 
ATOM   1706 C CB   . CYS   A 1 81  ? 34.836 -2.630  3.047   1.00 11.39 ?  81  CYS   A CB   1 
ATOM   1707 S SG   . CYS   A 1 81  ? 33.946 -1.045  3.062   1.00 11.47 ?  81  CYS   A SG   1 
ATOM   1708 H H    . CYS   A 1 81  ? 32.167 -3.683  2.663   1.00 12.50 ?  81  CYS   A H    1 
ATOM   1709 H HA   . CYS   A 1 81  ? 34.531 -4.594  3.546   1.00 12.69 ?  81  CYS   A HA   1 
ATOM   1710 H HB2  . CYS   A 1 81  ? 35.588 -2.560  3.657   1.00 13.66 ?  81  CYS   A HB2  1 
ATOM   1711 H HB3  . CYS   A 1 81  ? 35.161 -2.787  2.143   1.00 13.66 ?  81  CYS   A HB3  1 
ATOM   1712 H HG   . CYS   A 1 81  ? 34.696 -0.174  2.718   1.00 13.77 ?  81  CYS   A HG   1 
ATOM   1713 N N    . VAL   A 1 82  ? 34.078 -3.844  5.880   1.00 10.69 ?  82  VAL   A N    1 
ATOM   1714 C CA   . VAL   A 1 82  ? 33.656 -3.596  7.251   1.00 11.21 ?  82  VAL   A CA   1 
ATOM   1715 C C    . VAL   A 1 82  ? 34.267 -2.286  7.719   1.00 11.54 ?  82  VAL   A C    1 
ATOM   1716 O O    . VAL   A 1 82  ? 35.496 -2.126  7.706   1.00 12.28 ?  82  VAL   A O    1 
ATOM   1717 C CB   . VAL   A 1 82  ? 34.076 -4.736  8.191   1.00 12.82 ?  82  VAL   A CB   1 
ATOM   1718 C CG1  . VAL   A 1 82  ? 33.619 -4.432  9.610   1.00 14.26 ?  82  VAL   A CG1  1 
ATOM   1719 C CG2  . VAL   A 1 82  ? 33.525 -6.068  7.718   1.00 13.82 ?  82  VAL   A CG2  1 
ATOM   1720 H H    . VAL   A 1 82  ? 34.873 -4.186  5.823   1.00 12.83 ?  82  VAL   A H    1 
ATOM   1721 H HA   . VAL   A 1 82  ? 32.690 -3.513  7.278   1.00 13.45 ?  82  VAL   A HA   1 
ATOM   1722 H HB   . VAL   A 1 82  ? 35.043 -4.795  8.200   1.00 15.39 ?  82  VAL   A HB   1 
ATOM   1723 H HG11 . VAL   A 1 82  ? 33.690 -5.239  10.144  1.00 17.11 ?  82  VAL   A HG11 1 
ATOM   1724 H HG12 . VAL   A 1 82  ? 34.181 -3.737  9.988   1.00 17.11 ?  82  VAL   A HG12 1 
ATOM   1725 H HG13 . VAL   A 1 82  ? 32.694 -4.134  9.589   1.00 17.11 ?  82  VAL   A HG13 1 
ATOM   1726 H HG21 . VAL   A 1 82  ? 33.769 -6.753  8.358   1.00 16.58 ?  82  VAL   A HG21 1 
ATOM   1727 H HG22 . VAL   A 1 82  ? 32.559 -6.002  7.653   1.00 16.58 ?  82  VAL   A HG22 1 
ATOM   1728 H HG23 . VAL   A 1 82  ? 33.903 -6.272  6.850   1.00 16.58 ?  82  VAL   A HG23 1 
ATOM   1729 N N    . LEU   A 1 83  ? 33.416 -1.361  8.152   1.00 10.94 ?  83  LEU   A N    1 
ATOM   1730 C CA   . LEU   A 1 83  ? 33.833 -0.098  8.733   1.00 11.05 ?  83  LEU   A CA   1 
ATOM   1731 C C    . LEU   A 1 83  ? 33.122 0.079   10.072  1.00 11.20 ?  83  LEU   A C    1 
ATOM   1732 O O    . LEU   A 1 83  ? 32.400 -0.808  10.540  1.00 11.62 ?  83  LEU   A O    1 
ATOM   1733 C CB   . LEU   A 1 83  ? 33.589 1.064   7.755   1.00 11.67 ?  83  LEU   A CB   1 
ATOM   1734 C CG   . LEU   A 1 83  ? 34.492 1.058   6.513   1.00 12.33 ?  83  LEU   A CG   1 
ATOM   1735 C CD1  . LEU   A 1 83  ? 34.072 2.117   5.511   1.00 12.96 ?  83  LEU   A CD1  1 
ATOM   1736 C CD2  . LEU   A 1 83  ? 35.958 1.250   6.898   1.00 13.10 ?  83  LEU   A CD2  1 
ATOM   1737 H H    . LEU   A 1 83  ? 32.561 -1.452  8.113   1.00 13.13 ?  83  LEU   A H    1 
ATOM   1738 H HA   . LEU   A 1 83  ? 34.783 -0.131  8.911   1.00 13.26 ?  83  LEU   A HA   1 
ATOM   1739 H HB2  . LEU   A 1 83  ? 32.670 1.024   7.444   1.00 14.01 ?  83  LEU   A HB2  1 
ATOM   1740 H HB3  . LEU   A 1 83  ? 33.737 1.902   8.218   1.00 14.01 ?  83  LEU   A HB3  1 
ATOM   1741 H HG   . LEU   A 1 83  ? 34.416 0.195   6.079   1.00 14.79 ?  83  LEU   A HG   1 
ATOM   1742 H HD11 . LEU   A 1 83  ? 34.663 2.071   4.740   1.00 15.55 ?  83  LEU   A HD11 1 
ATOM   1743 H HD12 . LEU   A 1 83  ? 33.159 1.944   5.237   1.00 15.55 ?  83  LEU   A HD12 1 
ATOM   1744 H HD13 . LEU   A 1 83  ? 34.138 2.989   5.927   1.00 15.55 ?  83  LEU   A HD13 1 
ATOM   1745 H HD21 . LEU   A 1 83  ? 36.478 1.412   6.093   1.00 15.72 ?  83  LEU   A HD21 1 
ATOM   1746 H HD22 . LEU   A 1 83  ? 36.032 2.012   7.494   1.00 15.72 ?  83  LEU   A HD22 1 
ATOM   1747 H HD23 . LEU   A 1 83  ? 36.279 0.450   7.341   1.00 15.72 ?  83  LEU   A HD23 1 
ATOM   1748 N N    . SER   A 1 84  ? 33.351 1.225   10.709  1.00 11.61 ?  84  SER   A N    1 
ATOM   1749 C CA   . SER   A 1 84  ? 32.707 1.489   11.986  1.00 11.73 ?  84  SER   A CA   1 
ATOM   1750 C C    . SER   A 1 84  ? 31.189 1.568   11.838  1.00 11.63 ?  84  SER   A C    1 
ATOM   1751 O O    . SER   A 1 84  ? 30.659 2.026   10.825  1.00 11.91 ?  84  SER   A O    1 
ATOM   1752 C CB   . SER   A 1 84  ? 33.195 2.818   12.552  1.00 12.95 ?  84  SER   A CB   1 
ATOM   1753 O OG   . SER   A 1 84  ? 32.551 3.102   13.780  1.00 13.98 ?  84  SER   A OG   1 
ATOM   1754 H H    . SER   A 1 84  ? 33.871 1.857   10.423  1.00 13.93 ?  84  SER   A H    1 
ATOM   1755 H HA   . SER   A 1 84  ? 32.932 0.785   12.610  1.00 14.08 ?  84  SER   A HA   1 
ATOM   1756 H HB2  . SER   A 1 84  ? 34.154 2.774   12.696  1.00 15.54 ?  84  SER   A HB2  1 
ATOM   1757 H HB3  . SER   A 1 84  ? 32.991 3.528   11.919  1.00 15.54 ?  84  SER   A HB3  1 
ATOM   1758 H HG   . SER   A 1 84  ? 32.824 3.834   14.088  1.00 16.78 ?  84  SER   A HG   1 
ATOM   1759 N N    . GLY   A 1 85  ? 30.485 1.154   12.887  1.00 12.37 ?  85  GLY   A N    1 
ATOM   1760 C CA   . GLY   A 1 85  ? 29.061 1.386   12.976  1.00 13.01 ?  85  GLY   A CA   1 
ATOM   1761 C C    . GLY   A 1 85  ? 28.679 2.701   13.612  1.00 12.52 ?  85  GLY   A C    1 
ATOM   1762 O O    . GLY   A 1 85  ? 27.487 3.006   13.724  1.00 12.96 ?  85  GLY   A O    1 
ATOM   1763 H H    . GLY   A 1 85  ? 30.823 0.728   13.558  1.00 14.84 ?  85  GLY   A H    1 
ATOM   1764 H HA2  . GLY   A 1 85  ? 28.687 1.357   12.082  1.00 15.62 ?  85  GLY   A HA2  1 
ATOM   1765 H HA3  . GLY   A 1 85  ? 28.663 0.671   13.492  1.00 15.62 ?  85  GLY   A HA3  1 
ATOM   1766 N N    . HIS   A 1 86  ? 29.657 3.484   14.053  1.00 12.17 ?  86  HIS   A N    1 
ATOM   1767 C CA   . HIS   A 1 86  ? 29.413 4.820   14.613  1.00 12.72 ?  86  HIS   A CA   1 
ATOM   1768 C C    . HIS   A 1 86  ? 28.422 4.692   15.764  1.00 13.84 ?  86  HIS   A C    1 
ATOM   1769 O O    . HIS   A 1 86  ? 28.606 3.815   16.623  1.00 14.86 ?  86  HIS   A O    1 
ATOM   1770 C CB   . HIS   A 1 86  ? 29.036 5.792   13.502  1.00 12.79 ?  86  HIS   A CB   1 
ATOM   1771 C CG   . HIS   A 1 86  ? 30.099 5.900   12.468  1.00 12.94 ?  86  HIS   A CG   1 
ATOM   1772 N ND1  . HIS   A 1 86  ? 31.189 6.731   12.614  1.00 14.23 ?  86  HIS   A ND1  1 
ATOM   1773 C CD2  . HIS   A 1 86  ? 30.296 5.213   11.321  1.00 12.81 ?  86  HIS   A CD2  1 
ATOM   1774 C CE1  . HIS   A 1 86  ? 31.992 6.576   11.577  1.00 14.20 ?  86  HIS   A CE1  1 
ATOM   1775 N NE2  . HIS   A 1 86  ? 31.478 5.656   10.783  1.00 13.32 ?  86  HIS   A NE2  1 
ATOM   1776 H H    . HIS   A 1 86  ? 30.485 3.265   14.055  1.00 14.60 ?  86  HIS   A H    1 
ATOM   1777 H HA   . HIS   A 1 86  ? 30.245 5.144   14.993  1.00 15.26 ?  86  HIS   A HA   1 
ATOM   1778 H HB2  . HIS   A 1 86  ? 28.222 5.490   13.069  1.00 15.35 ?  86  HIS   A HB2  1 
ATOM   1779 H HB3  . HIS   A 1 86  ? 28.898 6.680   13.879  1.00 15.35 ?  86  HIS   A HB3  1 
ATOM   1780 H HD2  . HIS   A 1 86  ? 29.742 4.554   10.960  1.00 15.37 ?  86  HIS   A HD2  1 
ATOM   1781 H HE1  . HIS   A 1 86  ? 32.786 7.040   11.425  1.00 17.05 ?  86  HIS   A HE1  1 
ATOM   1782 H HE2  . HIS   A 1 86  ? 31.827 5.384   10.037  1.00 15.99 ?  86  HIS   A HE2  1 
ATOM   1783 N N    . ASN   A 1 87  ? 27.402 5.533   15.829  1.00 14.50 ?  87  ASN   A N    1 
ATOM   1784 C CA   . ASN   A 1 87  ? 26.400 5.510   16.880  1.00 15.77 ?  87  ASN   A CA   1 
ATOM   1785 C C    . ASN   A 1 87  ? 25.281 4.517   16.611  1.00 16.93 ?  87  ASN   A C    1 
ATOM   1786 O O    . ASN   A 1 87  ? 24.325 4.469   17.389  1.00 19.35 ?  87  ASN   A O    1 
ATOM   1787 C CB   . ASN   A 1 87  ? 25.803 6.914   17.055  1.00 16.77 ?  87  ASN   A CB   1 
ATOM   1788 C CG   . ASN   A 1 87  ? 25.295 7.509   15.745  1.00 17.43 ?  87  ASN   A CG   1 
ATOM   1789 O OD1  . ASN   A 1 87  ? 25.926 7.380   14.698  1.00 18.42 ?  87  ASN   A OD1  1 
ATOM   1790 N ND2  . ASN   A 1 87  ? 24.151 8.166   15.806  1.00 18.59 ?  87  ASN   A ND2  1 
ATOM   1791 H H    . ASN   A 1 87  ? 27.264 6.157   15.256  1.00 17.40 ?  87  ASN   A H    1 
ATOM   1792 H HA   . ASN   A 1 87  ? 26.815 5.256   17.720  1.00 18.92 ?  87  ASN   A HA   1 
ATOM   1793 H HB2  . ASN   A 1 87  ? 25.053 6.863   17.678  1.00 20.12 ?  87  ASN   A HB2  1 
ATOM   1794 H HB3  . ASN   A 1 87  ? 26.483 7.503   17.410  1.00 20.12 ?  87  ASN   A HB3  1 
ATOM   1795 H HD21 . ASN   A 1 87  ? 23.821 8.518   15.097  1.00 22.31 ?  87  ASN   A HD21 1 
ATOM   1796 H HD22 . ASN   A 1 87  ? 23.735 8.244   16.558  1.00 22.31 ?  87  ASN   A HD22 1 
ATOM   1797 N N    . LEU   A 1 88  ? 25.372 3.726   15.544  1.00 15.45 ?  88  LEU   A N    1 
ATOM   1798 C CA   . LEU   A 1 88  ? 24.278 2.853   15.138  1.00 15.70 ?  88  LEU   A CA   1 
ATOM   1799 C C    . LEU   A 1 88  ? 24.501 1.384   15.455  1.00 15.12 ?  88  LEU   A C    1 
ATOM   1800 O O    . LEU   A 1 88  ? 23.526 0.646   15.613  1.00 16.60 ?  88  LEU   A O    1 
ATOM   1801 C CB   . LEU   A 1 88  ? 24.036 2.993   13.631  1.00 16.63 ?  88  LEU   A CB   1 
ATOM   1802 C CG   . LEU   A 1 88  ? 23.752 4.417   13.142  1.00 18.69 ?  88  LEU   A CG   1 
ATOM   1803 C CD1  . LEU   A 1 88  ? 23.598 4.448   11.632  1.00 19.29 ?  88  LEU   A CD1  1 
ATOM   1804 C CD2  . LEU   A 1 88  ? 22.510 4.986   13.818  1.00 20.16 ?  88  LEU   A CD2  1 
ATOM   1805 H H    . LEU   A 1 88  ? 26.068 3.679   15.037  1.00 18.54 ?  88  LEU   A H    1 
ATOM   1806 H HA   . LEU   A 1 88  ? 23.470 3.139   15.591  1.00 18.84 ?  88  LEU   A HA   1 
ATOM   1807 H HB2  . LEU   A 1 88  ? 24.818 2.678   13.156  1.00 19.95 ?  88  LEU   A HB2  1 
ATOM   1808 H HB3  . LEU   A 1 88  ? 23.267 2.451   13.390  1.00 19.95 ?  88  LEU   A HB3  1 
ATOM   1809 H HG   . LEU   A 1 88  ? 24.502 4.986   13.370  1.00 22.43 ?  88  LEU   A HG   1 
ATOM   1810 H HD11 . LEU   A 1 88  ? 23.445 5.364   11.345  1.00 23.15 ?  88  LEU   A HD11 1 
ATOM   1811 H HD12 . LEU   A 1 88  ? 24.410 4.107   11.223  1.00 23.15 ?  88  LEU   A HD12 1 
ATOM   1812 H HD13 . LEU   A 1 88  ? 22.843 3.894   11.378  1.00 23.15 ?  88  LEU   A HD13 1 
ATOM   1813 H HD21 . LEU   A 1 88  ? 22.278 5.827   13.395  1.00 24.20 ?  88  LEU   A HD21 1 
ATOM   1814 H HD22 . LEU   A 1 88  ? 21.783 4.353   13.721  1.00 24.20 ?  88  LEU   A HD22 1 
ATOM   1815 H HD23 . LEU   A 1 88  ? 22.704 5.128   14.757  1.00 24.20 ?  88  LEU   A HD23 1 
ATOM   1816 N N    . ALA   A 1 89  ? 25.752 0.948   15.546  1.00 14.18 ?  89  ALA   A N    1 
ATOM   1817 C CA   . ALA   A 1 89  ? 26.099 -0.462  15.644  1.00 13.88 ?  89  ALA   A CA   1 
ATOM   1818 C C    . ALA   A 1 89  ? 27.584 -0.527  15.961  1.00 14.44 ?  89  ALA   A C    1 
ATOM   1819 O O    . ALA   A 1 89  ? 28.293 0.473   15.861  1.00 15.19 ?  89  ALA   A O    1 
ATOM   1820 C CB   . ALA   A 1 89  ? 25.817 -1.175  14.324  1.00 13.80 ?  89  ALA   A CB   1 
ATOM   1821 H H    . ALA   A 1 89  ? 26.435 1.473   15.545  1.00 17.01 ?  89  ALA   A H    1 
ATOM   1822 H HA   . ALA   A 1 89  ? 25.594 -0.879  16.359  1.00 16.65 ?  89  ALA   A HA   1 
ATOM   1823 H HB1  . ALA   A 1 89  ? 26.074 -2.107  14.410  1.00 16.56 ?  89  ALA   A HB1  1 
ATOM   1824 H HB2  . ALA   A 1 89  ? 24.866 -1.115  14.126  1.00 16.56 ?  89  ALA   A HB2  1 
ATOM   1825 H HB3  . ALA   A 1 89  ? 26.329 -0.754  13.619  1.00 16.56 ?  89  ALA   A HB3  1 
ATOM   1826 N N    . LYS   A 1 90  ? 28.064 -1.710  16.341  1.00 14.95 ?  90  LYS   A N    1 
ATOM   1827 C CA   . LYS   A 1 90  ? 29.508 -1.870  16.487  1.00 15.83 ?  90  LYS   A CA   1 
ATOM   1828 C C    . LYS   A 1 90  ? 30.207 -1.676  15.145  1.00 14.69 ?  90  LYS   A C    1 
ATOM   1829 O O    . LYS   A 1 90  ? 31.149 -0.874  15.022  1.00 15.82 ?  90  LYS   A O    1 
ATOM   1830 C CB   . LYS   A 1 90  ? 29.838 -3.237  17.087  1.00 18.72 ?  90  LYS   A CB   1 
ATOM   1831 C CG   . LYS   A 1 90  ? 31.309 -3.394  17.448  1.00 23.15 ?  90  LYS   A CG   1 
ATOM   1832 C CD   . LYS   A 1 90  ? 31.537 -4.626  18.308  1.00 27.41 ?  90  LYS   A CD   1 
ATOM   1833 C CE   . LYS   A 1 90  ? 32.938 -4.653  18.898  1.00 31.04 ?  90  LYS   A CE   1 
ATOM   1834 N NZ   . LYS   A 1 90  ? 33.977 -4.950  17.877  1.00 33.17 ?  90  LYS   A NZ   1 
ATOM   1835 H H    . LYS   A 1 90  ? 27.588 -2.400  16.519  1.00 17.95 ?  90  LYS   A H    1 
ATOM   1836 H HA   . LYS   A 1 90  ? 29.837 -1.190  17.094  1.00 19.00 ?  90  LYS   A HA   1 
ATOM   1837 H HB2  . LYS   A 1 90  ? 29.313 -3.360  17.895  1.00 22.46 ?  90  LYS   A HB2  1 
ATOM   1838 H HB3  . LYS   A 1 90  ? 29.611 -3.926  16.441  1.00 22.46 ?  90  LYS   A HB3  1 
ATOM   1839 H HG2  . LYS   A 1 90  ? 31.831 -3.488  16.636  1.00 27.78 ?  90  LYS   A HG2  1 
ATOM   1840 H HG3  . LYS   A 1 90  ? 31.601 -2.616  17.947  1.00 27.78 ?  90  LYS   A HG3  1 
ATOM   1841 H HD2  . LYS   A 1 90  ? 30.899 -4.628  19.040  1.00 32.89 ?  90  LYS   A HD2  1 
ATOM   1842 H HD3  . LYS   A 1 90  ? 31.422 -5.421  17.763  1.00 32.89 ?  90  LYS   A HD3  1 
ATOM   1843 H HE2  . LYS   A 1 90  ? 33.136 -3.786  19.286  1.00 37.25 ?  90  LYS   A HE2  1 
ATOM   1844 H HE3  . LYS   A 1 90  ? 32.982 -5.340  19.582  1.00 37.25 ?  90  LYS   A HE3  1 
ATOM   1845 H HZ1  . LYS   A 1 90  ? 34.783 -4.959  18.256  1.00 39.81 ?  90  LYS   A HZ1  1 
ATOM   1846 H HZ2  . LYS   A 1 90  ? 33.823 -5.746  17.509  1.00 39.81 ?  90  LYS   A HZ2  1 
ATOM   1847 H HZ3  . LYS   A 1 90  ? 33.965 -4.330  17.240  1.00 39.81 ?  90  LYS   A HZ3  1 
ATOM   1848 N N    . HIS   A 1 91  ? 29.725 -2.378  14.119  1.00 12.96 ?  91  HIS   A N    1 
ATOM   1849 C CA   . HIS   A 1 91  ? 30.298 -2.351  12.787  1.00 12.45 ?  91  HIS   A CA   1 
ATOM   1850 C C    . HIS   A 1 91  ? 29.210 -2.073  11.767  1.00 11.21 ?  91  HIS   A C    1 
ATOM   1851 O O    . HIS   A 1 91  ? 28.046 -2.448  11.954  1.00 11.72 ?  91  HIS   A O    1 
ATOM   1852 C CB   . HIS   A 1 91  ? 30.895 -3.717  12.418  1.00 15.00 ?  91  HIS   A CB   1 
ATOM   1853 C CG   . HIS   A 1 91  ? 31.877 -4.244  13.415  1.00 19.25 ?  91  HIS   A CG   1 
ATOM   1854 N ND1  . HIS   A 1 91  ? 33.156 -3.746  13.536  1.00 21.22 ?  91  HIS   A ND1  1 
ATOM   1855 C CD2  . HIS   A 1 91  ? 31.773 -5.237  14.330  1.00 21.09 ?  91  HIS   A CD2  1 
ATOM   1856 C CE1  . HIS   A 1 91  ? 33.797 -4.406  14.485  1.00 21.98 ?  91  HIS   A CE1  1 
ATOM   1857 N NE2  . HIS   A 1 91  ? 32.979 -5.317  14.983  1.00 22.22 ?  91  HIS   A NE2  1 
ATOM   1858 H H    . HIS   A 1 91  ? 29.047 -2.915  14.183  1.00 15.55 ?  91  HIS   A H    1 
ATOM   1859 H HA   . HIS   A 1 91  ? 30.986 -1.673  12.727  1.00 14.94 ?  91  HIS   A HA   1 
ATOM   1860 H HB2  . HIS   A 1 91  ? 30.176 -4.366  12.347  1.00 18.01 ?  91  HIS   A HB2  1 
ATOM   1861 H HB3  . HIS   A 1 91  ? 31.351 -3.640  11.566  1.00 18.01 ?  91  HIS   A HB3  1 
ATOM   1862 H HD1  . HIS   A 1 91  ? 33.487 -3.105  13.064  1.00 25.46 ?  91  HIS   A HD1  1 
ATOM   1863 H HD2  . HIS   A 1 91  ? 31.029 -5.767  14.489  1.00 25.31 ?  91  HIS   A HD2  1 
ATOM   1864 H HE1  . HIS   A 1 91  ? 34.676 -4.250  14.755  1.00 26.38 ?  91  HIS   A HE1  1 
ATOM   1865 N N    . CYS   A 1 92  ? 29.615 -1.468  10.655  1.00 10.89 ?  92  CYS   A N    1 
ATOM   1866 C CA   . CYS   A 1 92  ? 28.780 -1.391  9.467   1.00 10.68 ?  92  CYS   A CA   1 
ATOM   1867 C C    . CYS   A 1 92  ? 29.427 -2.213  8.360   1.00 10.35 ?  92  CYS   A C    1 
ATOM   1868 O O    . CYS   A 1 92  ? 30.587 -1.964  7.990   1.00 10.89 ?  92  CYS   A O    1 
ATOM   1869 C CB   . CYS   A 1 92  ? 28.575 0.054   9.016   1.00 11.21 ?  92  CYS   A CB   1 
ATOM   1870 S SG   . CYS   A 1 92  ? 27.554 0.171   7.515   1.00 10.78 ?  92  CYS   A SG   1 
ATOM   1871 H H    . CYS   A 1 92  ? 30.380 -1.082  10.568  1.00 13.07 ?  92  CYS   A H    1 
ATOM   1872 H HA   . CYS   A 1 92  ? 27.910 -1.771  9.662   1.00 12.82 ?  92  CYS   A HA   1 
ATOM   1873 H HB2  . CYS   A 1 92  ? 28.126 0.550   9.719   1.00 13.45 ?  92  CYS   A HB2  1 
ATOM   1874 H HB3  . CYS   A 1 92  ? 29.434 0.455   8.821   1.00 13.45 ?  92  CYS   A HB3  1 
ATOM   1875 H HG   . CYS   A 1 92  ? 27.424 1.324   7.224   1.00 12.94 ?  92  CYS   A HG   1 
ATOM   1876 N N    . LEU   A 1 93  ? 28.684 -3.194  7.854   1.00 9.97  ?  93  LEU   A N    1 
ATOM   1877 C CA   . LEU   A 1 93  ? 29.074 -3.949  6.672   1.00 9.65  ?  93  LEU   A CA   1 
ATOM   1878 C C    . LEU   A 1 93  ? 28.479 -3.248  5.455   1.00 9.39  ?  93  LEU   A C    1 
ATOM   1879 O O    . LEU   A 1 93  ? 27.266 -3.298  5.228   1.00 9.47  ?  93  LEU   A O    1 
ATOM   1880 C CB   . LEU   A 1 93  ? 28.584 -5.390  6.780   1.00 10.13 ?  93  LEU   A CB   1 
ATOM   1881 C CG   . LEU   A 1 93  ? 28.969 -6.293  5.610   1.00 10.65 ?  93  LEU   A CG   1 
ATOM   1882 C CD1  . LEU   A 1 93  ? 30.473 -6.567  5.600   1.00 11.61 ?  93  LEU   A CD1  1 
ATOM   1883 C CD2  . LEU   A 1 93  ? 28.185 -7.605  5.640   1.00 11.38 ?  93  LEU   A CD2  1 
ATOM   1884 H H    . LEU   A 1 93  ? 27.928 -3.435  8.185   1.00 11.96 ?  93  LEU   A H    1 
ATOM   1885 H HA   . LEU   A 1 93  ? 30.040 -3.948  6.595   1.00 11.59 ?  93  LEU   A HA   1 
ATOM   1886 H HB2  . LEU   A 1 93  ? 28.957 -5.777  7.590   1.00 12.16 ?  93  LEU   A HB2  1 
ATOM   1887 H HB3  . LEU   A 1 93  ? 27.619 -5.382  6.839   1.00 12.16 ?  93  LEU   A HB3  1 
ATOM   1888 H HG   . LEU   A 1 93  ? 28.755 -5.847  4.785   1.00 12.78 ?  93  LEU   A HG   1 
ATOM   1889 H HD11 . LEU   A 1 93  ? 30.684 -7.187  4.882   1.00 13.94 ?  93  LEU   A HD11 1 
ATOM   1890 H HD12 . LEU   A 1 93  ? 30.952 -5.734  5.466   1.00 13.94 ?  93  LEU   A HD12 1 
ATOM   1891 H HD13 . LEU   A 1 93  ? 30.738 -6.961  6.453   1.00 13.94 ?  93  LEU   A HD13 1 
ATOM   1892 H HD21 . LEU   A 1 93  ? 28.456 -8.158  4.888   1.00 13.65 ?  93  LEU   A HD21 1 
ATOM   1893 H HD22 . LEU   A 1 93  ? 28.369 -8.074  6.472   1.00 13.65 ?  93  LEU   A HD22 1 
ATOM   1894 H HD23 . LEU   A 1 93  ? 27.236 -7.409  5.578   1.00 13.65 ?  93  LEU   A HD23 1 
ATOM   1895 N N    . HIS   A 1 94  ? 29.334 -2.559  4.700   1.00 9.32  ?  94  HIS   A N    1 
ATOM   1896 C CA   . HIS   A 1 94  ? 28.919 -1.880  3.478   1.00 9.30  ?  94  HIS   A CA   1 
ATOM   1897 C C    . HIS   A 1 94  ? 28.927 -2.911  2.364   1.00 9.18  ?  94  HIS   A C    1 
ATOM   1898 O O    . HIS   A 1 94  ? 29.988 -3.439  2.025   1.00 10.70 ?  94  HIS   A O    1 
ATOM   1899 C CB   . HIS   A 1 94  ? 29.885 -0.744  3.148   1.00 9.40  ?  94  HIS   A CB   1 
ATOM   1900 C CG   . HIS   A 1 94  ? 29.874 0.352   4.158   1.00 9.46  ?  94  HIS   A CG   1 
ATOM   1901 N ND1  . HIS   A 1 94  ? 29.000 1.418   4.094   1.00 9.67  ?  94  HIS   A ND1  1 
ATOM   1902 C CD2  . HIS   A 1 94  ? 30.603 0.513   5.285   1.00 10.19 ?  94  HIS   A CD2  1 
ATOM   1903 C CE1  . HIS   A 1 94  ? 29.212 2.194   5.141   1.00 9.72  ?  94  HIS   A CE1  1 
ATOM   1904 N NE2  . HIS   A 1 94  ? 30.178 1.671   5.877   1.00 10.31 ?  94  HIS   A NE2  1 
ATOM   1905 H H    . HIS   A 1 94  ? 30.175 -2.474  4.871   1.00 11.18 ?  94  HIS   A H    1 
ATOM   1906 H HA   . HIS   A 1 94  ? 28.020 -1.526  3.578   1.00 11.16 ?  94  HIS   A HA   1 
ATOM   1907 H HB2  . HIS   A 1 94  ? 30.780 -1.101  3.101   1.00 11.29 ?  94  HIS   A HB2  1 
ATOM   1908 H HB3  . HIS   A 1 94  ? 29.632 -0.361  2.291   1.00 11.29 ?  94  HIS   A HB3  1 
ATOM   1909 H HD2  . HIS   A 1 94  ? 31.267 -0.049  5.600   1.00 12.23 ?  94  HIS   A HD2  1 
ATOM   1910 H HE1  . HIS   A 1 94  ? 28.747 2.983   5.320   1.00 11.67 ?  94  HIS   A HE1  1 
ATOM   1911 H HE2  . HIS   A 1 94  ? 30.481 2.012   6.602   1.00 12.37 ?  94  HIS   A HE2  1 
ATOM   1912 N N    . VAL   A 1 95  ? 27.756 -3.231  1.812   1.00 8.71  ?  95  VAL   A N    1 
ATOM   1913 C CA   . VAL   A 1 95  ? 27.612 -4.265  0.792   1.00 9.16  ?  95  VAL   A CA   1 
ATOM   1914 C C    . VAL   A 1 95  ? 27.073 -3.623  -0.475  1.00 8.89  ?  95  VAL   A C    1 
ATOM   1915 O O    . VAL   A 1 95  ? 26.075 -2.892  -0.422  1.00 9.67  ?  95  VAL   A O    1 
ATOM   1916 C CB   . VAL   A 1 95  ? 26.677 -5.408  1.238   1.00 9.76  ?  95  VAL   A CB   1 
ATOM   1917 C CG1  . VAL   A 1 95  ? 26.572 -6.448  0.135   1.00 10.58 ?  95  VAL   A CG1  1 
ATOM   1918 C CG2  . VAL   A 1 95  ? 27.169 -6.037  2.521   1.00 10.07 ?  95  VAL   A CG2  1 
ATOM   1919 H H    . VAL   A 1 95  ? 27.009 -2.852  2.017   1.00 10.46 ?  95  VAL   A H    1 
ATOM   1920 H HA   . VAL   A 1 95  ? 28.479 -4.645  0.593   1.00 10.99 ?  95  VAL   A HA   1 
ATOM   1921 H HB   . VAL   A 1 95  ? 25.793 -5.052  1.400   1.00 11.71 ?  95  VAL   A HB   1 
ATOM   1922 H HG11 . VAL   A 1 95  ? 26.176 -7.259  0.499   1.00 12.69 ?  95  VAL   A HG11 1 
ATOM   1923 H HG12 . VAL   A 1 95  ? 26.017 -6.106  -0.581  1.00 12.69 ?  95  VAL   A HG12 1 
ATOM   1924 H HG13 . VAL   A 1 95  ? 27.463 -6.648  -0.203  1.00 12.69 ?  95  VAL   A HG13 1 
ATOM   1925 H HG21 . VAL   A 1 95  ? 26.600 -6.790  2.744   1.00 12.08 ?  95  VAL   A HG21 1 
ATOM   1926 H HG22 . VAL   A 1 95  ? 28.084 -6.341  2.396   1.00 12.08 ?  95  VAL   A HG22 1 
ATOM   1927 H HG23 . VAL   A 1 95  ? 27.137 -5.376  3.230   1.00 12.08 ?  95  VAL   A HG23 1 
ATOM   1928 N N    . VAL   A 1 96  ? 27.707 -3.916  -1.610  1.00 9.04  ?  96  VAL   A N    1 
ATOM   1929 C CA   . VAL   A 1 96  ? 27.306 -3.359  -2.897  1.00 9.65  ?  96  VAL   A CA   1 
ATOM   1930 C C    . VAL   A 1 96  ? 26.493 -4.400  -3.658  1.00 9.59  ?  96  VAL   A C    1 
ATOM   1931 O O    . VAL   A 1 96  ? 27.044 -5.342  -4.237  1.00 10.77 ?  96  VAL   A O    1 
ATOM   1932 C CB   . VAL   A 1 96  ? 28.505 -2.888  -3.724  1.00 10.13 ?  96  VAL   A CB   1 
ATOM   1933 C CG1  . VAL   A 1 96  ? 28.004 -2.238  -5.001  1.00 10.30 ?  96  VAL   A CG1  1 
ATOM   1934 C CG2  . VAL   A 1 96  ? 29.367 -1.919  -2.929  1.00 10.54 ?  96  VAL   A CG2  1 
ATOM   1935 H H    . VAL   A 1 96  ? 28.390 -4.443  -1.659  1.00 10.85 ?  96  VAL   A H    1 
ATOM   1936 H HA   . VAL   A 1 96  ? 26.738 -2.592  -2.744  1.00 11.58 ?  96  VAL   A HA   1 
ATOM   1937 H HB   . VAL   A 1 96  ? 29.051 -3.650  -3.969  1.00 12.15 ?  96  VAL   A HB   1 
ATOM   1938 H HG11 . VAL   A 1 96  ? 28.745 -1.774  -5.426  1.00 12.36 ?  96  VAL   A HG11 1 
ATOM   1939 H HG12 . VAL   A 1 96  ? 27.660 -2.921  -5.593  1.00 12.36 ?  96  VAL   A HG12 1 
ATOM   1940 H HG13 . VAL   A 1 96  ? 27.306 -1.603  -4.778  1.00 12.36 ?  96  VAL   A HG13 1 
ATOM   1941 H HG21 . VAL   A 1 96  ? 30.077 -1.581  -3.497  1.00 12.65 ?  96  VAL   A HG21 1 
ATOM   1942 H HG22 . VAL   A 1 96  ? 28.813 -1.179  -2.622  1.00 12.65 ?  96  VAL   A HG22 1 
ATOM   1943 H HG23 . VAL   A 1 96  ? 29.746 -2.381  -2.166  1.00 12.65 ?  96  VAL   A HG23 1 
ATOM   1944 N N    . GLY   A 1 97  ? 25.175 -4.232  -3.685  1.00 9.98  ?  97  GLY   A N    1 
ATOM   1945 C CA   . GLY   A 1 97  ? 24.353 -4.981  -4.600  1.00 10.38 ?  97  GLY   A CA   1 
ATOM   1946 C C    . GLY   A 1 97  ? 24.363 -4.324  -5.965  1.00 10.67 ?  97  GLY   A C    1 
ATOM   1947 O O    . GLY   A 1 97  ? 24.656 -3.131  -6.103  1.00 11.37 ?  97  GLY   A O    1 
ATOM   1948 H H    . GLY   A 1 97  ? 24.734 -3.688  -3.176  1.00 11.98 ?  97  GLY   A H    1 
ATOM   1949 H HA2  . GLY   A 1 97  ? 24.699 -5.888  -4.661  1.00 12.46 ?  97  GLY   A HA2  1 
ATOM   1950 H HA3  . GLY   A 1 97  ? 23.438 -5.023  -4.268  1.00 12.46 ?  97  GLY   A HA3  1 
ATOM   1951 N N    A PRO   A 1 98  ? 24.004 -5.068  -7.008  0.74 10.55 ?  98  PRO   A N    1 
ATOM   1952 N N    B PRO   A 1 98  ? 24.098 -5.111  -7.004  0.26 10.80 ?  98  PRO   A N    1 
ATOM   1953 C CA   A PRO   A 1 98  ? 23.884 -4.446  -8.332  0.74 11.80 ?  98  PRO   A CA   1 
ATOM   1954 C CA   B PRO   A 1 98  ? 24.070 -4.552  -8.357  0.26 11.55 ?  98  PRO   A CA   1 
ATOM   1955 C C    A PRO   A 1 98  ? 22.773 -3.402  -8.365  0.74 11.81 ?  98  PRO   A C    1 
ATOM   1956 C C    B PRO   A 1 98  ? 22.950 -3.538  -8.508  0.26 12.21 ?  98  PRO   A C    1 
ATOM   1957 O O    A PRO   A 1 98  ? 21.704 -3.581  -7.779  0.74 11.42 ?  98  PRO   A O    1 
ATOM   1958 O O    B PRO   A 1 98  ? 21.826 -3.745  -8.047  0.26 12.27 ?  98  PRO   A O    1 
ATOM   1959 C CB   A PRO   A 1 98  ? 23.568 -5.631  -9.251  0.74 12.27 ?  98  PRO   A CB   1 
ATOM   1960 C CB   B PRO   A 1 98  ? 23.826 -5.779  -9.240  0.26 11.46 ?  98  PRO   A CB   1 
ATOM   1961 C CG   A PRO   A 1 98  ? 22.922 -6.640  -8.352  0.74 12.12 ?  98  PRO   A CG   1 
ATOM   1962 C CG   B PRO   A 1 98  ? 23.186 -6.782  -8.329  0.26 11.44 ?  98  PRO   A CG   1 
ATOM   1963 C CD   A PRO   A 1 98  ? 23.656 -6.501  -7.036  0.74 11.09 ?  98  PRO   A CD   1 
ATOM   1964 C CD   B PRO   A 1 98  ? 23.849 -6.563  -7.003  0.26 10.87 ?  98  PRO   A CD   1 
ATOM   1965 H HA   A PRO   A 1 98  ? 24.726 -4.042  -8.588  0.74 14.16 ?  98  PRO   A HA   1 
ATOM   1966 H HA   B PRO   A 1 98  ? 24.924 -4.144  -8.575  0.26 13.86 ?  98  PRO   A HA   1 
ATOM   1967 H HB2  A PRO   A 1 98  ? 22.957 -5.347  -9.949  0.74 14.72 ?  98  PRO   A HB2  1 
ATOM   1968 H HB2  B PRO   A 1 98  ? 23.226 -5.537  -9.963  0.26 13.75 ?  98  PRO   A HB2  1 
ATOM   1969 H HB3  A PRO   A 1 98  ? 24.389 -5.981  -9.629  0.74 14.72 ?  98  PRO   A HB3  1 
ATOM   1970 H HB3  B PRO   A 1 98  ? 24.668 -6.107  -9.580  0.26 13.75 ?  98  PRO   A HB3  1 
ATOM   1971 H HG2  A PRO   A 1 98  ? 21.981 -6.427  -8.249  0.74 14.54 ?  98  PRO   A HG2  1 
ATOM   1972 H HG2  B PRO   A 1 98  ? 22.232 -6.609  -8.269  0.26 13.73 ?  98  PRO   A HG2  1 
ATOM   1973 H HG3  A PRO   A 1 98  ? 23.038 -7.526  -8.723  0.74 14.54 ?  98  PRO   A HG3  1 
ATOM   1974 H HG3  B PRO   A 1 98  ? 23.356 -7.675  -8.659  0.26 13.73 ?  98  PRO   A HG3  1 
ATOM   1975 H HD2  A PRO   A 1 98  ? 23.065 -6.731  -6.296  0.74 13.30 ?  98  PRO   A HD2  1 
ATOM   1976 H HD2  B PRO   A 1 98  ? 23.251 -6.810  -6.278  0.26 13.04 ?  98  PRO   A HD2  1 
ATOM   1977 H HD3  A PRO   A 1 98  ? 24.457 -7.047  -7.032  0.74 13.30 ?  98  PRO   A HD3  1 
ATOM   1978 H HD3  B PRO   A 1 98  ? 24.687 -7.053  -6.955  0.26 13.04 ?  98  PRO   A HD3  1 
ATOM   1979 N N    A ASN   A 1 99  ? 23.041 -2.296  -9.059  0.74 13.05 ?  99  ASN   A N    1 
ATOM   1980 N N    B ASN   A 1 99  ? 23.267 -2.433  -9.169  0.26 12.98 ?  99  ASN   A N    1 
ATOM   1981 C CA   A ASN   A 1 99  ? 22.068 -1.223  -9.257  0.74 14.32 ?  99  ASN   A CA   1 
ATOM   1982 C CA   B ASN   A 1 99  ? 22.280 -1.407  -9.475  0.26 13.89 ?  99  ASN   A CA   1 
ATOM   1983 C C    A ASN   A 1 99  ? 21.499 -1.349  -10.668 0.74 15.44 ?  99  ASN   A C    1 
ATOM   1984 C C    B ASN   A 1 99  ? 21.734 -1.695  -10.870 0.26 14.43 ?  99  ASN   A C    1 
ATOM   1985 O O    A ASN   A 1 99  ? 22.175 -1.024  -11.653 0.74 16.41 ?  99  ASN   A O    1 
ATOM   1986 O O    B ASN   A 1 99  ? 22.453 -1.569  -11.868 0.26 14.13 ?  99  ASN   A O    1 
ATOM   1987 C CB   A ASN   A 1 99  ? 22.716 0.145   -9.046  0.74 14.20 ?  99  ASN   A CB   1 
ATOM   1988 C CB   B ASN   A 1 99  ? 22.904 -0.018  -9.383  0.26 14.85 ?  99  ASN   A CB   1 
ATOM   1989 C CG   A ASN   A 1 99  ? 21.702 1.292   -9.059  0.74 14.47 ?  99  ASN   A CG   1 
ATOM   1990 C CG   B ASN   A 1 99  ? 21.872 1.088   -9.471  0.26 15.66 ?  99  ASN   A CG   1 
ATOM   1991 O OD1  A ASN   A 1 99  ? 20.691 1.236   -9.761  0.74 14.86 ?  99  ASN   A OD1  1 
ATOM   1992 O OD1  B ASN   A 1 99  ? 21.012 1.074   -10.349 0.26 15.50 ?  99  ASN   A OD1  1 
ATOM   1993 N ND2  A ASN   A 1 99  ? 21.987 2.346   -8.291  0.74 15.13 ?  99  ASN   A ND2  1 
ATOM   1994 N ND2  B ASN   A 1 99  ? 21.947 2.048   -8.551  0.26 16.39 ?  99  ASN   A ND2  1 
ATOM   1995 H H    A ASN   A 1 99  ? 23.805 -2.135  -9.414  0.74 15.66 ?  99  ASN   A H    1 
ATOM   1996 H H    B ASN   A 1 99  ? 24.058 -2.252  -9.453  0.26 15.58 ?  99  ASN   A H    1 
ATOM   1997 H HA   A ASN   A 1 99  ? 21.343 -1.320  -8.611  0.74 17.18 ?  99  ASN   A HA   1 
ATOM   1998 H HA   B ASN   A 1 99  ? 21.550 -1.458  -8.834  0.26 16.67 ?  99  ASN   A HA   1 
ATOM   1999 H HB2  A ASN   A 1 99  ? 23.173 0.158   -8.191  0.74 17.05 ?  99  ASN   A HB2  1 
ATOM   2000 H HB2  B ASN   A 1 99  ? 23.365 0.070   -8.534  0.26 17.82 ?  99  ASN   A HB2  1 
ATOM   2001 H HB3  A ASN   A 1 99  ? 23.355 0.300   -9.763  0.74 17.05 ?  99  ASN   A HB3  1 
ATOM   2002 H HB3  B ASN   A 1 99  ? 23.528 0.098   -10.112 0.26 17.82 ?  99  ASN   A HB3  1 
ATOM   2003 H HD21 A ASN   A 1 99  ? 21.454 3.018   -8.265  0.74 18.15 ?  99  ASN   A HD21 1 
ATOM   2004 H HD21 B ASN   A 1 99  ? 21.380 2.695   -8.552  0.26 19.67 ?  99  ASN   A HD21 1 
ATOM   2005 H HD22 A ASN   A 1 99  ? 22.707 2.348   -7.817  0.74 18.15 ?  99  ASN   A HD22 1 
ATOM   2006 H HD22 B ASN   A 1 99  ? 22.563 2.020   -7.949  0.26 19.67 ?  99  ASN   A HD22 1 
ATOM   2007 N N    A VAL   A 1 100 ? 20.249 -1.816  -10.752 0.74 16.12 ?  100 VAL   A N    1 
ATOM   2008 N N    B VAL   A 1 100 ? 20.472 -2.120  -10.931 0.26 15.63 ?  100 VAL   A N    1 
ATOM   2009 C CA   A VAL   A 1 100 ? 19.603 -2.035  -12.043 0.74 18.19 ?  100 VAL   A CA   1 
ATOM   2010 C CA   B VAL   A 1 100 ? 19.853 -2.432  -12.215 0.26 17.69 ?  100 VAL   A CA   1 
ATOM   2011 C C    A VAL   A 1 100 ? 19.484 -0.730  -12.817 0.74 18.39 ?  100 VAL   A C    1 
ATOM   2012 C C    B VAL   A 1 100 ? 19.761 -1.183  -13.080 0.26 18.92 ?  100 VAL   A C    1 
ATOM   2013 O O    A VAL   A 1 100 ? 19.546 -0.721  -14.053 0.74 19.30 ?  100 VAL   A O    1 
ATOM   2014 O O    B VAL   A 1 100 ? 19.900 -1.248  -14.308 0.26 19.52 ?  100 VAL   A O    1 
ATOM   2015 C CB   A VAL   A 1 100 ? 18.240 -2.734  -11.842 0.74 19.85 ?  100 VAL   A CB   1 
ATOM   2016 C CB   B VAL   A 1 100 ? 18.474 -3.080  -12.000 0.26 18.47 ?  100 VAL   A CB   1 
ATOM   2017 C CG1  A VAL   A 1 100 ? 17.500 -2.877  -13.164 0.74 20.46 ?  100 VAL   A CG1  1 
ATOM   2018 C CG1  B VAL   A 1 100 ? 17.846 -3.447  -13.336 0.26 18.84 ?  100 VAL   A CG1  1 
ATOM   2019 C CG2  A VAL   A 1 100 ? 18.443 -4.096  -11.196 0.74 20.89 ?  100 VAL   A CG2  1 
ATOM   2020 C CG2  B VAL   A 1 100 ? 18.601 -4.300  -11.106 0.26 18.82 ?  100 VAL   A CG2  1 
ATOM   2021 H H    A VAL   A 1 100 ? 19.749 -2.006  -10.067 0.74 19.35 ?  100 VAL   A H    1 
ATOM   2022 H H    B VAL   A 1 100 ? 19.964 -2.245  -10.247 0.26 18.75 ?  100 VAL   A H    1 
ATOM   2023 H HA   A VAL   A 1 100 ? 20.156 -2.631  -12.562 0.74 21.82 ?  100 VAL   A HA   1 
ATOM   2024 H HA   B VAL   A 1 100 ? 20.413 -3.072  -12.681 0.26 21.23 ?  100 VAL   A HA   1 
ATOM   2025 H HB   A VAL   A 1 100 ? 17.690 -2.201  -11.247 0.74 23.82 ?  100 VAL   A HB   1 
ATOM   2026 H HB   B VAL   A 1 100 ? 17.893 -2.440  -11.560 0.26 22.16 ?  100 VAL   A HB   1 
ATOM   2027 H HG11 A VAL   A 1 100 ? 16.752 -3.485  -13.042 0.74 24.55 ?  100 VAL   A HG11 1 
ATOM   2028 H HG11 B VAL   A 1 100 ? 17.054 -3.982  -13.173 0.26 22.60 ?  100 VAL   A HG11 1 
ATOM   2029 H HG12 A VAL   A 1 100 ? 17.175 -2.008  -13.443 0.74 24.55 ?  100 VAL   A HG12 1 
ATOM   2030 H HG12 B VAL   A 1 100 ? 17.603 -2.634  -13.808 0.26 22.60 ?  100 VAL   A HG12 1 
ATOM   2031 H HG13 A VAL   A 1 100 ? 18.108 -3.237  -13.829 0.74 24.55 ?  100 VAL   A HG13 1 
ATOM   2032 H HG13 B VAL   A 1 100 ? 18.487 -3.955  -13.857 0.26 22.60 ?  100 VAL   A HG13 1 
ATOM   2033 H HG21 A VAL   A 1 100 ? 17.585 -4.545  -11.125 0.74 25.07 ?  100 VAL   A HG21 1 
ATOM   2034 H HG21 B VAL   A 1 100 ? 17.754 -4.771  -11.099 0.26 22.59 ?  100 VAL   A HG21 1 
ATOM   2035 H HG22 A VAL   A 1 100 ? 19.046 -4.620  -11.746 0.74 25.07 ?  100 VAL   A HG22 1 
ATOM   2036 H HG22 B VAL   A 1 100 ? 19.298 -4.874  -11.457 0.26 22.59 ?  100 VAL   A HG22 1 
ATOM   2037 H HG23 A VAL   A 1 100 ? 18.825 -3.974  -10.312 0.74 25.07 ?  100 VAL   A HG23 1 
ATOM   2038 H HG23 B VAL   A 1 100 ? 18.828 -4.012  -10.208 0.26 22.59 ?  100 VAL   A HG23 1 
ATOM   2039 N N    A ASN   A 1 101 ? 19.314 0.388   -12.119 0.74 19.61 ?  101 ASN   A N    1 
ATOM   2040 N N    B ASN   A 1 101 ? 19.518 -0.027  -12.456 0.26 19.68 ?  101 ASN   A N    1 
ATOM   2041 C CA   A ASN   A 1 101 ? 19.266 1.671   -12.808 0.74 21.27 ?  101 ASN   A CA   1 
ATOM   2042 C CA   B ASN   A 1 101 ? 19.390 1.207   -13.223 0.26 20.53 ?  101 ASN   A CA   1 
ATOM   2043 C C    A ASN   A 1 101 ? 20.626 2.096   -13.368 0.74 23.31 ?  101 ASN   A C    1 
ATOM   2044 C C    B ASN   A 1 101 ? 20.724 1.636   -13.818 0.26 21.45 ?  101 ASN   A C    1 
ATOM   2045 O O    A ASN   A 1 101 ? 20.705 3.147   -14.017 0.74 24.56 ?  101 ASN   A O    1 
ATOM   2046 O O    B ASN   A 1 101 ? 20.751 2.271   -14.879 0.26 21.14 ?  101 ASN   A O    1 
ATOM   2047 C CB   A ASN   A 1 101 ? 18.641 2.719   -11.884 0.74 21.06 ?  101 ASN   A CB   1 
ATOM   2048 C CB   B ASN   A 1 101 ? 18.793 2.310   -12.347 0.26 20.33 ?  101 ASN   A CB   1 
ATOM   2049 C CG   A ASN   A 1 101 ? 17.254 2.303   -11.403 0.74 20.52 ?  101 ASN   A CG   1 
ATOM   2050 C CG   B ASN   A 1 101 ? 17.471 1.905   -11.725 0.26 20.11 ?  101 ASN   A CG   1 
ATOM   2051 O OD1  A ASN   A 1 101 ? 16.448 1.783   -12.179 0.74 20.94 ?  101 ASN   A OD1  1 
ATOM   2052 O OD1  B ASN   A 1 101 ? 16.633 1.270   -12.369 0.26 20.38 ?  101 ASN   A OD1  1 
ATOM   2053 N ND2  A ASN   A 1 101 ? 16.977 2.509   -10.122 0.74 20.57 ?  101 ASN   A ND2  1 
ATOM   2054 N ND2  B ASN   A 1 101 ? 17.281 2.262   -10.463 0.26 20.10 ?  101 ASN   A ND2  1 
ATOM   2055 H H    A ASN   A 1 101 ? 19.214 0.434   -11.268 0.74 23.53 ?  101 ASN   A H    1 
ATOM   2056 H H    B ASN   A 1 101 ? 19.431 0.067   -11.606 0.26 23.62 ?  101 ASN   A H    1 
ATOM   2057 H HA   A ASN   A 1 101 ? 18.674 1.584   -13.568 0.74 25.52 ?  101 ASN   A HA   1 
ATOM   2058 H HA   B ASN   A 1 101 ? 18.784 1.057   -13.959 0.26 24.63 ?  101 ASN   A HA   1 
ATOM   2059 H HB2  A ASN   A 1 101 ? 19.207 2.845   -11.109 0.74 25.27 ?  101 ASN   A HB2  1 
ATOM   2060 H HB2  B ASN   A 1 101 ? 19.408 2.519   -11.627 0.26 24.40 ?  101 ASN   A HB2  1 
ATOM   2061 H HB3  A ASN   A 1 101 ? 18.553 3.560   -12.370 0.74 25.27 ?  101 ASN   A HB3  1 
ATOM   2062 H HB3  B ASN   A 1 101 ? 18.636 3.100   -12.890 0.26 24.40 ?  101 ASN   A HB3  1 
ATOM   2063 H HD21 A ASN   A 1 101 ? 16.207 2.287   -9.810  0.74 24.68 ?  101 ASN   A HD21 1 
ATOM   2064 H HD21 B ASN   A 1 101 ? 16.549 2.052   -10.065 0.26 24.12 ?  101 ASN   A HD21 1 
ATOM   2065 H HD22 A ASN   A 1 101 ? 17.561 2.873   -9.609  0.74 24.68 ?  101 ASN   A HD22 1 
ATOM   2066 H HD22 B ASN   A 1 101 ? 17.889 2.702   -10.045 0.26 24.12 ?  101 ASN   A HD22 1 
ATOM   2067 N N    A LYS   A 1 102 ? 21.678 1.296   -13.157 0.74 25.47 ?  102 LYS   A N    1 
ATOM   2068 N N    B LYS   A 1 102 ? 21.833 1.290   -13.164 0.26 22.96 ?  102 LYS   A N    1 
ATOM   2069 C CA   A LYS   A 1 102 ? 22.965 1.465   -13.824 0.74 27.19 ?  102 LYS   A CA   1 
ATOM   2070 C CA   B LYS   A 1 102 ? 23.158 1.548   -13.714 0.26 24.36 ?  102 LYS   A CA   1 
ATOM   2071 C C    A LYS   A 1 102 ? 23.269 0.350   -14.817 0.74 27.24 ?  102 LYS   A C    1 
ATOM   2072 C C    B LYS   A 1 102 ? 23.588 0.492   -14.724 0.26 24.94 ?  102 LYS   A C    1 
ATOM   2073 O O    A LYS   A 1 102 ? 24.350 0.355   -15.415 0.74 27.86 ?  102 LYS   A O    1 
ATOM   2074 O O    B LYS   A 1 102 ? 24.680 0.610   -15.289 0.26 25.23 ?  102 LYS   A O    1 
ATOM   2075 C CB   A LYS   A 1 102 ? 24.107 1.517   -12.800 0.74 29.29 ?  102 LYS   A CB   1 
ATOM   2076 C CB   B LYS   A 1 102 ? 24.194 1.636   -12.589 0.26 25.22 ?  102 LYS   A CB   1 
ATOM   2077 C CG   A LYS   A 1 102 ? 24.026 2.644   -11.792 0.74 31.02 ?  102 LYS   A CG   1 
ATOM   2078 C CG   B LYS   A 1 102 ? 24.016 2.831   -11.664 0.26 25.98 ?  102 LYS   A CG   1 
ATOM   2079 C CD   A LYS   A 1 102 ? 25.204 2.576   -10.826 0.74 32.57 ?  102 LYS   A CD   1 
ATOM   2080 C CD   B LYS   A 1 102 ? 25.079 2.851   -10.574 0.26 26.60 ?  102 LYS   A CD   1 
ATOM   2081 C CE   A LYS   A 1 102 ? 25.155 3.686   -9.788  0.74 33.79 ?  102 LYS   A CE   1 
ATOM   2082 C CE   B LYS   A 1 102 ? 24.894 4.032   -9.632  0.26 27.06 ?  102 LYS   A CE   1 
ATOM   2083 N NZ   A LYS   A 1 102 ? 26.284 3.586   -8.817  0.74 34.42 ?  102 LYS   A NZ   1 
ATOM   2084 N NZ   B LYS   A 1 102 ? 25.875 4.018   -8.509  0.26 27.26 ?  102 LYS   A NZ   1 
ATOM   2085 H H    A LYS   A 1 102 ? 21.668 0.625   -12.617 0.74 30.56 ?  102 LYS   A H    1 
ATOM   2086 H H    B LYS   A 1 102 ? 21.843 0.895   -12.399 0.26 27.55 ?  102 LYS   A H    1 
ATOM   2087 H HA   A LYS   A 1 102 ? 22.963 2.303   -14.307 0.74 32.63 ?  102 LYS   A HA   1 
ATOM   2088 H HA   B LYS   A 1 102 ? 23.145 2.404   -14.165 0.26 29.23 ?  102 LYS   A HA   1 
ATOM   2089 H HB2  A LYS   A 1 102 ? 24.117 0.683   -12.305 0.74 35.15 ?  102 LYS   A HB2  1 
ATOM   2090 H HB2  B LYS   A 1 102 ? 24.139 0.832   -12.051 0.26 30.27 ?  102 LYS   A HB2  1 
ATOM   2091 H HB3  A LYS   A 1 102 ? 24.946 1.617   -13.280 0.74 35.15 ?  102 LYS   A HB3  1 
ATOM   2092 H HB3  B LYS   A 1 102 ? 25.076 1.702   -12.985 0.26 30.27 ?  102 LYS   A HB3  1 
ATOM   2093 H HG2  A LYS   A 1 102 ? 24.056 3.495   -12.256 0.74 37.23 ?  102 LYS   A HG2  1 
ATOM   2094 H HG2  B LYS   A 1 102 ? 24.094 3.649   -12.180 0.26 31.18 ?  102 LYS   A HG2  1 
ATOM   2095 H HG3  A LYS   A 1 102 ? 23.205 2.562   -11.284 0.74 37.23 ?  102 LYS   A HG3  1 
ATOM   2096 H HG3  B LYS   A 1 102 ? 23.145 2.783   -11.240 0.26 31.18 ?  102 LYS   A HG3  1 
ATOM   2097 H HD2  A LYS   A 1 102 ? 25.185 1.725   -10.360 0.74 39.09 ?  102 LYS   A HD2  1 
ATOM   2098 H HD2  B LYS   A 1 102 ? 25.018 2.035   -10.053 0.26 31.93 ?  102 LYS   A HD2  1 
ATOM   2099 H HD3  A LYS   A 1 102 ? 26.031 2.664   -11.325 0.74 39.09 ?  102 LYS   A HD3  1 
ATOM   2100 H HD3  B LYS   A 1 102 ? 25.955 2.923   -10.983 0.26 31.93 ?  102 LYS   A HD3  1 
ATOM   2101 H HE2  A LYS   A 1 102 ? 25.215 4.544   -10.237 0.74 40.55 ?  102 LYS   A HE2  1 
ATOM   2102 H HE2  B LYS   A 1 102 ? 25.017 4.856   -10.129 0.26 32.47 ?  102 LYS   A HE2  1 
ATOM   2103 H HE3  A LYS   A 1 102 ? 24.322 3.624   -9.294  0.74 40.55 ?  102 LYS   A HE3  1 
ATOM   2104 H HE3  B LYS   A 1 102 ? 24.002 4.000   -9.254  0.26 32.47 ?  102 LYS   A HE3  1 
ATOM   2105 H HZ1  A LYS   A 1 102 ? 26.233 4.245   -8.222  0.74 41.30 ?  102 LYS   A HZ1  1 
ATOM   2106 H HZ1  B LYS   A 1 102 ? 25.740 4.720   -7.979  0.26 32.72 ?  102 LYS   A HZ1  1 
ATOM   2107 H HZ2  A LYS   A 1 102 ? 26.248 2.806   -8.389  0.74 41.30 ?  102 LYS   A HZ2  1 
ATOM   2108 H HZ2  B LYS   A 1 102 ? 25.780 3.273   -8.032  0.26 32.72 ?  102 LYS   A HZ2  1 
ATOM   2109 H HZ3  A LYS   A 1 102 ? 27.061 3.643   -9.247  0.74 41.30 ?  102 LYS   A HZ3  1 
ATOM   2110 H HZ3  B LYS   A 1 102 ? 26.705 4.053   -8.829  0.26 32.72 ?  102 LYS   A HZ3  1 
ATOM   2111 N N    A GLY   A 1 103 ? 22.373 -0.620  -14.987 0.74 27.38 ?  103 GLY   A N    1 
ATOM   2112 N N    B GLY   A 1 103 ? 22.765 -0.529  -14.958 0.26 25.17 ?  103 GLY   A N    1 
ATOM   2113 C CA   A GLY   A 1 103 ? 22.604 -1.704  -15.922 0.74 26.99 ?  103 GLY   A CA   1 
ATOM   2114 C CA   B GLY   A 1 103 ? 23.093 -1.557  -15.925 0.26 25.16 ?  103 GLY   A CA   1 
ATOM   2115 C C    A GLY   A 1 103 ? 23.437 -2.850  -15.393 0.74 26.71 ?  103 GLY   A C    1 
ATOM   2116 C C    B GLY   A 1 103 ? 23.985 -2.656  -15.399 0.26 25.32 ?  103 GLY   A C    1 
ATOM   2117 O O    A GLY   A 1 103 ? 23.937 -3.654  -16.185 0.74 27.53 ?  103 GLY   A O    1 
ATOM   2118 O O    B GLY   A 1 103 ? 24.791 -3.205  -16.157 0.26 25.60 ?  103 GLY   A O    1 
ATOM   2119 H H    A GLY   A 1 103 ? 21.628 -0.675  -14.565 0.74 32.85 ?  103 GLY   A H    1 
ATOM   2120 H H    B GLY   A 1 103 ? 22.011 -0.647  -14.566 0.26 30.21 ?  103 GLY   A H    1 
ATOM   2121 H HA2  A GLY   A 1 103 ? 21.749 -2.067  -16.202 0.74 32.39 ?  103 GLY   A HA2  1 
ATOM   2122 H HA2  B GLY   A 1 103 ? 22.271 -1.958  -16.249 0.26 30.19 ?  103 GLY   A HA2  1 
ATOM   2123 H HA3  A GLY   A 1 103 ? 23.048 -1.350  -16.711 0.74 32.39 ?  103 GLY   A HA3  1 
ATOM   2124 H HA3  B GLY   A 1 103 ? 23.546 -1.151  -16.678 0.26 30.19 ?  103 GLY   A HA3  1 
ATOM   2125 N N    A GLU   A 1 104 ? 23.591 -2.965  -14.079 0.74 24.87 ?  104 GLU   A N    1 
ATOM   2126 N N    B GLU   A 1 104 ? 23.862 -3.003  -14.121 0.26 24.84 ?  104 GLU   A N    1 
ATOM   2127 C CA   A GLU   A 1 104 ? 24.473 -3.969  -13.502 0.74 23.47 ?  104 GLU   A CA   1 
ATOM   2128 C CA   B GLU   A 1 104 ? 24.742 -3.972  -13.485 0.26 24.49 ?  104 GLU   A CA   1 
ATOM   2129 C C    A GLU   A 1 104 ? 23.778 -5.326  -13.403 0.74 23.29 ?  104 GLU   A C    1 
ATOM   2130 C C    B GLU   A 1 104 ? 24.048 -5.324  -13.353 0.26 24.85 ?  104 GLU   A C    1 
ATOM   2131 O O    A GLU   A 1 104 ? 22.553 -5.420  -13.279 0.74 23.90 ?  104 GLU   A O    1 
ATOM   2132 O O    B GLU   A 1 104 ? 22.841 -5.398  -13.102 0.26 24.84 ?  104 GLU   A O    1 
ATOM   2133 C CB   A GLU   A 1 104 ? 24.999 -3.487  -12.145 0.74 21.96 ?  104 GLU   A CB   1 
ATOM   2134 C CB   B GLU   A 1 104 ? 25.203 -3.445  -12.125 0.26 23.88 ?  104 GLU   A CB   1 
ATOM   2135 C CG   A GLU   A 1 104 ? 25.959 -2.300  -12.307 0.74 21.25 ?  104 GLU   A CG   1 
ATOM   2136 C CG   B GLU   A 1 104 ? 25.954 -2.117  -12.247 0.26 23.54 ?  104 GLU   A CG   1 
ATOM   2137 C CD   A GLU   A 1 104 ? 26.309 -1.548  -11.029 0.74 20.04 ?  104 GLU   A CD   1 
ATOM   2138 C CD   B GLU   A 1 104 ? 26.254 -1.463  -10.909 0.26 23.19 ?  104 GLU   A CD   1 
ATOM   2139 O OE1  A GLU   A 1 104 ? 25.718 -1.814  -9.959  0.74 18.80 ?  104 GLU   A OE1  1 
ATOM   2140 O OE1  B GLU   A 1 104 ? 25.751 -1.948  -9.875  0.26 22.84 ?  104 GLU   A OE1  1 
ATOM   2141 O OE2  A GLU   A 1 104 ? 27.193 -0.661  -11.121 0.74 20.80 -1 104 GLU   A OE2  1 
ATOM   2142 O OE2  B GLU   A 1 104 ? 26.994 -0.456  -10.896 0.26 23.43 -1 104 GLU   A OE2  1 
ATOM   2143 H H    A GLU   A 1 104 ? 23.190 -2.473  -13.504 0.74 29.85 ?  104 GLU   A H    1 
ATOM   2144 H H    B GLU   A 1 104 ? 23.268 -2.679  -13.589 0.26 29.80 ?  104 GLU   A H    1 
ATOM   2145 H HA   A GLU   A 1 104 ? 25.234 -4.078  -14.089 0.74 28.17 ?  104 GLU   A HA   1 
ATOM   2146 H HA   B GLU   A 1 104 ? 25.528 -4.096  -14.036 0.26 29.39 ?  104 GLU   A HA   1 
ATOM   2147 H HB2  A GLU   A 1 104 ? 24.251 -3.207  -11.597 0.74 26.35 ?  104 GLU   A HB2  1 
ATOM   2148 H HB2  B GLU   A 1 104 ? 24.430 -3.302  -11.557 0.26 28.65 ?  104 GLU   A HB2  1 
ATOM   2149 H HB3  A GLU   A 1 104 ? 25.478 -4.214  -11.718 0.74 26.35 ?  104 GLU   A HB3  1 
ATOM   2150 H HB3  B GLU   A 1 104 ? 25.801 -4.091  -11.716 0.26 28.65 ?  104 GLU   A HB3  1 
ATOM   2151 H HG2  A GLU   A 1 104 ? 26.788 -2.627  -12.685 0.74 25.50 ?  104 GLU   A HG2  1 
ATOM   2152 H HG2  B GLU   A 1 104 ? 26.798 -2.274  -12.702 0.26 28.25 ?  104 GLU   A HG2  1 
ATOM   2153 H HG3  A GLU   A 1 104 ? 25.553 -1.659  -12.910 0.74 25.50 ?  104 GLU   A HG3  1 
ATOM   2154 H HG3  B GLU   A 1 104 ? 25.416 -1.497  -12.768 0.26 28.25 ?  104 GLU   A HG3  1 
ATOM   2155 N N    A ASP   A 1 105 ? 24.587 -6.384  -13.455 0.74 23.85 ?  105 ASP   A N    1 
ATOM   2156 N N    B ASP   A 1 105 ? 24.826 -6.391  -13.529 0.26 25.68 ?  105 ASP   A N    1 
ATOM   2157 C CA   A ASP   A 1 105 ? 24.088 -7.748  -13.599 0.74 24.91 ?  105 ASP   A CA   1 
ATOM   2158 C CA   B ASP   A 1 105 ? 24.283 -7.741  -13.623 0.26 26.53 ?  105 ASP   A CA   1 
ATOM   2159 C C    A ASP   A 1 105 ? 23.402 -8.209  -12.316 0.74 22.53 ?  105 ASP   A C    1 
ATOM   2160 C C    B ASP   A 1 105 ? 23.553 -8.118  -12.340 0.26 25.69 ?  105 ASP   A C    1 
ATOM   2161 O O    A ASP   A 1 105 ? 24.040 -8.313  -11.266 0.74 19.91 ?  105 ASP   A O    1 
ATOM   2162 O O    B ASP   A 1 105 ? 24.145 -8.129  -11.257 0.26 25.22 ?  105 ASP   A O    1 
ATOM   2163 C CB   A ASP   A 1 105 ? 25.262 -8.668  -13.934 0.74 28.46 ?  105 ASP   A CB   1 
ATOM   2164 C CB   B ASP   A 1 105 ? 25.432 -8.715  -13.889 0.26 28.17 ?  105 ASP   A CB   1 
ATOM   2165 C CG   A ASP   A 1 105 ? 24.840 -10.102 -14.157 0.74 31.48 ?  105 ASP   A CG   1 
ATOM   2166 C CG   B ASP   A 1 105 ? 24.950 -10.106 -14.250 0.26 29.61 ?  105 ASP   A CG   1 
ATOM   2167 O OD1  A ASP   A 1 105 ? 23.621 -10.359 -14.236 0.74 32.06 ?  105 ASP   A OD1  1 
ATOM   2168 O OD1  B ASP   A 1 105 ? 23.721 -10.319 -14.300 0.26 30.04 ?  105 ASP   A OD1  1 
ATOM   2169 O OD2  A ASP   A 1 105 ? 25.735 -10.971 -14.253 0.74 33.25 -1 105 ASP   A OD2  1 
ATOM   2170 O OD2  B ASP   A 1 105 ? 25.805 -10.987 -14.487 0.26 30.26 -1 105 ASP   A OD2  1 
ATOM   2171 H H    A ASP   A 1 105 ? 25.446 -6.336  -13.409 0.74 28.62 ?  105 ASP   A H    1 
ATOM   2172 H H    B ASP   A 1 105 ? 25.681 -6.357  -13.594 0.26 30.82 ?  105 ASP   A H    1 
ATOM   2173 H HA   A ASP   A 1 105 ? 23.448 -7.792  -14.324 0.74 29.89 ?  105 ASP   A HA   1 
ATOM   2174 H HA   B ASP   A 1 105 ? 23.657 -7.793  -14.362 0.26 31.84 ?  105 ASP   A HA   1 
ATOM   2175 H HB2  A ASP   A 1 105 ? 25.692 -8.352  -14.746 0.74 34.15 ?  105 ASP   A HB2  1 
ATOM   2176 H HB2  B ASP   A 1 105 ? 25.967 -8.378  -14.627 0.26 33.80 ?  105 ASP   A HB2  1 
ATOM   2177 H HB3  A ASP   A 1 105 ? 25.896 -8.658  -13.200 0.74 34.15 ?  105 ASP   A HB3  1 
ATOM   2178 H HB3  B ASP   A 1 105 ? 25.978 -8.788  -13.092 0.26 33.80 ?  105 ASP   A HB3  1 
ATOM   2179 N N    A ILE   A 1 106 ? 22.106 -8.520  -12.409 0.74 22.50 ?  106 ILE   A N    1 
ATOM   2180 N N    B ILE   A 1 106 ? 22.261 -8.437  -12.467 0.26 25.33 ?  106 ILE   A N    1 
ATOM   2181 C CA   A ILE   A 1 106 ? 21.346 -8.940  -11.238 0.74 22.14 ?  106 ILE   A CA   1 
ATOM   2182 C CA   B ILE   A 1 106 ? 21.464 -8.803  -11.302 0.26 24.93 ?  106 ILE   A CA   1 
ATOM   2183 C C    A ILE   A 1 106 ? 21.885 -10.233 -10.647 0.74 21.14 ?  106 ILE   A C    1 
ATOM   2184 C C    B ILE   A 1 106 ? 21.913 -10.129 -10.701 0.26 24.29 ?  106 ILE   A C    1 
ATOM   2185 O O    A ILE   A 1 106 ? 21.673 -10.499 -9.459  0.74 20.29 ?  106 ILE   A O    1 
ATOM   2186 O O    B ILE   A 1 106 ? 21.642 -10.392 -9.524  0.26 23.93 ?  106 ILE   A O    1 
ATOM   2187 C CB   A ILE   A 1 106 ? 19.840 -9.043  -11.574 0.74 23.39 ?  106 ILE   A CB   1 
ATOM   2188 C CB   B ILE   A 1 106 ? 19.958 -8.799  -11.643 0.26 25.36 ?  106 ILE   A CB   1 
ATOM   2189 C CG1  A ILE   A 1 106 ? 19.004 -9.161  -10.296 0.74 23.64 ?  106 ILE   A CG1  1 
ATOM   2190 C CG1  B ILE   A 1 106 ? 19.108 -8.899  -10.372 0.26 25.43 ?  106 ILE   A CG1  1 
ATOM   2191 C CG2  A ILE   A 1 106 ? 19.569 -10.234 -12.482 0.74 24.11 ?  106 ILE   A CG2  1 
ATOM   2192 C CG2  B ILE   A 1 106 ? 19.619 -9.944  -12.581 0.26 25.59 ?  106 ILE   A CG2  1 
ATOM   2193 C CD1  A ILE   A 1 106 ? 19.099 -7.956  -9.388  0.74 23.88 ?  106 ILE   A CD1  1 
ATOM   2194 C CD1  B ILE   A 1 106 ? 19.416 -7.835  -9.339  0.26 25.44 ?  106 ILE   A CD1  1 
ATOM   2195 H H    A ILE   A 1 106 ? 21.657 -8.491  -13.135 0.74 27.00 ?  106 ILE   A H    1 
ATOM   2196 H H    B ILE   A 1 106 ? 21.828 -8.437  -13.208 0.26 30.40 ?  106 ILE   A H    1 
ATOM   2197 H HA   A ILE   A 1 106 ? 21.448 -8.267  -10.559 0.74 26.57 ?  106 ILE   A HA   1 
ATOM   2198 H HA   B ILE   A 1 106 ? 21.612 -8.129  -10.629 0.26 29.92 ?  106 ILE   A HA   1 
ATOM   2199 H HB   A ILE   A 1 106 ? 19.576 -8.236  -12.042 0.74 28.07 ?  106 ILE   A HB   1 
ATOM   2200 H HB   B ILE   A 1 106 ? 19.745 -7.965  -12.088 0.26 30.43 ?  106 ILE   A HB   1 
ATOM   2201 H HG12 A ILE   A 1 106 ? 18.072 -9.270  -10.544 0.74 28.37 ?  106 ILE   A HG12 1 
ATOM   2202 H HG12 B ILE   A 1 106 ? 18.171 -8.809  -10.615 0.26 30.51 ?  106 ILE   A HG12 1 
ATOM   2203 H HG13 A ILE   A 1 106 ? 19.301 -9.936  -9.795  0.74 28.37 ?  106 ILE   A HG13 1 
ATOM   2204 H HG13 B ILE   A 1 106 ? 19.256 -9.764  -9.961  0.26 30.51 ?  106 ILE   A HG13 1 
ATOM   2205 H HG21 A ILE   A 1 106 ? 18.671 -10.156 -12.840 0.74 28.94 ?  106 ILE   A HG21 1 
ATOM   2206 H HG21 B ILE   A 1 106 ? 18.716 -9.820  -12.914 0.26 30.71 ?  106 ILE   A HG21 1 
ATOM   2207 H HG22 A ILE   A 1 106 ? 20.216 -10.230 -13.204 0.74 28.94 ?  106 ILE   A HG22 1 
ATOM   2208 H HG22 B ILE   A 1 106 ? 20.247 -9.941  -13.318 0.26 30.71 ?  106 ILE   A HG22 1 
ATOM   2209 H HG23 A ILE   A 1 106 ? 19.651 -11.050 -11.966 0.74 28.94 ?  106 ILE   A HG23 1 
ATOM   2210 H HG23 B ILE   A 1 106 ? 19.680 -10.781 -12.095 0.26 30.71 ?  106 ILE   A HG23 1 
ATOM   2211 H HD11 A ILE   A 1 106 ? 18.377 -7.992  -8.743  0.74 28.65 ?  106 ILE   A HD11 1 
ATOM   2212 H HD11 B ILE   A 1 106 ? 18.678 -7.782  -8.714  0.26 30.53 ?  106 ILE   A HD11 1 
ATOM   2213 H HD12 A ILE   A 1 106 ? 19.954 -7.971  -8.929  0.74 28.65 ?  106 ILE   A HD12 1 
ATOM   2214 H HD12 B ILE   A 1 106 ? 20.230 -8.078  -8.870  0.26 30.53 ?  106 ILE   A HD12 1 
ATOM   2215 H HD13 A ILE   A 1 106 ? 19.024 -7.151  -9.924  0.74 28.65 ?  106 ILE   A HD13 1 
ATOM   2216 H HD13 B ILE   A 1 106 ? 19.532 -6.984  -9.789  0.26 30.53 ?  106 ILE   A HD13 1 
ATOM   2217 N N    A GLN   A 1 107 ? 22.579 -11.049 -11.451 0.74 21.92 ?  107 GLN   A N    1 
ATOM   2218 N N    B GLN   A 1 107 ? 22.602 -10.973 -11.475 0.26 24.19 ?  107 GLN   A N    1 
ATOM   2219 C CA   A GLN   A 1 107 ? 23.201 -12.262 -10.928 0.74 24.32 ?  107 GLN   A CA   1 
ATOM   2220 C CA   B GLN   A 1 107 ? 23.148 -12.208 -10.925 0.26 24.34 ?  107 GLN   A CA   1 
ATOM   2221 C C    A GLN   A 1 107 ? 24.174 -11.948 -9.799  0.74 21.90 ?  107 GLN   A C    1 
ATOM   2222 C C    B GLN   A 1 107 ? 24.156 -11.938 -9.818  0.26 21.51 ?  107 GLN   A C    1 
ATOM   2223 O O    A GLN   A 1 107 ? 24.413 -12.795 -8.930  0.74 23.42 ?  107 GLN   A O    1 
ATOM   2224 O O    B GLN   A 1 107 ? 24.409 -12.824 -8.994  0.26 22.24 ?  107 GLN   A O    1 
ATOM   2225 C CB   A GLN   A 1 107 ? 23.914 -13.014 -12.058 0.74 28.94 ?  107 GLN   A CB   1 
ATOM   2226 C CB   B GLN   A 1 107 ? 23.794 -13.041 -12.036 0.26 27.23 ?  107 GLN   A CB   1 
ATOM   2227 C CG   A GLN   A 1 107 ? 23.035 -13.289 -13.274 0.74 33.65 ?  107 GLN   A CG   1 
ATOM   2228 C CG   B GLN   A 1 107 ? 22.863 -13.338 -13.202 0.26 30.05 ?  107 GLN   A CG   1 
ATOM   2229 C CD   A GLN   A 1 107 ? 21.788 -14.077 -12.928 0.74 37.69 ?  107 GLN   A CD   1 
ATOM   2230 C CD   B GLN   A 1 107 ? 21.553 -13.959 -12.759 0.26 32.41 ?  107 GLN   A CD   1 
ATOM   2231 O OE1  A GLN   A 1 107 ? 21.858 -15.115 -12.270 0.74 39.21 ?  107 GLN   A OE1  1 
ATOM   2232 O OE1  B GLN   A 1 107 ? 21.529 -14.848 -11.907 0.26 33.27 ?  107 GLN   A OE1  1 
ATOM   2233 N NE2  A GLN   A 1 107 ? 20.635 -13.580 -13.363 0.74 39.11 ?  107 GLN   A NE2  1 
ATOM   2234 N NE2  B GLN   A 1 107 ? 20.452 -13.484 -13.328 0.26 33.26 ?  107 GLN   A NE2  1 
ATOM   2235 H H    A GLN   A 1 107 ? 22.699 -10.925 -12.292 0.74 26.31 ?  107 GLN   A H    1 
ATOM   2236 H H    B GLN   A 1 107 ? 22.763 -10.853 -12.310 0.26 29.03 ?  107 GLN   A H    1 
ATOM   2237 H HA   A GLN   A 1 107 ? 22.521 -12.848 -10.570 0.74 29.18 ?  107 GLN   A HA   1 
ATOM   2238 H HA   B GLN   A 1 107 ? 22.431 -12.730 -10.541 0.26 29.20 ?  107 GLN   A HA   1 
ATOM   2239 H HB2  A GLN   A 1 107 ? 24.673 -12.490 -12.360 0.74 34.73 ?  107 GLN   A HB2  1 
ATOM   2240 H HB2  B GLN   A 1 107 ? 24.561 -12.561 -12.386 0.26 32.68 ?  107 GLN   A HB2  1 
ATOM   2241 H HB3  A GLN   A 1 107 ? 24.223 -13.872 -11.724 0.74 34.73 ?  107 GLN   A HB3  1 
ATOM   2242 H HB3  B GLN   A 1 107 ? 24.081 -13.892 -11.666 0.26 32.68 ?  107 GLN   A HB3  1 
ATOM   2243 H HG2  A GLN   A 1 107 ? 22.757 -12.448 -13.667 0.74 40.39 ?  107 GLN   A HG2  1 
ATOM   2244 H HG2  B GLN   A 1 107 ? 22.662 -12.510 -13.665 0.26 36.06 ?  107 GLN   A HG2  1 
ATOM   2245 H HG3  A GLN   A 1 107 ? 23.543 -13.803 -13.922 0.74 40.39 ?  107 GLN   A HG3  1 
ATOM   2246 H HG3  B GLN   A 1 107 ? 23.301 -13.959 -13.806 0.26 36.06 ?  107 GLN   A HG3  1 
ATOM   2247 H HE21 A GLN   A 1 107 ? 20.625 -12.851 -13.819 0.74 46.94 ?  107 GLN   A HE21 1 
ATOM   2248 H HE21 B GLN   A 1 107 ? 20.509 -12.861 -13.917 0.26 39.91 ?  107 GLN   A HE21 1 
ATOM   2249 H HE22 A GLN   A 1 107 ? 19.899 -13.990 -13.191 0.74 46.94 ?  107 GLN   A HE22 1 
ATOM   2250 H HE22 B GLN   A 1 107 ? 19.684 -13.802 -13.109 0.26 39.91 ?  107 GLN   A HE22 1 
ATOM   2251 N N    . LEU   A 1 108 ? 24.727 -10.733 -9.775  1.00 18.20 ?  108 LEU   A N    1 
ATOM   2252 C CA   . LEU   A 1 108 ? 25.656 -10.362 -8.720  1.00 14.75 ?  108 LEU   A CA   1 
ATOM   2253 C C    . LEU   A 1 108 ? 24.967 -10.206 -7.375  1.00 12.96 ?  108 LEU   A C    1 
ATOM   2254 O O    . LEU   A 1 108 ? 25.659 -10.062 -6.363  1.00 13.25 ?  108 LEU   A O    1 
ATOM   2255 C CB   . LEU   A 1 108 ? 26.400 -9.074  -9.096  1.00 14.43 ?  108 LEU   A CB   1 
ATOM   2256 C CG   . LEU   A 1 108 ? 27.402 -9.262  -10.236 1.00 16.02 ?  108 LEU   A CG   1 
ATOM   2257 C CD1  . LEU   A 1 108 ? 27.897 -7.926  -10.764 1.00 16.74 ?  108 LEU   A CD1  1 
ATOM   2258 C CD2  . LEU   A 1 108 ? 28.582 -10.113 -9.781  1.00 17.80 ?  108 LEU   A CD2  1 
ATOM   2259 H H    A LEU   A 1 108 ? 24.575 -10.113 -10.345 0.74 21.84 ?  108 LEU   A H    1 
ATOM   2260 H H    B LEU   A 1 108 ? 24.592 -10.114 -10.350 0.26 21.84 ?  108 LEU   A H    1 
ATOM   2261 H HA   . LEU   A 1 108 ? 26.315 -11.067 -8.620  1.00 17.70 ?  108 LEU   A HA   1 
ATOM   2262 H HB2  . LEU   A 1 108 ? 25.749 -8.410  -9.378  1.00 17.32 ?  108 LEU   A HB2  1 
ATOM   2263 H HB3  . LEU   A 1 108 ? 26.883 -8.751  -8.321  1.00 17.32 ?  108 LEU   A HB3  1 
ATOM   2264 H HG   . LEU   A 1 108 ? 26.965 -9.731  -10.964 1.00 19.23 ?  108 LEU   A HG   1 
ATOM   2265 H HD11 . LEU   A 1 108 ? 28.495 -8.086  -11.512 1.00 20.09 ?  108 LEU   A HD11 1 
ATOM   2266 H HD12 . LEU   A 1 108 ? 27.136 -7.401  -11.054 1.00 20.09 ?  108 LEU   A HD12 1 
ATOM   2267 H HD13 . LEU   A 1 108 ? 28.371 -7.463  -10.056 1.00 20.09 ?  108 LEU   A HD13 1 
ATOM   2268 H HD21 . LEU   A 1 108 ? 29.278 -10.068 -10.451 1.00 21.36 ?  108 LEU   A HD21 1 
ATOM   2269 H HD22 . LEU   A 1 108 ? 28.910 -9.767  -8.935  1.00 21.36 ?  108 LEU   A HD22 1 
ATOM   2270 H HD23 . LEU   A 1 108 ? 28.287 -11.031 -9.668  1.00 21.36 ?  108 LEU   A HD23 1 
ATOM   2271 N N    . LEU   A 1 109 ? 23.632 -10.250 -7.331  1.00 12.39 ?  109 LEU   A N    1 
ATOM   2272 C CA   . LEU   A 1 109 ? 22.944 -10.122 -6.057  1.00 11.71 ?  109 LEU   A CA   1 
ATOM   2273 C C    . LEU   A 1 109 ? 23.291 -11.276 -5.121  1.00 11.20 ?  109 LEU   A C    1 
ATOM   2274 O O    . LEU   A 1 109 ? 23.423 -11.078 -3.910  1.00 11.45 ?  109 LEU   A O    1 
ATOM   2275 C CB   . LEU   A 1 109 ? 21.439 -10.036 -6.302  1.00 12.92 ?  109 LEU   A CB   1 
ATOM   2276 C CG   . LEU   A 1 109 ? 20.560 -9.744  -5.088  1.00 13.05 ?  109 LEU   A CG   1 
ATOM   2277 C CD1  . LEU   A 1 109 ? 21.020 -8.477  -4.380  1.00 13.21 ?  109 LEU   A CD1  1 
ATOM   2278 C CD2  . LEU   A 1 109 ? 19.102 -9.620  -5.510  1.00 14.16 ?  109 LEU   A CD2  1 
ATOM   2279 H H    . LEU   A 1 109 ? 23.116 -10.355 -8.009  1.00 14.87 ?  109 LEU   A H    1 
ATOM   2280 H HA   . LEU   A 1 109 ? 23.225 -9.300  -5.628  1.00 14.05 ?  109 LEU   A HA   1 
ATOM   2281 H HB2  . LEU   A 1 109 ? 21.277 -9.328  -6.947  1.00 15.50 ?  109 LEU   A HB2  1 
ATOM   2282 H HB3  . LEU   A 1 109 ? 21.140 -10.880 -6.672  1.00 15.50 ?  109 LEU   A HB3  1 
ATOM   2283 H HG   . LEU   A 1 109 ? 20.631 -10.479 -4.461  1.00 15.66 ?  109 LEU   A HG   1 
ATOM   2284 H HD11 . LEU   A 1 109 ? 20.342 -8.200  -3.748  1.00 15.85 ?  109 LEU   A HD11 1 
ATOM   2285 H HD12 . LEU   A 1 109 ? 21.854 -8.657  -3.915  1.00 15.85 ?  109 LEU   A HD12 1 
ATOM   2286 H HD13 . LEU   A 1 109 ? 21.159 -7.778  -5.042  1.00 15.85 ?  109 LEU   A HD13 1 
ATOM   2287 H HD21 . LEU   A 1 109 ? 18.579 -9.312  -4.752  1.00 17.00 ?  109 LEU   A HD21 1 
ATOM   2288 H HD22 . LEU   A 1 109 ? 19.034 -8.982  -6.237  1.00 17.00 ?  109 LEU   A HD22 1 
ATOM   2289 H HD23 . LEU   A 1 109 ? 18.782 -10.489 -5.801  1.00 17.00 ?  109 LEU   A HD23 1 
ATOM   2290 N N    . LYS   A 1 110 ? 23.429 -12.493 -5.656  1.00 11.03 ?  110 LYS   A N    1 
ATOM   2291 C CA   . LYS   A 1 110 ? 23.808 -13.616 -4.800  1.00 10.75 ?  110 LYS   A CA   1 
ATOM   2292 C C    . LYS   A 1 110 ? 25.190 -13.394 -4.193  1.00 10.48 ?  110 LYS   A C    1 
ATOM   2293 O O    . LYS   A 1 110 ? 25.389 -13.596 -2.993  1.00 10.65 ?  110 LYS   A O    1 
ATOM   2294 C CB   . LYS   A 1 110 ? 23.724 -14.942 -5.564  1.00 11.54 ?  110 LYS   A CB   1 
ATOM   2295 C CG   . LYS   A 1 110 ? 23.943 -16.157 -4.664  1.00 11.90 ?  110 LYS   A CG   1 
ATOM   2296 C CD   . LYS   A 1 110 ? 23.686 -17.477 -5.372  1.00 12.41 ?  110 LYS   A CD   1 
ATOM   2297 C CE   . LYS   A 1 110 ? 23.791 -18.655 -4.410  1.00 13.52 ?  110 LYS   A CE   1 
ATOM   2298 N NZ   . LYS   A 1 110 ? 22.616 -18.783 -3.510  1.00 13.68 ?  110 LYS   A NZ   1 
ATOM   2299 H H    . LYS   A 1 110 ? 23.308 -12.691 -6.484  1.00 13.24 ?  110 LYS   A H    1 
ATOM   2300 H HA   . LYS   A 1 110 ? 23.172 -13.665 -4.066  1.00 12.90 ?  110 LYS   A HA   1 
ATOM   2301 H HB2  . LYS   A 1 110 ? 22.845 -15.024 -5.963  1.00 13.85 ?  110 LYS   A HB2  1 
ATOM   2302 H HB3  . LYS   A 1 110 ? 24.406 -14.953 -6.250  1.00 13.85 ?  110 LYS   A HB3  1 
ATOM   2303 H HG2  . LYS   A 1 110 ? 24.864 -16.160 -4.350  1.00 14.28 ?  110 LYS   A HG2  1 
ATOM   2304 H HG3  . LYS   A 1 110 ? 23.341 -16.104 -3.903  1.00 14.28 ?  110 LYS   A HG3  1 
ATOM   2305 H HD2  . LYS   A 1 110 ? 22.795 -17.473 -5.746  1.00 14.90 ?  110 LYS   A HD2  1 
ATOM   2306 H HD3  . LYS   A 1 110 ? 24.349 -17.599 -6.070  1.00 14.90 ?  110 LYS   A HD3  1 
ATOM   2307 H HE2  . LYS   A 1 110 ? 23.871 -19.473 -4.919  1.00 16.23 ?  110 LYS   A HE2  1 
ATOM   2308 H HE3  . LYS   A 1 110 ? 24.580 -18.535 -3.851  1.00 16.23 ?  110 LYS   A HE3  1 
ATOM   2309 H HZ1  . LYS   A 1 110 ? 22.721 -19.479 -2.967  1.00 16.42 ?  110 LYS   A HZ1  1 
ATOM   2310 H HZ2  . LYS   A 1 110 ? 22.524 -18.045 -3.019  1.00 16.42 ?  110 LYS   A HZ2  1 
ATOM   2311 H HZ3  . LYS   A 1 110 ? 21.877 -18.901 -3.993  1.00 16.42 ?  110 LYS   A HZ3  1 
ATOM   2312 N N    . SER   A 1 111 ? 26.154 -12.956 -5.010  1.00 10.65 ?  111 SER   A N    1 
ATOM   2313 C CA   . SER   A 1 111 ? 27.487 -12.656 -4.494  1.00 10.91 ?  111 SER   A CA   1 
ATOM   2314 C C    . SER   A 1 111 ? 27.421 -11.610 -3.386  1.00 10.37 ?  111 SER   A C    1 
ATOM   2315 O O    . SER   A 1 111 ? 28.117 -11.715 -2.371  1.00 11.00 ?  111 SER   A O    1 
ATOM   2316 C CB   . SER   A 1 111 ? 28.383 -12.171 -5.634  1.00 12.35 ?  111 SER   A CB   1 
ATOM   2317 O OG   . SER   A 1 111 ? 28.495 -13.170 -6.635  1.00 14.38 ?  111 SER   A OG   1 
ATOM   2318 H H    . SER   A 1 111 ? 26.057 -12.825 -5.853  1.00 12.78 ?  111 SER   A H    1 
ATOM   2319 H HA   . SER   A 1 111 ? 27.875 -13.464 -4.124  1.00 13.09 ?  111 SER   A HA   1 
ATOM   2320 H HB2  . SER   A 1 111 ? 27.990 -11.378 -6.028  1.00 14.82 ?  111 SER   A HB2  1 
ATOM   2321 H HB3  . SER   A 1 111 ? 29.261 -11.968 -5.279  1.00 14.82 ?  111 SER   A HB3  1 
ATOM   2322 H HG   . SER   A 1 111 ? 29.003 -12.894 -7.256  1.00 17.26 ?  111 SER   A HG   1 
ATOM   2323 N N    . ALA   A 1 112 ? 26.579 -10.592 -3.566  1.00 10.52 ?  112 ALA   A N    1 
ATOM   2324 C CA   . ALA   A 1 112 ? 26.433 -9.555  -2.546  1.00 10.50 ?  112 ALA   A CA   1 
ATOM   2325 C C    . ALA   A 1 112 ? 25.950 -10.152 -1.226  1.00 10.32 ?  112 ALA   A C    1 
ATOM   2326 O O    . ALA   A 1 112 ? 26.501 -9.866  -0.157  1.00 10.45 ?  112 ALA   A O    1 
ATOM   2327 C CB   . ALA   A 1 112 ? 25.477 -8.466  -3.039  1.00 10.78 ?  112 ALA   A CB   1 
ATOM   2328 H H    . ALA   A 1 112 ? 26.090 -10.472 -4.262  1.00 12.63 ?  112 ALA   A H    1 
ATOM   2329 H HA   . ALA   A 1 112 ? 27.295 -9.135  -2.385  1.00 12.60 ?  112 ALA   A HA   1 
ATOM   2330 H HB1  . ALA   A 1 112 ? 25.403 -7.769  -2.358  1.00 12.93 ?  112 ALA   A HB1  1 
ATOM   2331 H HB2  . ALA   A 1 112 ? 25.825 -8.078  -3.858  1.00 12.93 ?  112 ALA   A HB2  1 
ATOM   2332 H HB3  . ALA   A 1 112 ? 24.604 -8.853  -3.201  1.00 12.93 ?  112 ALA   A HB3  1 
ATOM   2333 N N    . TYR   A 1 113 ? 24.914 -10.993 -1.278  1.00 10.37 ?  113 TYR   A N    1 
ATOM   2334 C CA   . TYR   A 1 113 ? 24.399 -11.600 -0.052  1.00 10.13 ?  113 TYR   A CA   1 
ATOM   2335 C C    . TYR   A 1 113 ? 25.397 -12.561 0.593   1.00 9.64  ?  113 TYR   A C    1 
ATOM   2336 O O    . TYR   A 1 113 ? 25.360 -12.744 1.813   1.00 10.36 ?  113 TYR   A O    1 
ATOM   2337 C CB   . TYR   A 1 113 ? 23.074 -12.317 -0.324  1.00 10.89 ?  113 TYR   A CB   1 
ATOM   2338 C CG   . TYR   A 1 113 ? 21.861 -11.417 -0.225  1.00 10.96 ?  113 TYR   A CG   1 
ATOM   2339 C CD1  . TYR   A 1 113 ? 21.507 -10.833 0.984   1.00 11.50 ?  113 TYR   A CD1  1 
ATOM   2340 C CD2  . TYR   A 1 113 ? 21.057 -11.167 -1.332  1.00 11.41 ?  113 TYR   A CD2  1 
ATOM   2341 C CE1  . TYR   A 1 113 ? 20.391 -10.026 1.092   1.00 12.10 ?  113 TYR   A CE1  1 
ATOM   2342 C CE2  . TYR   A 1 113 ? 19.918 -10.355 -1.232  1.00 12.01 ?  113 TYR   A CE2  1 
ATOM   2343 C CZ   . TYR   A 1 113 ? 19.596 -9.790  -0.017  1.00 12.03 ?  113 TYR   A CZ   1 
ATOM   2344 O OH   . TYR   A 1 113 ? 18.479 -8.988  0.121   1.00 13.16 ?  113 TYR   A OH   1 
ATOM   2345 H H    . TYR   A 1 113 ? 24.499 -11.224 -1.997  1.00 12.44 ?  113 TYR   A H    1 
ATOM   2346 H HA   . TYR   A 1 113 ? 24.225 -10.895 0.589   1.00 12.16 ?  113 TYR   A HA   1 
ATOM   2347 H HB2  . TYR   A 1 113 ? 23.089 -12.681 -1.219  1.00 13.06 ?  113 TYR   A HB2  1 
ATOM   2348 H HB3  . TYR   A 1 113 ? 22.962 -13.027 0.324   1.00 13.06 ?  113 TYR   A HB3  1 
ATOM   2349 H HD1  . TYR   A 1 113 ? 22.032 -10.992 1.735   1.00 13.80 ?  113 TYR   A HD1  1 
ATOM   2350 H HD2  . TYR   A 1 113 ? 21.267 -11.556 -2.148  1.00 13.70 ?  113 TYR   A HD2  1 
ATOM   2351 H HE1  . TYR   A 1 113 ? 20.174 -9.644  1.912   1.00 14.52 ?  113 TYR   A HE1  1 
ATOM   2352 H HE2  . TYR   A 1 113 ? 19.383 -10.193 -1.978  1.00 14.41 ?  113 TYR   A HE2  1 
ATOM   2353 H HH   . TYR   A 1 113 ? 18.016 -9.027  -0.586  1.00 15.79 ?  113 TYR   A HH   1 
ATOM   2354 N N    . GLU   A 1 114 ? 26.298 -13.175 -0.187  1.00 9.88  ?  114 GLU   A N    1 
ATOM   2355 C CA   . GLU   A 1 114 ? 27.288 -14.076 0.407   1.00 10.07 ?  114 GLU   A CA   1 
ATOM   2356 C C    . GLU   A 1 114 ? 28.135 -13.372 1.463   1.00 10.11 ?  114 GLU   A C    1 
ATOM   2357 O O    . GLU   A 1 114 ? 28.607 -14.009 2.412   1.00 10.49 ?  114 GLU   A O    1 
ATOM   2358 C CB   . GLU   A 1 114 ? 28.157 -14.716 -0.684  1.00 10.20 ?  114 GLU   A CB   1 
ATOM   2359 C CG   . GLU   A 1 114 ? 27.396 -15.771 -1.467  1.00 10.76 ?  114 GLU   A CG   1 
ATOM   2360 C CD   . GLU   A 1 114 ? 28.104 -16.307 -2.704  1.00 11.26 ?  114 GLU   A CD   1 
ATOM   2361 O OE1  . GLU   A 1 114 ? 29.054 -15.676 -3.208  1.00 11.45 ?  114 GLU   A OE1  1 
ATOM   2362 O OE2  . GLU   A 1 114 ? 27.653 -17.370 -3.189  1.00 12.25 -1 114 GLU   A OE2  1 
ATOM   2363 H H    . GLU   A 1 114 ? 26.349 -13.085 -1.046  1.00 11.85 ?  114 GLU   A H    1 
ATOM   2364 H HA   . GLU   A 1 114 ? 26.814 -14.791 0.846   1.00 12.09 ?  114 GLU   A HA   1 
ATOM   2365 H HB2  . GLU   A 1 114 ? 28.453 -14.034 -1.310  1.00 12.24 ?  114 GLU   A HB2  1 
ATOM   2366 H HB3  . GLU   A 1 114 ? 28.925 -15.145 -0.274  1.00 12.24 ?  114 GLU   A HB3  1 
ATOM   2367 H HG2  . GLU   A 1 114 ? 27.223 -16.526 -0.885  1.00 12.92 ?  114 GLU   A HG2  1 
ATOM   2368 H HG3  . GLU   A 1 114 ? 26.550 -15.390 -1.759  1.00 12.92 ?  114 GLU   A HG3  1 
ATOM   2369 N N    . ASN   A 1 115 ? 28.331 -12.057 1.332   1.00 9.91  ?  115 ASN   A N    1 
ATOM   2370 C CA   . ASN   A 1 115 ? 29.095 -11.333 2.340   1.00 10.42 ?  115 ASN   A CA   1 
ATOM   2371 C C    . ASN   A 1 115 ? 28.479 -11.471 3.727   1.00 9.89  ?  115 ASN   A C    1 
ATOM   2372 O O    . ASN   A 1 115 ? 29.191 -11.395 4.735   1.00 10.47 ?  115 ASN   A O    1 
ATOM   2373 C CB   . ASN   A 1 115 ? 29.198 -9.854  1.969   1.00 10.35 ?  115 ASN   A CB   1 
ATOM   2374 C CG   . ASN   A 1 115 ? 30.001 -9.623  0.716   1.00 11.28 ?  115 ASN   A CG   1 
ATOM   2375 O OD1  . ASN   A 1 115 ? 31.218 -9.700  0.741   1.00 14.74 ?  115 ASN   A OD1  1 
ATOM   2376 N ND2  . ASN   A 1 115 ? 29.330 -9.331  -0.381  1.00 11.01 ?  115 ASN   A ND2  1 
ATOM   2377 H H    . ASN   A 1 115 ? 28.035 -11.570 0.685   1.00 11.89 ?  115 ASN   A H    1 
ATOM   2378 H HA   . ASN   A 1 115 ? 29.989 -11.698 2.377   1.00 12.51 ?  115 ASN   A HA   1 
ATOM   2379 H HB2  . ASN   A 1 115 ? 28.304 -9.500  1.834   1.00 12.42 ?  115 ASN   A HB2  1 
ATOM   2380 H HB3  . ASN   A 1 115 ? 29.630 -9.379  2.701   1.00 12.42 ?  115 ASN   A HB3  1 
ATOM   2381 H HD21 . ASN   A 1 115 ? 29.748 -9.182  -1.115  1.00 13.22 ?  115 ASN   A HD21 1 
ATOM   2382 H HD22 . ASN   A 1 115 ? 28.468 -9.295  -0.362  1.00 13.22 ?  115 ASN   A HD22 1 
ATOM   2383 N N    . PHE   A 1 116 ? 27.151 -11.634 3.805   1.00 10.02 ?  116 PHE   A N    1 
ATOM   2384 C CA   . PHE   A 1 116 ? 26.499 -11.738 5.106   1.00 10.10 ?  116 PHE   A CA   1 
ATOM   2385 C C    . PHE   A 1 116 ? 26.970 -12.975 5.872   1.00 10.26 ?  116 PHE   A C    1 
ATOM   2386 O O    . PHE   A 1 116 ? 26.896 -12.996 7.100   1.00 10.92 ?  116 PHE   A O    1 
ATOM   2387 C CB   . PHE   A 1 116 ? 24.968 -11.859 4.965   1.00 10.26 ?  116 PHE   A CB   1 
ATOM   2388 C CG   . PHE   A 1 116 ? 24.216 -10.603 4.516   1.00 9.91  ?  116 PHE   A CG   1 
ATOM   2389 C CD1  . PHE   A 1 116 ? 24.794 -9.578  3.775   1.00 10.10 ?  116 PHE   A CD1  1 
ATOM   2390 C CD2  . PHE   A 1 116 ? 22.864 -10.504 4.827   1.00 10.70 ?  116 PHE   A CD2  1 
ATOM   2391 C CE1  . PHE   A 1 116 ? 24.023 -8.482  3.371   1.00 10.42 ?  116 PHE   A CE1  1 
ATOM   2392 C CE2  . PHE   A 1 116 ? 22.101 -9.421  4.430   1.00 11.03 ?  116 PHE   A CE2  1 
ATOM   2393 C CZ   . PHE   A 1 116 ? 22.676 -8.409  3.702   1.00 10.42 ?  116 PHE   A CZ   1 
ATOM   2394 H H    . PHE   A 1 116 ? 26.615 -11.676 3.128   1.00 12.02 ?  116 PHE   A H    1 
ATOM   2395 H HA   . PHE   A 1 116 ? 26.694 -10.950 5.633   1.00 12.12 ?  116 PHE   A HA   1 
ATOM   2396 H HB2  . PHE   A 1 116 ? 24.780 -12.556 4.311   1.00 12.31 ?  116 PHE   A HB2  1 
ATOM   2397 H HB3  . PHE   A 1 116 ? 24.604 -12.124 5.822   1.00 12.31 ?  116 PHE   A HB3  1 
ATOM   2398 H HD1  . PHE   A 1 116 ? 25.690 -9.633  3.541   1.00 12.12 ?  116 PHE   A HD1  1 
ATOM   2399 H HD2  . PHE   A 1 116 ? 22.460 -11.192 5.313   1.00 12.84 ?  116 PHE   A HD2  1 
ATOM   2400 H HE1  . PHE   A 1 116 ? 24.421 -7.803  2.880   1.00 12.51 ?  116 PHE   A HE1  1 
ATOM   2401 H HE2  . PHE   A 1 116 ? 21.201 -9.384  4.661   1.00 13.23 ?  116 PHE   A HE2  1 
ATOM   2402 H HZ   . PHE   A 1 116 ? 22.170 -7.674  3.441   1.00 12.50 ?  116 PHE   A HZ   1 
ATOM   2403 N N    . ASN   A 1 117 ? 27.415 -14.024 5.168   1.00 10.47 ?  117 ASN   A N    1 
ATOM   2404 C CA   . ASN   A 1 117 ? 27.782 -15.269 5.837   1.00 10.70 ?  117 ASN   A CA   1 
ATOM   2405 C C    . ASN   A 1 117 ? 29.043 -15.149 6.674   1.00 11.03 ?  117 ASN   A C    1 
ATOM   2406 O O    . ASN   A 1 117 ? 29.346 -16.067 7.443   1.00 12.00 ?  117 ASN   A O    1 
ATOM   2407 C CB   . ASN   A 1 117 ? 27.893 -16.400 4.817   1.00 10.91 ?  117 ASN   A CB   1 
ATOM   2408 C CG   . ASN   A 1 117 ? 26.537 -16.775 4.276   1.00 10.71 ?  117 ASN   A CG   1 
ATOM   2409 O OD1  . ASN   A 1 117 ? 25.567 -16.814 5.028   1.00 11.88 ?  117 ASN   A OD1  1 
ATOM   2410 N ND2  . ASN   A 1 117 ? 26.448 -17.023 2.985   1.00 10.76 ?  117 ASN   A ND2  1 
ATOM   2411 H H    . ASN   A 1 117 ? 27.497 -14.040 4.309   1.00 12.57 ?  117 ASN   A H    1 
ATOM   2412 H HA   . ASN   A 1 117 ? 27.060 -15.503 6.440   1.00 12.85 ?  117 ASN   A HA   1 
ATOM   2413 H HB2  . ASN   A 1 117 ? 28.448 -16.113 4.075   1.00 13.10 ?  117 ASN   A HB2  1 
ATOM   2414 H HB3  . ASN   A 1 117 ? 28.277 -17.179 5.244   1.00 13.10 ?  117 ASN   A HB3  1 
ATOM   2415 H HD21 . ASN   A 1 117 ? 25.690 -17.234 2.641   1.00 12.92 ?  117 ASN   A HD21 1 
ATOM   2416 H HD22 . ASN   A 1 117 ? 27.149 -16.975 2.489   1.00 12.92 ?  117 ASN   A HD22 1 
ATOM   2417 N N    . GLN   A 1 118 ? 29.769 -14.039 6.557   1.00 11.06 ?  118 GLN   A N    1 
ATOM   2418 C CA   . GLN   A 1 118 ? 30.952 -13.805 7.372   1.00 11.73 ?  118 GLN   A CA   1 
ATOM   2419 C C    . GLN   A 1 118 ? 30.614 -13.236 8.743   1.00 11.69 ?  118 GLN   A C    1 
ATOM   2420 O O    . GLN   A 1 118 ? 31.527 -12.943 9.521   1.00 13.56 ?  118 GLN   A O    1 
ATOM   2421 C CB   . GLN   A 1 118 ? 31.940 -12.897 6.631   1.00 12.05 ?  118 GLN   A CB   1 
ATOM   2422 C CG   . GLN   A 1 118 ? 32.419 -13.477 5.308   1.00 12.34 ?  118 GLN   A CG   1 
ATOM   2423 C CD   . GLN   A 1 118 ? 33.247 -14.740 5.486   1.00 12.43 ?  118 GLN   A CD   1 
ATOM   2424 O OE1  . GLN   A 1 118 ? 34.100 -14.820 6.379   1.00 13.34 ?  118 GLN   A OE1  1 
ATOM   2425 N NE2  . GLN   A 1 118 ? 32.989 -15.742 4.643   1.00 12.57 ?  118 GLN   A NE2  1 
ATOM   2426 H H    . GLN   A 1 118 ? 29.591 -13.395 6.005   1.00 13.27 ?  118 GLN   A H    1 
ATOM   2427 H HA   . GLN   A 1 118 ? 31.388 -14.659 7.512   1.00 14.08 ?  118 GLN   A HA   1 
ATOM   2428 H HB2  . GLN   A 1 118 ? 31.508 -12.049 6.448   1.00 14.46 ?  118 GLN   A HB2  1 
ATOM   2429 H HB3  . GLN   A 1 118 ? 32.716 -12.760 7.195   1.00 14.46 ?  118 GLN   A HB3  1 
ATOM   2430 H HG2  . GLN   A 1 118 ? 31.648 -13.692 4.754   1.00 14.81 ?  118 GLN   A HG2  1 
ATOM   2431 H HG3  . GLN   A 1 118 ? 32.973 -12.821 4.854   1.00 14.81 ?  118 GLN   A HG3  1 
ATOM   2432 H HE21 . GLN   A 1 118 ? 32.382 -15.649 4.031   1.00 15.08 ?  118 GLN   A HE21 1 
ATOM   2433 H HE22 . GLN   A 1 118 ? 33.424 -16.479 4.697   1.00 15.08 ?  118 GLN   A HE22 1 
ATOM   2434 N N    . HIS   A 1 119 ? 29.326 -13.078 9.056   1.00 11.60 ?  119 HIS   A N    1 
ATOM   2435 C CA   . HIS   A 1 119 ? 28.871 -12.477 10.305  1.00 12.04 ?  119 HIS   A CA   1 
ATOM   2436 C C    . HIS   A 1 119 ? 27.731 -13.302 10.877  1.00 12.13 ?  119 HIS   A C    1 
ATOM   2437 O O    . HIS   A 1 119 ? 26.779 -13.628 10.164  1.00 12.70 ?  119 HIS   A O    1 
ATOM   2438 C CB   . HIS   A 1 119 ? 28.411 -11.045 10.039  1.00 12.78 ?  119 HIS   A CB   1 
ATOM   2439 C CG   . HIS   A 1 119 ? 29.492 -10.223 9.439   1.00 14.20 ?  119 HIS   A CG   1 
ATOM   2440 N ND1  . HIS   A 1 119 ? 30.461 -9.618  10.205  1.00 16.29 ?  119 HIS   A ND1  1 
ATOM   2441 C CD2  . HIS   A 1 119 ? 29.842 -10.023 8.148   1.00 15.14 ?  119 HIS   A CD2  1 
ATOM   2442 C CE1  . HIS   A 1 119 ? 31.332 -9.025  9.408   1.00 16.97 ?  119 HIS   A CE1  1 
ATOM   2443 N NE2  . HIS   A 1 119 ? 30.988 -9.266  8.155   1.00 16.72 ?  119 HIS   A NE2  1 
ATOM   2444 H H    . HIS   A 1 119 ? 28.674 -13.333 8.551   1.00 13.92 ?  119 HIS   A H    1 
ATOM   2445 H HA   . HIS   A 1 119 ? 29.605 -12.463 10.946  1.00 14.44 ?  119 HIS   A HA   1 
ATOM   2446 H HB2  . HIS   A 1 119 ? 27.664 -11.067 9.422   1.00 15.34 ?  119 HIS   A HB2  1 
ATOM   2447 H HB3  . HIS   A 1 119 ? 28.147 -10.640 10.877  1.00 15.34 ?  119 HIS   A HB3  1 
ATOM   2448 H HD2  . HIS   A 1 119 ? 29.390 -10.336 7.396   1.00 18.17 ?  119 HIS   A HD2  1 
ATOM   2449 H HE1  . HIS   A 1 119 ? 32.066 -8.523  9.680   1.00 20.36 ?  119 HIS   A HE1  1 
ATOM   2450 H HE2  . HIS   A 1 119 ? 31.396 -8.971  7.457   1.00 20.06 ?  119 HIS   A HE2  1 
ATOM   2451 N N    . GLU   A 1 120 ? 27.819 -13.622 12.168  1.00 12.94 ?  120 GLU   A N    1 
ATOM   2452 C CA   . GLU   A 1 120 ? 26.858 -14.553 12.756  1.00 15.18 ?  120 GLU   A CA   1 
ATOM   2453 C C    . GLU   A 1 120 ? 25.445 -13.982 12.824  1.00 13.80 ?  120 GLU   A C    1 
ATOM   2454 O O    . GLU   A 1 120 ? 24.465 -14.740 12.705  1.00 13.78 ?  120 GLU   A O    1 
ATOM   2455 C CB   . GLU   A 1 120 ? 27.325 -14.982 14.149  1.00 21.23 ?  120 GLU   A CB   1 
ATOM   2456 C CG   . GLU   A 1 120 ? 28.499 -15.946 14.143  1.00 29.82 ?  120 GLU   A CG   1 
ATOM   2457 C CD   . GLU   A 1 120 ? 28.698 -16.625 15.483  1.00 37.36 ?  120 GLU   A CD   1 
ATOM   2458 O OE1  . GLU   A 1 120 ? 28.312 -16.034 16.514  1.00 39.56 ?  120 GLU   A OE1  1 
ATOM   2459 O OE2  . GLU   A 1 120 ? 29.234 -17.754 15.505  1.00 41.85 -1 120 GLU   A OE2  1 
ATOM   2460 H H    . GLU   A 1 120 ? 28.422 -13.331 12.715  1.00 15.53 ?  120 GLU   A H    1 
ATOM   2461 H HA   . GLU   A 1 120 ? 26.825 -15.349 12.210  1.00 18.22 ?  120 GLU   A HA   1 
ATOM   2462 H HB2  . GLU   A 1 120 ? 27.597 -14.198 14.651  1.00 25.47 ?  120 GLU   A HB2  1 
ATOM   2463 H HB3  . GLU   A 1 120 ? 26.590 -15.424 14.607  1.00 25.47 ?  120 GLU   A HB3  1 
ATOM   2464 H HG2  . GLU   A 1 120 ? 28.348 -16.631 13.472  1.00 35.78 ?  120 GLU   A HG2  1 
ATOM   2465 H HG3  . GLU   A 1 120 ? 29.313 -15.459 13.944  1.00 35.78 ?  120 GLU   A HG3  1 
ATOM   2466 N N    . VAL   A 1 121 ? 25.319 -12.672 13.040  1.00 13.10 ?  121 VAL   A N    1 
ATOM   2467 C CA   . VAL   A 1 121 ? 24.031 -11.996 13.181  1.00 13.30 ?  121 VAL   A CA   1 
ATOM   2468 C C    . VAL   A 1 121 ? 24.145 -10.612 12.546  1.00 12.02 ?  121 VAL   A C    1 
ATOM   2469 O O    . VAL   A 1 121 ? 25.113 -9.888  12.797  1.00 12.76 ?  121 VAL   A O    1 
ATOM   2470 C CB   . VAL   A 1 121 ? 23.622 -11.853 14.665  1.00 16.08 ?  121 VAL   A CB   1 
ATOM   2471 C CG1  . VAL   A 1 121 ? 22.265 -11.179 14.786  1.00 16.64 ?  121 VAL   A CG1  1 
ATOM   2472 C CG2  . VAL   A 1 121 ? 23.607 -13.195 15.376  1.00 18.26 ?  121 VAL   A CG2  1 
ATOM   2473 H H    . VAL   A 1 121 ? 25.989 -12.133 13.114  1.00 15.71 ?  121 VAL   A H    1 
ATOM   2474 H HA   . VAL   A 1 121 ? 23.347 -12.499 12.718  1.00 15.96 ?  121 VAL   A HA   1 
ATOM   2475 H HB   . VAL   A 1 121 ? 24.267 -11.291 15.117  1.00 19.29 ?  121 VAL   A HB   1 
ATOM   2476 H HG11 . VAL   A 1 121 ? 21.952 -11.260 15.701  1.00 19.97 ?  121 VAL   A HG11 1 
ATOM   2477 H HG12 . VAL   A 1 121 ? 22.355 -10.241 14.553  1.00 19.97 ?  121 VAL   A HG12 1 
ATOM   2478 H HG13 . VAL   A 1 121 ? 21.641 -11.613 14.185  1.00 19.97 ?  121 VAL   A HG13 1 
ATOM   2479 H HG21 . VAL   A 1 121 ? 23.271 -13.073 16.283  1.00 21.92 ?  121 VAL   A HG21 1 
ATOM   2480 H HG22 . VAL   A 1 121 ? 23.021 -13.805 14.895  1.00 21.92 ?  121 VAL   A HG22 1 
ATOM   2481 H HG23 . VAL   A 1 121 ? 24.504 -13.552 15.405  1.00 21.92 ?  121 VAL   A HG23 1 
ATOM   2482 N N    . LEU   A 1 122 ? 23.133 -10.220 11.763  1.00 11.65 ?  122 LEU   A N    1 
ATOM   2483 C CA   . LEU   A 1 122 ? 23.129 -8.923  11.087  1.00 11.45 ?  122 LEU   A CA   1 
ATOM   2484 C C    . LEU   A 1 122 ? 21.730 -8.332  11.059  1.00 11.21 ?  122 LEU   A C    1 
ATOM   2485 O O    . LEU   A 1 122 ? 20.741 -9.049  10.909  1.00 12.46 ?  122 LEU   A O    1 
ATOM   2486 C CB   . LEU   A 1 122 ? 23.544 -9.013  9.612   1.00 13.02 ?  122 LEU   A CB   1 
ATOM   2487 C CG   . LEU   A 1 122 ? 24.747 -9.866  9.245   1.00 12.73 ?  122 LEU   A CG   1 
ATOM   2488 C CD1  . LEU   A 1 122 ? 24.343 -11.312 9.001   1.00 13.75 ?  122 LEU   A CD1  1 
ATOM   2489 C CD2  . LEU   A 1 122 ? 25.430 -9.290  8.023   1.00 12.52 ?  122 LEU   A CD2  1 
ATOM   2490 H H    . LEU   A 1 122 ? 22.430 -10.690 11.605  1.00 13.98 ?  122 LEU   A H    1 
ATOM   2491 H HA   . LEU   A 1 122 ? 23.726 -8.305  11.543  1.00 13.74 ?  122 LEU   A HA   1 
ATOM   2492 H HB2  . LEU   A 1 122 ? 22.796 -9.366  9.113   1.00 15.62 ?  122 LEU   A HB2  1 
ATOM   2493 H HB3  . LEU   A 1 122 ? 23.740 -8.116  9.301   1.00 15.62 ?  122 LEU   A HB3  1 
ATOM   2494 H HG   . LEU   A 1 122 ? 25.392 -9.855  9.973   1.00 15.28 ?  122 LEU   A HG   1 
ATOM   2495 H HD11 . LEU   A 1 122 ? 25.125 -11.827 8.741   1.00 16.50 ?  122 LEU   A HD11 1 
ATOM   2496 H HD12 . LEU   A 1 122 ? 23.968 -11.679 9.818   1.00 16.50 ?  122 LEU   A HD12 1 
ATOM   2497 H HD13 . LEU   A 1 122 ? 23.681 -11.342 8.293   1.00 16.50 ?  122 LEU   A HD13 1 
ATOM   2498 H HD21 . LEU   A 1 122 ? 26.170 -9.866  7.764   1.00 15.02 ?  122 LEU   A HD21 1 
ATOM   2499 H HD22 . LEU   A 1 122 ? 24.789 -9.232  7.299   1.00 15.02 ?  122 LEU   A HD22 1 
ATOM   2500 H HD23 . LEU   A 1 122 ? 25.768 -8.403  8.237   1.00 15.02 ?  122 LEU   A HD23 1 
ATOM   2501 N N    . LEU   A 1 123 ? 21.676 -7.000  11.159  1.00 10.75 ?  123 LEU   A N    1 
ATOM   2502 C CA   . LEU   A 1 123 ? 20.505 -6.196  10.802  1.00 10.72 ?  123 LEU   A CA   1 
ATOM   2503 C C    . LEU   A 1 123 ? 20.742 -5.654  9.398   1.00 10.14 ?  123 LEU   A C    1 
ATOM   2504 O O    . LEU   A 1 123 ? 21.788 -5.053  9.151   1.00 10.92 ?  123 LEU   A O    1 
ATOM   2505 C CB   . LEU   A 1 123 ? 20.383 -5.031  11.786  1.00 11.44 ?  123 LEU   A CB   1 
ATOM   2506 C CG   . LEU   A 1 123 ? 19.331 -3.967  11.470  1.00 12.16 ?  123 LEU   A CG   1 
ATOM   2507 C CD1  . LEU   A 1 123 ? 17.939 -4.565  11.471  1.00 13.04 ?  123 LEU   A CD1  1 
ATOM   2508 C CD2  . LEU   A 1 123 ? 19.420 -2.804  12.460  1.00 12.82 ?  123 LEU   A CD2  1 
ATOM   2509 H H    . LEU   A 1 123 ? 22.334 -6.517  11.437  1.00 12.90 ?  123 LEU   A H    1 
ATOM   2510 H HA   . LEU   A 1 123 ? 19.697 -6.734  10.821  1.00 12.86 ?  123 LEU   A HA   1 
ATOM   2511 H HB2  . LEU   A 1 123 ? 20.160 -5.394  12.660  1.00 13.73 ?  123 LEU   A HB2  1 
ATOM   2512 H HB3  . LEU   A 1 123 ? 21.237 -4.582  11.835  1.00 13.73 ?  123 LEU   A HB3  1 
ATOM   2513 H HG   . LEU   A 1 123 ? 19.496 -3.602  10.586  1.00 14.59 ?  123 LEU   A HG   1 
ATOM   2514 H HD11 . LEU   A 1 123 ? 17.289 -3.862  11.333  1.00 15.65 ?  123 LEU   A HD11 1 
ATOM   2515 H HD12 . LEU   A 1 123 ? 17.881 -5.219  10.757  1.00 15.65 ?  123 LEU   A HD12 1 
ATOM   2516 H HD13 . LEU   A 1 123 ? 17.786 -4.997  12.327  1.00 15.65 ?  123 LEU   A HD13 1 
ATOM   2517 H HD21 . LEU   A 1 123 ? 18.745 -2.144  12.241  1.00 15.39 ?  123 LEU   A HD21 1 
ATOM   2518 H HD22 . LEU   A 1 123 ? 19.265 -3.146  13.359  1.00 15.39 ?  123 LEU   A HD22 1 
ATOM   2519 H HD23 . LEU   A 1 123 ? 20.303 -2.409  12.407  1.00 15.39 ?  123 LEU   A HD23 1 
ATOM   2520 N N    A ALA   A 1 124 ? 19.779 -5.824  8.489   0.74 9.99  ?  124 ALA   A N    1 
ATOM   2521 N N    B ALA   A 1 124 ? 19.801 -5.885  8.489   0.26 9.84  ?  124 ALA   A N    1 
ATOM   2522 C CA   A ALA   A 1 124 ? 20.055 -5.534  7.087   0.74 10.10 ?  124 ALA   A CA   1 
ATOM   2523 C CA   B ALA   A 1 124 ? 20.057 -5.582  7.091   0.26 9.66  ?  124 ALA   A CA   1 
ATOM   2524 C C    A ALA   A 1 124 ? 18.807 -5.081  6.341   0.74 10.30 ?  124 ALA   A C    1 
ATOM   2525 C C    B ALA   A 1 124 ? 18.829 -5.020  6.394   0.26 9.55  ?  124 ALA   A C    1 
ATOM   2526 O O    A ALA   A 1 124 ? 17.681 -5.450  6.707   0.74 11.21 ?  124 ALA   A O    1 
ATOM   2527 O O    B ALA   A 1 124 ? 17.691 -5.344  6.757   0.26 10.05 ?  124 ALA   A O    1 
ATOM   2528 C CB   A ALA   A 1 124 ? 20.642 -6.758  6.377   0.74 10.65 ?  124 ALA   A CB   1 
ATOM   2529 C CB   B ALA   A 1 124 ? 20.535 -6.826  6.326   0.26 9.61  ?  124 ALA   A CB   1 
ATOM   2530 H H    A ALA   A 1 124 ? 18.982 -6.107  8.652   0.74 11.99 ?  124 ALA   A H    1 
ATOM   2531 H H    B ALA   A 1 124 ? 19.021 -6.214  8.652   0.26 11.80 ?  124 ALA   A H    1 
ATOM   2532 H HA   A ALA   A 1 124 ? 20.717 -4.831  7.050   0.74 12.12 ?  124 ALA   A HA   1 
ATOM   2533 H HA   B ALA   A 1 124 ? 20.765 -4.926  7.052   0.26 11.60 ?  124 ALA   A HA   1 
ATOM   2534 H HB1  A ALA   A 1 124 ? 20.820 -6.538  5.448   0.74 12.78 ?  124 ALA   A HB1  1 
ATOM   2535 H HB1  B ALA   A 1 124 ? 20.700 -6.587  5.399   0.26 11.53 ?  124 ALA   A HB1  1 
ATOM   2536 H HB2  A ALA   A 1 124 ? 21.477 -7.013  6.814   0.74 12.78 ?  124 ALA   A HB2  1 
ATOM   2537 H HB2  B ALA   A 1 124 ? 21.361 -7.151  6.730   0.26 11.53 ?  124 ALA   A HB2  1 
ATOM   2538 H HB3  A ALA   A 1 124 ? 20.013 -7.494  6.427   0.74 12.78 ?  124 ALA   A HB3  1 
ATOM   2539 H HB3  B ALA   A 1 124 ? 19.855 -7.514  6.375   0.26 11.53 ?  124 ALA   A HB3  1 
ATOM   2540 N N    A PRO   A 1 125 ? 18.988 -4.345  5.242   0.74 10.15 ?  125 PRO   A N    1 
ATOM   2541 N N    B PRO   A 1 125 ? 19.039 -4.175  5.384   0.26 9.28  ?  125 PRO   A N    1 
ATOM   2542 C CA   A PRO   A 1 125 ? 17.923 -4.101  4.271   0.74 10.54 ?  125 PRO   A CA   1 
ATOM   2543 C CA   B PRO   A 1 125 ? 17.954 -3.794  4.477   0.26 9.27  ?  125 PRO   A CA   1 
ATOM   2544 C C    A PRO   A 1 125 ? 17.976 -5.160  3.174   0.74 10.54 ?  125 PRO   A C    1 
ATOM   2545 C C    B PRO   A 1 125 ? 17.921 -4.738  3.284   0.26 9.10  ?  125 PRO   A C    1 
ATOM   2546 O O    A PRO   A 1 125 ? 18.950 -5.905  3.041   0.74 10.78 ?  125 PRO   A O    1 
ATOM   2547 O O    B PRO   A 1 125 ? 18.720 -5.679  3.215   0.26 9.42  ?  125 PRO   A O    1 
ATOM   2548 C CB   A PRO   A 1 125 ? 18.351 -2.752  3.684   0.74 10.76 ?  125 PRO   A CB   1 
ATOM   2549 C CB   B PRO   A 1 125 ? 18.373 -2.386  4.045   0.26 9.49  ?  125 PRO   A CB   1 
ATOM   2550 C CG   A PRO   A 1 125 ? 19.869 -2.896  3.585   0.74 10.24 ?  125 PRO   A CG   1 
ATOM   2551 C CG   B PRO   A 1 125 ? 19.883 -2.486  3.981   0.26 9.88  ?  125 PRO   A CG   1 
ATOM   2552 C CD   A PRO   A 1 125 ? 20.262 -3.725  4.811   0.74 10.27 ?  125 PRO   A CD   1 
ATOM   2553 C CD   B PRO   A 1 125 ? 20.296 -3.478  5.052   0.26 9.61  ?  125 PRO   A CD   1 
ATOM   2554 H HA   A PRO   A 1 125 ? 17.046 -4.061  4.687   0.74 12.65 ?  125 PRO   A HA   1 
ATOM   2555 H HA   B PRO   A 1 125 ? 17.091 -3.772  4.933   0.26 11.12 ?  125 PRO   A HA   1 
ATOM   2556 H HB2  A PRO   A 1 125 ? 17.945 -2.629  2.808   0.74 12.92 ?  125 PRO   A HB2  1 
ATOM   2557 H HB2  B PRO   A 1 125 ? 17.997 -2.182  3.174   0.26 11.39 ?  125 PRO   A HB2  1 
ATOM   2558 H HB3  A PRO   A 1 125 ? 18.097 -2.038  4.288   0.74 12.92 ?  125 PRO   A HB3  1 
ATOM   2559 H HB3  B PRO   A 1 125 ? 18.092 -1.734  4.708   0.26 11.39 ?  125 PRO   A HB3  1 
ATOM   2560 H HG2  A PRO   A 1 125 ? 20.104 -3.362  2.764   0.74 12.28 ?  125 PRO   A HG2  1 
ATOM   2561 H HG2  B PRO   A 1 125 ? 20.149 -2.806  3.106   0.26 11.86 ?  125 PRO   A HG2  1 
ATOM   2562 H HG3  A PRO   A 1 125 ? 20.283 -2.020  3.612   0.74 12.28 ?  125 PRO   A HG3  1 
ATOM   2563 H HG3  B PRO   A 1 125 ? 20.273 -1.617  4.160   0.26 11.86 ?  125 PRO   A HG3  1 
ATOM   2564 H HD2  A PRO   A 1 125 ? 20.919 -4.399  4.564   0.74 12.33 ?  125 PRO   A HD2  1 
ATOM   2565 H HD2  B PRO   A 1 125 ? 20.943 -4.111  4.700   0.26 11.54 ?  125 PRO   A HD2  1 
ATOM   2566 H HD3  A PRO   A 1 125 ? 20.600 -3.145  5.512   0.74 12.33 ?  125 PRO   A HD3  1 
ATOM   2567 H HD3  B PRO   A 1 125 ? 20.642 -3.014  5.830   0.26 11.54 ?  125 PRO   A HD3  1 
ATOM   2568 N N    A LEU   A 1 126 ? 16.923 -5.196  2.364   0.74 11.22 ?  126 LEU   A N    1 
ATOM   2569 N N    B LEU   A 1 126 ? 17.020 -4.496  2.336   0.26 9.58  ?  126 LEU   A N    1 
ATOM   2570 C CA   A LEU   A 1 126 ? 16.949 -6.034  1.173   0.74 11.25 ?  126 LEU   A CA   1 
ATOM   2571 C CA   B LEU   A 1 126 ? 16.938 -5.307  1.124   0.26 9.91  ?  126 LEU   A CA   1 
ATOM   2572 C C    A LEU   A 1 126 ? 17.885 -5.430  0.132   0.74 11.17 ?  126 LEU   A C    1 
ATOM   2573 C C    B LEU   A 1 126 ? 17.943 -4.787  0.099   0.26 9.74  ?  126 LEU   A C    1 
ATOM   2574 O O    A LEU   A 1 126 ? 17.666 -4.312  -0.342  0.74 11.55 ?  126 LEU   A O    1 
ATOM   2575 O O    B LEU   A 1 126 ? 17.773 -3.697  -0.456  0.26 10.01 ?  126 LEU   A O    1 
ATOM   2576 C CB   A LEU   A 1 126 ? 15.549 -6.191  0.596   0.74 12.29 ?  126 LEU   A CB   1 
ATOM   2577 C CB   B LEU   A 1 126 ? 15.521 -5.251  0.562   0.26 10.75 ?  126 LEU   A CB   1 
ATOM   2578 C CG   A LEU   A 1 126 ? 14.631 -7.129  1.371   0.74 13.94 ?  126 LEU   A CG   1 
ATOM   2579 C CG   B LEU   A 1 126 ? 14.450 -5.987  1.366   0.26 12.20 ?  126 LEU   A CG   1 
ATOM   2580 C CD1  A LEU   A 1 126 ? 13.216 -6.971  0.863   0.74 15.27 ?  126 LEU   A CD1  1 
ATOM   2581 C CD1  B LEU   A 1 126 ? 13.063 -5.519  0.951   0.26 13.20 ?  126 LEU   A CD1  1 
ATOM   2582 C CD2  A LEU   A 1 126 ? 15.095 -8.575  1.223   0.74 14.02 ?  126 LEU   A CD2  1 
ATOM   2583 C CD2  B LEU   A 1 126 ? 14.589 -7.496  1.193   0.26 12.82 ?  126 LEU   A CD2  1 
ATOM   2584 H H    A LEU   A 1 126 ? 16.196 -4.743  2.467   0.74 13.46 ?  126 LEU   A H    1 
ATOM   2585 H H    B LEU   A 1 126 ? 16.427 -3.876  2.385   0.26 11.50 ?  126 LEU   A H    1 
ATOM   2586 H HA   A LEU   A 1 126 ? 17.284 -6.908  1.400   0.74 13.50 ?  126 LEU   A HA   1 
ATOM   2587 H HA   B LEU   A 1 126 ? 17.154 -6.232  1.335   0.26 11.90 ?  126 LEU   A HA   1 
ATOM   2588 H HB2  A LEU   A 1 126 ? 15.118 -5.322  0.575   0.74 14.75 ?  126 LEU   A HB2  1 
ATOM   2589 H HB2  B LEU   A 1 126 ? 15.254 -4.321  0.507   0.26 12.89 ?  126 LEU   A HB2  1 
ATOM   2590 H HB3  A LEU   A 1 126 ? 15.616 -6.541  -0.306  0.74 14.75 ?  126 LEU   A HB3  1 
ATOM   2591 H HB3  B LEU   A 1 126 ? 15.534 -5.639  -0.325  0.26 12.89 ?  126 LEU   A HB3  1 
ATOM   2592 H HG   A LEU   A 1 126 ? 14.639 -6.896  2.315   0.74 16.73 ?  126 LEU   A HG   1 
ATOM   2593 H HG   B LEU   A 1 126 ? 14.563 -5.781  2.306   0.26 14.64 ?  126 LEU   A HG   1 
ATOM   2594 H HD11 A LEU   A 1 126 ? 12.635 -7.579  1.348   0.74 18.32 ?  126 LEU   A HD11 1 
ATOM   2595 H HD11 B LEU   A 1 126 ? 12.398 -6.000  1.468   0.26 15.84 ?  126 LEU   A HD11 1 
ATOM   2596 H HD12 A LEU   A 1 126 ? 12.930 -6.057  1.004   0.74 18.32 ?  126 LEU   A HD12 1 
ATOM   2597 H HD12 B LEU   A 1 126 ? 12.987 -4.566  1.119   0.26 15.84 ?  126 LEU   A HD12 1 
ATOM   2598 H HD13 A LEU   A 1 126 ? 13.199 -7.184  -0.084  0.74 18.32 ?  126 LEU   A HD13 1 
ATOM   2599 H HD13 B LEU   A 1 126 ? 12.939 -5.697  0.005   0.26 15.84 ?  126 LEU   A HD13 1 
ATOM   2600 H HD21 A LEU   A 1 126 ? 14.432 -9.167  1.606   0.74 16.83 ?  126 LEU   A HD21 1 
ATOM   2601 H HD21 B LEU   A 1 126 ? 13.878 -7.939  1.685   0.26 15.38 ?  126 LEU   A HD21 1 
ATOM   2602 H HD22 A LEU   A 1 126 ? 15.213 -8.772  0.280   0.74 16.83 ?  126 LEU   A HD22 1 
ATOM   2603 H HD22 B LEU   A 1 126 ? 14.521 -7.715  0.249   0.26 15.38 ?  126 LEU   A HD22 1 
ATOM   2604 H HD23 A LEU   A 1 126 ? 15.942 -8.682  1.688   0.74 16.83 ?  126 LEU   A HD23 1 
ATOM   2605 H HD23 B LEU   A 1 126 ? 15.451 -7.777  1.535   0.26 15.38 ?  126 LEU   A HD23 1 
ATOM   2606 N N    A LEU   A 1 127 ? 18.920 -6.175  -0.239  0.74 11.11 ?  127 LEU   A N    1 
ATOM   2607 N N    B LEU   A 1 127 ? 18.985 -5.568  -0.165  0.26 9.06  ?  127 LEU   A N    1 
ATOM   2608 C CA   A LEU   A 1 127 ? 19.912 -5.667  -1.176  0.74 10.52 ?  127 LEU   A CA   1 
ATOM   2609 C CA   B LEU   A 1 127 ? 19.988 -5.163  -1.138  0.26 9.20  ?  127 LEU   A CA   1 
ATOM   2610 C C    A LEU   A 1 127 ? 19.298 -5.447  -2.551  0.74 9.88  ?  127 LEU   A C    1 
ATOM   2611 C C    B LEU   A 1 127 ? 19.405 -5.151  -2.550  0.26 9.55  ?  127 LEU   A C    1 
ATOM   2612 O O    A LEU   A 1 127 ? 18.457 -6.224  -3.015  0.74 10.26 ?  127 LEU   A O    1 
ATOM   2613 O O    B LEU   A 1 127 ? 18.543 -5.961  -2.903  0.26 9.84  ?  127 LEU   A O    1 
ATOM   2614 C CB   A LEU   A 1 127 ? 21.080 -6.645  -1.288  0.74 10.90 ?  127 LEU   A CB   1 
ATOM   2615 C CB   B LEU   A 1 127 ? 21.180 -6.117  -1.089  0.26 9.57  ?  127 LEU   A CB   1 
ATOM   2616 C CG   A LEU   A 1 127 ? 21.900 -6.878  -0.018  0.74 11.42 ?  127 LEU   A CG   1 
ATOM   2617 C CG   B LEU   A 1 127 ? 21.941 -6.185  0.239   0.26 9.91  ?  127 LEU   A CG   1 
ATOM   2618 C CD1  A LEU   A 1 127 ? 23.008 -7.864  -0.302  0.74 11.67 ?  127 LEU   A CD1  1 
ATOM   2619 C CD1  B LEU   A 1 127 ? 23.080 -7.186  0.145   0.26 10.29 ?  127 LEU   A CD1  1 
ATOM   2620 C CD2  A LEU   A 1 127 ? 22.490 -5.584  0.509   0.74 12.36 ?  127 LEU   A CD2  1 
ATOM   2621 C CD2  B LEU   A 1 127 ? 22.462 -4.812  0.641   0.26 10.13 ?  127 LEU   A CD2  1 
ATOM   2622 H H    A LEU   A 1 127 ? 19.070 -6.972  0.044   0.74 13.33 ?  127 LEU   A H    1 
ATOM   2623 H H    B LEU   A 1 127 ? 19.138 -6.325  0.216   0.26 10.87 ?  127 LEU   A H    1 
ATOM   2624 H HA   A LEU   A 1 127 ? 20.250 -4.823  -0.857  0.74 12.63 ?  127 LEU   A HA   1 
ATOM   2625 H HA   B LEU   A 1 127 ? 20.304 -4.265  -0.919  0.26 11.04 ?  127 LEU   A HA   1 
ATOM   2626 H HB2  A LEU   A 1 127 ? 20.733 -7.507  -1.563  0.74 13.08 ?  127 LEU   A HB2  1 
ATOM   2627 H HB2  B LEU   A 1 127 ? 20.858 -7.011  -1.284  0.26 11.49 ?  127 LEU   A HB2  1 
ATOM   2628 H HB3  A LEU   A 1 127 ? 21.690 -6.312  -1.963  0.74 13.08 ?  127 LEU   A HB3  1 
ATOM   2629 H HB3  B LEU   A 1 127 ? 21.813 -5.846  -1.770  0.26 11.49 ?  127 LEU   A HB3  1 
ATOM   2630 H HG   A LEU   A 1 127 ? 21.328 -7.251  0.672   0.74 13.71 ?  127 LEU   A HG   1 
ATOM   2631 H HG   B LEU   A 1 127 ? 21.336 -6.492  0.933   0.26 11.89 ?  127 LEU   A HG   1 
ATOM   2632 H HD11 A LEU   A 1 127 ? 23.501 -8.030  0.519   0.74 14.00 ?  127 LEU   A HD11 1 
ATOM   2633 H HD11 B LEU   A 1 127 ? 23.606 -7.140  0.958   0.26 12.35 ?  127 LEU   A HD11 1 
ATOM   2634 H HD12 A LEU   A 1 127 ? 22.620 -8.690  -0.626  0.74 14.00 ?  127 LEU   A HD12 1 
ATOM   2635 H HD12 B LEU   A 1 127 ? 22.710 -8.078  0.041   0.26 12.35 ?  127 LEU   A HD12 1 
ATOM   2636 H HD13 A LEU   A 1 127 ? 23.600 -7.489  -0.971  0.74 14.00 ?  127 LEU   A HD13 1 
ATOM   2637 H HD13 B LEU   A 1 127 ? 23.632 -6.964  -0.619  0.26 12.35 ?  127 LEU   A HD13 1 
ATOM   2638 H HD21 A LEU   A 1 127 ? 23.100 -5.784  1.238   0.74 14.84 ?  127 LEU   A HD21 1 
ATOM   2639 H HD21 B LEU   A 1 127 ? 23.052 -4.911  1.406   0.26 12.15 ?  127 LEU   A HD21 1 
ATOM   2640 H HD22 A LEU   A 1 127 ? 22.976 -5.141  -0.209  0.74 14.84 ?  127 LEU   A HD22 1 
ATOM   2641 H HD22 B LEU   A 1 127 ? 22.952 -4.432  -0.105  0.26 12.15 ?  127 LEU   A HD22 1 
ATOM   2642 H HD23 A LEU   A 1 127 ? 21.777 -5.008  0.825   0.74 14.84 ?  127 LEU   A HD23 1 
ATOM   2643 H HD23 B LEU   A 1 127 ? 21.713 -4.245  0.872   0.26 12.15 ?  127 LEU   A HD23 1 
ATOM   2644 N N    A SER   A 1 128 ? 19.736 -4.377  -3.202  0.74 9.86  ?  128 SER   A N    1 
ATOM   2645 N N    B SER   A 1 128 ? 19.887 -4.202  -3.355  0.26 10.08 ?  128 SER   A N    1 
ATOM   2646 C CA   A SER   A 1 128 ? 19.323 -3.966  -4.539  0.74 10.14 ?  128 SER   A CA   1 
ATOM   2647 C CA   B SER   A 1 128 ? 19.516 -4.037  -4.760  0.26 9.92  ?  128 SER   A CA   1 
ATOM   2648 C C    A SER   A 1 128 ? 17.864 -3.519  -4.621  0.74 10.58 ?  128 SER   A C    1 
ATOM   2649 C C    B SER   A 1 128 ? 18.095 -3.520  -4.977  0.26 9.64  ?  128 SER   A C    1 
ATOM   2650 O O    A SER   A 1 128 ? 17.393 -3.204  -5.714  0.74 11.77 ?  128 SER   A O    1 
ATOM   2651 O O    B SER   A 1 128 ? 17.725 -3.197  -6.110  0.26 9.64  ?  128 SER   A O    1 
ATOM   2652 C CB   A SER   A 1 128 ? 19.671 -4.995  -5.622  0.74 10.16 ?  128 SER   A CB   1 
ATOM   2653 C CB   B SER   A 1 128 ? 19.761 -5.313  -5.572  0.26 10.26 ?  128 SER   A CB   1 
ATOM   2654 O OG   A SER   A 1 128 ? 21.081 -5.190  -5.686  0.74 10.60 ?  128 SER   A OG   1 
ATOM   2655 O OG   B SER   A 1 128 ? 21.147 -5.489  -5.824  0.26 10.51 ?  128 SER   A OG   1 
ATOM   2656 H H    A SER   A 1 128 ? 20.326 -3.842  -2.869  0.74 11.83 ?  128 SER   A H    1 
ATOM   2657 H H    B SER   A 1 128 ? 20.466 -3.620  -3.095  0.26 12.09 ?  128 SER   A H    1 
ATOM   2658 H HA   A SER   A 1 128 ? 19.843 -3.182  -4.753  0.74 12.17 ?  128 SER   A HA   1 
ATOM   2659 H HA   B SER   A 1 128 ? 20.104 -3.366  -5.126  0.26 11.91 ?  128 SER   A HA   1 
ATOM   2660 H HB2  A SER   A 1 128 ? 19.244 -5.839  -5.414  0.74 12.20 ?  128 SER   A HB2  1 
ATOM   2661 H HB2  B SER   A 1 128 ? 19.428 -6.079  -5.086  0.26 12.31 ?  128 SER   A HB2  1 
ATOM   2662 H HB3  A SER   A 1 128 ? 19.353 -4.668  -6.482  0.74 12.20 ?  128 SER   A HB3  1 
ATOM   2663 H HB3  B SER   A 1 128 ? 19.294 -5.234  -6.422  0.26 12.31 ?  128 SER   A HB3  1 
ATOM   2664 H HG   A SER   A 1 128 ? 21.465 -4.467  -5.882  0.74 12.72 ?  128 SER   A HG   1 
ATOM   2665 H HG   B SER   A 1 128 ? 21.443 -4.832  -6.257  0.26 12.62 ?  128 SER   A HG   1 
ATOM   2666 N N    A ALA   A 1 129 ? 17.154 -3.439  -3.496  0.74 10.93 ?  129 ALA   A N    1 
ATOM   2667 N N    B ALA   A 1 129 ? 17.300 -3.416  -3.914  0.26 9.90  ?  129 ALA   A N    1 
ATOM   2668 C CA   A ALA   A 1 129 ? 15.796 -2.920  -3.480  0.74 11.12 ?  129 ALA   A CA   1 
ATOM   2669 C CA   B ALA   A 1 129 ? 15.968 -2.842  -4.022  0.26 10.18 ?  129 ALA   A CA   1 
ATOM   2670 C C    A ALA   A 1 129 ? 15.813 -1.388  -3.471  0.74 10.87 ?  129 ALA   A C    1 
ATOM   2671 C C    B ALA   A 1 129 ? 16.048 -1.312  -4.007  0.26 10.31 ?  129 ALA   A C    1 
ATOM   2672 O O    A ALA   A 1 129 ? 16.865 -0.742  -3.557  0.74 10.84 ?  129 ALA   A O    1 
ATOM   2673 O O    B ALA   A 1 129 ? 17.128 -0.716  -3.972  0.26 10.39 ?  129 ALA   A O    1 
ATOM   2674 C CB   A ALA   A 1 129 ? 15.033 -3.474  -2.277  0.74 12.51 ?  129 ALA   A CB   1 
ATOM   2675 C CB   B ALA   A 1 129 ? 15.067 -3.385  -2.913  0.26 10.36 ?  129 ALA   A CB   1 
ATOM   2676 H H    A ALA   A 1 129 ? 17.444 -3.679  -2.721  0.74 13.12 ?  129 ALA   A H    1 
ATOM   2677 H H    B ALA   A 1 129 ? 17.511 -3.670  -3.118  0.26 11.88 ?  129 ALA   A H    1 
ATOM   2678 H HA   A ALA   A 1 129 ? 15.338 -3.212  -4.282  0.74 13.34 ?  129 ALA   A HA   1 
ATOM   2679 H HA   B ALA   A 1 129 ? 15.583 -3.107  -4.869  0.26 12.21 ?  129 ALA   A HA   1 
ATOM   2680 H HB1  A ALA   A 1 129 ? 14.123 -3.126  -2.292  0.74 15.01 ?  129 ALA   A HB1  1 
ATOM   2681 H HB1  B ALA   A 1 129 ? 14.182 -2.998  -3.008  0.26 12.43 ?  129 ALA   A HB1  1 
ATOM   2682 H HB2  A ALA   A 1 129 ? 15.014 -4.440  -2.330  0.74 15.01 ?  129 ALA   A HB2  1 
ATOM   2683 H HB2  B ALA   A 1 129 ? 15.014 -4.351  -2.993  0.26 12.43 ?  129 ALA   A HB2  1 
ATOM   2684 H HB3  A ALA   A 1 129 ? 15.476 -3.193  -1.462  0.74 15.01 ?  129 ALA   A HB3  1 
ATOM   2685 H HB3  B ALA   A 1 129 ? 15.443 -3.145  -2.052  0.26 12.43 ?  129 ALA   A HB3  1 
ATOM   2686 N N    A GLY   A 1 130 ? 14.627 -0.792  -3.383  0.74 12.06 ?  130 GLY   A N    1 
ATOM   2687 N N    B GLY   A 1 130 ? 14.888 -0.662  -4.055  0.26 10.31 ?  130 GLY   A N    1 
ATOM   2688 C CA   A GLY   A 1 130 ? 14.550 0.658   -3.336  0.74 12.66 ?  130 GLY   A CA   1 
ATOM   2689 C CA   B GLY   A 1 130 ? 14.867 0.791   -4.008  0.26 10.53 ?  130 GLY   A CA   1 
ATOM   2690 C C    A GLY   A 1 130 ? 15.141 1.281   -4.583  0.74 12.46 ?  130 GLY   A C    1 
ATOM   2691 C C    B GLY   A 1 130 ? 15.550 1.395   -5.217  0.26 10.63 ?  130 GLY   A C    1 
ATOM   2692 O O    A GLY   A 1 130 ? 14.884 0.839   -5.706  0.74 12.42 ?  130 GLY   A O    1 
ATOM   2693 O O    B GLY   A 1 130 ? 15.368 0.950   -6.355  0.26 10.75 ?  130 GLY   A O    1 
ATOM   2694 H H    A GLY   A 1 130 ? 13.862 -1.199  -3.361  0.74 14.47 ?  130 GLY   A H    1 
ATOM   2695 H H    B GLY   A 1 130 ? 14.114 -1.030  -4.124  0.26 12.37 ?  130 GLY   A H    1 
ATOM   2696 H HA2  A GLY   A 1 130 ? 13.617 0.933   -3.255  0.74 15.19 ?  130 GLY   A HA2  1 
ATOM   2697 H HA2  B GLY   A 1 130 ? 13.947 1.106   -3.977  0.26 12.63 ?  130 GLY   A HA2  1 
ATOM   2698 H HA3  A GLY   A 1 130 ? 15.035 0.984   -2.569  0.74 15.19 ?  130 GLY   A HA3  1 
ATOM   2699 H HA3  B GLY   A 1 130 ? 15.325 1.103   -3.214  0.26 12.63 ?  130 GLY   A HA3  1 
ATOM   2700 N N    A ILE   A 1 131 ? 15.949 2.328   -4.385  0.74 12.04 ?  131 ILE   A N    1 
ATOM   2701 N N    B ILE   A 1 131 ? 16.377 2.414   -4.968  0.26 10.96 ?  131 ILE   A N    1 
ATOM   2702 C CA   A ILE   A 1 131 ? 16.511 3.076   -5.506  0.74 11.95 ?  131 ILE   A CA   1 
ATOM   2703 C CA   B ILE   A 1 131 ? 17.019 3.148   -6.052  0.26 10.94 ?  131 ILE   A CA   1 
ATOM   2704 C C    A ILE   A 1 131 ? 17.528 2.285   -6.317  0.74 11.54 ?  131 ILE   A C    1 
ATOM   2705 C C    B ILE   A 1 131 ? 18.013 2.302   -6.833  0.26 11.22 ?  131 ILE   A C    1 
ATOM   2706 O O    A ILE   A 1 131 ? 17.947 2.762   -7.378  0.74 12.27 ?  131 ILE   A O    1 
ATOM   2707 O O    B ILE   A 1 131 ? 18.494 2.749   -7.879  0.26 11.55 ?  131 ILE   A O    1 
ATOM   2708 C CB   A ILE   A 1 131 ? 17.082 4.447   -5.078  0.74 12.60 ?  131 ILE   A CB   1 
ATOM   2709 C CB   B ILE   A 1 131 ? 17.659 4.462   -5.551  0.26 10.89 ?  131 ILE   A CB   1 
ATOM   2710 C CG1  A ILE   A 1 131 ? 18.323 4.293   -4.191  0.74 14.23 ?  131 ILE   A CG1  1 
ATOM   2711 C CG1  B ILE   A 1 131 ? 18.828 4.188   -4.602  0.26 10.86 ?  131 ILE   A CG1  1 
ATOM   2712 C CG2  A ILE   A 1 131 ? 16.009 5.267   -4.373  0.74 13.28 ?  131 ILE   A CG2  1 
ATOM   2713 C CG2  B ILE   A 1 131 ? 16.614 5.333   -4.869  0.26 11.02 ?  131 ILE   A CG2  1 
ATOM   2714 C CD1  A ILE   A 1 131 ? 18.966 5.627   -3.807  0.74 15.75 ?  131 ILE   A CD1  1 
ATOM   2715 C CD1  B ILE   A 1 131 ? 19.525 5.451   -4.129  0.26 11.30 ?  131 ILE   A CD1  1 
ATOM   2716 H H    A ILE   A 1 131 ? 16.164 2.624   -3.614  0.74 14.44 ?  131 ILE   A H    1 
ATOM   2717 H H    B ILE   A 1 131 ? 16.594 2.683   -4.186  0.26 13.15 ?  131 ILE   A H    1 
ATOM   2718 H HA   A ILE   A 1 131 ? 15.780 3.270   -6.112  0.74 14.33 ?  131 ILE   A HA   1 
ATOM   2719 H HA   B ILE   A 1 131 ? 16.332 3.403   -6.682  0.26 13.13 ?  131 ILE   A HA   1 
ATOM   2720 H HB   A ILE   A 1 131 ? 17.338 4.924   -5.879  0.74 15.12 ?  131 ILE   A HB   1 
ATOM   2721 H HB   B ILE   A 1 131 ? 18.000 4.950   -6.315  0.26 13.07 ?  131 ILE   A HB   1 
ATOM   2722 H HG12 A ILE   A 1 131 ? 18.068 3.838   -3.372  0.74 17.07 ?  131 ILE   A HG12 1 
ATOM   2723 H HG12 B ILE   A 1 131 ? 18.498 3.721   -3.820  0.26 13.04 ?  131 ILE   A HG12 1 
ATOM   2724 H HG13 A ILE   A 1 131 ? 18.985 3.771   -4.666  0.74 17.07 ?  131 ILE   A HG13 1 
ATOM   2725 H HG13 B ILE   A 1 131 ? 19.488 3.647   -5.060  0.26 13.04 ?  131 ILE   A HG13 1 
ATOM   2726 H HG21 A ILE   A 1 131 ? 16.321 6.178   -4.271  0.74 15.93 ?  131 ILE   A HG21 1 
ATOM   2727 H HG21 B ILE   A 1 131 ? 16.977 6.223   -4.739  0.26 13.22 ?  131 ILE   A HG21 1 
ATOM   2728 H HG22 A ILE   A 1 131 ? 15.199 5.253   -4.909  0.74 15.93 ?  131 ILE   A HG22 1 
ATOM   2729 H HG22 B ILE   A 1 131 ? 15.829 5.375   -5.434  0.26 13.22 ?  131 ILE   A HG22 1 
ATOM   2730 H HG23 A ILE   A 1 131 ? 15.832 4.876   -3.502  0.74 15.93 ?  131 ILE   A HG23 1 
ATOM   2731 H HG23 B ILE   A 1 131 ? 16.387 4.938   -4.013  0.26 13.22 ?  131 ILE   A HG23 1 
ATOM   2732 H HD11 A ILE   A 1 131 ? 19.809 5.452   -3.357  0.74 18.90 ?  131 ILE   A HD11 1 
ATOM   2733 H HD11 B ILE   A 1 131 ? 20.339 5.207   -3.665  0.26 13.55 ?  131 ILE   A HD11 1 
ATOM   2734 H HD12 A ILE   A 1 131 ? 19.123 6.146   -4.611  0.74 18.90 ?  131 ILE   A HD12 1 
ATOM   2735 H HD12 B ILE   A 1 131 ? 19.733 6.004   -4.899  0.26 13.55 ?  131 ILE   A HD12 1 
ATOM   2736 H HD13 A ILE   A 1 131 ? 18.370 6.110   -3.212  0.74 18.90 ?  131 ILE   A HD13 1 
ATOM   2737 H HD13 B ILE   A 1 131 ? 18.933 5.933   -3.529  0.26 13.55 ?  131 ILE   A HD13 1 
ATOM   2738 N N    A PHE   A 1 132 ? 17.924 1.087   -5.865  0.74 11.05 ?  132 PHE   A N    1 
ATOM   2739 N N    B PHE   A 1 132 ? 18.336 1.096   -6.358  0.26 11.07 ?  132 PHE   A N    1 
ATOM   2740 C CA   A PHE   A 1 132 ? 18.772 0.225   -6.682  0.74 11.13 ?  132 PHE   A CA   1 
ATOM   2741 C CA   B PHE   A 1 132 ? 19.191 0.183   -7.112  0.26 11.02 ?  132 PHE   A CA   1 
ATOM   2742 C C    A PHE   A 1 132 ? 17.992 -0.534  -7.756  0.74 11.73 ?  132 PHE   A C    1 
ATOM   2743 C C    B PHE   A 1 132 ? 18.447 -0.553  -8.224  0.26 11.56 ?  132 PHE   A C    1 
ATOM   2744 O O    A PHE   A 1 132 ? 18.608 -1.179  -8.611  0.74 12.89 ?  132 PHE   A O    1 
ATOM   2745 O O    B PHE   A 1 132 ? 19.097 -1.193  -9.061  0.26 11.90 ?  132 PHE   A O    1 
ATOM   2746 C CB   A PHE   A 1 132 ? 19.565 -0.748  -5.799  0.74 10.90 ?  132 PHE   A CB   1 
ATOM   2747 C CB   B PHE   A 1 132 ? 19.861 -0.826  -6.173  0.26 10.42 ?  132 PHE   A CB   1 
ATOM   2748 C CG   A PHE   A 1 132 ? 20.811 -0.152  -5.163  0.74 11.05 ?  132 PHE   A CG   1 
ATOM   2749 C CG   B PHE   A 1 132 ? 20.960 -0.240  -5.320  0.26 10.79 ?  132 PHE   A CG   1 
ATOM   2750 C CD1  A PHE   A 1 132 ? 20.732 0.892   -4.254  0.74 11.55 ?  132 PHE   A CD1  1 
ATOM   2751 C CD1  B PHE   A 1 132 ? 20.667 0.639   -4.291  0.26 11.22 ?  132 PHE   A CD1  1 
ATOM   2752 C CD2  A PHE   A 1 132 ? 22.057 -0.689  -5.438  0.74 12.27 ?  132 PHE   A CD2  1 
ATOM   2753 C CD2  B PHE   A 1 132 ? 22.283 -0.601  -5.526  0.26 11.23 ?  132 PHE   A CD2  1 
ATOM   2754 C CE1  A PHE   A 1 132 ? 21.877 1.413   -3.662  0.74 11.66 ?  132 PHE   A CE1  1 
ATOM   2755 C CE1  B PHE   A 1 132 ? 21.671 1.167   -3.499  0.26 11.11 ?  132 PHE   A CE1  1 
ATOM   2756 C CE2  A PHE   A 1 132 ? 23.205 -0.175  -4.849  0.74 12.69 ?  132 PHE   A CE2  1 
ATOM   2757 C CE2  B PHE   A 1 132 ? 23.292 -0.077  -4.734  0.26 11.11 ?  132 PHE   A CE2  1 
ATOM   2758 C CZ   A PHE   A 1 132 ? 23.109 0.878   -3.957  0.74 12.28 ?  132 PHE   A CZ   1 
ATOM   2759 C CZ   B PHE   A 1 132 ? 22.983 0.807   -3.719  0.26 10.82 ?  132 PHE   A CZ   1 
ATOM   2760 H H    A PHE   A 1 132 ? 17.715 0.758   -5.095  0.74 13.26 ?  132 PHE   A H    1 
ATOM   2761 H H    B PHE   A 1 132 ? 18.084 0.792   -5.594  0.26 13.28 ?  132 PHE   A H    1 
ATOM   2762 H HA   A PHE   A 1 132 ? 19.417 0.784   -7.133  0.74 13.35 ?  132 PHE   A HA   1 
ATOM   2763 H HA   B PHE   A 1 132 ? 19.897 0.698   -7.526  0.26 13.23 ?  132 PHE   A HA   1 
ATOM   2764 H HB2  A PHE   A 1 132 ? 18.986 -1.059  -5.082  0.74 13.08 ?  132 PHE   A HB2  1 
ATOM   2765 H HB2  B PHE   A 1 132 ? 19.192 -1.186  -5.573  0.26 12.50 ?  132 PHE   A HB2  1 
ATOM   2766 H HB3  A PHE   A 1 132 ? 19.839 -1.506  -6.343  0.74 13.08 ?  132 PHE   A HB3  1 
ATOM   2767 H HB3  B PHE   A 1 132 ? 20.248 -1.542  -6.702  0.26 12.50 ?  132 PHE   A HB3  1 
ATOM   2768 H HD1  A PHE   A 1 132 ? 19.901 1.253   -4.045  0.74 13.86 ?  132 PHE   A HD1  1 
ATOM   2769 H HD1  B PHE   A 1 132 ? 19.784 0.885   -4.134  0.26 13.47 ?  132 PHE   A HD1  1 
ATOM   2770 H HD2  A PHE   A 1 132 ? 22.131 -1.399  -6.043  0.74 14.73 ?  132 PHE   A HD2  1 
ATOM   2771 H HD2  B PHE   A 1 132 ? 22.497 -1.198  -6.209  0.26 13.48 ?  132 PHE   A HD2  1 
ATOM   2772 H HE1  A PHE   A 1 132 ? 21.806 2.116   -3.061  0.74 13.99 ?  132 PHE   A HE1  1 
ATOM   2773 H HE1  B PHE   A 1 132 ? 21.459 1.760   -2.815  0.26 13.34 ?  132 PHE   A HE1  1 
ATOM   2774 H HE2  A PHE   A 1 132 ? 24.037 -0.537  -5.059  0.74 15.23 ?  132 PHE   A HE2  1 
ATOM   2775 H HE2  B PHE   A 1 132 ? 24.177 -0.322  -4.888  0.26 13.33 ?  132 PHE   A HE2  1 
ATOM   2776 H HZ   A PHE   A 1 132 ? 23.874 1.226   -3.565  0.74 14.74 ?  132 PHE   A HZ   1 
ATOM   2777 H HZ   B PHE   A 1 132 ? 23.657 1.160   -3.189  0.26 12.98 ?  132 PHE   A HZ   1 
ATOM   2778 N N    A GLY   A 1 133 ? 16.661 -0.488  -7.735  0.74 11.70 ?  133 GLY   A N    1 
ATOM   2779 N N    B GLY   A 1 133 ? 17.115 -0.504  -8.243  0.26 11.40 ?  133 GLY   A N    1 
ATOM   2780 C CA   A GLY   A 1 133 ? 15.865 -0.856  -8.889  0.74 12.70 ?  133 GLY   A CA   1 
ATOM   2781 C CA   B GLY   A 1 133 ? 16.349 -0.876  -9.414  0.26 11.68 ?  133 GLY   A CA   1 
ATOM   2782 C C    A GLY   A 1 133 ? 15.480 -2.313  -9.039  0.74 12.83 ?  133 GLY   A C    1 
ATOM   2783 C C    B GLY   A 1 133 ? 15.800 -2.287  -9.465  0.26 11.80 ?  133 GLY   A C    1 
ATOM   2784 O O    A GLY   A 1 133 ? 14.732 -2.630  -9.973  0.74 14.22 ?  133 GLY   A O    1 
ATOM   2785 O O    B GLY   A 1 133 ? 15.089 -2.606  -10.425 0.26 11.39 ?  133 GLY   A O    1 
ATOM   2786 H H    A GLY   A 1 133 ? 16.191 -0.242  -7.057  0.74 14.04 ?  133 GLY   A H    1 
ATOM   2787 H H    B GLY   A 1 133 ? 16.631 -0.247  -7.579  0.26 13.68 ?  133 GLY   A H    1 
ATOM   2788 H HA2  A GLY   A 1 133 ? 15.034 -0.357  -8.867  0.74 15.24 ?  133 GLY   A HA2  1 
ATOM   2789 H HA2  B GLY   A 1 133 ? 15.601 -0.264  -9.499  0.26 14.01 ?  133 GLY   A HA2  1 
ATOM   2790 H HA3  A GLY   A 1 133 ? 16.341 -0.595  -9.694  0.74 15.24 ?  133 GLY   A HA3  1 
ATOM   2791 H HA3  B GLY   A 1 133 ? 16.908 -0.765  -10.198 0.26 14.01 ?  133 GLY   A HA3  1 
ATOM   2792 N N    A ALA   A 1 134 ? 15.955 -3.213  -8.177  0.74 12.80 ?  134 ALA   A N    1 
ATOM   2793 N N    B ALA   A 1 134 ? 16.104 -3.145  -8.493  0.26 12.07 ?  134 ALA   A N    1 
ATOM   2794 C CA   A ALA   A 1 134 ? 15.606 -4.615  -8.343  0.74 13.59 ?  134 ALA   A CA   1 
ATOM   2795 C CA   B ALA   A 1 134 ? 15.624 -4.520  -8.528  0.26 11.96 ?  134 ALA   A CA   1 
ATOM   2796 C C    A ALA   A 1 134 ? 14.242 -4.907  -7.718  0.74 14.06 ?  134 ALA   A C    1 
ATOM   2797 C C    B ALA   A 1 134 ? 14.362 -4.698  -7.686  0.26 11.58 ?  134 ALA   A C    1 
ATOM   2798 O O    A ALA   A 1 134 ? 13.693 -4.121  -6.940  0.74 14.99 ?  134 ALA   A O    1 
ATOM   2799 O O    B ALA   A 1 134 ? 14.017 -3.865  -6.842  0.26 11.92 ?  134 ALA   A O    1 
ATOM   2800 C CB   A ALA   A 1 134 ? 16.679 -5.526  -7.745  0.74 14.62 ?  134 ALA   A CB   1 
ATOM   2801 C CB   B ALA   A 1 134 ? 16.706 -5.494  -8.058  0.26 12.56 ?  134 ALA   A CB   1 
ATOM   2802 H H    A ALA   A 1 134 ? 16.476 -3.039  -7.507  0.74 15.36 ?  134 ALA   A H    1 
ATOM   2803 H H    B ALA   A 1 134 ? 16.606 -2.959  -7.810  0.26 14.49 ?  134 ALA   A H    1 
ATOM   2804 H HA   A ALA   A 1 134 ? 15.548 -4.812  -9.290  0.74 16.30 ?  134 ALA   A HA   1 
ATOM   2805 H HA   B ALA   A 1 134 ? 15.407 -4.745  -9.447  0.26 14.35 ?  134 ALA   A HA   1 
ATOM   2806 H HB1  A ALA   A 1 134 ? 16.424 -6.450  -7.891  0.74 17.55 ?  134 ALA   A HB1  1 
ATOM   2807 H HB1  B ALA   A 1 134 ? 16.356 -6.397  -8.113  0.26 15.07 ?  134 ALA   A HB1  1 
ATOM   2808 H HB2  A ALA   A 1 134 ? 17.528 -5.346  -8.187  0.74 17.55 ?  134 ALA   A HB2  1 
ATOM   2809 H HB2  B ALA   A 1 134 ? 17.482 -5.403  -8.633  0.26 15.07 ?  134 ALA   A HB2  1 
ATOM   2810 H HB3  A ALA   A 1 134 ? 16.758 -5.347  -6.798  0.74 17.55 ?  134 ALA   A HB3  1 
ATOM   2811 H HB3  B ALA   A 1 134 ? 16.942 -5.283  -7.144  0.26 15.07 ?  134 ALA   A HB3  1 
ATOM   2812 N N    A ASP   A 1 135 ? 13.695 -6.063  -8.077  0.74 14.64 ?  135 ASP   A N    1 
ATOM   2813 N N    B ASP   A 1 135 ? 13.682 -5.820  -7.928  0.26 11.90 ?  135 ASP   A N    1 
ATOM   2814 C CA   A ASP   A 1 135 ? 12.432 -6.533  -7.514  0.74 15.63 ?  135 ASP   A CA   1 
ATOM   2815 C CA   B ASP   A 1 135 ? 12.423 -6.134  -7.257  0.26 12.42 ?  135 ASP   A CA   1 
ATOM   2816 C C    A ASP   A 1 135 ? 12.669 -7.004  -6.084  0.74 15.20 ?  135 ASP   A C    1 
ATOM   2817 C C    B ASP   A 1 135 ? 12.697 -6.569  -5.821  0.26 11.89 ?  135 ASP   A C    1 
ATOM   2818 O O    A ASP   A 1 135 ? 13.442 -7.949  -5.877  0.74 14.74 ?  135 ASP   A O    1 
ATOM   2819 O O    B ASP   A 1 135 ? 13.431 -7.543  -5.610  0.26 11.95 ?  135 ASP   A O    1 
ATOM   2820 C CB   A ASP   A 1 135 ? 11.926 -7.690  -8.371  0.74 18.13 ?  135 ASP   A CB   1 
ATOM   2821 C CB   B ASP   A 1 135 ? 11.728 -7.266  -8.006  0.26 13.27 ?  135 ASP   A CB   1 
ATOM   2822 C CG   A ASP   A 1 135 ? 10.653 -8.334  -7.827  0.74 20.58 ?  135 ASP   A CG   1 
ATOM   2823 C CG   B ASP   A 1 135 ? 10.296 -7.491  -7.549  0.26 14.27 ?  135 ASP   A CG   1 
ATOM   2824 O OD1  A ASP   A 1 135 ? 10.099 -7.856  -6.817  0.74 20.67 ?  135 ASP   A OD1  1 
ATOM   2825 O OD1  B ASP   A 1 135 ? 9.958  -7.094  -6.414  0.26 14.50 ?  135 ASP   A OD1  1 
ATOM   2826 O OD2  A ASP   A 1 135 ? 10.204 -9.332  -8.429  0.74 23.10 -1 135 ASP   A OD2  1 
ATOM   2827 O OD2  B ASP   A 1 135 ? 9.514  -8.086  -8.325  0.26 14.94 -1 135 ASP   A OD2  1 
ATOM   2828 H H    A ASP   A 1 135 ? 14.041 -6.600  -8.647  0.74 17.57 ?  135 ASP   A H    1 
ATOM   2829 H H    B ASP   A 1 135 ? 13.927 -6.421  -8.488  0.26 14.28 ?  135 ASP   A H    1 
ATOM   2830 H HA   A ASP   A 1 135 ? 11.776 -5.815  -7.531  0.74 18.75 ?  135 ASP   A HA   1 
ATOM   2831 H HA   B ASP   A 1 135 ? 11.844 -5.352  -7.266  0.26 14.90 ?  135 ASP   A HA   1 
ATOM   2832 H HB2  A ASP   A 1 135 ? 11.734 -7.358  -9.261  0.74 21.75 ?  135 ASP   A HB2  1 
ATOM   2833 H HB2  B ASP   A 1 135 ? 11.733 -7.062  -8.955  0.26 15.92 ?  135 ASP   A HB2  1 
ATOM   2834 H HB3  A ASP   A 1 135 ? 12.611 -8.372  -8.409  0.74 21.75 ?  135 ASP   A HB3  1 
ATOM   2835 H HB3  B ASP   A 1 135 ? 12.204 -8.093  -7.842  0.26 15.92 ?  135 ASP   A HB3  1 
ATOM   2836 N N    A PRO   A 1 136 ? 12.051 -6.383  -5.075  0.74 15.14 ?  136 PRO   A N    1 
ATOM   2837 N N    B PRO   A 1 136 ? 12.128 -5.897  -4.814  0.26 11.50 ?  136 PRO   A N    1 
ATOM   2838 C CA   A PRO   A 1 136 ? 12.305 -6.814  -3.688  0.74 15.20 ?  136 PRO   A CA   1 
ATOM   2839 C CA   B PRO   A 1 136 ? 12.360 -6.327  -3.423  0.26 11.58 ?  136 PRO   A CA   1 
ATOM   2840 C C    A PRO   A 1 136 ? 11.881 -8.241  -3.386  0.74 14.56 ?  136 PRO   A C    1 
ATOM   2841 C C    B PRO   A 1 136 ? 11.921 -7.756  -3.144  0.26 11.26 ?  136 PRO   A C    1 
ATOM   2842 O O    A PRO   A 1 136 ? 12.477 -8.877  -2.508  0.74 14.41 ?  136 PRO   A O    1 
ATOM   2843 O O    B PRO   A 1 136 ? 12.518 -8.426  -2.291  0.26 11.11 ?  136 PRO   A O    1 
ATOM   2844 C CB   A PRO   A 1 136 ? 11.521 -5.792  -2.853  0.74 16.12 ?  136 PRO   A CB   1 
ATOM   2845 C CB   B PRO   A 1 136 ? 11.571 -5.296  -2.597  0.26 12.04 ?  136 PRO   A CB   1 
ATOM   2846 C CG   A PRO   A 1 136 ? 10.486 -5.243  -3.791  0.74 17.15 ?  136 PRO   A CG   1 
ATOM   2847 C CG   B PRO   A 1 136 ? 10.583 -4.701  -3.560  0.26 12.35 ?  136 PRO   A CG   1 
ATOM   2848 C CD   A PRO   A 1 136 ? 11.121 -5.243  -5.142  0.74 16.18 ?  136 PRO   A CD   1 
ATOM   2849 C CD   B PRO   A 1 136 ? 11.277 -4.697  -4.882  0.26 11.97 ?  136 PRO   A CD   1 
ATOM   2850 H HA   A PRO   A 1 136 ? 13.249 -6.725  -3.484  0.74 18.25 ?  136 PRO   A HA   1 
ATOM   2851 H HA   B PRO   A 1 136 ? 13.301 -6.234  -3.200  0.26 13.90 ?  136 PRO   A HA   1 
ATOM   2852 H HB2  A PRO   A 1 136 ? 11.102 -6.239  -2.099  0.74 19.34 ?  136 PRO   A HB2  1 
ATOM   2853 H HB2  B PRO   A 1 136 ? 11.112 -5.733  -1.864  0.26 14.45 ?  136 PRO   A HB2  1 
ATOM   2854 H HB3  A PRO   A 1 136 ? 12.121 -5.094  -2.548  0.74 19.34 ?  136 PRO   A HB3  1 
ATOM   2855 H HB3  B PRO   A 1 136 ? 12.171 -4.605  -2.260  0.26 14.45 ?  136 PRO   A HB3  1 
ATOM   2856 H HG2  A PRO   A 1 136 ? 9.706  -5.815  -3.783  0.74 20.58 ?  136 PRO   A HG2  1 
ATOM   2857 H HG2  B PRO   A 1 136 ? 9.787  -5.256  -3.595  0.26 14.83 ?  136 PRO   A HG2  1 
ATOM   2858 H HG3  A PRO   A 1 136 ? 10.258 -4.341  -3.526  0.74 20.58 ?  136 PRO   A HG3  1 
ATOM   2859 H HG3  B PRO   A 1 136 ? 10.356 -3.797  -3.288  0.26 14.83 ?  136 PRO   A HG3  1 
ATOM   2860 H HD2  A PRO   A 1 136 ? 10.449 -5.395  -5.828  0.74 19.42 ?  136 PRO   A HD2  1 
ATOM   2861 H HD2  B PRO   A 1 136 ? 10.629 -4.777  -5.600  0.26 14.36 ?  136 PRO   A HD2  1 
ATOM   2862 H HD3  A PRO   A 1 136 ? 11.607 -4.420  -5.295  0.74 19.42 ?  136 PRO   A HD3  1 
ATOM   2863 H HD3  B PRO   A 1 136 ? 11.819 -3.895  -4.982  0.26 14.36 ?  136 PRO   A HD3  1 
ATOM   2864 N N    A ILE   A 1 137 ? 10.854 -8.759  -4.061  0.74 14.46 ?  137 ILE   A N    1 
ATOM   2865 N N    B ILE   A 1 137 ? 10.893 -8.248  -3.839  0.26 11.27 ?  137 ILE   A N    1 
ATOM   2866 C CA   A ILE   A 1 137 ? 10.481 -10.156 -3.866  0.74 15.15 ?  137 ILE   A CA   1 
ATOM   2867 C CA   B ILE   A 1 137 ? 10.498 -9.647  -3.694  0.26 11.96 ?  137 ILE   A CA   1 
ATOM   2868 C C    A ILE   A 1 137 ? 11.623 -11.070 -4.289  0.74 14.50 ?  137 ILE   A C    1 
ATOM   2869 C C    B ILE   A 1 137 ? 11.661 -10.560 -4.057  0.26 11.57 ?  137 ILE   A C    1 
ATOM   2870 O O    A ILE   A 1 137 ? 11.940 -12.054 -3.609  0.74 14.51 ?  137 ILE   A O    1 
ATOM   2871 O O    B ILE   A 1 137 ? 11.941 -11.549 -3.369  0.26 11.84 ?  137 ILE   A O    1 
ATOM   2872 C CB   A ILE   A 1 137 ? 9.170  -10.476 -4.611  0.74 16.55 ?  137 ILE   A CB   1 
ATOM   2873 C CB   B ILE   A 1 137 ? 9.263  -9.940  -4.568  0.26 13.14 ?  137 ILE   A CB   1 
ATOM   2874 C CG1  A ILE   A 1 137 ? 8.016  -9.625  -4.058  0.74 18.14 ?  137 ILE   A CG1  1 
ATOM   2875 C CG1  B ILE   A 1 137 ? 8.073  -9.071  -4.144  0.26 14.27 ?  137 ILE   A CG1  1 
ATOM   2876 C CG2  A ILE   A 1 137 ? 8.853  -11.966 -4.502  0.74 17.15 ?  137 ILE   A CG2  1 
ATOM   2877 C CG2  B ILE   A 1 137 ? 8.922  -11.423 -4.518  0.26 13.31 ?  137 ILE   A CG2  1 
ATOM   2878 C CD1  A ILE   A 1 137 ? 6.716  -9.762  -4.817  0.74 19.73 ?  137 ILE   A CD1  1 
ATOM   2879 C CD1  B ILE   A 1 137 ? 6.835  -9.310  -4.979  0.26 15.10 ?  137 ILE   A CD1  1 
ATOM   2880 H H    A ILE   A 1 137 ? 10.369 -8.335  -4.623  0.74 17.35 ?  137 ILE   A H    1 
ATOM   2881 H H    B ILE   A 1 137 ? 10.421 -7.791  -4.392  0.26 13.52 ?  137 ILE   A H    1 
ATOM   2882 H HA   A ILE   A 1 137 ? 10.327 -10.317 -2.925  0.74 18.18 ?  137 ILE   A HA   1 
ATOM   2883 H HA   B ILE   A 1 137 ? 10.259 -9.808  -2.768  0.26 14.35 ?  137 ILE   A HA   1 
ATOM   2884 H HB   A ILE   A 1 137 ? 9.287  -10.263 -5.548  0.74 19.86 ?  137 ILE   A HB   1 
ATOM   2885 H HB   B ILE   A 1 137 ? 9.487  -9.709  -5.481  0.26 15.77 ?  137 ILE   A HB   1 
ATOM   2886 H HG12 A ILE   A 1 137 ? 7.855  -9.881  -3.138  0.74 21.76 ?  137 ILE   A HG12 1 
ATOM   2887 H HG12 B ILE   A 1 137 ? 7.852  -9.265  -3.221  0.26 17.13 ?  137 ILE   A HG12 1 
ATOM   2888 H HG13 A ILE   A 1 137 ? 8.283  -8.690  -4.094  0.74 21.76 ?  137 ILE   A HG13 1 
ATOM   2889 H HG13 B ILE   A 1 137 ? 8.314  -8.134  -4.237  0.26 17.13 ?  137 ILE   A HG13 1 
ATOM   2890 H HG21 A ILE   A 1 137 ? 7.939  -12.126 -4.790  0.74 20.58 ?  137 ILE   A HG21 1 
ATOM   2891 H HG21 B ILE   A 1 137 ? 8.084  -11.576 -4.979  0.26 15.97 ?  137 ILE   A HG21 1 
ATOM   2892 H HG22 A ILE   A 1 137 ? 9.461  -12.463 -5.069  0.74 20.58 ?  137 ILE   A HG22 1 
ATOM   2893 H HG22 B ILE   A 1 137 ? 9.627  -11.922 -4.955  0.26 15.97 ?  137 ILE   A HG22 1 
ATOM   2894 H HG23 A ILE   A 1 137 ? 8.955  -12.243 -3.579  0.74 20.58 ?  137 ILE   A HG23 1 
ATOM   2895 H HG23 B ILE   A 1 137 ? 8.844  -11.694 -3.592  0.26 15.97 ?  137 ILE   A HG23 1 
ATOM   2896 H HD11 A ILE   A 1 137 ? 6.027  -10.057 -4.205  0.74 23.67 ?  137 ILE   A HD11 1 
ATOM   2897 H HD11 B ILE   A 1 137 ? 6.419  -8.461  -5.172  0.26 18.12 ?  137 ILE   A HD11 1 
ATOM   2898 H HD12 A ILE   A 1 137 ? 6.489  -8.898  -5.190  0.74 23.67 ?  137 ILE   A HD12 1 
ATOM   2899 H HD12 B ILE   A 1 137 ? 7.094  -9.746  -5.809  0.26 18.12 ?  137 ILE   A HD12 1 
ATOM   2900 H HD13 A ILE   A 1 137 ? 6.831  -10.407 -5.531  0.74 23.67 ?  137 ILE   A HD13 1 
ATOM   2901 H HD13 B ILE   A 1 137 ? 6.226  -9.883  -4.485  0.26 18.12 ?  137 ILE   A HD13 1 
ATOM   2902 N N    A HIS   A 1 138 ? 12.263 -10.753 -5.418  0.74 14.28 ?  138 HIS   A N    1 
ATOM   2903 N N    B HIS   A 1 138 ? 12.342 -10.247 -5.161  0.26 11.31 ?  138 HIS   A N    1 
ATOM   2904 C CA   A HIS   A 1 138 ? 13.420 -11.526 -5.857  0.74 13.88 ?  138 HIS   A CA   1 
ATOM   2905 C CA   B HIS   A 1 138 ? 13.498 -11.027 -5.590  0.26 11.14 ?  138 HIS   A CA   1 
ATOM   2906 C C    A HIS   A 1 138 ? 14.573 -11.402 -4.870  0.74 13.03 ?  138 HIS   A C    1 
ATOM   2907 C C    B HIS   A 1 138 ? 14.647 -10.907 -4.597  0.26 10.35 ?  138 HIS   A C    1 
ATOM   2908 O O    A HIS   A 1 138 ? 15.236 -12.396 -4.547  0.74 13.34 ?  138 HIS   A O    1 
ATOM   2909 O O    B HIS   A 1 138 ? 15.358 -11.887 -4.338  0.26 10.48 ?  138 HIS   A O    1 
ATOM   2910 C CB   A HIS   A 1 138 ? 13.849 -11.070 -7.250  0.74 14.71 ?  138 HIS   A CB   1 
ATOM   2911 C CB   B HIS   A 1 138 ? 13.927 -10.550 -6.977  0.26 11.94 ?  138 HIS   A CB   1 
ATOM   2912 C CG   A HIS   A 1 138 ? 15.123 -11.700 -7.713  0.74 15.39 ?  138 HIS   A CG   1 
ATOM   2913 C CG   B HIS   A 1 138 ? 15.151 -11.230 -7.504  0.26 13.05 ?  138 HIS   A CG   1 
ATOM   2914 N ND1  A HIS   A 1 138 ? 15.238 -13.052 -7.960  0.74 16.50 ?  138 HIS   A ND1  1 
ATOM   2915 N ND1  B HIS   A 1 138 ? 15.189 -12.577 -7.794  0.26 13.65 ?  138 HIS   A ND1  1 
ATOM   2916 C CD2  A HIS   A 1 138 ? 16.345 -11.169 -7.951  0.74 15.77 ?  138 HIS   A CD2  1 
ATOM   2917 C CD2  B HIS   A 1 138 ? 16.381 -10.746 -7.799  0.26 13.52 ?  138 HIS   A CD2  1 
ATOM   2918 C CE1  A HIS   A 1 138 ? 16.473 -13.324 -8.341  0.74 16.99 ?  138 HIS   A CE1  1 
ATOM   2919 C CE1  B HIS   A 1 138 ? 16.391 -12.893 -8.243  0.26 13.79 ?  138 HIS   A CE1  1 
ATOM   2920 N NE2  A HIS   A 1 138 ? 17.165 -12.199 -8.345  0.74 16.20 ?  138 HIS   A NE2  1 
ATOM   2921 N NE2  B HIS   A 1 138 ? 17.132 -11.801 -8.256  0.26 13.73 ?  138 HIS   A NE2  1 
ATOM   2922 H H    A HIS   A 1 138 ? 12.045 -10.107 -5.944  0.74 17.14 ?  138 HIS   A H    1 
ATOM   2923 H H    B HIS   A 1 138 ? 12.143 -9.590  -5.679  0.26 13.57 ?  138 HIS   A H    1 
ATOM   2924 H HA   A HIS   A 1 138 ? 13.169 -12.463 -5.923  0.74 16.65 ?  138 HIS   A HA   1 
ATOM   2925 H HA   B HIS   A 1 138 ? 13.249 -11.956 -5.649  0.26 13.37 ?  138 HIS   A HA   1 
ATOM   2926 H HB2  A HIS   A 1 138 ? 13.152 -11.302 -7.890  0.74 17.65 ?  138 HIS   A HB2  1 
ATOM   2927 H HB2  B HIS   A 1 138 ? 13.202 -10.716 -7.599  0.26 14.32 ?  138 HIS   A HB2  1 
ATOM   2928 H HB3  A HIS   A 1 138 ? 13.977 -10.109 -7.242  0.74 17.65 ?  138 HIS   A HB3  1 
ATOM   2929 H HB3  B HIS   A 1 138 ? 14.110 -9.595  -6.938  0.26 14.32 ?  138 HIS   A HB3  1 
ATOM   2930 H HD1  A HIS   A 1 138 ? 14.603 -13.627 -7.884  0.74 19.81 ?  138 HIS   A HD1  1 
ATOM   2931 H HD2  A HIS   A 1 138 ? 16.579 -10.271 -7.867  0.74 18.92 ?  138 HIS   A HD2  1 
ATOM   2932 H HD2  B HIS   A 1 138 ? 16.663 -9.863  -7.710  0.26 16.23 ?  138 HIS   A HD2  1 
ATOM   2933 H HE1  A HIS   A 1 138 ? 16.800 -14.161 -8.568  0.74 20.39 ?  138 HIS   A HE1  1 
ATOM   2934 H HE1  B HIS   A 1 138 ? 16.664 -13.741 -8.504  0.26 16.55 ?  138 HIS   A HE1  1 
ATOM   2935 H HE2  B HIS   A 1 138 ? 17.951 -11.757 -8.510  0.26 16.48 ?  138 HIS   A HE2  1 
ATOM   2936 N N    A SER   A 1 139 ? 14.829 -10.190 -4.380  0.74 12.49 ?  139 SER   A N    1 
ATOM   2937 N N    B SER   A 1 139 ? 14.839 -9.713  -4.029  0.26 10.07 ?  139 SER   A N    1 
ATOM   2938 C CA   A SER   A 1 139 ? 15.909 -10.005 -3.419  0.74 12.23 ?  139 SER   A CA   1 
ATOM   2939 C CA   B SER   A 1 139 ? 15.911 -9.512  -3.061  0.26 9.85  ?  139 SER   A CA   1 
ATOM   2940 C C    A SER   A 1 139 ? 15.693 -10.849 -2.172  0.74 11.90 ?  139 SER   A C    1 
ATOM   2941 C C    B SER   A 1 139 ? 15.708 -10.387 -1.830  0.26 9.73  ?  139 SER   A C    1 
ATOM   2942 O O    A SER   A 1 139 ? 16.644 -11.439 -1.645  0.74 11.58 ?  139 SER   A O    1 
ATOM   2943 O O    B SER   A 1 139 ? 16.656 -11.012 -1.338  0.26 10.04 ?  139 SER   A O    1 
ATOM   2944 C CB   A SER   A 1 139 ? 16.039 -8.533  -3.050  0.74 12.05 ?  139 SER   A CB   1 
ATOM   2945 C CB   B SER   A 1 139 ? 15.994 -8.032  -2.680  0.26 10.20 ?  139 SER   A CB   1 
ATOM   2946 O OG   A SER   A 1 139 ? 17.139 -8.362  -2.175  0.74 11.94 ?  139 SER   A OG   1 
ATOM   2947 O OG   B SER   A 1 139 ? 17.014 -7.822  -1.721  0.26 10.36 ?  139 SER   A OG   1 
ATOM   2948 H H    A SER   A 1 139 ? 14.400 -9.477  -4.585  0.74 14.99 ?  139 SER   A H    1 
ATOM   2949 H H    B SER   A 1 139 ? 14.365 -9.008  -4.180  0.26 12.08 ?  139 SER   A H    1 
ATOM   2950 H HA   A SER   A 1 139 ? 16.743 -10.288 -3.826  0.74 14.67 ?  139 SER   A HA   1 
ATOM   2951 H HA   B SER   A 1 139 ? 16.755 -9.758  -3.462  0.26 11.83 ?  139 SER   A HA   1 
ATOM   2952 H HB2  A SER   A 1 139 ? 16.184 -8.015  -3.854  0.74 14.47 ?  139 SER   A HB2  1 
ATOM   2953 H HB2  B SER   A 1 139 ? 16.193 -7.506  -3.476  0.26 12.25 ?  139 SER   A HB2  1 
ATOM   2954 H HB3  A SER   A 1 139 ? 15.226 -8.245  -2.604  0.74 14.47 ?  139 SER   A HB3  1 
ATOM   2955 H HB3  B SER   A 1 139 ? 15.146 -7.744  -2.305  0.26 12.25 ?  139 SER   A HB3  1 
ATOM   2956 H HG   A SER   A 1 139 ? 17.216 -7.555  -1.965  0.74 14.33 ?  139 SER   A HG   1 
ATOM   2957 H HG   B SER   A 1 139 ? 17.769 -7.887  -2.082  0.26 12.44 ?  139 SER   A HG   1 
ATOM   2958 N N    A LEU   A 1 140 ? 14.454 -10.915 -1.680  0.74 11.91 ?  140 LEU   A N    1 
ATOM   2959 N N    B LEU   A 1 140 ? 14.476 -10.446 -1.317  0.26 9.39  ?  140 LEU   A N    1 
ATOM   2960 C CA   A LEU   A 1 140 ? 14.173 -11.742 -0.510  0.74 11.62 ?  140 LEU   A CA   1 
ATOM   2961 C CA   B LEU   A 1 140 ? 14.199 -11.299 -0.163  0.26 9.16  ?  140 LEU   A CA   1 
ATOM   2962 C C    A LEU   A 1 140 ? 14.428 -13.211 -0.810  0.74 11.44 ?  140 LEU   A C    1 
ATOM   2963 C C    B LEU   A 1 140 ? 14.457 -12.770 -0.483  0.26 9.44  ?  140 LEU   A C    1 
ATOM   2964 O O    A LEU   A 1 140 ? 15.003 -13.934 0.015   0.74 11.96 ?  140 LEU   A O    1 
ATOM   2965 O O    B LEU   A 1 140 ? 14.949 -13.524 0.366   0.26 9.70  ?  140 LEU   A O    1 
ATOM   2966 C CB   A LEU   A 1 140 ? 12.728 -11.534 -0.062  0.74 12.34 ?  140 LEU   A CB   1 
ATOM   2967 C CB   B LEU   A 1 140 ? 12.754 -11.085 0.292   0.26 8.72  ?  140 LEU   A CB   1 
ATOM   2968 C CG   A LEU   A 1 140 ? 12.273 -12.399 1.114   0.74 12.97 ?  140 LEU   A CG   1 
ATOM   2969 C CG   B LEU   A 1 140 ? 12.253 -12.016 1.394   0.26 8.85  ?  140 LEU   A CG   1 
ATOM   2970 C CD1  A LEU   A 1 140 ? 13.185 -12.232 2.319   0.74 13.29 ?  140 LEU   A CD1  1 
ATOM   2971 C CD1  B LEU   A 1 140 ? 13.092 -11.860 2.648   0.26 8.55  ?  140 LEU   A CD1  1 
ATOM   2972 C CD2  A LEU   A 1 140 ? 10.827 -12.062 1.483   0.74 14.22 ?  140 LEU   A CD2  1 
ATOM   2973 C CD2  B LEU   A 1 140 ? 10.785 -11.749 1.683   0.26 9.62  ?  140 LEU   A CD2  1 
ATOM   2974 H H    A LEU   A 1 140 ? 13.771 -10.504 -1.995  0.74 14.30 ?  140 LEU   A H    1 
ATOM   2975 H H    B LEU   A 1 140 ? 13.796 -10.004 -1.614  0.26 11.26 ?  140 LEU   A H    1 
ATOM   2976 H HA   A LEU   A 1 140 ? 14.753 -11.485 0.218   0.74 13.94 ?  140 LEU   A HA   1 
ATOM   2977 H HA   B LEU   A 1 140 ? 14.779 -11.032 0.569   0.26 10.99 ?  140 LEU   A HA   1 
ATOM   2978 H HB2  A LEU   A 1 140 ? 12.616 -10.613 0.201   0.74 14.80 ?  140 LEU   A HB2  1 
ATOM   2979 H HB2  B LEU   A 1 140 ? 12.664 -10.173 0.623   0.26 10.46 ?  140 LEU   A HB2  1 
ATOM   2980 H HB3  A LEU   A 1 140 ? 12.139 -11.736 -0.809  0.74 14.80 ?  140 LEU   A HB3  1 
ATOM   2981 H HB3  B LEU   A 1 140 ? 12.170 -11.201 -0.474  0.26 10.46 ?  140 LEU   A HB3  1 
ATOM   2982 H HG   A LEU   A 1 140 ? 12.287 -13.336 0.851   0.74 15.56 ?  140 LEU   A HG   1 
ATOM   2983 H HG   B LEU   A 1 140 ? 12.329 -12.932 1.091   0.26 10.62 ?  140 LEU   A HG   1 
ATOM   2984 H HD11 A LEU   A 1 140 ? 12.790 -12.692 3.078   0.74 15.95 ?  140 LEU   A HD11 1 
ATOM   2985 H HD11 B LEU   A 1 140 ? 12.716 -12.420 3.345   0.26 10.26 ?  140 LEU   A HD11 1 
ATOM   2986 H HD12 A LEU   A 1 140 ? 14.048 -12.619 2.112   0.74 15.95 ?  140 LEU   A HD12 1 
ATOM   2987 H HD12 B LEU   A 1 140 ? 13.999 -12.137 2.454   0.26 10.26 ?  140 LEU   A HD12 1 
ATOM   2988 H HD13 A LEU   A 1 140 ? 13.276 -11.290 2.514   0.74 15.95 ?  140 LEU   A HD13 1 
ATOM   2989 H HD13 B LEU   A 1 140 ? 13.075 -10.932 2.923   0.26 10.26 ?  140 LEU   A HD13 1 
ATOM   2990 H HD21 A LEU   A 1 140 ? 10.546 -12.617 2.230   0.74 17.07 ?  140 LEU   A HD21 1 
ATOM   2991 H HD21 B LEU   A 1 140 ? 10.448 -12.446 2.270   0.26 11.55 ?  140 LEU   A HD21 1 
ATOM   2992 H HD22 A LEU   A 1 140 ? 10.773 -11.125 1.734   0.74 17.07 ?  140 LEU   A HD22 1 
ATOM   2993 H HD22 B LEU   A 1 140 ? 10.699 -10.885 2.110   0.26 11.55 ?  140 LEU   A HD22 1 
ATOM   2994 H HD23 A LEU   A 1 140 ? 10.251 -12.229 0.717   0.74 17.07 ?  140 LEU   A HD23 1 
ATOM   2995 H HD23 B LEU   A 1 140 ? 10.290 -11.759 0.846   0.26 11.55 ?  140 LEU   A HD23 1 
ATOM   2996 N N    A ARG   A 1 141 ? 14.004 -13.669 -1.988  0.74 12.16 ?  141 ARG   A N    1 
ATOM   2997 N N    B ARG   A 1 141 ? 14.129 -13.193 -1.705  0.26 9.89  ?  141 ARG   A N    1 
ATOM   2998 C CA   A ARG   A 1 141 ? 14.271 -15.042 -2.390  0.74 13.67 ?  141 ARG   A CA   1 
ATOM   2999 C CA   B ARG   A 1 141 ? 14.268 -14.595 -2.096  0.26 10.85 ?  141 ARG   A CA   1 
ATOM   3000 C C    A ARG   A 1 141 ? 15.767 -15.308 -2.394  0.74 12.64 ?  141 ARG   A C    1 
ATOM   3001 C C    B ARG   A 1 141 ? 15.736 -15.034 -2.111  0.26 11.17 ?  141 ARG   A C    1 
ATOM   3002 O O    A ARG   A 1 141 ? 16.224 -16.338 -1.883  0.74 12.18 ?  141 ARG   A O    1 
ATOM   3003 O O    B ARG   A 1 141 ? 16.126 -15.979 -1.412  0.26 10.61 ?  141 ARG   A O    1 
ATOM   3004 C CB   A ARG   A 1 141 ? 13.679 -15.282 -3.780  0.74 15.52 ?  141 ARG   A CB   1 
ATOM   3005 C CB   B ARG   A 1 141 ? 13.611 -14.784 -3.468  0.26 11.94 ?  141 ARG   A CB   1 
ATOM   3006 C CG   A ARG   A 1 141 ? 13.631 -16.734 -4.221  0.74 18.21 ?  141 ARG   A CG   1 
ATOM   3007 C CG   B ARG   A 1 141 ? 13.588 -16.201 -3.992  0.26 13.24 ?  141 ARG   A CG   1 
ATOM   3008 C CD   A ARG   A 1 141 ? 12.586 -17.486 -3.444  0.74 19.87 ?  141 ARG   A CD   1 
ATOM   3009 C CD   B ARG   A 1 141 ? 12.559 -17.040 -3.268  0.26 14.19 ?  141 ARG   A CD   1 
ATOM   3010 N NE   A ARG   A 1 141 ? 13.190 -18.304 -2.404  0.74 20.86 ?  141 ARG   A NE   1 
ATOM   3011 N NE   B ARG   A 1 141 ? 13.175 -17.912 -2.278  0.26 14.42 ?  141 ARG   A NE   1 
ATOM   3012 C CZ   A ARG   A 1 141 ? 12.518 -18.834 -1.392  0.74 21.45 ?  141 ARG   A CZ   1 
ATOM   3013 C CZ   B ARG   A 1 141 ? 12.499 -18.714 -1.469  0.26 15.66 ?  141 ARG   A CZ   1 
ATOM   3014 N NH1  A ARG   A 1 141 ? 11.232 -18.579 -1.207  0.74 21.33 ?  141 ARG   A NH1  1 
ATOM   3015 N NH1  B ARG   A 1 141 ? 11.176 -18.742 -1.471  0.26 16.47 ?  141 ARG   A NH1  1 
ATOM   3016 N NH2  A ARG   A 1 141 ? 13.152 -19.635 -0.542  0.74 22.02 ?  141 ARG   A NH2  1 
ATOM   3017 N NH2  B ARG   A 1 141 ? 13.166 -19.511 -0.640  0.26 16.05 ?  141 ARG   A NH2  1 
ATOM   3018 H H    A ARG   A 1 141 ? 13.565 -13.219 -2.564  0.74 14.60 ?  141 ARG   A H    1 
ATOM   3019 H H    B ARG   A 1 141 ? 13.803 -12.679 -2.318  0.26 11.87 ?  141 ARG   A H    1 
ATOM   3020 H HA   A ARG   A 1 141 ? 13.858 -15.666 -1.770  0.74 16.40 ?  141 ARG   A HA   1 
ATOM   3021 H HA   B ARG   A 1 141 ? 13.791 -15.142 -1.458  0.26 13.02 ?  141 ARG   A HA   1 
ATOM   3022 H HB2  A ARG   A 1 141 ? 12.772 -14.944 -3.794  0.74 18.63 ?  141 ARG   A HB2  1 
ATOM   3023 H HB2  B ARG   A 1 141 ? 12.688 -14.474 -3.416  0.26 14.33 ?  141 ARG   A HB2  1 
ATOM   3024 H HB3  A ARG   A 1 141 ? 14.214 -14.804 -4.431  0.74 18.63 ?  141 ARG   A HB3  1 
ATOM   3025 H HB3  B ARG   A 1 141 ? 14.089 -14.242 -4.115  0.26 14.33 ?  141 ARG   A HB3  1 
ATOM   3026 H HG2  A ARG   A 1 141 ? 13.406 -16.781 -5.166  0.74 21.85 ?  141 ARG   A HG2  1 
ATOM   3027 H HG2  B ARG   A 1 141 ? 13.360 -16.188 -4.936  0.26 15.89 ?  141 ARG   A HG2  1 
ATOM   3028 H HG3  A ARG   A 1 141 ? 14.494 -17.153 -4.062  0.74 21.85 ?  141 ARG   A HG3  1 
ATOM   3029 H HG3  B ARG   A 1 141 ? 14.459 -16.607 -3.865  0.26 15.89 ?  141 ARG   A HG3  1 
ATOM   3030 H HD2  A ARG   A 1 141 ? 11.986 -16.851 -3.018  0.74 23.84 ?  141 ARG   A HD2  1 
ATOM   3031 H HD2  B ARG   A 1 141 ? 11.931 -16.458 -2.810  0.26 17.02 ?  141 ARG   A HD2  1 
ATOM   3032 H HD3  A ARG   A 1 141 ? 12.088 -18.060 -4.048  0.74 23.84 ?  141 ARG   A HD3  1 
ATOM   3033 H HD3  B ARG   A 1 141 ? 12.090 -17.595 -3.911  0.26 17.02 ?  141 ARG   A HD3  1 
ATOM   3034 H HE   A ARG   A 1 141 ? 14.008 -18.543 -2.509  0.74 25.03 ?  141 ARG   A HE   1 
ATOM   3035 H HE   B ARG   A 1 141 ? 14.026 -17.861 -2.173  0.26 17.31 ?  141 ARG   A HE   1 
ATOM   3036 H HH11 A ARG   A 1 141 ? 10.804 -18.074 -1.757  0.74 25.60 ?  141 ARG   A HH11 1 
ATOM   3037 H HH11 B ARG   A 1 141 ? 10.733 -18.235 -2.005  0.26 19.77 ?  141 ARG   A HH11 1 
ATOM   3038 H HH12 A ARG   A 1 141 ? 10.814 -18.935 -0.543  0.74 25.60 ?  141 ARG   A HH12 1 
ATOM   3039 H HH12 B ARG   A 1 141 ? 10.758 -19.273 -0.938  0.26 19.77 ?  141 ARG   A HH12 1 
ATOM   3040 H HH21 A ARG   A 1 141 ? 13.989 -19.802 -0.653  0.74 26.43 ?  141 ARG   A HH21 1 
ATOM   3041 H HH21 B ARG   A 1 141 ? 14.026 -19.499 -0.630  0.26 19.27 ?  141 ARG   A HH21 1 
ATOM   3042 H HH22 A ARG   A 1 141 ? 12.730 -19.977 0.124   0.74 26.43 ?  141 ARG   A HH22 1 
ATOM   3043 H HH22 B ARG   A 1 141 ? 12.738 -20.036 -0.109  0.26 19.27 ?  141 ARG   A HH22 1 
ATOM   3044 N N    . VAL   A 1 142 ? 16.554 -14.375 -2.938  1.00 12.53 ?  142 VAL   A N    1 
ATOM   3045 C CA   . VAL   A 1 142 ? 18.001 -14.600 -2.969  1.00 12.73 ?  142 VAL   A CA   1 
ATOM   3046 C C    . VAL   A 1 142 ? 18.578 -14.594 -1.559  1.00 12.23 ?  142 VAL   A C    1 
ATOM   3047 O O    . VAL   A 1 142 ? 19.437 -15.414 -1.222  1.00 12.09 ?  142 VAL   A O    1 
ATOM   3048 C CB   . VAL   A 1 142 ? 18.701 -13.575 -3.884  1.00 13.05 ?  142 VAL   A CB   1 
ATOM   3049 C CG1  . VAL   A 1 142 ? 20.218 -13.790 -3.854  1.00 12.82 ?  142 VAL   A CG1  1 
ATOM   3050 C CG2  . VAL   A 1 142 ? 18.198 -13.692 -5.311  1.00 14.18 ?  142 VAL   A CG2  1 
ATOM   3051 H H    A VAL   A 1 142 ? 16.287 -13.624 -3.274  0.74 15.04 ?  142 VAL   A H    1 
ATOM   3052 H H    B VAL   A 1 142 ? 16.289 -13.775 -3.501  0.26 15.04 ?  142 VAL   A H    1 
ATOM   3053 H HA   . VAL   A 1 142 ? 18.164 -15.472 -3.348  1.00 15.28 ?  142 VAL   A HA   1 
ATOM   3054 H HB   . VAL   A 1 142 ? 18.520 -12.672 -3.571  1.00 15.66 ?  142 VAL   A HB   1 
ATOM   3055 H HG11 . VAL   A 1 142 ? 20.622 -13.295 -4.585  1.00 15.38 ?  142 VAL   A HG11 1 
ATOM   3056 H HG12 . VAL   A 1 142 ? 20.569 -13.468 -3.008  1.00 15.38 ?  142 VAL   A HG12 1 
ATOM   3057 H HG13 . VAL   A 1 142 ? 20.402 -14.735 -3.954  1.00 15.38 ?  142 VAL   A HG13 1 
ATOM   3058 H HG21 . VAL   A 1 142 ? 18.687 -13.066 -5.869  1.00 17.02 ?  142 VAL   A HG21 1 
ATOM   3059 H HG22 . VAL   A 1 142 ? 18.357 -14.599 -5.619  1.00 17.02 ?  142 VAL   A HG22 1 
ATOM   3060 H HG23 . VAL   A 1 142 ? 17.256 -13.492 -5.331  1.00 17.02 ?  142 VAL   A HG23 1 
ATOM   3061 N N    . CYS   A 1 143 ? 18.121 -13.672 -0.714  1.00 12.10 ?  143 CYS   A N    1 
ATOM   3062 C CA   . CYS   A 1 143 ? 18.587 -13.635 0.669   1.00 12.03 ?  143 CYS   A CA   1 
ATOM   3063 C C    . CYS   A 1 143 ? 18.357 -14.978 1.353   1.00 11.60 ?  143 CYS   A C    1 
ATOM   3064 O O    . CYS   A 1 143 ? 19.273 -15.568 1.928   1.00 11.40 ?  143 CYS   A O    1 
ATOM   3065 C CB   . CYS   A 1 143 ? 17.857 -12.524 1.419   1.00 12.55 ?  143 CYS   A CB   1 
ATOM   3066 S SG   . CYS   A 1 143 ? 18.349 -12.353 3.144   1.00 12.68 ?  143 CYS   A SG   1 
ATOM   3067 H H    . CYS   A 1 143 ? 17.545 -13.072 -0.915  1.00 14.52 ?  143 CYS   A H    1 
ATOM   3068 H HA   . CYS   A 1 143 ? 19.536 -13.450 0.683   1.00 14.44 ?  143 CYS   A HA   1 
ATOM   3069 H HB2  . CYS   A 1 143 ? 18.024 -11.683 0.973   1.00 15.06 ?  143 CYS   A HB2  1 
ATOM   3070 H HB3  . CYS   A 1 143 ? 16.907 -12.714 1.408   1.00 15.06 ?  143 CYS   A HB3  1 
ATOM   3071 H HG   . CYS   A 1 143 ? 17.757 -11.424 3.621   1.00 15.22 ?  143 CYS   A HG   1 
ATOM   3072 N N    . VAL   A 1 144 ? 17.124 -15.472 1.299   1.00 12.40 ?  144 VAL   A N    1 
ATOM   3073 C CA   . VAL   A 1 144 ? 16.779 -16.702 2.001   1.00 13.40 ?  144 VAL   A CA   1 
ATOM   3074 C C    . VAL   A 1 144 ? 17.580 -17.877 1.463   1.00 13.19 ?  144 VAL   A C    1 
ATOM   3075 O O    . VAL   A 1 144 ? 17.950 -18.790 2.214   1.00 13.73 ?  144 VAL   A O    1 
ATOM   3076 C CB   . VAL   A 1 144 ? 15.260 -16.932 1.894   1.00 16.06 ?  144 VAL   A CB   1 
ATOM   3077 C CG1  . VAL   A 1 144 ? 14.898 -18.359 2.232   1.00 17.67 ?  144 VAL   A CG1  1 
ATOM   3078 C CG2  . VAL   A 1 144 ? 14.524 -15.926 2.781   1.00 15.92 ?  144 VAL   A CG2  1 
ATOM   3079 H H    . VAL   A 1 144 ? 16.471 -15.116 0.861   1.00 14.89 ?  144 VAL   A H    1 
ATOM   3080 H HA   . VAL   A 1 144 ? 16.993 -16.598 2.936   1.00 16.07 ?  144 VAL   A HA   1 
ATOM   3081 H HB   . VAL   A 1 144 ? 14.980 -16.767 0.976   1.00 19.28 ?  144 VAL   A HB   1 
ATOM   3082 H HG11 . VAL   A 1 144 ? 13.945 -18.408 2.420   1.00 21.20 ?  144 VAL   A HG11 1 
ATOM   3083 H HG12 . VAL   A 1 144 ? 15.109 -18.932 1.478   1.00 21.20 ?  144 VAL   A HG12 1 
ATOM   3084 H HG13 . VAL   A 1 144 ? 15.399 -18.637 3.013   1.00 21.20 ?  144 VAL   A HG13 1 
ATOM   3085 H HG21 . VAL   A 1 144 ? 13.564 -16.064 2.695   1.00 19.10 ?  144 VAL   A HG21 1 
ATOM   3086 H HG22 . VAL   A 1 144 ? 14.791 -16.057 3.703   1.00 19.10 ?  144 VAL   A HG22 1 
ATOM   3087 H HG23 . VAL   A 1 144 ? 14.748 -15.023 2.497   1.00 19.10 ?  144 VAL   A HG23 1 
ATOM   3088 N N    . ASP   A 1 145 ? 17.839 -17.892 0.159   1.00 13.47 ?  145 ASP   A N    1 
ATOM   3089 C CA   . ASP   A 1 145 ? 18.543 -18.997 -0.478  1.00 13.96 ?  145 ASP   A CA   1 
ATOM   3090 C C    . ASP   A 1 145 ? 20.064 -18.861 -0.439  1.00 13.46 ?  145 ASP   A C    1 
ATOM   3091 O O    . ASP   A 1 145 ? 20.760 -19.757 -0.930  1.00 15.46 ?  145 ASP   A O    1 
ATOM   3092 C CB   . ASP   A 1 145 ? 18.079 -19.148 -1.929  1.00 15.43 ?  145 ASP   A CB   1 
ATOM   3093 C CG   . ASP   A 1 145 ? 16.605 -19.513 -2.038  1.00 17.38 ?  145 ASP   A CG   1 
ATOM   3094 O OD1  . ASP   A 1 145 ? 16.044 -20.059 -1.062  1.00 17.90 ?  145 ASP   A OD1  1 
ATOM   3095 O OD2  . ASP   A 1 145 ? 16.007 -19.256 -3.102  1.00 18.66 -1 145 ASP   A OD2  1 
ATOM   3096 H H    . ASP   A 1 145 ? 17.600 -17.268 -0.389  1.00 16.16 ?  145 ASP   A H    1 
ATOM   3097 H HA   . ASP   A 1 145 ? 18.312 -19.812 -0.013  1.00 16.75 ?  145 ASP   A HA   1 
ATOM   3098 H HB2  . ASP   A 1 145 ? 18.220 -18.316 -2.401  1.00 18.51 ?  145 ASP   A HB2  1 
ATOM   3099 H HB3  . ASP   A 1 145 ? 18.585 -19.862 -2.350  1.00 18.51 ?  145 ASP   A HB3  1 
ATOM   3100 N N    . THR   A 1 146 ? 20.600 -17.778 0.119   1.00 11.81 ?  146 THR   A N    1 
ATOM   3101 C CA   . THR   A 1 146 ? 22.045 -17.541 0.135   1.00 11.19 ?  146 THR   A CA   1 
ATOM   3102 C C    . THR   A 1 146 ? 22.607 -17.375 1.534   1.00 11.04 ?  146 THR   A C    1 
ATOM   3103 O O    . THR   A 1 146 ? 23.686 -17.903 1.832   1.00 12.24 ?  146 THR   A O    1 
ATOM   3104 C CB   . THR   A 1 146 ? 22.380 -16.282 -0.692  1.00 11.45 ?  146 THR   A CB   1 
ATOM   3105 O OG1  . THR   A 1 146 ? 21.849 -16.424 -2.010  1.00 11.97 ?  146 THR   A OG1  1 
ATOM   3106 C CG2  . THR   A 1 146 ? 23.890 -16.064 -0.791  1.00 11.96 ?  146 THR   A CG2  1 
ATOM   3107 H H    . THR   A 1 146 ? 20.144 -17.148 0.496   1.00 14.18 ?  146 THR   A H    1 
ATOM   3108 H HA   . THR   A 1 146 ? 22.497 -18.291 -0.272  1.00 13.43 ?  146 THR   A HA   1 
ATOM   3109 H HB   . THR   A 1 146 ? 21.994 -15.503 -0.265  1.00 13.74 ?  146 THR   A HB   1 
ATOM   3110 H HG1  . THR   A 1 146 ? 21.009 -16.487 -1.967  1.00 14.37 ?  146 THR   A HG1  1 
ATOM   3111 H HG21 . THR   A 1 146 ? 24.081 -15.386 -1.456  1.00 14.35 ?  146 THR   A HG21 1 
ATOM   3112 H HG22 . THR   A 1 146 ? 24.243 -15.777 0.065   1.00 14.35 ?  146 THR   A HG22 1 
ATOM   3113 H HG23 . THR   A 1 146 ? 24.326 -16.892 -1.052  1.00 14.35 ?  146 THR   A HG23 1 
ATOM   3114 N N    . VAL   A 1 147 ? 21.928 -16.606 2.379   1.00 11.08 ?  147 VAL   A N    1 
ATOM   3115 C CA   . VAL   A 1 147 ? 22.418 -16.310 3.717   1.00 11.22 ?  147 VAL   A CA   1 
ATOM   3116 C C    . VAL   A 1 147 ? 22.088 -17.478 4.632   1.00 11.32 ?  147 VAL   A C    1 
ATOM   3117 O O    . VAL   A 1 147 ? 20.940 -17.940 4.683   1.00 12.09 ?  147 VAL   A O    1 
ATOM   3118 C CB   . VAL   A 1 147 ? 21.812 -14.996 4.238   1.00 11.45 ?  147 VAL   A CB   1 
ATOM   3119 C CG1  . VAL   A 1 147 ? 22.367 -14.679 5.611   1.00 12.44 ?  147 VAL   A CG1  1 
ATOM   3120 C CG2  . VAL   A 1 147 ? 22.075 -13.849 3.263   1.00 11.89 ?  147 VAL   A CG2  1 
ATOM   3121 H H    . VAL   A 1 147 ? 21.166 -16.245 2.205   1.00 13.30 ?  147 VAL   A H    1 
ATOM   3122 H HA   . VAL   A 1 147 ? 23.380 -16.207 3.690   1.00 13.47 ?  147 VAL   A HA   1 
ATOM   3123 H HB   . VAL   A 1 147 ? 20.853 -15.101 4.324   1.00 13.74 ?  147 VAL   A HB   1 
ATOM   3124 H HG11 . VAL   A 1 147 ? 22.123 -13.774 5.851   1.00 14.92 ?  147 VAL   A HG11 1 
ATOM   3125 H HG12 . VAL   A 1 147 ? 21.995 -15.304 6.256   1.00 14.92 ?  147 VAL   A HG12 1 
ATOM   3126 H HG13 . VAL   A 1 147 ? 23.334 -14.767 5.588   1.00 14.92 ?  147 VAL   A HG13 1 
ATOM   3127 H HG21 . VAL   A 1 147 ? 21.753 -13.021 3.656   1.00 14.27 ?  147 VAL   A HG21 1 
ATOM   3128 H HG22 . VAL   A 1 147 ? 23.028 -13.787 3.098   1.00 14.27 ?  147 VAL   A HG22 1 
ATOM   3129 H HG23 . VAL   A 1 147 ? 21.604 -14.025 2.434   1.00 14.27 ?  147 VAL   A HG23 1 
ATOM   3130 N N    . ARG   A 1 148 ? 23.105 -17.957 5.348   1.00 11.58 ?  148 ARG   A N    1 
ATOM   3131 C CA   . ARG   A 1 148 ? 22.973 -19.039 6.309   1.00 11.95 ?  148 ARG   A CA   1 
ATOM   3132 C C    . ARG   A 1 148 ? 23.097 -18.565 7.744   1.00 12.26 ?  148 ARG   A C    1 
ATOM   3133 O O    . ARG   A 1 148 ? 22.686 -19.285 8.659   1.00 13.76 ?  148 ARG   A O    1 
ATOM   3134 C CB   . ARG   A 1 148 ? 24.020 -20.129 6.029   1.00 12.46 ?  148 ARG   A CB   1 
ATOM   3135 C CG   . ARG   A 1 148 ? 23.855 -20.771 4.658   1.00 13.63 ?  148 ARG   A CG   1 
ATOM   3136 C CD   . ARG   A 1 148 ? 24.936 -21.812 4.358   1.00 14.48 ?  148 ARG   A CD   1 
ATOM   3137 N NE   . ARG   A 1 148 ? 26.273 -21.230 4.377   1.00 14.45 ?  148 ARG   A NE   1 
ATOM   3138 C CZ   . ARG   A 1 148 ? 26.777 -20.484 3.404   1.00 13.82 ?  148 ARG   A CZ   1 
ATOM   3139 N NH1  . ARG   A 1 148 ? 26.095 -20.238 2.295   1.00 14.34 ?  148 ARG   A NH1  1 
ATOM   3140 N NH2  . ARG   A 1 148 ? 27.998 -19.963 3.545   1.00 14.23 ?  148 ARG   A NH2  1 
ATOM   3141 H H    . ARG   A 1 148 ? 23.912 -17.660 5.276   1.00 13.89 ?  148 ARG   A H    1 
ATOM   3142 H HA   . ARG   A 1 148 ? 22.100 -19.439 6.206   1.00 14.34 ?  148 ARG   A HA   1 
ATOM   3143 H HB2  . ARG   A 1 148 ? 24.906 -19.743 6.073   1.00 14.96 ?  148 ARG   A HB2  1 
ATOM   3144 H HB3  . ARG   A 1 148 ? 23.929 -20.831 6.695   1.00 14.96 ?  148 ARG   A HB3  1 
ATOM   3145 H HG2  . ARG   A 1 148 ? 22.990 -21.208 4.618   1.00 16.35 ?  148 ARG   A HG2  1 
ATOM   3146 H HG3  . ARG   A 1 148 ? 23.906 -20.076 3.982   1.00 16.35 ?  148 ARG   A HG3  1 
ATOM   3147 H HD2  . ARG   A 1 148 ? 24.902 -22.509 5.030   1.00 17.37 ?  148 ARG   A HD2  1 
ATOM   3148 H HD3  . ARG   A 1 148 ? 24.780 -22.187 3.477   1.00 17.37 ?  148 ARG   A HD3  1 
ATOM   3149 H HE   . ARG   A 1 148 ? 26.765 -21.374 5.063   1.00 17.35 ?  148 ARG   A HE   1 
ATOM   3150 H HH11 . ARG   A 1 148 ? 25.307 -20.559 2.191   1.00 17.20 ?  148 ARG   A HH11 1 
ATOM   3151 H HH12 . ARG   A 1 148 ? 26.443 -19.745 1.678   1.00 17.20 ?  148 ARG   A HH12 1 
ATOM   3152 H HH21 . ARG   A 1 148 ? 28.445 -20.108 4.263   1.00 17.08 ?  148 ARG   A HH21 1 
ATOM   3153 H HH22 . ARG   A 1 148 ? 28.333 -19.471 2.922   1.00 17.08 ?  148 ARG   A HH22 1 
ATOM   3154 N N    . THR   A 1 149 ? 23.648 -17.376 7.954   1.00 11.96 ?  149 THR   A N    1 
ATOM   3155 C CA   . THR   A 1 149 ? 23.731 -16.779 9.272   1.00 12.20 ?  149 THR   A CA   1 
ATOM   3156 C C    . THR   A 1 149 ? 22.408 -16.077 9.583   1.00 11.82 ?  149 THR   A C    1 
ATOM   3157 O O    . THR   A 1 149 ? 21.469 -16.072 8.777   1.00 12.42 ?  149 THR   A O    1 
ATOM   3158 C CB   . THR   A 1 149 ? 24.935 -15.846 9.331   1.00 12.72 ?  149 THR   A CB   1 
ATOM   3159 O OG1  . THR   A 1 149 ? 24.807 -14.899 8.267   1.00 12.62 ?  149 THR   A OG1  1 
ATOM   3160 C CG2  . THR   A 1 149 ? 26.250 -16.646 9.199   1.00 13.18 ?  149 THR   A CG2  1 
ATOM   3161 H H    . THR   A 1 149 ? 23.993 -16.885 7.333   1.00 14.36 ?  149 THR   A H    1 
ATOM   3162 H HA   . THR   A 1 149 ? 23.856 -17.479 9.927   1.00 14.64 ?  149 THR   A HA   1 
ATOM   3163 H HB   . THR   A 1 149 ? 24.937 -15.379 10.178  1.00 15.27 ?  149 THR   A HB   1 
ATOM   3164 H HG1  . THR   A 1 149 ? 25.465 -14.375 8.267   1.00 15.14 ?  149 THR   A HG1  1 
ATOM   3165 H HG21 . THR   A 1 149 ? 27.011 -16.049 9.253   1.00 15.82 ?  149 THR   A HG21 1 
ATOM   3166 H HG22 . THR   A 1 149 ? 26.315 -17.302 9.914   1.00 15.82 ?  149 THR   A HG22 1 
ATOM   3167 H HG23 . THR   A 1 149 ? 26.276 -17.113 8.347   1.00 15.82 ?  149 THR   A HG23 1 
ATOM   3168 N N    . ASN   A 1 150 ? 22.295 -15.532 10.786  1.00 12.30 ?  150 ASN   A N    1 
ATOM   3169 C CA   . ASN   A 1 150 ? 21.013 -15.023 11.273  1.00 12.89 ?  150 ASN   A CA   1 
ATOM   3170 C C    . ASN   A 1 150 ? 20.832 -13.583 10.817  1.00 12.22 ?  150 ASN   A C    1 
ATOM   3171 O O    . ASN   A 1 150 ? 21.576 -12.693 11.239  1.00 13.76 ?  150 ASN   A O    1 
ATOM   3172 C CB   . ASN   A 1 150 ? 20.951 -15.138 12.791  1.00 15.46 ?  150 ASN   A CB   1 
ATOM   3173 C CG   . ASN   A 1 150 ? 20.824 -16.568 13.246  1.00 19.58 ?  150 ASN   A CG   1 
ATOM   3174 O OD1  . ASN   A 1 150 ? 20.210 -17.385 12.564  1.00 20.71 ?  150 ASN   A OD1  1 
ATOM   3175 N ND2  . ASN   A 1 150 ? 21.416 -16.887 14.395  1.00 21.95 ?  150 ASN   A ND2  1 
ATOM   3176 H H    . ASN   A 1 150 ? 22.941 -15.449 11.345  1.00 14.76 ?  150 ASN   A H    1 
ATOM   3177 H HA   . ASN   A 1 150 ? 20.290 -15.555 10.903  1.00 15.46 ?  150 ASN   A HA   1 
ATOM   3178 H HB2  . ASN   A 1 150 ? 21.762 -14.773 13.175  1.00 18.55 ?  150 ASN   A HB2  1 
ATOM   3179 H HB3  . ASN   A 1 150 ? 20.177 -14.657 13.122  1.00 18.55 ?  150 ASN   A HB3  1 
ATOM   3180 H HD21 . ASN   A 1 150 ? 21.380 -17.695 14.697  1.00 26.34 ?  150 ASN   A HD21 1 
ATOM   3181 H HD22 . ASN   A 1 150 ? 21.837 -16.285 14.845  1.00 26.34 ?  150 ASN   A HD22 1 
ATOM   3182 N N    . VAL   A 1 151 ? 19.844 -13.349 9.962   1.00 11.86 ?  151 VAL   A N    1 
ATOM   3183 C CA   . VAL   A 1 151 ? 19.630 -12.036 9.372   1.00 12.15 ?  151 VAL   A CA   1 
ATOM   3184 C C    . VAL   A 1 151 ? 18.246 -11.517 9.747   1.00 12.00 ?  151 VAL   A C    1 
ATOM   3185 O O    . VAL   A 1 151 ? 17.235 -12.228 9.620   1.00 13.39 ?  151 VAL   A O    1 
ATOM   3186 C CB   . VAL   A 1 151 ? 19.912 -12.023 7.855   1.00 13.33 ?  151 VAL   A CB   1 
ATOM   3187 C CG1  . VAL   A 1 151 ? 19.104 -13.057 7.110   1.00 14.50 ?  151 VAL   A CG1  1 
ATOM   3188 C CG2  . VAL   A 1 151 ? 19.687 -10.627 7.275   1.00 13.59 ?  151 VAL   A CG2  1 
ATOM   3189 H H    . VAL   A 1 151 ? 19.284 -13.947 9.696   1.00 14.23 ?  151 VAL   A H    1 
ATOM   3190 H HA   . VAL   A 1 151 ? 20.271 -11.428 9.766   1.00 14.58 ?  151 VAL   A HA   1 
ATOM   3191 H HB   . VAL   A 1 151 ? 20.853 -12.238 7.715   1.00 16.00 ?  151 VAL   A HB   1 
ATOM   3192 H HG11 . VAL   A 1 151 ? 19.295 -12.993 6.159   1.00 17.39 ?  151 VAL   A HG11 1 
ATOM   3193 H HG12 . VAL   A 1 151 ? 19.351 -13.944 7.431   1.00 17.39 ?  151 VAL   A HG12 1 
ATOM   3194 H HG13 . VAL   A 1 151 ? 18.162 -12.902 7.270   1.00 17.39 ?  151 VAL   A HG13 1 
ATOM   3195 H HG21 . VAL   A 1 151 ? 20.015 -10.605 6.358   1.00 16.30 ?  151 VAL   A HG21 1 
ATOM   3196 H HG22 . VAL   A 1 151 ? 18.737 -10.427 7.285   1.00 16.30 ?  151 VAL   A HG22 1 
ATOM   3197 H HG23 . VAL   A 1 151 ? 20.169 -9.978  7.809   1.00 16.30 ?  151 VAL   A HG23 1 
ATOM   3198 N N    . TYR   A 1 152 ? 18.235 -10.268 10.225  1.00 11.88 ?  152 TYR   A N    1 
ATOM   3199 C CA   . TYR   A 1 152 ? 17.048 -9.527  10.622  1.00 11.53 ?  152 TYR   A CA   1 
ATOM   3200 C C    . TYR   A 1 152 ? 16.848 -8.418  9.602   1.00 11.00 ?  152 TYR   A C    1 
ATOM   3201 O O    . TYR   A 1 152 ? 17.631 -7.461  9.552   1.00 11.45 ?  152 TYR   A O    1 
ATOM   3202 C CB   . TYR   A 1 152 ? 17.234 -8.992  12.041  1.00 12.20 ?  152 TYR   A CB   1 
ATOM   3203 C CG   . TYR   A 1 152 ? 17.202 -10.125 13.033  1.00 13.07 ?  152 TYR   A CG   1 
ATOM   3204 C CD1  . TYR   A 1 152 ? 18.336 -10.883 13.294  1.00 14.46 ?  152 TYR   A CD1  1 
ATOM   3205 C CD2  . TYR   A 1 152 ? 16.023 -10.478 13.670  1.00 13.39 ?  152 TYR   A CD2  1 
ATOM   3206 C CE1  . TYR   A 1 152 ? 18.305 -11.950 14.172  1.00 16.13 ?  152 TYR   A CE1  1 
ATOM   3207 C CE2  . TYR   A 1 152 ? 15.979 -11.555 14.556  1.00 15.07 ?  152 TYR   A CE2  1 
ATOM   3208 C CZ   . TYR   A 1 152 ? 17.126 -12.286 14.802  1.00 16.10 ?  152 TYR   A CZ   1 
ATOM   3209 O OH   . TYR   A 1 152 ? 17.092 -13.356 15.676  1.00 18.28 ?  152 TYR   A OH   1 
ATOM   3210 H H    . TYR   A 1 152 ? 18.957 -9.801  10.319  1.00 14.26 ?  152 TYR   A H    1 
ATOM   3211 H HA   . TYR   A 1 152 ? 16.277 -10.113 10.605  1.00 13.83 ?  152 TYR   A HA   1 
ATOM   3212 H HB2  . TYR   A 1 152 ? 18.091 -8.550  12.111  1.00 14.64 ?  152 TYR   A HB2  1 
ATOM   3213 H HB3  . TYR   A 1 152 ? 16.516 -8.375  12.252  1.00 14.64 ?  152 TYR   A HB3  1 
ATOM   3214 H HD1  . TYR   A 1 152 ? 19.132 -10.662 12.863  1.00 17.35 ?  152 TYR   A HD1  1 
ATOM   3215 H HD2  . TYR   A 1 152 ? 15.242 -9.989  13.500  1.00 16.07 ?  152 TYR   A HD2  1 
ATOM   3216 H HE1  . TYR   A 1 152 ? 19.076 -12.434 14.337  1.00 19.36 ?  152 TYR   A HE1  1 
ATOM   3217 H HE2  . TYR   A 1 152 ? 15.182 -11.771 14.984  1.00 18.09 ?  152 TYR   A HE2  1 
ATOM   3218 H HH   . TYR   A 1 152 ? 16.315 -13.429 15.991  1.00 21.94 ?  152 TYR   A HH   1 
ATOM   3219 N N    A LEU   A 1 153 ? 15.843 -8.596  8.742   0.74 11.11 ?  153 LEU   A N    1 
ATOM   3220 N N    B LEU   A 1 153 ? 15.786 -8.513  8.812   0.26 10.79 ?  153 LEU   A N    1 
ATOM   3221 C CA   A LEU   A 1 153 ? 15.573 -7.704  7.621   0.74 11.75 ?  153 LEU   A CA   1 
ATOM   3222 C CA   B LEU   A 1 153 ? 15.531 -7.548  7.752   0.26 10.58 ?  153 LEU   A CA   1 
ATOM   3223 C C    A LEU   A 1 153 ? 14.571 -6.630  8.014   0.74 12.13 ?  153 LEU   A C    1 
ATOM   3224 C C    B LEU   A 1 153 ? 14.570 -6.474  8.250   0.26 10.53 ?  153 LEU   A C    1 
ATOM   3225 O O    A LEU   A 1 153 ? 13.482 -6.934  8.517   0.74 13.25 ?  153 LEU   A O    1 
ATOM   3226 O O    B LEU   A 1 153 ? 13.452 -6.783  8.678   0.26 11.16 ?  153 LEU   A O    1 
ATOM   3227 C CB   A LEU   A 1 153 ? 15.006 -8.496  6.441   0.74 12.08 ?  153 LEU   A CB   1 
ATOM   3228 C CB   B LEU   A 1 153 ? 14.964 -8.251  6.522   0.26 10.85 ?  153 LEU   A CB   1 
ATOM   3229 C CG   A LEU   A 1 153 ? 15.943 -9.502  5.765   0.74 12.18 ?  153 LEU   A CG   1 
ATOM   3230 C CG   B LEU   A 1 153 ? 15.886 -9.279  5.864   0.26 11.28 ?  153 LEU   A CG   1 
ATOM   3231 C CD1  A LEU   A 1 153 ? 15.161 -10.400 4.818   0.74 12.58 ?  153 LEU   A CD1  1 
ATOM   3232 C CD1  B LEU   A 1 153 ? 15.118 -10.043 4.808   0.26 11.74 ?  153 LEU   A CD1  1 
ATOM   3233 C CD2  A LEU   A 1 153 ? 17.051 -8.785  5.018   0.74 12.66 ?  153 LEU   A CD2  1 
ATOM   3234 C CD2  B LEU   A 1 153 ? 17.112 -8.611  5.258   0.26 11.50 ?  153 LEU   A CD2  1 
ATOM   3235 H H    A LEU   A 1 153 ? 15.292 -9.260  8.791   0.74 13.33 ?  153 LEU   A H    1 
ATOM   3236 H H    B LEU   A 1 153 ? 15.188 -9.133  8.874   0.26 12.95 ?  153 LEU   A H    1 
ATOM   3237 H HA   A LEU   A 1 153 ? 16.397 -7.284  7.343   0.74 14.11 ?  153 LEU   A HA   1 
ATOM   3238 H HA   B LEU   A 1 153 ? 16.363 -7.121  7.506   0.26 12.69 ?  153 LEU   A HA   1 
ATOM   3239 H HB2  A LEU   A 1 153 ? 14.227 -8.990  6.750   0.74 14.49 ?  153 LEU   A HB2  1 
ATOM   3240 H HB2  B LEU   A 1 153 ? 14.154 -8.714  6.781   0.26 13.02 ?  153 LEU   A HB2  1 
ATOM   3241 H HB3  A LEU   A 1 153 ? 14.728 -7.863  5.759   0.74 14.49 ?  153 LEU   A HB3  1 
ATOM   3242 H HB3  B LEU   A 1 153 ? 14.759 -7.580  5.855   0.26 13.02 ?  153 LEU   A HB3  1 
ATOM   3243 H HG   A LEU   A 1 153 ? 16.347 -10.064 6.447   0.74 14.61 ?  153 LEU   A HG   1 
ATOM   3244 H HG   B LEU   A 1 153 ? 16.188 -9.913  6.535   0.26 13.54 ?  153 LEU   A HG   1 
ATOM   3245 H HD11 A LEU   A 1 153 ? 15.742 -11.109 4.503   0.74 15.09 ?  153 LEU   A HD11 1 
ATOM   3246 H HD11 B LEU   A 1 153 ? 15.706 -10.698 4.405   0.26 14.09 ?  153 LEU   A HD11 1 
ATOM   3247 H HD12 A LEU   A 1 153 ? 14.404 -10.777 5.290   0.74 15.09 ?  153 LEU   A HD12 1 
ATOM   3248 H HD12 B LEU   A 1 153 ? 14.364 -10.485 5.228   0.26 14.09 ?  153 LEU   A HD12 1 
ATOM   3249 H HD13 A LEU   A 1 153 ? 14.851 -9.868  4.067   0.74 15.09 ?  153 LEU   A HD13 1 
ATOM   3250 H HD13 B LEU   A 1 153 ? 14.805 -9.417  4.137   0.26 14.09 ?  153 LEU   A HD13 1 
ATOM   3251 H HD21 A LEU   A 1 153 ? 17.635 -9.446  4.620   0.74 15.20 ?  153 LEU   A HD21 1 
ATOM   3252 H HD21 B LEU   A 1 153 ? 17.631 -9.280  4.784   0.26 13.80 ?  153 LEU   A HD21 1 
ATOM   3253 H HD22 A LEU   A 1 153 ? 16.653 -8.232  4.331   0.74 15.20 ?  153 LEU   A HD22 1 
ATOM   3254 H HD22 B LEU   A 1 153 ? 16.822 -7.920  4.645   0.26 13.80 ?  153 LEU   A HD22 1 
ATOM   3255 H HD23 A LEU   A 1 153 ? 17.545 -8.238  5.645   0.74 15.20 ?  153 LEU   A HD23 1 
ATOM   3256 H HD23 B LEU   A 1 153 ? 17.645 -8.224  5.970   0.26 13.80 ?  153 LEU   A HD23 1 
ATOM   3257 N N    A ALA   A 1 154 ? 14.927 -5.380  7.743   0.74 11.66 ?  154 ALA   A N    1 
ATOM   3258 N N    B ALA   A 1 154 ? 15.014 -5.216  8.199   0.26 9.79  ?  154 ALA   A N    1 
ATOM   3259 C CA   A ALA   A 1 154 ? 14.072 -4.232  7.998   0.74 12.22 ?  154 ALA   A CA   1 
ATOM   3260 C CA   B ALA   A 1 154 ? 14.194 -4.062  8.558   0.26 9.49  ?  154 ALA   A CA   1 
ATOM   3261 C C    A ALA   A 1 154 ? 13.573 -3.707  6.660   0.74 12.09 ?  154 ALA   A C    1 
ATOM   3262 C C    B ALA   A 1 154 ? 13.642 -3.442  7.277   0.26 9.27  ?  154 ALA   A C    1 
ATOM   3263 O O    A ALA   A 1 154 ? 14.375 -3.327  5.796   0.74 13.14 ?  154 ALA   A O    1 
ATOM   3264 O O    B ALA   A 1 154 ? 14.399 -2.891  6.468   0.26 9.14  ?  154 ALA   A O    1 
ATOM   3265 C CB   A ALA   A 1 154 ? 14.841 -3.146  8.746   0.74 12.66 ?  154 ALA   A CB   1 
ATOM   3266 C CB   B ALA   A 1 154 ? 15.018 -3.044  9.345   0.26 9.92  ?  154 ALA   A CB   1 
ATOM   3267 H H    A ALA   A 1 154 ? 15.683 -5.177  7.384   0.74 13.99 ?  154 ALA   A H    1 
ATOM   3268 H H    B ALA   A 1 154 ? 15.817 -5.003  7.968   0.26 11.75 ?  154 ALA   A H    1 
ATOM   3269 H HA   A ALA   A 1 154 ? 13.311 -4.509  8.534   0.74 14.66 ?  154 ALA   A HA   1 
ATOM   3270 H HA   B ALA   A 1 154 ? 13.452 -4.347  9.111   0.26 11.39 ?  154 ALA   A HA   1 
ATOM   3271 H HB1  A ALA   A 1 154 ? 14.249 -2.398  8.902   0.74 15.19 ?  154 ALA   A HB1  1 
ATOM   3272 H HB1  B ALA   A 1 154 ? 14.469 -2.267  9.532   0.26 11.90 ?  154 ALA   A HB1  1 
ATOM   3273 H HB2  A ALA   A 1 154 ? 15.155 -3.507  9.591   0.74 15.19 ?  154 ALA   A HB2  1 
ATOM   3274 H HB2  B ALA   A 1 154 ? 15.312 -3.449  10.177  0.26 11.90 ?  154 ALA   A HB2  1 
ATOM   3275 H HB3  A ALA   A 1 154 ? 15.597 -2.869  8.204   0.74 15.19 ?  154 ALA   A HB3  1 
ATOM   3276 H HB3  B ALA   A 1 154 ? 15.788 -2.784  8.815   0.26 11.90 ?  154 ALA   A HB3  1 
ATOM   3277 N N    A VAL   A 1 155 ? 12.252 -3.695  6.497   0.74 12.17 ?  155 VAL   A N    1 
ATOM   3278 N N    B VAL   A 1 155 ? 12.324 -3.519  7.103   0.26 9.21  ?  155 VAL   A N    1 
ATOM   3279 C CA   A VAL   A 1 155 ? 11.585 -3.225  5.288   0.74 13.29 ?  155 VAL   A CA   1 
ATOM   3280 C CA   B VAL   A 1 155 ? 11.647 -3.025  5.907   0.26 9.32  ?  155 VAL   A CA   1 
ATOM   3281 C C    A VAL   A 1 155 ? 10.841 -1.943  5.647   0.74 15.14 ?  155 VAL   A C    1 
ATOM   3282 C C    B VAL   A 1 155 ? 10.975 -1.697  6.238   0.26 10.03 ?  155 VAL   A C    1 
ATOM   3283 O O    A VAL   A 1 155 ? 9.908  -1.969  6.458   0.74 15.34 ?  155 VAL   A O    1 
ATOM   3284 O O    B VAL   A 1 155 ? 10.085 -1.636  7.093   0.26 10.23 ?  155 VAL   A O    1 
ATOM   3285 C CB   A VAL   A 1 155 ? 10.642 -4.298  4.717   0.74 13.15 ?  155 VAL   A CB   1 
ATOM   3286 C CB   B VAL   A 1 155 ? 10.635 -4.047  5.368   0.26 9.37  ?  155 VAL   A CB   1 
ATOM   3287 C CG1  A VAL   A 1 155 ? 9.942  -3.798  3.456   0.74 13.98 ?  155 VAL   A CG1  1 
ATOM   3288 C CG1  B VAL   A 1 155 ? 9.927  -3.485  4.143   0.26 9.51  ?  155 VAL   A CG1  1 
ATOM   3289 C CG2  A VAL   A 1 155 ? 11.420 -5.575  4.411   0.74 13.62 ?  155 VAL   A CG2  1 
ATOM   3290 C CG2  B VAL   A 1 155 ? 11.333 -5.357  5.038   0.26 10.22 ?  155 VAL   A CG2  1 
ATOM   3291 H H    A VAL   A 1 155 ? 11.703 -3.982  7.096   0.74 14.60 ?  155 VAL   A H    1 
ATOM   3292 H H    B VAL   A 1 155 ? 11.790 -3.862  7.684   0.26 11.05 ?  155 VAL   A H    1 
ATOM   3293 H HA   A VAL   A 1 155 ? 12.253 -3.025  4.613   0.74 15.95 ?  155 VAL   A HA   1 
ATOM   3294 H HA   B VAL   A 1 155 ? 12.309 -2.864  5.217   0.26 11.18 ?  155 VAL   A HA   1 
ATOM   3295 H HB   A VAL   A 1 155 ? 9.963  -4.515  5.376   0.74 15.78 ?  155 VAL   A HB   1 
ATOM   3296 H HB   B VAL   A 1 155 ? 9.969  -4.225  6.052   0.26 11.25 ?  155 VAL   A HB   1 
ATOM   3297 H HG11 A VAL   A 1 155 ? 9.414  -4.523  3.079   0.74 16.78 ?  155 VAL   A HG11 1 
ATOM   3298 H HG11 B VAL   A 1 155 ? 9.442  -4.200  3.705   0.26 11.41 ?  155 VAL   A HG11 1 
ATOM   3299 H HG12 A VAL   A 1 155 ? 9.363  -3.057  3.686   0.74 16.78 ?  155 VAL   A HG12 1 
ATOM   3300 H HG12 B VAL   A 1 155 ? 9.311  -2.790  4.422   0.26 11.41 ?  155 VAL   A HG12 1 
ATOM   3301 H HG13 A VAL   A 1 155 ? 10.611 -3.514  2.814   0.74 16.78 ?  155 VAL   A HG13 1 
ATOM   3302 H HG13 B VAL   A 1 155 ? 10.591 -3.116  3.537   0.26 11.41 ?  155 VAL   A HG13 1 
ATOM   3303 H HG21 A VAL   A 1 155 ? 10.832 -6.216  3.981   0.74 16.35 ?  155 VAL   A HG21 1 
ATOM   3304 H HG21 B VAL   A 1 155 ? 10.700 -5.952  4.610   0.26 12.27 ?  155 VAL   A HG21 1 
ATOM   3305 H HG22 A VAL   A 1 155 ? 12.162 -5.362  3.820   0.74 16.35 ?  155 VAL   A HG22 1 
ATOM   3306 H HG22 B VAL   A 1 155 ? 12.076 -5.177  4.440   0.26 12.27 ?  155 VAL   A HG22 1 
ATOM   3307 H HG23 A VAL   A 1 155 ? 11.762 -5.949  5.241   0.74 16.35 ?  155 VAL   A HG23 1 
ATOM   3308 H HG23 B VAL   A 1 155 ? 11.663 -5.758  5.859   0.26 12.27 ?  155 VAL   A HG23 1 
ATOM   3309 N N    A PHE   A 1 156 ? 11.262 -0.821  5.052   0.74 16.77 ?  156 PHE   A N    1 
ATOM   3310 N N    B PHE   A 1 156 ? 11.395 -0.643  5.536   0.26 10.18 ?  156 PHE   A N    1 
ATOM   3311 C CA   A PHE   A 1 156 ? 10.736 0.488   5.452   0.74 18.38 ?  156 PHE   A CA   1 
ATOM   3312 C CA   B PHE   A 1 156 ? 10.948 0.715   5.834   0.26 11.43 ?  156 PHE   A CA   1 
ATOM   3313 C C    A PHE   A 1 156 ? 9.268  0.650   5.070   0.74 18.69 ?  156 PHE   A C    1 
ATOM   3314 C C    B PHE   A 1 156 ? 9.449  0.873   5.600   0.26 11.53 ?  156 PHE   A C    1 
ATOM   3315 O O    A PHE   A 1 156 ? 8.482  1.239   5.824   0.74 19.86 ?  156 PHE   A O    1 
ATOM   3316 O O    B PHE   A 1 156 ? 8.724  1.380   6.465   0.26 12.27 ?  156 PHE   A O    1 
ATOM   3317 C CB   A PHE   A 1 156 ? 11.591 1.588   4.815   0.74 19.54 ?  156 PHE   A CB   1 
ATOM   3318 C CB   B PHE   A 1 156 ? 11.749 1.678   4.952   0.26 12.44 ?  156 PHE   A CB   1 
ATOM   3319 C CG   A PHE   A 1 156 ? 11.152 2.997   5.150   0.74 21.23 ?  156 PHE   A CG   1 
ATOM   3320 C CG   B PHE   A 1 156 ? 11.488 3.134   5.219   0.26 13.19 ?  156 PHE   A CG   1 
ATOM   3321 C CD1  A PHE   A 1 156 ? 11.195 3.463   6.456   0.74 22.37 ?  156 PHE   A CD1  1 
ATOM   3322 C CD1  B PHE   A 1 156 ? 12.053 3.763   6.314   0.26 13.28 ?  156 PHE   A CD1  1 
ATOM   3323 C CD2  A PHE   A 1 156 ? 10.737 3.862   4.149   0.74 22.28 ?  156 PHE   A CD2  1 
ATOM   3324 C CD2  B PHE   A 1 156 ? 10.712 3.881   4.349   0.26 13.83 ?  156 PHE   A CD2  1 
ATOM   3325 C CE1  A PHE   A 1 156 ? 10.806 4.758   6.760   0.74 23.35 ?  156 PHE   A CE1  1 
ATOM   3326 C CE1  B PHE   A 1 156 ? 11.824 5.099   6.553   0.26 13.64 ?  156 PHE   A CE1  1 
ATOM   3327 C CE2  A PHE   A 1 156 ? 10.345 5.159   4.445   0.74 23.44 ?  156 PHE   A CE2  1 
ATOM   3328 C CE2  B PHE   A 1 156 ? 10.482 5.222   4.582   0.26 14.27 ?  156 PHE   A CE2  1 
ATOM   3329 C CZ   A PHE   A 1 156 ? 10.384 5.608   5.752   0.74 23.79 ?  156 PHE   A CZ   1 
ATOM   3330 C CZ   B PHE   A 1 156 ? 11.040 5.832   5.684   0.26 13.77 ?  156 PHE   A CZ   1 
ATOM   3331 H H    A PHE   A 1 156 ? 11.844 -0.805  4.419   0.74 20.12 ?  156 PHE   A H    1 
ATOM   3332 H H    B PHE   A 1 156 ? 11.938 -0.696  4.879   0.26 12.22 ?  156 PHE   A H    1 
ATOM   3333 H HA   A PHE   A 1 156 ? 10.817 0.564   6.416   0.74 22.06 ?  156 PHE   A HA   1 
ATOM   3334 H HA   B PHE   A 1 156 ? 11.139 0.921   6.763   0.26 13.72 ?  156 PHE   A HA   1 
ATOM   3335 H HB2  A PHE   A 1 156 ? 12.510 1.480   5.118   0.74 23.45 ?  156 PHE   A HB2  1 
ATOM   3336 H HB2  B PHE   A 1 156 ? 12.699 1.515   5.096   0.26 14.93 ?  156 PHE   A HB2  1 
ATOM   3337 H HB3  A PHE   A 1 156 ? 11.556 1.484   3.852   0.74 23.45 ?  156 PHE   A HB3  1 
ATOM   3338 H HB3  B PHE   A 1 156 ? 11.529 1.506   4.024   0.26 14.93 ?  156 PHE   A HB3  1 
ATOM   3339 H HD1  A PHE   A 1 156 ? 11.480 2.892   7.140   0.74 26.85 ?  156 PHE   A HD1  1 
ATOM   3340 H HD1  B PHE   A 1 156 ? 12.585 3.268   6.902   0.26 15.93 ?  156 PHE   A HD1  1 
ATOM   3341 H HD2  A PHE   A 1 156 ? 10.708 3.560   3.270   0.74 26.73 ?  156 PHE   A HD2  1 
ATOM   3342 H HD2  B PHE   A 1 156 ? 10.333 3.467   3.606   0.26 16.59 ?  156 PHE   A HD2  1 
ATOM   3343 H HE1  A PHE   A 1 156 ? 10.833 5.057   7.641   0.74 28.01 ?  156 PHE   A HE1  1 
ATOM   3344 H HE1  B PHE   A 1 156 ? 12.206 5.506   7.297   0.26 16.37 ?  156 PHE   A HE1  1 
ATOM   3345 H HE2  A PHE   A 1 156 ? 10.061 5.724   3.766   0.74 28.13 ?  156 PHE   A HE2  1 
ATOM   3346 H HE2  B PHE   A 1 156 ? 9.951  5.706   3.997   0.26 17.12 ?  156 PHE   A HE2  1 
ATOM   3347 H HZ   A PHE   A 1 156 ? 10.121 6.477   5.954   0.74 28.55 ?  156 PHE   A HZ   1 
ATOM   3348 H HZ   B PHE   A 1 156 ? 10.887 6.730   5.845   0.26 16.52 ?  156 PHE   A HZ   1 
ATOM   3349 N N    A ASP   A 1 157 ? 8.881  0.148   3.906   0.74 18.39 ?  157 ASP   A N    1 
ATOM   3350 N N    B ASP   A 1 157 ? 8.965  0.438   4.440   0.26 11.11 ?  157 ASP   A N    1 
ATOM   3351 C CA   A ASP   A 1 157 ? 7.550  0.387   3.361   0.74 19.23 ?  157 ASP   A CA   1 
ATOM   3352 C CA   B ASP   A 1 157 ? 7.595  0.712   4.019   0.26 11.78 ?  157 ASP   A CA   1 
ATOM   3353 C C    A ASP   A 1 157 ? 6.578  -0.686  3.850   0.74 19.12 ?  157 ASP   A C    1 
ATOM   3354 C C    B ASP   A 1 157 ? 6.652  -0.385  4.500   0.26 12.51 ?  157 ASP   A C    1 
ATOM   3355 O O    A ASP   A 1 157 ? 6.778  -1.874  3.580   0.74 18.07 ?  157 ASP   A O    1 
ATOM   3356 O O    B ASP   A 1 157 ? 6.925  -1.575  4.307   0.26 12.32 ?  157 ASP   A O    1 
ATOM   3357 C CB   A ASP   A 1 157 ? 7.631  0.370   1.840   0.74 20.84 ?  157 ASP   A CB   1 
ATOM   3358 C CB   B ASP   A 1 157 ? 7.533  0.800   2.496   0.26 11.92 ?  157 ASP   A CB   1 
ATOM   3359 C CG   A ASP   A 1 157 ? 6.376  0.901   1.186   0.74 22.50 ?  157 ASP   A CG   1 
ATOM   3360 C CG   B ASP   A 1 157 ? 6.154  1.162   1.994   0.26 12.00 ?  157 ASP   A CG   1 
ATOM   3361 O OD1  A ASP   A 1 157 ? 6.135  2.124   1.264   0.74 24.16 ?  157 ASP   A OD1  1 
ATOM   3362 O OD1  B ASP   A 1 157 ? 5.692  2.293   2.256   0.26 12.19 ?  157 ASP   A OD1  1 
ATOM   3363 O OD2  A ASP   A 1 157 ? 5.621  0.093   0.601   0.74 22.46 -1 157 ASP   A OD2  1 
ATOM   3364 O OD2  B ASP   A 1 157 ? 5.526  0.307   1.341   0.26 11.90 -1 157 ASP   A OD2  1 
ATOM   3365 H H    A ASP   A 1 157 ? 9.376  -0.350  3.411   0.74 22.07 ?  157 ASP   A H    1 
ATOM   3366 H H    B ASP   A 1 157 ? 9.419  -0.023  3.873   0.26 13.33 ?  157 ASP   A H    1 
ATOM   3367 H HA   A ASP   A 1 157 ? 7.228  1.249   3.658   0.74 23.08 ?  157 ASP   A HA   1 
ATOM   3368 H HA   B ASP   A 1 157 ? 7.307  1.560   4.391   0.26 14.14 ?  157 ASP   A HA   1 
ATOM   3369 H HB2  A ASP   A 1 157 ? 8.399  0.902   1.571   0.74 25.01 ?  157 ASP   A HB2  1 
ATOM   3370 H HB2  B ASP   A 1 157 ? 8.152  1.478   2.191   0.26 14.31 ?  157 ASP   A HB2  1 
ATOM   3371 H HB3  A ASP   A 1 157 ? 7.746  -0.545  1.544   0.74 25.01 ?  157 ASP   A HB3  1 
ATOM   3372 H HB3  B ASP   A 1 157 ? 7.772  -0.063  2.121   0.26 14.31 ?  157 ASP   A HB3  1 
ATOM   3373 N N    A LYS   A 1 158 ? 5.517  -0.263  4.552   0.74 20.37 ?  158 LYS   A N    1 
ATOM   3374 N N    B LYS   A 1 158 ? 5.527  0.018   5.101   0.26 13.64 ?  158 LYS   A N    1 
ATOM   3375 C CA   A LYS   A 1 158 ? 4.554  -1.213  5.111   0.74 21.45 ?  158 LYS   A CA   1 
ATOM   3376 C CA   B LYS   A 1 158 ? 4.569  -0.965  5.600   0.26 14.83 ?  158 LYS   A CA   1 
ATOM   3377 C C    A LYS   A 1 158 ? 3.859  -2.008  4.009   0.74 20.88 ?  158 LYS   A C    1 
ATOM   3378 C C    B LYS   A 1 158 ? 3.919  -1.732  4.455   0.26 14.77 ?  158 LYS   A C    1 
ATOM   3379 O O    A LYS   A 1 158 ? 3.685  -3.228  4.122   0.74 20.69 ?  158 LYS   A O    1 
ATOM   3380 O O    B LYS   A 1 158 ? 3.803  -2.962  4.510   0.26 15.40 ?  158 LYS   A O    1 
ATOM   3381 C CB   A LYS   A 1 158 ? 3.542  -0.461  5.988   0.74 23.44 ?  158 LYS   A CB   1 
ATOM   3382 C CB   B LYS   A 1 158 ? 3.511  -0.298  6.483   0.26 16.24 ?  158 LYS   A CB   1 
ATOM   3383 C CG   A LYS   A 1 158 ? 2.349  -1.281  6.486   0.74 25.23 ?  158 LYS   A CG   1 
ATOM   3384 C CG   B LYS   A 1 158 ? 2.335  -1.215  6.850   0.26 17.40 ?  158 LYS   A CG   1 
ATOM   3385 C CD   A LYS   A 1 158 ? 2.762  -2.505  7.300   0.74 26.48 ?  158 LYS   A CD   1 
ATOM   3386 C CD   B LYS   A 1 158 ? 2.775  -2.454  7.631   0.26 18.34 ?  158 LYS   A CD   1 
ATOM   3387 C CE   A LYS   A 1 158 ? 1.530  -3.199  7.866   0.74 27.59 ?  158 LYS   A CE   1 
ATOM   3388 C CE   B LYS   A 1 158 ? 1.571  -3.279  8.071   0.26 19.30 ?  158 LYS   A CE   1 
ATOM   3389 N NZ   A LYS   A 1 158 ? 1.823  -4.556  8.404   0.74 28.01 ?  158 LYS   A NZ   1 
ATOM   3390 N NZ   B LYS   A 1 158 ? 1.960  -4.489  8.848   0.26 19.76 ?  158 LYS   A NZ   1 
ATOM   3391 H H    A LYS   A 1 158 ? 5.340  0.558   4.722   0.74 24.44 ?  158 LYS   A H    1 
ATOM   3392 H H    B LYS   A 1 158 ? 5.304  0.841   5.224   0.26 16.36 ?  158 LYS   A H    1 
ATOM   3393 H HA   A LYS   A 1 158 ? 5.020  -1.842  5.688   0.74 25.74 ?  158 LYS   A HA   1 
ATOM   3394 H HA   B LYS   A 1 158 ? 5.046  -1.604  6.149   0.26 17.80 ?  158 LYS   A HA   1 
ATOM   3395 H HB2  A LYS   A 1 158 ? 4.002  -0.121  6.775   0.74 28.13 ?  158 LYS   A HB2  1 
ATOM   3396 H HB2  B LYS   A 1 158 ? 3.931  -0.013  7.312   0.26 19.49 ?  158 LYS   A HB2  1 
ATOM   3397 H HB3  A LYS   A 1 158 ? 3.185  0.285   5.480   0.74 28.13 ?  158 LYS   A HB3  1 
ATOM   3398 H HB3  B LYS   A 1 158 ? 3.153  0.473   6.017   0.26 19.49 ?  158 LYS   A HB3  1 
ATOM   3399 H HG2  A LYS   A 1 158 ? 1.798  -0.716  7.056   0.74 30.28 ?  158 LYS   A HG2  1 
ATOM   3400 H HG2  B LYS   A 1 158 ? 1.716  -0.720  7.404   0.26 20.88 ?  158 LYS   A HG2  1 
ATOM   3401 H HG3  A LYS   A 1 158 ? 1.830  -1.581  5.726   0.74 30.28 ?  158 LYS   A HG3  1 
ATOM   3402 H HG3  B LYS   A 1 158 ? 1.885  -1.509  6.040   0.26 20.88 ?  158 LYS   A HG3  1 
ATOM   3403 H HD2  A LYS   A 1 158 ? 3.233  -3.129  6.727   0.74 31.77 ?  158 LYS   A HD2  1 
ATOM   3404 H HD2  B LYS   A 1 158 ? 3.336  -3.010  7.070   0.26 22.01 ?  158 LYS   A HD2  1 
ATOM   3405 H HD3  A LYS   A 1 158 ? 3.328  -2.227  8.038   0.74 31.77 ?  158 LYS   A HD3  1 
ATOM   3406 H HD3  B LYS   A 1 158 ? 3.259  -2.177  8.425   0.26 22.01 ?  158 LYS   A HD3  1 
ATOM   3407 H HE2  A LYS   A 1 158 ? 1.159  -2.662  8.583   0.74 33.11 ?  158 LYS   A HE2  1 
ATOM   3408 H HE2  B LYS   A 1 158 ? 0.998  -2.733  8.632   0.26 23.16 ?  158 LYS   A HE2  1 
ATOM   3409 H HE3  A LYS   A 1 158 ? 0.874  -3.296  7.160   0.74 33.11 ?  158 LYS   A HE3  1 
ATOM   3410 H HE3  B LYS   A 1 158 ? 1.080  -3.570  7.285   0.26 23.16 ?  158 LYS   A HE3  1 
ATOM   3411 H HZ1  A LYS   A 1 158 ? 1.076  -4.924  8.725   0.74 33.61 ?  158 LYS   A HZ1  1 
ATOM   3412 H HZ1  B LYS   A 1 158 ? 1.233  -4.946  9.087   0.26 23.72 ?  158 LYS   A HZ1  1 
ATOM   3413 H HZ2  A LYS   A 1 158 ? 2.145  -5.076  7.759   0.74 33.61 ?  158 LYS   A HZ2  1 
ATOM   3414 H HZ2  B LYS   A 1 158 ? 2.481  -5.014  8.354   0.26 23.72 ?  158 LYS   A HZ2  1 
ATOM   3415 H HZ3  A LYS   A 1 158 ? 2.421  -4.502  9.060   0.74 33.61 ?  158 LYS   A HZ3  1 
ATOM   3416 H HZ3  B LYS   A 1 158 ? 2.403  -4.249  9.582   0.26 23.72 ?  158 LYS   A HZ3  1 
ATOM   3417 N N    A ASN   A 1 159 ? 3.459  -1.336  2.931   0.74 21.74 ?  159 ASN   A N    1 
ATOM   3418 N N    B ASN   A 1 159 ? 3.475  -1.028  3.409   0.26 14.11 ?  159 ASN   A N    1 
ATOM   3419 C CA   A ASN   A 1 159 ? 2.800  -2.037  1.835   0.74 22.26 ?  159 ASN   A CA   1 
ATOM   3420 C CA   B ASN   A 1 159 ? 2.868  -1.727  2.279   0.26 13.66 ?  159 ASN   A CA   1 
ATOM   3421 C C    A ASN   A 1 159 ? 3.706  -3.120  1.243   0.74 20.48 ?  159 ASN   A C    1 
ATOM   3422 C C    B ASN   A 1 159 ? 3.821  -2.775  1.721   0.26 13.03 ?  159 ASN   A C    1 
ATOM   3423 O O    A ASN   A 1 159 ? 3.266  -4.251  1.003   0.74 20.54 ?  159 ASN   A O    1 
ATOM   3424 O O    B ASN   A 1 159 ? 3.414  -3.906  1.433   0.26 12.71 ?  159 ASN   A O    1 
ATOM   3425 C CB   A ASN   A 1 159 ? 2.345  -1.016  0.787   0.74 24.79 ?  159 ASN   A CB   1 
ATOM   3426 C CB   B ASN   A 1 159 ? 2.449  -0.740  1.184   0.26 14.36 ?  159 ASN   A CB   1 
ATOM   3427 C CG   A ASN   A 1 159 ? 1.179  -0.165  1.275   0.74 27.43 ?  159 ASN   A CG   1 
ATOM   3428 C CG   B ASN   A 1 159 ? 1.728  -1.422  0.028   0.26 15.46 ?  159 ASN   A CG   1 
ATOM   3429 O OD1  A ASN   A 1 159 ? 0.317  -0.653  2.005   0.74 28.34 ?  159 ASN   A OD1  1 
ATOM   3430 O OD1  B ASN   A 1 159 ? 0.497  -1.443  -0.020  0.26 17.01 ?  159 ASN   A OD1  1 
ATOM   3431 N ND2  A ASN   A 1 159 ? 1.148  1.108   0.878   0.74 28.65 ?  159 ASN   A ND2  1 
ATOM   3432 N ND2  B ASN   A 1 159 ? 2.492  -1.977  -0.911  0.26 15.43 ?  159 ASN   A ND2  1 
ATOM   3433 H H    A ASN   A 1 159 ? 3.562  -0.491  2.818   0.74 26.09 ?  159 ASN   A H    1 
ATOM   3434 H H    B ASN   A 1 159 ? 3.521  -0.174  3.329   0.26 16.94 ?  159 ASN   A H    1 
ATOM   3435 H HA   A ASN   A 1 159 ? 2.006  -2.470  2.184   0.74 26.71 ?  159 ASN   A HA   1 
ATOM   3436 H HA   B ASN   A 1 159 ? 2.072  -2.184  2.586   0.26 16.39 ?  159 ASN   A HA   1 
ATOM   3437 H HB2  A ASN   A 1 159 ? 3.081  -0.419  0.582   0.74 29.75 ?  159 ASN   A HB2  1 
ATOM   3438 H HB2  B ASN   A 1 159 ? 1.842  -0.085  1.561   0.26 17.23 ?  159 ASN   A HB2  1 
ATOM   3439 H HB3  A ASN   A 1 159 ? 2.058  -1.484  -0.007  0.74 29.75 ?  159 ASN   A HB3  1 
ATOM   3440 H HB3  B ASN   A 1 159 ? 3.235  -0.304  0.828   0.26 17.23 ?  159 ASN   A HB3  1 
ATOM   3441 H HD21 A ASN   A 1 159 ? 0.510  1.627   1.132   0.74 34.38 ?  159 ASN   A HD21 1 
ATOM   3442 H HD21 B ASN   A 1 159 ? 2.135  -2.384  -1.582  0.26 18.52 ?  159 ASN   A HD21 1 
ATOM   3443 H HD22 A ASN   A 1 159 ? 1.771  1.416   0.374   0.74 34.38 ?  159 ASN   A HD22 1 
ATOM   3444 H HD22 B ASN   A 1 159 ? 3.351  -1.940  -0.846  0.26 18.52 ?  159 ASN   A HD22 1 
ATOM   3445 N N    A LEU   A 1 160 ? 4.986  -2.805  1.044   0.74 18.76 ?  160 LEU   A N    1 
ATOM   3446 N N    B LEU   A 1 160 ? 5.097  -2.420  1.574   0.26 12.29 ?  160 LEU   A N    1 
ATOM   3447 C CA   A LEU   A 1 160 ? 5.915  -3.788  0.496   0.74 17.51 ?  160 LEU   A CA   1 
ATOM   3448 C CA   B LEU   A 1 160 ? 6.072  -3.387  1.085   0.26 11.11 ?  160 LEU   A CA   1 
ATOM   3449 C C    A LEU   A 1 160 ? 6.136  -4.939  1.466   0.74 16.56 ?  160 LEU   A C    1 
ATOM   3450 C C    B LEU   A 1 160 ? 6.233  -4.547  2.058   0.26 10.61 ?  160 LEU   A C    1 
ATOM   3451 O O    A LEU   A 1 160 ? 6.183  -6.107  1.058   0.74 17.11 ?  160 LEU   A O    1 
ATOM   3452 O O    B LEU   A 1 160 ? 6.276  -5.712  1.645   0.26 10.82 ?  160 LEU   A O    1 
ATOM   3453 C CB   A LEU   A 1 160 ? 7.245  -3.110  0.184   0.74 17.23 ?  160 LEU   A CB   1 
ATOM   3454 C CB   B LEU   A 1 160 ? 7.412  -2.699  0.837   0.26 10.86 ?  160 LEU   A CB   1 
ATOM   3455 C CG   A LEU   A 1 160 ? 8.368  -4.052  -0.236  0.74 17.30 ?  160 LEU   A CG   1 
ATOM   3456 C CG   B LEU   A 1 160 ? 8.536  -3.644  0.411   0.26 10.79 ?  160 LEU   A CG   1 
ATOM   3457 C CD1  A LEU   A 1 160 ? 7.934  -4.813  -1.467  0.74 17.88 ?  160 LEU   A CD1  1 
ATOM   3458 C CD1  B LEU   A 1 160 ? 8.156  -4.425  -0.840  0.26 11.06 ?  160 LEU   A CD1  1 
ATOM   3459 C CD2  A LEU   A 1 160 ? 9.654  -3.290  -0.491  0.74 17.31 ?  160 LEU   A CD2  1 
ATOM   3460 C CD2  B LEU   A 1 160 ? 9.818  -2.864  0.190   0.26 10.56 ?  160 LEU   A CD2  1 
ATOM   3461 H H    A LEU   A 1 160 ? 5.338  -2.049  1.236   0.74 22.52 ?  160 LEU   A H    1 
ATOM   3462 H H    B LEU   A 1 160 ? 5.414  -1.640  1.749   0.26 14.75 ?  160 LEU   A H    1 
ATOM   3463 H HA   A LEU   A 1 160 ? 5.546  -4.146  -0.325  0.74 21.01 ?  160 LEU   A HA   1 
ATOM   3464 H HA   B LEU   A 1 160 ? 5.757  -3.745  0.243   0.26 13.33 ?  160 LEU   A HA   1 
ATOM   3465 H HB2  A LEU   A 1 160 ? 7.104  -2.476  -0.536  0.74 20.67 ?  160 LEU   A HB2  1 
ATOM   3466 H HB2  B LEU   A 1 160 ? 7.297  -2.039  0.134   0.26 13.04 ?  160 LEU   A HB2  1 
ATOM   3467 H HB3  A LEU   A 1 160 ? 7.540  -2.641  0.979   0.74 20.67 ?  160 LEU   A HB3  1 
ATOM   3468 H HB3  B LEU   A 1 160 ? 7.690  -2.259  1.655   0.26 13.04 ?  160 LEU   A HB3  1 
ATOM   3469 H HG   A LEU   A 1 160 ? 8.537  -4.692  0.473   0.74 20.77 ?  160 LEU   A HG   1 
ATOM   3470 H HG   B LEU   A 1 160 ? 8.701  -4.279  1.124   0.26 12.94 ?  160 LEU   A HG   1 
ATOM   3471 H HD11 A LEU   A 1 160 ? 8.681  -5.333  -1.789  0.74 21.45 ?  160 LEU   A HD11 1 
ATOM   3472 H HD11 B LEU   A 1 160 ? 8.937  -4.900  -1.161  0.26 13.27 ?  160 LEU   A HD11 1 
ATOM   3473 H HD12 A LEU   A 1 160 ? 7.197  -5.399  -1.235  0.74 21.45 ?  160 LEU   A HD12 1 
ATOM   3474 H HD12 B LEU   A 1 160 ? 7.453  -5.055  -0.618  0.26 13.27 ?  160 LEU   A HD12 1 
ATOM   3475 H HD13 A LEU   A 1 160 ? 7.651  -4.177  -2.144  0.74 21.45 ?  160 LEU   A HD13 1 
ATOM   3476 H HD13 B LEU   A 1 160 ? 7.845  -3.804  -1.517  0.26 13.27 ?  160 LEU   A HD13 1 
ATOM   3477 H HD21 A LEU   A 1 160 ? 10.345 -3.918  -0.754  0.74 20.77 ?  160 LEU   A HD21 1 
ATOM   3478 H HD21 B LEU   A 1 160 ? 10.519 -3.479  -0.074  0.26 12.68 ?  160 LEU   A HD21 1 
ATOM   3479 H HD22 A LEU   A 1 160 ? 9.503  -2.647  -1.201  0.74 20.77 ?  160 LEU   A HD22 1 
ATOM   3480 H HD22 B LEU   A 1 160 ? 9.672  -2.206  -0.507  0.26 12.68 ?  160 LEU   A HD22 1 
ATOM   3481 H HD23 A LEU   A 1 160 ? 9.916  -2.831  0.322   0.74 20.77 ?  160 LEU   A HD23 1 
ATOM   3482 H HD23 B LEU   A 1 160 ? 10.064 -2.418  1.018   0.26 12.68 ?  160 LEU   A HD23 1 
ATOM   3483 N N    A TYR   A 1 161 ? 6.297  -4.626  2.750   0.74 15.76 ?  161 TYR   A N    1 
ATOM   3484 N N    B TYR   A 1 161 ? 6.326  -4.250  3.356   0.26 10.62 ?  161 TYR   A N    1 
ATOM   3485 C CA   A TYR   A 1 161 ? 6.440  -5.663  3.763   0.74 15.60 ?  161 TYR   A CA   1 
ATOM   3486 C CA   B TYR   A 1 161 ? 6.460  -5.312  4.347   0.26 10.94 ?  161 TYR   A CA   1 
ATOM   3487 C C    A TYR   A 1 161 ? 5.286  -6.654  3.700   0.74 16.19 ?  161 TYR   A C    1 
ATOM   3488 C C    B TYR   A 1 161 ? 5.346  -6.345  4.213   0.26 11.81 ?  161 TYR   A C    1 
ATOM   3489 O O    A TYR   A 1 161 ? 5.494  -7.871  3.642   0.74 15.39 ?  161 TYR   A O    1 
ATOM   3490 O O    B TYR   A 1 161 ? 5.596  -7.554  4.291   0.26 11.54 ?  161 TYR   A O    1 
ATOM   3491 C CB   A TYR   A 1 161 ? 6.510  -5.025  5.151   0.74 15.61 ?  161 TYR   A CB   1 
ATOM   3492 C CB   B TYR   A 1 161 ? 6.487  -4.719  5.760   0.26 11.08 ?  161 TYR   A CB   1 
ATOM   3493 C CG   A TYR   A 1 161 ? 6.391  -6.035  6.265   0.74 15.49 ?  161 TYR   A CG   1 
ATOM   3494 C CG   B TYR   A 1 161 ? 6.402  -5.771  6.842   0.26 11.23 ?  161 TYR   A CG   1 
ATOM   3495 C CD1  A TYR   A 1 161 ? 7.503  -6.732  6.711   0.74 15.29 ?  161 TYR   A CD1  1 
ATOM   3496 C CD1  B TYR   A 1 161 ? 7.535  -6.453  7.268   0.26 11.08 ?  161 TYR   A CD1  1 
ATOM   3497 C CD2  A TYR   A 1 161 ? 5.162  -6.309  6.864   0.74 15.78 ?  161 TYR   A CD2  1 
ATOM   3498 C CD2  B TYR   A 1 161 ? 5.187  -6.092  7.431   0.26 11.68 ?  161 TYR   A CD2  1 
ATOM   3499 C CE1  A TYR   A 1 161 ? 7.400  -7.672  7.718   0.74 15.25 ?  161 TYR   A CE1  1 
ATOM   3500 C CE1  B TYR   A 1 161 ? 7.456  -7.425  8.251   0.26 11.70 ?  161 TYR   A CE1  1 
ATOM   3501 C CE2  A TYR   A 1 161 ? 5.050  -7.251  7.874   0.74 15.60 ?  161 TYR   A CE2  1 
ATOM   3502 C CE2  B TYR   A 1 161 ? 5.099  -7.062  8.413   0.26 12.18 ?  161 TYR   A CE2  1 
ATOM   3503 C CZ   A TYR   A 1 161 ? 6.172  -7.929  8.297   0.74 15.47 ?  161 TYR   A CZ   1 
ATOM   3504 C CZ   B TYR   A 1 161 ? 6.235  -7.725  8.820   0.26 12.33 ?  161 TYR   A CZ   1 
ATOM   3505 O OH   A TYR   A 1 161 ? 6.088  -8.871  9.299   0.74 16.26 ?  161 TYR   A OH   1 
ATOM   3506 O OH   B TYR   A 1 161 ? 6.156  -8.689  9.800   0.26 13.07 ?  161 TYR   A OH   1 
ATOM   3507 H H    A TYR   A 1 161 ? 6.321  -3.839  3.059   0.74 18.92 ?  161 TYR   A H    1 
ATOM   3508 H H    B TYR   A 1 161 ? 6.318  -3.454  3.683   0.26 12.74 ?  161 TYR   A H    1 
ATOM   3509 H HA   A TYR   A 1 161 ? 7.258  -6.164  3.613   0.74 18.72 ?  161 TYR   A HA   1 
ATOM   3510 H HA   B TYR   A 1 161 ? 7.301  -5.768  4.208   0.26 13.12 ?  161 TYR   A HA   1 
ATOM   3511 H HB2  A TYR   A 1 161 ? 7.364  -4.579  5.244   0.74 18.73 ?  161 TYR   A HB2  1 
ATOM   3512 H HB2  B TYR   A 1 161 ? 7.318  -4.230  5.885   0.26 13.29 ?  161 TYR   A HB2  1 
ATOM   3513 H HB3  A TYR   A 1 161 ? 5.785  -4.392  5.244   0.74 18.73 ?  161 TYR   A HB3  1 
ATOM   3514 H HB3  B TYR   A 1 161 ? 5.733  -4.117  5.871   0.26 13.29 ?  161 TYR   A HB3  1 
ATOM   3515 H HD1  A TYR   A 1 161 ? 8.331  -6.574  6.321   0.74 18.34 ?  161 TYR   A HD1  1 
ATOM   3516 H HD1  B TYR   A 1 161 ? 8.361  -6.253  6.888   0.26 13.30 ?  161 TYR   A HD1  1 
ATOM   3517 H HD2  A TYR   A 1 161 ? 4.402  -5.858  6.583   0.74 18.94 ?  161 TYR   A HD2  1 
ATOM   3518 H HD2  B TYR   A 1 161 ? 4.417  -5.649  7.160   0.26 14.02 ?  161 TYR   A HD2  1 
ATOM   3519 H HE1  A TYR   A 1 161 ? 8.156  -8.135  8.008   0.74 18.31 ?  161 TYR   A HE1  1 
ATOM   3520 H HE1  B TYR   A 1 161 ? 8.224  -7.872  8.526   0.26 14.04 ?  161 TYR   A HE1  1 
ATOM   3521 H HE2  A TYR   A 1 161 ? 4.224  -7.422  8.273   0.74 18.72 ?  161 TYR   A HE2  1 
ATOM   3522 H HE2  B TYR   A 1 161 ? 4.276  -7.267  8.797   0.26 14.62 ?  161 TYR   A HE2  1 
ATOM   3523 H HH   A TYR   A 1 161 ? 5.294  -8.930  9.582   0.74 19.51 ?  161 TYR   A HH   1 
ATOM   3524 H HH   B TYR   A 1 161 ? 6.915  -9.014  9.946   0.26 15.68 ?  161 TYR   A HH   1 
ATOM   3525 N N    A ASP   A 1 162 ? 4.053  -6.145  3.732   0.74 17.68 ?  162 ASP   A N    1 
ATOM   3526 N N    B ASP   A 1 162 ? 4.107  -5.893  3.994   0.26 13.23 ?  162 ASP   A N    1 
ATOM   3527 C CA   A ASP   A 1 162 ? 2.888  -7.022  3.649   0.74 18.84 ?  162 ASP   A CA   1 
ATOM   3528 C CA   B ASP   A 1 162 ? 2.992  -6.838  3.954   0.26 14.72 ?  162 ASP   A CA   1 
ATOM   3529 C C    A ASP   A 1 162 ? 2.933  -7.851  2.375   0.74 18.84 ?  162 ASP   A C    1 
ATOM   3530 C C    B ASP   A 1 162 ? 3.037  -7.723  2.714   0.26 15.58 ?  162 ASP   A C    1 
ATOM   3531 O O    A ASP   A 1 162 ? 2.621  -9.050  2.389   0.74 19.40 ?  162 ASP   A O    1 
ATOM   3532 O O    B ASP   A 1 162 ? 2.617  -8.886  2.770   0.26 15.72 ?  162 ASP   A O    1 
ATOM   3533 C CB   A ASP   A 1 162 ? 1.596  -6.194  3.703   0.74 20.21 ?  162 ASP   A CB   1 
ATOM   3534 C CB   B ASP   A 1 162 ? 1.652  -6.104  4.030   0.26 15.22 ?  162 ASP   A CB   1 
ATOM   3535 C CG   A ASP   A 1 162 ? 1.317  -5.607  5.075   0.74 21.72 ?  162 ASP   A CG   1 
ATOM   3536 C CG   B ASP   A 1 162 ? 1.337  -5.599  5.427   0.26 15.78 ?  162 ASP   A CG   1 
ATOM   3537 O OD1  A ASP   A 1 162 ? 1.890  -6.090  6.072   0.74 22.83 ?  162 ASP   A OD1  1 
ATOM   3538 O OD1  B ASP   A 1 162 ? 2.116  -5.882  6.362   0.26 16.51 ?  162 ASP   A OD1  1 
ATOM   3539 O OD2  A ASP   A 1 162 ? 0.485  -4.670  5.152   0.74 22.88 -1 162 ASP   A OD2  1 
ATOM   3540 O OD2  B ASP   A 1 162 ? 0.299  -4.920  5.589   0.26 15.80 -1 162 ASP   A OD2  1 
ATOM   3541 H H    A ASP   A 1 162 ? 3.861  -5.322  3.808   0.74 21.21 ?  162 ASP   A H    1 
ATOM   3542 H H    B ASP   A 1 162 ? 3.891  -5.068  3.865   0.26 15.88 ?  162 ASP   A H    1 
ATOM   3543 H HA   A ASP   A 1 162 ? 2.877  -7.645  4.394   0.74 22.60 ?  162 ASP   A HA   1 
ATOM   3544 H HA   B ASP   A 1 162 ? 3.054  -7.418  4.725   0.26 17.67 ?  162 ASP   A HA   1 
ATOM   3545 H HB2  A ASP   A 1 162 ? 1.672  -5.450  3.093   0.74 24.25 ?  162 ASP   A HB2  1 
ATOM   3546 H HB2  B ASP   A 1 162 ? 1.673  -5.341  3.437   0.26 18.26 ?  162 ASP   A HB2  1 
ATOM   3547 H HB3  A ASP   A 1 162 ? 0.841  -6.752  3.466   0.74 24.25 ?  162 ASP   A HB3  1 
ATOM   3548 H HB3  B ASP   A 1 162 ? 0.944  -6.716  3.762   0.26 18.26 ?  162 ASP   A HB3  1 
ATOM   3549 N N    A LYS   A 1 163 ? 3.320  -7.228  1.261   0.74 19.76 ?  163 LYS   A N    1 
ATOM   3550 N N    B LYS   A 1 163 ? 3.541  -7.200  1.594   0.26 16.62 ?  163 LYS   A N    1 
ATOM   3551 C CA   A LYS   A 1 163 ? 3.454  -7.975  0.018   0.74 20.61 ?  163 LYS   A CA   1 
ATOM   3552 C CA   B LYS   A 1 163 ? 3.534  -7.961  0.347   0.26 17.74 ?  163 LYS   A CA   1 
ATOM   3553 C C    A LYS   A 1 163 ? 4.579  -8.995  0.116   0.74 19.50 ?  163 LYS   A C    1 
ATOM   3554 C C    B LYS   A 1 163 ? 4.562  -9.089  0.371   0.26 16.83 ?  163 LYS   A C    1 
ATOM   3555 O O    A LYS   A 1 163 ? 4.461  -10.104 -0.417  0.74 20.06 ?  163 LYS   A O    1 
ATOM   3556 O O    B LYS   A 1 163 ? 4.291  -10.188 -0.124  0.26 17.12 ?  163 LYS   A O    1 
ATOM   3557 C CB   A LYS   A 1 163 ? 3.686  -7.023  -1.156  0.74 23.36 ?  163 LYS   A CB   1 
ATOM   3558 C CB   B LYS   A 1 163 ? 3.784  -7.018  -0.831  0.26 20.07 ?  163 LYS   A CB   1 
ATOM   3559 C CG   A LYS   A 1 163 ? 3.719  -7.731  -2.501  0.74 26.63 ?  163 LYS   A CG   1 
ATOM   3560 C CG   B LYS   A 1 163 ? 3.821  -7.684  -2.201  0.26 22.29 ?  163 LYS   A CG   1 
ATOM   3561 C CD   A LYS   A 1 163 ? 4.068  -6.781  -3.629  0.74 29.63 ?  163 LYS   A CD   1 
ATOM   3562 C CD   B LYS   A 1 163 ? 4.425  -6.745  -3.234  0.26 24.36 ?  163 LYS   A CD   1 
ATOM   3563 C CE   A LYS   A 1 163 ? 3.982  -7.478  -4.976  0.74 31.91 ?  163 LYS   A CE   1 
ATOM   3564 C CE   B LYS   A 1 163 ? 4.043  -7.135  -4.652  0.26 25.92 ?  163 LYS   A CE   1 
ATOM   3565 N NZ   A LYS   A 1 163 ? 4.640  -6.694  -6.056  0.74 33.10 ?  163 LYS   A NZ   1 
ATOM   3566 N NZ   B LYS   A 1 163 ? 4.682  -6.237  -5.656  0.26 26.79 ?  163 LYS   A NZ   1 
ATOM   3567 H H    A LYS   A 1 163 ? 3.500  -6.383  1.201   0.74 23.72 ?  163 LYS   A H    1 
ATOM   3568 H H    B LYS   A 1 163 ? 3.885  -6.415  1.530   0.26 19.95 ?  163 LYS   A H    1 
ATOM   3569 H HA   A LYS   A 1 163 ? 2.627  -8.451  -0.151  0.74 24.73 ?  163 LYS   A HA   1 
ATOM   3570 H HA   B LYS   A 1 163 ? 2.662  -8.363  0.225   0.26 21.29 ?  163 LYS   A HA   1 
ATOM   3571 H HB2  A LYS   A 1 163 ? 2.965  -6.369  -1.187  0.74 28.04 ?  163 LYS   A HB2  1 
ATOM   3572 H HB2  B LYS   A 1 163 ? 3.072  -6.356  -0.854  0.26 24.09 ?  163 LYS   A HB2  1 
ATOM   3573 H HB3  A LYS   A 1 163 ? 4.534  -6.571  -1.038  0.74 28.04 ?  163 LYS   A HB3  1 
ATOM   3574 H HB3  B LYS   A 1 163 ? 4.635  -6.574  -0.702  0.26 24.09 ?  163 LYS   A HB3  1 
ATOM   3575 H HG2  A LYS   A 1 163 ? 4.389  -8.431  -2.479  0.74 31.96 ?  163 LYS   A HG2  1 
ATOM   3576 H HG2  B LYS   A 1 163 ? 4.367  -8.485  -2.167  0.26 26.75 ?  163 LYS   A HG2  1 
ATOM   3577 H HG3  A LYS   A 1 163 ? 2.844  -8.110  -2.683  0.74 31.96 ?  163 LYS   A HG3  1 
ATOM   3578 H HG3  B LYS   A 1 163 ? 2.918  -7.904  -2.478  0.26 26.75 ?  163 LYS   A HG3  1 
ATOM   3579 H HD2  A LYS   A 1 163 ? 3.444  -6.039  -3.629  0.74 35.56 ?  163 LYS   A HD2  1 
ATOM   3580 H HD2  B LYS   A 1 163 ? 4.105  -5.844  -3.072  0.26 29.23 ?  163 LYS   A HD2  1 
ATOM   3581 H HD3  A LYS   A 1 163 ? 4.975  -6.459  -3.508  0.74 35.56 ?  163 LYS   A HD3  1 
ATOM   3582 H HD3  B LYS   A 1 163 ? 5.393  -6.773  -3.164  0.26 29.23 ?  163 LYS   A HD3  1 
ATOM   3583 H HE2  A LYS   A 1 163 ? 4.414  -8.344  -4.916  0.74 38.29 ?  163 LYS   A HE2  1 
ATOM   3584 H HE2  B LYS   A 1 163 ? 4.327  -8.045  -4.827  0.26 31.11 ?  163 LYS   A HE2  1 
ATOM   3585 H HE3  A LYS   A 1 163 ? 3.049  -7.590  -5.213  0.74 38.29 ?  163 LYS   A HE3  1 
ATOM   3586 H HE3  B LYS   A 1 163 ? 3.082  -7.062  -4.753  0.26 31.11 ?  163 LYS   A HE3  1 
ATOM   3587 H HZ1  A LYS   A 1 163 ? 4.574  -7.127  -6.830  0.74 39.71 ?  163 LYS   A HZ1  1 
ATOM   3588 H HZ1  B LYS   A 1 163 ? 4.446  -6.482  -6.478  0.26 32.15 ?  163 LYS   A HZ1  1 
ATOM   3589 H HZ2  A LYS   A 1 163 ? 4.248  -5.898  -6.135  0.74 39.71 ?  163 LYS   A HZ2  1 
ATOM   3590 H HZ2  B LYS   A 1 163 ? 4.423  -5.396  -5.519  0.26 32.15 ?  163 LYS   A HZ2  1 
ATOM   3591 H HZ3  A LYS   A 1 163 ? 5.501  -6.573  -5.864  0.74 39.71 ?  163 LYS   A HZ3  1 
ATOM   3592 H HZ3  B LYS   A 1 163 ? 5.568  -6.281  -5.584  0.26 32.15 ?  163 LYS   A HZ3  1 
ATOM   3593 N N    A LEU   A 1 164 ? 5.676  -8.634  0.792   0.74 17.71 ?  164 LEU   A N    1 
ATOM   3594 N N    B LEU   A 1 164 ? 5.742  -8.839  0.946   0.26 15.42 ?  164 LEU   A N    1 
ATOM   3595 C CA   A LEU   A 1 164 ? 6.783  -9.570  0.976   0.74 16.70 ?  164 LEU   A CA   1 
ATOM   3596 C CA   B LEU   A 1 164 ? 6.811  -9.836  0.922   0.26 14.10 ?  164 LEU   A CA   1 
ATOM   3597 C C    A LEU   A 1 164 ? 6.368  -10.756 1.837   0.74 16.50 ?  164 LEU   A C    1 
ATOM   3598 C C    B LEU   A 1 164 ? 6.398  -11.101 1.658   0.26 13.62 ?  164 LEU   A C    1 
ATOM   3599 O O    A LEU   A 1 164 ? 6.665  -11.911 1.506   0.74 16.82 ?  164 LEU   A O    1 
ATOM   3600 O O    B LEU   A 1 164 ? 6.739  -12.215 1.242   0.26 13.51 ?  164 LEU   A O    1 
ATOM   3601 C CB   A LEU   A 1 164 ? 7.973  -8.848  1.600   0.74 15.91 ?  164 LEU   A CB   1 
ATOM   3602 C CB   B LEU   A 1 164 ? 8.075  -9.250  1.550   0.26 13.43 ?  164 LEU   A CB   1 
ATOM   3603 C CG   A LEU   A 1 164 ? 8.766  -7.937  0.662   0.74 16.33 ?  164 LEU   A CG   1 
ATOM   3604 C CG   B LEU   A 1 164 ? 8.694  -8.065  0.811   0.26 13.52 ?  164 LEU   A CG   1 
ATOM   3605 C CD1  A LEU   A 1 164 ? 9.665  -7.028  1.478   0.74 15.79 ?  164 LEU   A CD1  1 
ATOM   3606 C CD1  B LEU   A 1 164 ? 9.792  -7.406  1.633   0.26 13.93 ?  164 LEU   A CD1  1 
ATOM   3607 C CD2  A LEU   A 1 164 ? 9.585  -8.734  -0.353  0.74 16.82 ?  164 LEU   A CD2  1 
ATOM   3608 C CD2  B LEU   A 1 164 ? 9.234  -8.524  -0.527  0.26 13.41 ?  164 LEU   A CD2  1 
ATOM   3609 H H    A LEU   A 1 164 ? 5.803  -7.849  1.143   0.74 21.25 ?  164 LEU   A H    1 
ATOM   3610 H H    B LEU   A 1 164 ? 5.941  -8.118  1.366   0.26 18.51 ?  164 LEU   A H    1 
ATOM   3611 H HA   A LEU   A 1 164 ? 7.056  -9.901  0.112   0.74 20.04 ?  164 LEU   A HA   1 
ATOM   3612 H HA   B LEU   A 1 164 ? 7.009  -10.078 0.006   0.26 16.92 ?  164 LEU   A HA   1 
ATOM   3613 H HB2  A LEU   A 1 164 ? 7.654  -8.290  2.330   0.74 19.09 ?  164 LEU   A HB2  1 
ATOM   3614 H HB2  B LEU   A 1 164 ? 7.865  -8.953  2.448   0.26 16.11 ?  164 LEU   A HB2  1 
ATOM   3615 H HB3  A LEU   A 1 164 ? 8.590  -9.508  1.943   0.74 19.09 ?  164 LEU   A HB3  1 
ATOM   3616 H HB3  B LEU   A 1 164 ? 8.749  -9.947  1.590   0.26 16.11 ?  164 LEU   A HB3  1 
ATOM   3617 H HG   A LEU   A 1 164 ? 8.150  -7.372  0.169   0.74 19.59 ?  164 LEU   A HG   1 
ATOM   3618 H HG   B LEU   A 1 164 ? 8.007  -7.401  0.645   0.26 16.23 ?  164 LEU   A HG   1 
ATOM   3619 H HD11 A LEU   A 1 164 ? 10.139 -6.426  0.884   0.74 18.95 ?  164 LEU   A HD11 1 
ATOM   3620 H HD11 B LEU   A 1 164 ? 10.154 -6.655  1.134   0.26 16.72 ?  164 LEU   A HD11 1 
ATOM   3621 H HD12 A LEU   A 1 164 ? 9.120  -6.519  2.099   0.74 18.95 ?  164 LEU   A HD12 1 
ATOM   3622 H HD12 B LEU   A 1 164 ? 9.416  -7.095  2.471   0.26 16.72 ?  164 LEU   A HD12 1 
ATOM   3623 H HD13 A LEU   A 1 164 ? 10.301 -7.572  1.972   0.74 18.95 ?  164 LEU   A HD13 1 
ATOM   3624 H HD13 B LEU   A 1 164 ? 10.492 -8.056  1.805   0.26 16.72 ?  164 LEU   A HD13 1 
ATOM   3625 H HD21 A LEU   A 1 164 ? 10.113 -8.119  -0.888  0.74 20.19 ?  164 LEU   A HD21 1 
ATOM   3626 H HD21 B LEU   A 1 164 ? 9.725  -7.795  -0.935  0.26 16.09 ?  164 LEU   A HD21 1 
ATOM   3627 H HD22 A LEU   A 1 164 ? 10.169 -9.343  0.122   0.74 20.19 ?  164 LEU   A HD22 1 
ATOM   3628 H HD22 B LEU   A 1 164 ? 9.823  -9.282  -0.384  0.26 16.09 ?  164 LEU   A HD22 1 
ATOM   3629 H HD23 A LEU   A 1 164 ? 8.979  -9.232  -0.924  0.74 20.19 ?  164 LEU   A HD23 1 
ATOM   3630 H HD23 B LEU   A 1 164 ? 8.492  -8.783  -1.092  0.26 16.09 ?  164 LEU   A HD23 1 
ATOM   3631 N N    A VAL   A 1 165 ? 5.697  -10.489 2.960   0.74 15.47 ?  165 VAL   A N    1 
ATOM   3632 N N    B VAL   A 1 165 ? 5.668  -10.946 2.760   0.26 13.10 ?  165 VAL   A N    1 
ATOM   3633 C CA   A VAL   A 1 165 ? 5.220  -11.580 3.806   0.74 15.59 ?  165 VAL   A CA   1 
ATOM   3634 C CA   B VAL   A 1 165 ? 5.253  -12.102 3.544   0.26 12.48 ?  165 VAL   A CA   1 
ATOM   3635 C C    A VAL   A 1 165 ? 4.187  -12.410 3.061   0.74 15.39 ?  165 VAL   A C    1 
ATOM   3636 C C    B VAL   A 1 165 ? 4.209  -12.914 2.788   0.26 12.31 ?  165 VAL   A C    1 
ATOM   3637 O O    A VAL   A 1 165 ? 4.282  -13.643 2.988   0.74 15.52 ?  165 VAL   A O    1 
ATOM   3638 O O    B VAL   A 1 165 ? 4.284  -14.147 2.733   0.26 11.97 ?  165 VAL   A O    1 
ATOM   3639 C CB   A VAL   A 1 165 ? 4.658  -11.032 5.129   0.74 15.70 ?  165 VAL   A CB   1 
ATOM   3640 C CB   B VAL   A 1 165 ? 4.751  -11.644 4.926   0.26 12.41 ?  165 VAL   A CB   1 
ATOM   3641 C CG1  A VAL   A 1 165 ? 3.939  -12.135 5.896   0.74 15.98 ?  165 VAL   A CG1  1 
ATOM   3642 C CG1  B VAL   A 1 165 ? 4.272  -12.838 5.739   0.26 12.66 ?  165 VAL   A CG1  1 
ATOM   3643 C CG2  A VAL   A 1 165 ? 5.762  -10.404 5.969   0.74 16.27 ?  165 VAL   A CG2  1 
ATOM   3644 C CG2  B VAL   A 1 165 ? 5.848  -10.895 5.666   0.26 12.42 ?  165 VAL   A CG2  1 
ATOM   3645 H H    A VAL   A 1 165 ? 5.512  -9.694  3.254   0.74 18.57 ?  165 VAL   A H    1 
ATOM   3646 H H    B VAL   A 1 165 ? 5.405  -10.193 3.072   0.26 15.72 ?  165 VAL   A H    1 
ATOM   3647 H HA   A VAL   A 1 165 ? 5.967  -12.152 4.025   0.74 18.71 ?  165 VAL   A HA   1 
ATOM   3648 H HA   B VAL   A 1 165 ? 6.020  -12.677 3.688   0.26 14.98 ?  165 VAL   A HA   1 
ATOM   3649 H HB   A VAL   A 1 165 ? 4.012  -10.330 4.936   0.74 18.84 ?  165 VAL   A HB   1 
ATOM   3650 H HB   B VAL   A 1 165 ? 4.000  -11.045 4.810   0.26 14.89 ?  165 VAL   A HB   1 
ATOM   3651 H HG11 A VAL   A 1 165 ? 3.851  -11.863 6.824   0.74 19.17 ?  165 VAL   A HG11 1 
ATOM   3652 H HG11 B VAL   A 1 165 ? 4.145  -12.565 6.661   0.26 15.19 ?  165 VAL   A HG11 1 
ATOM   3653 H HG12 A VAL   A 1 165 ? 3.057  -12.258 5.508   0.74 19.17 ?  165 VAL   A HG12 1 
ATOM   3654 H HG12 B VAL   A 1 165 ? 3.434  -13.162 5.373   0.26 15.19 ?  165 VAL   A HG12 1 
ATOM   3655 H HG13 A VAL   A 1 165 ? 4.455  -12.945 5.832   0.74 19.17 ?  165 VAL   A HG13 1 
ATOM   3656 H HG13 B VAL   A 1 165 ? 4.944  -13.541 5.696   0.26 15.19 ?  165 VAL   A HG13 1 
ATOM   3657 H HG21 A VAL   A 1 165 ? 5.399  -10.144 6.833   0.74 19.53 ?  165 VAL   A HG21 1 
ATOM   3658 H HG21 B VAL   A 1 165 ? 5.539  -10.683 6.560   0.26 14.90 ?  165 VAL   A HG21 1 
ATOM   3659 H HG22 A VAL   A 1 165 ? 6.472  -11.052 6.094   0.74 19.53 ?  165 VAL   A HG22 1 
ATOM   3660 H HG22 B VAL   A 1 165 ? 6.637  -11.460 5.715   0.26 14.90 ?  165 VAL   A HG22 1 
ATOM   3661 H HG23 A VAL   A 1 165 ? 6.108  -9.620  5.510   0.74 19.53 ?  165 VAL   A HG23 1 
ATOM   3662 H HG23 B VAL   A 1 165 ? 6.055  -10.081 5.183   0.26 14.90 ?  165 VAL   A HG23 1 
ATOM   3663 N N    A SER   A 1 166 ? 3.176  -11.743 2.497   0.74 15.87 ?  166 SER   A N    1 
ATOM   3664 N N    B SER   A 1 166 ? 3.233  -12.241 2.176   0.26 12.98 ?  166 SER   A N    1 
ATOM   3665 C CA   A SER   A 1 166 ? 2.053  -12.466 1.910   0.74 17.07 ?  166 SER   A CA   1 
ATOM   3666 C CA   B SER   A 1 166 ? 2.104  -12.949 1.584   0.26 13.72 ?  166 SER   A CA   1 
ATOM   3667 C C    A SER   A 1 166 ? 2.446  -13.272 0.683   0.74 17.58 ?  166 SER   A C    1 
ATOM   3668 C C    B SER   A 1 166 ? 2.520  -13.793 0.387   0.26 14.31 ?  166 SER   A C    1 
ATOM   3669 O O    A SER   A 1 166 ? 1.754  -14.244 0.353   0.74 19.49 ?  166 SER   A O    1 
ATOM   3670 O O    B SER   A 1 166 ? 1.933  -14.856 0.148   0.26 15.00 ?  166 SER   A O    1 
ATOM   3671 C CB   A SER   A 1 166 ? 0.917  -11.508 1.539   0.74 19.57 ?  166 SER   A CB   1 
ATOM   3672 C CB   B SER   A 1 166 ? 1.019  -11.949 1.189   0.26 14.56 ?  166 SER   A CB   1 
ATOM   3673 O OG   A SER   A 1 166 ? 0.187  -11.086 2.680   0.74 21.78 ?  166 SER   A OG   1 
ATOM   3674 O OG   B SER   A 1 166 ? 0.745  -11.069 2.265   0.26 15.84 ?  166 SER   A OG   1 
ATOM   3675 H H    A SER   A 1 166 ? 3.117  -10.878 2.451   0.74 19.04 ?  166 SER   A H    1 
ATOM   3676 H H    B SER   A 1 166 ? 3.202  -11.390 2.094   0.26 15.58 ?  166 SER   A H    1 
ATOM   3677 H HA   A SER   A 1 166 ? 1.708  -13.082 2.569   0.74 20.48 ?  166 SER   A HA   1 
ATOM   3678 H HA   B SER   A 1 166 ? 1.724  -13.546 2.244   0.26 16.46 ?  166 SER   A HA   1 
ATOM   3679 H HB2  A SER   A 1 166 ? 1.285  -10.734 1.084   0.74 23.48 ?  166 SER   A HB2  1 
ATOM   3680 H HB2  B SER   A 1 166 ? 1.321  -11.434 0.424   0.26 17.47 ?  166 SER   A HB2  1 
ATOM   3681 H HB3  A SER   A 1 166 ? 0.296  -11.968 0.955   0.74 23.48 ?  166 SER   A HB3  1 
ATOM   3682 H HB3  B SER   A 1 166 ? 0.205  -12.430 0.964   0.26 17.47 ?  166 SER   A HB3  1 
ATOM   3683 H HG   A SER   A 1 166 ? -0.411 -10.538 2.456   0.74 26.14 ?  166 SER   A HG   1 
ATOM   3684 H HG   B SER   A 1 166 ? 1.422  -10.596 2.430   0.26 19.01 ?  166 SER   A HG   1 
ATOM   3685 N N    A SER   A 1 167 ? 3.529  -12.900 0.002   0.74 17.24 ?  167 SER   A N    1 
ATOM   3686 N N    B SER   A 1 167 ? 3.526  -13.352 -0.364  0.26 14.39 ?  167 SER   A N    1 
ATOM   3687 C CA   A SER   A 1 167 ? 3.957  -13.605 -1.198  0.74 17.72 ?  167 SER   A CA   1 
ATOM   3688 C CA   B SER   A 1 167 ? 3.957  -14.038 -1.572  0.26 15.11 ?  167 SER   A CA   1 
ATOM   3689 C C    A SER   A 1 167 ? 5.110  -14.570 -0.949  0.74 17.71 ?  167 SER   A C    1 
ATOM   3690 C C    B SER   A 1 167 ? 5.145  -14.959 -1.340  0.26 15.83 ?  167 SER   A C    1 
ATOM   3691 O O    A SER   A 1 167 ? 5.614  -15.166 -1.905  0.74 18.75 ?  167 SER   A O    1 
ATOM   3692 O O    B SER   A 1 167 ? 5.616  -15.591 -2.291  0.26 16.12 ?  167 SER   A O    1 
ATOM   3693 C CB   A SER   A 1 167 ? 4.358  -12.608 -2.296  0.74 18.35 ?  167 SER   A CB   1 
ATOM   3694 C CB   B SER   A 1 167 ? 4.300  -13.018 -2.663  0.26 14.87 ?  167 SER   A CB   1 
ATOM   3695 O OG   A SER   A 1 167 ? 5.417  -11.767 -1.860  0.74 18.34 ?  167 SER   A OG   1 
ATOM   3696 O OG   B SER   A 1 167 ? 5.481  -12.306 -2.340  0.26 14.53 ?  167 SER   A OG   1 
ATOM   3697 H H    A SER   A 1 167 ? 4.038  -12.228 0.217   0.74 20.69 ?  167 SER   A H    1 
ATOM   3698 H H    B SER   A 1 167 ? 3.987  -12.649 -0.182  0.26 17.27 ?  167 SER   A H    1 
ATOM   3699 H HA   A SER   A 1 167 ? 3.205  -14.113 -1.532  0.74 21.27 ?  167 SER   A HA   1 
ATOM   3700 H HA   B SER   A 1 167 ? 3.229  -14.583 -1.898  0.26 18.13 ?  167 SER   A HA   1 
ATOM   3701 H HB2  A SER   A 1 167 ? 4.658  -13.107 -3.074  0.74 22.03 ?  167 SER   A HB2  1 
ATOM   3702 H HB2  B SER   A 1 167 ? 4.434  -13.486 -3.501  0.26 17.84 ?  167 SER   A HB2  1 
ATOM   3703 H HB3  A SER   A 1 167 ? 3.583  -12.071 -2.534  0.74 22.03 ?  167 SER   A HB3  1 
ATOM   3704 H HB3  B SER   A 1 167 ? 3.564  -12.390 -2.748  0.26 17.84 ?  167 SER   A HB3  1 
ATOM   3705 H HG   A SER   A 1 167 ? 5.184  -11.366 -1.156  0.74 22.01 ?  167 SER   A HG   1 
ATOM   3706 H HG   B SER   A 1 167 ? 5.376  -11.892 -1.615  0.26 17.44 ?  167 SER   A HG   1 
ATOM   3707 N N    A PHE   A 1 168 ? 5.545  -14.738 0.297   0.74 16.87 ?  168 PHE   A N    1 
ATOM   3708 N N    B PHE   A 1 168 ? 5.635  -15.059 -0.108  0.26 16.60 ?  168 PHE   A N    1 
ATOM   3709 C CA   A PHE   A 1 168 ? 6.725  -15.549 0.573   0.74 17.18 ?  168 PHE   A CA   1 
ATOM   3710 C CA   B PHE   A 1 168 ? 6.813  -15.873 0.151   0.26 17.74 ?  168 PHE   A CA   1 
ATOM   3711 C C    A PHE   A 1 168 ? 6.410  -17.032 0.450   0.74 19.09 ?  168 PHE   A C    1 
ATOM   3712 C C    B PHE   A 1 168 ? 6.464  -17.350 0.042   0.26 20.63 ?  168 PHE   A C    1 
ATOM   3713 O O    A PHE   A 1 168 ? 5.466  -17.529 1.070   0.74 20.04 ?  168 PHE   A O    1 
ATOM   3714 O O    B PHE   A 1 168 ? 5.465  -17.808 0.605   0.26 21.02 ?  168 PHE   A O    1 
ATOM   3715 C CB   A PHE   A 1 168 ? 7.248  -15.275 1.977   0.74 16.30 ?  168 PHE   A CB   1 
ATOM   3716 C CB   B PHE   A 1 168 ? 7.377  -15.581 1.537   0.26 16.46 ?  168 PHE   A CB   1 
ATOM   3717 C CG   A PHE   A 1 168 ? 8.517  -16.012 2.282   0.74 15.29 ?  168 PHE   A CG   1 
ATOM   3718 C CG   B PHE   A 1 168 ? 8.599  -16.387 1.863   0.26 15.22 ?  168 PHE   A CG   1 
ATOM   3719 C CD1  A PHE   A 1 168 ? 9.696  -15.628 1.681   0.74 15.63 ?  168 PHE   A CD1  1 
ATOM   3720 C CD1  B PHE   A 1 168 ? 9.801  -16.128 1.226   0.26 14.68 ?  168 PHE   A CD1  1 
ATOM   3721 C CD2  A PHE   A 1 168 ? 8.537  -17.098 3.142   0.74 15.07 ?  168 PHE   A CD2  1 
ATOM   3722 C CD2  B PHE   A 1 168 ? 8.547  -17.414 2.792   0.26 14.67 ?  168 PHE   A CD2  1 
ATOM   3723 C CE1  A PHE   A 1 168 ? 10.874 -16.296 1.937   0.74 15.23 ?  168 PHE   A CE1  1 
ATOM   3724 C CE1  B PHE   A 1 168 ? 10.931 -16.869 1.515   0.26 14.37 ?  168 PHE   A CE1  1 
ATOM   3725 C CE2  A PHE   A 1 168 ? 9.721  -17.766 3.404   0.74 15.18 ?  168 PHE   A CE2  1 
ATOM   3726 C CE2  B PHE   A 1 168 ? 9.676  -18.158 3.085   0.26 14.55 ?  168 PHE   A CE2  1 
ATOM   3727 C CZ   A PHE   A 1 168 ? 10.886 -17.363 2.797   0.74 15.31 ?  168 PHE   A CZ   1 
ATOM   3728 C CZ   B PHE   A 1 168 ? 10.867 -17.886 2.444   0.26 14.42 ?  168 PHE   A CZ   1 
ATOM   3729 H H    A PHE   A 1 168 ? 5.183  -14.380 0.998   0.74 20.24 ?  168 PHE   A H    1 
ATOM   3730 H H    B PHE   A 1 168 ? 5.306  -14.673 0.587   0.26 19.92 ?  168 PHE   A H    1 
ATOM   3731 H HA   A PHE   A 1 168 ? 7.419  -15.325 -0.068  0.74 20.61 ?  168 PHE   A HA   1 
ATOM   3732 H HA   B PHE   A 1 168 ? 7.494  -15.671 -0.507  0.26 21.29 ?  168 PHE   A HA   1 
ATOM   3733 H HB2  A PHE   A 1 168 ? 7.425  -14.324 2.067   0.74 19.56 ?  168 PHE   A HB2  1 
ATOM   3734 H HB2  B PHE   A 1 168 ? 7.619  -14.645 1.587   0.26 19.75 ?  168 PHE   A HB2  1 
ATOM   3735 H HB3  A PHE   A 1 168 ? 6.578  -15.548 2.620   0.74 19.56 ?  168 PHE   A HB3  1 
ATOM   3736 H HB3  B PHE   A 1 168 ? 6.700  -15.785 2.201   0.26 19.75 ?  168 PHE   A HB3  1 
ATOM   3737 H HD1  A PHE   A 1 168 ? 9.701  -14.903 1.097   0.74 18.76 ?  168 PHE   A HD1  1 
ATOM   3738 H HD1  B PHE   A 1 168 ? 9.848  -15.445 0.597   0.26 17.62 ?  168 PHE   A HD1  1 
ATOM   3739 H HD2  A PHE   A 1 168 ? 7.748  -17.372 3.555   0.74 18.08 ?  168 PHE   A HD2  1 
ATOM   3740 H HD2  B PHE   A 1 168 ? 7.747  -17.604 3.227   0.26 17.60 ?  168 PHE   A HD2  1 
ATOM   3741 H HE1  A PHE   A 1 168 ? 11.669 -16.023 1.530   0.74 18.27 ?  168 PHE   A HE1  1 
ATOM   3742 H HE1  B PHE   A 1 168 ? 11.733 -16.684 1.080   0.26 17.25 ?  168 PHE   A HE1  1 
ATOM   3743 H HE2  A PHE   A 1 168 ? 9.723  -18.490 3.986   0.74 18.22 ?  168 PHE   A HE2  1 
ATOM   3744 H HE2  B PHE   A 1 168 ? 9.632  -18.845 3.711   0.26 17.46 ?  168 PHE   A HE2  1 
ATOM   3745 H HZ   A PHE   A 1 168 ? 11.682 -17.813 2.973   0.74 18.37 ?  168 PHE   A HZ   1 
ATOM   3746 H HZ   B PHE   A 1 168 ? 11.626 -18.388 2.640   0.26 17.30 ?  168 PHE   A HZ   1 
ATOM   3747 N N    A LEU   A 1 169 ? 7.232  -17.746 -0.312  0.74 22.08 ?  169 LEU   A N    1 
ATOM   3748 N N    B LEU   A 1 169 ? 7.293  -18.095 -0.679  0.26 23.22 ?  169 LEU   A N    1 
ATOM   3749 C CA   A LEU   A 1 169 ? 7.048  -19.180 -0.470  0.74 26.52 ?  169 LEU   A CA   1 
ATOM   3750 C CA   B LEU   A 1 169 ? 7.085  -19.527 -0.834  0.26 25.88 ?  169 LEU   A CA   1 
ATOM   3751 C C    A LEU   A 1 169 ? 7.930  -19.931 0.515   0.74 27.62 ?  169 LEU   A C    1 
ATOM   3752 C C    B LEU   A 1 169 ? 8.027  -20.307 0.074   0.26 26.68 ?  169 LEU   A C    1 
ATOM   3753 O O    A LEU   A 1 169 ? 7.440  -20.429 1.531   0.74 28.19 ?  169 LEU   A O    1 
ATOM   3754 O O    B LEU   A 1 169 ? 7.588  -21.086 0.921   0.26 27.01 ?  169 LEU   A O    1 
ATOM   3755 C CB   A LEU   A 1 169 ? 7.350  -19.611 -1.908  0.74 29.15 ?  169 LEU   A CB   1 
ATOM   3756 C CB   B LEU   A 1 169 ? 7.303  -19.945 -2.288  0.26 27.38 ?  169 LEU   A CB   1 
ATOM   3757 C CG   A LEU   A 1 169 ? 7.042  -21.074 -2.241  0.74 31.35 ?  169 LEU   A CG   1 
ATOM   3758 C CG   B LEU   A 1 169 ? 7.109  -21.433 -2.583  0.26 28.59 ?  169 LEU   A CG   1 
ATOM   3759 C CD1  A LEU   A 1 169 ? 5.625  -21.438 -1.825  0.74 32.17 ?  169 LEU   A CD1  1 
ATOM   3760 C CD1  B LEU   A 1 169 ? 5.791  -21.924 -2.007  0.26 29.01 ?  169 LEU   A CD1  1 
ATOM   3761 C CD2  A LEU   A 1 169 ? 7.249  -21.344 -3.725  0.74 32.04 ?  169 LEU   A CD2  1 
ATOM   3762 C CD2  B LEU   A 1 169 ? 7.168  -21.689 -4.079  0.26 28.97 ?  169 LEU   A CD2  1 
ATOM   3763 O OXT  A LEU   A 1 169 ? 9.142  -20.047 0.327   0.74 27.36 -1 169 LEU   A OXT  1 
ATOM   3764 O OXT  B LEU   A 1 169 ? 9.247  -20.173 -0.016  0.26 26.89 -1 169 LEU   A OXT  1 
ATOM   3765 H H    A LEU   A 1 169 ? 7.899  -17.422 -0.743  0.74 26.49 ?  169 LEU   A H    1 
ATOM   3766 H H    B LEU   A 1 169 ? 7.982  -17.791 -1.093  0.26 27.86 ?  169 LEU   A H    1 
ATOM   3767 H HA   A LEU   A 1 169 ? 6.130  -19.405 -0.266  0.74 31.82 ?  169 LEU   A HA   1 
ATOM   3768 H HA   B LEU   A 1 169 ? 6.173  -19.741 -0.584  0.26 31.06 ?  169 LEU   A HA   1 
ATOM   3769 H HB2  A LEU   A 1 169 ? 6.822  -19.061 -2.507  0.74 34.98 ?  169 LEU   A HB2  1 
ATOM   3770 H HB2  B LEU   A 1 169 ? 6.679  -19.455 -2.845  0.26 32.85 ?  169 LEU   A HB2  1 
ATOM   3771 H HB3  A LEU   A 1 169 ? 8.292  -19.467 -2.082  0.74 34.98 ?  169 LEU   A HB3  1 
ATOM   3772 H HB3  B LEU   A 1 169 ? 8.211  -19.715 -2.539  0.26 32.85 ?  169 LEU   A HB3  1 
ATOM   3773 H HG   A LEU   A 1 169 ? 7.652  -21.646 -1.749  0.74 37.63 ?  169 LEU   A HG   1 
ATOM   3774 H HG   B LEU   A 1 169 ? 7.827  -21.935 -2.165  0.26 34.31 ?  169 LEU   A HG   1 
ATOM   3775 H HD11 A LEU   A 1 169 ? 5.381  -22.280 -2.238  0.74 38.61 ?  169 LEU   A HD11 1 
ATOM   3776 H HD11 B LEU   A 1 169 ? 5.598  -22.801 -2.371  0.26 34.81 ?  169 LEU   A HD11 1 
ATOM   3777 H HD12 A LEU   A 1 169 ? 5.591  -21.521 -0.859  0.74 38.61 ?  169 LEU   A HD12 1 
ATOM   3778 H HD12 B LEU   A 1 169 ? 5.867  -21.976 -1.041  0.26 34.81 ?  169 LEU   A HD12 1 
ATOM   3779 H HD13 A LEU   A 1 169 ? 5.021  -20.738 -2.120  0.74 38.61 ?  169 LEU   A HD13 1 
ATOM   3780 H HD13 B LEU   A 1 169 ? 5.089  -21.301 -2.253  0.26 34.81 ?  169 LEU   A HD13 1 
ATOM   3781 H HD21 A LEU   A 1 169 ? 7.055  -22.278 -3.907  0.74 38.45 ?  169 LEU   A HD21 1 
ATOM   3782 H HD21 B LEU   A 1 169 ? 7.049  -22.637 -4.242  0.26 34.77 ?  169 LEU   A HD21 1 
ATOM   3783 H HD22 A LEU   A 1 169 ? 6.649  -20.777 -4.236  0.74 38.45 ?  169 LEU   A HD22 1 
ATOM   3784 H HD22 B LEU   A 1 169 ? 6.460  -21.186 -4.512  0.26 34.77 ?  169 LEU   A HD22 1 
ATOM   3785 H HD23 A LEU   A 1 169 ? 8.169  -21.147 -3.957  0.74 38.45 ?  169 LEU   A HD23 1 
ATOM   3786 H HD23 B LEU   A 1 169 ? 8.031  -21.400 -4.415  0.26 34.77 ?  169 LEU   A HD23 1 
ATOM   3787 N N    A SER   B 1 1   ? 50.790 -9.227  -23.757 0.74 27.20 ?  1   SER   B N    1 
ATOM   3788 N N    B SER   B 1 1   ? 50.763 -9.269  -23.773 0.26 27.06 ?  1   SER   B N    1 
ATOM   3789 C CA   A SER   B 1 1   ? 51.262 -10.282 -22.840 0.74 26.83 ?  1   SER   B CA   1 
ATOM   3790 C CA   B SER   B 1 1   ? 51.237 -10.276 -22.799 0.26 27.00 ?  1   SER   B CA   1 
ATOM   3791 C C    A SER   B 1 1   ? 50.187 -11.337 -22.613 0.74 25.66 ?  1   SER   B C    1 
ATOM   3792 C C    B SER   B 1 1   ? 50.175 -11.344 -22.578 0.26 26.62 ?  1   SER   B C    1 
ATOM   3793 O O    A SER   B 1 1   ? 48.995 -11.142 -22.909 0.74 24.89 ?  1   SER   B O    1 
ATOM   3794 O O    B SER   B 1 1   ? 49.010 -11.172 -22.946 0.26 26.31 ?  1   SER   B O    1 
ATOM   3795 C CB   A SER   B 1 1   ? 51.694 -9.685  -21.501 0.74 27.70 ?  1   SER   B CB   1 
ATOM   3796 C CB   B SER   B 1 1   ? 51.584 -9.612  -21.470 0.26 27.34 ?  1   SER   B CB   1 
ATOM   3797 O OG   A SER   B 1 1   ? 50.573 -9.443  -20.672 0.74 29.40 ?  1   SER   B OG   1 
ATOM   3798 O OG   B SER   B 1 1   ? 50.412 -9.328  -20.728 0.26 27.94 ?  1   SER   B OG   1 
ATOM   3799 H H1   A SER   B 1 1   ? 50.698 -9.572  -24.569 0.74 32.65 ?  1   SER   B H1   1 
ATOM   3800 H H1   B SER   B 1 1   ? 50.718 -9.643  -24.577 0.26 32.47 ?  1   SER   B H1   1 
ATOM   3801 H H2   A SER   B 1 1   ? 50.013 -8.919  -23.466 0.74 32.65 ?  1   SER   B H2   1 
ATOM   3802 H H2   B SER   B 1 1   ? 49.962 -8.983  -23.526 0.26 32.47 ?  1   SER   B H2   1 
ATOM   3803 H H3   A SER   B 1 1   ? 51.390 -8.572  -23.774 0.74 32.65 ?  1   SER   B H3   1 
ATOM   3804 H H3   B SER   B 1 1   ? 51.337 -8.592  -23.787 0.26 32.47 ?  1   SER   B H3   1 
ATOM   3805 H HA   A SER   B 1 1   ? 52.032 -10.709 -23.242 0.74 32.20 ?  1   SER   B HA   1 
ATOM   3806 H HA   B SER   B 1 1   ? 52.032 -10.694 -23.155 0.26 32.40 ?  1   SER   B HA   1 
ATOM   3807 H HB2  A SER   B 1 1   ? 52.283 -10.313 -21.057 0.74 33.24 ?  1   SER   B HB2  1 
ATOM   3808 H HB2  B SER   B 1 1   ? 52.152 -10.214 -20.966 0.26 32.81 ?  1   SER   B HB2  1 
ATOM   3809 H HB3  A SER   B 1 1   ? 52.162 -8.849  -21.662 0.74 33.24 ?  1   SER   B HB3  1 
ATOM   3810 H HB3  B SER   B 1 1   ? 52.050 -8.780  -21.644 0.26 32.81 ?  1   SER   B HB3  1 
ATOM   3811 H HG   A SER   B 1 1   ? 50.805 -8.969  -20.016 0.74 35.28 ?  1   SER   B HG   1 
ATOM   3812 H HG   B SER   B 1 1   ? 50.607 -8.861  -20.059 0.26 33.53 ?  1   SER   B HG   1 
ATOM   3813 N N    A MET   B 1 2   ? 50.632 -12.463 -22.075 0.74 25.51 ?  2   MET   B N    1 
ATOM   3814 N N    B MET   B 1 2   ? 50.589 -12.444 -21.962 0.26 26.58 ?  2   MET   B N    1 
ATOM   3815 C CA   A MET   B 1 2   ? 49.808 -13.650 -21.904 0.74 25.60 ?  2   MET   B CA   1 
ATOM   3816 C CA   B MET   B 1 2   ? 49.755 -13.627 -21.794 0.26 26.41 ?  2   MET   B CA   1 
ATOM   3817 C C    A MET   B 1 2   ? 49.565 -13.843 -20.415 0.74 22.95 ?  2   MET   B C    1 
ATOM   3818 C C    B MET   B 1 2   ? 49.490 -13.829 -20.309 0.26 24.46 ?  2   MET   B C    1 
ATOM   3819 O O    A MET   B 1 2   ? 50.502 -14.115 -19.659 0.74 23.11 ?  2   MET   B O    1 
ATOM   3820 O O    B MET   B 1 2   ? 50.390 -14.227 -19.561 0.26 24.70 ?  2   MET   B O    1 
ATOM   3821 C CB   A MET   B 1 2   ? 50.535 -14.848 -22.502 0.74 29.61 ?  2   MET   B CB   1 
ATOM   3822 C CB   B MET   B 1 2   ? 50.472 -14.832 -22.386 0.26 28.40 ?  2   MET   B CB   1 
ATOM   3823 C CG   A MET   B 1 2   ? 49.683 -16.092 -22.677 0.74 33.13 ?  2   MET   B CG   1 
ATOM   3824 C CG   B MET   B 1 2   ? 49.567 -15.986 -22.783 0.26 30.11 ?  2   MET   B CG   1 
ATOM   3825 S SD   A MET   B 1 2   ? 50.527 -17.326 -23.684 0.74 36.35 ?  2   MET   B SD   1 
ATOM   3826 S SD   B MET   B 1 2   ? 50.437 -17.189 -23.800 0.26 31.57 ?  2   MET   B SD   1 
ATOM   3827 C CE   A MET   B 1 2   ? 51.098 -16.290 -25.023 0.74 36.82 ?  2   MET   B CE   1 
ATOM   3828 C CE   B MET   B 1 2   ? 51.423 -16.090 -24.809 0.26 31.85 ?  2   MET   B CE   1 
ATOM   3829 H H    A MET   B 1 2   ? 51.440 -12.573 -21.792 0.74 30.61 ?  2   MET   B H    1 
ATOM   3830 H H    B MET   B 1 2   ? 51.379 -12.535 -21.634 0.26 31.90 ?  2   MET   B H    1 
ATOM   3831 H HA   A MET   B 1 2   ? 48.967 -13.543 -22.367 0.74 30.72 ?  2   MET   B HA   1 
ATOM   3832 H HA   B MET   B 1 2   ? 48.920 -13.511 -22.274 0.26 31.69 ?  2   MET   B HA   1 
ATOM   3833 H HB2  A MET   B 1 2   ? 50.865 -14.566 -23.365 0.74 35.53 ?  2   MET   B HB2  1 
ATOM   3834 H HB2  B MET   B 1 2   ? 50.936 -14.497 -23.163 0.26 34.08 ?  2   MET   B HB2  1 
ATOM   3835 H HB3  A MET   B 1 2   ? 51.279 -15.095 -21.935 0.74 35.53 ?  2   MET   B HB3  1 
ATOM   3836 H HB3  B MET   B 1 2   ? 51.113 -15.182 -21.751 0.26 34.08 ?  2   MET   B HB3  1 
ATOM   3837 H HG2  A MET   B 1 2   ? 49.499 -16.478 -21.803 0.74 39.76 ?  2   MET   B HG2  1 
ATOM   3838 H HG2  B MET   B 1 2   ? 49.254 -16.434 -21.979 0.26 36.13 ?  2   MET   B HG2  1 
ATOM   3839 H HG3  A MET   B 1 2   ? 48.854 -15.861 -23.124 0.74 39.76 ?  2   MET   B HG3  1 
ATOM   3840 H HG3  B MET   B 1 2   ? 48.814 -15.656 -23.292 0.26 36.13 ?  2   MET   B HG3  1 
ATOM   3841 H HE1  A MET   B 1 2   ? 51.265 -16.844 -25.788 0.74 44.19 ?  2   MET   B HE1  1 
ATOM   3842 H HE1  B MET   B 1 2   ? 51.727 -16.575 -25.574 0.26 38.23 ?  2   MET   B HE1  1 
ATOM   3843 H HE2  A MET   B 1 2   ? 50.405 -15.638 -25.222 0.74 44.19 ?  2   MET   B HE2  1 
ATOM   3844 H HE2  B MET   B 1 2   ? 50.871 -15.337 -25.088 0.26 38.23 ?  2   MET   B HE2  1 
ATOM   3845 H HE3  A MET   B 1 2   ? 51.914 -15.832 -24.754 0.74 44.19 ?  2   MET   B HE3  1 
ATOM   3846 H HE3  B MET   B 1 2   ? 52.184 -15.771 -24.289 0.26 38.23 ?  2   MET   B HE3  1 
ATOM   3847 N N    A VAL   B 1 3   ? 48.313 -13.681 -19.995 0.74 20.50 ?  3   VAL   B N    1 
ATOM   3848 N N    B VAL   B 1 3   ? 48.261 -13.553 -19.886 0.26 22.25 ?  3   VAL   B N    1 
ATOM   3849 C CA   A VAL   B 1 3   ? 47.902 -13.932 -18.620 0.74 19.50 ?  3   VAL   B CA   1 
ATOM   3850 C CA   B VAL   B 1 3   ? 47.830 -13.802 -18.518 0.26 20.25 ?  3   VAL   B CA   1 
ATOM   3851 C C    A VAL   B 1 3   ? 46.669 -14.823 -18.643 0.74 17.86 ?  3   VAL   B C    1 
ATOM   3852 C C    B VAL   B 1 3   ? 46.573 -14.657 -18.545 0.26 18.00 ?  3   VAL   B C    1 
ATOM   3853 O O    A VAL   B 1 3   ? 45.956 -14.917 -19.646 0.74 18.27 ?  3   VAL   B O    1 
ATOM   3854 O O    B VAL   B 1 3   ? 45.748 -14.560 -19.459 0.26 17.70 ?  3   VAL   B O    1 
ATOM   3855 C CB   A VAL   B 1 3   ? 47.618 -12.628 -17.840 0.74 21.50 ?  3   VAL   B CB   1 
ATOM   3856 C CB   B VAL   B 1 3   ? 47.578 -12.503 -17.723 0.26 20.78 ?  3   VAL   B CB   1 
ATOM   3857 C CG1  A VAL   B 1 3   ? 48.881 -11.767 -17.748 0.74 22.04 ?  3   VAL   B CG1  1 
ATOM   3858 C CG1  B VAL   B 1 3   ? 48.847 -11.666 -17.647 0.26 20.97 ?  3   VAL   B CG1  1 
ATOM   3859 C CG2  A VAL   B 1 3   ? 46.479 -11.855 -18.490 0.74 22.47 ?  3   VAL   B CG2  1 
ATOM   3860 C CG2  B VAL   B 1 3   ? 46.436 -11.713 -18.340 0.26 21.03 ?  3   VAL   B CG2  1 
ATOM   3861 H H    A VAL   B 1 3   ? 47.671 -13.426 -20.502 0.74 24.60 ?  3   VAL   B H    1 
ATOM   3862 H H    B VAL   B 1 3   ? 47.653 -13.213 -20.390 0.26 26.70 ?  3   VAL   B H    1 
ATOM   3863 H HA   A VAL   B 1 3   ? 48.608 -14.410 -18.155 0.74 23.40 ?  3   VAL   B HA   1 
ATOM   3864 H HA   B VAL   B 1 3   ? 48.523 -14.302 -18.062 0.26 24.30 ?  3   VAL   B HA   1 
ATOM   3865 H HB   A VAL   B 1 3   ? 47.350 -12.855 -16.936 0.74 25.81 ?  3   VAL   B HB   1 
ATOM   3866 H HB   B VAL   B 1 3   ? 47.323 -12.741 -16.818 0.26 24.94 ?  3   VAL   B HB   1 
ATOM   3867 H HG11 A VAL   B 1 3   ? 48.679 -10.964 -17.245 0.74 26.45 ?  3   VAL   B HG11 1 
ATOM   3868 H HG11 B VAL   B 1 3   ? 48.666 -10.871 -17.123 0.26 25.17 ?  3   VAL   B HG11 1 
ATOM   3869 H HG12 A VAL   B 1 3   ? 49.576 -12.274 -17.298 0.74 26.45 ?  3   VAL   B HG12 1 
ATOM   3870 H HG12 B VAL   B 1 3   ? 49.545 -12.190 -17.224 0.26 25.17 ?  3   VAL   B HG12 1 
ATOM   3871 H HG13 A VAL   B 1 3   ? 49.169 -11.534 -18.644 0.74 26.45 ?  3   VAL   B HG13 1 
ATOM   3872 H HG13 B VAL   B 1 3   ? 49.116 -11.419 -18.545 0.26 25.17 ?  3   VAL   B HG13 1 
ATOM   3873 H HG21 A VAL   B 1 3   ? 46.429 -10.975 -18.091 0.74 26.96 ?  3   VAL   B HG21 1 
ATOM   3874 H HG21 B VAL   B 1 3   ? 46.410 -10.834 -17.936 0.26 25.23 ?  3   VAL   B HG21 1 
ATOM   3875 H HG22 A VAL   B 1 3   ? 46.650 -11.781 -19.441 0.74 26.96 ?  3   VAL   B HG22 1 
ATOM   3876 H HG22 B VAL   B 1 3   ? 46.585 -11.636 -19.295 0.26 25.23 ?  3   VAL   B HG22 1 
ATOM   3877 H HG23 A VAL   B 1 3   ? 45.648 -12.335 -18.340 0.74 26.96 ?  3   VAL   B HG23 1 
ATOM   3878 H HG23 B VAL   B 1 3   ? 45.601 -12.180 -18.173 0.26 25.23 ?  3   VAL   B HG23 1 
ATOM   3879 N N    . ASN   B 1 4   ? 46.423 -15.488 -17.516 1.00 16.32 ?  4   ASN   B N    1 
ATOM   3880 C CA   . ASN   B 1 4   ? 45.286 -16.400 -17.400 1.00 15.00 ?  4   ASN   B CA   1 
ATOM   3881 C C    . ASN   B 1 4   ? 45.226 -17.373 -18.576 1.00 15.27 ?  4   ASN   B C    1 
ATOM   3882 O O    . ASN   B 1 4   ? 44.161 -17.635 -19.132 1.00 15.96 ?  4   ASN   B O    1 
ATOM   3883 C CB   . ASN   B 1 4   ? 43.965 -15.644 -17.222 1.00 14.39 ?  4   ASN   B CB   1 
ATOM   3884 C CG   . ASN   B 1 4   ? 43.938 -14.838 -15.942 1.00 13.54 ?  4   ASN   B CG   1 
ATOM   3885 O OD1  . ASN   B 1 4   ? 44.234 -15.350 -14.867 1.00 13.53 ?  4   ASN   B OD1  1 
ATOM   3886 N ND2  . ASN   B 1 4   ? 43.595 -13.561 -16.055 1.00 14.55 ?  4   ASN   B ND2  1 
ATOM   3887 H H    A ASN   B 1 4   ? 46.905 -15.436 -16.808 0.74 19.59 ?  4   ASN   B H    1 
ATOM   3888 H H    B ASN   B 1 4   ? 46.971 -15.535 -16.857 0.26 19.59 ?  4   ASN   B H    1 
ATOM   3889 H HA   . ASN   B 1 4   ? 45.415 -16.934 -16.603 1.00 18.00 ?  4   ASN   B HA   1 
ATOM   3890 H HB2  . ASN   B 1 4   ? 43.843 -15.033 -17.964 1.00 17.27 ?  4   ASN   B HB2  1 
ATOM   3891 H HB3  . ASN   B 1 4   ? 43.235 -16.283 -17.193 1.00 17.27 ?  4   ASN   B HB3  1 
ATOM   3892 H HD21 . ASN   B 1 4   ? 43.568 -13.057 -15.355 1.00 17.46 ?  4   ASN   B HD21 1 
ATOM   3893 H HD22 . ASN   B 1 4   ? 43.396 -13.231 -16.824 1.00 17.46 ?  4   ASN   B HD22 1 
ATOM   3894 N N    . SER   B 1 5   ? 46.384 -17.913 -18.961 1.00 16.18 ?  5   SER   B N    1 
ATOM   3895 C CA   . SER   B 1 5   ? 46.485 -18.832 -20.096 1.00 18.61 ?  5   SER   B CA   1 
ATOM   3896 C C    . SER   B 1 5   ? 46.490 -20.255 -19.549 1.00 19.99 ?  5   SER   B C    1 
ATOM   3897 O O    . SER   B 1 5   ? 47.521 -20.917 -19.466 1.00 22.09 ?  5   SER   B O    1 
ATOM   3898 C CB   . SER   B 1 5   ? 47.737 -18.536 -20.916 1.00 20.49 ?  5   SER   B CB   1 
ATOM   3899 O OG   . SER   B 1 5   ? 48.908 -18.760 -20.148 1.00 23.51 ?  5   SER   B OG   1 
ATOM   3900 H H    . SER   B 1 5   ? 47.139 -17.755 -18.577 1.00 19.41 ?  5   SER   B H    1 
ATOM   3901 H HA   . SER   B 1 5   ? 45.713 -18.728 -20.670 1.00 22.33 ?  5   SER   B HA   1 
ATOM   3902 H HB2  . SER   B 1 5   ? 47.749 -19.111 -21.701 1.00 24.59 ?  5   SER   B HB2  1 
ATOM   3903 H HB3  . SER   B 1 5   ? 47.704 -17.607 -21.193 1.00 24.59 ?  5   SER   B HB3  1 
ATOM   3904 H HG   . SER   B 1 5   ? 48.970 -19.573 -19.951 1.00 28.22 ?  5   SER   B HG   1 
ATOM   3905 N N    . PHE   B 1 6   ? 45.307 -20.717 -19.154 1.00 20.35 ?  6   PHE   B N    1 
ATOM   3906 C CA   . PHE   B 1 6   ? 45.146 -22.063 -18.622 1.00 19.95 ?  6   PHE   B CA   1 
ATOM   3907 C C    . PHE   B 1 6   ? 45.075 -23.060 -19.770 1.00 23.59 ?  6   PHE   B C    1 
ATOM   3908 O O    . PHE   B 1 6   ? 44.382 -22.829 -20.764 1.00 25.41 ?  6   PHE   B O    1 
ATOM   3909 C CB   . PHE   B 1 6   ? 43.867 -22.140 -17.786 1.00 17.93 ?  6   PHE   B CB   1 
ATOM   3910 C CG   . PHE   B 1 6   ? 43.877 -21.256 -16.565 1.00 16.13 ?  6   PHE   B CG   1 
ATOM   3911 C CD1  . PHE   B 1 6   ? 44.388 -21.723 -15.368 1.00 14.85 ?  6   PHE   B CD1  1 
ATOM   3912 C CD2  . PHE   B 1 6   ? 43.376 -19.961 -16.617 1.00 15.88 ?  6   PHE   B CD2  1 
ATOM   3913 C CE1  . PHE   B 1 6   ? 44.389 -20.921 -14.236 1.00 14.59 ?  6   PHE   B CE1  1 
ATOM   3914 C CE2  . PHE   B 1 6   ? 43.383 -19.148 -15.492 1.00 16.21 ?  6   PHE   B CE2  1 
ATOM   3915 C CZ   . PHE   B 1 6   ? 43.896 -19.624 -14.302 1.00 15.05 ?  6   PHE   B CZ   1 
ATOM   3916 H H    . PHE   B 1 6   ? 44.577 -20.266 -19.190 1.00 24.42 ?  6   PHE   B H    1 
ATOM   3917 H HA   . PHE   B 1 6   ? 45.900 -22.288 -18.057 1.00 23.94 ?  6   PHE   B HA   1 
ATOM   3918 H HB2  . PHE   B 1 6   ? 43.115 -21.872 -18.336 1.00 21.51 ?  6   PHE   B HB2  1 
ATOM   3919 H HB3  . PHE   B 1 6   ? 43.743 -23.055 -17.485 1.00 21.51 ?  6   PHE   B HB3  1 
ATOM   3920 H HD1  . PHE   B 1 6   ? 44.729 -22.587 -15.316 1.00 17.82 ?  6   PHE   B HD1  1 
ATOM   3921 H HD2  . PHE   B 1 6   ? 43.027 -19.639 -17.415 1.00 19.05 ?  6   PHE   B HD2  1 
ATOM   3922 H HE1  . PHE   B 1 6   ? 44.747 -21.240 -13.434 1.00 17.51 ?  6   PHE   B HE1  1 
ATOM   3923 H HE2  . PHE   B 1 6   ? 43.041 -18.283 -15.538 1.00 19.45 ?  6   PHE   B HE2  1 
ATOM   3924 H HZ   . PHE   B 1 6   ? 43.902 -19.083 -13.544 1.00 18.06 ?  6   PHE   B HZ   1 
ATOM   3925 N N    A SER   B 1 7   ? 45.793 -24.174 -19.628 0.74 23.90 ?  7   SER   B N    1 
ATOM   3926 N N    B SER   B 1 7   ? 45.802 -24.169 -19.629 0.26 24.44 ?  7   SER   B N    1 
ATOM   3927 C CA   A SER   B 1 7   ? 45.871 -25.177 -20.682 0.74 25.67 ?  7   SER   B CA   1 
ATOM   3928 C CA   B SER   B 1 7   ? 45.901 -25.171 -20.681 0.26 25.68 ?  7   SER   B CA   1 
ATOM   3929 C C    A SER   B 1 7   ? 45.850 -26.573 -20.077 0.74 24.92 ?  7   SER   B C    1 
ATOM   3930 C C    B SER   B 1 7   ? 45.870 -26.563 -20.071 0.26 25.30 ?  7   SER   B C    1 
ATOM   3931 O O    A SER   B 1 7   ? 46.461 -26.819 -19.033 0.74 25.83 ?  7   SER   B O    1 
ATOM   3932 O O    B SER   B 1 7   ? 46.470 -26.805 -19.019 0.26 25.66 ?  7   SER   B O    1 
ATOM   3933 C CB   A SER   B 1 7   ? 47.144 -24.993 -21.521 0.74 28.29 ?  7   SER   B CB   1 
ATOM   3934 C CB   B SER   B 1 7   ? 47.198 -24.999 -21.483 0.26 27.09 ?  7   SER   B CB   1 
ATOM   3935 O OG   A SER   B 1 7   ? 47.104 -25.784 -22.694 0.74 30.33 ?  7   SER   B OG   1 
ATOM   3936 O OG   B SER   B 1 7   ? 47.325 -26.006 -22.472 0.26 28.06 ?  7   SER   B OG   1 
ATOM   3937 H H    A SER   B 1 7   ? 46.248 -24.373 -18.923 0.74 28.68 ?  7   SER   B H    1 
ATOM   3938 H H    B SER   B 1 7   ? 46.253 -24.365 -18.923 0.26 29.33 ?  7   SER   B H    1 
ATOM   3939 H HA   A SER   B 1 7   ? 45.105 -25.090 -21.267 0.74 30.81 ?  7   SER   B HA   1 
ATOM   3940 H HA   B SER   B 1 7   ? 45.150 -25.085 -21.286 0.26 30.81 ?  7   SER   B HA   1 
ATOM   3941 H HB2  A SER   B 1 7   ? 47.218 -24.060 -21.778 0.74 33.95 ?  7   SER   B HB2  1 
ATOM   3942 H HB2  B SER   B 1 7   ? 47.187 -24.130 -21.915 0.26 32.51 ?  7   SER   B HB2  1 
ATOM   3943 H HB3  A SER   B 1 7   ? 47.913 -25.251 -20.989 0.74 33.95 ?  7   SER   B HB3  1 
ATOM   3944 H HB3  B SER   B 1 7   ? 47.954 -25.059 -20.879 0.26 32.51 ?  7   SER   B HB3  1 
ATOM   3945 H HG   A SER   B 1 7   ? 47.808 -25.676 -23.139 0.74 36.40 ?  7   SER   B HG   1 
ATOM   3946 H HG   B SER   B 1 7   ? 48.036 -25.894 -22.906 0.26 33.67 ?  7   SER   B HG   1 
ATOM   3947 N N    A GLY   B 1 8   ? 45.145 -27.485 -20.744 0.74 24.43 ?  8   GLY   B N    1 
ATOM   3948 N N    B GLY   B 1 8   ? 45.169 -27.476 -20.740 0.26 24.74 ?  8   GLY   B N    1 
ATOM   3949 C CA   A GLY   B 1 8   ? 45.129 -28.872 -20.332 0.74 23.78 ?  8   GLY   B CA   1 
ATOM   3950 C CA   B GLY   B 1 8   ? 45.141 -28.861 -20.319 0.26 23.95 ?  8   GLY   B CA   1 
ATOM   3951 C C    A GLY   B 1 8   ? 44.143 -29.205 -19.242 0.74 22.77 ?  8   GLY   B C    1 
ATOM   3952 C C    B GLY   B 1 8   ? 44.179 -29.173 -19.200 0.26 22.91 ?  8   GLY   B C    1 
ATOM   3953 O O    A GLY   B 1 8   ? 44.247 -30.279 -18.638 0.74 23.85 ?  8   GLY   B O    1 
ATOM   3954 O O    B GLY   B 1 8   ? 44.346 -30.195 -18.527 0.26 23.36 ?  8   GLY   B O    1 
ATOM   3955 H H    A GLY   B 1 8   ? 44.669 -27.317 -21.439 0.74 29.32 ?  8   GLY   B H    1 
ATOM   3956 H H    B GLY   B 1 8   ? 44.700 -27.311 -21.443 0.26 29.69 ?  8   GLY   B H    1 
ATOM   3957 H HA2  A GLY   B 1 8   ? 44.921 -29.426 -21.100 0.74 28.53 ?  8   GLY   B HA2  1 
ATOM   3958 H HA2  B GLY   B 1 8   ? 44.908 -29.416 -21.081 0.26 28.74 ?  8   GLY   B HA2  1 
ATOM   3959 H HA3  A GLY   B 1 8   ? 46.009 -29.119 -20.013 0.74 28.53 ?  8   GLY   B HA3  1 
ATOM   3960 H HA3  B GLY   B 1 8   ? 46.024 -29.118 -20.019 0.26 28.74 ?  8   GLY   B HA3  1 
ATOM   3961 N N    . TYR   B 1 9   ? 43.174 -28.332 -18.976 1.00 21.60 ?  9   TYR   B N    1 
ATOM   3962 C CA   . TYR   B 1 9   ? 42.193 -28.584 -17.934 1.00 19.32 ?  9   TYR   B CA   1 
ATOM   3963 C C    . TYR   B 1 9   ? 41.008 -29.370 -18.468 1.00 18.76 ?  9   TYR   B C    1 
ATOM   3964 O O    . TYR   B 1 9   ? 40.599 -29.226 -19.625 1.00 20.68 ?  9   TYR   B O    1 
ATOM   3965 C CB   . TYR   B 1 9   ? 41.694 -27.284 -17.306 1.00 18.80 ?  9   TYR   B CB   1 
ATOM   3966 C CG   . TYR   B 1 9   ? 42.711 -26.658 -16.380 1.00 17.97 ?  9   TYR   B CG   1 
ATOM   3967 C CD1  . TYR   B 1 9   ? 43.821 -25.998 -16.889 1.00 18.67 ?  9   TYR   B CD1  1 
ATOM   3968 C CD2  . TYR   B 1 9   ? 42.579 -26.747 -15.003 1.00 17.18 ?  9   TYR   B CD2  1 
ATOM   3969 C CE1  . TYR   B 1 9   ? 44.766 -25.436 -16.055 1.00 19.08 ?  9   TYR   B CE1  1 
ATOM   3970 C CE2  . TYR   B 1 9   ? 43.520 -26.187 -14.157 1.00 17.65 ?  9   TYR   B CE2  1 
ATOM   3971 C CZ   . TYR   B 1 9   ? 44.612 -25.528 -14.693 1.00 18.79 ?  9   TYR   B CZ   1 
ATOM   3972 O OH   . TYR   B 1 9   ? 45.558 -24.979 -13.868 1.00 19.56 ?  9   TYR   B OH   1 
ATOM   3973 H H    A TYR   B 1 9   ? 43.052 -27.594 -19.399 0.74 25.92 ?  9   TYR   B H    1 
ATOM   3974 H H    B TYR   B 1 9   ? 43.030 -27.612 -19.423 0.26 25.92 ?  9   TYR   B H    1 
ATOM   3975 H HA   . TYR   B 1 9   ? 42.598 -29.110 -17.233 1.00 23.19 ?  9   TYR   B HA   1 
ATOM   3976 H HB2  . TYR   B 1 9   ? 41.489 -26.641 -18.004 1.00 22.56 ?  9   TYR   B HB2  1 
ATOM   3977 H HB3  . TYR   B 1 9   ? 40.904 -27.478 -16.786 1.00 22.56 ?  9   TYR   B HB3  1 
ATOM   3978 H HD1  . TYR   B 1 9   ? 43.929 -25.934 -17.810 1.00 22.41 ?  9   TYR   B HD1  1 
ATOM   3979 H HD2  . TYR   B 1 9   ? 41.839 -27.190 -14.641 1.00 20.62 ?  9   TYR   B HD2  1 
ATOM   3980 H HE1  . TYR   B 1 9   ? 45.497 -24.999 -16.413 1.00 22.90 ?  9   TYR   B HE1  1 
ATOM   3981 H HE2  . TYR   B 1 9   ? 43.407 -26.254 -13.234 1.00 21.18 ?  9   TYR   B HE2  1 
ATOM   3982 H HH   . TYR   B 1 9   ? 46.153 -24.617 -14.328 1.00 23.47 ?  9   TYR   B HH   1 
ATOM   3983 N N    . LEU   B 1 10  ? 40.468 -30.216 -17.602 1.00 16.84 ?  10  LEU   B N    1 
ATOM   3984 C CA   . LEU   B 1 10  ? 39.256 -30.964 -17.882 1.00 16.70 ?  10  LEU   B CA   1 
ATOM   3985 C C    . LEU   B 1 10  ? 38.069 -30.194 -17.318 1.00 15.89 ?  10  LEU   B C    1 
ATOM   3986 O O    . LEU   B 1 10  ? 38.085 -29.777 -16.157 1.00 15.65 ?  10  LEU   B O    1 
ATOM   3987 C CB   . LEU   B 1 10  ? 39.352 -32.337 -17.218 1.00 17.50 ?  10  LEU   B CB   1 
ATOM   3988 C CG   . LEU   B 1 10  ? 38.186 -33.273 -17.513 1.00 19.34 ?  10  LEU   B CG   1 
ATOM   3989 C CD1  . LEU   B 1 10  ? 38.259 -33.777 -18.950 1.00 20.83 ?  10  LEU   B CD1  1 
ATOM   3990 C CD2  . LEU   B 1 10  ? 38.156 -34.428 -16.526 1.00 20.68 ?  10  LEU   B CD2  1 
ATOM   3991 H H    . LEU   B 1 10  ? 40.793 -30.378 -16.821 1.00 20.21 ?  10  LEU   B H    1 
ATOM   3992 H HA   . LEU   B 1 10  ? 39.139 -31.079 -18.835 1.00 20.04 ?  10  LEU   B HA   1 
ATOM   3993 H HB2  . LEU   B 1 10  ? 40.163 -32.775 -17.524 1.00 21.00 ?  10  LEU   B HB2  1 
ATOM   3994 H HB3  . LEU   B 1 10  ? 39.393 -32.218 -16.255 1.00 21.00 ?  10  LEU   B HB3  1 
ATOM   3995 H HG   . LEU   B 1 10  ? 37.355 -32.784 -17.415 1.00 23.21 ?  10  LEU   B HG   1 
ATOM   3996 H HD11 . LEU   B 1 10  ? 37.539 -34.410 -19.099 1.00 24.99 ?  10  LEU   B HD11 1 
ATOM   3997 H HD12 . LEU   B 1 10  ? 38.164 -33.022 -19.553 1.00 24.99 ?  10  LEU   B HD12 1 
ATOM   3998 H HD13 . LEU   B 1 10  ? 39.115 -34.209 -19.091 1.00 24.99 ?  10  LEU   B HD13 1 
ATOM   3999 H HD21 . LEU   B 1 10  ? 37.409 -35.005 -16.743 1.00 24.81 ?  10  LEU   B HD21 1 
ATOM   4000 H HD22 . LEU   B 1 10  ? 38.988 -34.917 -16.591 1.00 24.81 ?  10  LEU   B HD22 1 
ATOM   4001 H HD23 . LEU   B 1 10  ? 38.049 -34.068 -15.631 1.00 24.81 ?  10  LEU   B HD23 1 
ATOM   4002 N N    . LYS   B 1 11  ? 37.041 -30.017 -18.136 1.00 17.01 ?  11  LYS   B N    1 
ATOM   4003 C CA   . LYS   B 1 11  ? 35.847 -29.297 -17.720 1.00 18.70 ?  11  LYS   B CA   1 
ATOM   4004 C C    . LYS   B 1 11  ? 34.954 -30.220 -16.895 1.00 17.99 ?  11  LYS   B C    1 
ATOM   4005 O O    . LYS   B 1 11  ? 34.557 -31.293 -17.363 1.00 19.97 ?  11  LYS   B O    1 
ATOM   4006 C CB   . LYS   B 1 11  ? 35.111 -28.805 -18.965 1.00 22.59 ?  11  LYS   B CB   1 
ATOM   4007 C CG   . LYS   B 1 11  ? 33.950 -27.865 -18.706 1.00 26.03 ?  11  LYS   B CG   1 
ATOM   4008 C CD   . LYS   B 1 11  ? 33.217 -27.556 -20.008 1.00 29.01 ?  11  LYS   B CD   1 
ATOM   4009 C CE   . LYS   B 1 11  ? 32.183 -26.460 -19.827 1.00 31.19 ?  11  LYS   B CE   1 
ATOM   4010 N NZ   . LYS   B 1 11  ? 32.821 -25.150 -19.540 1.00 32.46 ?  11  LYS   B NZ   1 
ATOM   4011 H H    . LYS   B 1 11  ? 37.004 -30.318 -18.940 1.00 20.41 ?  11  LYS   B H    1 
ATOM   4012 H HA   . LYS   B 1 11  ? 36.096 -28.533 -17.177 1.00 22.44 ?  11  LYS   B HA   1 
ATOM   4013 H HB2  . LYS   B 1 11  ? 35.745 -28.334 -19.529 1.00 27.11 ?  11  LYS   B HB2  1 
ATOM   4014 H HB3  . LYS   B 1 11  ? 34.763 -29.574 -19.441 1.00 27.11 ?  11  LYS   B HB3  1 
ATOM   4015 H HG2  . LYS   B 1 11  ? 33.324 -28.283 -18.095 1.00 31.24 ?  11  LYS   B HG2  1 
ATOM   4016 H HG3  . LYS   B 1 11  ? 34.282 -27.033 -18.336 1.00 31.24 ?  11  LYS   B HG3  1 
ATOM   4017 H HD2  . LYS   B 1 11  ? 33.858 -27.261 -20.674 1.00 34.81 ?  11  LYS   B HD2  1 
ATOM   4018 H HD3  . LYS   B 1 11  ? 32.761 -28.356 -20.316 1.00 34.81 ?  11  LYS   B HD3  1 
ATOM   4019 H HE2  . LYS   B 1 11  ? 31.662 -26.374 -20.641 1.00 37.43 ?  11  LYS   B HE2  1 
ATOM   4020 H HE3  . LYS   B 1 11  ? 31.604 -26.689 -19.082 1.00 37.43 ?  11  LYS   B HE3  1 
ATOM   4021 H HZ1  . LYS   B 1 11  ? 32.200 -24.516 -19.481 1.00 38.95 ?  11  LYS   B HZ1  1 
ATOM   4022 H HZ2  . LYS   B 1 11  ? 33.267 -25.190 -18.771 1.00 38.95 ?  11  LYS   B HZ2  1 
ATOM   4023 H HZ3  . LYS   B 1 11  ? 33.388 -24.939 -20.193 1.00 38.95 ?  11  LYS   B HZ3  1 
ATOM   4024 N N    . LEU   B 1 12  ? 34.629 -29.801 -15.672 1.00 16.53 ?  12  LEU   B N    1 
ATOM   4025 C CA   . LEU   B 1 12  ? 33.667 -30.507 -14.833 1.00 16.26 ?  12  LEU   B CA   1 
ATOM   4026 C C    . LEU   B 1 12  ? 32.276 -29.900 -14.925 1.00 16.21 ?  12  LEU   B C    1 
ATOM   4027 O O    . LEU   B 1 12  ? 31.288 -30.616 -15.103 1.00 17.22 ?  12  LEU   B O    1 
ATOM   4028 C CB   . LEU   B 1 12  ? 34.127 -30.521 -13.371 1.00 15.99 ?  12  LEU   B CB   1 
ATOM   4029 C CG   . LEU   B 1 12  ? 35.467 -31.198 -13.096 1.00 16.05 ?  12  LEU   B CG   1 
ATOM   4030 C CD1  . LEU   B 1 12  ? 35.806 -31.148 -11.616 1.00 16.21 ?  12  LEU   B CD1  1 
ATOM   4031 C CD2  . LEU   B 1 12  ? 35.466 -32.638 -13.597 1.00 16.97 ?  12  LEU   B CD2  1 
ATOM   4032 H H    . LEU   B 1 12  ? 34.951 -29.093 -15.303 1.00 19.84 ?  12  LEU   B H    1 
ATOM   4033 H HA   . LEU   B 1 12  ? 33.599 -31.425 -15.139 1.00 19.52 ?  12  LEU   B HA   1 
ATOM   4034 H HB2  . LEU   B 1 12  ? 34.195 -29.606 -13.067 1.00 19.19 ?  12  LEU   B HB2  1 
ATOM   4035 H HB3  . LEU   B 1 12  ? 33.452 -30.986 -12.848 1.00 19.19 ?  12  LEU   B HB3  1 
ATOM   4036 H HG   . LEU   B 1 12  ? 36.159 -30.722 -13.578 1.00 19.27 ?  12  LEU   B HG   1 
ATOM   4037 H HD11 . LEU   B 1 12  ? 36.664 -31.584 -11.475 1.00 19.46 ?  12  LEU   B HD11 1 
ATOM   4038 H HD12 . LEU   B 1 12  ? 35.857 -30.223 -11.335 1.00 19.46 ?  12  LEU   B HD12 1 
ATOM   4039 H HD13 . LEU   B 1 12  ? 35.116 -31.611 -11.116 1.00 19.46 ?  12  LEU   B HD13 1 
ATOM   4040 H HD21 . LEU   B 1 12  ? 36.269 -33.081 -13.283 1.00 20.36 ?  12  LEU   B HD21 1 
ATOM   4041 H HD22 . LEU   B 1 12  ? 34.680 -33.092 -13.253 1.00 20.36 ?  12  LEU   B HD22 1 
ATOM   4042 H HD23 . LEU   B 1 12  ? 35.446 -32.636 -14.568 1.00 20.36 ?  12  LEU   B HD23 1 
ATOM   4043 N N    . THR   B 1 13  ? 32.189 -28.581 -14.802 1.00 16.30 ?  13  THR   B N    1 
ATOM   4044 C CA   . THR   B 1 13  ? 30.962 -27.829 -15.007 1.00 16.31 ?  13  THR   B CA   1 
ATOM   4045 C C    . THR   B 1 13  ? 31.289 -26.631 -15.892 1.00 17.93 ?  13  THR   B C    1 
ATOM   4046 O O    . THR   B 1 13  ? 32.431 -26.437 -16.322 1.00 18.68 ?  13  THR   B O    1 
ATOM   4047 C CB   . THR   B 1 13  ? 30.360 -27.357 -13.678 1.00 15.90 ?  13  THR   B CB   1 
ATOM   4048 O OG1  . THR   B 1 13  ? 31.206 -26.341 -13.124 1.00 15.70 ?  13  THR   B OG1  1 
ATOM   4049 C CG2  . THR   B 1 13  ? 30.230 -28.516 -12.693 1.00 16.57 ?  13  THR   B CG2  1 
ATOM   4050 H H    . THR   B 1 13  ? 32.856 -28.081 -14.591 1.00 19.57 ?  13  THR   B H    1 
ATOM   4051 H HA   . THR   B 1 13  ? 30.310 -28.384 -15.459 1.00 19.57 ?  13  THR   B HA   1 
ATOM   4052 H HB   . THR   B 1 13  ? 29.472 -26.991 -13.835 1.00 19.09 ?  13  THR   B HB   1 
ATOM   4053 H HG1  . THR   B 1 13  ? 30.910 -25.579 -13.327 1.00 18.85 ?  13  THR   B HG1  1 
ATOM   4054 H HG21 . THR   B 1 13  ? 29.721 -28.238 -11.914 1.00 19.89 ?  13  THR   B HG21 1 
ATOM   4055 H HG22 . THR   B 1 13  ? 29.770 -29.261 -13.116 1.00 19.89 ?  13  THR   B HG22 1 
ATOM   4056 H HG23 . THR   B 1 13  ? 31.108 -28.811 -12.408 1.00 19.89 ?  13  THR   B HG23 1 
ATOM   4057 N N    A ASP   B 1 14  ? 30.271 -25.809 -16.149 0.74 18.98 ?  14  ASP   B N    1 
ATOM   4058 N N    B ASP   B 1 14  ? 30.276 -25.796 -16.141 0.26 18.68 ?  14  ASP   B N    1 
ATOM   4059 C CA   A ASP   B 1 14  ? 30.471 -24.641 -17.000 0.74 20.59 ?  14  ASP   B CA   1 
ATOM   4060 C CA   B ASP   B 1 14  ? 30.465 -24.635 -17.005 0.26 19.50 ?  14  ASP   B CA   1 
ATOM   4061 C C    A ASP   B 1 14  ? 31.570 -23.727 -16.472 0.74 18.82 ?  14  ASP   B C    1 
ATOM   4062 C C    B ASP   B 1 14  ? 31.468 -23.634 -16.446 0.26 17.92 ?  14  ASP   B C    1 
ATOM   4063 O O    A ASP   B 1 14  ? 32.223 -23.032 -17.261 0.74 19.98 ?  14  ASP   B O    1 
ATOM   4064 O O    B ASP   B 1 14  ? 31.922 -22.757 -17.189 0.26 18.12 ?  14  ASP   B O    1 
ATOM   4065 C CB   A ASP   B 1 14  ? 29.160 -23.869 -17.148 0.74 24.42 ?  14  ASP   B CB   1 
ATOM   4066 C CB   B ASP   B 1 14  ? 29.133 -23.924 -17.243 0.26 21.91 ?  14  ASP   B CB   1 
ATOM   4067 C CG   A ASP   B 1 14  ? 28.198 -24.530 -18.111 0.74 28.30 ?  14  ASP   B CG   1 
ATOM   4068 C CG   B ASP   B 1 14  ? 28.250 -24.660 -18.232 0.26 24.00 ?  14  ASP   B CG   1 
ATOM   4069 O OD1  A ASP   B 1 14  ? 28.578 -25.529 -18.760 0.74 29.49 ?  14  ASP   B OD1  1 
ATOM   4070 O OD1  B ASP   B 1 14  ? 28.798 -25.273 -19.171 0.26 24.58 ?  14  ASP   B OD1  1 
ATOM   4071 O OD2  A ASP   B 1 14  ? 27.051 -24.050 -18.212 0.74 29.85 -1 14  ASP   B OD2  1 
ATOM   4072 O OD2  B ASP   B 1 14  ? 27.012 -24.631 -18.069 0.26 24.74 -1 14  ASP   B OD2  1 
ATOM   4073 H H    A ASP   B 1 14  ? 29.473 -25.897 -15.840 0.74 22.78 ?  14  ASP   B H    1 
ATOM   4074 H H    B ASP   B 1 14  ? 29.480 -25.881 -15.826 0.26 22.42 ?  14  ASP   B H    1 
ATOM   4075 H HA   A ASP   B 1 14  ? 30.741 -24.936 -17.878 0.74 24.70 ?  14  ASP   B HA   1 
ATOM   4076 H HA   B ASP   B 1 14  ? 30.793 -24.942 -17.864 0.26 23.40 ?  14  ASP   B HA   1 
ATOM   4077 H HB2  A ASP   B 1 14  ? 28.711 -23.825 -16.290 0.74 29.31 ?  14  ASP   B HB2  1 
ATOM   4078 H HB2  B ASP   B 1 14  ? 28.654 -23.860 -16.402 0.26 26.29 ?  14  ASP   B HB2  1 
ATOM   4079 H HB3  A ASP   B 1 14  ? 29.347 -22.975 -17.474 0.74 29.31 ?  14  ASP   B HB3  1 
ATOM   4080 H HB3  B ASP   B 1 14  ? 29.313 -23.031 -17.588 0.26 26.29 ?  14  ASP   B HB3  1 
ATOM   4081 N N    . ASN   B 1 15  ? 31.801 -23.719 -15.156 1.00 16.22 ?  15  ASN   B N    1 
ATOM   4082 C CA   . ASN   B 1 15  ? 32.763 -22.798 -14.556 1.00 14.00 ?  15  ASN   B CA   1 
ATOM   4083 C C    . ASN   B 1 15  ? 33.852 -23.453 -13.718 1.00 12.97 ?  15  ASN   B C    1 
ATOM   4084 O O    . ASN   B 1 15  ? 34.690 -22.723 -13.176 1.00 13.62 ?  15  ASN   B O    1 
ATOM   4085 C CB   . ASN   B 1 15  ? 32.047 -21.742 -13.699 1.00 14.16 ?  15  ASN   B CB   1 
ATOM   4086 C CG   . ASN   B 1 15  ? 31.422 -22.339 -12.457 1.00 14.12 ?  15  ASN   B CG   1 
ATOM   4087 O OD1  . ASN   B 1 15  ? 30.475 -23.132 -12.539 1.00 15.76 ?  15  ASN   B OD1  1 
ATOM   4088 N ND2  . ASN   B 1 15  ? 31.952 -21.988 -11.300 1.00 13.36 ?  15  ASN   B ND2  1 
ATOM   4089 H H    A ASN   B 1 15  ? 31.411 -24.244 -14.591 0.74 19.46 ?  15  ASN   B H    1 
ATOM   4090 H H    B ASN   B 1 15  ? 31.456 -24.284 -14.601 0.26 19.46 ?  15  ASN   B H    1 
ATOM   4091 H HA   . ASN   B 1 15  ? 33.210 -22.322 -15.264 1.00 16.80 ?  15  ASN   B HA   1 
ATOM   4092 H HB2  . ASN   B 1 15  ? 32.691 -21.065 -13.422 1.00 16.99 ?  15  ASN   B HB2  1 
ATOM   4093 H HB3  . ASN   B 1 15  ? 31.342 -21.322 -14.225 1.00 16.99 ?  15  ASN   B HB3  1 
ATOM   4094 H HD21 . ASN   B 1 15  ? 31.631 -22.297 -10.563 1.00 16.03 ?  15  ASN   B HD21 1 
ATOM   4095 H HD22 . ASN   B 1 15  ? 32.624 -21.444 -11.274 1.00 16.03 ?  15  ASN   B HD22 1 
ATOM   4096 N N    . VAL   B 1 16  ? 33.876 -24.778 -13.586 1.00 12.72 ?  16  VAL   B N    1 
ATOM   4097 C CA   . VAL   B 1 16  ? 34.875 -25.468 -12.775 1.00 12.70 ?  16  VAL   B CA   1 
ATOM   4098 C C    . VAL   B 1 16  ? 35.670 -26.414 -13.663 1.00 12.76 ?  16  VAL   B C    1 
ATOM   4099 O O    . VAL   B 1 16  ? 35.094 -27.288 -14.326 1.00 13.95 ?  16  VAL   B O    1 
ATOM   4100 C CB   . VAL   B 1 16  ? 34.242 -26.234 -11.600 1.00 13.17 ?  16  VAL   B CB   1 
ATOM   4101 C CG1  . VAL   B 1 16  ? 35.318 -26.968 -10.798 1.00 13.27 ?  16  VAL   B CG1  1 
ATOM   4102 C CG2  . VAL   B 1 16  ? 33.436 -25.289 -10.712 1.00 13.91 ?  16  VAL   B CG2  1 
ATOM   4103 H H    . VAL   B 1 16  ? 33.312 -25.311 -13.963 1.00 15.27 ?  16  VAL   B H    1 
ATOM   4104 H HA   . VAL   B 1 16  ? 35.491 -24.813 -12.407 1.00 15.24 ?  16  VAL   B HA   1 
ATOM   4105 H HB   . VAL   B 1 16  ? 33.636 -26.903 -11.956 1.00 15.80 ?  16  VAL   B HB   1 
ATOM   4106 H HG11 . VAL   B 1 16  ? 34.930 -27.269 -9.960  1.00 15.93 ?  16  VAL   B HG11 1 
ATOM   4107 H HG12 . VAL   B 1 16  ? 35.634 -27.729 -11.307 1.00 15.93 ?  16  VAL   B HG12 1 
ATOM   4108 H HG13 . VAL   B 1 16  ? 36.050 -26.356 -10.620 1.00 15.93 ?  16  VAL   B HG13 1 
ATOM   4109 H HG21 . VAL   B 1 16  ? 33.090 -25.788 -9.956  1.00 16.70 ?  16  VAL   B HG21 1 
ATOM   4110 H HG22 . VAL   B 1 16  ? 34.010 -24.575 -10.406 1.00 16.70 ?  16  VAL   B HG22 1 
ATOM   4111 H HG23 . VAL   B 1 16  ? 32.699 -24.925 -11.231 1.00 16.70 ?  16  VAL   B HG23 1 
ATOM   4112 N N    . TYR   B 1 17  ? 36.996 -26.256 -13.629 1.00 13.08 ?  17  TYR   B N    1 
ATOM   4113 C CA   . TYR   B 1 17  ? 37.946 -27.008 -14.435 1.00 13.43 ?  17  TYR   B CA   1 
ATOM   4114 C C    . TYR   B 1 17  ? 38.992 -27.614 -13.512 1.00 12.80 ?  17  TYR   B C    1 
ATOM   4115 O O    . TYR   B 1 17  ? 39.262 -27.077 -12.435 1.00 13.08 ?  17  TYR   B O    1 
ATOM   4116 C CB   . TYR   B 1 17  ? 38.654 -26.082 -15.433 1.00 15.79 ?  17  TYR   B CB   1 
ATOM   4117 C CG   . TYR   B 1 17  ? 37.731 -25.312 -16.343 1.00 18.68 ?  17  TYR   B CG   1 
ATOM   4118 C CD1  . TYR   B 1 17  ? 37.131 -24.130 -15.924 1.00 19.73 ?  17  TYR   B CD1  1 
ATOM   4119 C CD2  . TYR   B 1 17  ? 37.465 -25.763 -17.628 1.00 20.63 ?  17  TYR   B CD2  1 
ATOM   4120 C CE1  . TYR   B 1 17  ? 36.286 -23.423 -16.759 1.00 21.32 ?  17  TYR   B CE1  1 
ATOM   4121 C CE2  . TYR   B 1 17  ? 36.627 -25.062 -18.472 1.00 21.95 ?  17  TYR   B CE2  1 
ATOM   4122 C CZ   . TYR   B 1 17  ? 36.039 -23.897 -18.030 1.00 22.51 ?  17  TYR   B CZ   1 
ATOM   4123 O OH   . TYR   B 1 17  ? 35.207 -23.199 -18.867 1.00 24.23 ?  17  TYR   B OH   1 
ATOM   4124 H H    . TYR   B 1 17  ? 37.392 -25.682 -13.115 1.00 15.69 ?  17  TYR   B H    1 
ATOM   4125 H HA   . TYR   B 1 17  ? 37.491 -27.720 -14.916 1.00 16.11 ?  17  TYR   B HA   1 
ATOM   4126 H HB2  . TYR   B 1 17  ? 39.190 -25.444 -14.941 1.00 18.95 ?  17  TYR   B HB2  1 
ATOM   4127 H HB3  . TYR   B 1 17  ? 39.222 -26.625 -15.997 1.00 18.95 ?  17  TYR   B HB3  1 
ATOM   4128 H HD1  . TYR   B 1 17  ? 37.296 -23.812 -15.067 1.00 23.68 ?  17  TYR   B HD1  1 
ATOM   4129 H HD2  . TYR   B 1 17  ? 37.856 -26.550 -17.930 1.00 24.76 ?  17  TYR   B HD2  1 
ATOM   4130 H HE1  . TYR   B 1 17  ? 35.887 -22.632 -16.467 1.00 25.59 ?  17  TYR   B HE1  1 
ATOM   4131 H HE2  . TYR   B 1 17  ? 36.450 -25.376 -19.332 1.00 26.34 ?  17  TYR   B HE2  1 
ATOM   4132 H HH   . TYR   B 1 17  ? 35.131 -23.586 -19.609 1.00 29.07 ?  17  TYR   B HH   1 
ATOM   4133 N N    . ILE   B 1 18  ? 39.606 -28.723 -13.936 1.00 12.70 ?  18  ILE   B N    1 
ATOM   4134 C CA   . ILE   B 1 18  ? 40.540 -29.442 -13.074 1.00 12.50 ?  18  ILE   B CA   1 
ATOM   4135 C C    . ILE   B 1 18  ? 41.701 -29.997 -13.894 1.00 13.05 ?  18  ILE   B C    1 
ATOM   4136 O O    . ILE   B 1 18  ? 41.538 -30.398 -15.051 1.00 14.41 ?  18  ILE   B O    1 
ATOM   4137 C CB   . ILE   B 1 18  ? 39.795 -30.540 -12.272 1.00 13.31 ?  18  ILE   B CB   1 
ATOM   4138 C CG1  . ILE   B 1 18  ? 40.657 -31.085 -11.127 1.00 13.65 ?  18  ILE   B CG1  1 
ATOM   4139 C CG2  . ILE   B 1 18  ? 39.286 -31.654 -13.199 1.00 13.85 ?  18  ILE   B CG2  1 
ATOM   4140 C CD1  . ILE   B 1 18  ? 39.847 -31.885 -10.115 1.00 15.26 ?  18  ILE   B CD1  1 
ATOM   4141 H H    . ILE   B 1 18  ? 39.498 -29.080 -14.710 1.00 15.24 ?  18  ILE   B H    1 
ATOM   4142 H HA   . ILE   B 1 18  ? 40.906 -28.824 -12.424 1.00 15.00 ?  18  ILE   B HA   1 
ATOM   4143 H HB   . ILE   B 1 18  ? 39.016 -30.137 -11.865 1.00 15.98 ?  18  ILE   B HB   1 
ATOM   4144 H HG12 . ILE   B 1 18  ? 41.341 -31.667 -11.487 1.00 16.38 ?  18  ILE   B HG12 1 
ATOM   4145 H HG13 . ILE   B 1 18  ? 41.064 -30.340 -10.657 1.00 16.38 ?  18  ILE   B HG13 1 
ATOM   4146 H HG21 . ILE   B 1 18  ? 38.704 -32.246 -12.695 1.00 16.62 ?  18  ILE   B HG21 1 
ATOM   4147 H HG22 . ILE   B 1 18  ? 38.794 -31.249 -13.928 1.00 16.62 ?  18  ILE   B HG22 1 
ATOM   4148 H HG23 . ILE   B 1 18  ? 40.043 -32.152 -13.544 1.00 16.62 ?  18  ILE   B HG23 1 
ATOM   4149 H HD11 . ILE   B 1 18  ? 40.430 -32.162 -9.389  1.00 18.31 ?  18  ILE   B HD11 1 
ATOM   4150 H HD12 . ILE   B 1 18  ? 39.132 -31.327 -9.768  1.00 18.31 ?  18  ILE   B HD12 1 
ATOM   4151 H HD13 . ILE   B 1 18  ? 39.473 -32.666 -10.553 1.00 18.31 ?  18  ILE   B HD13 1 
ATOM   4152 N N    . LYS   B 1 19  ? 42.884 -30.027 -13.273 1.00 13.44 ?  19  LYS   B N    1 
ATOM   4153 C CA   . LYS   B 1 19  ? 44.096 -30.508 -13.923 1.00 14.09 ?  19  LYS   B CA   1 
ATOM   4154 C C    . LYS   B 1 19  ? 44.991 -31.182 -12.894 1.00 13.91 ?  19  LYS   B C    1 
ATOM   4155 O O    . LYS   B 1 19  ? 45.074 -30.739 -11.747 1.00 13.71 ?  19  LYS   B O    1 
ATOM   4156 C CB   . LYS   B 1 19  ? 44.869 -29.346 -14.567 1.00 15.68 ?  19  LYS   B CB   1 
ATOM   4157 C CG   . LYS   B 1 19  ? 46.086 -29.754 -15.376 1.00 17.41 ?  19  LYS   B CG   1 
ATOM   4158 C CD   . LYS   B 1 19  ? 46.825 -28.522 -15.888 1.00 19.20 ?  19  LYS   B CD   1 
ATOM   4159 C CE   . LYS   B 1 19  ? 47.973 -28.897 -16.804 1.00 20.99 ?  19  LYS   B CE   1 
ATOM   4160 N NZ   . LYS   B 1 19  ? 48.744 -27.709 -17.259 1.00 22.17 ?  19  LYS   B NZ   1 
ATOM   4161 H H    . LYS   B 1 19  ? 43.003 -29.771 -12.457 1.00 16.13 ?  19  LYS   B H    1 
ATOM   4162 H HA   . LYS   B 1 19  ? 43.863 -31.152 -14.609 1.00 16.91 ?  19  LYS   B HA   1 
ATOM   4163 H HB2  . LYS   B 1 19  ? 44.266 -28.872 -15.161 1.00 18.82 ?  19  LYS   B HB2  1 
ATOM   4164 H HB3  . LYS   B 1 19  ? 45.166 -28.747 -13.861 1.00 18.82 ?  19  LYS   B HB3  1 
ATOM   4165 H HG2  . LYS   B 1 19  ? 46.687 -30.268 -14.816 1.00 20.89 ?  19  LYS   B HG2  1 
ATOM   4166 H HG3  . LYS   B 1 19  ? 45.797 -30.283 -16.138 1.00 20.89 ?  19  LYS   B HG3  1 
ATOM   4167 H HD2  . LYS   B 1 19  ? 46.205 -27.962 -16.384 1.00 23.04 ?  19  LYS   B HD2  1 
ATOM   4168 H HD3  . LYS   B 1 19  ? 47.183 -28.030 -15.131 1.00 23.04 ?  19  LYS   B HD3  1 
ATOM   4169 H HE2  . LYS   B 1 19  ? 48.577 -29.488 -16.327 1.00 25.19 ?  19  LYS   B HE2  1 
ATOM   4170 H HE3  . LYS   B 1 19  ? 47.617 -29.347 -17.587 1.00 25.19 ?  19  LYS   B HE3  1 
ATOM   4171 H HZ1  . LYS   B 1 19  ? 49.366 -27.957 -17.845 1.00 26.61 ?  19  LYS   B HZ1  1 
ATOM   4172 H HZ2  . LYS   B 1 19  ? 48.198 -27.123 -17.647 1.00 26.61 ?  19  LYS   B HZ2  1 
ATOM   4173 H HZ3  . LYS   B 1 19  ? 49.140 -27.319 -16.564 1.00 26.61 ?  19  LYS   B HZ3  1 
ATOM   4174 N N    . ASN   B 1 20  ? 45.679 -32.237 -13.321 1.00 15.09 ?  20  ASN   B N    1 
ATOM   4175 C CA   . ASN   B 1 20  ? 46.712 -32.866 -12.501 1.00 16.20 ?  20  ASN   B CA   1 
ATOM   4176 C C    . ASN   B 1 20  ? 47.985 -32.047 -12.691 1.00 16.67 ?  20  ASN   B C    1 
ATOM   4177 O O    . ASN   B 1 20  ? 48.639 -32.132 -13.734 1.00 18.51 ?  20  ASN   B O    1 
ATOM   4178 C CB   . ASN   B 1 20  ? 46.887 -34.321 -12.930 1.00 17.59 ?  20  ASN   B CB   1 
ATOM   4179 C CG   . ASN   B 1 20  ? 48.050 -35.017 -12.250 1.00 19.10 ?  20  ASN   B CG   1 
ATOM   4180 O OD1  . ASN   B 1 20  ? 48.715 -35.864 -12.859 1.00 21.23 ?  20  ASN   B OD1  1 
ATOM   4181 N ND2  . ASN   B 1 20  ? 48.291 -34.694 -10.986 1.00 18.75 ?  20  ASN   B ND2  1 
ATOM   4182 H H    . ASN   B 1 20  ? 45.566 -32.610 -14.087 1.00 18.10 ?  20  ASN   B H    1 
ATOM   4183 H HA   . ASN   B 1 20  ? 46.439 -32.841 -11.568 1.00 19.44 ?  20  ASN   B HA   1 
ATOM   4184 H HB2  . ASN   B 1 20  ? 46.081 -34.812 -12.706 1.00 21.11 ?  20  ASN   B HB2  1 
ATOM   4185 H HB3  . ASN   B 1 20  ? 47.038 -34.345 -13.885 1.00 21.11 ?  20  ASN   B HB3  1 
ATOM   4186 H HD21 . ASN   B 1 20  ? 48.947 -35.056 -10.567 1.00 22.50 ?  20  ASN   B HD21 1 
ATOM   4187 H HD22 . ASN   B 1 20  ? 47.804 -34.103 -10.584 1.00 22.50 ?  20  ASN   B HD22 1 
ATOM   4188 N N    . ALA   B 1 21  ? 48.323 -31.225 -11.693 1.00 16.43 ?  21  ALA   B N    1 
ATOM   4189 C CA   . ALA   B 1 21  ? 49.428 -30.292 -11.842 1.00 17.09 ?  21  ALA   B CA   1 
ATOM   4190 C C    . ALA   B 1 21  ? 49.883 -29.801 -10.477 1.00 16.11 ?  21  ALA   B C    1 
ATOM   4191 O O    . ALA   B 1 21  ? 49.136 -29.834 -9.496  1.00 16.03 ?  21  ALA   B O    1 
ATOM   4192 C CB   . ALA   B 1 21  ? 49.031 -29.109 -12.730 1.00 18.58 ?  21  ALA   B CB   1 
ATOM   4193 H H    . ALA   B 1 21  ? 47.919 -31.186 -10.923 1.00 19.71 ?  21  ALA   B H    1 
ATOM   4194 H HA   . ALA   B 1 21  ? 50.167 -30.754 -12.257 1.00 20.51 ?  21  ALA   B HA   1 
ATOM   4195 H HB1  . ALA   B 1 21  ? 49.814 -28.562 -12.876 1.00 22.30 ?  21  ALA   B HB1  1 
ATOM   4196 H HB2  . ALA   B 1 21  ? 48.703 -29.456 -13.574 1.00 22.30 ?  21  ALA   B HB2  1 
ATOM   4197 H HB3  . ALA   B 1 21  ? 48.336 -28.600 -12.287 1.00 22.30 ?  21  ALA   B HB3  1 
ATOM   4198 N N    . ASP   B 1 22  ? 51.140 -29.357 -10.447 1.00 15.64 ?  22  ASP   B N    1 
ATOM   4199 C CA   . ASP   B 1 22  ? 51.748 -28.660 -9.319  1.00 15.22 ?  22  ASP   B CA   1 
ATOM   4200 C C    . ASP   B 1 22  ? 51.342 -27.189 -9.410  1.00 13.73 ?  22  ASP   B C    1 
ATOM   4201 O O    . ASP   B 1 22  ? 51.651 -26.521 -10.400 1.00 13.95 ?  22  ASP   B O    1 
ATOM   4202 C CB   . ASP   B 1 22  ? 53.265 -28.843 -9.467  1.00 16.82 ?  22  ASP   B CB   1 
ATOM   4203 C CG   . ASP   B 1 22  ? 54.096 -28.068 -8.447  1.00 18.51 ?  22  ASP   B CG   1 
ATOM   4204 O OD1  . ASP   B 1 22  ? 53.723 -26.952 -8.047  1.00 18.77 ?  22  ASP   B OD1  1 
ATOM   4205 O OD2  . ASP   B 1 22  ? 55.177 -28.573 -8.070  1.00 20.66 -1 22  ASP   B OD2  1 
ATOM   4206 H H    . ASP   B 1 22  ? 51.685 -29.454 -11.108 1.00 18.77 ?  22  ASP   B H    1 
ATOM   4207 H HA   . ASP   B 1 22  ? 51.451 -29.041 -8.476  1.00 18.27 ?  22  ASP   B HA   1 
ATOM   4208 H HB2  . ASP   B 1 22  ? 53.481 -29.781 -9.369  1.00 20.19 ?  22  ASP   B HB2  1 
ATOM   4209 H HB3  . ASP   B 1 22  ? 53.531 -28.532 -10.347 1.00 20.19 ?  22  ASP   B HB3  1 
ATOM   4210 N N    . ILE   B 1 23  ? 50.627 -26.691 -8.395  1.00 12.96 ?  23  ILE   B N    1 
ATOM   4211 C CA   . ILE   B 1 23  ? 50.039 -25.351 -8.475  1.00 12.37 ?  23  ILE   B CA   1 
ATOM   4212 C C    . ILE   B 1 23  ? 51.098 -24.264 -8.619  1.00 12.06 ?  23  ILE   B C    1 
ATOM   4213 O O    . ILE   B 1 23  ? 50.833 -23.221 -9.228  1.00 11.95 ?  23  ILE   B O    1 
ATOM   4214 C CB   . ILE   B 1 23  ? 49.098 -25.102 -7.281  1.00 12.97 ?  23  ILE   B CB   1 
ATOM   4215 C CG1  . ILE   B 1 23  ? 48.271 -23.830 -7.488  1.00 13.59 ?  23  ILE   B CG1  1 
ATOM   4216 C CG2  . ILE   B 1 23  ? 49.863 -25.065 -5.975  1.00 13.88 ?  23  ILE   B CG2  1 
ATOM   4217 C CD1  . ILE   B 1 23  ? 47.136 -23.665 -6.483  1.00 14.21 ?  23  ILE   B CD1  1 
ATOM   4218 H H    . ILE   B 1 23  ? 50.469 -27.112 -7.660  1.00 15.56 ?  23  ILE   B H    1 
ATOM   4219 H HA   . ILE   B 1 23  ? 49.493 -25.321 -9.275  1.00 14.85 ?  23  ILE   B HA   1 
ATOM   4220 H HB   . ILE   B 1 23  ? 48.476 -25.846 -7.238  1.00 15.57 ?  23  ILE   B HB   1 
ATOM   4221 H HG12 . ILE   B 1 23  ? 48.857 -23.057 -7.404  1.00 16.31 ?  23  ILE   B HG12 1 
ATOM   4222 H HG13 . ILE   B 1 23  ? 47.882 -23.845 -8.379  1.00 16.31 ?  23  ILE   B HG13 1 
ATOM   4223 H HG21 . ILE   B 1 23  ? 49.232 -25.048 -5.241  1.00 16.66 ?  23  ILE   B HG21 1 
ATOM   4224 H HG22 . ILE   B 1 23  ? 50.421 -25.856 -5.915  1.00 16.66 ?  23  ILE   B HG22 1 
ATOM   4225 H HG23 . ILE   B 1 23  ? 50.416 -24.268 -5.957  1.00 16.66 ?  23  ILE   B HG23 1 
ATOM   4226 H HD11 . ILE   B 1 23  ? 46.617 -22.884 -6.721  1.00 17.06 ?  23  ILE   B HD11 1 
ATOM   4227 H HD12 . ILE   B 1 23  ? 46.579 -24.458 -6.515  1.00 17.06 ?  23  ILE   B HD12 1 
ATOM   4228 H HD13 . ILE   B 1 23  ? 47.516 -23.560 -5.599  1.00 17.06 ?  23  ILE   B HD13 1 
ATOM   4229 N N    . VAL   B 1 24  ? 52.294 -24.467 -8.057  1.00 12.58 ?  24  VAL   B N    1 
ATOM   4230 C CA   . VAL   B 1 24  ? 53.367 -23.486 -8.223  1.00 13.15 ?  24  VAL   B CA   1 
ATOM   4231 C C    . VAL   B 1 24  ? 53.818 -23.439 -9.674  1.00 13.33 ?  24  VAL   B C    1 
ATOM   4232 O O    . VAL   B 1 24  ? 53.958 -22.363 -10.268 1.00 13.94 ?  24  VAL   B O    1 
ATOM   4233 C CB   . VAL   B 1 24  ? 54.545 -23.801 -7.279  1.00 14.31 ?  24  VAL   B CB   1 
ATOM   4234 C CG1  . VAL   B 1 24  ? 55.762 -22.934 -7.617  1.00 15.09 ?  24  VAL   B CG1  1 
ATOM   4235 C CG2  . VAL   B 1 24  ? 54.132 -23.598 -5.840  1.00 15.27 ?  24  VAL   B CG2  1 
ATOM   4236 H H    . VAL   B 1 24  ? 52.505 -25.154 -7.581  1.00 15.10 ?  24  VAL   B H    1 
ATOM   4237 H HA   . VAL   B 1 24  ? 53.030 -22.612 -7.988  1.00 15.78 ?  24  VAL   B HA   1 
ATOM   4238 H HB   . VAL   B 1 24  ? 54.802 -24.734 -7.384  1.00 17.18 ?  24  VAL   B HB   1 
ATOM   4239 H HG11 . VAL   B 1 24  ? 56.356 -22.911 -6.849  1.00 18.11 ?  24  VAL   B HG11 1 
ATOM   4240 H HG12 . VAL   B 1 24  ? 56.224 -23.322 -8.376  1.00 18.11 ?  24  VAL   B HG12 1 
ATOM   4241 H HG13 . VAL   B 1 24  ? 55.462 -22.038 -7.828  1.00 18.11 ?  24  VAL   B HG13 1 
ATOM   4242 H HG21 . VAL   B 1 24  ? 54.861 -23.867 -5.260  1.00 18.33 ?  24  VAL   B HG21 1 
ATOM   4243 H HG22 . VAL   B 1 24  ? 53.930 -22.660 -5.703  1.00 18.33 ?  24  VAL   B HG22 1 
ATOM   4244 H HG23 . VAL   B 1 24  ? 53.347 -24.138 -5.657  1.00 18.33 ?  24  VAL   B HG23 1 
ATOM   4245 N N    . GLU   B 1 25  ? 54.078 -24.611 -10.261 1.00 14.23 ?  25  GLU   B N    1 
ATOM   4246 C CA   . GLU   B 1 25  ? 54.476 -24.646 -11.661 1.00 15.61 ?  25  GLU   B CA   1 
ATOM   4247 C C    . GLU   B 1 25  ? 53.369 -24.104 -12.551 1.00 14.37 ?  25  GLU   B C    1 
ATOM   4248 O O    . GLU   B 1 25  ? 53.636 -23.385 -13.522 1.00 15.53 ?  25  GLU   B O    1 
ATOM   4249 C CB   . GLU   B 1 25  ? 54.875 -26.067 -12.057 1.00 19.50 ?  25  GLU   B CB   1 
ATOM   4250 C CG   . GLU   B 1 25  ? 56.172 -26.509 -11.400 1.00 24.86 ?  25  GLU   B CG   1 
ATOM   4251 C CD   . GLU   B 1 25  ? 57.293 -25.487 -11.545 1.00 29.53 ?  25  GLU   B CD   1 
ATOM   4252 O OE1  . GLU   B 1 25  ? 57.711 -25.215 -12.691 1.00 31.45 ?  25  GLU   B OE1  1 
ATOM   4253 O OE2  . GLU   B 1 25  ? 57.749 -24.939 -10.514 1.00 31.19 -1 25  GLU   B OE2  1 
ATOM   4254 H H    . GLU   B 1 25  ? 54.028 -25.383 -9.877  1.00 17.08 ?  25  GLU   B H    1 
ATOM   4255 H HA   . GLU   B 1 25  ? 55.235 -24.062 -11.781 1.00 18.74 ?  25  GLU   B HA   1 
ATOM   4256 H HB2  . GLU   B 1 25  ? 54.175 -26.683 -11.781 1.00 23.41 ?  25  GLU   B HB2  1 
ATOM   4257 H HB3  . GLU   B 1 25  ? 54.991 -26.108 -13.019 1.00 23.41 ?  25  GLU   B HB3  1 
ATOM   4258 H HG2  . GLU   B 1 25  ? 56.021 -26.639 -10.456 1.00 29.83 ?  25  GLU   B HG2  1 
ATOM   4259 H HG3  . GLU   B 1 25  ? 56.469 -27.334 -11.814 1.00 29.83 ?  25  GLU   B HG3  1 
ATOM   4260 N N    . GLU   B 1 26  ? 52.116 -24.421 -12.222 1.00 13.69 ?  26  GLU   B N    1 
ATOM   4261 C CA   . GLU   B 1 26  ? 50.996 -23.888 -12.987 1.00 14.02 ?  26  GLU   B CA   1 
ATOM   4262 C C    . GLU   B 1 26  ? 50.953 -22.369 -12.912 1.00 13.33 ?  26  GLU   B C    1 
ATOM   4263 O O    . GLU   B 1 26  ? 50.755 -21.694 -13.927 1.00 14.83 ?  26  GLU   B O    1 
ATOM   4264 C CB   . GLU   B 1 26  ? 49.681 -24.467 -12.469 1.00 15.63 ?  26  GLU   B CB   1 
ATOM   4265 C CG   . GLU   B 1 26  ? 49.286 -25.776 -13.100 1.00 19.15 ?  26  GLU   B CG   1 
ATOM   4266 C CD   . GLU   B 1 26  ? 49.046 -25.673 -14.601 1.00 21.32 ?  26  GLU   B CD   1 
ATOM   4267 O OE1  . GLU   B 1 26  ? 48.089 -24.998 -15.037 1.00 21.44 ?  26  GLU   B OE1  1 
ATOM   4268 O OE2  . GLU   B 1 26  ? 49.811 -26.299 -15.345 1.00 23.42 -1 26  GLU   B OE2  1 
ATOM   4269 H H    . GLU   B 1 26  ? 51.889 -24.936 -11.568 1.00 16.43 ?  26  GLU   B H    1 
ATOM   4270 H HA   . GLU   B 1 26  ? 51.096 -24.139 -13.916 1.00 16.83 ?  26  GLU   B HA   1 
ATOM   4271 H HB2  . GLU   B 1 26  ? 49.755 -24.613 -11.513 1.00 18.75 ?  26  GLU   B HB2  1 
ATOM   4272 H HB3  . GLU   B 1 26  ? 48.966 -23.829 -12.644 1.00 18.75 ?  26  GLU   B HB3  1 
ATOM   4273 H HG2  . GLU   B 1 26  ? 50.000 -26.410 -12.958 1.00 22.98 ?  26  GLU   B HG2  1 
ATOM   4274 H HG3  . GLU   B 1 26  ? 48.465 -26.090 -12.693 1.00 22.98 ?  26  GLU   B HG3  1 
ATOM   4275 N N    . ALA   B 1 27  ? 51.095 -21.816 -11.707 1.00 12.74 ?  27  ALA   B N    1 
ATOM   4276 C CA   . ALA   B 1 27  ? 51.051 -20.366 -11.562 1.00 13.08 ?  27  ALA   B CA   1 
ATOM   4277 C C    . ALA   B 1 27  ? 52.125 -19.699 -12.411 1.00 14.06 ?  27  ALA   B C    1 
ATOM   4278 O O    . ALA   B 1 27  ? 51.863 -18.694 -13.089 1.00 14.78 ?  27  ALA   B O    1 
ATOM   4279 C CB   . ALA   B 1 27  ? 51.195 -19.977 -10.092 1.00 13.27 ?  27  ALA   B CB   1 
ATOM   4280 H H    . ALA   B 1 27  ? 51.212 -22.251 -10.972 1.00 15.29 ?  27  ALA   B H    1 
ATOM   4281 H HA   . ALA   B 1 27  ? 50.195 -20.044 -11.872 1.00 15.69 ?  27  ALA   B HA   1 
ATOM   4282 H HB1  . ALA   B 1 27  ? 51.157 -19.011 -10.017 1.00 15.93 ?  27  ALA   B HB1  1 
ATOM   4283 H HB2  . ALA   B 1 27  ? 50.462 -20.375 -9.593  1.00 15.93 ?  27  ALA   B HB2  1 
ATOM   4284 H HB3  . ALA   B 1 27  ? 52.041 -20.305 -9.758  1.00 15.93 ?  27  ALA   B HB3  1 
ATOM   4285 N N    . LYS   B 1 28  ? 53.340 -20.250 -12.398 1.00 15.41 ?  28  LYS   B N    1 
ATOM   4286 C CA   . LYS   B 1 28  ? 54.421 -19.634 -13.160 1.00 18.01 ?  28  LYS   B CA   1 
ATOM   4287 C C    . LYS   B 1 28  ? 54.166 -19.701 -14.661 1.00 18.75 ?  28  LYS   B C    1 
ATOM   4288 O O    . LYS   B 1 28  ? 54.570 -18.792 -15.397 1.00 19.96 ?  28  LYS   B O    1 
ATOM   4289 C CB   . LYS   B 1 28  ? 55.771 -20.242 -12.768 1.00 20.96 ?  28  LYS   B CB   1 
ATOM   4290 C CG   . LYS   B 1 28  ? 56.176 -19.894 -11.338 1.00 23.81 ?  28  LYS   B CG   1 
ATOM   4291 C CD   . LYS   B 1 28  ? 57.600 -20.310 -11.003 1.00 27.89 ?  28  LYS   B CD   1 
ATOM   4292 C CE   . LYS   B 1 28  ? 57.683 -21.774 -10.637 1.00 31.28 ?  28  LYS   B CE   1 
ATOM   4293 N NZ   . LYS   B 1 28  ? 59.030 -22.127 -10.106 1.00 32.27 ?  28  LYS   B NZ   1 
ATOM   4294 H H    . LYS   B 1 28  ? 53.566 -20.960 -11.964 1.00 18.49 ?  28  LYS   B H    1 
ATOM   4295 H HA   . LYS   B 1 28  ? 54.462 -18.695 -12.928 1.00 21.61 ?  28  LYS   B HA   1 
ATOM   4296 H HB2  . LYS   B 1 28  ? 55.722 -21.206 -12.836 1.00 25.15 ?  28  LYS   B HB2  1 
ATOM   4297 H HB3  . LYS   B 1 28  ? 56.461 -19.900 -13.360 1.00 25.15 ?  28  LYS   B HB3  1 
ATOM   4298 H HG2  . LYS   B 1 28  ? 56.104 -18.933 -11.217 1.00 28.58 ?  28  LYS   B HG2  1 
ATOM   4299 H HG3  . LYS   B 1 28  ? 55.576 -20.348 -10.725 1.00 28.58 ?  28  LYS   B HG3  1 
ATOM   4300 H HD2  . LYS   B 1 28  ? 58.165 -20.155 -11.776 1.00 33.46 ?  28  LYS   B HD2  1 
ATOM   4301 H HD3  . LYS   B 1 28  ? 57.913 -19.786 -10.249 1.00 33.46 ?  28  LYS   B HD3  1 
ATOM   4302 H HE2  . LYS   B 1 28  ? 57.025 -21.969 -9.951  1.00 37.53 ?  28  LYS   B HE2  1 
ATOM   4303 H HE3  . LYS   B 1 28  ? 57.515 -22.313 -11.425 1.00 37.53 ?  28  LYS   B HE3  1 
ATOM   4304 H HZ1  . LYS   B 1 28  ? 59.057 -22.992 -9.896  1.00 38.72 ?  28  LYS   B HZ1  1 
ATOM   4305 H HZ2  . LYS   B 1 28  ? 59.652 -21.958 -10.720 1.00 38.72 ?  28  LYS   B HZ2  1 
ATOM   4306 H HZ3  . LYS   B 1 28  ? 59.205 -21.647 -9.377  1.00 38.72 ?  28  LYS   B HZ3  1 
ATOM   4307 N N    . LYS   B 1 29  ? 53.462 -20.732 -15.127 1.00 19.73 ?  29  LYS   B N    1 
ATOM   4308 C CA   . LYS   B 1 29  ? 53.172 -20.883 -16.550 1.00 22.15 ?  29  LYS   B CA   1 
ATOM   4309 C C    . LYS   B 1 29  ? 51.918 -20.132 -16.990 1.00 20.78 ?  29  LYS   B C    1 
ATOM   4310 O O    . LYS   B 1 29  ? 51.914 -19.516 -18.062 1.00 21.85 ?  29  LYS   B O    1 
ATOM   4311 C CB   . LYS   B 1 29  ? 53.037 -22.367 -16.897 1.00 26.89 ?  29  LYS   B CB   1 
ATOM   4312 C CG   . LYS   B 1 29  ? 52.925 -22.645 -18.386 1.00 31.10 ?  29  LYS   B CG   1 
ATOM   4313 C CD   . LYS   B 1 29  ? 53.168 -24.114 -18.698 1.00 34.37 ?  29  LYS   B CD   1 
ATOM   4314 C CE   . LYS   B 1 29  ? 52.094 -25.005 -18.095 1.00 36.74 ?  29  LYS   B CE   1 
ATOM   4315 N NZ   . LYS   B 1 29  ? 52.339 -26.444 -18.397 1.00 37.94 ?  29  LYS   B NZ   1 
ATOM   4316 H H    . LYS   B 1 29  ? 53.143 -21.361 -14.632 1.00 23.68 ?  29  LYS   B H    1 
ATOM   4317 H HA   . LYS   B 1 29  ? 53.914 -20.527 -17.054 1.00 26.58 ?  29  LYS   B HA   1 
ATOM   4318 H HB2  . LYS   B 1 29  ? 53.822 -22.836 -16.569 1.00 32.26 ?  29  LYS   B HB2  1 
ATOM   4319 H HB3  . LYS   B 1 29  ? 52.243 -22.719 -16.470 1.00 32.26 ?  29  LYS   B HB3  1 
ATOM   4320 H HG2  . LYS   B 1 29  ? 52.032 -22.414 -18.687 1.00 37.33 ?  29  LYS   B HG2  1 
ATOM   4321 H HG3  . LYS   B 1 29  ? 53.587 -22.119 -18.861 1.00 37.33 ?  29  LYS   B HG3  1 
ATOM   4322 H HD2  . LYS   B 1 29  ? 53.164 -24.241 -19.660 1.00 41.25 ?  29  LYS   B HD2  1 
ATOM   4323 H HD3  . LYS   B 1 29  ? 54.026 -24.381 -18.330 1.00 41.25 ?  29  LYS   B HD3  1 
ATOM   4324 H HE2  . LYS   B 1 29  ? 52.089 -24.896 -17.131 1.00 44.09 ?  29  LYS   B HE2  1 
ATOM   4325 H HE3  . LYS   B 1 29  ? 51.231 -24.759 -18.465 1.00 44.09 ?  29  LYS   B HE3  1 
ATOM   4326 H HZ1  . LYS   B 1 29  ? 51.698 -26.944 -18.034 1.00 45.53 ?  29  LYS   B HZ1  1 
ATOM   4327 H HZ2  . LYS   B 1 29  ? 52.344 -26.573 -19.278 1.00 45.53 ?  29  LYS   B HZ2  1 
ATOM   4328 H HZ3  . LYS   B 1 29  ? 53.125 -26.695 -18.064 1.00 45.53 ?  29  LYS   B HZ3  1 
ATOM   4329 N N    . VAL   B 1 30  ? 50.850 -20.185 -16.187 1.00 19.06 ?  30  VAL   B N    1 
ATOM   4330 C CA   . VAL   B 1 30  ? 49.556 -19.603 -16.558 1.00 18.96 ?  30  VAL   B CA   1 
ATOM   4331 C C    . VAL   B 1 30  ? 49.550 -18.087 -16.420 1.00 17.82 ?  30  VAL   B C    1 
ATOM   4332 O O    . VAL   B 1 30  ? 48.795 -17.393 -17.120 1.00 18.67 ?  30  VAL   B O    1 
ATOM   4333 C CB   . VAL   B 1 30  ? 48.458 -20.219 -15.668 1.00 20.02 ?  30  VAL   B CB   1 
ATOM   4334 C CG1  . VAL   B 1 30  ? 47.163 -19.419 -15.755 1.00 20.38 ?  30  VAL   B CG1  1 
ATOM   4335 C CG2  . VAL   B 1 30  ? 48.222 -21.678 -16.032 1.00 20.53 ?  30  VAL   B CG2  1 
ATOM   4336 H H    . VAL   B 1 30  ? 50.838 -20.579 -15.414 1.00 22.88 ?  30  VAL   B H    1 
ATOM   4337 H HA   . VAL   B 1 30  ? 49.353 -19.843 -17.478 1.00 22.75 ?  30  VAL   B HA   1 
ATOM   4338 H HB   . VAL   B 1 30  ? 48.751 -20.198 -14.744 1.00 24.02 ?  30  VAL   B HB   1 
ATOM   4339 H HG11 . VAL   B 1 30  ? 46.424 -20.002 -15.523 1.00 24.46 ?  30  VAL   B HG11 1 
ATOM   4340 H HG12 . VAL   B 1 30  ? 47.203 -18.678 -15.132 1.00 24.46 ?  30  VAL   B HG12 1 
ATOM   4341 H HG13 . VAL   B 1 30  ? 47.046 -19.099 -16.659 1.00 24.46 ?  30  VAL   B HG13 1 
ATOM   4342 H HG21 . VAL   B 1 30  ? 47.532 -22.046 -15.450 1.00 24.64 ?  30  VAL   B HG21 1 
ATOM   4343 H HG22 . VAL   B 1 30  ? 47.928 -21.730 -16.957 1.00 24.64 ?  30  VAL   B HG22 1 
ATOM   4344 H HG23 . VAL   B 1 30  ? 49.046 -22.171 -15.917 1.00 24.64 ?  30  VAL   B HG23 1 
ATOM   4345 N N    . LYS   B 1 31  ? 50.339 -17.566 -15.492 1.00 17.34 ?  31  LYS   B N    1 
ATOM   4346 C CA   . LYS   B 1 31  ? 50.364 -16.157 -15.132 1.00 17.76 ?  31  LYS   B CA   1 
ATOM   4347 C C    . LYS   B 1 31  ? 48.966 -15.686 -14.730 1.00 15.74 ?  31  LYS   B C    1 
ATOM   4348 O O    . LYS   B 1 31  ? 48.408 -14.776 -15.357 1.00 16.82 ?  31  LYS   B O    1 
ATOM   4349 C CB   . LYS   B 1 31  ? 50.991 -15.337 -16.267 1.00 21.03 ?  31  LYS   B CB   1 
ATOM   4350 C CG   . LYS   B 1 31  ? 52.403 -15.811 -16.623 1.00 24.54 ?  31  LYS   B CG   1 
ATOM   4351 C CD   . LYS   B 1 31  ? 52.997 -15.026 -17.773 1.00 27.95 ?  31  LYS   B CD   1 
ATOM   4352 C CE   . LYS   B 1 31  ? 54.479 -15.308 -17.913 1.00 30.65 ?  31  LYS   B CE   1 
ATOM   4353 N NZ   . LYS   B 1 31  ? 55.226 -14.897 -16.690 1.00 31.67 ?  31  LYS   B NZ   1 
ATOM   4354 H H    . LYS   B 1 31  ? 50.890 -18.046 -15.043 1.00 20.81 ?  31  LYS   B H    1 
ATOM   4355 H HA   . LYS   B 1 31  ? 50.925 -16.069 -14.360 1.00 21.31 ?  31  LYS   B HA   1 
ATOM   4356 H HB2  . LYS   B 1 31  ? 50.439 -15.413 -17.061 1.00 25.23 ?  31  LYS   B HB2  1 
ATOM   4357 H HB3  . LYS   B 1 31  ? 51.046 -14.414 -15.984 1.00 25.23 ?  31  LYS   B HB3  1 
ATOM   4358 H HG2  . LYS   B 1 31  ? 52.974 -15.704 -15.846 1.00 29.44 ?  31  LYS   B HG2  1 
ATOM   4359 H HG3  . LYS   B 1 31  ? 52.369 -16.748 -16.881 1.00 29.44 ?  31  LYS   B HG3  1 
ATOM   4360 H HD2  . LYS   B 1 31  ? 52.555 -15.285 -18.596 1.00 33.54 ?  31  LYS   B HD2  1 
ATOM   4361 H HD3  . LYS   B 1 31  ? 52.878 -14.080 -17.606 1.00 33.54 ?  31  LYS   B HD3  1 
ATOM   4362 H HE2  . LYS   B 1 31  ? 54.615 -16.260 -18.048 1.00 36.78 ?  31  LYS   B HE2  1 
ATOM   4363 H HE3  . LYS   B 1 31  ? 54.829 -14.809 -18.667 1.00 36.78 ?  31  LYS   B HE3  1 
ATOM   4364 H HZ1  . LYS   B 1 31  ? 56.102 -14.937 -16.840 1.00 38.00 ?  31  LYS   B HZ1  1 
ATOM   4365 H HZ2  . LYS   B 1 31  ? 55.009 -14.063 -16.467 1.00 38.00 ?  31  LYS   B HZ2  1 
ATOM   4366 H HZ3  . LYS   B 1 31  ? 55.025 -15.438 -16.012 1.00 38.00 ?  31  LYS   B HZ3  1 
ATOM   4367 N N    . PRO   B 1 32  ? 48.370 -16.278 -13.687 1.00 13.98 ?  32  PRO   B N    1 
ATOM   4368 C CA   . PRO   B 1 32  ? 46.994 -15.922 -13.319 1.00 12.95 ?  32  PRO   B CA   1 
ATOM   4369 C C    . PRO   B 1 32  ? 46.906 -14.578 -12.613 1.00 13.01 ?  32  PRO   B C    1 
ATOM   4370 O O    . PRO   B 1 32  ? 47.830 -14.147 -11.917 1.00 14.08 ?  32  PRO   B O    1 
ATOM   4371 C CB   . PRO   B 1 32  ? 46.601 -17.044 -12.349 1.00 13.20 ?  32  PRO   B CB   1 
ATOM   4372 C CG   . PRO   B 1 32  ? 47.902 -17.390 -11.679 1.00 13.43 ?  32  PRO   B CG   1 
ATOM   4373 C CD   . PRO   B 1 32  ? 48.960 -17.247 -12.741 1.00 13.78 ?  32  PRO   B CD   1 
ATOM   4374 H HA   . PRO   B 1 32  ? 46.409 -15.935 -14.097 1.00 15.54 ?  32  PRO   B HA   1 
ATOM   4375 H HB2  . PRO   B 1 32  ? 45.954 -16.715 -11.704 1.00 15.84 ?  32  PRO   B HB2  1 
ATOM   4376 H HB3  . PRO   B 1 32  ? 46.251 -17.803 -12.839 1.00 15.84 ?  32  PRO   B HB3  1 
ATOM   4377 H HG2  . PRO   B 1 32  ? 48.069 -16.771 -10.946 1.00 16.12 ?  32  PRO   B HG2  1 
ATOM   4378 H HG3  . PRO   B 1 32  ? 47.874 -18.301 -11.351 1.00 16.12 ?  32  PRO   B HG3  1 
ATOM   4379 H HD2  . PRO   B 1 32  ? 49.776 -16.884 -12.358 1.00 16.53 ?  32  PRO   B HD2  1 
ATOM   4380 H HD3  . PRO   B 1 32  ? 49.115 -18.091 -13.179 1.00 16.53 ?  32  PRO   B HD3  1 
ATOM   4381 N N    . THR   B 1 33  ? 45.752 -13.926 -12.779 1.00 12.32 ?  33  THR   B N    1 
ATOM   4382 C CA   . THR   B 1 33  ? 45.456 -12.751 -11.969 1.00 12.58 ?  33  THR   B CA   1 
ATOM   4383 C C    . THR   B 1 33  ? 45.408 -13.107 -10.489 1.00 12.34 ?  33  THR   B C    1 
ATOM   4384 O O    . THR   B 1 33  ? 45.880 -12.328 -9.647  1.00 13.25 ?  33  THR   B O    1 
ATOM   4385 C CB   . THR   B 1 33  ? 44.139 -12.115 -12.417 1.00 13.32 ?  33  THR   B CB   1 
ATOM   4386 O OG1  . THR   B 1 33  ? 44.183 -11.865 -13.824 1.00 13.52 ?  33  THR   B OG1  1 
ATOM   4387 C CG2  . THR   B 1 33  ? 43.887 -10.814 -11.668 1.00 14.50 ?  33  THR   B CG2  1 
ATOM   4388 H H    . THR   B 1 33  ? 45.129 -14.147 -13.335 1.00 14.78 ?  33  THR   B H    1 
ATOM   4389 H HA   . THR   B 1 33  ? 46.157 -12.098 -12.096 1.00 15.10 ?  33  THR   B HA   1 
ATOM   4390 H HB   . THR   B 1 33  ? 43.404 -12.723 -12.226 1.00 15.98 ?  33  THR   B HB   1 
ATOM   4391 H HG1  . THR   B 1 33  ? 43.463 -11.499 -14.077 1.00 16.22 ?  33  THR   B HG1  1 
ATOM   4392 H HG21 . THR   B 1 33  ? 43.134 -10.347 -12.057 1.00 17.41 ?  33  THR   B HG21 1 
ATOM   4393 H HG22 . THR   B 1 33  ? 43.696 -10.999 -10.734 1.00 17.41 ?  33  THR   B HG22 1 
ATOM   4394 H HG23 . THR   B 1 33  ? 44.673 -10.247 -11.722 1.00 17.41 ?  33  THR   B HG23 1 
ATOM   4395 N N    . VAL   B 1 34  ? 44.861 -14.280 -10.150 1.00 11.59 ?  34  VAL   B N    1 
ATOM   4396 C CA   . VAL   B 1 34  ? 44.669 -14.679 -8.760  1.00 10.98 ?  34  VAL   B CA   1 
ATOM   4397 C C    . VAL   B 1 34  ? 45.092 -16.130 -8.593  1.00 10.21 ?  34  VAL   B C    1 
ATOM   4398 O O    . VAL   B 1 34  ? 44.573 -17.016 -9.280  1.00 10.93 ?  34  VAL   B O    1 
ATOM   4399 C CB   . VAL   B 1 34  ? 43.198 -14.537 -8.320  1.00 12.42 ?  34  VAL   B CB   1 
ATOM   4400 C CG1  . VAL   B 1 34  ? 43.026 -14.994 -6.877  1.00 12.84 ?  34  VAL   B CG1  1 
ATOM   4401 C CG2  . VAL   B 1 34  ? 42.701 -13.109 -8.514  1.00 13.38 ?  34  VAL   B CG2  1 
ATOM   4402 H H    . VAL   B 1 34  ? 44.606 -14.872 -10.719 1.00 13.91 ?  34  VAL   B H    1 
ATOM   4403 H HA   . VAL   B 1 34  ? 45.224 -14.127 -8.183  1.00 13.18 ?  34  VAL   B HA   1 
ATOM   4404 H HB   . VAL   B 1 34  ? 42.657 -15.114 -8.881  1.00 14.90 ?  34  VAL   B HB   1 
ATOM   4405 H HG11 . VAL   B 1 34  ? 42.167 -14.680 -6.551  1.00 15.41 ?  34  VAL   B HG11 1 
ATOM   4406 H HG12 . VAL   B 1 34  ? 43.056 -15.963 -6.843  1.00 15.41 ?  34  VAL   B HG12 1 
ATOM   4407 H HG13 . VAL   B 1 34  ? 43.739 -14.619 -6.338  1.00 15.41 ?  34  VAL   B HG13 1 
ATOM   4408 H HG21 . VAL   B 1 34  ? 41.786 -13.048 -8.202  1.00 16.06 ?  34  VAL   B HG21 1 
ATOM   4409 H HG22 . VAL   B 1 34  ? 43.266 -12.504 -8.009  1.00 16.06 ?  34  VAL   B HG22 1 
ATOM   4410 H HG23 . VAL   B 1 34  ? 42.741 -12.883 -9.460  1.00 16.06 ?  34  VAL   B HG23 1 
ATOM   4411 N N    . VAL   B 1 35  ? 46.003 -16.378 -7.655  1.00 9.83  ?  35  VAL   B N    1 
ATOM   4412 C CA   . VAL   B 1 35  ? 46.239 -17.721 -7.136  1.00 9.87  ?  35  VAL   B CA   1 
ATOM   4413 C C    . VAL   B 1 35  ? 45.696 -17.773 -5.716  1.00 9.61  ?  35  VAL   B C    1 
ATOM   4414 O O    . VAL   B 1 35  ? 45.914 -16.848 -4.925  1.00 9.98  ?  35  VAL   B O    1 
ATOM   4415 C CB   . VAL   B 1 35  ? 47.725 -18.144 -7.206  1.00 10.39 ?  35  VAL   B CB   1 
ATOM   4416 C CG1  . VAL   B 1 35  ? 48.616 -17.299 -6.287  1.00 11.18 ?  35  VAL   B CG1  1 
ATOM   4417 C CG2  . VAL   B 1 35  ? 47.861 -19.628 -6.879  1.00 11.07 ?  35  VAL   B CG2  1 
ATOM   4418 H H    . VAL   B 1 35  ? 46.511 -15.778 -7.304  1.00 11.80 ?  35  VAL   B H    1 
ATOM   4419 H HA   . VAL   B 1 35  ? 45.728 -18.354 -7.664  1.00 11.85 ?  35  VAL   B HA   1 
ATOM   4420 H HB   . VAL   B 1 35  ? 48.039 -18.025 -8.114  1.00 12.47 ?  35  VAL   B HB   1 
ATOM   4421 H HG11 . VAL   B 1 35  ? 49.540 -17.522 -6.456  1.00 13.42 ?  35  VAL   B HG11 1 
ATOM   4422 H HG12 . VAL   B 1 35  ? 48.451 -16.366 -6.472  1.00 13.42 ?  35  VAL   B HG12 1 
ATOM   4423 H HG13 . VAL   B 1 35  ? 48.388 -17.500 -5.362  1.00 13.42 ?  35  VAL   B HG13 1 
ATOM   4424 H HG21 . VAL   B 1 35  ? 48.785 -19.900 -6.983  1.00 13.28 ?  35  VAL   B HG21 1 
ATOM   4425 H HG22 . VAL   B 1 35  ? 47.576 -19.783 -5.960  1.00 13.28 ?  35  VAL   B HG22 1 
ATOM   4426 H HG23 . VAL   B 1 35  ? 47.297 -20.146 -7.482  1.00 13.28 ?  35  VAL   B HG23 1 
ATOM   4427 N N    . VAL   B 1 36  ? 44.979 -18.855 -5.396  1.00 9.59  ?  36  VAL   B N    1 
ATOM   4428 C CA   . VAL   B 1 36  ? 44.435 -19.063 -4.064  1.00 9.32  ?  36  VAL   B CA   1 
ATOM   4429 C C    . VAL   B 1 36  ? 45.439 -19.827 -3.213  1.00 9.16  ?  36  VAL   B C    1 
ATOM   4430 O O    . VAL   B 1 36  ? 45.986 -20.857 -3.636  1.00 10.17 ?  36  VAL   B O    1 
ATOM   4431 C CB   . VAL   B 1 36  ? 43.098 -19.822 -4.143  1.00 9.73  ?  36  VAL   B CB   1 
ATOM   4432 C CG1  . VAL   B 1 36  ? 42.588 -20.180 -2.758  1.00 10.44 ?  36  VAL   B CG1  1 
ATOM   4433 C CG2  . VAL   B 1 36  ? 42.071 -18.989 -4.895  1.00 9.85  ?  36  VAL   B CG2  1 
ATOM   4434 H H    . VAL   B 1 36  ? 44.803 -19.494 -5.946  1.00 11.50 ?  36  VAL   B H    1 
ATOM   4435 H HA   . VAL   B 1 36  ? 44.268 -18.201 -3.649  1.00 11.18 ?  36  VAL   B HA   1 
ATOM   4436 H HB   . VAL   B 1 36  ? 43.230 -20.644 -4.638  1.00 11.67 ?  36  VAL   B HB   1 
ATOM   4437 H HG11 . VAL   B 1 36  ? 41.648 -20.411 -2.820  1.00 12.53 ?  36  VAL   B HG11 1 
ATOM   4438 H HG12 . VAL   B 1 36  ? 43.095 -20.922 -2.413  1.00 12.53 ?  36  VAL   B HG12 1 
ATOM   4439 H HG13 . VAL   B 1 36  ? 42.692 -19.402 -2.178  1.00 12.53 ?  36  VAL   B HG13 1 
ATOM   4440 H HG21 . VAL   B 1 36  ? 41.230 -19.465 -4.916  1.00 11.82 ?  36  VAL   B HG21 1 
ATOM   4441 H HG22 . VAL   B 1 36  ? 41.964 -18.137 -4.445  1.00 11.82 ?  36  VAL   B HG22 1 
ATOM   4442 H HG23 . VAL   B 1 36  ? 42.390 -18.840 -5.804  1.00 11.82 ?  36  VAL   B HG23 1 
ATOM   4443 N N    . ASN   B 1 37  ? 45.655 -19.332 -1.997  1.00 9.43  ?  37  ASN   B N    1 
ATOM   4444 C CA   . ASN   B 1 37  ? 46.406 -20.053 -0.986  1.00 9.81  ?  37  ASN   B CA   1 
ATOM   4445 C C    . ASN   B 1 37  ? 45.461 -20.726 -0.001  1.00 9.72  ?  37  ASN   B C    1 
ATOM   4446 O O    . ASN   B 1 37  ? 44.452 -20.147 0.411   1.00 10.15 ?  37  ASN   B O    1 
ATOM   4447 C CB   . ASN   B 1 37  ? 47.341 -19.108 -0.231  1.00 9.79  ?  37  ASN   B CB   1 
ATOM   4448 C CG   . ASN   B 1 37  ? 48.193 -19.822 0.787   1.00 10.33 ?  37  ASN   B CG   1 
ATOM   4449 O OD1  . ASN   B 1 37  ? 48.537 -20.999 0.616   1.00 10.92 ?  37  ASN   B OD1  1 
ATOM   4450 N ND2  . ASN   B 1 37  ? 48.534 -19.119 1.859   1.00 10.42 ?  37  ASN   B ND2  1 
ATOM   4451 H H    . ASN   B 1 37  ? 45.360 -18.569 -1.723  1.00 11.32 ?  37  ASN   B H    1 
ATOM   4452 H HA   . ASN   B 1 37  ? 46.939 -20.745 -1.407  1.00 11.78 ?  37  ASN   B HA   1 
ATOM   4453 H HB2  . ASN   B 1 37  ? 47.931 -18.683 -0.869  1.00 11.74 ?  37  ASN   B HB2  1 
ATOM   4454 H HB3  . ASN   B 1 37  ? 46.812 -18.444 0.233   1.00 11.74 ?  37  ASN   B HB3  1 
ATOM   4455 H HD21 . ASN   B 1 37  ? 49.027 -19.482 2.468   1.00 12.51 ?  37  ASN   B HD21 1 
ATOM   4456 H HD22 . ASN   B 1 37  ? 48.282 -18.311 1.944   1.00 12.51 ?  37  ASN   B HD22 1 
ATOM   4457 N N    . ALA   B 1 38  ? 45.807 -21.961 0.374   1.00 9.92  ?  38  ALA   B N    1 
ATOM   4458 C CA   . ALA   B 1 38  ? 45.151 -22.703 1.452   1.00 10.40 ?  38  ALA   B CA   1 
ATOM   4459 C C    . ALA   B 1 38  ? 45.738 -22.221 2.775   1.00 10.17 ?  38  ALA   B C    1 
ATOM   4460 O O    . ALA   B 1 38  ? 46.643 -22.827 3.357   1.00 11.02 ?  38  ALA   B O    1 
ATOM   4461 C CB   . ALA   B 1 38  ? 45.364 -24.200 1.267   1.00 11.56 ?  38  ALA   B CB   1 
ATOM   4462 H H    . ALA   B 1 38  ? 46.454 -22.400 0.018   1.00 11.90 ?  38  ALA   B H    1 
ATOM   4463 H HA   . ALA   B 1 38  ? 44.196 -22.519 1.445   1.00 12.48 ?  38  ALA   B HA   1 
ATOM   4464 H HB1  . ALA   B 1 38  ? 44.913 -24.674 1.992   1.00 13.87 ?  38  ALA   B HB1  1 
ATOM   4465 H HB2  . ALA   B 1 38  ? 44.980 -24.472 0.417   1.00 13.87 ?  38  ALA   B HB2  1 
ATOM   4466 H HB3  . ALA   B 1 38  ? 46.308 -24.393 1.287   1.00 13.87 ?  38  ALA   B HB3  1 
ATOM   4467 N N    . ALA   B 1 39  ? 45.221 -21.082 3.238   1.00 10.25 ?  39  ALA   B N    1 
ATOM   4468 C CA   . ALA   B 1 39  ? 45.768 -20.352 4.370   1.00 10.60 ?  39  ALA   B CA   1 
ATOM   4469 C C    . ALA   B 1 39  ? 45.145 -20.799 5.691   1.00 10.45 ?  39  ALA   B C    1 
ATOM   4470 O O    . ALA   B 1 39  ? 44.115 -21.475 5.737   1.00 11.31 ?  39  ALA   B O    1 
ATOM   4471 C CB   . ALA   B 1 39  ? 45.529 -18.852 4.178   1.00 11.40 ?  39  ALA   B CB   1 
ATOM   4472 H H    . ALA   B 1 39  ? 44.527 -20.702 2.892   1.00 12.30 ?  39  ALA   B H    1 
ATOM   4473 H HA   . ALA   B 1 39  ? 46.719 -20.506 4.418   1.00 12.72 ?  39  ALA   B HA   1 
ATOM   4474 H HB1  . ALA   B 1 39  ? 45.898 -18.375 4.938   1.00 13.68 ?  39  ALA   B HB1  1 
ATOM   4475 H HB2  . ALA   B 1 39  ? 45.974 -18.566 3.363   1.00 13.68 ?  39  ALA   B HB2  1 
ATOM   4476 H HB3  . ALA   B 1 39  ? 44.578 -18.685 4.111   1.00 13.68 ?  39  ALA   B HB3  1 
ATOM   4477 N N    . ASN   B 1 40  ? 45.788 -20.381 6.780   1.00 11.24 ?  40  ASN   B N    1 
ATOM   4478 C CA   . ASN   B 1 40  ? 45.225 -20.434 8.120   1.00 11.72 ?  40  ASN   B CA   1 
ATOM   4479 C C    . ASN   B 1 40  ? 45.049 -19.008 8.646   1.00 11.42 ?  40  ASN   B C    1 
ATOM   4480 O O    . ASN   B 1 40  ? 45.456 -18.026 8.016   1.00 11.55 ?  40  ASN   B O    1 
ATOM   4481 C CB   . ASN   B 1 40  ? 46.069 -21.315 9.058   1.00 12.53 ?  40  ASN   B CB   1 
ATOM   4482 C CG   . ASN   B 1 40  ? 47.527 -20.912 9.093   1.00 13.52 ?  40  ASN   B CG   1 
ATOM   4483 O OD1  . ASN   B 1 40  ? 47.851 -19.731 9.147   1.00 15.41 ?  40  ASN   B OD1  1 
ATOM   4484 N ND2  . ASN   B 1 40  ? 48.416 -21.891 9.058   1.00 13.67 ?  40  ASN   B ND2  1 
ATOM   4485 H H    . ASN   B 1 40  ? 46.584 -20.065 6.762   1.00 13.49 ?  40  ASN   B H    1 
ATOM   4486 H HA   . ASN   B 1 40  ? 44.339 -20.829 8.071   1.00 14.07 ?  40  ASN   B HA   1 
ATOM   4487 H HB2  . ASN   B 1 40  ? 45.717 -21.242 9.958   1.00 15.03 ?  40  ASN   B HB2  1 
ATOM   4488 H HB3  . ASN   B 1 40  ? 46.017 -22.233 8.752   1.00 15.03 ?  40  ASN   B HB3  1 
ATOM   4489 H HD21 . ASN   B 1 40  ? 49.257 -21.713 9.079   1.00 16.40 ?  40  ASN   B HD21 1 
ATOM   4490 H HD22 . ASN   B 1 40  ? 48.151 -22.709 9.026   1.00 16.40 ?  40  ASN   B HD22 1 
ATOM   4491 N N    . VAL   B 1 41  ? 44.394 -18.885 9.803   1.00 12.02 ?  41  VAL   B N    1 
ATOM   4492 C CA   . VAL   B 1 41  ? 43.933 -17.564 10.246  1.00 12.60 ?  41  VAL   B CA   1 
ATOM   4493 C C    . VAL   B 1 41  ? 45.082 -16.611 10.553  1.00 12.59 ?  41  VAL   B C    1 
ATOM   4494 O O    . VAL   B 1 41  ? 44.904 -15.389 10.472  1.00 12.86 ?  41  VAL   B O    1 
ATOM   4495 C CB   . VAL   B 1 41  ? 42.947 -17.637 11.428  1.00 13.93 ?  41  VAL   B CB   1 
ATOM   4496 C CG1  . VAL   B 1 41  ? 41.655 -18.325 11.015  1.00 14.42 ?  41  VAL   B CG1  1 
ATOM   4497 C CG2  . VAL   B 1 41  ? 43.584 -18.315 12.628  1.00 14.85 ?  41  VAL   B CG2  1 
ATOM   4498 H H    . VAL   B 1 41  ? 44.208 -19.527 10.334  1.00 14.42 ?  41  VAL   B H    1 
ATOM   4499 H HA   . VAL   B 1 41  ? 43.445 -17.164 9.512   1.00 15.12 ?  41  VAL   B HA   1 
ATOM   4500 H HB   . VAL   B 1 41  ? 42.717 -16.732 11.696  1.00 16.72 ?  41  VAL   B HB   1 
ATOM   4501 H HG11 . VAL   B 1 41  ? 41.042 -18.326 11.768  1.00 17.30 ?  41  VAL   B HG11 1 
ATOM   4502 H HG12 . VAL   B 1 41  ? 41.264 -17.844 10.270  1.00 17.30 ?  41  VAL   B HG12 1 
ATOM   4503 H HG13 . VAL   B 1 41  ? 41.856 -19.238 10.753  1.00 17.30 ?  41  VAL   B HG13 1 
ATOM   4504 H HG21 . VAL   B 1 41  ? 42.937 -18.357 13.347  1.00 17.82 ?  41  VAL   B HG21 1 
ATOM   4505 H HG22 . VAL   B 1 41  ? 43.854 -19.213 12.375  1.00 17.82 ?  41  VAL   B HG22 1 
ATOM   4506 H HG23 . VAL   B 1 41  ? 44.358 -17.803 12.906  1.00 17.82 ?  41  VAL   B HG23 1 
ATOM   4507 N N    . TYR   B 1 42  ? 46.249 -17.127 10.941  1.00 12.80 ?  42  TYR   B N    1 
ATOM   4508 C CA   . TYR   B 1 42  ? 47.406 -16.282 11.213  1.00 13.51 ?  42  TYR   B CA   1 
ATOM   4509 C C    . TYR   B 1 42  ? 48.373 -16.208 10.035  1.00 12.61 ?  42  TYR   B C    1 
ATOM   4510 O O    . TYR   B 1 42  ? 49.456 -15.629 10.168  1.00 13.62 ?  42  TYR   B O    1 
ATOM   4511 C CB   . TYR   B 1 42  ? 48.100 -16.688 12.520  1.00 15.48 ?  42  TYR   B CB   1 
ATOM   4512 C CG   . TYR   B 1 42  ? 47.494 -16.003 13.742  1.00 15.81 ?  42  TYR   B CG   1 
ATOM   4513 C CD1  . TYR   B 1 42  ? 47.728 -14.651 13.983  1.00 14.87 ?  42  TYR   B CD1  1 
ATOM   4514 C CD2  . TYR   B 1 42  ? 46.697 -16.693 14.640  1.00 17.67 ?  42  TYR   B CD2  1 
ATOM   4515 C CE1  . TYR   B 1 42  ? 47.185 -14.009 15.077  1.00 15.86 ?  42  TYR   B CE1  1 
ATOM   4516 C CE2  . TYR   B 1 42  ? 46.149 -16.058 15.746  1.00 17.86 ?  42  TYR   B CE2  1 
ATOM   4517 C CZ   . TYR   B 1 42  ? 46.395 -14.713 15.959  1.00 17.92 ?  42  TYR   B CZ   1 
ATOM   4518 O OH   . TYR   B 1 42  ? 45.862 -14.070 17.058  1.00 20.63 ?  42  TYR   B OH   1 
ATOM   4519 H H    . TYR   B 1 42  ? 46.394 -17.972 11.045  1.00 15.36 ?  42  TYR   B H    1 
ATOM   4520 H HA   . TYR   B 1 42  ? 47.081 -15.382 11.347  1.00 16.21 ?  42  TYR   B HA   1 
ATOM   4521 H HB2  . TYR   B 1 42  ? 48.017 -17.644 12.641  1.00 18.57 ?  42  TYR   B HB2  1 
ATOM   4522 H HB3  . TYR   B 1 42  ? 49.039 -16.439 12.467  1.00 18.57 ?  42  TYR   B HB3  1 
ATOM   4523 H HD1  . TYR   B 1 42  ? 48.266 -14.168 13.385  1.00 17.84 ?  42  TYR   B HD1  1 
ATOM   4524 H HD2  . TYR   B 1 42  ? 46.527 -17.597 14.494  1.00 21.20 ?  42  TYR   B HD2  1 
ATOM   4525 H HE1  . TYR   B 1 42  ? 47.358 -13.107 15.219  1.00 19.03 ?  42  TYR   B HE1  1 
ATOM   4526 H HE2  . TYR   B 1 42  ? 45.614 -16.536 16.335  1.00 21.43 ?  42  TYR   B HE2  1 
ATOM   4527 H HH   . TYR   B 1 42  ? 46.096 -13.266 17.050  1.00 24.75 ?  42  TYR   B HH   1 
ATOM   4528 N N    . LEU   B 1 43  ? 47.978 -16.722 8.873   1.00 11.67 ?  43  LEU   B N    1 
ATOM   4529 C CA   . LEU   B 1 43  ? 48.791 -16.645 7.663   1.00 11.44 ?  43  LEU   B CA   1 
ATOM   4530 C C    . LEU   B 1 43  ? 50.206 -17.154 7.915   1.00 11.70 ?  43  LEU   B C    1 
ATOM   4531 O O    . LEU   B 1 43  ? 51.186 -16.553 7.471   1.00 12.48 ?  43  LEU   B O    1 
ATOM   4532 C CB   . LEU   B 1 43  ? 48.804 -15.236 7.065   1.00 11.45 ?  43  LEU   B CB   1 
ATOM   4533 C CG   . LEU   B 1 43  ? 47.446 -14.631 6.683   1.00 11.72 ?  43  LEU   B CG   1 
ATOM   4534 C CD1  . LEU   B 1 43  ? 47.661 -13.229 6.099   1.00 12.94 ?  43  LEU   B CD1  1 
ATOM   4535 C CD2  . LEU   B 1 43  ? 46.681 -15.523 5.714   1.00 12.10 ?  43  LEU   B CD2  1 
ATOM   4536 H H    . LEU   B 1 43  ? 47.235 -17.140 8.757   1.00 14.00 ?  43  LEU   B H    1 
ATOM   4537 H HA   . LEU   B 1 43  ? 48.393 -17.231 6.995   1.00 13.72 ?  43  LEU   B HA   1 
ATOM   4538 H HB2  . LEU   B 1 43  ? 49.214 -14.640 7.706   1.00 13.74 ?  43  LEU   B HB2  1 
ATOM   4539 H HB3  . LEU   B 1 43  ? 49.338 -15.258 6.256   1.00 13.74 ?  43  LEU   B HB3  1 
ATOM   4540 H HG   . LEU   B 1 43  ? 46.910 -14.533 7.486   1.00 14.07 ?  43  LEU   B HG   1 
ATOM   4541 H HD11 . LEU   B 1 43  ? 46.803 -12.846 5.863   1.00 15.53 ?  43  LEU   B HD11 1 
ATOM   4542 H HD12 . LEU   B 1 43  ? 48.097 -12.671 6.768   1.00 15.53 ?  43  LEU   B HD12 1 
ATOM   4543 H HD13 . LEU   B 1 43  ? 48.223 -13.296 5.312   1.00 15.53 ?  43  LEU   B HD13 1 
ATOM   4544 H HD21 . LEU   B 1 43  ? 45.883 -15.060 5.419   1.00 14.52 ?  43  LEU   B HD21 1 
ATOM   4545 H HD22 . LEU   B 1 43  ? 47.250 -15.723 4.955   1.00 14.52 ?  43  LEU   B HD22 1 
ATOM   4546 H HD23 . LEU   B 1 43  ? 46.439 -16.345 6.170   1.00 14.52 ?  43  LEU   B HD23 1 
ATOM   4547 N N    . LYS   B 1 44  ? 50.310 -18.280 8.623   1.00 11.54 ?  44  LYS   B N    1 
ATOM   4548 C CA   . LYS   B 1 44  ? 51.576 -18.957 8.858   1.00 12.31 ?  44  LYS   B CA   1 
ATOM   4549 C C    . LYS   B 1 44  ? 51.694 -20.074 7.831   1.00 11.85 ?  44  LYS   B C    1 
ATOM   4550 O O    . LYS   B 1 44  ? 50.996 -21.091 7.918   1.00 13.06 ?  44  LYS   B O    1 
ATOM   4551 C CB   . LYS   B 1 44  ? 51.644 -19.464 10.297  1.00 13.96 ?  44  LYS   B CB   1 
ATOM   4552 C CG   . LYS   B 1 44  ? 51.826 -18.346 11.310  1.00 16.91 ?  44  LYS   B CG   1 
ATOM   4553 C CD   . LYS   B 1 44  ? 53.055 -17.505 10.940  1.00 20.00 ?  44  LYS   B CD   1 
ATOM   4554 C CE   . LYS   B 1 44  ? 53.434 -16.500 11.996  1.00 22.81 ?  44  LYS   B CE   1 
ATOM   4555 N NZ   . LYS   B 1 44  ? 54.686 -15.777 11.647  1.00 24.13 ?  44  LYS   B NZ   1 
ATOM   4556 H H    . LYS   B 1 44  ? 49.637 -18.671 8.985   1.00 13.85 ?  44  LYS   B H    1 
ATOM   4557 H HA   . LYS   B 1 44  ? 52.304 -18.341 8.686   1.00 14.77 ?  44  LYS   B HA   1 
ATOM   4558 H HB2  . LYS   B 1 44  ? 50.815 -19.924 10.507  1.00 16.75 ?  44  LYS   B HB2  1 
ATOM   4559 H HB3  . LYS   B 1 44  ? 52.392 -20.071 10.381  1.00 16.75 ?  44  LYS   B HB3  1 
ATOM   4560 H HG2  . LYS   B 1 44  ? 51.047 -17.774 11.310  1.00 20.29 ?  44  LYS   B HG2  1 
ATOM   4561 H HG3  . LYS   B 1 44  ? 51.971 -18.731 12.192  1.00 20.29 ?  44  LYS   B HG3  1 
ATOM   4562 H HD2  . LYS   B 1 44  ? 53.809 -18.105 10.787  1.00 24.00 ?  44  LYS   B HD2  1 
ATOM   4563 H HD3  . LYS   B 1 44  ? 52.863 -17.008 10.130  1.00 24.00 ?  44  LYS   B HD3  1 
ATOM   4564 H HE2  . LYS   B 1 44  ? 52.721 -15.850 12.078  1.00 27.38 ?  44  LYS   B HE2  1 
ATOM   4565 H HE3  . LYS   B 1 44  ? 53.576 -16.961 12.831  1.00 27.38 ?  44  LYS   B HE3  1 
ATOM   4566 H HZ1  . LYS   B 1 44  ? 54.879 -15.183 12.281  1.00 28.95 ?  44  LYS   B HZ1  1 
ATOM   4567 H HZ2  . LYS   B 1 44  ? 55.362 -16.351 11.571  1.00 28.95 ?  44  LYS   B HZ2  1 
ATOM   4568 H HZ3  . LYS   B 1 44  ? 54.587 -15.346 10.872  1.00 28.95 ?  44  LYS   B HZ3  1 
ATOM   4569 N N    . HIS   B 1 45  ? 52.549 -19.857 6.834   1.00 11.67 ?  45  HIS   B N    1 
ATOM   4570 C CA   . HIS   B 1 45  ? 52.573 -20.685 5.630   1.00 11.88 ?  45  HIS   B CA   1 
ATOM   4571 C C    . HIS   B 1 45  ? 53.595 -21.807 5.789   1.00 14.19 ?  45  HIS   B C    1 
ATOM   4572 O O    . HIS   B 1 45  ? 54.653 -21.823 5.167   1.00 16.30 ?  45  HIS   B O    1 
ATOM   4573 C CB   . HIS   B 1 45  ? 52.885 -19.826 4.418   1.00 11.63 ?  45  HIS   B CB   1 
ATOM   4574 C CG   . HIS   B 1 45  ? 52.011 -18.624 4.309   1.00 11.44 ?  45  HIS   B CG   1 
ATOM   4575 N ND1  . HIS   B 1 45  ? 50.632 -18.701 4.267   1.00 11.95 ?  45  HIS   B ND1  1 
ATOM   4576 C CD2  . HIS   B 1 45  ? 52.328 -17.311 4.250   1.00 12.17 ?  45  HIS   B CD2  1 
ATOM   4577 C CE1  . HIS   B 1 45  ? 50.146 -17.475 4.166   1.00 11.81 ?  45  HIS   B CE1  1 
ATOM   4578 N NE2  . HIS   B 1 45  ? 51.152 -16.616 4.154   1.00 12.10 ?  45  HIS   B NE2  1 
ATOM   4579 H H    . HIS   B 1 45  ? 53.121 -19.217 6.825   1.00 14.00 ?  45  HIS   B H    1 
ATOM   4580 H HA   . HIS   B 1 45  ? 51.695 -21.084 5.497   1.00 14.26 ?  45  HIS   B HA   1 
ATOM   4581 H HB2  . HIS   B 1 45  ? 53.803 -19.526 4.470   1.00 13.95 ?  45  HIS   B HB2  1 
ATOM   4582 H HB3  . HIS   B 1 45  ? 52.759 -20.361 3.612   1.00 13.95 ?  45  HIS   B HB3  1 
ATOM   4583 H HD2  . HIS   B 1 45  ? 53.185 -16.948 4.268   1.00 14.61 ?  45  HIS   B HD2  1 
ATOM   4584 H HE1  . HIS   B 1 45  ? 49.245 -17.253 4.101   1.00 14.18 ?  45  HIS   B HE1  1 
ATOM   4585 H HE2  . HIS   B 1 45  ? 51.079 -15.760 4.104   1.00 14.52 ?  45  HIS   B HE2  1 
ATOM   4586 N N    A GLY   B 1 46  ? 53.236 -22.776 6.628   0.74 14.95 ?  46  GLY   B N    1 
ATOM   4587 N N    B GLY   B 1 46  ? 53.247 -22.761 6.645   0.26 14.90 ?  46  GLY   B N    1 
ATOM   4588 C CA   A GLY   B 1 46  ? 54.159 -23.830 7.005   0.74 16.56 ?  46  GLY   B CA   1 
ATOM   4589 C CA   B GLY   B 1 46  ? 54.167 -23.826 6.983   0.26 15.88 ?  46  GLY   B CA   1 
ATOM   4590 C C    A GLY   B 1 46  ? 54.217 -25.043 6.099   0.74 17.85 ?  46  GLY   B C    1 
ATOM   4591 C C    B GLY   B 1 46  ? 54.199 -24.966 5.985   0.26 16.76 ?  46  GLY   B C    1 
ATOM   4592 O O    A GLY   B 1 46  ? 55.300 -25.467 5.685   0.74 20.94 ?  46  GLY   B O    1 
ATOM   4593 O O    B GLY   B 1 46  ? 55.234 -25.233 5.366   0.26 17.44 ?  46  GLY   B O    1 
ATOM   4594 H H    A GLY   B 1 46  ? 52.461 -22.828 7.007   0.74 17.94 ?  46  GLY   B H    1 
ATOM   4595 H H    B GLY   B 1 46  ? 52.483 -22.806 7.044   0.26 17.88 ?  46  GLY   B H    1 
ATOM   4596 H HA2  A GLY   B 1 46  ? 55.050 -23.454 7.055   0.74 19.87 ?  46  GLY   B HA2  1 
ATOM   4597 H HA2  B GLY   B 1 46  ? 55.061 -23.458 7.044   0.26 19.06 ?  46  GLY   B HA2  1 
ATOM   4598 H HA3  A GLY   B 1 46  ? 53.919 -24.149 7.887   0.74 19.87 ?  46  GLY   B HA3  1 
ATOM   4599 H HA3  B GLY   B 1 46  ? 53.927 -24.181 7.854   0.26 19.06 ?  46  GLY   B HA3  1 
ATOM   4600 N N    . GLY   B 1 47  ? 53.061 -25.635 5.801   1.00 17.14 ?  47  GLY   B N    1 
ATOM   4601 C CA   . GLY   B 1 47  ? 53.008 -26.898 5.095   1.00 15.25 ?  47  GLY   B CA   1 
ATOM   4602 C C    . GLY   B 1 47  ? 52.074 -26.877 3.901   1.00 13.31 ?  47  GLY   B C    1 
ATOM   4603 O O    . GLY   B 1 47  ? 51.412 -25.878 3.617   1.00 13.32 ?  47  GLY   B O    1 
ATOM   4604 H H    A GLY   B 1 47  ? 52.289 -25.334 6.028   0.74 20.56 ?  47  GLY   B H    1 
ATOM   4605 H H    B GLY   B 1 47  ? 52.294 -25.365 6.080   0.26 20.56 ?  47  GLY   B H    1 
ATOM   4606 H HA2  . GLY   B 1 47  ? 53.897 -27.139 4.781   1.00 18.30 ?  47  GLY   B HA2  1 
ATOM   4607 H HA3  . GLY   B 1 47  ? 52.711 -27.595 5.705   1.00 18.30 ?  47  GLY   B HA3  1 
ATOM   4608 N N    . GLY   B 1 48  ? 52.027 -28.016 3.211   1.00 12.54 ?  48  GLY   B N    1 
ATOM   4609 C CA   . GLY   B 1 48  ? 51.100 -28.162 2.107   1.00 12.68 ?  48  GLY   B CA   1 
ATOM   4610 C C    . GLY   B 1 48  ? 51.242 -27.057 1.086   1.00 11.88 ?  48  GLY   B C    1 
ATOM   4611 O O    . GLY   B 1 48  ? 52.346 -26.596 0.770   1.00 12.54 ?  48  GLY   B O    1 
ATOM   4612 H H    . GLY   B 1 48  ? 52.531 -28.699 3.352   1.00 15.05 ?  48  GLY   B H    1 
ATOM   4613 H HA2  . GLY   B 1 48  ? 51.253 -29.016 1.667   1.00 15.22 ?  48  GLY   B HA2  1 
ATOM   4614 H HA3  . GLY   B 1 48  ? 50.193 -28.151 2.446   1.00 15.22 ?  48  GLY   B HA3  1 
ATOM   4615 N N    . VAL   B 1 49  ? 50.097 -26.625 0.557   1.00 11.87 ?  49  VAL   B N    1 
ATOM   4616 C CA   . VAL   B 1 49  ? 50.076 -25.608 -0.490  1.00 11.80 ?  49  VAL   B CA   1 
ATOM   4617 C C    . VAL   B 1 49  ? 50.730 -24.319 -0.009  1.00 10.71 ?  49  VAL   B C    1 
ATOM   4618 O O    . VAL   B 1 49  ? 51.517 -23.700 -0.733  1.00 11.43 ?  49  VAL   B O    1 
ATOM   4619 C CB   . VAL   B 1 49  ? 48.631 -25.361 -0.964  1.00 13.05 ?  49  VAL   B CB   1 
ATOM   4620 C CG1  . VAL   B 1 49  ? 48.551 -24.113 -1.840  1.00 13.13 ?  49  VAL   B CG1  1 
ATOM   4621 C CG2  . VAL   B 1 49  ? 48.089 -26.573 -1.707  1.00 14.58 ?  49  VAL   B CG2  1 
ATOM   4622 H H    . VAL   B 1 49  ? 49.315 -26.899 0.788   1.00 14.24 ?  49  VAL   B H    1 
ATOM   4623 H HA   . VAL   B 1 49  ? 50.579 -25.926 -1.255  1.00 14.16 ?  49  VAL   B HA   1 
ATOM   4624 H HB   . VAL   B 1 49  ? 48.064 -25.212 -0.191  1.00 15.67 ?  49  VAL   B HB   1 
ATOM   4625 H HG11 . VAL   B 1 49  ? 47.718 -24.130 -2.342  1.00 15.76 ?  49  VAL   B HG11 1 
ATOM   4626 H HG12 . VAL   B 1 49  ? 48.570 -23.323 -1.273  1.00 15.76 ?  49  VAL   B HG12 1 
ATOM   4627 H HG13 . VAL   B 1 49  ? 49.302 -24.104 -2.450  1.00 15.76 ?  49  VAL   B HG13 1 
ATOM   4628 H HG21 . VAL   B 1 49  ? 47.177 -26.393 -1.991  1.00 17.50 ?  49  VAL   B HG21 1 
ATOM   4629 H HG22 . VAL   B 1 49  ? 48.647 -26.743 -2.484  1.00 17.50 ?  49  VAL   B HG22 1 
ATOM   4630 H HG23 . VAL   B 1 49  ? 48.105 -27.339 -1.114  1.00 17.50 ?  49  VAL   B HG23 1 
ATOM   4631 N N    . ALA   B 1 50  ? 50.385 -23.872 1.201   1.00 10.97 ?  50  ALA   B N    1 
ATOM   4632 C CA   . ALA   B 1 50  ? 50.904 -22.594 1.680   1.00 10.57 ?  50  ALA   B CA   1 
ATOM   4633 C C    . ALA   B 1 50  ? 52.423 -22.621 1.786   1.00 10.92 ?  50  ALA   B C    1 
ATOM   4634 O O    . ALA   B 1 50  ? 53.100 -21.652 1.420   1.00 10.92 ?  50  ALA   B O    1 
ATOM   4635 C CB   . ALA   B 1 50  ? 50.281 -22.245 3.029   1.00 11.10 ?  50  ALA   B CB   1 
ATOM   4636 H H    . ALA   B 1 50  ? 49.867 -24.282 1.750   1.00 13.17 ?  50  ALA   B H    1 
ATOM   4637 H HA   . ALA   B 1 50  ? 50.668 -21.897 1.056   1.00 12.69 ?  50  ALA   B HA   1 
ATOM   4638 H HB1  . ALA   B 1 50  ? 50.635 -21.394 3.335   1.00 13.32 ?  50  ALA   B HB1  1 
ATOM   4639 H HB2  . ALA   B 1 50  ? 49.317 -22.182 2.927   1.00 13.32 ?  50  ALA   B HB2  1 
ATOM   4640 H HB3  . ALA   B 1 50  ? 50.498 -22.940 3.672   1.00 13.32 ?  50  ALA   B HB3  1 
ATOM   4641 N N    . GLY   B 1 51  ? 52.979 -23.713 2.306   1.00 11.54 ?  51  GLY   B N    1 
ATOM   4642 C CA   . GLY   B 1 51  ? 54.424 -23.818 2.377   1.00 12.02 ?  51  GLY   B CA   1 
ATOM   4643 C C    . GLY   B 1 51  ? 55.072 -23.764 1.008   1.00 12.05 ?  51  GLY   B C    1 
ATOM   4644 O O    . GLY   B 1 51  ? 56.113 -23.128 0.827   1.00 13.00 ?  51  GLY   B O    1 
ATOM   4645 H H    . GLY   B 1 51  ? 52.552 -24.393 2.617   1.00 13.85 ?  51  GLY   B H    1 
ATOM   4646 H HA2  . GLY   B 1 51  ? 54.777 -23.088 2.913   1.00 14.42 ?  51  GLY   B HA2  1 
ATOM   4647 H HA3  . GLY   B 1 51  ? 54.671 -24.655 2.800   1.00 14.42 ?  51  GLY   B HA3  1 
ATOM   4648 N N    . ALA   B 1 52  ? 54.468 -24.429 0.024   1.00 11.90 ?  52  ALA   B N    1 
ATOM   4649 C CA   . ALA   B 1 52  ? 55.030 -24.436 -1.320  1.00 12.06 ?  52  ALA   B CA   1 
ATOM   4650 C C    . ALA   B 1 52  ? 54.953 -23.058 -1.969  1.00 11.60 ?  52  ALA   B C    1 
ATOM   4651 O O    . ALA   B 1 52  ? 55.919 -22.607 -2.604  1.00 12.28 ?  52  ALA   B O    1 
ATOM   4652 C CB   . ALA   B 1 52  ? 54.312 -25.470 -2.180  1.00 12.89 ?  52  ALA   B CB   1 
ATOM   4653 H H    . ALA   B 1 52  ? 53.737 -24.873 0.112   1.00 14.29 ?  52  ALA   B H    1 
ATOM   4654 H HA   . ALA   B 1 52  ? 55.961 -24.686 -1.265  1.00 14.47 ?  52  ALA   B HA   1 
ATOM   4655 H HB1  . ALA   B 1 52  ? 54.701 -25.461 -3.070  1.00 15.47 ?  52  ALA   B HB1  1 
ATOM   4656 H HB2  . ALA   B 1 52  ? 54.428 -26.347 -1.780  1.00 15.47 ?  52  ALA   B HB2  1 
ATOM   4657 H HB3  . ALA   B 1 52  ? 53.371 -25.249 -2.227  1.00 15.47 ?  52  ALA   B HB3  1 
ATOM   4658 N N    . LEU   B 1 53  ? 53.806 -22.385 -1.851  1.00 11.04 ?  53  LEU   B N    1 
ATOM   4659 C CA   . LEU   B 1 53  ? 53.692 -21.044 -2.416  1.00 11.33 ?  53  LEU   B CA   1 
ATOM   4660 C C    . LEU   B 1 53  ? 54.697 -20.103 -1.768  1.00 11.28 ?  53  LEU   B C    1 
ATOM   4661 O O    . LEU   B 1 53  ? 55.402 -19.357 -2.455  1.00 11.98 ?  53  LEU   B O    1 
ATOM   4662 C CB   . LEU   B 1 53  ? 52.265 -20.509 -2.246  1.00 11.78 ?  53  LEU   B CB   1 
ATOM   4663 C CG   . LEU   B 1 53  ? 51.132 -21.222 -2.997  1.00 12.08 ?  53  LEU   B CG   1 
ATOM   4664 C CD1  . LEU   B 1 53  ? 49.785 -20.630 -2.628  1.00 13.87 ?  53  LEU   B CD1  1 
ATOM   4665 C CD2  . LEU   B 1 53  ? 51.343 -21.179 -4.511  1.00 14.01 ?  53  LEU   B CD2  1 
ATOM   4666 H H    . LEU   B 1 53  ? 53.098 -22.673 -1.456  1.00 13.25 ?  53  LEU   B H    1 
ATOM   4667 H HA   . LEU   B 1 53  ? 53.886 -21.084 -3.367  1.00 13.59 ?  53  LEU   B HA   1 
ATOM   4668 H HB2  . LEU   B 1 53  ? 52.041 -20.547 -1.305  1.00 14.14 ?  53  LEU   B HB2  1 
ATOM   4669 H HB3  . LEU   B 1 53  ? 52.255 -19.584 -2.539  1.00 14.14 ?  53  LEU   B HB3  1 
ATOM   4670 H HG   . LEU   B 1 53  ? 51.122 -22.152 -2.731  1.00 14.50 ?  53  LEU   B HG   1 
ATOM   4671 H HD11 . LEU   B 1 53  ? 49.089 -21.102 -3.115  1.00 16.64 ?  53  LEU   B HD11 1 
ATOM   4672 H HD12 . LEU   B 1 53  ? 49.646 -20.737 -1.673  1.00 16.64 ?  53  LEU   B HD12 1 
ATOM   4673 H HD13 . LEU   B 1 53  ? 49.774 -19.691 -2.861  1.00 16.64 ?  53  LEU   B HD13 1 
ATOM   4674 H HD21 . LEU   B 1 53  ? 50.636 -21.685 -4.943  1.00 16.81 ?  53  LEU   B HD21 1 
ATOM   4675 H HD22 . LEU   B 1 53  ? 51.314 -20.256 -4.810  1.00 16.81 ?  53  LEU   B HD22 1 
ATOM   4676 H HD23 . LEU   B 1 53  ? 52.204 -21.569 -4.725  1.00 16.81 ?  53  LEU   B HD23 1 
ATOM   4677 N N    . ASN   B 1 54  ? 54.786 -20.132 -0.440  1.00 11.13 ?  54  ASN   B N    1 
ATOM   4678 C CA   . ASN   B 1 54  ? 55.698 -19.222 0.236   1.00 11.82 ?  54  ASN   B CA   1 
ATOM   4679 C C    . ASN   B 1 54  ? 57.141 -19.496 -0.161  1.00 12.19 ?  54  ASN   B C    1 
ATOM   4680 O O    . ASN   B 1 54  ? 57.915 -18.558 -0.390  1.00 12.38 ?  54  ASN   B O    1 
ATOM   4681 C CB   . ASN   B 1 54  ? 55.534 -19.304 1.745   1.00 12.45 ?  54  ASN   B CB   1 
ATOM   4682 C CG   . ASN   B 1 54  ? 56.511 -18.397 2.458   1.00 12.31 ?  54  ASN   B CG   1 
ATOM   4683 O OD1  . ASN   B 1 54  ? 56.534 -17.188 2.214   1.00 12.66 ?  54  ASN   B OD1  1 
ATOM   4684 N ND2  . ASN   B 1 54  ? 57.353 -18.972 3.307   1.00 13.79 ?  54  ASN   B ND2  1 
ATOM   4685 H H    . ASN   B 1 54  ? 54.336 -20.651 0.075   1.00 13.36 ?  54  ASN   B H    1 
ATOM   4686 H HA   . ASN   B 1 54  ? 55.485 -18.312 -0.038  1.00 14.18 ?  54  ASN   B HA   1 
ATOM   4687 H HB2  . ASN   B 1 54  ? 54.631 -19.027 1.981   1.00 14.94 ?  54  ASN   B HB2  1 
ATOM   4688 H HB3  . ASN   B 1 54  ? 55.692 -20.213 2.033   1.00 14.94 ?  54  ASN   B HB3  1 
ATOM   4689 H HD21 . ASN   B 1 54  ? 57.931 -18.496 3.730   1.00 16.54 ?  54  ASN   B HD21 1 
ATOM   4690 H HD22 . ASN   B 1 54  ? 57.316 -19.821 3.440   1.00 16.54 ?  54  ASN   B HD22 1 
ATOM   4691 N N    . LYS   B 1 55  ? 57.526 -20.773 -0.244  1.00 12.72 ?  55  LYS   B N    1 
ATOM   4692 C CA   . LYS   B 1 55  ? 58.883 -21.112 -0.658  1.00 13.60 ?  55  LYS   B CA   1 
ATOM   4693 C C    . LYS   B 1 55  ? 59.188 -20.567 -2.047  1.00 13.42 ?  55  LYS   B C    1 
ATOM   4694 O O    . LYS   B 1 55  ? 60.291 -20.065 -2.297  1.00 13.87 ?  55  LYS   B O    1 
ATOM   4695 C CB   . LYS   B 1 55  ? 59.074 -22.627 -0.619  1.00 15.14 ?  55  LYS   B CB   1 
ATOM   4696 C CG   . LYS   B 1 55  ? 60.465 -23.087 -1.006  1.00 18.98 ?  55  LYS   B CG   1 
ATOM   4697 C CD   . LYS   B 1 55  ? 60.631 -24.586 -0.824  1.00 22.52 ?  55  LYS   B CD   1 
ATOM   4698 C CE   . LYS   B 1 55  ? 60.676 -24.978 0.650   1.00 25.69 ?  55  LYS   B CE   1 
ATOM   4699 N NZ   . LYS   B 1 55  ? 61.066 -26.397 0.836   1.00 27.20 ?  55  LYS   B NZ   1 
ATOM   4700 H H    . LYS   B 1 55  ? 57.022 -21.448 -0.072  1.00 15.26 ?  55  LYS   B H    1 
ATOM   4701 H HA   . LYS   B 1 55  ? 59.510 -20.713 -0.040  1.00 16.32 ?  55  LYS   B HA   1 
ATOM   4702 H HB2  . LYS   B 1 55  ? 58.896 -22.935 0.282   1.00 18.17 ?  55  LYS   B HB2  1 
ATOM   4703 H HB3  . LYS   B 1 55  ? 58.445 -23.037 -1.235  1.00 18.17 ?  55  LYS   B HB3  1 
ATOM   4704 H HG2  . LYS   B 1 55  ? 60.624 -22.878 -1.940  1.00 22.78 ?  55  LYS   B HG2  1 
ATOM   4705 H HG3  . LYS   B 1 55  ? 61.116 -22.638 -0.445  1.00 22.78 ?  55  LYS   B HG3  1 
ATOM   4706 H HD2  . LYS   B 1 55  ? 59.883 -25.046 -1.235  1.00 27.03 ?  55  LYS   B HD2  1 
ATOM   4707 H HD3  . LYS   B 1 55  ? 61.464 -24.869 -1.234  1.00 27.03 ?  55  LYS   B HD3  1 
ATOM   4708 H HE2  . LYS   B 1 55  ? 61.325 -24.415 1.106   1.00 30.83 ?  55  LYS   B HE2  1 
ATOM   4709 H HE3  . LYS   B 1 55  ? 59.795 -24.846 1.038   1.00 30.83 ?  55  LYS   B HE3  1 
ATOM   4710 H HZ1  . LYS   B 1 55  ? 61.026 -26.610 1.699   1.00 32.65 ?  55  LYS   B HZ1  1 
ATOM   4711 H HZ2  . LYS   B 1 55  ? 60.510 -26.922 0.381   1.00 32.65 ?  55  LYS   B HZ2  1 
ATOM   4712 H HZ3  . LYS   B 1 55  ? 61.894 -26.524 0.541   1.00 32.65 ?  55  LYS   B HZ3  1 
ATOM   4713 N N    . ALA   B 1 56  ? 58.222 -20.654 -2.966  1.00 12.84 ?  56  ALA   B N    1 
ATOM   4714 C CA   . ALA   B 1 56  ? 58.442 -20.148 -4.315  1.00 13.63 ?  56  ALA   B CA   1 
ATOM   4715 C C    . ALA   B 1 56  ? 58.710 -18.652 -4.309  1.00 13.31 ?  56  ALA   B C    1 
ATOM   4716 O O    . ALA   B 1 56  ? 59.435 -18.149 -5.178  1.00 14.34 ?  56  ALA   B O    1 
ATOM   4717 C CB   . ALA   B 1 56  ? 57.246 -20.475 -5.211  1.00 14.64 ?  56  ALA   B CB   1 
ATOM   4718 H H    . ALA   B 1 56  ? 57.435 -20.981 -2.836  1.00 15.41 ?  56  ALA   B H    1 
ATOM   4719 H HA   . ALA   B 1 56  ? 59.220 -20.577 -4.692  1.00 16.36 ?  56  ALA   B HA   1 
ATOM   4720 H HB1  . ALA   B 1 56  ? 57.417 -20.134 -6.108  1.00 17.57 ?  56  ALA   B HB1  1 
ATOM   4721 H HB2  . ALA   B 1 56  ? 57.132 -21.436 -5.244  1.00 17.57 ?  56  ALA   B HB2  1 
ATOM   4722 H HB3  . ALA   B 1 56  ? 56.450 -20.056 -4.850  1.00 17.57 ?  56  ALA   B HB3  1 
ATOM   4723 N N    . THR   B 1 57  ? 58.147 -17.926 -3.339  1.00 13.04 ?  57  THR   B N    1 
ATOM   4724 C CA   . THR   B 1 57  ? 58.377 -16.492 -3.210  1.00 13.01 ?  57  THR   B CA   1 
ATOM   4725 C C    . THR   B 1 57  ? 59.629 -16.161 -2.402  1.00 13.64 ?  57  THR   B C    1 
ATOM   4726 O O    . THR   B 1 57  ? 59.864 -14.981 -2.103  1.00 14.24 ?  57  THR   B O    1 
ATOM   4727 C CB   . THR   B 1 57  ? 57.175 -15.766 -2.578  1.00 12.59 ?  57  THR   B CB   1 
ATOM   4728 O OG1  . THR   B 1 57  ? 57.151 -15.975 -1.159  1.00 12.74 ?  57  THR   B OG1  1 
ATOM   4729 C CG2  . THR   B 1 57  ? 55.857 -16.197 -3.206  1.00 12.46 ?  57  THR   B CG2  1 
ATOM   4730 H H    . THR   B 1 57  ? 57.614 -18.243 -2.742  1.00 15.65 ?  57  THR   B H    1 
ATOM   4731 H HA   . THR   B 1 57  ? 58.497 -16.119 -4.098  1.00 15.62 ?  57  THR   B HA   1 
ATOM   4732 H HB   . THR   B 1 57  ? 57.271 -14.814 -2.743  1.00 15.11 ?  57  THR   B HB   1 
ATOM   4733 H HG1  . THR   B 1 57  ? 57.088 -16.795 -0.988  1.00 15.29 ?  57  THR   B HG1  1 
ATOM   4734 H HG21 . THR   B 1 57  ? 55.130 -15.654 -2.868  1.00 14.95 ?  57  THR   B HG21 1 
ATOM   4735 H HG22 . THR   B 1 57  ? 55.901 -16.105 -4.170  1.00 14.95 ?  57  THR   B HG22 1 
ATOM   4736 H HG23 . THR   B 1 57  ? 55.676 -17.128 -2.992  1.00 14.95 ?  57  THR   B HG23 1 
ATOM   4737 N N    . ASN   B 1 58  ? 60.427 -17.164 -2.038  1.00 14.32 ?  58  ASN   B N    1 
ATOM   4738 C CA   . ASN   B 1 58  ? 61.624 -16.947 -1.230  1.00 17.37 ?  58  ASN   B CA   1 
ATOM   4739 C C    . ASN   B 1 58  ? 61.281 -16.224 0.073   1.00 15.36 ?  58  ASN   B C    1 
ATOM   4740 O O    . ASN   B 1 58  ? 62.013 -15.341 0.533   1.00 16.09 ?  58  ASN   B O    1 
ATOM   4741 C CB   . ASN   B 1 58  ? 62.716 -16.212 -2.013  1.00 25.26 ?  58  ASN   B CB   1 
ATOM   4742 C CG   . ASN   B 1 58  ? 64.079 -16.323 -1.357  1.00 33.85 ?  58  ASN   B CG   1 
ATOM   4743 O OD1  . ASN   B 1 58  ? 64.383 -17.317 -0.697  1.00 36.42 ?  58  ASN   B OD1  1 
ATOM   4744 N ND2  . ASN   B 1 58  ? 64.908 -15.300 -1.535  1.00 39.11 ?  58  ASN   B ND2  1 
ATOM   4745 H H    . ASN   B 1 58  ? 60.288 -17.993 -2.239  1.00 17.18 ?  58  ASN   B H    1 
ATOM   4746 H HA   . ASN   B 1 58  ? 61.985 -17.821 -0.995  1.00 20.85 ?  58  ASN   B HA   1 
ATOM   4747 H HB2  . ASN   B 1 58  ? 62.778 -16.594 -2.905  1.00 30.32 ?  58  ASN   B HB2  1 
ATOM   4748 H HB3  . ASN   B 1 58  ? 62.487 -15.274 -2.068  1.00 30.32 ?  58  ASN   B HB3  1 
ATOM   4749 H HD21 . ASN   B 1 58  ? 65.694 -15.315 -1.185  1.00 46.93 ?  58  ASN   B HD21 1 
ATOM   4750 H HD22 . ASN   B 1 58  ? 64.659 -14.621 -2.000  1.00 46.93 ?  58  ASN   B HD22 1 
ATOM   4751 N N    . ASN   B 1 59  ? 60.158 -16.615 0.680   1.00 14.26 ?  59  ASN   B N    1 
ATOM   4752 C CA   . ASN   B 1 59  ? 59.676 -16.144 1.979   1.00 14.19 ?  59  ASN   B CA   1 
ATOM   4753 C C    . ASN   B 1 59  ? 59.080 -14.739 1.925   1.00 13.54 ?  59  ASN   B C    1 
ATOM   4754 O O    . ASN   B 1 59  ? 58.641 -14.237 2.966   1.00 13.81 ?  59  ASN   B O    1 
ATOM   4755 C CB   . ASN   B 1 59  ? 60.746 -16.200 3.085   1.00 15.33 ?  59  ASN   B CB   1 
ATOM   4756 C CG   . ASN   B 1 59  ? 60.155 -16.385 4.463   1.00 16.51 ?  59  ASN   B CG   1 
ATOM   4757 O OD1  . ASN   B 1 59  ? 59.328 -17.276 4.681   1.00 16.72 ?  59  ASN   B OD1  1 
ATOM   4758 N ND2  . ASN   B 1 59  ? 60.574 -15.544 5.406   1.00 17.18 ?  59  ASN   B ND2  1 
ATOM   4759 H H    . ASN   B 1 59  ? 59.623 -17.198 0.335   1.00 17.11 ?  59  ASN   B H    1 
ATOM   4760 H HA   . ASN   B 1 59  ? 58.969 -16.744 2.260   1.00 17.02 ?  59  ASN   B HA   1 
ATOM   4761 H HB2  . ASN   B 1 59  ? 61.343 -16.949 2.922   1.00 18.39 ?  59  ASN   B HB2  1 
ATOM   4762 H HB3  . ASN   B 1 59  ? 61.248 -15.371 3.089   1.00 18.39 ?  59  ASN   B HB3  1 
ATOM   4763 H HD21 . ASN   B 1 59  ? 60.265 -15.606 6.209   1.00 20.62 ?  59  ASN   B HD21 1 
ATOM   4764 H HD22 . ASN   B 1 59  ? 61.149 -14.934 5.217   1.00 20.62 ?  59  ASN   B HD22 1 
ATOM   4765 N N    . ALA   B 1 60  ? 59.023 -14.095 0.757   1.00 13.39 ?  60  ALA   B N    1 
ATOM   4766 C CA   . ALA   B 1 60  ? 58.420 -12.766 0.686   1.00 13.39 ?  60  ALA   B CA   1 
ATOM   4767 C C    . ALA   B 1 60  ? 56.950 -12.796 1.085   1.00 12.46 ?  60  ALA   B C    1 
ATOM   4768 O O    . ALA   B 1 60  ? 56.440 -11.847 1.696   1.00 13.07 ?  60  ALA   B O    1 
ATOM   4769 C CB   . ALA   B 1 60  ? 58.585 -12.184 -0.717  1.00 14.45 ?  60  ALA   B CB   1 
ATOM   4770 H H    . ALA   B 1 60  ? 59.327 -14.398 0.015   1.00 16.07 ?  60  ALA   B H    1 
ATOM   4771 H HA   . ALA   B 1 60  ? 58.879 -12.184 1.311   1.00 16.07 ?  60  ALA   B HA   1 
ATOM   4772 H HB1  . ALA   B 1 60  ? 58.181 -11.305 -0.741  1.00 17.34 ?  60  ALA   B HB1  1 
ATOM   4773 H HB2  . ALA   B 1 60  ? 59.535 -12.118 -0.917  1.00 17.34 ?  60  ALA   B HB2  1 
ATOM   4774 H HB3  . ALA   B 1 60  ? 58.154 -12.770 -1.355  1.00 17.34 ?  60  ALA   B HB3  1 
ATOM   4775 N N    . MET   B 1 61  ? 56.245 -13.872 0.737   1.00 11.96 ?  61  MET   B N    1 
ATOM   4776 C CA   . MET   B 1 61  ? 54.848 -13.994 1.134   1.00 11.96 ?  61  MET   B CA   1 
ATOM   4777 C C    . MET   B 1 61  ? 54.710 -13.998 2.655   1.00 11.96 ?  61  MET   B C    1 
ATOM   4778 O O    . MET   B 1 61  ? 53.808 -13.354 3.208   1.00 11.74 ?  61  MET   B O    1 
ATOM   4779 C CB   . MET   B 1 61  ? 54.267 -15.266 0.506   1.00 11.83 ?  61  MET   B CB   1 
ATOM   4780 C CG   . MET   B 1 61  ? 52.825 -15.565 0.918   1.00 11.51 ?  61  MET   B CG   1 
ATOM   4781 S SD   . MET   B 1 61  ? 52.193 -17.074 0.160   1.00 12.33 ?  61  MET   B SD   1 
ATOM   4782 C CE   . MET   B 1 61  ? 51.941 -16.507 -1.523  1.00 13.55 ?  61  MET   B CE   1 
ATOM   4783 H H    . MET   B 1 61  ? 56.545 -14.538 0.276   1.00 14.35 ?  61  MET   B H    1 
ATOM   4784 H HA   . MET   B 1 61  ? 54.350 -13.245 0.772   1.00 14.35 ?  61  MET   B HA   1 
ATOM   4785 H HB2  . MET   B 1 61  ? 54.279 -15.176 -0.462  1.00 14.20 ?  61  MET   B HB2  1 
ATOM   4786 H HB3  . MET   B 1 61  ? 54.809 -16.025 0.769   1.00 14.20 ?  61  MET   B HB3  1 
ATOM   4787 H HG2  . MET   B 1 61  ? 52.781 -15.680 1.882   1.00 13.81 ?  61  MET   B HG2  1 
ATOM   4788 H HG3  . MET   B 1 61  ? 52.253 -14.829 0.646   1.00 13.81 ?  61  MET   B HG3  1 
ATOM   4789 H HE1  . MET   B 1 61  ? 51.567 -17.233 -2.048  1.00 16.27 ?  61  MET   B HE1  1 
ATOM   4790 H HE2  . MET   B 1 61  ? 51.329 -15.755 -1.515  1.00 16.27 ?  61  MET   B HE2  1 
ATOM   4791 H HE3  . MET   B 1 61  ? 52.794 -16.235 -1.897  1.00 16.27 ?  61  MET   B HE3  1 
ATOM   4792 N N    . GLN   B 1 62  ? 55.589 -14.722 3.353   1.00 11.65 ?  62  GLN   B N    1 
ATOM   4793 C CA   . GLN   B 1 62  ? 55.487 -14.784 4.807   1.00 11.96 ?  62  GLN   B CA   1 
ATOM   4794 C C    . GLN   B 1 62  ? 55.771 -13.432 5.446   1.00 12.44 ?  62  GLN   B C    1 
ATOM   4795 O O    . GLN   B 1 62  ? 55.085 -13.037 6.395   1.00 12.76 ?  62  GLN   B O    1 
ATOM   4796 C CB   . GLN   B 1 62  ? 56.440 -15.838 5.368   1.00 12.47 ?  62  GLN   B CB   1 
ATOM   4797 C CG   . GLN   B 1 62  ? 56.216 -16.103 6.849   1.00 12.66 ?  62  GLN   B CG   1 
ATOM   4798 C CD   . GLN   B 1 62  ? 54.844 -16.701 7.096   1.00 12.31 ?  62  GLN   B CD   1 
ATOM   4799 O OE1  . GLN   B 1 62  ? 54.593 -17.856 6.747   1.00 12.70 ?  62  GLN   B OE1  1 
ATOM   4800 N NE2  . GLN   B 1 62  ? 53.932 -15.909 7.653   1.00 12.84 ?  62  GLN   B NE2  1 
ATOM   4801 H H    . GLN   B 1 62  ? 56.232 -15.182 3.008   1.00 13.98 ?  62  GLN   B H    1 
ATOM   4802 H HA   . GLN   B 1 62  ? 54.581 -15.040 5.038   1.00 14.35 ?  62  GLN   B HA   1 
ATOM   4803 H HB2  . GLN   B 1 62  ? 56.307 -16.671 4.890   1.00 14.96 ?  62  GLN   B HB2  1 
ATOM   4804 H HB3  . GLN   B 1 62  ? 57.353 -15.529 5.249   1.00 14.96 ?  62  GLN   B HB3  1 
ATOM   4805 H HG2  . GLN   B 1 62  ? 56.887 -16.729 7.159   1.00 15.19 ?  62  GLN   B HG2  1 
ATOM   4806 H HG3  . GLN   B 1 62  ? 56.284 -15.267 7.336   1.00 15.19 ?  62  GLN   B HG3  1 
ATOM   4807 H HE21 . GLN   B 1 62  ? 54.141 -15.103 7.871   1.00 15.41 ?  62  GLN   B HE21 1 
ATOM   4808 H HE22 . GLN   B 1 62  ? 53.143 -16.207 7.800   1.00 15.41 ?  62  GLN   B HE22 1 
ATOM   4809 N N    . VAL   B 1 63  ? 56.781 -12.714 4.955   1.00 13.02 ?  63  VAL   B N    1 
ATOM   4810 C CA   . VAL   B 1 63  ? 57.081 -11.400 5.517   1.00 13.58 ?  63  VAL   B CA   1 
ATOM   4811 C C    . VAL   B 1 63  ? 55.887 -10.468 5.339   1.00 13.21 ?  63  VAL   B C    1 
ATOM   4812 O O    . VAL   B 1 63  ? 55.472 -9.768  6.274   1.00 13.81 ?  63  VAL   B O    1 
ATOM   4813 C CB   . VAL   B 1 63  ? 58.371 -10.836 4.898   1.00 15.04 ?  63  VAL   B CB   1 
ATOM   4814 C CG1  . VAL   B 1 63  ? 58.601 -9.407  5.363   1.00 15.75 ?  63  VAL   B CG1  1 
ATOM   4815 C CG2  . VAL   B 1 63  ? 59.557 -11.716 5.276   1.00 15.80 ?  63  VAL   B CG2  1 
ATOM   4816 H H    . VAL   B 1 63  ? 57.294 -12.959 4.307   1.00 15.63 ?  63  VAL   B H    1 
ATOM   4817 H HA   . VAL   B 1 63  ? 57.235 -11.499 6.465   1.00 16.30 ?  63  VAL   B HA   1 
ATOM   4818 H HB   . VAL   B 1 63  ? 58.298 -10.834 3.931   1.00 18.05 ?  63  VAL   B HB   1 
ATOM   4819 H HG11 . VAL   B 1 63  ? 59.520 -9.156  5.176   1.00 18.90 ?  63  VAL   B HG11 1 
ATOM   4820 H HG12 . VAL   B 1 63  ? 57.995 -8.818  4.891   1.00 18.90 ?  63  VAL   B HG12 1 
ATOM   4821 H HG13 . VAL   B 1 63  ? 58.437 -9.357  6.320   1.00 18.90 ?  63  VAL   B HG13 1 
ATOM   4822 H HG21 . VAL   B 1 63  ? 60.369 -11.336 4.904   1.00 18.96 ?  63  VAL   B HG21 1 
ATOM   4823 H HG22 . VAL   B 1 63  ? 59.627 -11.751 6.246   1.00 18.96 ?  63  VAL   B HG22 1 
ATOM   4824 H HG23 . VAL   B 1 63  ? 59.417 -12.608 4.925   1.00 18.96 ?  63  VAL   B HG23 1 
ATOM   4825 N N    . GLU   B 1 64  ? 55.321 -10.447 4.131   1.00 12.85 ?  64  GLU   B N    1 
ATOM   4826 C CA   . GLU   B 1 64  ? 54.153 -9.610  3.863   1.00 12.33 ?  64  GLU   B CA   1 
ATOM   4827 C C    . GLU   B 1 64  ? 52.973 -10.018 4.740   1.00 11.95 ?  64  GLU   B C    1 
ATOM   4828 O O    . GLU   B 1 64  ? 52.221 -9.163  5.239   1.00 12.66 ?  64  GLU   B O    1 
ATOM   4829 C CB   . GLU   B 1 64  ? 53.798 -9.748  2.383   1.00 12.63 ?  64  GLU   B CB   1 
ATOM   4830 C CG   . GLU   B 1 64  ? 52.538 -9.020  1.954   1.00 12.91 ?  64  GLU   B CG   1 
ATOM   4831 C CD   . GLU   B 1 64  ? 52.005 -9.517  0.615   1.00 13.84 ?  64  GLU   B CD   1 
ATOM   4832 O OE1  . GLU   B 1 64  ? 52.177 -10.726 0.294   1.00 14.58 ?  64  GLU   B OE1  1 
ATOM   4833 O OE2  . GLU   B 1 64  ? 51.386 -8.701  -0.112  1.00 14.82 -1 64  GLU   B OE2  1 
ATOM   4834 H H    . GLU   B 1 64  ? 55.598 -10.900 3.449   1.00 15.41 ?  64  GLU   B H    1 
ATOM   4835 H HA   . GLU   B 1 64  ? 54.370 -8.683  4.043   1.00 14.80 ?  64  GLU   B HA   1 
ATOM   4836 H HB2  . GLU   B 1 64  ? 54.530 -9.388  1.851   1.00 15.15 ?  64  GLU   B HB2  1 
ATOM   4837 H HB3  . GLU   B 1 64  ? 53.679 -10.684 2.177   1.00 15.15 ?  64  GLU   B HB3  1 
ATOM   4838 H HG2  . GLU   B 1 64  ? 51.838 -9.153  2.614   1.00 15.49 ?  64  GLU   B HG2  1 
ATOM   4839 H HG3  . GLU   B 1 64  ? 52.730 -8.072  1.868   1.00 15.49 ?  64  GLU   B HG3  1 
ATOM   4840 N N    . SER   B 1 65  ? 52.792 -11.326 4.923   1.00 11.90 ?  65  SER   B N    1 
ATOM   4841 C CA   . SER   B 1 65  ? 51.685 -11.837 5.723   1.00 11.99 ?  65  SER   B CA   1 
ATOM   4842 C C    . SER   B 1 65  ? 51.822 -11.441 7.186   1.00 12.13 ?  65  SER   B C    1 
ATOM   4843 O O    . SER   B 1 65  ? 50.825 -11.075 7.826   1.00 12.38 ?  65  SER   B O    1 
ATOM   4844 C CB   . SER   B 1 65  ? 51.606 -13.356 5.590   1.00 11.88 ?  65  SER   B CB   1 
ATOM   4845 O OG   . SER   B 1 65  ? 51.256 -13.756 4.271   1.00 12.41 ?  65  SER   B OG   1 
ATOM   4846 H H    . SER   B 1 65  ? 53.299 -11.946 4.595   1.00 14.28 ?  65  SER   B H    1 
ATOM   4847 H HA   . SER   B 1 65  ? 50.854 -11.464 5.388   1.00 14.39 ?  65  SER   B HA   1 
ATOM   4848 H HB2  . SER   B 1 65  ? 52.465 -13.738 5.809   1.00 14.25 ?  65  SER   B HB2  1 
ATOM   4849 H HB3  . SER   B 1 65  ? 50.929 -13.688 6.205   1.00 14.25 ?  65  SER   B HB3  1 
ATOM   4850 H HG   . SER   B 1 65  ? 51.825 -13.463 3.720   1.00 14.89 ?  65  SER   B HG   1 
ATOM   4851 N N    . ASP   B 1 66  ? 53.031 -11.543 7.747   1.00 12.47 ?  66  ASP   B N    1 
ATOM   4852 C CA   . ASP   B 1 66  ? 53.219 -11.154 9.142   1.00 12.72 ?  66  ASP   B CA   1 
ATOM   4853 C C    . ASP   B 1 66  ? 52.901 -9.678  9.346   1.00 12.82 ?  66  ASP   B C    1 
ATOM   4854 O O    . ASP   B 1 66  ? 52.325 -9.292  10.371  1.00 13.35 ?  66  ASP   B O    1 
ATOM   4855 C CB   . ASP   B 1 66  ? 54.651 -11.460 9.583   1.00 14.32 ?  66  ASP   B CB   1 
ATOM   4856 C CG   . ASP   B 1 66  ? 54.920 -12.948 9.735   1.00 16.32 ?  66  ASP   B CG   1 
ATOM   4857 O OD1  . ASP   B 1 66  ? 53.973 -13.762 9.663   1.00 17.03 ?  66  ASP   B OD1  1 
ATOM   4858 O OD2  . ASP   B 1 66  ? 56.097 -13.308 9.941   1.00 18.74 -1 66  ASP   B OD2  1 
ATOM   4859 H H    . ASP   B 1 66  ? 53.736 -11.843 7.355   1.00 14.97 ?  66  ASP   B H    1 
ATOM   4860 H HA   . ASP   B 1 66  ? 52.622 -11.666 9.704   1.00 15.26 ?  66  ASP   B HA   1 
ATOM   4861 H HB2  . ASP   B 1 66  ? 55.273 -11.120 8.921   1.00 17.18 ?  66  ASP   B HB2  1 
ATOM   4862 H HB3  . ASP   B 1 66  ? 54.820 -11.037 10.442  1.00 17.18 ?  66  ASP   B HB3  1 
ATOM   4863 N N    . ASP   B 1 67  ? 53.275 -8.831  8.384   1.00 12.63 ?  67  ASP   B N    1 
ATOM   4864 C CA   . ASP   B 1 67  ? 52.929 -7.418  8.478   1.00 13.14 ?  67  ASP   B CA   1 
ATOM   4865 C C    . ASP   B 1 67  ? 51.417 -7.211  8.397   1.00 13.44 ?  67  ASP   B C    1 
ATOM   4866 O O    . ASP   B 1 67  ? 50.855 -6.403  9.144   1.00 13.98 ?  67  ASP   B O    1 
ATOM   4867 C CB   . ASP   B 1 67  ? 53.641 -6.643  7.378   1.00 14.54 ?  67  ASP   B CB   1 
ATOM   4868 C CG   . ASP   B 1 67  ? 53.217 -5.202  7.346   1.00 15.86 ?  67  ASP   B CG   1 
ATOM   4869 O OD1  . ASP   B 1 67  ? 53.722 -4.397  8.166   1.00 16.98 ?  67  ASP   B OD1  1 
ATOM   4870 O OD2  . ASP   B 1 67  ? 52.344 -4.888  6.520   1.00 16.92 -1 67  ASP   B OD2  1 
ATOM   4871 H H    . ASP   B 1 67  ? 53.730 -9.045  7.685   1.00 15.16 ?  67  ASP   B H    1 
ATOM   4872 H HA   . ASP   B 1 67  ? 53.237 -7.072  9.332   1.00 15.76 ?  67  ASP   B HA   1 
ATOM   4873 H HB2  . ASP   B 1 67  ? 54.601 -6.668  7.535   1.00 17.44 ?  67  ASP   B HB2  1 
ATOM   4874 H HB3  . ASP   B 1 67  ? 53.440 -7.051  6.518   1.00 17.44 ?  67  ASP   B HB3  1 
ATOM   4875 N N    . TYR   B 1 68  ? 50.738 -7.948  7.510   1.00 13.09 ?  68  TYR   B N    1 
ATOM   4876 C CA   . TYR   B 1 68  ? 49.280 -7.874  7.441   1.00 13.82 ?  68  TYR   B CA   1 
ATOM   4877 C C    . TYR   B 1 68  ? 48.649 -8.212  8.788   1.00 13.31 ?  68  TYR   B C    1 
ATOM   4878 O O    . TYR   B 1 68  ? 47.718 -7.534  9.239   1.00 13.79 ?  68  TYR   B O    1 
ATOM   4879 C CB   . TYR   B 1 68  ? 48.746 -8.807  6.346   1.00 14.45 ?  68  TYR   B CB   1 
ATOM   4880 C CG   . TYR   B 1 68  ? 47.238 -8.953  6.401   1.00 15.60 ?  68  TYR   B CG   1 
ATOM   4881 C CD1  . TYR   B 1 68  ? 46.646 -9.914  7.214   1.00 16.41 ?  68  TYR   B CD1  1 
ATOM   4882 C CD2  . TYR   B 1 68  ? 46.408 -8.108  5.679   1.00 16.84 ?  68  TYR   B CD2  1 
ATOM   4883 C CE1  . TYR   B 1 68  ? 45.278 -10.033 7.300   1.00 17.68 ?  68  TYR   B CE1  1 
ATOM   4884 C CE2  . TYR   B 1 68  ? 45.026 -8.229  5.754   1.00 17.61 ?  68  TYR   B CE2  1 
ATOM   4885 C CZ   . TYR   B 1 68  ? 44.480 -9.188  6.569   1.00 17.77 ?  68  TYR   B CZ   1 
ATOM   4886 O OH   . TYR   B 1 68  ? 43.110 -9.298  6.651   1.00 18.85 ?  68  TYR   B OH   1 
ATOM   4887 H H    . TYR   B 1 68  ? 51.096 -8.504  6.953   1.00 15.70 ?  68  TYR   B H    1 
ATOM   4888 H HA   . TYR   B 1 68  ? 49.030 -6.969  7.215   1.00 16.59 ?  68  TYR   B HA   1 
ATOM   4889 H HB2  . TYR   B 1 68  ? 48.977 -8.440  5.481   1.00 17.34 ?  68  TYR   B HB2  1 
ATOM   4890 H HB3  . TYR   B 1 68  ? 49.137 -9.685  6.457   1.00 17.34 ?  68  TYR   B HB3  1 
ATOM   4891 H HD1  . TYR   B 1 68  ? 47.183 -10.490 7.711   1.00 19.69 ?  68  TYR   B HD1  1 
ATOM   4892 H HD2  . TYR   B 1 68  ? 46.784 -7.450  5.146   1.00 20.20 ?  68  TYR   B HD2  1 
ATOM   4893 H HE1  . TYR   B 1 68  ? 44.893 -10.694 7.835   1.00 21.21 ?  68  TYR   B HE1  1 
ATOM   4894 H HE2  . TYR   B 1 68  ? 44.477 -7.657  5.270   1.00 21.13 ?  68  TYR   B HE2  1 
ATOM   4895 H HH   . TYR   B 1 68  ? 42.734 -8.735  6.143   1.00 22.62 ?  68  TYR   B HH   1 
ATOM   4896 N N    . ILE   B 1 69  ? 49.124 -9.283  9.430   1.00 12.85 ?  69  ILE   B N    1 
ATOM   4897 C CA   . ILE   B 1 69  ? 48.570 -9.712  10.711  1.00 13.38 ?  69  ILE   B CA   1 
ATOM   4898 C C    . ILE   B 1 69  ? 48.825 -8.666  11.789  1.00 13.24 ?  69  ILE   B C    1 
ATOM   4899 O O    . ILE   B 1 69  ? 47.954 -8.387  12.620  1.00 13.70 ?  69  ILE   B O    1 
ATOM   4900 C CB   . ILE   B 1 69  ? 49.151 -11.086 11.099  1.00 14.17 ?  69  ILE   B CB   1 
ATOM   4901 C CG1  . ILE   B 1 69  ? 48.620 -12.189 10.174  1.00 14.41 ?  69  ILE   B CG1  1 
ATOM   4902 C CG2  . ILE   B 1 69  ? 48.880 -11.396 12.563  1.00 15.21 ?  69  ILE   B CG2  1 
ATOM   4903 C CD1  . ILE   B 1 69  ? 47.159 -12.516 10.348  1.00 15.00 ?  69  ILE   B CD1  1 
ATOM   4904 H H    . ILE   B 1 69  ? 49.768 -9.774  9.148   1.00 15.42 ?  69  ILE   B H    1 
ATOM   4905 H HA   . ILE   B 1 69  ? 47.612 -9.808  10.622  1.00 16.06 ?  69  ILE   B HA   1 
ATOM   4906 H HB   . ILE   B 1 69  ? 50.115 -11.038 10.984  1.00 17.00 ?  69  ILE   B HB   1 
ATOM   4907 H HG12 . ILE   B 1 69  ? 48.751 -11.906 9.255   1.00 17.29 ?  69  ILE   B HG12 1 
ATOM   4908 H HG13 . ILE   B 1 69  ? 49.127 -12.998 10.341  1.00 17.29 ?  69  ILE   B HG13 1 
ATOM   4909 H HG21 . ILE   B 1 69  ? 49.021 -12.347 12.709  1.00 18.25 ?  69  ILE   B HG21 1 
ATOM   4910 H HG22 . ILE   B 1 69  ? 49.495 -10.889 13.119  1.00 18.25 ?  69  ILE   B HG22 1 
ATOM   4911 H HG23 . ILE   B 1 69  ? 47.966 -11.162 12.774  1.00 18.25 ?  69  ILE   B HG23 1 
ATOM   4912 H HD11 . ILE   B 1 69  ? 46.922 -13.220 9.725   1.00 18.00 ?  69  ILE   B HD11 1 
ATOM   4913 H HD12 . ILE   B 1 69  ? 47.007 -12.817 11.258  1.00 18.00 ?  69  ILE   B HD12 1 
ATOM   4914 H HD13 . ILE   B 1 69  ? 46.630 -11.724 10.168  1.00 18.00 ?  69  ILE   B HD13 1 
ATOM   4915 N N    . ALA   B 1 70  ? 50.022 -8.080  11.813  1.00 13.21 ?  70  ALA   B N    1 
ATOM   4916 C CA   . ALA   B 1 70  ? 50.305 -7.044  12.801  1.00 13.17 ?  70  ALA   B CA   1 
ATOM   4917 C C    . ALA   B 1 70  ? 49.308 -5.897  12.692  1.00 13.60 ?  70  ALA   B C    1 
ATOM   4918 O O    . ALA   B 1 70  ? 48.866 -5.352  13.709  1.00 14.11 ?  70  ALA   B O    1 
ATOM   4919 C CB   . ALA   B 1 70  ? 51.738 -6.539  12.625  1.00 13.70 ?  70  ALA   B CB   1 
ATOM   4920 H H    . ALA   B 1 70  ? 50.668 -8.264  11.285  1.00 15.85 ?  70  ALA   B H    1 
ATOM   4921 H HA   . ALA   B 1 70  ? 50.234 -7.423  13.692  1.00 15.80 ?  70  ALA   B HA   1 
ATOM   4922 H HB1  . ALA   B 1 70  ? 51.928 -5.873  13.306  1.00 16.44 ?  70  ALA   B HB1  1 
ATOM   4923 H HB2  . ALA   B 1 70  ? 52.353 -7.286  12.717  1.00 16.44 ?  70  ALA   B HB2  1 
ATOM   4924 H HB3  . ALA   B 1 70  ? 51.831 -6.145  11.743  1.00 16.44 ?  70  ALA   B HB3  1 
ATOM   4925 N N    . THR   B 1 71  ? 48.932 -5.526  11.470  1.00 14.00 ?  71  THR   B N    1 
ATOM   4926 C CA   . THR   B 1 71  ? 48.039 -4.391  11.263  1.00 15.05 ?  71  THR   B CA   1 
ATOM   4927 C C    . THR   B 1 71  ? 46.571 -4.757  11.465  1.00 15.43 ?  71  THR   B C    1 
ATOM   4928 O O    . THR   B 1 71  ? 45.791 -3.942  11.977  1.00 17.13 ?  71  THR   B O    1 
ATOM   4929 C CB   . THR   B 1 71  ? 48.260 -3.826  9.859   1.00 16.99 ?  71  THR   B CB   1 
ATOM   4930 O OG1  . THR   B 1 71  ? 49.583 -3.288  9.765   1.00 18.83 ?  71  THR   B OG1  1 
ATOM   4931 C CG2  . THR   B 1 71  ? 47.244 -2.736  9.533   1.00 18.00 ?  71  THR   B CG2  1 
ATOM   4932 H H    . THR   B 1 71  ? 49.181 -5.916  10.750  1.00 16.80 ?  71  THR   B H    1 
ATOM   4933 H HA   . THR   B 1 71  ? 48.260 -3.693  11.901  1.00 18.06 ?  71  THR   B HA   1 
ATOM   4934 H HB   . THR   B 1 71  ? 48.166 -4.535  9.206   1.00 20.39 ?  71  THR   B HB   1 
ATOM   4935 H HG1  . THR   B 1 71  ? 49.715 -2.962  8.999   1.00 22.59 ?  71  THR   B HG1  1 
ATOM   4936 H HG21 . THR   B 1 71  ? 47.551 -2.212  8.774   1.00 21.60 ?  71  THR   B HG21 1 
ATOM   4937 H HG22 . THR   B 1 71  ? 46.387 -3.130  9.314   1.00 21.60 ?  71  THR   B HG22 1 
ATOM   4938 H HG23 . THR   B 1 71  ? 47.137 -2.143  10.295  1.00 21.60 ?  71  THR   B HG23 1 
ATOM   4939 N N    . ASN   B 1 72  ? 46.177 -5.973  11.074  1.00 14.94 ?  72  ASN   B N    1 
ATOM   4940 C CA   . ASN   B 1 72  ? 44.771 -6.331  10.944  1.00 15.64 ?  72  ASN   B CA   1 
ATOM   4941 C C    . ASN   B 1 72  ? 44.298 -7.434  11.881  1.00 16.25 ?  72  ASN   B C    1 
ATOM   4942 O O    . ASN   B 1 72  ? 43.082 -7.597  12.044  1.00 17.20 ?  72  ASN   B O    1 
ATOM   4943 C CB   . ASN   B 1 72  ? 44.471 -6.756  9.499   1.00 16.66 ?  72  ASN   B CB   1 
ATOM   4944 C CG   . ASN   B 1 72  ? 44.738 -5.648  8.509   1.00 17.76 ?  72  ASN   B CG   1 
ATOM   4945 O OD1  . ASN   B 1 72  ? 45.745 -5.657  7.795   1.00 18.87 ?  72  ASN   B OD1  1 
ATOM   4946 N ND2  . ASN   B 1 72  ? 43.856 -4.665  8.484   1.00 19.22 ?  72  ASN   B ND2  1 
ATOM   4947 H H    . ASN   B 1 72  ? 46.721 -6.615  10.873  1.00 17.93 ?  72  ASN   B H    1 
ATOM   4948 H HA   . ASN   B 1 72  ? 44.242 -5.545  11.130  1.00 18.77 ?  72  ASN   B HA   1 
ATOM   4949 H HB2  . ASN   B 1 72  ? 45.036 -7.511  9.265   1.00 19.99 ?  72  ASN   B HB2  1 
ATOM   4950 H HB3  . ASN   B 1 72  ? 43.538 -7.003  9.431   1.00 19.99 ?  72  ASN   B HB3  1 
ATOM   4951 H HD21 . ASN   B 1 72  ? 43.958 -4.007  7.939   1.00 23.06 ?  72  ASN   B HD21 1 
ATOM   4952 H HD22 . ASN   B 1 72  ? 43.166 -4.690  9.000   1.00 23.06 ?  72  ASN   B HD22 1 
ATOM   4953 N N    . GLY   B 1 73  ? 45.200 -8.186  12.501  1.00 15.81 ?  73  GLY   B N    1 
ATOM   4954 C CA   . GLY   B 1 73  ? 44.806 -9.329  13.285  1.00 15.06 ?  73  GLY   B CA   1 
ATOM   4955 C C    . GLY   B 1 73  ? 44.448 -10.515 12.413  1.00 13.74 ?  73  GLY   B C    1 
ATOM   4956 O O    . GLY   B 1 73  ? 44.435 -10.433 11.181  1.00 13.72 ?  73  GLY   B O    1 
ATOM   4957 H H    . GLY   B 1 73  ? 46.055 -8.053  12.474  1.00 18.98 ?  73  GLY   B H    1 
ATOM   4958 H HA2  . GLY   B 1 73  ? 45.534 -9.584  13.875  1.00 18.07 ?  73  GLY   B HA2  1 
ATOM   4959 H HA3  . GLY   B 1 73  ? 44.036 -9.096  13.828  1.00 18.07 ?  73  GLY   B HA3  1 
ATOM   4960 N N    . PRO   B 1 74  ? 44.140 -11.641 13.048  1.00 13.94 ?  74  PRO   B N    1 
ATOM   4961 C CA   . PRO   B 1 74  ? 43.895 -12.871 12.294  1.00 13.56 ?  74  PRO   B CA   1 
ATOM   4962 C C    . PRO   B 1 74  ? 42.594 -12.813 11.502  1.00 12.89 ?  74  PRO   B C    1 
ATOM   4963 O O    . PRO   B 1 74  ? 41.656 -12.071 11.818  1.00 14.26 ?  74  PRO   B O    1 
ATOM   4964 C CB   . PRO   B 1 74  ? 43.825 -13.940 13.389  1.00 14.47 ?  74  PRO   B CB   1 
ATOM   4965 C CG   . PRO   B 1 74  ? 43.373 -13.197 14.602  1.00 15.93 ?  74  PRO   B CG   1 
ATOM   4966 C CD   . PRO   B 1 74  ? 44.023 -11.849 14.500  1.00 15.63 ?  74  PRO   B CD   1 
ATOM   4967 H HA   . PRO   B 1 74  ? 44.638 -13.057 11.693  1.00 16.28 ?  74  PRO   B HA   1 
ATOM   4968 H HB2  . PRO   B 1 74  ? 43.183 -14.622 13.135  1.00 17.36 ?  74  PRO   B HB2  1 
ATOM   4969 H HB3  . PRO   B 1 74  ? 44.705 -14.326 13.524  1.00 17.36 ?  74  PRO   B HB3  1 
ATOM   4970 H HG2  . PRO   B 1 74  ? 42.406 -13.117 14.590  1.00 19.12 ?  74  PRO   B HG2  1 
ATOM   4971 H HG3  . PRO   B 1 74  ? 43.669 -13.665 15.396  1.00 19.12 ?  74  PRO   B HG3  1 
ATOM   4972 H HD2  . PRO   B 1 74  ? 43.453 -11.169 14.900  1.00 18.75 ?  74  PRO   B HD2  1 
ATOM   4973 H HD3  . PRO   B 1 74  ? 44.900 -11.862 14.910  1.00 18.75 ?  74  PRO   B HD3  1 
ATOM   4974 N N    . LEU   B 1 75  ? 42.559 -13.624 10.448  1.00 12.26 ?  75  LEU   B N    1 
ATOM   4975 C CA   . LEU   B 1 75  ? 41.343 -13.838 9.682   1.00 12.49 ?  75  LEU   B CA   1 
ATOM   4976 C C    . LEU   B 1 75  ? 40.370 -14.702 10.483  1.00 12.88 ?  75  LEU   B C    1 
ATOM   4977 O O    . LEU   B 1 75  ? 40.708 -15.261 11.525  1.00 13.98 ?  75  LEU   B O    1 
ATOM   4978 C CB   . LEU   B 1 75  ? 41.667 -14.543 8.364   1.00 12.38 ?  75  LEU   B CB   1 
ATOM   4979 C CG   . LEU   B 1 75  ? 42.516 -13.784 7.338   1.00 14.11 ?  75  LEU   B CG   1 
ATOM   4980 C CD1  . LEU   B 1 75  ? 42.708 -14.608 6.064   1.00 15.38 ?  75  LEU   B CD1  1 
ATOM   4981 C CD2  . LEU   B 1 75  ? 41.929 -12.436 7.002   1.00 17.01 ?  75  LEU   B CD2  1 
ATOM   4982 H H    . LEU   B 1 75  ? 43.236 -14.067 10.150  1.00 14.71 ?  75  LEU   B H    1 
ATOM   4983 H HA   . LEU   B 1 75  ? 40.918 -12.989 9.488   1.00 14.98 ?  75  LEU   B HA   1 
ATOM   4984 H HB2  . LEU   B 1 75  ? 42.143 -15.363 8.567   1.00 14.86 ?  75  LEU   B HB2  1 
ATOM   4985 H HB3  . LEU   B 1 75  ? 40.830 -14.765 7.923   1.00 14.86 ?  75  LEU   B HB3  1 
ATOM   4986 H HG   . LEU   B 1 75  ? 43.394 -13.630 7.717   1.00 16.94 ?  75  LEU   B HG   1 
ATOM   4987 H HD11 . LEU   B 1 75  ? 43.254 -14.098 5.437   1.00 18.45 ?  75  LEU   B HD11 1 
ATOM   4988 H HD12 . LEU   B 1 75  ? 43.157 -15.437 6.287   1.00 18.45 ?  75  LEU   B HD12 1 
ATOM   4989 H HD13 . LEU   B 1 75  ? 41.843 -14.792 5.669   1.00 18.45 ?  75  LEU   B HD13 1 
ATOM   4990 H HD21 . LEU   B 1 75  ? 42.444 -12.032 6.287   1.00 20.42 ?  75  LEU   B HD21 1 
ATOM   4991 H HD22 . LEU   B 1 75  ? 41.008 -12.553 6.721   1.00 20.42 ?  75  LEU   B HD22 1 
ATOM   4992 H HD23 . LEU   B 1 75  ? 41.963 -11.871 7.792   1.00 20.42 ?  75  LEU   B HD23 1 
ATOM   4993 N N    . LYS   B 1 76  ? 39.142 -14.805 9.973   1.00 14.04 ?  76  LYS   B N    1 
ATOM   4994 C CA   . LYS   B 1 76  ? 38.153 -15.768 10.444  1.00 15.15 ?  76  LYS   B CA   1 
ATOM   4995 C C    . LYS   B 1 76  ? 38.243 -17.037 9.599   1.00 13.43 ?  76  LYS   B C    1 
ATOM   4996 O O    . LYS   B 1 76  ? 38.507 -16.975 8.400   1.00 13.27 ?  76  LYS   B O    1 
ATOM   4997 C CB   . LYS   B 1 76  ? 36.736 -15.196 10.267  1.00 17.77 ?  76  LYS   B CB   1 
ATOM   4998 C CG   . LYS   B 1 76  ? 36.465 -13.815 10.886  1.00 19.83 ?  76  LYS   B CG   1 
ATOM   4999 C CD   . LYS   B 1 76  ? 35.074 -13.266 10.509  1.00 21.40 ?  76  LYS   B CD   1 
ATOM   5000 C CE   . LYS   B 1 76  ? 34.807 -11.906 11.140  1.00 23.33 ?  76  LYS   B CE   1 
ATOM   5001 N NZ   . LYS   B 1 76  ? 33.506 -11.322 10.706  1.00 24.17 ?  76  LYS   B NZ   1 
ATOM   5002 H H    . LYS   B 1 76  ? 38.850 -14.312 9.334   1.00 16.84 ?  76  LYS   B H    1 
ATOM   5003 H HA   . LYS   B 1 76  ? 38.299 -15.989 11.379  1.00 18.18 ?  76  LYS   B HA   1 
ATOM   5004 H HB2  . LYS   B 1 76  ? 36.555 -15.124 9.315   1.00 21.33 ?  76  LYS   B HB2  1 
ATOM   5005 H HB3  . LYS   B 1 76  ? 36.103 -15.816 10.664  1.00 21.33 ?  76  LYS   B HB3  1 
ATOM   5006 H HG2  . LYS   B 1 76  ? 36.511 -13.887 11.851  1.00 23.79 ?  76  LYS   B HG2  1 
ATOM   5007 H HG3  . LYS   B 1 76  ? 37.135 -13.189 10.566  1.00 23.79 ?  76  LYS   B HG3  1 
ATOM   5008 H HD2  . LYS   B 1 76  ? 35.023 -13.168 9.544   1.00 25.68 ?  76  LYS   B HD2  1 
ATOM   5009 H HD3  . LYS   B 1 76  ? 34.395 -13.884 10.819  1.00 25.68 ?  76  LYS   B HD3  1 
ATOM   5010 H HE2  . LYS   B 1 76  ? 34.789 -12.004 12.105  1.00 28.00 ?  76  LYS   B HE2  1 
ATOM   5011 H HE3  . LYS   B 1 76  ? 35.515 -11.294 10.882  1.00 28.00 ?  76  LYS   B HE3  1 
ATOM   5012 H HZ1  . LYS   B 1 76  ? 33.383 -10.529 11.094  1.00 29.00 ?  76  LYS   B HZ1  1 
ATOM   5013 H HZ2  . LYS   B 1 76  ? 33.499 -11.214 9.822   1.00 29.00 ?  76  LYS   B HZ2  1 
ATOM   5014 H HZ3  . LYS   B 1 76  ? 32.837 -11.862 10.937  1.00 29.00 ?  76  LYS   B HZ3  1 
ATOM   5015 N N    . VAL   B 1 77  ? 37.993 -18.196 10.220  1.00 13.82 ?  77  VAL   B N    1 
ATOM   5016 C CA   . VAL   B 1 77  ? 37.783 -19.404 9.426   1.00 13.79 ?  77  VAL   B CA   1 
ATOM   5017 C C    . VAL   B 1 77  ? 36.592 -19.165 8.510   1.00 12.98 ?  77  VAL   B C    1 
ATOM   5018 O O    . VAL   B 1 77  ? 35.527 -18.714 8.953   1.00 13.16 ?  77  VAL   B O    1 
ATOM   5019 C CB   . VAL   B 1 77  ? 37.593 -20.641 10.318  1.00 15.06 ?  77  VAL   B CB   1 
ATOM   5020 C CG1  . VAL   B 1 77  ? 37.326 -21.868 9.451   1.00 15.57 ?  77  VAL   B CG1  1 
ATOM   5021 C CG2  . VAL   B 1 77  ? 38.820 -20.871 11.202  1.00 16.57 ?  77  VAL   B CG2  1 
ATOM   5022 H H    . VAL   B 1 77  ? 37.945 -18.302 11.070  1.00 16.58 ?  77  VAL   B H    1 
ATOM   5023 H HA   . VAL   B 1 77  ? 38.559 -19.551 8.868   1.00 16.55 ?  77  VAL   B HA   1 
ATOM   5024 H HB   . VAL   B 1 77  ? 36.822 -20.501 10.893  1.00 18.08 ?  77  VAL   B HB   1 
ATOM   5025 H HG11 . VAL   B 1 77  ? 37.384 -22.661 10.008  1.00 18.68 ?  77  VAL   B HG11 1 
ATOM   5026 H HG12 . VAL   B 1 77  ? 36.436 -21.802 9.067   1.00 18.68 ?  77  VAL   B HG12 1 
ATOM   5027 H HG13 . VAL   B 1 77  ? 37.990 -21.908 8.747   1.00 18.68 ?  77  VAL   B HG13 1 
ATOM   5028 H HG21 . VAL   B 1 77  ? 38.679 -21.673 11.725  1.00 19.88 ?  77  VAL   B HG21 1 
ATOM   5029 H HG22 . VAL   B 1 77  ? 39.597 -20.971 10.635  1.00 19.88 ?  77  VAL   B HG22 1 
ATOM   5030 H HG23 . VAL   B 1 77  ? 38.930 -20.106 11.788  1.00 19.88 ?  77  VAL   B HG23 1 
ATOM   5031 N N    . GLY   B 1 78  ? 36.775 -19.436 7.220   1.00 12.46 ?  78  GLY   B N    1 
ATOM   5032 C CA   . GLY   B 1 78  ? 35.803 -19.103 6.206   1.00 11.96 ?  78  GLY   B CA   1 
ATOM   5033 C C    . GLY   B 1 78  ? 36.048 -17.783 5.515   1.00 11.43 ?  78  GLY   B C    1 
ATOM   5034 O O    . GLY   B 1 78  ? 35.368 -17.491 4.525   1.00 11.99 ?  78  GLY   B O    1 
ATOM   5035 H H    . GLY   B 1 78  ? 37.474 -19.827 6.909   1.00 14.96 ?  78  GLY   B H    1 
ATOM   5036 H HA2  . GLY   B 1 78  ? 35.795 -19.794 5.532   1.00 14.35 ?  78  GLY   B HA2  1 
ATOM   5037 H HA3  . GLY   B 1 78  ? 34.921 -19.062 6.611   1.00 14.35 ?  78  GLY   B HA3  1 
ATOM   5038 N N    . GLY   B 1 79  ? 36.997 -16.982 6.007   1.00 11.61 ?  79  GLY   B N    1 
ATOM   5039 C CA   . GLY   B 1 79  ? 37.304 -15.687 5.438   1.00 11.65 ?  79  GLY   B CA   1 
ATOM   5040 C C    . GLY   B 1 79  ? 38.537 -15.705 4.542   1.00 11.21 ?  79  GLY   B C    1 
ATOM   5041 O O    . GLY   B 1 79  ? 39.147 -16.739 4.282   1.00 11.48 ?  79  GLY   B O    1 
ATOM   5042 H H    . GLY   B 1 79  ? 37.494 -17.179 6.678   1.00 13.93 ?  79  GLY   B H    1 
ATOM   5043 H HA2  . GLY   B 1 79  ? 36.550 -15.374 4.911   1.00 13.99 ?  79  GLY   B HA2  1 
ATOM   5044 H HA3  . GLY   B 1 79  ? 37.461 -15.048 6.151   1.00 13.99 ?  79  GLY   B HA3  1 
ATOM   5045 N N    . SER   B 1 80  ? 38.902 -14.510 4.070   1.00 11.13 ?  80  SER   B N    1 
ATOM   5046 C CA   . SER   B 1 80  ? 40.009 -14.373 3.135   1.00 11.02 ?  80  SER   B CA   1 
ATOM   5047 C C    . SER   B 1 80  ? 40.587 -12.968 3.198   1.00 11.22 ?  80  SER   B C    1 
ATOM   5048 O O    . SER   B 1 80  ? 39.971 -12.036 3.721   1.00 12.42 ?  80  SER   B O    1 
ATOM   5049 C CB   . SER   B 1 80  ? 39.568 -14.657 1.696   1.00 11.41 ?  80  SER   B CB   1 
ATOM   5050 O OG   . SER   B 1 80  ? 38.727 -13.631 1.199   1.00 12.85 ?  80  SER   B OG   1 
ATOM   5051 H H    . SER   B 1 80  ? 38.517 -13.765 4.269   1.00 13.35 ?  80  SER   B H    1 
ATOM   5052 H HA   . SER   B 1 80  ? 40.699 -15.003 3.376   1.00 13.22 ?  80  SER   B HA   1 
ATOM   5053 H HB2  . SER   B 1 80  ? 40.353 -14.717 1.128   1.00 13.70 ?  80  SER   B HB2  1 
ATOM   5054 H HB3  . SER   B 1 80  ? 39.083 -15.500 1.673   1.00 13.70 ?  80  SER   B HB3  1 
ATOM   5055 H HG   . SER   B 1 80  ? 38.033 -13.572 1.674   1.00 15.42 ?  80  SER   B HG   1 
ATOM   5056 N N    . CYS   B 1 81  ? 41.774 -12.823 2.617   1.00 10.82 ?  81  CYS   B N    1 
ATOM   5057 C CA   . CYS   B 1 81  ? 42.323 -11.511 2.308   1.00 11.05 ?  81  CYS   B CA   1 
ATOM   5058 C C    . CYS   B 1 81  ? 43.094 -11.592 1.002   1.00 10.39 ?  81  CYS   B C    1 
ATOM   5059 O O    . CYS   B 1 81  ? 43.603 -12.654 0.628   1.00 11.37 ?  81  CYS   B O    1 
ATOM   5060 C CB   . CYS   B 1 81  ? 43.219 -10.953 3.427   1.00 11.99 ?  81  CYS   B CB   1 
ATOM   5061 S SG   . CYS   B 1 81  ? 44.732 -11.892 3.686   1.00 12.21 ?  81  CYS   B SG   1 
ATOM   5062 H H    . CYS   B 1 81  ? 42.284 -13.477 2.379   1.00 12.99 ?  81  CYS   B H    1 
ATOM   5063 H HA   . CYS   B 1 81  ? 41.588 -10.887 2.180   1.00 13.26 ?  81  CYS   B HA   1 
ATOM   5064 H HB2  . CYS   B 1 81  ? 43.469 -10.043 3.205   1.00 14.39 ?  81  CYS   B HB2  1 
ATOM   5065 H HB3  . CYS   B 1 81  ? 42.715 -10.958 4.259   1.00 14.39 ?  81  CYS   B HB3  1 
ATOM   5066 H HG   . CYS   B 1 81  ? 45.358 -11.391 4.580   1.00 14.65 ?  81  CYS   B HG   1 
ATOM   5067 N N    . VAL   B 1 82  ? 43.204 -10.450 0.328   1.00 10.73 ?  82  VAL   B N    1 
ATOM   5068 C CA   . VAL   B 1 82  ? 43.968 -10.328 -0.910  1.00 10.80 ?  82  VAL   B CA   1 
ATOM   5069 C C    . VAL   B 1 82  ? 45.308 -9.686  -0.585  1.00 11.02 ?  82  VAL   B C    1 
ATOM   5070 O O    . VAL   B 1 82  ? 45.355 -8.565  -0.056  1.00 12.20 ?  82  VAL   B O    1 
ATOM   5071 C CB   . VAL   B 1 82  ? 43.222 -9.483  -1.952  1.00 12.26 ?  82  VAL   B CB   1 
ATOM   5072 C CG1  . VAL   B 1 82  ? 44.067 -9.318  -3.208  1.00 13.73 ?  82  VAL   B CG1  1 
ATOM   5073 C CG2  . VAL   B 1 82  ? 41.873 -10.088 -2.277  1.00 13.08 ?  82  VAL   B CG2  1 
ATOM   5074 H H    . VAL   B 1 82  ? 42.834 -9.709  0.569   1.00 12.88 ?  82  VAL   B H    1 
ATOM   5075 H HA   . VAL   B 1 82  ? 44.126 -11.209 -1.286  1.00 12.97 ?  82  VAL   B HA   1 
ATOM   5076 H HB   . VAL   B 1 82  ? 43.068 -8.600  -1.584  1.00 14.71 ?  82  VAL   B HB   1 
ATOM   5077 H HG11 . VAL   B 1 82  ? 43.504 -8.994  -3.929  1.00 16.48 ?  82  VAL   B HG11 1 
ATOM   5078 H HG12 . VAL   B 1 82  ? 44.774 -8.669  -3.034  1.00 16.48 ?  82  VAL   B HG12 1 
ATOM   5079 H HG13 . VAL   B 1 82  ? 44.455 -10.171 -3.448  1.00 16.48 ?  82  VAL   B HG13 1 
ATOM   5080 H HG21 . VAL   B 1 82  ? 41.440 -9.555  -2.965  1.00 15.70 ?  82  VAL   B HG21 1 
ATOM   5081 H HG22 . VAL   B 1 82  ? 41.998 -10.997 -2.599  1.00 15.70 ?  82  VAL   B HG22 1 
ATOM   5082 H HG23 . VAL   B 1 82  ? 41.325 -10.097 -1.476  1.00 15.70 ?  82  VAL   B HG23 1 
ATOM   5083 N N    . LEU   B 1 83  ? 46.391 -10.365 -0.954  1.00 10.76 ?  83  LEU   B N    1 
ATOM   5084 C CA   . LEU   B 1 83  ? 47.744 -9.844  -0.831  1.00 10.83 ?  83  LEU   B CA   1 
ATOM   5085 C C    . LEU   B 1 83  ? 48.450 -9.983  -2.180  1.00 10.70 ?  83  LEU   B C    1 
ATOM   5086 O O    . LEU   B 1 83  ? 47.850 -10.396 -3.178  1.00 10.86 ?  83  LEU   B O    1 
ATOM   5087 C CB   . LEU   B 1 83  ? 48.490 -10.518 0.329   1.00 11.70 ?  83  LEU   B CB   1 
ATOM   5088 C CG   . LEU   B 1 83  ? 47.967 -10.157 1.725   1.00 12.69 ?  83  LEU   B CG   1 
ATOM   5089 C CD1  . LEU   B 1 83  ? 48.592 -11.034 2.800   1.00 13.36 ?  83  LEU   B CD1  1 
ATOM   5090 C CD2  . LEU   B 1 83  ? 48.181 -8.681  2.050   1.00 13.77 ?  83  LEU   B CD2  1 
ATOM   5091 H H    . LEU   B 1 83  ? 46.357 -11.162 -1.291  1.00 12.91 ?  83  LEU   B H    1 
ATOM   5092 H HA   . LEU   B 1 83  ? 47.687 -8.902  -0.637  1.00 13.00 ?  83  LEU   B HA   1 
ATOM   5093 H HB2  . LEU   B 1 83  ? 48.426 -11.476 0.230   1.00 14.05 ?  83  LEU   B HB2  1 
ATOM   5094 H HB3  . LEU   B 1 83  ? 49.423 -10.245 0.290   1.00 14.05 ?  83  LEU   B HB3  1 
ATOM   5095 H HG   . LEU   B 1 83  ? 47.011 -10.316 1.738   1.00 15.22 ?  83  LEU   B HG   1 
ATOM   5096 H HD11 . LEU   B 1 83  ? 48.227 -10.783 3.664   1.00 16.04 ?  83  LEU   B HD11 1 
ATOM   5097 H HD12 . LEU   B 1 83  ? 48.373 -11.964 2.611   1.00 16.04 ?  83  LEU   B HD12 1 
ATOM   5098 H HD13 . LEU   B 1 83  ? 49.550 -10.912 2.794   1.00 16.04 ?  83  LEU   B HD13 1 
ATOM   5099 H HD21 . LEU   B 1 83  ? 47.963 -8.528  2.982   1.00 16.52 ?  83  LEU   B HD21 1 
ATOM   5100 H HD22 . LEU   B 1 83  ? 49.110 -8.453  1.885   1.00 16.52 ?  83  LEU   B HD22 1 
ATOM   5101 H HD23 . LEU   B 1 83  ? 47.604 -8.144  1.483   1.00 16.52 ?  83  LEU   B HD23 1 
ATOM   5102 N N    . SER   B 1 84  ? 49.728 -9.610  -2.233  1.00 11.79 ?  84  SER   B N    1 
ATOM   5103 C CA   . SER   B 1 84  ? 50.464 -9.722  -3.483  1.00 12.10 ?  84  SER   B CA   1 
ATOM   5104 C C    . SER   B 1 84  ? 50.615 -11.181 -3.901  1.00 11.57 ?  84  SER   B C    1 
ATOM   5105 O O    . SER   B 1 84  ? 50.730 -12.082 -3.071  1.00 11.33 ?  84  SER   B O    1 
ATOM   5106 C CB   . SER   B 1 84  ? 51.859 -9.118  -3.335  1.00 14.14 ?  84  SER   B CB   1 
ATOM   5107 O OG   . SER   B 1 84  ? 52.606 -9.323  -4.517  1.00 15.66 ?  84  SER   B OG   1 
ATOM   5108 H H    . SER   B 1 84  ? 50.178 -9.286  -1.574  1.00 14.15 ?  84  SER   B H    1 
ATOM   5109 H HA   . SER   B 1 84  ? 49.994 -9.250  -4.185  1.00 14.52 ?  84  SER   B HA   1 
ATOM   5110 H HB2  . SER   B 1 84  ? 51.775 -8.164  -3.167  1.00 16.97 ?  84  SER   B HB2  1 
ATOM   5111 H HB3  . SER   B 1 84  ? 52.319 -9.546  -2.600  1.00 16.97 ?  84  SER   B HB3  1 
ATOM   5112 H HG   . SER   B 1 84  ? 53.371 -8.974  -4.443  1.00 18.79 ?  84  SER   B HG   1 
ATOM   5113 N N    . GLY   B 1 85  ? 50.676 -11.401 -5.208  1.00 12.47 ?  85  GLY   B N    1 
ATOM   5114 C CA   . GLY   B 1 85  ? 51.024 -12.689 -5.761  1.00 13.26 ?  85  GLY   B CA   1 
ATOM   5115 C C    . GLY   B 1 85  ? 52.497 -12.884 -6.059  1.00 12.40 ?  85  GLY   B C    1 
ATOM   5116 O O    . GLY   B 1 85  ? 52.875 -13.962 -6.521  1.00 12.91 ?  85  GLY   B O    1 
ATOM   5117 H H    . GLY   B 1 85  ? 50.525 -10.803 -5.801  1.00 14.97 ?  85  GLY   B H    1 
ATOM   5118 H HA2  . GLY   B 1 85  ? 50.749 -13.384 -5.141  1.00 15.91 ?  85  GLY   B HA2  1 
ATOM   5119 H HA3  . GLY   B 1 85  ? 50.541 -12.818 -6.588  1.00 15.91 ?  85  GLY   B HA3  1 
ATOM   5120 N N    . HIS   B 1 86  ? 53.348 -11.887 -5.824  1.00 12.22 ?  86  HIS   B N    1 
ATOM   5121 C CA   . HIS   B 1 86  ? 54.811 -12.059 -5.905  1.00 12.11 ?  86  HIS   B CA   1 
ATOM   5122 C C    . HIS   B 1 86  ? 55.184 -12.568 -7.296  1.00 12.25 ?  86  HIS   B C    1 
ATOM   5123 O O    . HIS   B 1 86  ? 54.796 -11.947 -8.298  1.00 13.15 ?  86  HIS   B O    1 
ATOM   5124 C CB   . HIS   B 1 86  ? 55.294 -12.908 -4.731  1.00 12.60 ?  86  HIS   B CB   1 
ATOM   5125 C CG   . HIS   B 1 86  ? 54.981 -12.304 -3.404  1.00 12.78 ?  86  HIS   B CG   1 
ATOM   5126 N ND1  . HIS   B 1 86  ? 55.804 -11.380 -2.797  1.00 14.21 ?  86  HIS   B ND1  1 
ATOM   5127 C CD2  . HIS   B 1 86  ? 53.910 -12.455 -2.589  1.00 13.17 ?  86  HIS   B CD2  1 
ATOM   5128 C CE1  . HIS   B 1 86  ? 55.253 -10.993 -1.661  1.00 14.28 ?  86  HIS   B CE1  1 
ATOM   5129 N NE2  . HIS   B 1 86  ? 54.101 -11.624 -1.514  1.00 13.58 ?  86  HIS   B NE2  1 
ATOM   5130 H H    . HIS   B 1 86  ? 53.108 -11.093 -5.617  1.00 14.67 ?  86  HIS   B H    1 
ATOM   5131 H HA   . HIS   B 1 86  ? 55.222 -11.186 -5.807  1.00 14.53 ?  86  HIS   B HA   1 
ATOM   5132 H HB2  . HIS   B 1 86  ? 54.872 -13.778 -4.774  1.00 15.12 ?  86  HIS   B HB2  1 
ATOM   5133 H HB3  . HIS   B 1 86  ? 56.260 -13.007 -4.789  1.00 15.12 ?  86  HIS   B HB3  1 
ATOM   5134 H HD2  . HIS   B 1 86  ? 53.172 -13.005 -2.740  1.00 15.80 ?  86  HIS   B HD2  1 
ATOM   5135 H HE1  . HIS   B 1 86  ? 55.622 -10.390 -1.058  1.00 17.14 ?  86  HIS   B HE1  1 
ATOM   5136 H HE2  . HIS   B 1 86  ? 53.569 -11.547 -0.842  1.00 16.30 ?  86  HIS   B HE2  1 
ATOM   5137 N N    . ASN   B 1 87  ? 55.954 -13.648 -7.407  1.00 12.84 ?  87  ASN   B N    1 
ATOM   5138 C CA   . ASN   B 1 87  ? 56.349 -14.225 -8.683  1.00 13.52 ?  87  ASN   B CA   1 
ATOM   5139 C C    . ASN   B 1 87  ? 55.365 -15.268 -9.189  1.00 13.19 ?  87  ASN   B C    1 
ATOM   5140 O O    . ASN   B 1 87  ? 55.681 -15.974 -10.153 1.00 14.66 ?  87  ASN   B O    1 
ATOM   5141 C CB   . ASN   B 1 87  ? 57.743 -14.856 -8.565  1.00 15.11 ?  87  ASN   B CB   1 
ATOM   5142 C CG   . ASN   B 1 87  ? 57.795 -15.981 -7.538  1.00 16.09 ?  87  ASN   B CG   1 
ATOM   5143 O OD1  . ASN   B 1 87  ? 57.162 -15.907 -6.482  1.00 15.29 ?  87  ASN   B OD1  1 
ATOM   5144 N ND2  . ASN   B 1 87  ? 58.538 -17.044 -7.858  1.00 18.09 ?  87  ASN   B ND2  1 
ATOM   5145 H H    . ASN   B 1 87  ? 56.266 -14.082 -6.732  1.00 15.41 ?  87  ASN   B H    1 
ATOM   5146 H HA   . ASN   B 1 87  ? 56.396 -13.519 -9.344  1.00 16.23 ?  87  ASN   B HA   1 
ATOM   5147 H HB2  . ASN   B 1 87  ? 57.996 -15.222 -9.429  1.00 18.14 ?  87  ASN   B HB2  1 
ATOM   5148 H HB3  . ASN   B 1 87  ? 58.374 -14.175 -8.294  1.00 18.14 ?  87  ASN   B HB3  1 
ATOM   5149 H HD21 . ASN   B 1 87  ? 58.598 -17.707 -7.316  1.00 21.71 ?  87  ASN   B HD21 1 
ATOM   5150 H HD22 . ASN   B 1 87  ? 58.963 -17.062 -8.609  1.00 21.71 ?  87  ASN   B HD22 1 
ATOM   5151 N N    . LEU   B 1 88  ? 54.186 -15.370 -8.571  1.00 12.36 ?  88  LEU   B N    1 
ATOM   5152 C CA   . LEU   B 1 88  ? 53.207 -16.397 -8.903  1.00 12.45 ?  88  LEU   B CA   1 
ATOM   5153 C C    . LEU   B 1 88  ? 51.978 -15.874 -9.626  1.00 12.01 ?  88  LEU   B C    1 
ATOM   5154 O O    . LEU   B 1 88  ? 51.379 -16.618 -10.414 1.00 13.86 ?  88  LEU   B O    1 
ATOM   5155 C CB   . LEU   B 1 88  ? 52.735 -17.089 -7.621  1.00 13.39 ?  88  LEU   B CB   1 
ATOM   5156 C CG   . LEU   B 1 88  ? 53.851 -17.747 -6.824  1.00 15.58 ?  88  LEU   B CG   1 
ATOM   5157 C CD1  . LEU   B 1 88  ? 53.350 -18.114 -5.437  1.00 17.07 ?  88  LEU   B CD1  1 
ATOM   5158 C CD2  . LEU   B 1 88  ? 54.357 -18.975 -7.557  1.00 18.51 ?  88  LEU   B CD2  1 
ATOM   5159 H H    . LEU   B 1 88  ? 53.928 -14.843 -7.935  1.00 14.83 ?  88  LEU   B H    1 
ATOM   5160 H HA   . LEU   B 1 88  ? 53.625 -17.061 -9.464  1.00 14.95 ?  88  LEU   B HA   1 
ATOM   5161 H HB2  . LEU   B 1 88  ? 52.309 -16.437 -7.044  1.00 16.06 ?  88  LEU   B HB2  1 
ATOM   5162 H HB3  . LEU   B 1 88  ? 52.097 -17.783 -7.857  1.00 16.06 ?  88  LEU   B HB3  1 
ATOM   5163 H HG   . LEU   B 1 88  ? 54.588 -17.126 -6.724  1.00 18.70 ?  88  LEU   B HG   1 
ATOM   5164 H HD11 . LEU   B 1 88  ? 53.986 -18.714 -5.019  1.00 20.48 ?  88  LEU   B HD11 1 
ATOM   5165 H HD12 . LEU   B 1 88  ? 53.259 -17.305 -4.911  1.00 20.48 ?  88  LEU   B HD12 1 
ATOM   5166 H HD13 . LEU   B 1 88  ? 52.488 -18.551 -5.523  1.00 20.48 ?  88  LEU   B HD13 1 
ATOM   5167 H HD21 . LEU   B 1 88  ? 55.010 -19.429 -7.001  1.00 22.22 ?  88  LEU   B HD21 1 
ATOM   5168 H HD22 . LEU   B 1 88  ? 53.609 -19.566 -7.738  1.00 22.22 ?  88  LEU   B HD22 1 
ATOM   5169 H HD23 . LEU   B 1 88  ? 54.768 -18.698 -8.390  1.00 22.22 ?  88  LEU   B HD23 1 
ATOM   5170 N N    . ALA   B 1 89  ? 51.564 -14.641 -9.350  1.00 11.59 ?  89  ALA   B N    1 
ATOM   5171 C CA   . ALA   B 1 89  ? 50.274 -14.144 -9.806  1.00 10.98 ?  89  ALA   B CA   1 
ATOM   5172 C C    . ALA   B 1 89  ? 50.247 -12.655 -9.527  1.00 11.32 ?  89  ALA   B C    1 
ATOM   5173 O O    . ALA   B 1 89  ? 51.079 -12.140 -8.783  1.00 12.33 ?  89  ALA   B O    1 
ATOM   5174 C CB   . ALA   B 1 89  ? 49.127 -14.815 -9.051  1.00 11.50 ?  89  ALA   B CB   1 
ATOM   5175 H H    . ALA   B 1 89  ? 52.012 -14.066 -8.889  1.00 13.90 ?  89  ALA   B H    1 
ATOM   5176 H HA   . ALA   B 1 89  ? 50.167 -14.297 -10.760 1.00 13.18 ?  89  ALA   B HA   1 
ATOM   5177 H HB1  . ALA   B 1 89  ? 48.283 -14.477 -9.396  1.00 13.80 ?  89  ALA   B HB1  1 
ATOM   5178 H HB2  . ALA   B 1 89  ? 49.178 -15.774 -9.191  1.00 13.80 ?  89  ALA   B HB2  1 
ATOM   5179 H HB3  . ALA   B 1 89  ? 49.208 -14.611 -8.110  1.00 13.80 ?  89  ALA   B HB3  1 
ATOM   5180 N N    . LYS   B 1 90  ? 49.259 -11.964 -10.089 1.00 12.23 ?  90  LYS   B N    1 
ATOM   5181 C CA   . LYS   B 1 90  ? 49.070 -10.576 -9.682  1.00 12.58 ?  90  LYS   B CA   1 
ATOM   5182 C C    . LYS   B 1 90  ? 48.748 -10.502 -8.194  1.00 12.47 ?  90  LYS   B C    1 
ATOM   5183 O O    . LYS   B 1 90  ? 49.388 -9.752  -7.440  1.00 13.78 ?  90  LYS   B O    1 
ATOM   5184 C CB   . LYS   B 1 90  ? 47.995 -9.908  -10.539 1.00 14.05 ?  90  LYS   B CB   1 
ATOM   5185 C CG   . LYS   B 1 90  ? 47.695 -8.470  -10.150 1.00 14.72 ?  90  LYS   B CG   1 
ATOM   5186 C CD   . LYS   B 1 90  ? 48.893 -7.564  -10.256 1.00 17.54 ?  90  LYS   B CD   1 
ATOM   5187 C CE   . LYS   B 1 90  ? 48.458 -6.143  -9.984  1.00 19.64 ?  90  LYS   B CE   1 
ATOM   5188 N NZ   . LYS   B 1 90  ? 49.605 -5.211  -9.885  1.00 19.68 ?  90  LYS   B NZ   1 
ATOM   5189 H H    . LYS   B 1 90  ? 48.709 -12.264 -10.679 1.00 14.68 ?  90  LYS   B H    1 
ATOM   5190 H HA   . LYS   B 1 90  ? 49.897 -10.100 -9.824  1.00 15.09 ?  90  LYS   B HA   1 
ATOM   5191 H HB2  . LYS   B 1 90  ? 48.293 -9.907  -11.465 1.00 16.86 ?  90  LYS   B HB2  1 
ATOM   5192 H HB3  . LYS   B 1 90  ? 47.172 -10.418 -10.466 1.00 16.86 ?  90  LYS   B HB3  1 
ATOM   5193 H HG2  . LYS   B 1 90  ? 47.004 -8.127  -10.738 1.00 17.67 ?  90  LYS   B HG2  1 
ATOM   5194 H HG3  . LYS   B 1 90  ? 47.378 -8.452  -9.231  1.00 17.67 ?  90  LYS   B HG3  1 
ATOM   5195 H HD2  . LYS   B 1 90  ? 49.556 -7.817  -9.594  1.00 21.05 ?  90  LYS   B HD2  1 
ATOM   5196 H HD3  . LYS   B 1 90  ? 49.263 -7.613  -11.150 1.00 21.05 ?  90  LYS   B HD3  1 
ATOM   5197 H HE2  . LYS   B 1 90  ? 47.891 -5.835  -10.710 1.00 23.57 ?  90  LYS   B HE2  1 
ATOM   5198 H HE3  . LYS   B 1 90  ? 47.975 -6.105  -9.146  1.00 23.57 ?  90  LYS   B HE3  1 
ATOM   5199 H HZ1  . LYS   B 1 90  ? 49.319 -4.380  -9.728  1.00 23.62 ?  90  LYS   B HZ1  1 
ATOM   5200 H HZ2  . LYS   B 1 90  ? 50.146 -5.456  -9.222  1.00 23.62 ?  90  LYS   B HZ2  1 
ATOM   5201 H HZ3  . LYS   B 1 90  ? 50.070 -5.210  -10.648 1.00 23.62 ?  90  LYS   B HZ3  1 
ATOM   5202 N N    . HIS   B 1 91  ? 47.783 -11.316 -7.750  1.00 10.95 ?  91  HIS   B N    1 
ATOM   5203 C CA   . HIS   B 1 91  ? 47.317 -11.345 -6.375  1.00 10.96 ?  91  HIS   B CA   1 
ATOM   5204 C C    . HIS   B 1 91  ? 47.322 -12.773 -5.858  1.00 10.41 ?  91  HIS   B C    1 
ATOM   5205 O O    . HIS   B 1 91  ? 47.093 -13.729 -6.609  1.00 10.92 ?  91  HIS   B O    1 
ATOM   5206 C CB   . HIS   B 1 91  ? 45.866 -10.866 -6.255  1.00 12.49 ?  91  HIS   B CB   1 
ATOM   5207 C CG   . HIS   B 1 91  ? 45.655 -9.453  -6.680  1.00 16.16 ?  91  HIS   B CG   1 
ATOM   5208 N ND1  . HIS   B 1 91  ? 46.241 -8.384  -6.035  1.00 18.50 ?  91  HIS   B ND1  1 
ATOM   5209 C CD2  . HIS   B 1 91  ? 44.897 -8.926  -7.667  1.00 18.37 ?  91  HIS   B CD2  1 
ATOM   5210 C CE1  . HIS   B 1 91  ? 45.870 -7.258  -6.620  1.00 19.49 ?  91  HIS   B CE1  1 
ATOM   5211 N NE2  . HIS   B 1 91  ? 45.049 -7.560  -7.611  1.00 19.54 ?  91  HIS   B NE2  1 
ATOM   5212 H H    . HIS   B 1 91  ? 47.355 -11.871 -8.256  1.00 13.14 ?  91  HIS   B H    1 
ATOM   5213 H HA   . HIS   B 1 91  ? 47.888 -10.790 -5.814  1.00 13.15 ?  91  HIS   B HA   1 
ATOM   5214 H HB2  . HIS   B 1 91  ? 45.301 -11.425 -6.805  1.00 14.99 ?  91  HIS   B HB2  1 
ATOM   5215 H HB3  . HIS   B 1 91  ? 45.588 -10.937 -5.323  1.00 14.99 ?  91  HIS   B HB3  1 
ATOM   5216 H HD1  . HIS   B 1 91  ? 46.772 -8.440  -5.357  1.00 22.20 ?  91  HIS   B HD1  1 
ATOM   5217 H HD2  . HIS   B 1 91  ? 44.380 -9.391  -8.278  1.00 22.04 ?  91  HIS   B HD2  1 
ATOM   5218 H HE1  . HIS   B 1 91  ? 46.137 -6.400  -6.368  1.00 23.39 ?  91  HIS   B HE1  1 
ATOM   5219 N N    . CYS   B 1 92  ? 47.520 -12.906 -4.552  1.00 10.18 ?  92  CYS   B N    1 
ATOM   5220 C CA   . CYS   B 1 92  ? 47.218 -14.143 -3.843  1.00 9.91  ?  92  CYS   B CA   1 
ATOM   5221 C C    . CYS   B 1 92  ? 46.001 -13.912 -2.956  1.00 9.72  ?  92  CYS   B C    1 
ATOM   5222 O O    . CYS   B 1 92  ? 46.000 -13.013 -2.104  1.00 10.65 ?  92  CYS   B O    1 
ATOM   5223 C CB   . CYS   B 1 92  ? 48.398 -14.603 -2.993  1.00 10.51 ?  92  CYS   B CB   1 
ATOM   5224 S SG   . CYS   B 1 92  ? 48.042 -16.138 -2.098  1.00 10.85 ?  92  CYS   B SG   1 
ATOM   5225 H H    . CYS   B 1 92  ? 47.844 -12.286 -4.045  1.00 12.22 ?  92  CYS   B H    1 
ATOM   5226 H HA   . CYS   B 1 92  ? 47.019 -14.839 -4.490  1.00 11.90 ?  92  CYS   B HA   1 
ATOM   5227 H HB2  . CYS   B 1 92  ? 49.164 -14.756 -3.564  1.00 12.61 ?  92  CYS   B HB2  1 
ATOM   5228 H HB3  . CYS   B 1 92  ? 48.600 -13.915 -2.339  1.00 12.61 ?  92  CYS   B HB3  1 
ATOM   5229 H HG   . CYS   B 1 92  ? 49.014 -16.447 -1.466  1.00 13.02 ?  92  CYS   B HG   1 
ATOM   5230 N N    . LEU   B 1 93  ? 44.961 -14.719 -3.173  1.00 9.50  ?  93  LEU   B N    1 
ATOM   5231 C CA   . LEU   B 1 93  ? 43.784 -14.737 -2.313  1.00 9.82  ?  93  LEU   B CA   1 
ATOM   5232 C C    . LEU   B 1 93  ? 44.005 -15.803 -1.248  1.00 9.22  ?  93  LEU   B C    1 
ATOM   5233 O O    . LEU   B 1 93  ? 43.952 -17.004 -1.540  1.00 9.80  ?  93  LEU   B O    1 
ATOM   5234 C CB   . LEU   B 1 93  ? 42.520 -15.025 -3.121  1.00 10.13 ?  93  LEU   B CB   1 
ATOM   5235 C CG   . LEU   B 1 93  ? 41.218 -15.049 -2.315  1.00 10.93 ?  93  LEU   B CG   1 
ATOM   5236 C CD1  . LEU   B 1 93  ? 40.858 -13.659 -1.823  1.00 11.33 ?  93  LEU   B CD1  1 
ATOM   5237 C CD2  . LEU   B 1 93  ? 40.095 -15.635 -3.148  1.00 11.03 ?  93  LEU   B CD2  1 
ATOM   5238 H H    . LEU   B 1 93  ? 44.919 -15.289 -3.830  1.00 11.40 ?  93  LEU   B H    1 
ATOM   5239 H HA   . LEU   B 1 93  ? 43.694 -13.875 -1.882  1.00 11.78 ?  93  LEU   B HA   1 
ATOM   5240 H HB2  . LEU   B 1 93  ? 42.427 -14.335 -3.800  1.00 12.15 ?  93  LEU   B HB2  1 
ATOM   5241 H HB3  . LEU   B 1 93  ? 42.614 -15.887 -3.546  1.00 12.15 ?  93  LEU   B HB3  1 
ATOM   5242 H HG   . LEU   B 1 93  ? 41.337 -15.612 -1.537  1.00 13.11 ?  93  LEU   B HG   1 
ATOM   5243 H HD11 . LEU   B 1 93  ? 40.008 -13.693 -1.360  1.00 13.59 ?  93  LEU   B HD11 1 
ATOM   5244 H HD12 . LEU   B 1 93  ? 41.552 -13.343 -1.222  1.00 13.59 ?  93  LEU   B HD12 1 
ATOM   5245 H HD13 . LEU   B 1 93  ? 40.792 -13.059 -2.588  1.00 13.59 ?  93  LEU   B HD13 1 
ATOM   5246 H HD21 . LEU   B 1 93  ? 39.279 -15.634 -2.624  1.00 13.23 ?  93  LEU   B HD21 1 
ATOM   5247 H HD22 . LEU   B 1 93  ? 39.977 -15.092 -3.945  1.00 13.23 ?  93  LEU   B HD22 1 
ATOM   5248 H HD23 . LEU   B 1 93  ? 40.329 -16.542 -3.398  1.00 13.23 ?  93  LEU   B HD23 1 
ATOM   5249 N N    . HIS   B 1 94  ? 44.280 -15.366 -0.025  1.00 9.41  ?  94  HIS   B N    1 
ATOM   5250 C CA   . HIS   B 1 94  ? 44.498 -16.275 1.093   1.00 9.44  ?  94  HIS   B CA   1 
ATOM   5251 C C    . HIS   B 1 94  ? 43.137 -16.635 1.665   1.00 9.74  ?  94  HIS   B C    1 
ATOM   5252 O O    . HIS   B 1 94  ? 42.466 -15.760 2.212   1.00 11.36 ?  94  HIS   B O    1 
ATOM   5253 C CB   . HIS   B 1 94  ? 45.368 -15.598 2.154   1.00 10.02 ?  94  HIS   B CB   1 
ATOM   5254 C CG   . HIS   B 1 94  ? 46.750 -15.296 1.687   1.00 10.07 ?  94  HIS   B CG   1 
ATOM   5255 N ND1  . HIS   B 1 94  ? 47.778 -16.210 1.774   1.00 10.34 ?  94  HIS   B ND1  1 
ATOM   5256 C CD2  . HIS   B 1 94  ? 47.257 -14.187 1.096   1.00 10.46 ?  94  HIS   B CD2  1 
ATOM   5257 C CE1  . HIS   B 1 94  ? 48.868 -15.657 1.270   1.00 10.47 ?  94  HIS   B CE1  1 
ATOM   5258 N NE2  . HIS   B 1 94  ? 48.582 -14.433 0.854   1.00 10.60 ?  94  HIS   B NE2  1 
ATOM   5259 H H    . HIS   B 1 94  ? 44.346 -14.530 0.184   1.00 11.29 ?  94  HIS   B H    1 
ATOM   5260 H HA   . HIS   B 1 94  ? 44.938 -17.082 0.781   1.00 11.32 ?  94  HIS   B HA   1 
ATOM   5261 H HB2  . HIS   B 1 94  ? 44.951 -14.765 2.412   1.00 12.02 ?  94  HIS   B HB2  1 
ATOM   5262 H HB3  . HIS   B 1 94  ? 45.436 -16.189 2.918   1.00 12.02 ?  94  HIS   B HB3  1 
ATOM   5263 H HD2  . HIS   B 1 94  ? 46.802 -13.403 0.899   1.00 12.55 ?  94  HIS   B HD2  1 
ATOM   5264 H HE1  . HIS   B 1 94  ? 49.704 -16.070 1.220   1.00 12.57 ?  94  HIS   B HE1  1 
ATOM   5265 H HE2  . HIS   B 1 94  ? 49.141 -13.891 0.490   1.00 12.72 ?  94  HIS   B HE2  1 
ATOM   5266 N N    . VAL   B 1 95  ? 42.710 -17.893 1.522   1.00 9.70  ?  95  VAL   B N    1 
ATOM   5267 C CA   . VAL   B 1 95  ? 41.381 -18.331 1.952   1.00 9.87  ?  95  VAL   B CA   1 
ATOM   5268 C C    . VAL   B 1 95  ? 41.548 -19.369 3.049   1.00 10.11 ?  95  VAL   B C    1 
ATOM   5269 O O    . VAL   B 1 95  ? 42.322 -20.320 2.893   1.00 10.65 ?  95  VAL   B O    1 
ATOM   5270 C CB   . VAL   B 1 95  ? 40.560 -18.929 0.792   1.00 10.20 ?  95  VAL   B CB   1 
ATOM   5271 C CG1  . VAL   B 1 95  ? 39.177 -19.380 1.273   1.00 11.24 ?  95  VAL   B CG1  1 
ATOM   5272 C CG2  . VAL   B 1 95  ? 40.437 -17.946 -0.352  1.00 10.45 ?  95  VAL   B CG2  1 
ATOM   5273 H H    . VAL   B 1 95  ? 43.176 -18.521 1.167   1.00 11.64 ?  95  VAL   B H    1 
ATOM   5274 H HA   . VAL   B 1 95  ? 40.888 -17.576 2.317   1.00 11.85 ?  95  VAL   B HA   1 
ATOM   5275 H HB   . VAL   B 1 95  ? 41.020 -19.709 0.456   1.00 12.24 ?  95  VAL   B HB   1 
ATOM   5276 H HG11 . VAL   B 1 95  ? 38.621 -19.583 0.499   1.00 13.49 ?  95  VAL   B HG11 1 
ATOM   5277 H HG12 . VAL   B 1 95  ? 39.272 -20.177 1.820   1.00 13.49 ?  95  VAL   B HG12 1 
ATOM   5278 H HG13 . VAL   B 1 95  ? 38.767 -18.670 1.790   1.00 13.49 ?  95  VAL   B HG13 1 
ATOM   5279 H HG21 . VAL   B 1 95  ? 39.865 -18.329 -1.035  1.00 12.54 ?  95  VAL   B HG21 1 
ATOM   5280 H HG22 . VAL   B 1 95  ? 40.049 -17.122 -0.018  1.00 12.54 ?  95  VAL   B HG22 1 
ATOM   5281 H HG23 . VAL   B 1 95  ? 41.319 -17.776 -0.713  1.00 12.54 ?  95  VAL   B HG23 1 
ATOM   5282 N N    . VAL   B 1 96  ? 40.813 -19.200 4.142   1.00 10.60 ?  96  VAL   B N    1 
ATOM   5283 C CA   . VAL   B 1 96  ? 40.895 -20.112 5.281   1.00 10.77 ?  96  VAL   B CA   1 
ATOM   5284 C C    . VAL   B 1 96  ? 39.707 -21.072 5.234   1.00 11.06 ?  96  VAL   B C    1 
ATOM   5285 O O    . VAL   B 1 96  ? 38.586 -20.718 5.611   1.00 11.79 ?  96  VAL   B O    1 
ATOM   5286 C CB   . VAL   B 1 96  ? 40.944 -19.363 6.616   1.00 11.47 ?  96  VAL   B CB   1 
ATOM   5287 C CG1  . VAL   B 1 96  ? 41.109 -20.354 7.762   1.00 12.30 ?  96  VAL   B CG1  1 
ATOM   5288 C CG2  . VAL   B 1 96  ? 42.062 -18.325 6.630   1.00 12.32 ?  96  VAL   B CG2  1 
ATOM   5289 H H    . VAL   B 1 96  ? 40.255 -18.559 4.255   1.00 12.72 ?  96  VAL   B H    1 
ATOM   5290 H HA   . VAL   B 1 96  ? 41.711 -20.638 5.211   1.00 12.92 ?  96  VAL   B HA   1 
ATOM   5291 H HB   . VAL   B 1 96  ? 40.103 -18.896 6.748   1.00 13.76 ?  96  VAL   B HB   1 
ATOM   5292 H HG11 . VAL   B 1 96  ? 41.298 -19.861 8.581   1.00 14.76 ?  96  VAL   B HG11 1 
ATOM   5293 H HG12 . VAL   B 1 96  ? 40.291 -20.860 7.869   1.00 14.76 ?  96  VAL   B HG12 1 
ATOM   5294 H HG13 . VAL   B 1 96  ? 41.849 -20.948 7.563   1.00 14.76 ?  96  VAL   B HG13 1 
ATOM   5295 H HG21 . VAL   B 1 96  ? 42.104 -17.907 7.509   1.00 14.78 ?  96  VAL   B HG21 1 
ATOM   5296 H HG22 . VAL   B 1 96  ? 42.906 -18.756 6.432   1.00 14.78 ?  96  VAL   B HG22 1 
ATOM   5297 H HG23 . VAL   B 1 96  ? 41.875 -17.643 5.959   1.00 14.78 ?  96  VAL   B HG23 1 
ATOM   5298 N N    . GLY   B 1 97  ? 39.943 -22.307 4.799   1.00 11.32 ?  97  GLY   B N    1 
ATOM   5299 C CA   . GLY   B 1 97  ? 38.965 -23.361 4.954   1.00 11.80 ?  97  GLY   B CA   1 
ATOM   5300 C C    . GLY   B 1 97  ? 39.080 -23.974 6.331   1.00 12.42 ?  97  GLY   B C    1 
ATOM   5301 O O    . GLY   B 1 97  ? 40.122 -23.866 6.989   1.00 13.02 ?  97  GLY   B O    1 
ATOM   5302 H H    . GLY   B 1 97  ? 40.675 -22.554 4.411   1.00 13.58 ?  97  GLY   B H    1 
ATOM   5303 H HA2  . GLY   B 1 97  ? 38.074 -22.991 4.835   1.00 14.16 ?  97  GLY   B HA2  1 
ATOM   5304 H HA3  . GLY   B 1 97  ? 39.110 -24.045 4.281   1.00 14.16 ?  97  GLY   B HA3  1 
ATOM   5305 N N    . PRO   B 1 98  ? 38.032 -24.664 6.786   1.00 13.05 ?  98  PRO   B N    1 
ATOM   5306 C CA   . PRO   B 1 98  ? 38.125 -25.361 8.071   1.00 13.85 ?  98  PRO   B CA   1 
ATOM   5307 C C    . PRO   B 1 98  ? 39.154 -26.479 8.029   1.00 13.19 ?  98  PRO   B C    1 
ATOM   5308 O O    . PRO   B 1 98  ? 39.265 -27.217 7.050   1.00 13.67 ?  98  PRO   B O    1 
ATOM   5309 C CB   . PRO   B 1 98  ? 36.710 -25.909 8.276   1.00 14.39 ?  98  PRO   B CB   1 
ATOM   5310 C CG   . PRO   B 1 98  ? 36.147 -26.029 6.900   1.00 13.97 ?  98  PRO   B CG   1 
ATOM   5311 C CD   . PRO   B 1 98  ? 36.714 -24.847 6.154   1.00 13.11 ?  98  PRO   B CD   1 
ATOM   5312 H HA   . PRO   B 1 98  ? 38.343 -24.742 8.778   1.00 16.62 ?  98  PRO   B HA   1 
ATOM   5313 H HB2  . PRO   B 1 98  ? 36.752 -26.781 8.704   1.00 17.26 ?  98  PRO   B HB2  1 
ATOM   5314 H HB3  . PRO   B 1 98  ? 36.190 -25.289 8.805   1.00 17.26 ?  98  PRO   B HB3  1 
ATOM   5315 H HG2  . PRO   B 1 98  ? 36.438 -26.866 6.500   1.00 16.76 ?  98  PRO   B HG2  1 
ATOM   5316 H HG3  . PRO   B 1 98  ? 35.180 -25.985 6.939   1.00 16.76 ?  98  PRO   B HG3  1 
ATOM   5317 H HD2  . PRO   B 1 98  ? 36.809 -25.058 5.207   1.00 15.73 ?  98  PRO   B HD2  1 
ATOM   5318 H HD3  . PRO   B 1 98  ? 36.165 -24.061 6.288   1.00 15.73 ?  98  PRO   B HD3  1 
ATOM   5319 N N    . ASN   B 1 99  ? 39.899 -26.606 9.119   1.00 14.03 ?  99  ASN   B N    1 
ATOM   5320 C CA   . ASN   B 1 99  ? 40.879 -27.678 9.285   1.00 14.90 ?  99  ASN   B CA   1 
ATOM   5321 C C    . ASN   B 1 99  ? 40.244 -28.762 10.156  1.00 17.17 ?  99  ASN   B C    1 
ATOM   5322 O O    . ASN   B 1 99  ? 40.151 -28.617 11.376  1.00 17.79 ?  99  ASN   B O    1 
ATOM   5323 C CB   . ASN   B 1 99  ? 42.150 -27.121 9.913   1.00 15.65 ?  99  ASN   B CB   1 
ATOM   5324 C CG   . ASN   B 1 99  ? 43.282 -28.125 9.920   1.00 16.57 ?  99  ASN   B CG   1 
ATOM   5325 O OD1  . ASN   B 1 99  ? 43.058 -29.320 10.092  1.00 17.50 ?  99  ASN   B OD1  1 
ATOM   5326 N ND2  . ASN   B 1 99  ? 44.506 -27.645 9.723   1.00 17.05 ?  99  ASN   B ND2  1 
ATOM   5327 H H    . ASN   B 1 99  ? 39.860 -26.071 9.789   1.00 16.84 ?  99  ASN   B H    1 
ATOM   5328 H HA   . ASN   B 1 99  ? 41.098 -28.065 8.424   1.00 17.89 ?  99  ASN   B HA   1 
ATOM   5329 H HB2  . ASN   B 1 99  ? 42.434 -26.345 9.412   1.00 18.78 ?  99  ASN   B HB2  1 
ATOM   5330 H HB3  . ASN   B 1 99  ? 41.962 -26.875 10.834  1.00 18.78 ?  99  ASN   B HB3  1 
ATOM   5331 H HD21 . ASN   B 1 99  ? 45.182 -28.172 9.715   1.00 20.46 ?  99  ASN   B HD21 1 
ATOM   5332 H HD22 . ASN   B 1 99  ? 44.619 -26.798 9.605   1.00 20.46 ?  99  ASN   B HD22 1 
ATOM   5333 N N    A VAL   B 1 100 ? 39.783 -29.840 9.515   0.74 18.98 ?  100 VAL   B N    1 
ATOM   5334 N N    B VAL   B 1 100 ? 39.794 -29.844 9.515   0.26 19.14 ?  100 VAL   B N    1 
ATOM   5335 C CA   A VAL   B 1 100 ? 39.151 -30.936 10.249  0.74 21.65 ?  100 VAL   B CA   1 
ATOM   5336 C CA   B VAL   B 1 100 ? 39.159 -30.941 10.243  0.26 21.37 ?  100 VAL   B CA   1 
ATOM   5337 C C    A VAL   B 1 100 ? 40.144 -31.622 11.180  0.74 22.04 ?  100 VAL   B C    1 
ATOM   5338 C C    B VAL   B 1 100 ? 40.148 -31.614 11.183  0.26 22.06 ?  100 VAL   B C    1 
ATOM   5339 O O    A VAL   B 1 100 ? 39.756 -32.156 12.226  0.74 22.40 ?  100 VAL   B O    1 
ATOM   5340 O O    B VAL   B 1 100 ? 39.763 -32.116 12.246  0.26 22.29 ?  100 VAL   B O    1 
ATOM   5341 C CB   A VAL   B 1 100 ? 38.496 -31.929 9.266   0.74 24.49 ?  100 VAL   B CB   1 
ATOM   5342 C CB   B VAL   B 1 100 ? 38.526 -31.940 9.253   0.26 23.02 ?  100 VAL   B CB   1 
ATOM   5343 C CG1  A VAL   B 1 100 ? 38.027 -33.180 9.994   0.74 25.61 ?  100 VAL   B CG1  1 
ATOM   5344 C CG1  B VAL   B 1 100 ? 37.999 -33.169 9.984   0.26 23.67 ?  100 VAL   B CG1  1 
ATOM   5345 C CG2  A VAL   B 1 100 ? 37.333 -31.269 8.539   0.74 25.28 ?  100 VAL   B CG2  1 
ATOM   5346 C CG2  B VAL   B 1 100 ? 37.411 -31.267 8.470   0.26 23.49 ?  100 VAL   B CG2  1 
ATOM   5347 H H    A VAL   B 1 100 ? 39.810 -29.951 8.662   0.74 22.77 ?  100 VAL   B H    1 
ATOM   5348 H H    B VAL   B 1 100 ? 39.843 -29.964 8.665   0.26 22.96 ?  100 VAL   B H    1 
ATOM   5349 H HA   A VAL   B 1 100 ? 38.441 -30.566 10.797  0.74 25.98 ?  100 VAL   B HA   1 
ATOM   5350 H HA   B VAL   B 1 100 ? 38.443 -30.578 10.785  0.26 25.65 ?  100 VAL   B HA   1 
ATOM   5351 H HB   A VAL   B 1 100 ? 39.152 -32.198 8.607   0.74 29.39 ?  100 VAL   B HB   1 
ATOM   5352 H HB   B VAL   B 1 100 ? 39.201 -32.235 8.623   0.26 27.63 ?  100 VAL   B HB   1 
ATOM   5353 H HG11 A VAL   B 1 100 ? 37.429 -33.676 9.411   0.74 30.73 ?  100 VAL   B HG11 1 
ATOM   5354 H HG11 B VAL   B 1 100 ? 37.421 -33.668 9.383   0.26 28.40 ?  100 VAL   B HG11 1 
ATOM   5355 H HG12 A VAL   B 1 100 ? 38.795 -33.729 10.217  0.74 30.73 ?  100 VAL   B HG12 1 
ATOM   5356 H HG12 B VAL   B 1 100 ? 38.746 -33.724 10.256  0.26 28.40 ?  100 VAL   B HG12 1 
ATOM   5357 H HG13 A VAL   B 1 100 ? 37.557 -32.921 10.802  0.74 30.73 ?  100 VAL   B HG13 1 
ATOM   5358 H HG13 B VAL   B 1 100 ? 37.495 -32.883 10.761  0.26 28.40 ?  100 VAL   B HG13 1 
ATOM   5359 H HG21 A VAL   B 1 100 ? 36.933 -31.915 7.934   0.74 30.33 ?  100 VAL   B HG21 1 
ATOM   5360 H HG21 B VAL   B 1 100 ? 37.006 -31.917 7.875   0.26 28.19 ?  100 VAL   B HG21 1 
ATOM   5361 H HG22 A VAL   B 1 100 ? 36.676 -30.979 9.192   0.74 30.33 ?  100 VAL   B HG22 1 
ATOM   5362 H HG22 B VAL   B 1 100 ? 36.748 -30.930 9.093   0.26 28.19 ?  100 VAL   B HG22 1 
ATOM   5363 H HG23 A VAL   B 1 100 ? 37.664 -30.509 8.040   0.74 30.33 ?  100 VAL   B HG23 1 
ATOM   5364 H HG23 B VAL   B 1 100 ? 37.785 -30.535 7.957   0.26 28.19 ?  100 VAL   B HG23 1 
ATOM   5365 N N    . ASN   B 1 101 ? 41.430 -31.645 10.812  1.00 22.43 ?  101 ASN   B N    1 
ATOM   5366 C CA   . ASN   B 1 101 ? 42.450 -32.195 11.703  1.00 24.38 ?  101 ASN   B CA   1 
ATOM   5367 C C    . ASN   B 1 101 ? 42.617 -31.369 12.973  1.00 26.08 ?  101 ASN   B C    1 
ATOM   5368 O O    . ASN   B 1 101 ? 43.226 -31.852 13.935  1.00 27.42 ?  101 ASN   B O    1 
ATOM   5369 C CB   . ASN   B 1 101 ? 43.790 -32.319 10.971  1.00 24.42 ?  101 ASN   B CB   1 
ATOM   5370 C CG   . ASN   B 1 101 ? 43.794 -33.443 9.954   1.00 24.07 ?  101 ASN   B CG   1 
ATOM   5371 O OD1  . ASN   B 1 101 ? 43.137 -34.459 10.145  1.00 25.07 ?  101 ASN   B OD1  1 
ATOM   5372 N ND2  . ASN   B 1 101 ? 44.530 -33.262 8.865   1.00 23.63 ?  101 ASN   B ND2  1 
ATOM   5373 H H    A ASN   B 1 101 ? 41.726 -31.372 10.053  0.74 26.91 ?  101 ASN   B H    1 
ATOM   5374 H H    B ASN   B 1 101 ? 41.726 -31.366 10.055  0.26 26.91 ?  101 ASN   B H    1 
ATOM   5375 H HA   . ASN   B 1 101 ? 42.180 -33.084 11.970  1.00 29.25 ?  101 ASN   B HA   1 
ATOM   5376 H HB2  . ASN   B 1 101 ? 43.981 -31.494 10.502  1.00 29.30 ?  101 ASN   B HB2  1 
ATOM   5377 H HB3  . ASN   B 1 101 ? 44.490 -32.499 11.622  1.00 29.30 ?  101 ASN   B HB3  1 
ATOM   5378 H HD21 . ASN   B 1 101 ? 44.565 -33.875 8.262   1.00 28.36 ?  101 ASN   B HD21 1 
ATOM   5379 H HD22 . ASN   B 1 101 ? 44.971 -32.532 8.761   1.00 28.36 ?  101 ASN   B HD22 1 
ATOM   5380 N N    . LYS   B 1 102 ? 42.105 -30.137 12.989  1.00 28.04 ?  102 LYS   B N    1 
ATOM   5381 C CA   . LYS   B 1 102 ? 42.073 -29.299 14.180  1.00 30.64 ?  102 LYS   B CA   1 
ATOM   5382 C C    . LYS   B 1 102 ? 40.688 -29.245 14.814  1.00 30.19 ?  102 LYS   B C    1 
ATOM   5383 O O    . LYS   B 1 102 ? 40.464 -28.437 15.720  1.00 31.16 ?  102 LYS   B O    1 
ATOM   5384 C CB   . LYS   B 1 102 ? 42.520 -27.875 13.844  1.00 34.09 ?  102 LYS   B CB   1 
ATOM   5385 C CG   . LYS   B 1 102 ? 43.987 -27.728 13.485  1.00 37.46 ?  102 LYS   B CG   1 
ATOM   5386 C CD   . LYS   B 1 102 ? 44.273 -26.308 13.020  1.00 40.51 ?  102 LYS   B CD   1 
ATOM   5387 C CE   . LYS   B 1 102 ? 45.759 -26.049 12.855  1.00 43.05 ?  102 LYS   B CE   1 
ATOM   5388 N NZ   . LYS   B 1 102 ? 46.017 -24.657 12.388  1.00 44.65 ?  102 LYS   B NZ   1 
ATOM   5389 H H    . LYS   B 1 102 ? 41.758 -29.755 12.300  1.00 33.65 ?  102 LYS   B H    1 
ATOM   5390 H HA   . LYS   B 1 102 ? 42.694 -29.656 14.833  1.00 36.77 ?  102 LYS   B HA   1 
ATOM   5391 H HB2  . LYS   B 1 102 ? 42.002 -27.556 13.089  1.00 40.91 ?  102 LYS   B HB2  1 
ATOM   5392 H HB3  . LYS   B 1 102 ? 42.352 -27.307 14.615  1.00 40.91 ?  102 LYS   B HB3  1 
ATOM   5393 H HG2  . LYS   B 1 102 ? 44.534 -27.912 14.265  1.00 44.96 ?  102 LYS   B HG2  1 
ATOM   5394 H HG3  . LYS   B 1 102 ? 44.207 -28.339 12.764  1.00 44.96 ?  102 LYS   B HG3  1 
ATOM   5395 H HD2  . LYS   B 1 102 ? 43.843 -26.162 12.162  1.00 48.61 ?  102 LYS   B HD2  1 
ATOM   5396 H HD3  . LYS   B 1 102 ? 43.927 -25.683 13.677  1.00 48.61 ?  102 LYS   B HD3  1 
ATOM   5397 H HE2  . LYS   B 1 102 ? 46.202 -26.170 13.710  1.00 51.67 ?  102 LYS   B HE2  1 
ATOM   5398 H HE3  . LYS   B 1 102 ? 46.121 -26.664 12.199  1.00 51.67 ?  102 LYS   B HE3  1 
ATOM   5399 H HZ1  . LYS   B 1 102 ? 46.892 -24.524 12.298  1.00 53.58 ?  102 LYS   B HZ1  1 
ATOM   5400 H HZ2  . LYS   B 1 102 ? 45.621 -24.522 11.602  1.00 53.58 ?  102 LYS   B HZ2  1 
ATOM   5401 H HZ3  . LYS   B 1 102 ? 45.695 -24.073 12.978  1.00 53.58 ?  102 LYS   B HZ3  1 
ATOM   5402 N N    . GLY   B 1 103 ? 39.752 -30.066 14.348  1.00 29.26 ?  103 GLY   B N    1 
ATOM   5403 C CA   . GLY   B 1 103 ? 38.419 -30.104 14.916  1.00 28.76 ?  103 GLY   B CA   1 
ATOM   5404 C C    . GLY   B 1 103 ? 37.493 -28.999 14.462  1.00 27.50 ?  103 GLY   B C    1 
ATOM   5405 O O    . GLY   B 1 103 ? 36.417 -28.833 15.049  1.00 28.01 ?  103 GLY   B O    1 
ATOM   5406 H H    . GLY   B 1 103 ? 39.869 -30.613 13.697  1.00 35.12 ?  103 GLY   B H    1 
ATOM   5407 H HA2  . GLY   B 1 103 ? 38.004 -30.948 14.682  1.00 34.51 ?  103 GLY   B HA2  1 
ATOM   5408 H HA3  . GLY   B 1 103 ? 38.490 -30.063 15.884  1.00 34.51 ?  103 GLY   B HA3  1 
ATOM   5409 N N    A GLU   B 1 104 ? 37.872 -28.236 13.441  0.74 25.91 ?  104 GLU   B N    1 
ATOM   5410 N N    B GLU   B 1 104 ? 37.862 -28.244 13.433  0.26 27.14 ?  104 GLU   B N    1 
ATOM   5411 C CA   A GLU   B 1 104 ? 37.052 -27.129 12.977  0.74 24.41 ?  104 GLU   B CA   1 
ATOM   5412 C CA   B GLU   B 1 104 ? 37.028 -27.146 12.970  0.26 26.61 ?  104 GLU   B CA   1 
ATOM   5413 C C    A GLU   B 1 104 ? 35.877 -27.640 12.148  0.74 25.02 ?  104 GLU   B C    1 
ATOM   5414 C C    B GLU   B 1 104 ? 35.868 -27.671 12.130  0.26 26.69 ?  104 GLU   B C    1 
ATOM   5415 O O    A GLU   B 1 104 ? 35.928 -28.719 11.549  0.74 25.97 ?  104 GLU   B O    1 
ATOM   5416 O O    B GLU   B 1 104 ? 35.952 -28.732 11.503  0.26 26.96 ?  104 GLU   B O    1 
ATOM   5417 C CB   A GLU   B 1 104 ? 37.908 -26.137 12.186  0.74 22.92 ?  104 GLU   B CB   1 
ATOM   5418 C CB   B GLU   B 1 104 ? 37.869 -26.145 12.178  0.26 26.00 ?  104 GLU   B CB   1 
ATOM   5419 C CG   A GLU   B 1 104 ? 39.035 -25.554 13.035  0.74 21.81 ?  104 GLU   B CG   1 
ATOM   5420 C CG   B GLU   B 1 104 ? 38.973 -25.518 13.020  0.26 25.50 ?  104 GLU   B CG   1 
ATOM   5421 C CD   A GLU   B 1 104 ? 39.967 -24.628 12.283  0.74 20.48 ?  104 GLU   B CD   1 
ATOM   5422 C CD   B GLU   B 1 104 ? 39.909 -24.634 12.220  0.26 25.07 ?  104 GLU   B CD   1 
ATOM   5423 O OE1  A GLU   B 1 104 ? 39.974 -24.627 11.032  0.74 18.63 ?  104 GLU   B OE1  1 
ATOM   5424 O OE1  B GLU   B 1 104 ? 39.838 -24.650 10.973  0.26 24.68 ?  104 GLU   B OE1  1 
ATOM   5425 O OE2  A GLU   B 1 104 ? 40.711 -23.896 12.969  0.74 21.36 -1 104 GLU   B OE2  1 
ATOM   5426 O OE2  B GLU   B 1 104 ? 40.722 -23.922 12.845  0.26 25.21 -1 104 GLU   B OE2  1 
ATOM   5427 H H    A GLU   B 1 104 ? 38.608 -28.337 13.008  0.74 31.09 ?  104 GLU   B H    1 
ATOM   5428 H H    B GLU   B 1 104 ? 38.592 -28.347 12.990  0.26 32.57 ?  104 GLU   B H    1 
ATOM   5429 H HA   A GLU   B 1 104 ? 36.695 -26.658 13.748  0.74 29.30 ?  104 GLU   B HA   1 
ATOM   5430 H HA   B GLU   B 1 104 ? 36.659 -26.684 13.738  0.26 31.93 ?  104 GLU   B HA   1 
ATOM   5431 H HB2  A GLU   B 1 104 ? 38.307 -26.591 11.428  0.74 27.50 ?  104 GLU   B HB2  1 
ATOM   5432 H HB2  B GLU   B 1 104 ? 38.284 -26.600 11.429  0.26 31.20 ?  104 GLU   B HB2  1 
ATOM   5433 H HB3  A GLU   B 1 104 ? 37.351 -25.404 11.882  0.74 27.50 ?  104 GLU   B HB3  1 
ATOM   5434 H HB3  B GLU   B 1 104 ? 37.294 -25.432 11.857  0.26 31.20 ?  104 GLU   B HB3  1 
ATOM   5435 H HG2  A GLU   B 1 104 ? 38.652 -25.044 13.766  0.74 26.17 ?  104 GLU   B HG2  1 
ATOM   5436 H HG2  B GLU   B 1 104 ? 38.567 -24.975 13.715  0.26 30.60 ?  104 GLU   B HG2  1 
ATOM   5437 H HG3  A GLU   B 1 104 ? 39.576 -26.276 13.389  0.74 26.17 ?  104 GLU   B HG3  1 
ATOM   5438 H HG3  B GLU   B 1 104 ? 39.502 -26.224 13.423  0.26 30.60 ?  104 GLU   B HG3  1 
ATOM   5439 N N    A ASP   B 1 105 ? 34.807 -26.847 12.128  0.74 25.19 ?  105 ASP   B N    1 
ATOM   5440 N N    B ASP   B 1 105 ? 34.775 -26.911 12.127  0.26 26.51 ?  105 ASP   B N    1 
ATOM   5441 C CA   A ASP   B 1 105 ? 33.528 -27.294 11.587  0.74 25.98 ?  105 ASP   B CA   1 
ATOM   5442 C CA   B ASP   B 1 105 ? 33.519 -27.383 11.557  0.26 26.43 ?  105 ASP   B CA   1 
ATOM   5443 C C    A ASP   B 1 105 ? 33.579 -27.341 10.064  0.74 24.04 ?  105 ASP   B C    1 
ATOM   5444 C C    B ASP   B 1 105 ? 33.599 -27.401 10.034  0.26 25.57 ?  105 ASP   B C    1 
ATOM   5445 O O    A ASP   B 1 105 ? 33.710 -26.305 9.406   0.74 23.09 ?  105 ASP   B O    1 
ATOM   5446 O O    B ASP   B 1 105 ? 33.820 -26.362 9.402   0.26 25.24 ?  105 ASP   B O    1 
ATOM   5447 C CB   A ASP   B 1 105 ? 32.420 -26.350 12.055  0.74 28.95 ?  105 ASP   B CB   1 
ATOM   5448 C CB   B ASP   B 1 105 ? 32.376 -26.484 12.022  0.26 27.14 ?  105 ASP   B CB   1 
ATOM   5449 C CG   A ASP   B 1 105 ? 31.036 -26.822 11.645  0.74 31.48 ?  105 ASP   B CG   1 
ATOM   5450 C CG   B ASP   B 1 105 ? 31.010 -27.072 11.713  0.26 27.75 ?  105 ASP   B CG   1 
ATOM   5451 O OD1  A ASP   B 1 105 ? 30.928 -27.881 10.992  0.74 31.94 ?  105 ASP   B OD1  1 
ATOM   5452 O OD1  B ASP   B 1 105 ? 30.945 -28.065 10.958  0.26 27.89 ?  105 ASP   B OD1  1 
ATOM   5453 O OD2  A ASP   B 1 105 ? 30.049 -26.133 11.984  0.74 33.02 -1 105 ASP   B OD2  1 
ATOM   5454 O OD2  B ASP   B 1 105 ? 30.003 -26.550 12.236  0.26 27.95 -1 105 ASP   B OD2  1 
ATOM   5455 H H    A ASP   B 1 105 ? 34.803 -26.041 12.418  0.74 30.23 ?  105 ASP   B H    1 
ATOM   5456 H H    B ASP   B 1 105 ? 34.737 -26.115 12.447  0.26 31.81 ?  105 ASP   B H    1 
ATOM   5457 H HA   A ASP   B 1 105 ? 33.330 -28.183 11.916  0.74 31.18 ?  105 ASP   B HA   1 
ATOM   5458 H HA   B ASP   B 1 105 ? 33.339 -28.286 11.863  0.26 31.72 ?  105 ASP   B HA   1 
ATOM   5459 H HB2  A ASP   B 1 105 ? 32.448 -26.282 13.024  0.74 34.74 ?  105 ASP   B HB2  1 
ATOM   5460 H HB2  B ASP   B 1 105 ? 32.440 -26.362 12.983  0.26 32.57 ?  105 ASP   B HB2  1 
ATOM   5461 H HB3  A ASP   B 1 105 ? 32.562 -25.473 11.662  0.74 34.74 ?  105 ASP   B HB3  1 
ATOM   5462 H HB3  B ASP   B 1 105 ? 32.448 -25.623 11.576  0.26 32.57 ?  105 ASP   B HB3  1 
ATOM   5463 N N    A ILE   B 1 106 ? 33.453 -28.548 9.506   0.74 23.55 ?  106 ILE   B N    1 
ATOM   5464 N N    B ILE   B 1 106 ? 33.409 -28.586 9.447   0.26 25.14 ?  106 ILE   B N    1 
ATOM   5465 C CA   A ILE   B 1 106 ? 33.444 -28.724 8.058   0.74 22.56 ?  106 ILE   B CA   1 
ATOM   5466 C CA   B ILE   B 1 106 ? 33.424 -28.734 7.997   0.26 24.71 ?  106 ILE   B CA   1 
ATOM   5467 C C    A ILE   B 1 106 ? 32.345 -27.900 7.395   0.74 21.35 ?  106 ILE   B C    1 
ATOM   5468 C C    B ILE   B 1 106 ? 32.328 -27.909 7.334   0.26 24.14 ?  106 ILE   B C    1 
ATOM   5469 O O    A ILE   B 1 106 ? 32.444 -27.574 6.207   0.74 20.18 ?  106 ILE   B O    1 
ATOM   5470 O O    B ILE   B 1 106 ? 32.419 -27.605 6.139   0.26 23.90 ?  106 ILE   B O    1 
ATOM   5471 C CB   A ILE   B 1 106 ? 33.337 -30.231 7.725   0.74 23.71 ?  106 ILE   B CB   1 
ATOM   5472 C CB   B ILE   B 1 106 ? 33.327 -30.233 7.628   0.26 25.01 ?  106 ILE   B CB   1 
ATOM   5473 C CG1  A ILE   B 1 106 ? 33.586 -30.484 6.238   0.74 24.23 ?  106 ILE   B CG1  1 
ATOM   5474 C CG1  B ILE   B 1 106 ? 33.589 -30.449 6.135   0.26 25.08 ?  106 ILE   B CG1  1 
ATOM   5475 C CG2  A ILE   B 1 106 ? 31.979 -30.780 8.149   0.74 24.67 ?  106 ILE   B CG2  1 
ATOM   5476 C CG2  B ILE   B 1 106 ? 31.966 -30.795 8.018   0.26 25.34 ?  106 ILE   B CG2  1 
ATOM   5477 C CD1  A ILE   B 1 106 ? 34.947 -30.027 5.771   0.74 24.51 ?  106 ILE   B CD1  1 
ATOM   5478 C CD1  B ILE   B 1 106 ? 34.954 -29.981 5.685   0.26 25.14 ?  106 ILE   B CD1  1 
ATOM   5479 H H    A ILE   B 1 106 ? 33.378 -29.276 9.949   0.74 28.27 ?  106 ILE   B H    1 
ATOM   5480 H H    B ILE   B 1 106 ? 33.278 -29.319 9.872   0.26 30.17 ?  106 ILE   B H    1 
ATOM   5481 H HA   A ILE   B 1 106 ? 34.290 -28.404 7.712   0.74 27.08 ?  106 ILE   B HA   1 
ATOM   5482 H HA   B ILE   B 1 106 ? 34.271 -28.403 7.669   0.26 29.66 ?  106 ILE   B HA   1 
ATOM   5483 H HB   A ILE   B 1 106 ? 34.021 -30.701 8.230   0.74 28.46 ?  106 ILE   B HB   1 
ATOM   5484 H HB   B ILE   B 1 106 ? 34.006 -30.713 8.126   0.26 30.02 ?  106 ILE   B HB   1 
ATOM   5485 H HG12 A ILE   B 1 106 ? 33.522 -31.439 6.067   0.74 29.08 ?  106 ILE   B HG12 1 
ATOM   5486 H HG12 B ILE   B 1 106 ? 33.526 -31.399 5.942   0.26 30.10 ?  106 ILE   B HG12 1 
ATOM   5487 H HG13 A ILE   B 1 106 ? 32.918 -30.012 5.720   0.74 29.08 ?  106 ILE   B HG13 1 
ATOM   5488 H HG13 B ILE   B 1 106 ? 32.924 -29.966 5.623   0.26 30.10 ?  106 ILE   B HG13 1 
ATOM   5489 H HG21 A ILE   B 1 106 ? 31.987 -31.746 8.057   0.74 29.61 ?  106 ILE   B HG21 1 
ATOM   5490 H HG21 B ILE   B 1 106 ? 31.980 -31.759 7.910   0.26 30.41 ?  106 ILE   B HG21 1 
ATOM   5491 H HG22 A ILE   B 1 106 ? 31.815 -30.540 9.075   0.74 29.61 ?  106 ILE   B HG22 1 
ATOM   5492 H HG22 B ILE   B 1 106 ? 31.786 -30.570 8.945   0.26 30.41 ?  106 ILE   B HG22 1 
ATOM   5493 H HG23 A ILE   B 1 106 ? 31.291 -30.400 7.582   0.74 29.61 ?  106 ILE   B HG23 1 
ATOM   5494 H HG23 B ILE   B 1 106 ? 31.285 -30.408 7.446   0.26 30.41 ?  106 ILE   B HG23 1 
ATOM   5495 H HD11 A ILE   B 1 106 ? 35.145 -30.440 4.918   0.74 29.42 ?  106 ILE   B HD11 1 
ATOM   5496 H HD11 B ILE   B 1 106 ? 35.147 -30.364 4.816   0.26 30.17 ?  106 ILE   B HD11 1 
ATOM   5497 H HD12 A ILE   B 1 106 ? 34.941 -29.060 5.677   0.74 29.42 ?  106 ILE   B HD12 1 
ATOM   5498 H HD12 B ILE   B 1 106 ? 34.953 -29.013 5.627   0.26 30.17 ?  106 ILE   B HD12 1 
ATOM   5499 H HD13 A ILE   B 1 106 ? 35.612 -30.290 6.428   0.74 29.42 ?  106 ILE   B HD13 1 
ATOM   5500 H HD13 B ILE   B 1 106 ? 35.617 -30.275 6.330   0.26 30.17 ?  106 ILE   B HD13 1 
ATOM   5501 N N    A GLN   B 1 107 ? 31.305 -27.524 8.143   0.74 22.27 ?  107 GLN   B N    1 
ATOM   5502 N N    B GLN   B 1 107 ? 31.288 -27.532 8.083   0.26 24.05 ?  107 GLN   B N    1 
ATOM   5503 C CA   A GLN   B 1 107 ? 30.223 -26.734 7.565   0.74 23.11 ?  107 GLN   B CA   1 
ATOM   5504 C CA   B GLN   B 1 107 ? 30.209 -26.727 7.521   0.26 23.96 ?  107 GLN   B CA   1 
ATOM   5505 C C    A GLN   B 1 107 ? 30.710 -25.390 7.032   0.74 21.06 ?  107 GLN   B C    1 
ATOM   5506 C C    B GLN   B 1 107 ? 30.694 -25.362 7.039   0.26 21.57 ?  107 GLN   B C    1 
ATOM   5507 O O    A GLN   B 1 107 ? 30.080 -24.829 6.131   0.74 21.56 ?  107 GLN   B O    1 
ATOM   5508 O O    B GLN   B 1 107 ? 30.034 -24.748 6.195   0.26 21.83 ?  107 GLN   B O    1 
ATOM   5509 C CB   A GLN   B 1 107 ? 29.118 -26.530 8.607   0.74 27.14 ?  107 GLN   B CB   1 
ATOM   5510 C CB   B GLN   B 1 107 ? 29.097 -26.560 8.562   0.26 26.44 ?  107 GLN   B CB   1 
ATOM   5511 C CG   A GLN   B 1 107 ? 27.794 -26.027 8.042   0.74 31.26 ?  107 GLN   B CG   1 
ATOM   5512 C CG   B GLN   B 1 107 ? 27.770 -26.060 8.002   0.26 28.79 ?  107 GLN   B CG   1 
ATOM   5513 C CD   A GLN   B 1 107 ? 27.730 -24.513 7.941   0.74 34.54 ?  107 GLN   B CD   1 
ATOM   5514 C CD   B GLN   B 1 107 ? 27.662 -24.546 8.000   0.26 30.65 ?  107 GLN   B CD   1 
ATOM   5515 O OE1  A GLN   B 1 107 ? 28.575 -23.804 8.492   0.74 35.73 ?  107 GLN   B OE1  1 
ATOM   5516 O OE1  B GLN   B 1 107 ? 28.500 -23.849 8.573   0.26 31.32 ?  107 GLN   B OE1  1 
ATOM   5517 N NE2  A GLN   B 1 107 ? 26.721 -24.011 7.236   0.74 35.70 ?  107 GLN   B NE2  1 
ATOM   5518 N NE2  B GLN   B 1 107 ? 26.620 -24.029 7.356   0.26 31.31 ?  107 GLN   B NE2  1 
ATOM   5519 H H    A GLN   B 1 107 ? 31.215 -27.693 8.978   0.74 26.73 ?  107 GLN   B H    1 
ATOM   5520 H H    B GLN   B 1 107 ? 31.183 -27.734 8.911   0.26 28.87 ?  107 GLN   B H    1 
ATOM   5521 H HA   A GLN   B 1 107 ? 29.840 -27.230 6.825   0.74 27.73 ?  107 GLN   B HA   1 
ATOM   5522 H HA   B GLN   B 1 107 ? 29.832 -27.198 6.759   0.26 28.75 ?  107 GLN   B HA   1 
ATOM   5523 H HB2  A GLN   B 1 107 ? 28.945 -27.378 9.040   0.74 32.57 ?  107 GLN   B HB2  1 
ATOM   5524 H HB2  B GLN   B 1 107 ? 28.929 -27.420 8.976   0.26 31.73 ?  107 GLN   B HB2  1 
ATOM   5525 H HB3  A GLN   B 1 107 ? 29.425 -25.885 9.264   0.74 32.57 ?  107 GLN   B HB3  1 
ATOM   5526 H HB3  B GLN   B 1 107 ? 29.392 -25.928 9.236   0.26 31.73 ?  107 GLN   B HB3  1 
ATOM   5527 H HG2  A GLN   B 1 107 ? 27.668 -26.388 7.151   0.74 37.51 ?  107 GLN   B HG2  1 
ATOM   5528 H HG2  B GLN   B 1 107 ? 27.675 -26.366 7.087   0.26 34.55 ?  107 GLN   B HG2  1 
ATOM   5529 H HG3  A GLN   B 1 107 ? 27.070 -26.322 8.622   0.74 37.51 ?  107 GLN   B HG3  1 
ATOM   5530 H HG3  B GLN   B 1 107 ? 27.044 -26.413 8.545   0.26 34.55 ?  107 GLN   B HG3  1 
ATOM   5531 H HE21 A GLN   B 1 107 ? 26.150 -24.537 6.863   0.74 42.84 ?  107 GLN   B HE21 1 
ATOM   5532 H HE21 B GLN   B 1 107 ? 26.054 -24.547 6.966   0.26 37.57 ?  107 GLN   B HE21 1 
ATOM   5533 H HE22 A GLN   B 1 107 ? 26.636 -23.159 7.152   0.74 42.84 ?  107 GLN   B HE22 1 
ATOM   5534 H HE22 B GLN   B 1 107 ? 26.512 -23.177 7.329   0.26 37.57 ?  107 GLN   B HE22 1 
ATOM   5535 N N    . LEU   B 1 108 ? 31.829 -24.877 7.546   1.00 19.15 ?  108 LEU   B N    1 
ATOM   5536 C CA   . LEU   B 1 108 ? 32.380 -23.583 7.139   1.00 16.70 ?  108 LEU   B CA   1 
ATOM   5537 C C    . LEU   B 1 108 ? 33.034 -23.604 5.764   1.00 14.71 ?  108 LEU   B C    1 
ATOM   5538 O O    . LEU   B 1 108 ? 33.461 -22.544 5.277   1.00 14.37 ?  108 LEU   B O    1 
ATOM   5539 C CB   . LEU   B 1 108 ? 33.388 -23.102 8.181   1.00 17.09 ?  108 LEU   B CB   1 
ATOM   5540 C CG   . LEU   B 1 108 ? 32.771 -22.647 9.500   1.00 18.52 ?  108 LEU   B CG   1 
ATOM   5541 C CD1  . LEU   B 1 108 ? 33.805 -22.615 10.611  1.00 18.95 ?  108 LEU   B CD1  1 
ATOM   5542 C CD2  . LEU   B 1 108 ? 32.148 -21.272 9.327   1.00 19.88 ?  108 LEU   B CD2  1 
ATOM   5543 H H    A LEU   B 1 108 ? 32.287 -25.270 8.154   0.74 22.98 ?  108 LEU   B H    1 
ATOM   5544 H H    B LEU   B 1 108 ? 32.297 -25.285 8.137   0.26 22.98 ?  108 LEU   B H    1 
ATOM   5545 H HA   . LEU   B 1 108 ? 31.658 -22.939 7.107   1.00 20.04 ?  108 LEU   B HA   1 
ATOM   5546 H HB2  . LEU   B 1 108 ? 33.997 -23.829 8.383   1.00 20.51 ?  108 LEU   B HB2  1 
ATOM   5547 H HB3  . LEU   B 1 108 ? 33.880 -22.353 7.816   1.00 20.51 ?  108 LEU   B HB3  1 
ATOM   5548 H HG   . LEU   B 1 108 ? 32.067 -23.266 9.759   1.00 22.22 ?  108 LEU   B HG   1 
ATOM   5549 H HD11 . LEU   B 1 108 ? 33.375 -22.334 11.436  1.00 22.74 ?  108 LEU   B HD11 1 
ATOM   5550 H HD12 . LEU   B 1 108 ? 34.178 -23.503 10.721  1.00 22.74 ?  108 LEU   B HD12 1 
ATOM   5551 H HD13 . LEU   B 1 108 ? 34.504 -21.988 10.373  1.00 22.74 ?  108 LEU   B HD13 1 
ATOM   5552 H HD21 . LEU   B 1 108 ? 31.803 -20.970 10.182  1.00 23.85 ?  108 LEU   B HD21 1 
ATOM   5553 H HD22 . LEU   B 1 108 ? 32.828 -20.658 9.009   1.00 23.85 ?  108 LEU   B HD22 1 
ATOM   5554 H HD23 . LEU   B 1 108 ? 31.427 -21.330 8.681   1.00 23.85 ?  108 LEU   B HD23 1 
ATOM   5555 N N    . LEU   B 1 109 ? 33.109 -24.771 5.131   1.00 13.78 ?  109 LEU   B N    1 
ATOM   5556 C CA   . LEU   B 1 109 ? 33.738 -24.878 3.824   1.00 12.94 ?  109 LEU   B CA   1 
ATOM   5557 C C    . LEU   B 1 109 ? 32.971 -24.097 2.761   1.00 12.49 ?  109 LEU   B C    1 
ATOM   5558 O O    . LEU   B 1 109 ? 33.582 -23.502 1.865   1.00 12.37 ?  109 LEU   B O    1 
ATOM   5559 C CB   . LEU   B 1 109 ? 33.860 -26.353 3.446   1.00 13.21 ?  109 LEU   B CB   1 
ATOM   5560 C CG   . LEU   B 1 109 ? 34.640 -26.691 2.178   1.00 13.06 ?  109 LEU   B CG   1 
ATOM   5561 C CD1  . LEU   B 1 109 ? 36.027 -26.052 2.193   1.00 13.11 ?  109 LEU   B CD1  1 
ATOM   5562 C CD2  . LEU   B 1 109 ? 34.754 -28.203 2.020   1.00 13.71 ?  109 LEU   B CD2  1 
ATOM   5563 H H    . LEU   B 1 109 ? 32.814 -25.514 5.440   1.00 16.53 ?  109 LEU   B H    1 
ATOM   5564 H HA   . LEU   B 1 109 ? 34.630 -24.508 3.870   1.00 15.52 ?  109 LEU   B HA   1 
ATOM   5565 H HB2  . LEU   B 1 109 ? 34.302 -26.814 4.175   1.00 15.85 ?  109 LEU   B HB2  1 
ATOM   5566 H HB3  . LEU   B 1 109 ? 32.968 -26.714 3.334   1.00 15.85 ?  109 LEU   B HB3  1 
ATOM   5567 H HG   . LEU   B 1 109 ? 34.158 -26.355 1.403   1.00 15.67 ?  109 LEU   B HG   1 
ATOM   5568 H HD11 . LEU   B 1 109 ? 36.550 -26.410 1.456   1.00 15.74 ?  109 LEU   B HD11 1 
ATOM   5569 H HD12 . LEU   B 1 109 ? 35.934 -25.095 2.099   1.00 15.74 ?  109 LEU   B HD12 1 
ATOM   5570 H HD13 . LEU   B 1 109 ? 36.461 -26.267 3.035   1.00 15.74 ?  109 LEU   B HD13 1 
ATOM   5571 H HD21 . LEU   B 1 109 ? 35.328 -28.403 1.262   1.00 16.46 ?  109 LEU   B HD21 1 
ATOM   5572 H HD22 . LEU   B 1 109 ? 35.135 -28.578 2.829   1.00 16.46 ?  109 LEU   B HD22 1 
ATOM   5573 H HD23 . LEU   B 1 109 ? 33.869 -28.577 1.869   1.00 16.46 ?  109 LEU   B HD23 1 
ATOM   5574 N N    . LYS   B 1 110 ? 31.638 -24.066 2.841   1.00 12.14 ?  110 LYS   B N    1 
ATOM   5575 C CA   . LYS   B 1 110 ? 30.879 -23.301 1.854   1.00 11.83 ?  110 LYS   B CA   1 
ATOM   5576 C C    . LYS   B 1 110 ? 31.219 -21.811 1.944   1.00 11.49 ?  110 LYS   B C    1 
ATOM   5577 O O    . LYS   B 1 110 ? 31.473 -21.158 0.925   1.00 11.44 ?  110 LYS   B O    1 
ATOM   5578 C CB   . LYS   B 1 110 ? 29.373 -23.552 1.998   1.00 12.54 ?  110 LYS   B CB   1 
ATOM   5579 C CG   . LYS   B 1 110 ? 28.573 -22.920 0.865   1.00 12.91 ?  110 LYS   B CG   1 
ATOM   5580 C CD   . LYS   B 1 110 ? 27.108 -23.348 0.890   1.00 13.39 ?  110 LYS   B CD   1 
ATOM   5581 C CE   . LYS   B 1 110 ? 26.340 -22.815 -0.318  1.00 14.10 ?  110 LYS   B CE   1 
ATOM   5582 N NZ   . LYS   B 1 110 ? 26.674 -23.527 -1.582  1.00 14.47 ?  110 LYS   B NZ   1 
ATOM   5583 H H    . LYS   B 1 110 ? 31.165 -24.475 3.430   1.00 14.57 ?  110 LYS   B H    1 
ATOM   5584 H HA   . LYS   B 1 110 ? 31.137 -23.603 0.968   1.00 14.19 ?  110 LYS   B HA   1 
ATOM   5585 H HB2  . LYS   B 1 110 ? 29.207 -24.512 1.982   1.00 15.05 ?  110 LYS   B HB2  1 
ATOM   5586 H HB3  . LYS   B 1 110 ? 29.063 -23.177 2.834   1.00 15.05 ?  110 LYS   B HB3  1 
ATOM   5587 H HG2  . LYS   B 1 110 ? 28.597 -21.954 0.951   1.00 15.49 ?  110 LYS   B HG2  1 
ATOM   5588 H HG3  . LYS   B 1 110 ? 28.944 -23.189 0.011   1.00 15.49 ?  110 LYS   B HG3  1 
ATOM   5589 H HD2  . LYS   B 1 110 ? 27.054 -24.319 0.877   1.00 16.07 ?  110 LYS   B HD2  1 
ATOM   5590 H HD3  . LYS   B 1 110 ? 26.683 -23.004 1.694   1.00 16.07 ?  110 LYS   B HD3  1 
ATOM   5591 H HE2  . LYS   B 1 110 ? 25.388 -22.917 -0.159  1.00 16.91 ?  110 LYS   B HE2  1 
ATOM   5592 H HE3  . LYS   B 1 110 ? 26.557 -21.877 -0.437  1.00 16.91 ?  110 LYS   B HE3  1 
ATOM   5593 H HZ1  . LYS   B 1 110 ? 26.208 -23.184 -2.256  1.00 17.37 ?  110 LYS   B HZ1  1 
ATOM   5594 H HZ2  . LYS   B 1 110 ? 27.542 -23.444 -1.756  1.00 17.37 ?  110 LYS   B HZ2  1 
ATOM   5595 H HZ3  . LYS   B 1 110 ? 26.477 -24.392 -1.502  1.00 17.37 ?  110 LYS   B HZ3  1 
ATOM   5596 N N    . SER   B 1 111 ? 31.246 -21.263 3.162   1.00 11.81 ?  111 SER   B N    1 
ATOM   5597 C CA   . SER   B 1 111 ? 31.632 -19.864 3.335   1.00 12.04 ?  111 SER   B CA   1 
ATOM   5598 C C    . SER   B 1 111 ? 33.016 -19.604 2.750   1.00 11.51 ?  111 SER   B C    1 
ATOM   5599 O O    . SER   B 1 111 ? 33.248 -18.565 2.114   1.00 11.78 ?  111 SER   B O    1 
ATOM   5600 C CB   . SER   B 1 111 ? 31.618 -19.499 4.818   1.00 13.21 ?  111 SER   B CB   1 
ATOM   5601 O OG   . SER   B 1 111 ? 30.310 -19.512 5.341   1.00 15.17 ?  111 SER   B OG   1 
ATOM   5602 H H    . SER   B 1 111 ? 31.050 -21.679 3.890   1.00 14.17 ?  111 SER   B H    1 
ATOM   5603 H HA   . SER   B 1 111 ? 30.995 -19.300 2.873   1.00 14.44 ?  111 SER   B HA   1 
ATOM   5604 H HB2  . SER   B 1 111 ? 32.151 -20.143 5.306   1.00 15.86 ?  111 SER   B HB2  1 
ATOM   5605 H HB3  . SER   B 1 111 ? 31.982 -18.611 4.926   1.00 15.86 ?  111 SER   B HB3  1 
ATOM   5606 H HG   . SER   B 1 111 ? 30.319 -19.310 6.164   1.00 18.21 ?  111 SER   B HG   1 
ATOM   5607 N N    . ALA   B 1 112 ? 33.954 -20.524 2.973   1.00 11.53 ?  112 ALA   B N    1 
ATOM   5608 C CA   . ALA   B 1 112 ? 35.298 -20.358 2.430   1.00 11.34 ?  112 ALA   B CA   1 
ATOM   5609 C C    . ALA   B 1 112 ? 35.267 -20.257 0.907   1.00 10.71 ?  112 ALA   B C    1 
ATOM   5610 O O    . ALA   B 1 112 ? 35.896 -19.369 0.320   1.00 11.08 ?  112 ALA   B O    1 
ATOM   5611 C CB   . ALA   B 1 112 ? 36.200 -21.503 2.901   1.00 11.95 ?  112 ALA   B CB   1 
ATOM   5612 H H    . ALA   B 1 112 ? 33.839 -21.245 3.434   1.00 13.84 ?  112 ALA   B H    1 
ATOM   5613 H HA   . ALA   B 1 112 ? 35.667 -19.532 2.772   1.00 13.61 ?  112 ALA   B HA   1 
ATOM   5614 H HB1  . ALA   B 1 112 ? 37.091 -21.369 2.535   1.00 14.34 ?  112 ALA   B HB1  1 
ATOM   5615 H HB2  . ALA   B 1 112 ? 36.241 -21.492 3.872   1.00 14.34 ?  112 ALA   B HB2  1 
ATOM   5616 H HB3  . ALA   B 1 112 ? 35.837 -22.343 2.593   1.00 14.34 ?  112 ALA   B HB3  1 
ATOM   5617 N N    . TYR   B 1 113 ? 34.539 -21.161 0.245   1.00 10.72 ?  113 TYR   B N    1 
ATOM   5618 C CA   . TYR   B 1 113 ? 34.459 -21.106 -1.211  1.00 10.42 ?  113 TYR   B CA   1 
ATOM   5619 C C    . TYR   B 1 113 ? 33.754 -19.856 -1.728  1.00 10.23 ?  113 TYR   B C    1 
ATOM   5620 O O    . TYR   B 1 113 ? 34.036 -19.421 -2.848  1.00 10.37 ?  113 TYR   B O    1 
ATOM   5621 C CB   . TYR   B 1 113 ? 33.788 -22.366 -1.757  1.00 10.87 ?  113 TYR   B CB   1 
ATOM   5622 C CG   . TYR   B 1 113 ? 34.749 -23.520 -2.013  1.00 10.91 ?  113 TYR   B CG   1 
ATOM   5623 C CD1  . TYR   B 1 113 ? 35.748 -23.414 -2.978  1.00 11.63 ?  113 TYR   B CD1  1 
ATOM   5624 C CD2  . TYR   B 1 113 ? 34.652 -24.712 -1.304  1.00 11.41 ?  113 TYR   B CD2  1 
ATOM   5625 C CE1  . TYR   B 1 113 ? 36.631 -24.451 -3.221  1.00 11.32 ?  113 TYR   B CE1  1 
ATOM   5626 C CE2  . TYR   B 1 113 ? 35.520 -25.761 -1.548  1.00 11.70 ?  113 TYR   B CE2  1 
ATOM   5627 C CZ   . TYR   B 1 113 ? 36.502 -25.631 -2.511  1.00 11.68 ?  113 TYR   B CZ   1 
ATOM   5628 O OH   . TYR   B 1 113 ? 37.388 -26.649 -2.784  1.00 12.06 ?  113 TYR   B OH   1 
ATOM   5629 H H    . TYR   B 1 113 ? 34.089 -21.803 0.614   1.00 12.87 ?  113 TYR   B H    1 
ATOM   5630 H HA   . TYR   B 1 113 ? 35.359 -21.092 -1.552  1.00 12.51 ?  113 TYR   B HA   1 
ATOM   5631 H HB2  . TYR   B 1 113 ? 33.124 -22.679 -1.116  1.00 13.04 ?  113 TYR   B HB2  1 
ATOM   5632 H HB3  . TYR   B 1 113 ? 33.349 -22.150 -2.594  1.00 13.04 ?  113 TYR   B HB3  1 
ATOM   5633 H HD1  . TYR   B 1 113 ? 35.830 -22.620 -3.466  1.00 13.96 ?  113 TYR   B HD1  1 
ATOM   5634 H HD2  . TYR   B 1 113 ? 33.983 -24.804 -0.669  1.00 13.70 ?  113 TYR   B HD2  1 
ATOM   5635 H HE1  . TYR   B 1 113 ? 37.287 -24.364 -3.881  1.00 13.58 ?  113 TYR   B HE1  1 
ATOM   5636 H HE2  . TYR   B 1 113 ? 35.433 -26.553 -1.077  1.00 14.04 ?  113 TYR   B HE2  1 
ATOM   5637 H HH   . TYR   B 1 113 ? 37.206 -27.321 -2.314  1.00 14.48 ?  113 TYR   B HH   1 
ATOM   5638 N N    . GLU   B 1 114 ? 32.830 -19.281 -0.951  1.00 10.58 ?  114 GLU   B N    1 
ATOM   5639 C CA   . GLU   B 1 114 ? 32.145 -18.074 -1.406  1.00 10.61 ?  114 GLU   B CA   1 
ATOM   5640 C C    . GLU   B 1 114 ? 33.127 -16.948 -1.698  1.00 10.29 ?  114 GLU   B C    1 
ATOM   5641 O O    . GLU   B 1 114 ? 32.853 -16.090 -2.540  1.00 10.68 ?  114 GLU   B O    1 
ATOM   5642 C CB   . GLU   B 1 114 ? 31.089 -17.645 -0.386  1.00 11.03 ?  114 GLU   B CB   1 
ATOM   5643 C CG   . GLU   B 1 114 ? 29.873 -18.571 -0.436  1.00 11.25 ?  114 GLU   B CG   1 
ATOM   5644 C CD   . GLU   B 1 114 ? 28.849 -18.367 0.669   1.00 11.27 ?  114 GLU   B CD   1 
ATOM   5645 O OE1  . GLU   B 1 114 ? 29.143 -17.744 1.708   1.00 11.79 ?  114 GLU   B OE1  1 
ATOM   5646 O OE2  . GLU   B 1 114 ? 27.721 -18.899 0.508   1.00 12.32 -1 114 GLU   B OE2  1 
ATOM   5647 H H    . GLU   B 1 114 ? 32.580 -19.569 -0.176  1.00 12.70 ?  114 GLU   B H    1 
ATOM   5648 H HA   . GLU   B 1 114 ? 31.689 -18.273 -2.231  1.00 12.73 ?  114 GLU   B HA   1 
ATOM   5649 H HB2  . GLU   B 1 114 ? 31.465 -17.687 0.509   1.00 13.24 ?  114 GLU   B HB2  1 
ATOM   5650 H HB3  . GLU   B 1 114 ? 30.792 -16.747 -0.586  1.00 13.24 ?  114 GLU   B HB3  1 
ATOM   5651 H HG2  . GLU   B 1 114 ? 29.425 -18.443 -1.283  1.00 13.50 ?  114 GLU   B HG2  1 
ATOM   5652 H HG3  . GLU   B 1 114 ? 30.187 -19.492 -0.372  1.00 13.50 ?  114 GLU   B HG3  1 
ATOM   5653 N N    . ASN   B 1 115 ? 34.291 -16.941 -1.040  1.00 10.24 ?  115 ASN   B N    1 
ATOM   5654 C CA   . ASN   B 1 115 ? 35.289 -15.912 -1.334  1.00 10.35 ?  115 ASN   B CA   1 
ATOM   5655 C C    . ASN   B 1 115 ? 35.700 -15.930 -2.799  1.00 9.99  ?  115 ASN   B C    1 
ATOM   5656 O O    . ASN   B 1 115 ? 36.095 -14.893 -3.351  1.00 10.76 ?  115 ASN   B O    1 
ATOM   5657 C CB   . ASN   B 1 115 ? 36.527 -16.092 -0.450  1.00 10.79 ?  115 ASN   B CB   1 
ATOM   5658 C CG   . ASN   B 1 115 ? 36.255 -15.827 1.008   1.00 11.26 ?  115 ASN   B CG   1 
ATOM   5659 O OD1  . ASN   B 1 115 ? 36.251 -14.680 1.447   1.00 13.45 ?  115 ASN   B OD1  1 
ATOM   5660 N ND2  . ASN   B 1 115 ? 36.092 -16.891 1.782   1.00 11.53 ?  115 ASN   B ND2  1 
ATOM   5661 H H    . ASN   B 1 115 ? 34.523 -17.498 -0.422  1.00 12.29 ?  115 ASN   B H    1 
ATOM   5662 H HA   . ASN   B 1 115 ? 34.917 -15.037 -1.140  1.00 12.42 ?  115 ASN   B HA   1 
ATOM   5663 H HB2  . ASN   B 1 115 ? 36.849 -17.004 -0.538  1.00 12.95 ?  115 ASN   B HB2  1 
ATOM   5664 H HB3  . ASN   B 1 115 ? 37.217 -15.472 -0.739  1.00 12.95 ?  115 ASN   B HB3  1 
ATOM   5665 H HD21 . ASN   B 1 115 ? 35.945 -16.793 2.625   1.00 13.84 ?  115 ASN   B HD21 1 
ATOM   5666 H HD22 . ASN   B 1 115 ? 36.122 -17.683 1.445   1.00 13.84 ?  115 ASN   B HD22 1 
ATOM   5667 N N    . PHE   B 1 116 ? 35.674 -17.109 -3.434  1.00 9.88  ?  116 PHE   B N    1 
ATOM   5668 C CA   . PHE   B 1 116 ? 36.108 -17.203 -4.825  1.00 10.17 ?  116 PHE   B CA   1 
ATOM   5669 C C    . PHE   B 1 116 ? 35.212 -16.376 -5.741  1.00 9.93  ?  116 PHE   B C    1 
ATOM   5670 O O    . PHE   B 1 116 ? 35.649 -15.949 -6.815  1.00 10.41 ?  116 PHE   B O    1 
ATOM   5671 C CB   . PHE   B 1 116 ? 36.078 -18.654 -5.344  1.00 9.89  ?  116 PHE   B CB   1 
ATOM   5672 C CG   . PHE   B 1 116 ? 37.145 -19.605 -4.797  1.00 9.84  ?  116 PHE   B CG   1 
ATOM   5673 C CD1  . PHE   B 1 116 ? 37.793 -19.426 -3.586  1.00 10.81 ?  116 PHE   B CD1  1 
ATOM   5674 C CD2  . PHE   B 1 116 ? 37.446 -20.741 -5.535  1.00 10.07 ?  116 PHE   B CD2  1 
ATOM   5675 C CE1  . PHE   B 1 116 ? 38.726 -20.366 -3.133  1.00 10.73 ?  116 PHE   B CE1  1 
ATOM   5676 C CE2  . PHE   B 1 116 ? 38.368 -21.677 -5.088  1.00 10.51 ?  116 PHE   B CE2  1 
ATOM   5677 C CZ   . PHE   B 1 116 ? 39.007 -21.489 -3.889  1.00 10.57 ?  116 PHE   B CZ   1 
ATOM   5678 H H    . PHE   B 1 116 ? 35.412 -17.855 -3.087  1.00 11.85 ?  116 PHE   B H    1 
ATOM   5679 H HA   . PHE   B 1 116 ? 37.017 -16.876 -4.903  1.00 12.20 ?  116 PHE   B HA   1 
ATOM   5680 H HB2  . PHE   B 1 116 ? 35.207 -19.031 -5.126  1.00 11.87 ?  116 PHE   B HB2  1 
ATOM   5681 H HB3  . PHE   B 1 116 ? 36.176 -18.629 -6.310  1.00 11.87 ?  116 PHE   B HB3  1 
ATOM   5682 H HD1  . PHE   B 1 116 ? 37.600 -18.678 -3.065  1.00 12.97 ?  116 PHE   B HD1  1 
ATOM   5683 H HD2  . PHE   B 1 116 ? 37.008 -20.887 -6.341  1.00 12.09 ?  116 PHE   B HD2  1 
ATOM   5684 H HE1  . PHE   B 1 116 ? 39.168 -20.235 -2.321  1.00 12.88 ?  116 PHE   B HE1  1 
ATOM   5685 H HE2  . PHE   B 1 116 ? 38.560 -22.427 -5.603  1.00 12.61 ?  116 PHE   B HE2  1 
ATOM   5686 H HZ   . PHE   B 1 116 ? 39.643 -22.107 -3.595  1.00 12.69 ?  116 PHE   B HZ   1 
ATOM   5687 N N    . ASN   B 1 117 ? 33.944 -16.172 -5.360  1.00 10.36 ?  117 ASN   B N    1 
ATOM   5688 C CA   . ASN   B 1 117 ? 33.001 -15.467 -6.226  1.00 10.72 ?  117 ASN   B CA   1 
ATOM   5689 C C    . ASN   B 1 117 ? 33.317 -13.985 -6.379  1.00 10.73 ?  117 ASN   B C    1 
ATOM   5690 O O    . ASN   B 1 117 ? 32.719 -13.327 -7.234  1.00 11.77 ?  117 ASN   B O    1 
ATOM   5691 C CB   . ASN   B 1 117 ? 31.577 -15.688 -5.732  1.00 10.91 ?  117 ASN   B CB   1 
ATOM   5692 C CG   . ASN   B 1 117 ? 31.120 -17.094 -5.985  1.00 10.90 ?  117 ASN   B CG   1 
ATOM   5693 O OD1  . ASN   B 1 117 ? 31.468 -17.681 -7.011  1.00 11.74 ?  117 ASN   B OD1  1 
ATOM   5694 N ND2  . ASN   B 1 117 ? 30.379 -17.666 -5.046  1.00 10.99 ?  117 ASN   B ND2  1 
ATOM   5695 H H    . ASN   B 1 117 ? 33.618 -16.431 -4.606  1.00 12.43 ?  117 ASN   B H    1 
ATOM   5696 H HA   . ASN   B 1 117 ? 33.060 -15.865 -7.106  1.00 12.87 ?  117 ASN   B HA   1 
ATOM   5697 H HB2  . ASN   B 1 117 ? 31.542 -15.520 -4.773  1.00 13.09 ?  117 ASN   B HB2  1 
ATOM   5698 H HB3  . ASN   B 1 117 ? 30.983 -15.074 -6.196  1.00 13.09 ?  117 ASN   B HB3  1 
ATOM   5699 H HD21 . ASN   B 1 117 ? 30.094 -18.468 -5.153  1.00 13.19 ?  117 ASN   B HD21 1 
ATOM   5700 H HD22 . ASN   B 1 117 ? 30.160 -17.220 -4.341  1.00 13.19 ?  117 ASN   B HD22 1 
ATOM   5701 N N    . GLN   B 1 118 ? 34.256 -13.460 -5.601  1.00 10.59 ?  118 GLN   B N    1 
ATOM   5702 C CA   . GLN   B 1 118 ? 34.680 -12.073 -5.739  1.00 11.31 ?  118 GLN   B CA   1 
ATOM   5703 C C    . GLN   B 1 118 ? 35.750 -11.884 -6.810  1.00 11.32 ?  118 GLN   B C    1 
ATOM   5704 O O    . GLN   B 1 118 ? 36.231 -10.760 -6.990  1.00 12.80 ?  118 GLN   B O    1 
ATOM   5705 C CB   . GLN   B 1 118 ? 35.162 -11.537 -4.389  1.00 11.99 ?  118 GLN   B CB   1 
ATOM   5706 C CG   . GLN   B 1 118 ? 34.078 -11.580 -3.320  1.00 12.10 ?  118 GLN   B CG   1 
ATOM   5707 C CD   . GLN   B 1 118 ? 32.913 -10.669 -3.646  1.00 11.95 ?  118 GLN   B CD   1 
ATOM   5708 O OE1  . GLN   B 1 118 ? 33.102 -9.527  -4.079  1.00 12.63 ?  118 GLN   B OE1  1 
ATOM   5709 N NE2  . GLN   B 1 118 ? 31.702 -11.157 -3.439  1.00 12.44 ?  118 GLN   B NE2  1 
ATOM   5710 H H    . GLN   B 1 118 ? 34.683 -13.895 -4.985  1.00 12.71 ?  118 GLN   B H    1 
ATOM   5711 H HA   . GLN   B 1 118 ? 33.913 -11.550 -6.010  1.00 13.57 ?  118 GLN   B HA   1 
ATOM   5712 H HB2  . GLN   B 1 118 ? 35.914 -12.063 -4.085  1.00 14.38 ?  118 GLN   B HB2  1 
ATOM   5713 H HB3  . GLN   B 1 118 ? 35.434 -10.606 -4.501  1.00 14.38 ?  118 GLN   B HB3  1 
ATOM   5714 H HG2  . GLN   B 1 118 ? 33.747 -12.488 -3.247  1.00 14.52 ?  118 GLN   B HG2  1 
ATOM   5715 H HG3  . GLN   B 1 118 ? 34.462 -11.296 -2.474  1.00 14.52 ?  118 GLN   B HG3  1 
ATOM   5716 H HE21 . GLN   B 1 118 ? 31.609 -11.957 -3.137  1.00 14.93 ?  118 GLN   B HE21 1 
ATOM   5717 H HE22 . GLN   B 1 118 ? 31.018 -10.675 -3.611  1.00 14.93 ?  118 GLN   B HE22 1 
ATOM   5718 N N    . HIS   B 1 119 ? 36.107 -12.945 -7.539  1.00 10.66 ?  119 HIS   B N    1 
ATOM   5719 C CA   . HIS   B 1 119 ? 37.146 -12.898 -8.561  1.00 10.90 ?  119 HIS   B CA   1 
ATOM   5720 C C    . HIS   B 1 119 ? 36.665 -13.636 -9.796  1.00 11.01 ?  119 HIS   B C    1 
ATOM   5721 O O    . HIS   B 1 119 ? 36.160 -14.753 -9.690  1.00 11.72 ?  119 HIS   B O    1 
ATOM   5722 C CB   . HIS   B 1 119 ? 38.430 -13.530 -8.018  1.00 11.63 ?  119 HIS   B CB   1 
ATOM   5723 C CG   . HIS   B 1 119 ? 38.910 -12.838 -6.789  1.00 12.63 ?  119 HIS   B CG   1 
ATOM   5724 N ND1  . HIS   B 1 119 ? 39.706 -11.715 -6.838  1.00 14.38 ?  119 HIS   B ND1  1 
ATOM   5725 C CD2  . HIS   B 1 119 ? 38.615 -13.040 -5.486  1.00 13.79 ?  119 HIS   B CD2  1 
ATOM   5726 C CE1  . HIS   B 1 119 ? 39.916 -11.281 -5.608  1.00 15.46 ?  119 HIS   B CE1  1 
ATOM   5727 N NE2  . HIS   B 1 119 ? 39.256 -12.060 -4.771  1.00 15.36 ?  119 HIS   B NE2  1 
ATOM   5728 H H    . HIS   B 1 119 ? 35.749 -13.728 -7.462  1.00 12.80 ?  119 HIS   B H    1 
ATOM   5729 H HA   . HIS   B 1 119 ? 37.324 -11.973 -8.803  1.00 13.08 ?  119 HIS   B HA   1 
ATOM   5730 H HB2  . HIS   B 1 119 ? 38.262 -14.458 -7.804  1.00 13.96 ?  119 HIS   B HB2  1 
ATOM   5731 H HB3  . HIS   B 1 119 ? 39.125 -13.465 -8.698  1.00 13.96 ?  119 HIS   B HB3  1 
ATOM   5732 H HD2  . HIS   B 1 119 ? 38.082 -13.720 -5.141  1.00 16.54 ?  119 HIS   B HD2  1 
ATOM   5733 H HE1  . HIS   B 1 119 ? 40.448 -10.557 -5.370  1.00 18.55 ?  119 HIS   B HE1  1 
ATOM   5734 H HE2  . HIS   B 1 119 ? 39.262 -11.993 -3.914  1.00 18.43 ?  119 HIS   B HE2  1 
ATOM   5735 N N    . GLU   B 1 120 ? 36.817 -13.021 -10.970 1.00 11.46 ?  120 GLU   B N    1 
ATOM   5736 C CA   . GLU   B 1 120 ? 36.220 -13.608 -12.165 1.00 12.80 ?  120 GLU   B CA   1 
ATOM   5737 C C    . GLU   B 1 120 ? 36.898 -14.907 -12.582 1.00 11.58 ?  120 GLU   B C    1 
ATOM   5738 O O    . GLU   B 1 120 ? 36.237 -15.778 -13.159 1.00 11.80 ?  120 GLU   B O    1 
ATOM   5739 C CB   . GLU   B 1 120 ? 36.208 -12.602 -13.316 1.00 17.20 ?  120 GLU   B CB   1 
ATOM   5740 C CG   . GLU   B 1 120 ? 35.272 -11.428 -13.075 1.00 23.39 ?  120 GLU   B CG   1 
ATOM   5741 C CD   . GLU   B 1 120 ? 35.089 -10.546 -14.295 1.00 29.40 ?  120 GLU   B CD   1 
ATOM   5742 O OE1  . GLU   B 1 120 ? 36.066 -10.359 -15.051 1.00 31.50 ?  120 GLU   B OE1  1 
ATOM   5743 O OE2  . GLU   B 1 120 ? 33.965 -10.038 -14.492 1.00 32.10 -1 120 GLU   B OE2  1 
ATOM   5744 H H    . GLU   B 1 120 ? 37.243 -12.283 -11.103 1.00 13.75 ?  120 GLU   B H    1 
ATOM   5745 H HA   . GLU   B 1 120 ? 35.297 -13.823 -11.968 1.00 15.36 ?  120 GLU   B HA   1 
ATOM   5746 H HB2  . GLU   B 1 120 ? 37.099 -12.250 -13.441 1.00 20.64 ?  120 GLU   B HB2  1 
ATOM   5747 H HB3  . GLU   B 1 120 ? 35.912 -13.053 -14.126 1.00 20.64 ?  120 GLU   B HB3  1 
ATOM   5748 H HG2  . GLU   B 1 120 ? 34.398 -11.767 -12.822 1.00 28.06 ?  120 GLU   B HG2  1 
ATOM   5749 H HG3  . GLU   B 1 120 ? 35.634 -10.879 -12.365 1.00 28.06 ?  120 GLU   B HG3  1 
ATOM   5750 N N    . VAL   B 1 121 ? 38.199 -15.048 -12.320 1.00 11.32 ?  121 VAL   B N    1 
ATOM   5751 C CA   . VAL   B 1 121 ? 38.947 -16.257 -12.662 1.00 11.38 ?  121 VAL   B CA   1 
ATOM   5752 C C    . VAL   B 1 121 ? 40.060 -16.456 -11.639 1.00 10.77 ?  121 VAL   B C    1 
ATOM   5753 O O    . VAL   B 1 121 ? 40.735 -15.498 -11.245 1.00 11.53 ?  121 VAL   B O    1 
ATOM   5754 C CB   . VAL   B 1 121 ? 39.459 -16.225 -14.123 1.00 13.14 ?  121 VAL   B CB   1 
ATOM   5755 C CG1  . VAL   B 1 121 ? 40.339 -15.004 -14.388 1.00 14.26 ?  121 VAL   B CG1  1 
ATOM   5756 C CG2  . VAL   B 1 121 ? 40.182 -17.518 -14.472 1.00 14.83 ?  121 VAL   B CG2  1 
ATOM   5757 H H    . VAL   B 1 121 ? 38.677 -14.446 -11.937 1.00 13.58 ?  121 VAL   B H    1 
ATOM   5758 H HA   . VAL   B 1 121 ? 38.342 -17.012 -12.590 1.00 13.66 ?  121 VAL   B HA   1 
ATOM   5759 H HB   . VAL   B 1 121 ? 38.688 -16.161 -14.714 1.00 15.77 ?  121 VAL   B HB   1 
ATOM   5760 H HG11 . VAL   B 1 121 ? 40.635 -15.021 -15.312 1.00 17.11 ?  121 VAL   B HG11 1 
ATOM   5761 H HG12 . VAL   B 1 121 ? 39.822 -14.199 -14.222 1.00 17.11 ?  121 VAL   B HG12 1 
ATOM   5762 H HG13 . VAL   B 1 121 ? 41.106 -15.033 -13.794 1.00 17.11 ?  121 VAL   B HG13 1 
ATOM   5763 H HG21 . VAL   B 1 121 ? 40.384 -17.520 -15.422 1.00 17.79 ?  121 VAL   B HG21 1 
ATOM   5764 H HG22 . VAL   B 1 121 ? 41.006 -17.567 -13.961 1.00 17.79 ?  121 VAL   B HG22 1 
ATOM   5765 H HG23 . VAL   B 1 121 ? 39.611 -18.270 -14.255 1.00 17.79 ?  121 VAL   B HG23 1 
ATOM   5766 N N    . LEU   B 1 122 ? 40.242 -17.711 -11.204 1.00 10.45 ?  122 LEU   B N    1 
ATOM   5767 C CA   . LEU   B 1 122 ? 41.222 -18.060 -10.179 1.00 10.56 ?  122 LEU   B CA   1 
ATOM   5768 C C    . LEU   B 1 122 ? 41.877 -19.392 -10.501 1.00 10.08 ?  122 LEU   B C    1 
ATOM   5769 O O    . LEU   B 1 122 ? 41.216 -20.314 -10.997 1.00 11.32 ?  122 LEU   B O    1 
ATOM   5770 C CB   . LEU   B 1 122 ? 40.572 -18.289 -8.802  1.00 12.40 ?  122 LEU   B CB   1 
ATOM   5771 C CG   . LEU   B 1 122 ? 39.539 -17.267 -8.317  1.00 12.12 ?  122 LEU   B CG   1 
ATOM   5772 C CD1  . LEU   B 1 122 ? 38.139 -17.617 -8.799  1.00 13.07 ?  122 LEU   B CD1  1 
ATOM   5773 C CD2  . LEU   B 1 122 ? 39.579 -17.164 -6.805  1.00 11.73 ?  122 LEU   B CD2  1 
ATOM   5774 H H    . LEU   B 1 122 ? 39.801 -18.392 -11.494 1.00 12.55 ?  122 LEU   B H    1 
ATOM   5775 H HA   . LEU   B 1 122 ? 41.902 -17.367 -10.106 1.00 12.67 ?  122 LEU   B HA   1 
ATOM   5776 H HB2  . LEU   B 1 122 ? 40.131 -19.147 -8.820  1.00 14.88 ?  122 LEU   B HB2  1 
ATOM   5777 H HB3  . LEU   B 1 122 ? 41.281 -18.306 -8.138  1.00 14.88 ?  122 LEU   B HB3  1 
ATOM   5778 H HG   . LEU   B 1 122 ? 39.767 -16.394 -8.673  1.00 14.55 ?  122 LEU   B HG   1 
ATOM   5779 H HD11 . LEU   B 1 122 ? 37.512 -16.977 -8.428  1.00 15.68 ?  122 LEU   B HD11 1 
ATOM   5780 H HD12 . LEU   B 1 122 ? 38.123 -17.569 -9.768  1.00 15.68 ?  122 LEU   B HD12 1 
ATOM   5781 H HD13 . LEU   B 1 122 ? 37.919 -18.510 -8.505  1.00 15.68 ?  122 LEU   B HD13 1 
ATOM   5782 H HD21 . LEU   B 1 122 ? 38.897 -16.539 -6.508  1.00 14.08 ?  122 LEU   B HD21 1 
ATOM   5783 H HD22 . LEU   B 1 122 ? 39.410 -18.040 -6.420  1.00 14.08 ?  122 LEU   B HD22 1 
ATOM   5784 H HD23 . LEU   B 1 122 ? 40.455 -16.847 -6.528  1.00 14.08 ?  122 LEU   B HD23 1 
ATOM   5785 N N    . LEU   B 1 123 ? 43.167 -19.498 -10.153 1.00 9.89  ?  123 LEU   B N    1 
ATOM   5786 C CA   . LEU   B 1 123 ? 43.879 -20.768 -10.026 1.00 10.09 ?  123 LEU   B CA   1 
ATOM   5787 C C    . LEU   B 1 123 ? 43.853 -21.162 -8.553  1.00 10.04 ?  123 LEU   B C    1 
ATOM   5788 O O    . LEU   B 1 123 ? 44.206 -20.340 -7.700  1.00 10.57 ?  123 LEU   B O    1 
ATOM   5789 C CB   . LEU   B 1 123 ? 45.326 -20.584 -10.491 1.00 10.64 ?  123 LEU   B CB   1 
ATOM   5790 C CG   . LEU   B 1 123 ? 46.271 -21.761 -10.239 1.00 11.05 ?  123 LEU   B CG   1 
ATOM   5791 C CD1  . LEU   B 1 123 ? 45.852 -23.011 -11.011 1.00 11.94 ?  123 LEU   B CD1  1 
ATOM   5792 C CD2  . LEU   B 1 123 ? 47.691 -21.373 -10.603 1.00 11.97 ?  123 LEU   B CD2  1 
ATOM   5793 H H    . LEU   B 1 123 ? 43.665 -18.819 -9.966  1.00 11.87 ?  123 LEU   B H    1 
ATOM   5794 H HA   . LEU   B 1 123 ? 43.443 -21.456 -10.557 1.00 12.11 ?  123 LEU   B HA   1 
ATOM   5795 H HB2  . LEU   B 1 123 ? 45.317 -20.429 -11.452 1.00 12.77 ?  123 LEU   B HB2  1 
ATOM   5796 H HB3  . LEU   B 1 123 ? 45.697 -19.816 -10.043 1.00 12.77 ?  123 LEU   B HB3  1 
ATOM   5797 H HG   . LEU   B 1 123 ? 46.262 -21.983 -9.294  1.00 13.26 ?  123 LEU   B HG   1 
ATOM   5798 H HD11 . LEU   B 1 123 ? 46.489 -23.718 -10.832 1.00 14.33 ?  123 LEU   B HD11 1 
ATOM   5799 H HD12 . LEU   B 1 123 ? 44.967 -23.277 -10.715 1.00 14.33 ?  123 LEU   B HD12 1 
ATOM   5800 H HD13 . LEU   B 1 123 ? 45.839 -22.803 -11.956 1.00 14.33 ?  123 LEU   B HD13 1 
ATOM   5801 H HD21 . LEU   B 1 123 ? 48.279 -22.124 -10.436 1.00 14.36 ?  123 LEU   B HD21 1 
ATOM   5802 H HD22 . LEU   B 1 123 ? 47.720 -21.128 -11.541 1.00 14.36 ?  123 LEU   B HD22 1 
ATOM   5803 H HD23 . LEU   B 1 123 ? 47.958 -20.615 -10.055 1.00 14.36 ?  123 LEU   B HD23 1 
ATOM   5804 N N    . ALA   B 1 124 ? 43.424 -22.394 -8.244  1.00 10.08 ?  124 ALA   B N    1 
ATOM   5805 C CA   . ALA   B 1 124 ? 43.170 -22.719 -6.847  1.00 10.03 ?  124 ALA   B CA   1 
ATOM   5806 C C    . ALA   B 1 124 ? 43.436 -24.178 -6.513  1.00 9.89  ?  124 ALA   B C    1 
ATOM   5807 O O    . ALA   B 1 124 ? 43.298 -25.053 -7.376  1.00 10.52 ?  124 ALA   B O    1 
ATOM   5808 C CB   . ALA   B 1 124 ? 41.715 -22.401 -6.475  1.00 10.56 ?  124 ALA   B CB   1 
ATOM   5809 H H    . ALA   B 1 124 ? 43.262 -23.034 -8.805  1.00 12.09 ?  124 ALA   B H    1 
ATOM   5810 H HA   . ALA   B 1 124 ? 43.744 -22.167 -6.301  1.00 12.04 ?  124 ALA   B HA   1 
ATOM   5811 H HB1  . ALA   B 1 124 ? 41.565 -22.619 -5.542  1.00 12.67 ?  124 ALA   B HB1  1 
ATOM   5812 H HB2  . ALA   B 1 124 ? 41.553 -21.451 -6.619  1.00 12.67 ?  124 ALA   B HB2  1 
ATOM   5813 H HB3  . ALA   B 1 124 ? 41.119 -22.921 -7.037  1.00 12.67 ?  124 ALA   B HB3  1 
ATOM   5814 N N    . PRO   B 1 125 ? 43.736 -24.468 -5.250  1.00 10.17 ?  125 PRO   B N    1 
ATOM   5815 C CA   . PRO   B 1 125 ? 43.669 -25.833 -4.728  1.00 10.77 ?  125 PRO   B CA   1 
ATOM   5816 C C    . PRO   B 1 125 ? 42.266 -26.110 -4.188  1.00 10.77 ?  125 PRO   B C    1 
ATOM   5817 O O    . PRO   B 1 125 ? 41.465 -25.199 -3.980  1.00 11.28 ?  125 PRO   B O    1 
ATOM   5818 C CB   . PRO   B 1 125 ? 44.651 -25.765 -3.555  1.00 11.94 ?  125 PRO   B CB   1 
ATOM   5819 C CG   . PRO   B 1 125 ? 44.406 -24.374 -2.987  1.00 11.96 ?  125 PRO   B CG   1 
ATOM   5820 C CD   . PRO   B 1 125 ? 44.061 -23.497 -4.187  1.00 10.76 ?  125 PRO   B CD   1 
ATOM   5821 H HA   . PRO   B 1 125 ? 43.940 -26.502 -5.376  1.00 12.92 ?  125 PRO   B HA   1 
ATOM   5822 H HB2  . PRO   B 1 125 ? 44.442 -26.448 -2.895  1.00 14.32 ?  125 PRO   B HB2  1 
ATOM   5823 H HB3  . PRO   B 1 125 ? 45.561 -25.855 -3.873  1.00 14.32 ?  125 PRO   B HB3  1 
ATOM   5824 H HG2  . PRO   B 1 125 ? 43.663 -24.392 -2.360  1.00 14.35 ?  125 PRO   B HG2  1 
ATOM   5825 H HG3  . PRO   B 1 125 ? 45.209 -24.045 -2.546  1.00 14.35 ?  125 PRO   B HG3  1 
ATOM   5826 H HD2  . PRO   B 1 125 ? 43.296 -22.931 -3.993  1.00 12.91 ?  125 PRO   B HD2  1 
ATOM   5827 H HD3  . PRO   B 1 125 ? 44.834 -22.962 -4.449  1.00 12.91 ?  125 PRO   B HD3  1 
ATOM   5828 N N    . LEU   B 1 126 ? 41.995 -27.390 -3.918  1.00 11.56 ?  126 LEU   B N    1 
ATOM   5829 C CA   . LEU   B 1 126 ? 40.774 -27.760 -3.205  1.00 11.78 ?  126 LEU   B CA   1 
ATOM   5830 C C    . LEU   B 1 126 ? 40.887 -27.361 -1.739  1.00 11.89 ?  126 LEU   B C    1 
ATOM   5831 O O    . LEU   B 1 126 ? 41.779 -27.823 -1.019  1.00 13.68 ?  126 LEU   B O    1 
ATOM   5832 C CB   . LEU   B 1 126 ? 40.517 -29.257 -3.327  1.00 12.98 ?  126 LEU   B CB   1 
ATOM   5833 C CG   . LEU   B 1 126 ? 39.983 -29.728 -4.681  1.00 13.83 ?  126 LEU   B CG   1 
ATOM   5834 C CD1  . LEU   B 1 126 ? 40.040 -31.239 -4.790  1.00 15.58 ?  126 LEU   B CD1  1 
ATOM   5835 C CD2  . LEU   B 1 126 ? 38.560 -29.237 -4.909  1.00 14.17 ?  126 LEU   B CD2  1 
ATOM   5836 H H    . LEU   B 1 126 ? 42.503 -28.058 -4.122  1.00 13.87 ?  126 LEU   B H    1 
ATOM   5837 H HA   . LEU   B 1 126 ? 40.028 -27.285 -3.594  1.00 14.14 ?  126 LEU   B HA   1 
ATOM   5838 H HB2  . LEU   B 1 126 ? 41.347 -29.728 -3.165  1.00 15.57 ?  126 LEU   B HB2  1 
ATOM   5839 H HB3  . LEU   B 1 126 ? 39.863 -29.511 -2.656  1.00 15.57 ?  126 LEU   B HB3  1 
ATOM   5840 H HG   . LEU   B 1 126 ? 40.540 -29.355 -5.383  1.00 16.59 ?  126 LEU   B HG   1 
ATOM   5841 H HD11 . LEU   B 1 126 ? 39.695 -31.505 -5.657  1.00 18.69 ?  126 LEU   B HD11 1 
ATOM   5842 H HD12 . LEU   B 1 126 ? 40.959 -31.527 -4.695  1.00 18.69 ?  126 LEU   B HD12 1 
ATOM   5843 H HD13 . LEU   B 1 126 ? 39.495 -31.625 -4.086  1.00 18.69 ?  126 LEU   B HD13 1 
ATOM   5844 H HD21 . LEU   B 1 126 ? 38.212 -29.640 -5.721  1.00 17.00 ?  126 LEU   B HD21 1 
ATOM   5845 H HD22 . LEU   B 1 126 ? 38.011 -29.492 -4.152  1.00 17.00 ?  126 LEU   B HD22 1 
ATOM   5846 H HD23 . LEU   B 1 126 ? 38.566 -28.269 -5.000  1.00 17.00 ?  126 LEU   B HD23 1 
ATOM   5847 N N    . LEU   B 1 127 ? 39.956 -26.530 -1.287  1.00 11.57 ?  127 LEU   B N    1 
ATOM   5848 C CA   . LEU   B 1 127 ? 40.003 -26.034 0.076   1.00 12.01 ?  127 LEU   B CA   1 
ATOM   5849 C C    . LEU   B 1 127 ? 39.732 -27.157 1.073   1.00 11.84 ?  127 LEU   B C    1 
ATOM   5850 O O    . LEU   B 1 127 ? 38.914 -28.056 0.841   1.00 11.95 ?  127 LEU   B O    1 
ATOM   5851 C CB   . LEU   B 1 127 ? 38.977 -24.915 0.271   1.00 12.45 ?  127 LEU   B CB   1 
ATOM   5852 C CG   . LEU   B 1 127 ? 39.162 -23.647 -0.563  1.00 13.20 ?  127 LEU   B CG   1 
ATOM   5853 C CD1  . LEU   B 1 127 ? 38.042 -22.677 -0.233  1.00 13.27 ?  127 LEU   B CD1  1 
ATOM   5854 C CD2  . LEU   B 1 127 ? 40.515 -23.002 -0.318  1.00 14.18 ?  127 LEU   B CD2  1 
ATOM   5855 H H    . LEU   B 1 127 ? 39.289 -26.234 -1.748  1.00 13.88 ?  127 LEU   B H    1 
ATOM   5856 H HA   . LEU   B 1 127 ? 40.887 -25.669 0.253   1.00 14.41 ?  127 LEU   B HA   1 
ATOM   5857 H HB2  . LEU   B 1 127 ? 38.099 -25.271 0.061   1.00 14.94 ?  127 LEU   B HB2  1 
ATOM   5858 H HB3  . LEU   B 1 127 ? 38.995 -24.645 1.203   1.00 14.94 ?  127 LEU   B HB3  1 
ATOM   5859 H HG   . LEU   B 1 127 ? 39.087 -23.868 -1.503  1.00 15.83 ?  127 LEU   B HG   1 
ATOM   5860 H HD11 . LEU   B 1 127 ? 38.156 -21.866 -0.756  1.00 15.93 ?  127 LEU   B HD11 1 
ATOM   5861 H HD12 . LEU   B 1 127 ? 37.186 -23.085 -0.444  1.00 15.93 ?  127 LEU   B HD12 1 
ATOM   5862 H HD13 . LEU   B 1 127 ? 38.076 -22.461 0.715   1.00 15.93 ?  127 LEU   B HD13 1 
ATOM   5863 H HD21 . LEU   B 1 127 ? 40.547 -22.150 -0.781  1.00 17.02 ?  127 LEU   B HD21 1 
ATOM   5864 H HD22 . LEU   B 1 127 ? 40.630 -22.865 0.635   1.00 17.02 ?  127 LEU   B HD22 1 
ATOM   5865 H HD23 . LEU   B 1 127 ? 41.204 -23.591 -0.656  1.00 17.02 ?  127 LEU   B HD23 1 
ATOM   5866 N N    . SER   B 1 128 ? 40.416 -27.074 2.204   1.00 11.96 ?  128 SER   B N    1 
ATOM   5867 C CA   . SER   B 1 128 ? 40.306 -27.985 3.331   1.00 12.60 ?  128 SER   B CA   1 
ATOM   5868 C C    . SER   B 1 128 ? 40.803 -29.393 3.016   1.00 13.28 ?  128 SER   B C    1 
ATOM   5869 O O    . SER   B 1 128 ? 40.702 -30.272 3.869   1.00 14.43 ?  128 SER   B O    1 
ATOM   5870 C CB   . SER   B 1 128 ? 38.902 -27.997 3.958   1.00 12.83 ?  128 SER   B CB   1 
ATOM   5871 O OG   . SER   B 1 128 ? 38.586 -26.721 4.500   1.00 13.48 ?  128 SER   B OG   1 
ATOM   5872 H H    . SER   B 1 128 ? 40.995 -26.454 2.350   1.00 14.36 ?  128 SER   B H    1 
ATOM   5873 H HA   . SER   B 1 128 ? 40.893 -27.640 4.023   1.00 15.12 ?  128 SER   B HA   1 
ATOM   5874 H HB2  . SER   B 1 128 ? 38.247 -28.235 3.284   1.00 15.39 ?  128 SER   B HB2  1 
ATOM   5875 H HB3  . SER   B 1 128 ? 38.881 -28.662 4.679   1.00 15.39 ?  128 SER   B HB3  1 
ATOM   5876 H HG   . SER   B 1 128 ? 39.148 -26.512 5.089   1.00 16.17 ?  128 SER   B HG   1 
ATOM   5877 N N    . ALA   B 1 129 ? 41.384 -29.617 1.837   1.00 14.27 ?  129 ALA   B N    1 
ATOM   5878 C CA   . ALA   B 1 129 ? 41.925 -30.917 1.477   1.00 15.00 ?  129 ALA   B CA   1 
ATOM   5879 C C    . ALA   B 1 129 ? 43.319 -31.092 2.065   1.00 14.06 ?  129 ALA   B C    1 
ATOM   5880 O O    . ALA   B 1 129 ? 43.882 -30.186 2.694   1.00 14.13 ?  129 ALA   B O    1 
ATOM   5881 C CB   . ALA   B 1 129 ? 41.952 -31.074 -0.040  1.00 17.10 ?  129 ALA   B CB   1 
ATOM   5882 H H    . ALA   B 1 129 ? 41.473 -29.021 1.223   1.00 17.12 ?  129 ALA   B H    1 
ATOM   5883 H HA   . ALA   B 1 129 ? 41.354 -31.606 1.844   1.00 18.00 ?  129 ALA   B HA   1 
ATOM   5884 H HB1  . ALA   B 1 129 ? 42.311 -31.949 -0.257  1.00 20.52 ?  129 ALA   B HB1  1 
ATOM   5885 H HB2  . ALA   B 1 129 ? 41.048 -30.994 -0.380  1.00 20.52 ?  129 ALA   B HB2  1 
ATOM   5886 H HB3  . ALA   B 1 129 ? 42.513 -30.382 -0.420  1.00 20.52 ?  129 ALA   B HB3  1 
ATOM   5887 N N    . GLY   B 1 130 ? 43.869 -32.287 1.865   1.00 14.07 ?  130 GLY   B N    1 
ATOM   5888 C CA   . GLY   B 1 130 ? 45.262 -32.522 2.204   1.00 15.20 ?  130 GLY   B CA   1 
ATOM   5889 C C    . GLY   B 1 130 ? 45.486 -32.419 3.695   1.00 14.96 ?  130 GLY   B C    1 
ATOM   5890 O O    . GLY   B 1 130 ? 44.799 -33.069 4.497   1.00 16.15 ?  130 GLY   B O    1 
ATOM   5891 H H    . GLY   B 1 130 ? 43.457 -32.969 1.538   1.00 16.89 ?  130 GLY   B H    1 
ATOM   5892 H HA2  . GLY   B 1 130 ? 45.523 -33.412 1.911   1.00 18.24 ?  130 GLY   B HA2  1 
ATOM   5893 H HA3  . GLY   B 1 130 ? 45.822 -31.871 1.757   1.00 18.24 ?  130 GLY   B HA3  1 
ATOM   5894 N N    . ILE   B 1 131 ? 46.454 -31.580 4.078   1.00 15.51 ?  131 ILE   B N    1 
ATOM   5895 C CA   . ILE   B 1 131 ? 46.809 -31.435 5.480   1.00 16.31 ?  131 ILE   B CA   1 
ATOM   5896 C C    . ILE   B 1 131 ? 45.681 -30.852 6.314   1.00 15.49 ?  131 ILE   B C    1 
ATOM   5897 O O    . ILE   B 1 131 ? 45.741 -30.937 7.544   1.00 16.92 ?  131 ILE   B O    1 
ATOM   5898 C CB   . ILE   B 1 131 ? 48.128 -30.646 5.681   1.00 18.27 ?  131 ILE   B CB   1 
ATOM   5899 C CG1  . ILE   B 1 131 ? 47.956 -29.167 5.306   1.00 19.15 ?  131 ILE   B CG1  1 
ATOM   5900 C CG2  . ILE   B 1 131 ? 49.262 -31.290 4.884   1.00 19.52 ?  131 ILE   B CG2  1 
ATOM   5901 C CD1  . ILE   B 1 131 ? 49.159 -28.302 5.655   1.00 20.27 ?  131 ILE   B CD1  1 
ATOM   5902 H H    . ILE   B 1 131 ? 46.916 -31.093 3.542   1.00 18.61 ?  131 ILE   B H    1 
ATOM   5903 H HA   . ILE   B 1 131 ? 46.961 -32.321 5.830   1.00 19.58 ?  131 ILE   B HA   1 
ATOM   5904 H HB   . ILE   B 1 131 ? 48.354 -30.691 6.624   1.00 21.92 ?  131 ILE   B HB   1 
ATOM   5905 H HG12 . ILE   B 1 131 ? 47.808 -29.104 4.349   1.00 22.98 ?  131 ILE   B HG12 1 
ATOM   5906 H HG13 . ILE   B 1 131 ? 47.187 -28.802 5.777   1.00 22.98 ?  131 ILE   B HG13 1 
ATOM   5907 H HG21 . ILE   B 1 131 ? 50.096 -30.871 5.138   1.00 23.42 ?  131 ILE   B HG21 1 
ATOM   5908 H HG22 . ILE   B 1 131 ? 49.286 -32.236 5.085   1.00 23.42 ?  131 ILE   B HG22 1 
ATOM   5909 H HG23 . ILE   B 1 131 ? 49.092 -31.154 3.938   1.00 23.42 ?  131 ILE   B HG23 1 
ATOM   5910 H HD11 . ILE   B 1 131 ? 48.943 -27.374 5.475   1.00 24.33 ?  131 ILE   B HD11 1 
ATOM   5911 H HD12 . ILE   B 1 131 ? 49.367 -28.418 6.595   1.00 24.33 ?  131 ILE   B HD12 1 
ATOM   5912 H HD13 . ILE   B 1 131 ? 49.913 -28.579 5.112   1.00 24.33 ?  131 ILE   B HD13 1 
ATOM   5913 N N    . PHE   B 1 132 ? 44.653 -30.270 5.682   1.00 14.17 ?  132 PHE   B N    1 
ATOM   5914 C CA   . PHE   B 1 132 ? 43.489 -29.776 6.412   1.00 14.35 ?  132 PHE   B CA   1 
ATOM   5915 C C    . PHE   B 1 132 ? 42.467 -30.870 6.731   1.00 15.75 ?  132 PHE   B C    1 
ATOM   5916 O O    . PHE   B 1 132 ? 41.553 -30.620 7.525   1.00 17.34 ?  132 PHE   B O    1 
ATOM   5917 C CB   . PHE   B 1 132 ? 42.807 -28.639 5.638   1.00 13.72 ?  132 PHE   B CB   1 
ATOM   5918 C CG   . PHE   B 1 132 ? 43.507 -27.295 5.743   1.00 13.80 ?  132 PHE   B CG   1 
ATOM   5919 C CD1  . PHE   B 1 132 ? 44.793 -27.108 5.255   1.00 14.76 ?  132 PHE   B CD1  1 
ATOM   5920 C CD2  . PHE   B 1 132 ? 42.843 -26.199 6.280   1.00 13.29 ?  132 PHE   B CD2  1 
ATOM   5921 C CE1  . PHE   B 1 132 ? 45.409 -25.865 5.340   1.00 15.24 ?  132 PHE   B CE1  1 
ATOM   5922 C CE2  . PHE   B 1 132 ? 43.453 -24.955 6.362   1.00 13.67 ?  132 PHE   B CE2  1 
ATOM   5923 C CZ   . PHE   B 1 132 ? 44.736 -24.795 5.894   1.00 14.77 ?  132 PHE   B CZ   1 
ATOM   5924 H H    . PHE   B 1 132 ? 44.604 -30.151 4.827   1.00 17.00 ?  132 PHE   B H    1 
ATOM   5925 H HA   . PHE   B 1 132 ? 43.792 -29.406 7.253   1.00 17.22 ?  132 PHE   B HA   1 
ATOM   5926 H HB2  . PHE   B 1 132 ? 42.779 -28.878 4.702   1.00 16.47 ?  132 PHE   B HB2  1 
ATOM   5927 H HB3  . PHE   B 1 132 ? 41.902 -28.528 5.977   1.00 16.47 ?  132 PHE   B HB3  1 
ATOM   5928 H HD1  . PHE   B 1 132 ? 45.256 -27.826 4.888   1.00 17.71 ?  132 PHE   B HD1  1 
ATOM   5929 H HD2  . PHE   B 1 132 ? 41.978 -26.302 6.602   1.00 15.95 ?  132 PHE   B HD2  1 
ATOM   5930 H HE1  . PHE   B 1 132 ? 46.280 -25.758 5.024   1.00 18.29 ?  132 PHE   B HE1  1 
ATOM   5931 H HE2  . PHE   B 1 132 ? 43.003 -24.231 6.738   1.00 16.41 ?  132 PHE   B HE2  1 
ATOM   5932 H HZ   . PHE   B 1 132 ? 45.154 -23.961 5.950   1.00 17.72 ?  132 PHE   B HZ   1 
ATOM   5933 N N    . GLY   B 1 133 ? 42.570 -32.061 6.126   1.00 15.22 ?  133 GLY   B N    1 
ATOM   5934 C CA   . GLY   B 1 133 ? 41.860 -33.234 6.612   1.00 16.08 ?  133 GLY   B CA   1 
ATOM   5935 C C    . GLY   B 1 133 ? 40.460 -33.494 6.081   1.00 16.50 ?  133 GLY   B C    1 
ATOM   5936 O O    . GLY   B 1 133 ? 39.872 -34.516 6.444   1.00 18.29 ?  133 GLY   B O    1 
ATOM   5937 H H    . GLY   B 1 133 ? 43.059 -32.206 5.430   1.00 18.26 ?  133 GLY   B H    1 
ATOM   5938 H HA2  . GLY   B 1 133 ? 42.397 -34.014 6.407   1.00 19.30 ?  133 GLY   B HA2  1 
ATOM   5939 H HA3  . GLY   B 1 133 ? 41.799 -33.167 7.577   1.00 19.30 ?  133 GLY   B HA3  1 
ATOM   5940 N N    . ALA   B 1 134 ? 39.896 -32.621 5.255   1.00 15.78 ?  134 ALA   B N    1 
ATOM   5941 C CA   . ALA   B 1 134 ? 38.570 -32.896 4.722   1.00 15.72 ?  134 ALA   B CA   1 
ATOM   5942 C C    . ALA   B 1 134 ? 38.655 -33.888 3.567   1.00 15.61 ?  134 ALA   B C    1 
ATOM   5943 O O    . ALA   B 1 134 ? 39.708 -34.081 2.954   1.00 16.79 ?  134 ALA   B O    1 
ATOM   5944 C CB   . ALA   B 1 134 ? 37.898 -31.607 4.251   1.00 16.13 ?  134 ALA   B CB   1 
ATOM   5945 H H    . ALA   B 1 134 ? 40.248 -31.873 5.000   1.00 18.93 ?  134 ALA   B H    1 
ATOM   5946 H HA   . ALA   B 1 134 ? 38.023 -33.283 5.424   1.00 18.86 ?  134 ALA   B HA   1 
ATOM   5947 H HB1  . ALA   B 1 134 ? 37.012 -31.821 3.917   1.00 19.36 ?  134 ALA   B HB1  1 
ATOM   5948 H HB2  . ALA   B 1 134 ? 37.829 -30.993 5.000   1.00 19.36 ?  134 ALA   B HB2  1 
ATOM   5949 H HB3  . ALA   B 1 134 ? 38.432 -31.211 3.546   1.00 19.36 ?  134 ALA   B HB3  1 
ATOM   5950 N N    . ASP   B 1 135 ? 37.522 -34.516 3.277   1.00 15.81 ?  135 ASP   B N    1 
ATOM   5951 C CA   . ASP   B 1 135 ? 37.425 -35.416 2.135   1.00 16.56 ?  135 ASP   B CA   1 
ATOM   5952 C C    . ASP   B 1 135 ? 37.527 -34.587 0.861   1.00 15.51 ?  135 ASP   B C    1 
ATOM   5953 O O    . ASP   B 1 135 ? 36.679 -33.712 0.636   1.00 15.45 ?  135 ASP   B O    1 
ATOM   5954 C CB   . ASP   B 1 135 ? 36.083 -36.143 2.197   1.00 18.38 ?  135 ASP   B CB   1 
ATOM   5955 C CG   . ASP   B 1 135 ? 35.881 -37.125 1.056   1.00 20.37 ?  135 ASP   B CG   1 
ATOM   5956 O OD1  . ASP   B 1 135 ? 36.745 -37.196 0.157   1.00 20.42 ?  135 ASP   B OD1  1 
ATOM   5957 O OD2  . ASP   B 1 135 ? 34.857 -37.851 1.076   1.00 23.36 -1 135 ASP   B OD2  1 
ATOM   5958 H H    . ASP   B 1 135 ? 36.796 -34.436 3.727   1.00 18.97 ?  135 ASP   B H    1 
ATOM   5959 H HA   . ASP   B 1 135 ? 38.144 -36.068 2.172   1.00 19.87 ?  135 ASP   B HA   1 
ATOM   5960 H HB2  . ASP   B 1 135 ? 36.039 -36.639 3.027   1.00 22.06 ?  135 ASP   B HB2  1 
ATOM   5961 H HB3  . ASP   B 1 135 ? 35.375 -35.487 2.157   1.00 22.06 ?  135 ASP   B HB3  1 
ATOM   5962 N N    . PRO   B 1 136 ? 38.540 -34.798 0.016   1.00 15.62 ?  136 PRO   B N    1 
ATOM   5963 C CA   . PRO   B 1 136 ? 38.642 -33.975 -1.201  1.00 15.10 ?  136 PRO   B CA   1 
ATOM   5964 C C    . PRO   B 1 136 ? 37.453 -34.121 -2.129  1.00 14.10 ?  136 PRO   B C    1 
ATOM   5965 O O    . PRO   B 1 136 ? 37.132 -33.169 -2.850  1.00 13.69 ?  136 PRO   B O    1 
ATOM   5966 C CB   . PRO   B 1 136 ? 39.951 -34.456 -1.845  1.00 16.30 ?  136 PRO   B CB   1 
ATOM   5967 C CG   . PRO   B 1 136 ? 40.133 -35.850 -1.313  1.00 17.17 ?  136 PRO   B CG   1 
ATOM   5968 C CD   . PRO   B 1 136 ? 39.617 -35.798 0.095   1.00 16.85 ?  136 PRO   B CD   1 
ATOM   5969 H HA   . PRO   B 1 136 ? 38.739 -33.038 -0.966  1.00 18.12 ?  136 PRO   B HA   1 
ATOM   5970 H HB2  . PRO   B 1 136 ? 39.862 -34.466 -2.813  1.00 19.56 ?  136 PRO   B HB2  1 
ATOM   5971 H HB3  . PRO   B 1 136 ? 40.685 -33.883 -1.574  1.00 19.56 ?  136 PRO   B HB3  1 
ATOM   5972 H HG2  . PRO   B 1 136 ? 39.616 -36.476 -1.843  1.00 20.61 ?  136 PRO   B HG2  1 
ATOM   5973 H HG3  . PRO   B 1 136 ? 41.074 -36.086 -1.322  1.00 20.61 ?  136 PRO   B HG3  1 
ATOM   5974 H HD2  . PRO   B 1 136 ? 39.255 -36.659 0.358   1.00 20.22 ?  136 PRO   B HD2  1 
ATOM   5975 H HD3  . PRO   B 1 136 ? 40.310 -35.501 0.707   1.00 20.22 ?  136 PRO   B HD3  1 
ATOM   5976 N N    . ILE   B 1 137 ? 36.791 -35.282 -2.136  1.00 14.44 ?  137 ILE   B N    1 
ATOM   5977 C CA   . ILE   B 1 137 ? 35.578 -35.448 -2.935  1.00 15.00 ?  137 ILE   B CA   1 
ATOM   5978 C C    . ILE   B 1 137 ? 34.500 -34.480 -2.462  1.00 14.55 ?  137 ILE   B C    1 
ATOM   5979 O O    . ILE   B 1 137 ? 33.789 -33.865 -3.267  1.00 14.22 ?  137 ILE   B O    1 
ATOM   5980 C CB   . ILE   B 1 137 ? 35.107 -36.917 -2.879  1.00 17.13 ?  137 ILE   B CB   1 
ATOM   5981 C CG1  . ILE   B 1 137 ? 36.102 -37.821 -3.611  1.00 19.73 ?  137 ILE   B CG1  1 
ATOM   5982 C CG2  . ILE   B 1 137 ? 33.707 -37.062 -3.476  1.00 17.83 ?  137 ILE   B CG2  1 
ATOM   5983 C CD1  . ILE   B 1 137 ? 35.796 -39.298 -3.480  1.00 21.99 ?  137 ILE   B CD1  1 
ATOM   5984 H H    . ILE   B 1 137 ? 37.022 -35.982 -1.694  1.00 17.33 ?  137 ILE   B H    1 
ATOM   5985 H HA   . ILE   B 1 137 ? 35.778 -35.241 -3.864  1.00 18.00 ?  137 ILE   B HA   1 
ATOM   5986 H HB   . ILE   B 1 137 ? 35.070 -37.191 -1.954  1.00 20.55 ?  137 ILE   B HB   1 
ATOM   5987 H HG12 . ILE   B 1 137 ? 36.091 -37.601 -4.557  1.00 23.68 ?  137 ILE   B HG12 1 
ATOM   5988 H HG13 . ILE   B 1 137 ? 36.987 -37.670 -3.249  1.00 23.68 ?  137 ILE   B HG13 1 
ATOM   5989 H HG21 . ILE   B 1 137 ? 33.458 -38.003 -3.497  1.00 21.40 ?  137 ILE   B HG21 1 
ATOM   5990 H HG22 . ILE   B 1 137 ? 33.069 -36.584 -2.927  1.00 21.40 ?  137 ILE   B HG22 1 
ATOM   5991 H HG23 . ILE   B 1 137 ? 33.705 -36.706 -4.377  1.00 21.40 ?  137 ILE   B HG23 1 
ATOM   5992 H HD11 . ILE   B 1 137 ? 36.465 -39.788 -3.975  1.00 26.38 ?  137 ILE   B HD11 1 
ATOM   5993 H HD12 . ILE   B 1 137 ? 35.822 -39.546 -2.543  1.00 26.38 ?  137 ILE   B HD12 1 
ATOM   5994 H HD13 . ILE   B 1 137 ? 34.919 -39.486 -3.850  1.00 26.38 ?  137 ILE   B HD13 1 
ATOM   5995 N N    . HIS   B 1 138 ? 34.367 -34.327 -1.149  1.00 14.40 ?  138 HIS   B N    1 
ATOM   5996 C CA   . HIS   B 1 138 ? 33.418 -33.358 -0.617  1.00 14.84 ?  138 HIS   B CA   1 
ATOM   5997 C C    . HIS   B 1 138 ? 33.839 -31.929 -0.934  1.00 13.90 ?  138 HIS   B C    1 
ATOM   5998 O O    . HIS   B 1 138 ? 32.992 -31.083 -1.241  1.00 14.60 ?  138 HIS   B O    1 
ATOM   5999 C CB   . HIS   B 1 138 ? 33.292 -33.538 0.887   1.00 16.04 ?  138 HIS   B CB   1 
ATOM   6000 C CG   . HIS   B 1 138 ? 32.359 -32.558 1.520   1.00 17.10 ?  138 HIS   B CG   1 
ATOM   6001 N ND1  . HIS   B 1 138 ? 31.019 -32.497 1.202   1.00 18.55 ?  138 HIS   B ND1  1 
ATOM   6002 C CD2  . HIS   B 1 138 ? 32.576 -31.578 2.428   1.00 17.79 ?  138 HIS   B CD2  1 
ATOM   6003 C CE1  . HIS   B 1 138 ? 30.448 -31.532 1.900   1.00 18.50 ?  138 HIS   B CE1  1 
ATOM   6004 N NE2  . HIS   B 1 138 ? 31.370 -30.962 2.655   1.00 18.03 ?  138 HIS   B NE2  1 
ATOM   6005 H H    . HIS   B 1 138 ? 34.808 -34.767 -0.560  1.00 17.28 ?  138 HIS   B H    1 
ATOM   6006 H HA   . HIS   B 1 138 ? 32.547 -33.517 -1.018  1.00 17.81 ?  138 HIS   B HA   1 
ATOM   6007 H HB2  . HIS   B 1 138 ? 32.954 -34.428 1.069   1.00 19.24 ?  138 HIS   B HB2  1 
ATOM   6008 H HB3  . HIS   B 1 138 ? 34.164 -33.422 1.289   1.00 19.24 ?  138 HIS   B HB3  1 
ATOM   6009 H HD1  . HIS   B 1 138 ? 30.618 -33.016 0.640   1.00 22.27 ?  138 HIS   B HD1  1 
ATOM   6010 H HD2  . HIS   B 1 138 ? 33.382 -31.368 2.833   1.00 21.35 ?  138 HIS   B HD2  1 
ATOM   6011 H HE1  . HIS   B 1 138 ? 29.543 -31.306 1.869   1.00 22.20 ?  138 HIS   B HE1  1 
ATOM   6012 N N    . SER   B 1 139 ? 35.134 -31.632 -0.851  1.00 13.58 ?  139 SER   B N    1 
ATOM   6013 C CA   . SER   B 1 139 ? 35.577 -30.284 -1.170  1.00 12.98 ?  139 SER   B CA   1 
ATOM   6014 C C    . SER   B 1 139 ? 35.237 -29.932 -2.608  1.00 12.18 ?  139 SER   B C    1 
ATOM   6015 O O    . SER   B 1 139 ? 34.789 -28.816 -2.887  1.00 12.45 ?  139 SER   B O    1 
ATOM   6016 C CB   . SER   B 1 139 ? 37.074 -30.150 -0.910  1.00 13.39 ?  139 SER   B CB   1 
ATOM   6017 O OG   . SER   B 1 139 ? 37.474 -28.812 -1.151  1.00 13.75 ?  139 SER   B OG   1 
ATOM   6018 H H    . SER   B 1 139 ? 35.754 -32.179 -0.628  1.00 16.30 ?  139 SER   B H    1 
ATOM   6019 H HA   . SER   B 1 139 ? 35.114 -29.658 -0.601  1.00 15.57 ?  139 SER   B HA   1 
ATOM   6020 H HB2  . SER   B 1 139 ? 37.260 -30.378 0.015   1.00 16.07 ?  139 SER   B HB2  1 
ATOM   6021 H HB3  . SER   B 1 139 ? 37.564 -30.743 -1.505  1.00 16.07 ?  139 SER   B HB3  1 
ATOM   6022 H HG   . SER   B 1 139 ? 38.298 -28.726 -1.008  1.00 16.51 ?  139 SER   B HG   1 
ATOM   6023 N N    . LEU   B 1 140 ? 35.422 -30.877 -3.532  1.00 11.94 ?  140 LEU   B N    1 
ATOM   6024 C CA   . LEU   B 1 140 ? 35.062 -30.628 -4.922  1.00 11.83 ?  140 LEU   B CA   1 
ATOM   6025 C C    . LEU   B 1 140 ? 33.561 -30.398 -5.055  1.00 12.23 ?  140 LEU   B C    1 
ATOM   6026 O O    . LEU   B 1 140 ? 33.124 -29.516 -5.799  1.00 12.37 ?  140 LEU   B O    1 
ATOM   6027 C CB   . LEU   B 1 140 ? 35.540 -31.788 -5.803  1.00 12.26 ?  140 LEU   B CB   1 
ATOM   6028 C CG   . LEU   B 1 140 ? 35.180 -31.680 -7.281  1.00 12.45 ?  140 LEU   B CG   1 
ATOM   6029 C CD1  . LEU   B 1 140 ? 35.741 -30.402 -7.887  1.00 13.20 ?  140 LEU   B CD1  1 
ATOM   6030 C CD2  . LEU   B 1 140 ? 35.670 -32.902 -8.035  1.00 13.35 ?  140 LEU   B CD2  1 
ATOM   6031 H H    . LEU   B 1 140 ? 35.750 -31.658 -3.385  1.00 14.33 ?  140 LEU   B H    1 
ATOM   6032 H HA   . LEU   B 1 140 ? 35.518 -29.825 -5.225  1.00 14.20 ?  140 LEU   B HA   1 
ATOM   6033 H HB2  . LEU   B 1 140 ? 36.510 -31.843 -5.750  1.00 14.71 ?  140 LEU   B HB2  1 
ATOM   6034 H HB3  . LEU   B 1 140 ? 35.151 -32.611 -5.475  1.00 14.71 ?  140 LEU   B HB3  1 
ATOM   6035 H HG   . LEU   B 1 140 ? 34.214 -31.644 -7.368  1.00 14.95 ?  140 LEU   B HG   1 
ATOM   6036 H HD11 . LEU   B 1 140 ? 35.604 -30.425 -8.847  1.00 15.85 ?  140 LEU   B HD11 1 
ATOM   6037 H HD12 . LEU   B 1 140 ? 35.274 -29.640 -7.507  1.00 15.85 ?  140 LEU   B HD12 1 
ATOM   6038 H HD13 . LEU   B 1 140 ? 36.686 -30.347 -7.687  1.00 15.85 ?  140 LEU   B HD13 1 
ATOM   6039 H HD21 . LEU   B 1 140 ? 35.425 -32.809 -8.971  1.00 16.02 ?  140 LEU   B HD21 1 
ATOM   6040 H HD22 . LEU   B 1 140 ? 36.630 -32.961 -7.947  1.00 16.02 ?  140 LEU   B HD22 1 
ATOM   6041 H HD23 . LEU   B 1 140 ? 35.246 -33.687 -7.660  1.00 16.02 ?  140 LEU   B HD23 1 
ATOM   6042 N N    . ARG   B 1 141 ? 32.759 -31.188 -4.336  1.00 12.42 ?  141 ARG   B N    1 
ATOM   6043 C CA   . ARG   B 1 141 ? 31.307 -31.013 -4.321  1.00 13.61 ?  141 ARG   B CA   1 
ATOM   6044 C C    . ARG   B 1 141 ? 30.930 -29.599 -3.895  1.00 12.95 ?  141 ARG   B C    1 
ATOM   6045 O O    . ARG   B 1 141 ? 30.127 -28.922 -4.553  1.00 12.99 ?  141 ARG   B O    1 
ATOM   6046 C CB   . ARG   B 1 141 ? 30.718 -32.037 -3.341  1.00 15.45 ?  141 ARG   B CB   1 
ATOM   6047 C CG   . ARG   B 1 141 ? 29.255 -31.919 -3.014  1.00 17.49 ?  141 ARG   B CG   1 
ATOM   6048 C CD   . ARG   B 1 141 ? 28.456 -32.565 -4.072  1.00 19.36 ?  141 ARG   B CD   1 
ATOM   6049 N NE   . ARG   B 1 141 ? 28.195 -31.659 -5.179  1.00 19.96 ?  141 ARG   B NE   1 
ATOM   6050 C CZ   . ARG   B 1 141 ? 28.183 -32.014 -6.457  1.00 19.83 ?  141 ARG   B CZ   1 
ATOM   6051 N NH1  . ARG   B 1 141 ? 28.609 -33.204 -6.850  1.00 19.68 ?  141 ARG   B NH1  1 
ATOM   6052 N NH2  . ARG   B 1 141 ? 27.732 -31.151 -7.362  1.00 20.35 ?  141 ARG   B NH2  1 
ATOM   6053 H H    . ARG   B 1 141 ? 33.040 -31.826 -3.839  1.00 14.90 ?  141 ARG   B H    1 
ATOM   6054 H HA   . ARG   B 1 141 ? 30.948 -31.179 -5.204  1.00 16.33 ?  141 ARG   B HA   1 
ATOM   6055 H HB2  . ARG   B 1 141 ? 30.872 -32.924 -3.707  1.00 18.53 ?  141 ARG   B HB2  1 
ATOM   6056 H HB3  . ARG   B 1 141 ? 31.203 -31.960 -2.505  1.00 18.53 ?  141 ARG   B HB3  1 
ATOM   6057 H HG2  . ARG   B 1 141 ? 29.083 -32.362 -2.171  1.00 20.99 ?  141 ARG   B HG2  1 
ATOM   6058 H HG3  . ARG   B 1 141 ? 28.999 -30.980 -2.956  1.00 20.99 ?  141 ARG   B HG3  1 
ATOM   6059 H HD2  . ARG   B 1 141 ? 28.936 -33.345 -4.405  1.00 23.24 ?  141 ARG   B HD2  1 
ATOM   6060 H HD3  . ARG   B 1 141 ? 27.610 -32.844 -3.697  1.00 23.24 ?  141 ARG   B HD3  1 
ATOM   6061 H HE   . ARG   B 1 141 ? 28.009 -30.843 -4.989  1.00 23.95 ?  141 ARG   B HE   1 
ATOM   6062 H HH11 . ARG   B 1 141 ? 28.884 -33.783 -6.277  1.00 23.62 ?  141 ARG   B HH11 1 
ATOM   6063 H HH12 . ARG   B 1 141 ? 28.593 -33.409 -7.684  1.00 23.62 ?  141 ARG   B HH12 1 
ATOM   6064 H HH21 . ARG   B 1 141 ? 27.466 -30.369 -7.118  1.00 24.42 ?  141 ARG   B HH21 1 
ATOM   6065 H HH22 . ARG   B 1 141 ? 27.740 -31.358 -8.198  1.00 24.42 ?  141 ARG   B HH22 1 
ATOM   6066 N N    . VAL   B 1 142 ? 31.477 -29.149 -2.768  1.00 12.67 ?  142 VAL   B N    1 
ATOM   6067 C CA   . VAL   B 1 142 ? 31.139 -27.816 -2.285  1.00 12.53 ?  142 VAL   B CA   1 
ATOM   6068 C C    . VAL   B 1 142 ? 31.614 -26.760 -3.276  1.00 12.24 ?  142 VAL   B C    1 
ATOM   6069 O O    . VAL   B 1 142 ? 30.918 -25.770 -3.529  1.00 12.91 ?  142 VAL   B O    1 
ATOM   6070 C CB   . VAL   B 1 142 ? 31.683 -27.586 -0.862  1.00 13.27 ?  142 VAL   B CB   1 
ATOM   6071 C CG1  . VAL   B 1 142 ? 31.363 -26.169 -0.387  1.00 13.34 ?  142 VAL   B CG1  1 
ATOM   6072 C CG2  . VAL   B 1 142 ? 31.095 -28.607 0.099   1.00 14.13 ?  142 VAL   B CG2  1 
ATOM   6073 H H    . VAL   B 1 142 ? 32.036 -29.583 -2.278  1.00 15.21 ?  142 VAL   B H    1 
ATOM   6074 H HA   . VAL   B 1 142 ? 30.178 -27.746 -2.234  1.00 15.04 ?  142 VAL   B HA   1 
ATOM   6075 H HB   . VAL   B 1 142 ? 32.648 -27.693 -0.864  1.00 15.93 ?  142 VAL   B HB   1 
ATOM   6076 H HG11 . VAL   B 1 142 ? 31.547 -26.109 0.562   1.00 16.01 ?  142 VAL   B HG11 1 
ATOM   6077 H HG12 . VAL   B 1 142 ? 31.917 -25.539 -0.873  1.00 16.01 ?  142 VAL   B HG12 1 
ATOM   6078 H HG13 . VAL   B 1 142 ? 30.425 -25.988 -0.555  1.00 16.01 ?  142 VAL   B HG13 1 
ATOM   6079 H HG21 . VAL   B 1 142 ? 31.414 -28.421 0.995   1.00 16.95 ?  142 VAL   B HG21 1 
ATOM   6080 H HG22 . VAL   B 1 142 ? 30.126 -28.542 0.073   1.00 16.95 ?  142 VAL   B HG22 1 
ATOM   6081 H HG23 . VAL   B 1 142 ? 31.372 -29.496 -0.174  1.00 16.95 ?  142 VAL   B HG23 1 
ATOM   6082 N N    . CYS   B 1 143 ? 32.801 -26.952 -3.855  1.00 11.73 ?  143 CYS   B N    1 
ATOM   6083 C CA   . CYS   B 1 143 ? 33.297 -26.014 -4.858  1.00 11.88 ?  143 CYS   B CA   1 
ATOM   6084 C C    . CYS   B 1 143 ? 32.298 -25.864 -6.000  1.00 11.70 ?  143 CYS   B C    1 
ATOM   6085 O O    . CYS   B 1 143 ? 31.893 -24.751 -6.354  1.00 12.23 ?  143 CYS   B O    1 
ATOM   6086 C CB   . CYS   B 1 143 ? 34.656 -26.494 -5.382  1.00 12.40 ?  143 CYS   B CB   1 
ATOM   6087 S SG   . CYS   B 1 143 ? 35.405 -25.399 -6.604  1.00 12.73 ?  143 CYS   B SG   1 
ATOM   6088 H H    . CYS   B 1 143 ? 33.330 -27.604 -3.687  1.00 14.08 ?  143 CYS   B H    1 
ATOM   6089 H HA   . CYS   B 1 143 ? 33.422 -25.142 -4.452  1.00 14.26 ?  143 CYS   B HA   1 
ATOM   6090 H HB2  . CYS   B 1 143 ? 35.274 -26.570 -4.636  1.00 14.88 ?  143 CYS   B HB2  1 
ATOM   6091 H HB3  . CYS   B 1 143 ? 34.542 -27.361 -5.793  1.00 14.88 ?  143 CYS   B HB3  1 
ATOM   6092 H HG   . CYS   B 1 143 ? 36.480 -25.838 -6.919  1.00 15.27 ?  143 CYS   B HG   1 
ATOM   6093 N N    . VAL   B 1 144 ? 31.886 -26.986 -6.589  1.00 12.12 ?  144 VAL   B N    1 
ATOM   6094 C CA   . VAL   B 1 144 ? 30.986 -26.925 -7.735  1.00 13.19 ?  144 VAL   B CA   1 
ATOM   6095 C C    . VAL   B 1 144 ? 29.647 -26.314 -7.357  1.00 13.05 ?  144 VAL   B C    1 
ATOM   6096 O O    . VAL   B 1 144 ? 29.031 -25.604 -8.163  1.00 14.37 ?  144 VAL   B O    1 
ATOM   6097 C CB   . VAL   B 1 144 ? 30.828 -28.335 -8.320  1.00 15.81 ?  144 VAL   B CB   1 
ATOM   6098 C CG1  . VAL   B 1 144 ? 29.559 -28.445 -9.168  1.00 18.38 ?  144 VAL   B CG1  1 
ATOM   6099 C CG2  . VAL   B 1 144 ? 32.077 -28.735 -9.100  1.00 15.90 ?  144 VAL   B CG2  1 
ATOM   6100 H H    . VAL   B 1 144 ? 32.123 -27.781 -6.361  1.00 14.55 ?  144 VAL   B H    1 
ATOM   6101 H HA   . VAL   B 1 144 ? 31.376 -26.367 -8.423  1.00 15.83 ?  144 VAL   B HA   1 
ATOM   6102 H HB   . VAL   B 1 144 ? 30.732 -28.966 -7.588  1.00 18.98 ?  144 VAL   B HB   1 
ATOM   6103 H HG11 . VAL   B 1 144 ? 29.636 -29.222 -9.746  1.00 22.06 ?  144 VAL   B HG11 1 
ATOM   6104 H HG12 . VAL   B 1 144 ? 28.795 -28.549 -8.581  1.00 22.06 ?  144 VAL   B HG12 1 
ATOM   6105 H HG13 . VAL   B 1 144 ? 29.467 -27.645 -9.705  1.00 22.06 ?  144 VAL   B HG13 1 
ATOM   6106 H HG21 . VAL   B 1 144 ? 31.954 -29.631 -9.458  1.00 19.08 ?  144 VAL   B HG21 1 
ATOM   6107 H HG22 . VAL   B 1 144 ? 32.206 -28.106 -9.829  1.00 19.08 ?  144 VAL   B HG22 1 
ATOM   6108 H HG23 . VAL   B 1 144 ? 32.838 -28.717 -8.505  1.00 19.08 ?  144 VAL   B HG23 1 
ATOM   6109 N N    . ASP   B 1 145 ? 29.180 -26.561 -6.136  1.00 13.31 ?  145 ASP   B N    1 
ATOM   6110 C CA   . ASP   B 1 145 ? 27.871 -26.090 -5.705  1.00 14.17 ?  145 ASP   B CA   1 
ATOM   6111 C C    . ASP   B 1 145 ? 27.900 -24.664 -5.166  1.00 13.68 ?  145 ASP   B C    1 
ATOM   6112 O O    . ASP   B 1 145 ? 26.837 -24.117 -4.847  1.00 15.53 ?  145 ASP   B O    1 
ATOM   6113 C CB   . ASP   B 1 145 ? 27.279 -27.010 -4.629  1.00 15.82 ?  145 ASP   B CB   1 
ATOM   6114 C CG   . ASP   B 1 145 ? 26.920 -28.384 -5.145  1.00 17.52 ?  145 ASP   B CG   1 
ATOM   6115 O OD1  . ASP   B 1 145 ? 26.827 -28.581 -6.371  1.00 18.13 ?  145 ASP   B OD1  1 
ATOM   6116 O OD2  . ASP   B 1 145 ? 26.717 -29.268 -4.295  1.00 19.61 -1 145 ASP   B OD2  1 
ATOM   6117 H H    . ASP   B 1 145 ? 29.610 -26.996 -5.533  1.00 15.98 ?  145 ASP   B H    1 
ATOM   6118 H HA   . ASP   B 1 145 ? 27.274 -26.091 -6.465  1.00 17.01 ?  145 ASP   B HA   1 
ATOM   6119 H HB2  . ASP   B 1 145 ? 27.919 -27.131 -3.925  1.00 18.98 ?  145 ASP   B HB2  1 
ATOM   6120 H HB3  . ASP   B 1 145 ? 26.465 -26.603 -4.285  1.00 18.98 ?  145 ASP   B HB3  1 
ATOM   6121 N N    . THR   B 1 146 ? 29.078 -24.049 -5.051  1.00 12.18 ?  146 THR   B N    1 
ATOM   6122 C CA   . THR   B 1 146 ? 29.214 -22.727 -4.442  1.00 11.77 ?  146 THR   B CA   1 
ATOM   6123 C C    . THR   B 1 146 ? 29.842 -21.694 -5.359  1.00 11.52 ?  146 THR   B C    1 
ATOM   6124 O O    . THR   B 1 146 ? 29.388 -20.536 -5.400  1.00 12.17 ?  146 THR   B O    1 
ATOM   6125 C CB   . THR   B 1 146 ? 30.042 -22.835 -3.154  1.00 12.27 ?  146 THR   B CB   1 
ATOM   6126 O OG1  . THR   B 1 146 ? 29.457 -23.823 -2.298  1.00 12.26 ?  146 THR   B OG1  1 
ATOM   6127 C CG2  . THR   B 1 146 ? 30.119 -21.499 -2.429  1.00 12.51 ?  146 THR   B CG2  1 
ATOM   6128 H H    . THR   B 1 146 ? 29.828 -24.382 -5.320  1.00 14.62 ?  146 THR   B H    1 
ATOM   6129 H HA   . THR   B 1 146 ? 28.341 -22.400 -4.201  1.00 14.13 ?  146 THR   B HA   1 
ATOM   6130 H HB   . THR   B 1 146 ? 30.948 -23.099 -3.378  1.00 14.73 ?  146 THR   B HB   1 
ATOM   6131 H HG1  . THR   B 1 146 ? 29.492 -24.581 -2.676  1.00 14.72 ?  146 THR   B HG1  1 
ATOM   6132 H HG21 . THR   B 1 146 ? 30.480 -21.630 -1.539  1.00 15.01 ?  146 THR   B HG21 1 
ATOM   6133 H HG22 . THR   B 1 146 ? 30.698 -20.890 -2.916  1.00 15.01 ?  146 THR   B HG22 1 
ATOM   6134 H HG23 . THR   B 1 146 ? 29.236 -21.111 -2.360  1.00 15.01 ?  146 THR   B HG23 1 
ATOM   6135 N N    . VAL   B 1 147 ? 30.908 -22.065 -6.058  1.00 11.41 ?  147 VAL   B N    1 
ATOM   6136 C CA   . VAL   B 1 147 ? 31.632 -21.125 -6.900  1.00 11.24 ?  147 VAL   B CA   1 
ATOM   6137 C C    . VAL   B 1 147 ? 30.899 -20.993 -8.222  1.00 11.55 ?  147 VAL   B C    1 
ATOM   6138 O O    . VAL   B 1 147 ? 30.531 -21.997 -8.849  1.00 12.25 ?  147 VAL   B O    1 
ATOM   6139 C CB   . VAL   B 1 147 ? 33.083 -21.588 -7.107  1.00 11.63 ?  147 VAL   B CB   1 
ATOM   6140 C CG1  . VAL   B 1 147 ? 33.849 -20.574 -7.925  1.00 11.86 ?  147 VAL   B CG1  1 
ATOM   6141 C CG2  . VAL   B 1 147 ? 33.763 -21.807 -5.765  1.00 11.80 ?  147 VAL   B CG2  1 
ATOM   6142 H H    . VAL   B 1 147 ? 31.242 -22.861 -6.061  1.00 13.69 ?  147 VAL   B H    1 
ATOM   6143 H HA   . VAL   B 1 147 ? 31.658 -20.256 -6.475  1.00 13.49 ?  147 VAL   B HA   1 
ATOM   6144 H HB   . VAL   B 1 147 ? 33.092 -22.434 -7.593  1.00 13.96 ?  147 VAL   B HB   1 
ATOM   6145 H HG11 . VAL   B 1 147 ? 34.793 -20.801 -7.914  1.00 14.23 ?  147 VAL   B HG11 1 
ATOM   6146 H HG12 . VAL   B 1 147 ? 33.520 -20.582 -8.837  1.00 14.23 ?  147 VAL   B HG12 1 
ATOM   6147 H HG13 . VAL   B 1 147 ? 33.719 -19.694 -7.533  1.00 14.23 ?  147 VAL   B HG13 1 
ATOM   6148 H HG21 . VAL   B 1 147 ? 34.704 -21.998 -5.914  1.00 14.16 ?  147 VAL   B HG21 1 
ATOM   6149 H HG22 . VAL   B 1 147 ? 33.671 -21.000 -5.235  1.00 14.16 ?  147 VAL   B HG22 1 
ATOM   6150 H HG23 . VAL   B 1 147 ? 33.342 -22.552 -5.314  1.00 14.16 ?  147 VAL   B HG23 1 
ATOM   6151 N N    . ARG   B 1 148 ? 30.698 -19.747 -8.650  1.00 11.49 ?  148 ARG   B N    1 
ATOM   6152 C CA   . ARG   B 1 148 ? 30.074 -19.429 -9.921  1.00 11.84 ?  148 ARG   B CA   1 
ATOM   6153 C C    . ARG   B 1 148 ? 31.033 -18.761 -10.894 1.00 11.76 ?  148 ARG   B C    1 
ATOM   6154 O O    . ARG   B 1 148 ? 30.750 -18.739 -12.094 1.00 13.11 ?  148 ARG   B O    1 
ATOM   6155 C CB   . ARG   B 1 148 ? 28.837 -18.539 -9.700  1.00 12.14 ?  148 ARG   B CB   1 
ATOM   6156 C CG   . ARG   B 1 148 ? 27.758 -19.243 -8.874  1.00 12.91 ?  148 ARG   B CG   1 
ATOM   6157 C CD   . ARG   B 1 148 ? 26.548 -18.350 -8.572  1.00 13.69 ?  148 ARG   B CD   1 
ATOM   6158 N NE   . ARG   B 1 148 ? 26.939 -17.148 -7.844  1.00 13.69 ?  148 ARG   B NE   1 
ATOM   6159 C CZ   . ARG   B 1 148 ? 27.249 -17.114 -6.554  1.00 12.89 ?  148 ARG   B CZ   1 
ATOM   6160 N NH1  . ARG   B 1 148 ? 27.172 -18.192 -5.793  1.00 12.76 ?  148 ARG   B NH1  1 
ATOM   6161 N NH2  . ARG   B 1 148 ? 27.650 -15.965 -6.015  1.00 13.06 ?  148 ARG   B NH2  1 
ATOM   6162 H H    . ARG   B 1 148 ? 30.933 -19.049 -8.201  1.00 13.79 ?  148 ARG   B H    1 
ATOM   6163 H HA   . ARG   B 1 148 ? 29.773 -20.252 -10.329 1.00 14.21 ?  148 ARG   B HA   1 
ATOM   6164 H HB2  . ARG   B 1 148 ? 29.098 -17.738 -9.225  1.00 14.57 ?  148 ARG   B HB2  1 
ATOM   6165 H HB3  . ARG   B 1 148 ? 28.450 -18.314 -10.558 1.00 14.57 ?  148 ARG   B HB3  1 
ATOM   6166 H HG2  . ARG   B 1 148 ? 27.439 -20.022 -9.361  1.00 15.50 ?  148 ARG   B HG2  1 
ATOM   6167 H HG3  . ARG   B 1 148 ? 28.138 -19.523 -8.024  1.00 15.50 ?  148 ARG   B HG3  1 
ATOM   6168 H HD2  . ARG   B 1 148 ? 26.134 -18.078 -9.406  1.00 16.43 ?  148 ARG   B HD2  1 
ATOM   6169 H HD3  . ARG   B 1 148 ? 25.907 -18.845 -8.030  1.00 16.43 ?  148 ARG   B HD3  1 
ATOM   6170 H HE   . ARG   B 1 148 ? 26.967 -16.413 -8.277  1.00 16.43 ?  148 ARG   B HE   1 
ATOM   6171 H HH11 . ARG   B 1 148 ? 26.906 -18.945 -6.122  1.00 15.31 ?  148 ARG   B HH11 1 
ATOM   6172 H HH12 . ARG   B 1 148 ? 27.373 -18.149 -4.954  1.00 15.31 ?  148 ARG   B HH12 1 
ATOM   6173 H HH21 . ARG   B 1 148 ? 27.710 -15.264 -6.503  1.00 15.68 ?  148 ARG   B HH21 1 
ATOM   6174 H HH22 . ARG   B 1 148 ? 27.858 -15.932 -5.181  1.00 15.68 ?  148 ARG   B HH22 1 
ATOM   6175 N N    . THR   B 1 149 ? 32.143 -18.212 -10.406 1.00 11.65 ?  149 THR   B N    1 
ATOM   6176 C CA   . THR   B 1 149 ? 33.183 -17.650 -11.253 1.00 11.72 ?  149 THR   B CA   1 
ATOM   6177 C C    . THR   B 1 149 ? 34.073 -18.789 -11.753 1.00 11.29 ?  149 THR   B C    1 
ATOM   6178 O O    . THR   B 1 149 ? 33.885 -19.957 -11.407 1.00 11.87 ?  149 THR   B O    1 
ATOM   6179 C CB   . THR   B 1 149 ? 33.951 -16.593 -10.471 1.00 12.03 ?  149 THR   B CB   1 
ATOM   6180 O OG1  . THR   B 1 149 ? 34.412 -17.195 -9.261  1.00 11.88 ?  149 THR   B OG1  1 
ATOM   6181 C CG2  . THR   B 1 149 ? 33.056 -15.390 -10.161 1.00 12.41 ?  149 THR   B CG2  1 
ATOM   6182 H H    . THR   B 1 149 ? 32.317 -18.153 -9.566  1.00 13.98 ?  149 THR   B H    1 
ATOM   6183 H HA   . THR   B 1 149 ? 32.772 -17.219 -12.021 1.00 14.07 ?  149 THR   B HA   1 
ATOM   6184 H HB   . THR   B 1 149 ? 34.712 -16.296 -10.989 1.00 14.43 ?  149 THR   B HB   1 
ATOM   6185 H HG1  . THR   B 1 149 ? 34.832 -16.628 -8.797  1.00 14.26 ?  149 THR   B HG1  1 
ATOM   6186 H HG21 . THR   B 1 149 ? 33.561 -14.720 -9.677  1.00 14.89 ?  149 THR   B HG21 1 
ATOM   6187 H HG22 . THR   B 1 149 ? 32.728 -15.003 -10.988 1.00 14.89 ?  149 THR   B HG22 1 
ATOM   6188 H HG23 . THR   B 1 149 ? 32.300 -15.668 -9.622  1.00 14.89 ?  149 THR   B HG23 1 
ATOM   6189 N N    . ASN   B 1 150 ? 35.035 -18.470 -12.607 1.00 11.62 ?  150 ASN   B N    1 
ATOM   6190 C CA   . ASN   B 1 150 ? 35.799 -19.501 -13.300 1.00 12.08 ?  150 ASN   B CA   1 
ATOM   6191 C C    . ASN   B 1 150 ? 36.964 -19.951 -12.430 1.00 11.83 ?  150 ASN   B C    1 
ATOM   6192 O O    . ASN   B 1 150 ? 37.890 -19.177 -12.166 1.00 12.57 ?  150 ASN   B O    1 
ATOM   6193 C CB   . ASN   B 1 150 ? 36.270 -18.980 -14.650 1.00 13.55 ?  150 ASN   B CB   1 
ATOM   6194 C CG   . ASN   B 1 150 ? 35.119 -18.746 -15.589 1.00 16.18 ?  150 ASN   B CG   1 
ATOM   6195 O OD1  . ASN   B 1 150 ? 34.227 -19.584 -15.701 1.00 17.42 ?  150 ASN   B OD1  1 
ATOM   6196 N ND2  . ASN   B 1 150 ? 35.101 -17.592 -16.237 1.00 17.49 ?  150 ASN   B ND2  1 
ATOM   6197 H H    . ASN   B 1 150 ? 35.281 -17.661 -12.795 1.00 13.94 ?  150 ASN   B H    1 
ATOM   6198 H HA   . ASN   B 1 150 ? 35.220 -20.266 -13.459 1.00 14.49 ?  150 ASN   B HA   1 
ATOM   6199 H HB2  . ASN   B 1 150 ? 36.732 -18.136 -14.521 1.00 16.26 ?  150 ASN   B HB2  1 
ATOM   6200 H HB3  . ASN   B 1 150 ? 36.863 -19.629 -15.054 1.00 16.26 ?  150 ASN   B HB3  1 
ATOM   6201 H HD21 . ASN   B 1 150 ? 34.462 -17.409 -16.786 1.00 20.99 ?  150 ASN   B HD21 1 
ATOM   6202 H HD22 . ASN   B 1 150 ? 35.740 -17.022 -16.127 1.00 20.99 ?  150 ASN   B HD22 1 
ATOM   6203 N N    . VAL   B 1 151 ? 36.917 -21.201 -11.978 1.00 11.33 ?  151 VAL   B N    1 
ATOM   6204 C CA   . VAL   B 1 151 ? 37.933 -21.735 -11.087 1.00 11.44 ?  151 VAL   B CA   1 
ATOM   6205 C C    . VAL   B 1 151 ? 38.641 -22.902 -11.761 1.00 11.17 ?  151 VAL   B C    1 
ATOM   6206 O O    . VAL   B 1 151 ? 38.002 -23.834 -12.273 1.00 12.16 ?  151 VAL   B O    1 
ATOM   6207 C CB   . VAL   B 1 151 ? 37.376 -22.064 -9.688  1.00 12.84 ?  151 VAL   B CB   1 
ATOM   6208 C CG1  . VAL   B 1 151 ? 36.214 -23.061 -9.755  1.00 13.69 ?  151 VAL   B CG1  1 
ATOM   6209 C CG2  . VAL   B 1 151 ? 38.493 -22.544 -8.773  1.00 13.60 ?  151 VAL   B CG2  1 
ATOM   6210 H H    . VAL   B 1 151 ? 36.285 -21.761 -12.171 1.00 13.59 ?  151 VAL   B H    1 
ATOM   6211 H HA   . VAL   B 1 151 ? 38.597 -21.042 -10.957 1.00 13.73 ?  151 VAL   B HA   1 
ATOM   6212 H HB   . VAL   B 1 151 ? 37.025 -21.246 -9.300  1.00 15.41 ?  151 VAL   B HB   1 
ATOM   6213 H HG11 . VAL   B 1 151 ? 35.901 -23.249 -8.853  1.00 16.43 ?  151 VAL   B HG11 1 
ATOM   6214 H HG12 . VAL   B 1 151 ? 35.491 -22.676 -10.278 1.00 16.43 ?  151 VAL   B HG12 1 
ATOM   6215 H HG13 . VAL   B 1 151 ? 36.520 -23.882 -10.172 1.00 16.43 ?  151 VAL   B HG13 1 
ATOM   6216 H HG21 . VAL   B 1 151 ? 38.149 -22.621 -7.867  1.00 16.32 ?  151 VAL   B HG21 1 
ATOM   6217 H HG22 . VAL   B 1 151 ? 38.809 -23.407 -9.079  1.00 16.32 ?  151 VAL   B HG22 1 
ATOM   6218 H HG23 . VAL   B 1 151 ? 39.218 -21.898 -8.792  1.00 16.32 ?  151 VAL   B HG23 1 
ATOM   6219 N N    . TYR   B 1 152 ? 39.971 -22.809 -11.778 1.00 10.84 ?  152 TYR   B N    1 
ATOM   6220 C CA   . TYR   B 1 152 ? 40.884 -23.786 -12.356 1.00 11.04 ?  152 TYR   B CA   1 
ATOM   6221 C C    . TYR   B 1 152 ? 41.604 -24.465 -11.195 1.00 10.61 ?  152 TYR   B C    1 
ATOM   6222 O O    . TYR   B 1 152 ? 42.450 -23.851 -10.540 1.00 11.09 ?  152 TYR   B O    1 
ATOM   6223 C CB   . TYR   B 1 152 ? 41.855 -23.075 -13.302 1.00 11.96 ?  152 TYR   B CB   1 
ATOM   6224 C CG   . TYR   B 1 152 ? 41.177 -22.617 -14.572 1.00 12.36 ?  152 TYR   B CG   1 
ATOM   6225 C CD1  . TYR   B 1 152 ? 40.507 -21.399 -14.642 1.00 12.81 ?  152 TYR   B CD1  1 
ATOM   6226 C CD2  . TYR   B 1 152 ? 41.182 -23.428 -15.694 1.00 13.50 ?  152 TYR   B CD2  1 
ATOM   6227 C CE1  . TYR   B 1 152 ? 39.866 -21.009 -15.803 1.00 13.92 ?  152 TYR   B CE1  1 
ATOM   6228 C CE2  . TYR   B 1 152 ? 40.550 -23.050 -16.854 1.00 14.52 ?  152 TYR   B CE2  1 
ATOM   6229 C CZ   . TYR   B 1 152 ? 39.896 -21.838 -16.910 1.00 14.49 ?  152 TYR   B CZ   1 
ATOM   6230 O OH   . TYR   B 1 152 ? 39.268 -21.475 -18.078 1.00 17.05 ?  152 TYR   B OH   1 
ATOM   6231 H H    . TYR   B 1 152 ? 40.393 -22.145 -11.427 1.00 13.01 ?  152 TYR   B H    1 
ATOM   6232 H HA   . TYR   B 1 152 ? 40.381 -24.457 -12.853 1.00 13.25 ?  152 TYR   B HA   1 
ATOM   6233 H HB2  . TYR   B 1 152 ? 42.213 -22.297 -12.848 1.00 14.36 ?  152 TYR   B HB2  1 
ATOM   6234 H HB3  . TYR   B 1 152 ? 42.570 -23.684 -13.536 1.00 14.36 ?  152 TYR   B HB3  1 
ATOM   6235 H HD1  . TYR   B 1 152 ? 40.482 -20.846 -13.892 1.00 15.37 ?  152 TYR   B HD1  1 
ATOM   6236 H HD2  . TYR   B 1 152 ? 41.621 -24.251 -15.659 1.00 16.21 ?  152 TYR   B HD2  1 
ATOM   6237 H HE1  . TYR   B 1 152 ? 39.427 -20.192 -15.842 1.00 16.71 ?  152 TYR   B HE1  1 
ATOM   6238 H HE2  . TYR   B 1 152 ? 40.573 -23.604 -17.600 1.00 17.43 ?  152 TYR   B HE2  1 
ATOM   6239 H HH   . TYR   B 1 152 ? 38.917 -20.718 -17.983 1.00 20.46 ?  152 TYR   B HH   1 
ATOM   6240 N N    . LEU   B 1 153 ? 41.242 -25.723 -10.927 1.00 10.87 ?  153 LEU   B N    1 
ATOM   6241 C CA   . LEU   B 1 153 ? 41.743 -26.474 -9.785  1.00 10.85 ?  153 LEU   B CA   1 
ATOM   6242 C C    . LEU   B 1 153 ? 42.976 -27.278 -10.173 1.00 11.31 ?  153 LEU   B C    1 
ATOM   6243 O O    . LEU   B 1 153 ? 42.963 -28.006 -11.169 1.00 12.40 ?  153 LEU   B O    1 
ATOM   6244 C CB   . LEU   B 1 153 ? 40.659 -27.425 -9.269  1.00 11.14 ?  153 LEU   B CB   1 
ATOM   6245 C CG   . LEU   B 1 153 ? 39.402 -26.767 -8.710  1.00 11.94 ?  153 LEU   B CG   1 
ATOM   6246 C CD1  . LEU   B 1 153 ? 38.303 -27.807 -8.552  1.00 12.75 ?  153 LEU   B CD1  1 
ATOM   6247 C CD2  . LEU   B 1 153 ? 39.695 -26.094 -7.378  1.00 12.69 ?  153 LEU   B CD2  1 
ATOM   6248 H H    . LEU   B 1 153 ? 40.681 -26.175 -11.408 1.00 13.05 ?  153 LEU   B H    1 
ATOM   6249 H HA   . LEU   B 1 153 ? 41.975 -25.860 -9.075  1.00 13.03 ?  153 LEU   B HA   1 
ATOM   6250 H HB2  . LEU   B 1 153 ? 40.384 -28.004 -9.995  1.00 13.37 ?  153 LEU   B HB2  1 
ATOM   6251 H HB3  . LEU   B 1 153 ? 41.042 -27.965 -8.555  1.00 13.37 ?  153 LEU   B HB3  1 
ATOM   6252 H HG   . LEU   B 1 153 ? 39.090 -26.086 -9.329  1.00 14.32 ?  153 LEU   B HG   1 
ATOM   6253 H HD11 . LEU   B 1 153 ? 37.498 -27.365 -8.233  1.00 15.30 ?  153 LEU   B HD11 1 
ATOM   6254 H HD12 . LEU   B 1 153 ? 38.138 -28.217 -9.411  1.00 15.30 ?  153 LEU   B HD12 1 
ATOM   6255 H HD13 . LEU   B 1 153 ? 38.593 -28.470 -7.910  1.00 15.30 ?  153 LEU   B HD13 1 
ATOM   6256 H HD21 . LEU   B 1 153 ? 38.877 -25.717 -7.022  1.00 15.23 ?  153 LEU   B HD21 1 
ATOM   6257 H HD22 . LEU   B 1 153 ? 40.054 -26.752 -6.764  1.00 15.23 ?  153 LEU   B HD22 1 
ATOM   6258 H HD23 . LEU   B 1 153 ? 40.349 -25.386 -7.520  1.00 15.23 ?  153 LEU   B HD23 1 
ATOM   6259 N N    . ALA   B 1 154 ? 44.025 -27.164 -9.368  1.00 11.27 ?  154 ALA   B N    1 
ATOM   6260 C CA   . ALA   B 1 154 ? 45.254 -27.925 -9.543  1.00 12.45 ?  154 ALA   B CA   1 
ATOM   6261 C C    . ALA   B 1 154 ? 45.317 -29.003 -8.468  1.00 12.65 ?  154 ALA   B C    1 
ATOM   6262 O O    . ALA   B 1 154 ? 45.230 -28.705 -7.270  1.00 14.33 ?  154 ALA   B O    1 
ATOM   6263 C CB   . ALA   B 1 154 ? 46.473 -27.010 -9.464  1.00 13.34 ?  154 ALA   B CB   1 
ATOM   6264 H H    . ALA   B 1 154 ? 44.043 -26.632 -8.688  1.00 13.53 ?  154 ALA   B H    1 
ATOM   6265 H HA   . ALA   B 1 154 ? 45.251 -28.354 -10.406 1.00 14.94 ?  154 ALA   B HA   1 
ATOM   6266 H HB1  . ALA   B 1 154 ? 47.279 -27.539 -9.580  1.00 16.01 ?  154 ALA   B HB1  1 
ATOM   6267 H HB2  . ALA   B 1 154 ? 46.416 -26.340 -10.164 1.00 16.01 ?  154 ALA   B HB2  1 
ATOM   6268 H HB3  . ALA   B 1 154 ? 46.493 -26.572 -8.594  1.00 16.01 ?  154 ALA   B HB3  1 
ATOM   6269 N N    . VAL   B 1 155 ? 45.445 -30.251 -8.898  1.00 12.06 ?  155 VAL   B N    1 
ATOM   6270 C CA   . VAL   B 1 155 ? 45.554 -31.395 -8.003  1.00 12.40 ?  155 VAL   B CA   1 
ATOM   6271 C C    . VAL   B 1 155 ? 46.897 -32.061 -8.280  1.00 12.45 ?  155 VAL   B C    1 
ATOM   6272 O O    . VAL   B 1 155 ? 47.130 -32.563 -9.387  1.00 14.08 ?  155 VAL   B O    1 
ATOM   6273 C CB   . VAL   B 1 155 ? 44.397 -32.387 -8.210  1.00 13.50 ?  155 VAL   B CB   1 
ATOM   6274 C CG1  . VAL   B 1 155 ? 44.578 -33.597 -7.314  1.00 13.66 ?  155 VAL   B CG1  1 
ATOM   6275 C CG2  . VAL   B 1 155 ? 43.063 -31.698 -7.947  1.00 14.55 ?  155 VAL   B CG2  1 
ATOM   6276 H H    . VAL   B 1 155 ? 45.473 -30.465 -9.728  1.00 14.47 ?  155 VAL   B H    1 
ATOM   6277 H HA   . VAL   B 1 155 ? 45.543 -31.096 -7.078  1.00 14.88 ?  155 VAL   B HA   1 
ATOM   6278 H HB   . VAL   B 1 155 ? 44.404 -32.690 -9.131  1.00 16.20 ?  155 VAL   B HB   1 
ATOM   6279 H HG11 . VAL   B 1 155 ? 43.751 -34.103 -7.293  1.00 16.39 ?  155 VAL   B HG11 1 
ATOM   6280 H HG12 . VAL   B 1 155 ? 45.293 -34.156 -7.668  1.00 16.39 ?  155 VAL   B HG12 1 
ATOM   6281 H HG13 . VAL   B 1 155 ? 44.806 -33.301 -6.418  1.00 16.39 ?  155 VAL   B HG13 1 
ATOM   6282 H HG21 . VAL   B 1 155 ? 42.354 -32.352 -8.031  1.00 17.46 ?  155 VAL   B HG21 1 
ATOM   6283 H HG22 . VAL   B 1 155 ? 43.074 -31.333 -7.048  1.00 17.46 ?  155 VAL   B HG22 1 
ATOM   6284 H HG23 . VAL   B 1 155 ? 42.944 -30.988 -8.594  1.00 17.46 ?  155 VAL   B HG23 1 
ATOM   6285 N N    . PHE   B 1 156 ? 47.764 -32.100 -7.265  1.00 12.70 ?  156 PHE   B N    1 
ATOM   6286 C CA   . PHE   B 1 156 ? 49.142 -32.559 -7.463  1.00 13.80 ?  156 PHE   B CA   1 
ATOM   6287 C C    . PHE   B 1 156 ? 49.234 -34.060 -7.739  1.00 14.46 ?  156 PHE   B C    1 
ATOM   6288 O O    . PHE   B 1 156 ? 49.967 -34.491 -8.640  1.00 16.35 ?  156 PHE   B O    1 
ATOM   6289 C CB   . PHE   B 1 156 ? 49.969 -32.191 -6.232  1.00 13.84 ?  156 PHE   B CB   1 
ATOM   6290 C CG   . PHE   B 1 156 ? 51.393 -32.650 -6.292  1.00 14.35 ?  156 PHE   B CG   1 
ATOM   6291 C CD1  . PHE   B 1 156 ? 52.273 -32.102 -7.201  1.00 16.01 ?  156 PHE   B CD1  1 
ATOM   6292 C CD2  . PHE   B 1 156 ? 51.855 -33.616 -5.422  1.00 14.82 ?  156 PHE   B CD2  1 
ATOM   6293 C CE1  . PHE   B 1 156 ? 53.591 -32.508 -7.249  1.00 17.10 ?  156 PHE   B CE1  1 
ATOM   6294 C CE2  . PHE   B 1 156 ? 53.170 -34.029 -5.466  1.00 16.17 ?  156 PHE   B CE2  1 
ATOM   6295 C CZ   . PHE   B 1 156 ? 54.035 -33.476 -6.385  1.00 16.80 ?  156 PHE   B CZ   1 
ATOM   6296 H H    . PHE   B 1 156 ? 47.587 -31.866 -6.457  1.00 15.24 ?  156 PHE   B H    1 
ATOM   6297 H HA   . PHE   B 1 156 ? 49.522 -32.095 -8.223  1.00 16.56 ?  156 PHE   B HA   1 
ATOM   6298 H HB2  . PHE   B 1 156 ? 49.974 -31.227 -6.140  1.00 16.61 ?  156 PHE   B HB2  1 
ATOM   6299 H HB3  . PHE   B 1 156 ? 49.563 -32.595 -5.451  1.00 16.61 ?  156 PHE   B HB3  1 
ATOM   6300 H HD1  . PHE   B 1 156 ? 51.981 -31.441 -7.789  1.00 19.21 ?  156 PHE   B HD1  1 
ATOM   6301 H HD2  . PHE   B 1 156 ? 51.268 -33.995 -4.806  1.00 17.79 ?  156 PHE   B HD2  1 
ATOM   6302 H HE1  . PHE   B 1 156 ? 54.177 -32.129 -7.870  1.00 20.52 ?  156 PHE   B HE1  1 
ATOM   6303 H HE2  . PHE   B 1 156 ? 53.466 -34.691 -4.882  1.00 19.41 ?  156 PHE   B HE2  1 
ATOM   6304 H HZ   . PHE   B 1 156 ? 54.921 -33.756 -6.416  1.00 20.16 ?  156 PHE   B HZ   1 
ATOM   6305 N N    . ASP   B 1 157 ? 48.564 -34.876 -6.935  1.00 15.03 ?  157 ASP   B N    1 
ATOM   6306 C CA   . ASP   B 1 157 ? 48.706 -36.325 -7.022  1.00 16.25 ?  157 ASP   B CA   1 
ATOM   6307 C C    . ASP   B 1 157 ? 47.801 -36.876 -8.119  1.00 16.45 ?  157 ASP   B C    1 
ATOM   6308 O O    . ASP   B 1 157 ? 46.577 -36.760 -8.024  1.00 15.85 ?  157 ASP   B O    1 
ATOM   6309 C CB   . ASP   B 1 157 ? 48.329 -36.935 -5.679  1.00 18.17 ?  157 ASP   B CB   1 
ATOM   6310 C CG   . ASP   B 1 157 ? 48.486 -38.447 -5.653  1.00 20.15 ?  157 ASP   B CG   1 
ATOM   6311 O OD1  . ASP   B 1 157 ? 48.823 -39.055 -6.697  1.00 20.84 ?  157 ASP   B OD1  1 
ATOM   6312 O OD2  . ASP   B 1 157 ? 48.296 -39.029 -4.567  1.00 21.99 -1 157 ASP   B OD2  1 
ATOM   6313 H H    . ASP   B 1 157 ? 48.020 -34.612 -6.325  1.00 18.04 ?  157 ASP   B H    1 
ATOM   6314 H HA   . ASP   B 1 157 ? 49.629 -36.555 -7.224  1.00 19.50 ?  157 ASP   B HA   1 
ATOM   6315 H HB2  . ASP   B 1 157 ? 48.892 -36.552 -4.992  1.00 21.80 ?  157 ASP   B HB2  1 
ATOM   6316 H HB3  . ASP   B 1 157 ? 47.396 -36.725 -5.495  1.00 21.80 ?  157 ASP   B HB3  1 
ATOM   6317 N N    . LYS   B 1 158 ? 48.399 -37.500 -9.143  1.00 17.61 ?  158 LYS   B N    1 
ATOM   6318 C CA   . LYS   B 1 158 ? 47.622 -38.115 -10.225 1.00 18.68 ?  158 LYS   B CA   1 
ATOM   6319 C C    . LYS   B 1 158 ? 46.563 -39.079 -9.695  1.00 18.41 ?  158 LYS   B C    1 
ATOM   6320 O O    . LYS   B 1 158 ? 45.458 -39.168 -10.246 1.00 18.78 ?  158 LYS   B O    1 
ATOM   6321 C CB   . LYS   B 1 158 ? 48.568 -38.835 -11.194 1.00 20.34 ?  158 LYS   B CB   1 
ATOM   6322 C CG   . LYS   B 1 158 ? 47.885 -39.726 -12.223 1.00 22.57 ?  158 LYS   B CG   1 
ATOM   6323 C CD   . LYS   B 1 158 ? 47.060 -38.937 -13.218 1.00 25.07 ?  158 LYS   B CD   1 
ATOM   6324 C CE   . LYS   B 1 158 ? 46.455 -39.855 -14.268 1.00 26.50 ?  158 LYS   B CE   1 
ATOM   6325 N NZ   . LYS   B 1 158 ? 45.397 -39.172 -15.066 1.00 26.72 ?  158 LYS   B NZ   1 
ATOM   6326 H H    . LYS   B 1 158 ? 49.257 -37.584 -9.233  1.00 21.14 ?  158 LYS   B H    1 
ATOM   6327 H HA   . LYS   B 1 158 ? 47.174 -37.415 -10.723 1.00 22.41 ?  158 LYS   B HA   1 
ATOM   6328 H HB2  . LYS   B 1 158 ? 49.080 -38.170 -11.687 1.00 24.41 ?  158 LYS   B HB2  1 
ATOM   6329 H HB3  . LYS   B 1 158 ? 49.175 -39.393 -10.684 1.00 24.41 ?  158 LYS   B HB3  1 
ATOM   6330 H HG2  . LYS   B 1 158 ? 48.565 -40.206 -12.720 1.00 27.08 ?  158 LYS   B HG2  1 
ATOM   6331 H HG3  . LYS   B 1 158 ? 47.302 -40.364 -11.779 1.00 27.08 ?  158 LYS   B HG3  1 
ATOM   6332 H HD2  . LYS   B 1 158 ? 46.340 -38.484 -12.755 1.00 30.08 ?  158 LYS   B HD2  1 
ATOM   6333 H HD3  . LYS   B 1 158 ? 47.631 -38.294 -13.669 1.00 30.08 ?  158 LYS   B HD3  1 
ATOM   6334 H HE2  . LYS   B 1 158 ? 47.149 -40.149 -14.877 1.00 31.80 ?  158 LYS   B HE2  1 
ATOM   6335 H HE3  . LYS   B 1 158 ? 46.052 -40.622 -13.828 1.00 31.80 ?  158 LYS   B HE3  1 
ATOM   6336 H HZ1  . LYS   B 1 158 ? 45.060 -39.731 -15.670 1.00 32.07 ?  158 LYS   B HZ1  1 
ATOM   6337 H HZ2  . LYS   B 1 158 ? 44.742 -38.895 -14.530 1.00 32.07 ?  158 LYS   B HZ2  1 
ATOM   6338 H HZ3  . LYS   B 1 158 ? 45.743 -38.467 -15.486 1.00 32.07 ?  158 LYS   B HZ3  1 
ATOM   6339 N N    . ASN   B 1 159 ? 46.885 -39.837 -8.647  1.00 18.66 ?  159 ASN   B N    1 
ATOM   6340 C CA   . ASN   B 1 159 ? 45.926 -40.814 -8.142  1.00 19.30 ?  159 ASN   B CA   1 
ATOM   6341 C C    . ASN   B 1 159 ? 44.729 -40.136 -7.476  1.00 18.46 ?  159 ASN   B C    1 
ATOM   6342 O O    . ASN   B 1 159 ? 43.599 -40.624 -7.594  1.00 18.69 ?  159 ASN   B O    1 
ATOM   6343 C CB   . ASN   B 1 159 ? 46.626 -41.784 -7.199  1.00 21.22 ?  159 ASN   B CB   1 
ATOM   6344 C CG   . ASN   B 1 159 ? 47.661 -42.626 -7.911  1.00 23.35 ?  159 ASN   B CG   1 
ATOM   6345 O OD1  . ASN   B 1 159 ? 47.416 -43.137 -9.011  1.00 24.44 ?  159 ASN   B OD1  1 
ATOM   6346 N ND2  . ASN   B 1 159 ? 48.827 -42.778 -7.293  1.00 24.29 ?  159 ASN   B ND2  1 
ATOM   6347 H H    . ASN   B 1 159 ? 47.626 -39.792 -8.221  1.00 22.40 ?  159 ASN   B H    1 
ATOM   6348 H HA   . ASN   B 1 159 ? 45.592 -41.328 -8.896  1.00 23.16 ?  159 ASN   B HA   1 
ATOM   6349 H HB2  . ASN   B 1 159 ? 47.075 -41.284 -6.502  1.00 25.46 ?  159 ASN   B HB2  1 
ATOM   6350 H HB3  . ASN   B 1 159 ? 45.970 -42.383 -6.816  1.00 25.46 ?  159 ASN   B HB3  1 
ATOM   6351 H HD21 . ASN   B 1 159 ? 49.451 -43.249 -7.657  1.00 29.15 ?  159 ASN   B HD21 1 
ATOM   6352 H HD22 . ASN   B 1 159 ? 48.959 -42.416 -6.524  1.00 29.15 ?  159 ASN   B HD22 1 
ATOM   6353 N N    . LEU   B 1 160 ? 44.938 -39.002 -6.801  1.00 17.31 ?  160 LEU   B N    1 
ATOM   6354 C CA   . LEU   B 1 160 ? 43.802 -38.271 -6.255  1.00 16.08 ?  160 LEU   B CA   1 
ATOM   6355 C C    . LEU   B 1 160 ? 43.014 -37.605 -7.369  1.00 15.06 ?  160 LEU   B C    1 
ATOM   6356 O O    . LEU   B 1 160 ? 41.779 -37.614 -7.356  1.00 14.76 ?  160 LEU   B O    1 
ATOM   6357 C CB   . LEU   B 1 160 ? 44.260 -37.245 -5.220  1.00 15.98 ?  160 LEU   B CB   1 
ATOM   6358 C CG   . LEU   B 1 160 ? 43.140 -36.341 -4.687  1.00 15.71 ?  160 LEU   B CG   1 
ATOM   6359 C CD1  . LEU   B 1 160 ? 42.010 -37.167 -4.091  1.00 16.55 ?  160 LEU   B CD1  1 
ATOM   6360 C CD2  . LEU   B 1 160 ? 43.679 -35.353 -3.665  1.00 15.54 ?  160 LEU   B CD2  1 
ATOM   6361 H H    . LEU   B 1 160 ? 45.714 -38.641 -6.667  1.00 20.77 ?  160 LEU   B H    1 
ATOM   6362 H HA   . LEU   B 1 160 ? 43.220 -38.904 -5.819  1.00 19.30 ?  160 LEU   B HA   1 
ATOM   6363 H HB2  . LEU   B 1 160 ? 44.649 -37.723 -4.467  1.00 19.17 ?  160 LEU   B HB2  1 
ATOM   6364 H HB3  . LEU   B 1 160 ? 44.939 -36.677 -5.624  1.00 19.17 ?  160 LEU   B HB3  1 
ATOM   6365 H HG   . LEU   B 1 160 ? 42.778 -35.833 -5.425  1.00 18.85 ?  160 LEU   B HG   1 
ATOM   6366 H HD11 . LEU   B 1 160 ? 41.379 -36.568 -3.667  1.00 19.87 ?  160 LEU   B HD11 1 
ATOM   6367 H HD12 . LEU   B 1 160 ? 41.570 -37.665 -4.799  1.00 19.87 ?  160 LEU   B HD12 1 
ATOM   6368 H HD13 . LEU   B 1 160 ? 42.378 -37.782 -3.435  1.00 19.87 ?  160 LEU   B HD13 1 
ATOM   6369 H HD21 . LEU   B 1 160 ? 42.953 -34.784 -3.370  1.00 18.65 ?  160 LEU   B HD21 1 
ATOM   6370 H HD22 . LEU   B 1 160 ? 44.045 -35.844 -2.912  1.00 18.65 ?  160 LEU   B HD22 1 
ATOM   6371 H HD23 . LEU   B 1 160 ? 44.374 -34.818 -4.080  1.00 18.65 ?  160 LEU   B HD23 1 
ATOM   6372 N N    . TYR   B 1 161 ? 43.714 -37.033 -8.350  1.00 15.27 ?  161 TYR   B N    1 
ATOM   6373 C CA   . TYR   B 1 161 ? 43.046 -36.474 -9.520  1.00 15.17 ?  161 TYR   B CA   1 
ATOM   6374 C C    . TYR   B 1 161 ? 42.105 -37.497 -10.142 1.00 15.09 ?  161 TYR   B C    1 
ATOM   6375 O O    . TYR   B 1 161 ? 40.934 -37.204 -10.405 1.00 14.91 ?  161 TYR   B O    1 
ATOM   6376 C CB   . TYR   B 1 161 ? 44.096 -36.000 -10.534 1.00 15.91 ?  161 TYR   B CB   1 
ATOM   6377 C CG   . TYR   B 1 161 ? 43.522 -35.531 -11.849 1.00 16.43 ?  161 TYR   B CG   1 
ATOM   6378 C CD1  . TYR   B 1 161 ? 43.121 -34.214 -12.017 1.00 16.53 ?  161 TYR   B CD1  1 
ATOM   6379 C CD2  . TYR   B 1 161 ? 43.363 -36.406 -12.918 1.00 17.34 ?  161 TYR   B CD2  1 
ATOM   6380 C CE1  . TYR   B 1 161 ? 42.590 -33.779 -13.206 1.00 17.91 ?  161 TYR   B CE1  1 
ATOM   6381 C CE2  . TYR   B 1 161 ? 42.828 -35.980 -14.113 1.00 18.73 ?  161 TYR   B CE2  1 
ATOM   6382 C CZ   . TYR   B 1 161 ? 42.444 -34.662 -14.251 1.00 18.79 ?  161 TYR   B CZ   1 
ATOM   6383 O OH   . TYR   B 1 161 ? 41.906 -34.222 -15.435 1.00 20.49 ?  161 TYR   B OH   1 
ATOM   6384 H H    . TYR   B 1 161 ? 44.568 -36.965 -8.369  1.00 18.33 ?  161 TYR   B H    1 
ATOM   6385 H HA   . TYR   B 1 161 ? 42.520 -35.707 -9.256  1.00 18.20 ?  161 TYR   B HA   1 
ATOM   6386 H HB2  . TYR   B 1 161 ? 44.589 -35.254 -10.151 1.00 19.09 ?  161 TYR   B HB2  1 
ATOM   6387 H HB3  . TYR   B 1 161 ? 44.706 -36.729 -10.726 1.00 19.09 ?  161 TYR   B HB3  1 
ATOM   6388 H HD1  . TYR   B 1 161 ? 43.220 -33.609 -11.316 1.00 19.84 ?  161 TYR   B HD1  1 
ATOM   6389 H HD2  . TYR   B 1 161 ? 43.620 -37.296 -12.829 1.00 20.81 ?  161 TYR   B HD2  1 
ATOM   6390 H HE1  . TYR   B 1 161 ? 42.330 -32.889 -13.302 1.00 21.49 ?  161 TYR   B HE1  1 
ATOM   6391 H HE2  . TYR   B 1 161 ? 42.728 -36.575 -14.823 1.00 22.48 ?  161 TYR   B HE2  1 
ATOM   6392 H HH   . TYR   B 1 161 ? 41.870 -34.858 -15.986 1.00 24.59 ?  161 TYR   B HH   1 
ATOM   6393 N N    . ASP   B 1 162 ? 42.602 -38.718 -10.364 1.00 15.71 ?  162 ASP   B N    1 
ATOM   6394 C CA   . ASP   B 1 162 ? 41.778 -39.754 -10.980 1.00 16.12 ?  162 ASP   B CA   1 
ATOM   6395 C C    . ASP   B 1 162 ? 40.570 -40.096 -10.116 1.00 15.53 ?  162 ASP   B C    1 
ATOM   6396 O O    . ASP   B 1 162 ? 39.469 -40.314 -10.636 1.00 15.76 ?  162 ASP   B O    1 
ATOM   6397 C CB   . ASP   B 1 162 ? 42.607 -41.015 -11.239 1.00 17.80 ?  162 ASP   B CB   1 
ATOM   6398 C CG   . ASP   B 1 162 ? 43.611 -40.848 -12.366 1.00 19.16 ?  162 ASP   B CG   1 
ATOM   6399 O OD1  . ASP   B 1 162 ? 43.482 -39.905 -13.170 1.00 19.50 ?  162 ASP   B OD1  1 
ATOM   6400 O OD2  . ASP   B 1 162 ? 44.524 -41.694 -12.460 1.00 21.11 -1 162 ASP   B OD2  1 
ATOM   6401 H H    . ASP   B 1 162 ? 43.402 -38.966 -10.175 1.00 18.85 ?  162 ASP   B H    1 
ATOM   6402 H HA   . ASP   B 1 162 ? 41.450 -39.435 -11.834 1.00 19.34 ?  162 ASP   B HA   1 
ATOM   6403 H HB2  . ASP   B 1 162 ? 43.100 -41.241 -10.436 1.00 21.37 ?  162 ASP   B HB2  1 
ATOM   6404 H HB3  . ASP   B 1 162 ? 42.012 -41.741 -11.481 1.00 21.37 ?  162 ASP   B HB3  1 
ATOM   6405 N N    A LYS   B 1 163 ? 40.758 -40.170 -8.797  0.74 14.68 ?  163 LYS   B N    1 
ATOM   6406 N N    B LYS   B 1 163 ? 40.750 -40.140 -8.793  0.26 15.83 ?  163 LYS   B N    1 
ATOM   6407 C CA   A LYS   B 1 163 ? 39.627 -40.438 -7.915  0.74 15.01 ?  163 LYS   B CA   1 
ATOM   6408 C CA   B LYS   B 1 163 ? 39.625 -40.440 -7.911  0.26 16.48 ?  163 LYS   B CA   1 
ATOM   6409 C C    A LYS   B 1 163 ? 38.586 -39.327 -7.996  0.74 14.10 ?  163 LYS   B C    1 
ATOM   6410 C C    B LYS   B 1 163 ? 38.587 -39.322 -7.931  0.26 14.91 ?  163 LYS   B C    1 
ATOM   6411 O O    A LYS   B 1 163 ? 37.377 -39.597 -8.028  0.74 14.85 ?  163 LYS   B O    1 
ATOM   6412 O O    B LYS   B 1 163 ? 37.381 -39.585 -7.848  0.26 15.15 ?  163 LYS   B O    1 
ATOM   6413 C CB   A LYS   B 1 163 ? 40.103 -40.612 -6.476  0.74 17.53 ?  163 LYS   B CB   1 
ATOM   6414 C CB   B LYS   B 1 163 ? 40.118 -40.681 -6.485  0.26 19.02 ?  163 LYS   B CB   1 
ATOM   6415 C CG   A LYS   B 1 163 ? 39.020 -41.166 -5.571  0.74 22.29 ?  163 LYS   B CG   1 
ATOM   6416 C CG   B LYS   B 1 163 ? 39.033 -41.202 -5.561  0.26 21.84 ?  163 LYS   B CG   1 
ATOM   6417 C CD   A LYS   B 1 163 ? 39.416 -41.168 -4.108  0.74 26.07 ?  163 LYS   B CD   1 
ATOM   6418 C CD   B LYS   B 1 163 ? 39.492 -41.284 -4.118  0.26 24.21 ?  163 LYS   B CD   1 
ATOM   6419 C CE   A LYS   B 1 163 ? 38.346 -41.859 -3.272  0.74 28.64 ?  163 LYS   B CE   1 
ATOM   6420 C CE   B LYS   B 1 163 ? 38.425 -41.941 -3.257  0.26 26.14 ?  163 LYS   B CE   1 
ATOM   6421 N NZ   A LYS   B 1 163 ? 38.408 -41.476 -1.835  0.74 30.29 ?  163 LYS   B NZ   1 
ATOM   6422 N NZ   B LYS   B 1 163 ? 38.588 -41.623 -1.813  0.26 27.14 ?  163 LYS   B NZ   1 
ATOM   6423 H H    A LYS   B 1 163 ? 41.517 -40.073 -8.400  0.74 17.62 ?  163 LYS   B H    1 
ATOM   6424 H H    B LYS   B 1 163 ? 41.500 -40.007 -8.391  0.26 19.00 ?  163 LYS   B H    1 
ATOM   6425 H HA   A LYS   B 1 163 ? 39.207 -41.266 -8.193  0.74 18.01 ?  163 LYS   B HA   1 
ATOM   6426 H HA   B LYS   B 1 163 ? 39.195 -41.252 -8.217  0.26 19.78 ?  163 LYS   B HA   1 
ATOM   6427 H HB2  A LYS   B 1 163 ? 40.853 -41.230 -6.462  0.74 21.04 ?  163 LYS   B HB2  1 
ATOM   6428 H HB2  B LYS   B 1 163 ? 40.833 -41.338 -6.504  0.26 22.82 ?  163 LYS   B HB2  1 
ATOM   6429 H HB3  A LYS   B 1 163 ? 40.376 -39.751 -6.126  0.74 21.04 ?  163 LYS   B HB3  1 
ATOM   6430 H HB3  B LYS   B 1 163 ? 40.448 -39.846 -6.118  0.26 22.82 ?  163 LYS   B HB3  1 
ATOM   6431 H HG2  A LYS   B 1 163 ? 38.220 -40.626 -5.663  0.74 26.75 ?  163 LYS   B HG2  1 
ATOM   6432 H HG2  B LYS   B 1 163 ? 38.268 -40.606 -5.597  0.26 26.21 ?  163 LYS   B HG2  1 
ATOM   6433 H HG3  A LYS   B 1 163 ? 38.830 -42.084 -5.831  0.74 26.75 ?  163 LYS   B HG3  1 
ATOM   6434 H HG3  B LYS   B 1 163 ? 38.773 -42.093 -5.846  0.26 26.21 ?  163 LYS   B HG3  1 
ATOM   6435 H HD2  A LYS   B 1 163 ? 40.251 -41.651 -3.999  0.74 31.29 ?  163 LYS   B HD2  1 
ATOM   6436 H HD2  B LYS   B 1 163 ? 40.301 -41.818 -4.066  0.26 29.05 ?  163 LYS   B HD2  1 
ATOM   6437 H HD3  A LYS   B 1 163 ? 39.509 -40.254 -3.797  0.74 31.29 ?  163 LYS   B HD3  1 
ATOM   6438 H HD3  B LYS   B 1 163 ? 39.654 -40.390 -3.778  0.26 29.05 ?  163 LYS   B HD3  1 
ATOM   6439 H HE2  A LYS   B 1 163 ? 37.469 -41.625 -3.614  0.74 34.37 ?  163 LYS   B HE2  1 
ATOM   6440 H HE2  B LYS   B 1 163 ? 37.550 -41.632 -3.541  0.26 31.37 ?  163 LYS   B HE2  1 
ATOM   6441 H HE3  A LYS   B 1 163 ? 38.474 -42.818 -3.330  0.74 34.37 ?  163 LYS   B HE3  1 
ATOM   6442 H HE3  B LYS   B 1 163 ? 38.484 -42.904 -3.362  0.26 31.37 ?  163 LYS   B HE3  1 
ATOM   6443 H HZ1  A LYS   B 1 163 ? 37.769 -41.897 -1.380  0.74 36.34 ?  163 LYS   B HZ1  1 
ATOM   6444 H HZ1  B LYS   B 1 163 ? 37.947 -42.022 -1.341  0.26 32.57 ?  163 LYS   B HZ1  1 
ATOM   6445 H HZ2  A LYS   B 1 163 ? 39.200 -41.699 -1.496  0.74 36.34 ?  163 LYS   B HZ2  1 
ATOM   6446 H HZ2  B LYS   B 1 163 ? 39.380 -41.909 -1.527  0.26 32.57 ?  163 LYS   B HZ2  1 
ATOM   6447 H HZ3  A LYS   B 1 163 ? 38.294 -40.598 -1.749  0.74 36.34 ?  163 LYS   B HZ3  1 
ATOM   6448 H HZ3  B LYS   B 1 163 ? 38.534 -40.743 -1.688  0.26 32.57 ?  163 LYS   B HZ3  1 
ATOM   6449 N N    . LEU   B 1 164 ? 39.038 -38.070 -8.033  1.00 13.45 ?  164 LEU   B N    1 
ATOM   6450 C CA   . LEU   B 1 164 ? 38.120 -36.935 -8.083  1.00 12.99 ?  164 LEU   B CA   1 
ATOM   6451 C C    . LEU   B 1 164 ? 37.336 -36.918 -9.389  1.00 13.60 ?  164 LEU   B C    1 
ATOM   6452 O O    . LEU   B 1 164 ? 36.112 -36.728 -9.389  1.00 14.55 ?  164 LEU   B O    1 
ATOM   6453 C CB   . LEU   B 1 164 ? 38.919 -35.642 -7.933  1.00 12.92 ?  164 LEU   B CB   1 
ATOM   6454 C CG   . LEU   B 1 164 ? 39.446 -35.362 -6.531  1.00 13.52 ?  164 LEU   B CG   1 
ATOM   6455 C CD1  . LEU   B 1 164 ? 40.537 -34.303 -6.592  1.00 13.93 ?  164 LEU   B CD1  1 
ATOM   6456 C CD2  . LEU   B 1 164 ? 38.330 -34.932 -5.604  1.00 15.39 ?  164 LEU   B CD2  1 
ATOM   6457 H H    A LEU   B 1 164 ? 39.870 -37.852 -8.031  0.74 16.14 ?  164 LEU   B H    1 
ATOM   6458 H H    B LEU   B 1 164 ? 39.870 -37.855 -8.082  0.26 16.14 ?  164 LEU   B H    1 
ATOM   6459 H HA   . LEU   B 1 164 ? 37.490 -36.999 -7.356  1.00 15.59 ?  164 LEU   B HA   1 
ATOM   6460 H HB2  . LEU   B 1 164 ? 39.687 -35.683 -8.530  1.00 15.50 ?  164 LEU   B HB2  1 
ATOM   6461 H HB3  . LEU   B 1 164 ? 38.355 -34.899 -8.187  1.00 15.50 ?  164 LEU   B HB3  1 
ATOM   6462 H HG   . LEU   B 1 164 ? 39.843 -36.169 -6.175  1.00 16.22 ?  164 LEU   B HG   1 
ATOM   6463 H HD11 . LEU   B 1 164 ? 40.860 -34.123 -5.694  1.00 16.71 ?  164 LEU   B HD11 1 
ATOM   6464 H HD12 . LEU   B 1 164 ? 41.272 -34.631 -7.142  1.00 16.71 ?  164 LEU   B HD12 1 
ATOM   6465 H HD13 . LEU   B 1 164 ? 40.177 -33.491 -6.982  1.00 16.71 ?  164 LEU   B HD13 1 
ATOM   6466 H HD21 . LEU   B 1 164 ? 38.707 -34.696 -4.742  1.00 18.47 ?  164 LEU   B HD21 1 
ATOM   6467 H HD22 . LEU   B 1 164 ? 37.877 -34.164 -5.988  1.00 18.47 ?  164 LEU   B HD22 1 
ATOM   6468 H HD23 . LEU   B 1 164 ? 37.706 -35.667 -5.503  1.00 18.47 ?  164 LEU   B HD23 1 
ATOM   6469 N N    . VAL   B 1 165 ? 38.029 -37.098 -10.515 1.00 14.75 ?  165 VAL   B N    1 
ATOM   6470 C CA   . VAL   B 1 165 ? 37.374 -37.039 -11.818 1.00 16.09 ?  165 VAL   B CA   1 
ATOM   6471 C C    . VAL   B 1 165 ? 36.454 -38.237 -12.000 1.00 17.48 ?  165 VAL   B C    1 
ATOM   6472 O O    . VAL   B 1 165 ? 35.297 -38.100 -12.415 1.00 18.34 ?  165 VAL   B O    1 
ATOM   6473 C CB   . VAL   B 1 165 ? 38.421 -36.949 -12.944 1.00 16.75 ?  165 VAL   B CB   1 
ATOM   6474 C CG1  . VAL   B 1 165 ? 37.761 -37.048 -14.304 1.00 17.80 ?  165 VAL   B CG1  1 
ATOM   6475 C CG2  . VAL   B 1 165 ? 39.219 -35.659 -12.829 1.00 16.54 ?  165 VAL   B CG2  1 
ATOM   6476 H H    . VAL   B 1 165 ? 38.877 -37.243 -10.554 1.00 17.70 ?  165 VAL   B H    1 
ATOM   6477 H HA   . VAL   B 1 165 ? 36.828 -36.243 -11.864 1.00 19.31 ?  165 VAL   B HA   1 
ATOM   6478 H HB   . VAL   B 1 165 ? 39.044 -37.687 -12.860 1.00 20.10 ?  165 VAL   B HB   1 
ATOM   6479 H HG11 . VAL   B 1 165 ? 38.388 -36.761 -14.983 1.00 21.36 ?  165 VAL   B HG11 1 
ATOM   6480 H HG12 . VAL   B 1 165 ? 37.511 -37.976 -14.464 1.00 21.36 ?  165 VAL   B HG12 1 
ATOM   6481 H HG13 . VAL   B 1 165 ? 36.973 -36.488 -14.316 1.00 21.36 ?  165 VAL   B HG13 1 
ATOM   6482 H HG21 . VAL   B 1 165 ? 39.853 -35.609 -13.564 1.00 19.84 ?  165 VAL   B HG21 1 
ATOM   6483 H HG22 . VAL   B 1 165 ? 38.610 -34.903 -12.870 1.00 19.84 ?  165 VAL   B HG22 1 
ATOM   6484 H HG23 . VAL   B 1 165 ? 39.695 -35.653 -11.984 1.00 19.84 ?  165 VAL   B HG23 1 
ATOM   6485 N N    . SER   B 1 166 ? 36.960 -39.434 -11.689 1.00 18.39 ?  166 SER   B N    1 
ATOM   6486 C CA   . SER   B 1 166 ? 36.200 -40.645 -11.965 1.00 19.77 ?  166 SER   B CA   1 
ATOM   6487 C C    . SER   B 1 166 ? 34.943 -40.726 -11.114 1.00 19.97 ?  166 SER   B C    1 
ATOM   6488 O O    . SER   B 1 166 ? 33.972 -41.356 -11.531 1.00 21.95 ?  166 SER   B O    1 
ATOM   6489 C CB   . SER   B 1 166 ? 37.064 -41.899 -11.788 1.00 20.99 ?  166 SER   B CB   1 
ATOM   6490 O OG   . SER   B 1 166 ? 37.424 -42.103 -10.435 1.00 21.13 ?  166 SER   B OG   1 
ATOM   6491 H H    . SER   B 1 166 ? 37.735 -39.570 -11.330 1.00 22.06 ?  166 SER   B H    1 
ATOM   6492 H HA   . SER   B 1 166 ? 35.921 -40.625 -12.892 1.00 23.72 ?  166 SER   B HA   1 
ATOM   6493 H HB2  . SER   B 1 166 ? 36.564 -42.671 -12.098 1.00 25.19 ?  166 SER   B HB2  1 
ATOM   6494 H HB3  . SER   B 1 166 ? 37.872 -41.801 -12.319 1.00 25.19 ?  166 SER   B HB3  1 
ATOM   6495 H HG   . SER   B 1 166 ? 37.873 -41.452 -10.156 1.00 25.36 ?  166 SER   B HG   1 
ATOM   6496 N N    . SER   B 1 167 ? 34.927 -40.104 -9.937  1.00 18.56 ?  167 SER   B N    1 
ATOM   6497 C CA   . SER   B 1 167 ? 33.771 -40.161 -9.052  1.00 17.95 ?  167 SER   B CA   1 
ATOM   6498 C C    . SER   B 1 167 ? 32.856 -38.942 -9.155  1.00 17.65 ?  167 SER   B C    1 
ATOM   6499 O O    . SER   B 1 167 ? 31.781 -38.939 -8.542  1.00 18.01 ?  167 SER   B O    1 
ATOM   6500 C CB   . SER   B 1 167 ? 34.214 -40.339 -7.596  1.00 17.99 ?  167 SER   B CB   1 
ATOM   6501 O OG   . SER   B 1 167 ? 34.893 -39.183 -7.130  1.00 17.54 ?  167 SER   B OG   1 
ATOM   6502 H H    . SER   B 1 167 ? 35.578 -39.639 -9.630  1.00 22.27 ?  167 SER   B H    1 
ATOM   6503 H HA   . SER   B 1 167 ? 33.239 -40.939 -9.293  1.00 21.54 ?  167 SER   B HA   1 
ATOM   6504 H HB2  . SER   B 1 167 ? 33.427 -40.493 -7.045  1.00 21.59 ?  167 SER   B HB2  1 
ATOM   6505 H HB3  . SER   B 1 167 ? 34.804 -41.111 -7.541  1.00 21.59 ?  167 SER   B HB3  1 
ATOM   6506 H HG   . SER   B 1 167 ? 35.578 -39.057 -7.599  1.00 21.05 ?  167 SER   B HG   1 
ATOM   6507 N N    . PHE   B 1 168 ? 33.231 -37.915 -9.919  1.00 17.29 ?  168 PHE   B N    1 
ATOM   6508 C CA   . PHE   B 1 168 ? 32.400 -36.713 -9.982  1.00 16.93 ?  168 PHE   B CA   1 
ATOM   6509 C C    . PHE   B 1 168 ? 31.085 -36.974 -10.711 1.00 15.23 ?  168 PHE   B C    1 
ATOM   6510 O O    . PHE   B 1 168 ? 30.046 -36.380 -10.368 1.00 15.78 ?  168 PHE   B O    1 
ATOM   6511 C CB   . PHE   B 1 168 ? 33.167 -35.579 -10.657 1.00 17.51 ?  168 PHE   B CB   1 
ATOM   6512 C CG   . PHE   B 1 168 ? 32.366 -34.326 -10.784 1.00 17.60 ?  168 PHE   B CG   1 
ATOM   6513 C CD1  . PHE   B 1 168 ? 32.045 -33.584 -9.656  1.00 18.70 ?  168 PHE   B CD1  1 
ATOM   6514 C CD2  . PHE   B 1 168 ? 31.914 -33.892 -12.015 1.00 16.90 ?  168 PHE   B CD2  1 
ATOM   6515 C CE1  . PHE   B 1 168 ? 31.288 -32.430 -9.751  1.00 19.12 ?  168 PHE   B CE1  1 
ATOM   6516 C CE2  . PHE   B 1 168 ? 31.167 -32.723 -12.122 1.00 17.79 ?  168 PHE   B CE2  1 
ATOM   6517 C CZ   . PHE   B 1 168 ? 30.849 -31.994 -10.986 1.00 18.27 ?  168 PHE   B CZ   1 
ATOM   6518 H H    . PHE   B 1 168 ? 33.949 -37.886 -10.392 1.00 20.75 ?  168 PHE   B H    1 
ATOM   6519 H HA   . PHE   B 1 168 ? 32.183 -36.433 -9.084  1.00 20.31 ?  168 PHE   B HA   1 
ATOM   6520 H HB2  . PHE   B 1 168 ? 33.954 -35.375 -10.128 1.00 21.02 ?  168 PHE   B HB2  1 
ATOM   6521 H HB3  . PHE   B 1 168 ? 33.428 -35.855 -11.547 1.00 21.02 ?  168 PHE   B HB3  1 
ATOM   6522 H HD1  . PHE   B 1 168 ? 32.332 -33.877 -8.821  1.00 22.44 ?  168 PHE   B HD1  1 
ATOM   6523 H HD2  . PHE   B 1 168 ? 32.126 -34.372 -12.780 1.00 20.28 ?  168 PHE   B HD2  1 
ATOM   6524 H HE1  . PHE   B 1 168 ? 31.078 -31.946 -8.985  1.00 22.94 ?  168 PHE   B HE1  1 
ATOM   6525 H HE2  . PHE   B 1 168 ? 30.868 -32.435 -12.956 1.00 21.34 ?  168 PHE   B HE2  1 
ATOM   6526 H HZ   . PHE   B 1 168 ? 30.342 -31.218 -11.055 1.00 21.93 ?  168 PHE   B HZ   1 
ATOM   6527 N N    . LEU   B 1 169 ? 31.113 -37.855 -11.709 1.00 15.89 ?  169 LEU   B N    1 
ATOM   6528 C CA   . LEU   B 1 169 ? 29.937 -38.162 -12.514 1.00 18.45 ?  169 LEU   B CA   1 
ATOM   6529 C C    . LEU   B 1 169 ? 29.934 -39.602 -13.012 1.00 20.97 ?  169 LEU   B C    1 
ATOM   6530 O O    . LEU   B 1 169 ? 29.041 -40.016 -13.752 1.00 23.27 ?  169 LEU   B O    1 
ATOM   6531 C CB   . LEU   B 1 169 ? 29.864 -37.217 -13.714 1.00 20.21 ?  169 LEU   B CB   1 
ATOM   6532 C CG   . LEU   B 1 169 ? 28.603 -36.359 -13.796 1.00 23.20 ?  169 LEU   B CG   1 
ATOM   6533 C CD1  . LEU   B 1 169 ? 28.567 -35.608 -15.113 1.00 24.35 ?  169 LEU   B CD1  1 
ATOM   6534 C CD2  . LEU   B 1 169 ? 27.356 -37.207 -13.626 1.00 23.45 ?  169 LEU   B CD2  1 
ATOM   6535 O OXT  . LEU   B 1 169 ? 30.833 -40.373 -12.695 1.00 21.73 -1 169 LEU   B OXT  1 
ATOM   6536 H H    . LEU   B 1 169 ? 31.820 -38.291 -11.951 1.00 19.07 ?  169 LEU   B H    1 
ATOM   6537 H HA   . LEU   B 1 169 ? 29.153 -38.028 -11.968 1.00 22.14 ?  169 LEU   B HA   1 
ATOM   6538 H HB2  . LEU   B 1 169 ? 30.624 -36.613 -13.681 1.00 24.25 ?  169 LEU   B HB2  1 
ATOM   6539 H HB3  . LEU   B 1 169 ? 29.907 -37.743 -14.528 1.00 24.25 ?  169 LEU   B HB3  1 
ATOM   6540 H HG   . LEU   B 1 169 ? 28.621 -35.702 -13.082 1.00 27.85 ?  169 LEU   B HG   1 
ATOM   6541 H HD11 . LEU   B 1 169 ? 27.772 -35.054 -15.137 1.00 29.22 ?  169 LEU   B HD11 1 
ATOM   6542 H HD12 . LEU   B 1 169 ? 29.360 -35.056 -15.183 1.00 29.22 ?  169 LEU   B HD12 1 
ATOM   6543 H HD13 . LEU   B 1 169 ? 28.546 -36.252 -15.839 1.00 29.22 ?  169 LEU   B HD13 1 
ATOM   6544 H HD21 . LEU   B 1 169 ? 26.607 -36.758 -14.041 1.00 28.14 ?  169 LEU   B HD21 1 
ATOM   6545 H HD22 . LEU   B 1 169 ? 27.503 -38.069 -14.048 1.00 28.14 ?  169 LEU   B HD22 1 
ATOM   6546 H HD23 . LEU   B 1 169 ? 27.189 -37.330 -12.679 1.00 28.14 ?  169 LEU   B HD23 1 
HETATM 6547 N N2   B A1A42 C 2 .   ? 15.234 5.618   6.355   0.26 10.43 ?  201 A1A42 A N2   1 
HETATM 6548 C C3   B A1A42 C 2 .   ? 14.275 0.059   -0.695  0.26 11.55 ?  201 A1A42 A C3   1 
HETATM 6549 C C6   B A1A42 C 2 .   ? 11.991 -0.573  2.319   0.26 10.67 ?  201 A1A42 A C6   1 
HETATM 6550 C C9   B A1A42 C 2 .   ? 15.523 3.329   2.810   0.26 9.48  ?  201 A1A42 A C9   1 
HETATM 6551 C C12  B A1A42 C 2 .   ? 15.344 4.849   5.182   0.26 9.42  ?  201 A1A42 A C12  1 
HETATM 6552 C C14  B A1A42 C 2 .   ? 14.655 7.551   4.954   0.26 11.51 ?  201 A1A42 A C14  1 
HETATM 6553 C C1   B A1A42 C 2 .   ? 16.545 -0.553  0.342   0.26 12.54 ?  201 A1A42 A C1   1 
HETATM 6554 C C10  B A1A42 C 2 .   ? 15.549 2.711   4.082   0.26 9.27  ?  201 A1A42 A C10  1 
HETATM 6555 C C11  B A1A42 C 2 .   ? 15.439 3.452   5.267   0.26 9.63  ?  201 A1A42 A C11  1 
HETATM 6556 C C13  B A1A42 C 2 .   ? 14.924 6.918   6.331   0.26 11.58 ?  201 A1A42 A C13  1 
HETATM 6557 C C15  B A1A42 C 2 .   ? 15.344 5.490   3.925   0.26 9.80  ?  201 A1A42 A C15  1 
HETATM 6558 C C16  B A1A42 C 2 .   ? 15.453 4.735   2.743   0.26 9.36  ?  201 A1A42 A C16  1 
HETATM 6559 C C2   B A1A42 C 2 .   ? 15.510 0.559   0.073   0.26 11.59 ?  201 A1A42 A C2   1 
HETATM 6560 C C4   B A1A42 C 2 .   ? 13.313 -0.716  0.203   0.26 11.08 ?  201 A1A42 A C4   1 
HETATM 6561 C C5   B A1A42 C 2 .   ? 12.970 0.163   1.410   0.26 10.66 ?  201 A1A42 A C5   1 
HETATM 6562 C C7   B A1A42 C 2 .   ? 14.253 0.502   2.195   0.26 10.63 ?  201 A1A42 A C7   1 
HETATM 6563 C C8   B A1A42 C 2 .   ? 15.705 2.512   1.557   0.26 9.45  ?  201 A1A42 A C8   1 
HETATM 6564 N N1   B A1A42 C 2 .   ? 15.176 1.271   1.334   0.26 10.24 ?  201 A1A42 A N1   1 
HETATM 6565 O O1   B A1A42 C 2 .   ? 12.490 -1.430  3.071   0.26 10.15 ?  201 A1A42 A O1   1 
HETATM 6566 O O2   B A1A42 C 2 .   ? 16.451 3.030   0.727   0.26 9.40  ?  201 A1A42 A O2   1 
HETATM 6567 O O3   B A1A42 C 2 .   ? 14.843 7.587   7.359   0.26 12.71 ?  201 A1A42 A O3   1 
HETATM 6568 O O4   B A1A42 C 2 .   ? 15.252 6.861   3.847   0.26 10.53 ?  201 A1A42 A O4   1 
HETATM 6569 O O5   B A1A42 C 2 .   ? 10.784 -0.267  2.245   0.26 10.61 ?  201 A1A42 A O5   1 
HETATM 6570 H H14  B A1A42 C 2 .   ? 15.412 5.166   7.238   0.26 12.51 ?  201 A1A42 A H14  1 
HETATM 6571 H H7   B A1A42 C 2 .   ? 14.572 -0.558  -1.539  0.26 13.86 ?  201 A1A42 A H7   1 
HETATM 6572 H H6   B A1A42 C 2 .   ? 13.745 0.917   -1.112  0.26 13.86 ?  201 A1A42 A H6   1 
HETATM 6573 H H16  B A1A42 C 2 .   ? 13.578 7.605   4.786   0.26 13.81 ?  201 A1A42 A H16  1 
HETATM 6574 H H15  B A1A42 C 2 .   ? 15.012 8.583   4.967   0.26 13.81 ?  201 A1A42 A H15  1 
HETATM 6575 H H4   B A1A42 C 2 .   ? 16.913 -0.970  -0.594  0.26 15.04 ?  201 A1A42 A H4   1 
HETATM 6576 H H5   B A1A42 C 2 .   ? 16.129 -1.368  0.927   0.26 15.04 ?  201 A1A42 A H5   1 
HETATM 6577 H H3   B A1A42 C 2 .   ? 17.404 -0.161  0.889   0.26 15.04 ?  201 A1A42 A H3   1 
HETATM 6578 H H12  B A1A42 C 2 .   ? 15.636 1.640   4.153   0.26 11.13 ?  201 A1A42 A H12  1 
HETATM 6579 H H13  B A1A42 C 2 .   ? 15.434 2.955   6.225   0.26 11.56 ?  201 A1A42 A H13  1 
HETATM 6580 H H17  B A1A42 C 2 .   ? 15.474 5.238   1.786   0.26 11.23 ?  201 A1A42 A H17  1 
HETATM 6581 H H1   B A1A42 C 2 .   ? 15.996 1.238   -0.627  0.26 13.90 ?  201 A1A42 A H1   1 
HETATM 6582 H H8   B A1A42 C 2 .   ? 13.761 -1.657  0.523   0.26 13.30 ?  201 A1A42 A H8   1 
HETATM 6583 H H9   B A1A42 C 2 .   ? 12.412 -0.980  -0.357  0.26 13.30 ?  201 A1A42 A H9   1 
HETATM 6584 H H2   B A1A42 C 2 .   ? 12.503 1.091   1.065   0.26 12.79 ?  201 A1A42 A H2   1 
HETATM 6585 H H11  B A1A42 C 2 .   ? 13.981 1.078   3.069   0.26 12.75 ?  201 A1A42 A H11  1 
HETATM 6586 H H10  B A1A42 C 2 .   ? 14.692 -0.405  2.609   0.26 12.75 ?  201 A1A42 A H10  1 
HETATM 6587 O O    . HOH   D 3 .   ? 34.379 -1.920  12.492  1.00 39.43 ?  301 HOH   A O    1 
HETATM 6588 O O    . HOH   D 3 .   ? 15.171 -21.581 14.190  1.00 17.43 ?  302 HOH   A O    1 
HETATM 6589 O O    . HOH   D 3 .   ? 4.569  3.911   0.693   1.00 24.27 ?  303 HOH   A O    1 
HETATM 6590 O O    . HOH   D 3 .   ? 26.945 11.467  1.621   1.00 17.47 ?  304 HOH   A O    1 
HETATM 6591 O O    . HOH   D 3 .   ? 14.857 -4.652  20.601  1.00 42.59 ?  305 HOH   A O    1 
HETATM 6592 O O    . HOH   D 3 .   ? 7.990  -12.547 -0.863  1.00 20.05 ?  306 HOH   A O    1 
HETATM 6593 O O    . HOH   D 3 .   ? 9.224  -10.172 19.396  1.00 45.51 ?  307 HOH   A O    1 
HETATM 6594 O O    . HOH   D 3 .   ? 20.158 4.588   -7.685  1.00 19.65 ?  308 HOH   A O    1 
HETATM 6595 O O    . HOH   D 3 .   ? 7.615  -6.234  -6.563  1.00 40.43 ?  309 HOH   A O    1 
HETATM 6596 O O    . HOH   D 3 .   ? 17.068 -18.048 15.047  1.00 26.06 ?  310 HOH   A O    1 
HETATM 6597 O O    . HOH   D 3 .   ? 22.775 12.532  1.610   1.00 14.95 ?  311 HOH   A O    1 
HETATM 6598 O O    . HOH   D 3 .   ? 14.205 -4.501  -11.888 1.00 29.90 ?  312 HOH   A O    1 
HETATM 6599 O O    . HOH   D 3 .   ? 15.219 -12.253 18.742  1.00 34.65 ?  313 HOH   A O    1 
HETATM 6600 O O    . HOH   D 3 .   ? 29.046 0.501   -9.696  1.00 20.91 ?  314 HOH   A O    1 
HETATM 6601 O O    A HOH   D 3 .   ? 3.609  -9.414  9.720   0.74 30.63 ?  315 HOH   A O    1 
HETATM 6602 O O    . HOH   D 3 .   ? 42.493 10.529  5.158   1.00 19.57 ?  316 HOH   A O    1 
HETATM 6603 O O    . HOH   D 3 .   ? 10.386 -22.085 -1.345  1.00 43.77 ?  317 HOH   A O    1 
HETATM 6604 O O    . HOH   D 3 .   ? 11.646 -10.698 -10.095 1.00 42.38 ?  318 HOH   A O    1 
HETATM 6605 O O    . HOH   D 3 .   ? 15.267 4.048   17.758  1.00 42.77 ?  319 HOH   A O    1 
HETATM 6606 O O    . HOH   D 3 .   ? 14.788 -14.009 16.721  1.00 25.65 ?  320 HOH   A O    1 
HETATM 6607 O O    . HOH   D 3 .   ? 28.406 -0.056  -13.368 1.00 32.73 ?  321 HOH   A O    1 
HETATM 6608 O O    . HOH   D 3 .   ? 28.227 -6.378  19.636  1.00 43.07 ?  322 HOH   A O    1 
HETATM 6609 O O    . HOH   D 3 .   ? 18.846 -21.953 6.839   1.00 32.18 ?  323 HOH   A O    1 
HETATM 6610 O O    . HOH   D 3 .   ? 13.389 -1.310  -6.730  1.00 19.31 ?  324 HOH   A O    1 
HETATM 6611 O O    . HOH   D 3 .   ? 36.162 -5.064  -0.572  1.00 30.21 ?  325 HOH   A O    1 
HETATM 6612 O O    . HOH   D 3 .   ? 0.705  -4.555  0.427   1.00 29.09 ?  326 HOH   A O    1 
HETATM 6613 O O    B HOH   D 3 .   ? 14.835 -2.574  3.496   0.26 12.38 ?  327 HOH   A O    1 
HETATM 6614 O O    . HOH   D 3 .   ? 12.143 0.328   14.949  1.00 31.97 ?  328 HOH   A O    1 
HETATM 6615 O O    . HOH   D 3 .   ? 18.687 -2.314  -16.404 1.00 46.04 ?  329 HOH   A O    1 
HETATM 6616 O O    . HOH   D 3 .   ? 19.874 -12.405 -9.033  1.00 23.42 ?  330 HOH   A O    1 
HETATM 6617 O O    . HOH   D 3 .   ? 30.277 -13.308 -8.599  1.00 20.29 ?  331 HOH   A O    1 
HETATM 6618 O O    . HOH   D 3 .   ? 26.458 -19.321 -1.838  1.00 13.68 ?  332 HOH   A O    1 
HETATM 6619 O O    . HOH   D 3 .   ? 22.473 5.316   19.101  1.00 43.68 ?  333 HOH   A O    1 
HETATM 6620 O O    . HOH   D 3 .   ? 30.976 -18.156 7.758   1.00 20.11 ?  334 HOH   A O    1 
HETATM 6621 O O    . HOH   D 3 .   ? 38.304 10.142  7.177   1.00 44.98 ?  335 HOH   A O    1 
HETATM 6622 O O    . HOH   D 3 .   ? 34.043 -1.016  -8.943  1.00 28.47 ?  336 HOH   A O    1 
HETATM 6623 O O    . HOH   D 3 .   ? 27.404 -5.854  -14.009 1.00 36.30 ?  337 HOH   A O    1 
HETATM 6624 O O    B HOH   D 3 .   ? 9.374  2.468   8.824   0.26 18.11 ?  338 HOH   A O    1 
HETATM 6625 O O    . HOH   D 3 .   ? -0.429 -3.102  3.179   1.00 39.60 ?  339 HOH   A O    1 
HETATM 6626 O O    . HOH   D 3 .   ? 37.601 2.788   10.192  1.00 30.47 ?  340 HOH   A O    1 
HETATM 6627 O O    A HOH   D 3 .   ? 9.778  -21.298 5.710   0.74 15.88 ?  341 HOH   A O    1 
HETATM 6628 O O    B HOH   D 3 .   ? 7.673  3.958   2.990   0.26 15.82 ?  342 HOH   A O    1 
HETATM 6629 O O    B HOH   D 3 .   ? 21.667 -2.346  -2.566  0.26 12.17 ?  343 HOH   A O    1 
HETATM 6630 O O    . HOH   D 3 .   ? 13.531 -15.093 -7.546  1.00 26.32 ?  344 HOH   A O    1 
HETATM 6631 O O    . HOH   D 3 .   ? 5.191  2.657   5.534   1.00 33.57 ?  345 HOH   A O    1 
HETATM 6632 O O    . HOH   D 3 .   ? -0.599 -8.541  2.202   1.00 43.90 ?  346 HOH   A O    1 
HETATM 6633 O O    . HOH   D 3 .   ? 23.511 11.416  4.079   1.00 12.29 ?  347 HOH   A O    1 
HETATM 6634 O O    A HOH   D 3 .   ? 8.180  -21.349 3.968   0.74 40.83 ?  348 HOH   A O    1 
HETATM 6635 O O    . HOH   D 3 .   ? 18.652 -19.436 13.522  1.00 35.62 ?  349 HOH   A O    1 
HETATM 6636 O O    . HOH   D 3 .   ? 27.323 13.804  2.847   1.00 31.38 ?  350 HOH   A O    1 
HETATM 6637 O O    . HOH   D 3 .   ? 17.134 -17.790 -5.088  1.00 25.53 ?  351 HOH   A O    1 
HETATM 6638 O O    . HOH   D 3 .   ? 38.606 4.959   6.957   1.00 15.30 ?  352 HOH   A O    1 
HETATM 6639 O O    B HOH   D 3 .   ? 3.180  1.659   3.121   0.26 14.86 ?  353 HOH   A O    1 
HETATM 6640 O O    . HOH   D 3 .   ? 14.536 -0.446  -12.133 1.00 25.28 ?  354 HOH   A O    1 
HETATM 6641 O O    . HOH   D 3 .   ? 39.816 -1.012  -5.178  1.00 20.94 ?  355 HOH   A O    1 
HETATM 6642 O O    . HOH   D 3 .   ? 20.597 -19.641 -5.121  1.00 28.91 ?  356 HOH   A O    1 
HETATM 6643 O O    . HOH   D 3 .   ? 31.733 8.189   14.854  1.00 25.70 ?  357 HOH   A O    1 
HETATM 6644 O O    A HOH   D 3 .   ? 14.657 -3.616  3.098   0.74 19.74 ?  358 HOH   A O    1 
HETATM 6645 O O    . HOH   D 3 .   ? 15.758 -0.910  5.169   1.00 35.48 ?  359 HOH   A O    1 
HETATM 6646 O O    . HOH   D 3 .   ? 24.087 -2.040  -2.093  1.00 10.38 ?  360 HOH   A O    1 
HETATM 6647 O O    . HOH   D 3 .   ? 44.377 7.103   6.515   1.00 26.09 ?  361 HOH   A O    1 
HETATM 6648 O O    . HOH   D 3 .   ? 37.250 -2.808  9.692   1.00 39.91 ?  362 HOH   A O    1 
HETATM 6649 O O    A HOH   D 3 .   ? 14.303 0.607   6.805   0.74 18.85 ?  363 HOH   A O    1 
HETATM 6650 O O    . HOH   D 3 .   ? 22.161 -19.270 11.355  1.00 34.37 ?  364 HOH   A O    1 
HETATM 6651 O O    . HOH   D 3 .   ? 35.759 -12.670 6.826   1.00 15.44 ?  365 HOH   A O    1 
HETATM 6652 O O    A HOH   D 3 .   ? 17.522 -1.678  0.446   0.74 17.85 ?  366 HOH   A O    1 
HETATM 6653 O O    . HOH   D 3 .   ? 31.068 -13.935 -2.503  1.00 13.01 ?  367 HOH   A O    1 
HETATM 6654 O O    . HOH   D 3 .   ? 15.523 12.002  7.975   1.00 37.79 ?  368 HOH   A O    1 
HETATM 6655 O O    . HOH   D 3 .   ? 42.647 4.276   5.375   1.00 30.67 ?  369 HOH   A O    1 
HETATM 6656 O O    . HOH   D 3 .   ? 14.038 -4.974  17.600  1.00 25.28 ?  370 HOH   A O    1 
HETATM 6657 O O    A HOH   D 3 .   ? 18.589 9.478   8.918   0.74 18.58 ?  371 HOH   A O    1 
HETATM 6658 O O    . HOH   D 3 .   ? 37.429 11.940  4.985   1.00 28.97 ?  372 HOH   A O    1 
HETATM 6659 O O    . HOH   D 3 .   ? 31.915 -9.298  -6.688  1.00 21.10 ?  373 HOH   A O    1 
HETATM 6660 O O    . HOH   D 3 .   ? 30.845 3.093   8.286   1.00 11.90 ?  374 HOH   A O    1 
HETATM 6661 O O    . HOH   D 3 .   ? 16.952 -19.218 4.898   1.00 14.39 ?  375 HOH   A O    1 
HETATM 6662 O O    . HOH   D 3 .   ? 21.828 -21.898 8.387   1.00 28.12 ?  376 HOH   A O    1 
HETATM 6663 O O    B HOH   D 3 .   ? 18.806 -1.225  -1.834  0.26 10.82 ?  377 HOH   A O    1 
HETATM 6664 O O    . HOH   D 3 .   ? 33.662 -7.158  4.306   1.00 16.36 ?  378 HOH   A O    1 
HETATM 6665 O O    . HOH   D 3 .   ? 27.483 -10.647 14.024  1.00 16.67 ?  379 HOH   A O    1 
HETATM 6666 O O    . HOH   D 3 .   ? 6.454  -5.471  11.326  1.00 20.35 ?  380 HOH   A O    1 
HETATM 6667 O O    . HOH   D 3 .   ? 14.301 -21.126 -4.245  1.00 29.49 ?  381 HOH   A O    1 
HETATM 6668 O O    . HOH   D 3 .   ? 43.414 7.824   2.702   1.00 28.49 ?  382 HOH   A O    1 
HETATM 6669 O O    . HOH   D 3 .   ? 43.988 8.449   -3.120  1.00 26.84 ?  383 HOH   A O    1 
HETATM 6670 O O    A HOH   D 3 .   ? 21.272 -2.364  -2.047  0.74 14.61 ?  384 HOH   A O    1 
HETATM 6671 O O    A HOH   D 3 .   ? 6.960  -8.121  11.840  0.74 20.06 ?  385 HOH   A O    1 
HETATM 6672 O O    . HOH   D 3 .   ? 31.762 -7.276  -9.885  1.00 21.11 ?  386 HOH   A O    1 
HETATM 6673 O O    B HOH   D 3 .   ? 15.906 7.812   10.235  0.26 19.79 ?  387 HOH   A O    1 
HETATM 6674 O O    A HOH   D 3 .   ? 24.462 3.630   -1.842  0.74 13.07 ?  388 HOH   A O    1 
HETATM 6675 O O    B HOH   D 3 .   ? 9.926  1.091   -0.043  0.26 12.53 ?  389 HOH   A O    1 
HETATM 6676 O O    . HOH   D 3 .   ? 33.495 -16.983 8.047   1.00 18.26 ?  390 HOH   A O    1 
HETATM 6677 O O    . HOH   D 3 .   ? 8.954  -12.004 17.233  1.00 43.45 ?  391 HOH   A O    1 
HETATM 6678 O O    . HOH   D 3 .   ? 16.461 -22.005 0.917   1.00 29.21 ?  392 HOH   A O    1 
HETATM 6679 O O    . HOH   D 3 .   ? 24.609 2.011   -7.009  1.00 17.60 ?  393 HOH   A O    1 
HETATM 6680 O O    . HOH   D 3 .   ? 24.259 -7.775  14.437  1.00 16.63 ?  394 HOH   A O    1 
HETATM 6681 O O    . HOH   D 3 .   ? 24.696 -17.543 12.691  1.00 23.02 ?  395 HOH   A O    1 
HETATM 6682 O O    B HOH   D 3 .   ? 12.246 -1.481  -3.467  0.26 13.98 ?  396 HOH   A O    1 
HETATM 6683 O O    . HOH   D 3 .   ? 25.750 -0.725  -7.324  1.00 14.73 ?  397 HOH   A O    1 
HETATM 6684 O O    . HOH   D 3 .   ? 22.663 -11.944 21.752  1.00 43.03 ?  398 HOH   A O    1 
HETATM 6685 O O    . HOH   D 3 .   ? 15.127 -7.982  -9.597  1.00 21.19 ?  399 HOH   A O    1 
HETATM 6686 O O    B HOH   D 3 .   ? 14.300 -0.068  6.791   0.26 12.53 ?  400 HOH   A O    1 
HETATM 6687 O O    B HOH   D 3 .   ? 16.975 2.730   -2.053  0.26 12.50 ?  401 HOH   A O    1 
HETATM 6688 O O    . HOH   D 3 .   ? 27.349 2.320   18.696  1.00 30.36 ?  402 HOH   A O    1 
HETATM 6689 O O    . HOH   D 3 .   ? 21.206 10.360  15.029  1.00 33.79 ?  403 HOH   A O    1 
HETATM 6690 O O    . HOH   D 3 .   ? 37.596 -2.021  5.783   1.00 26.79 ?  404 HOH   A O    1 
HETATM 6691 O O    . HOH   D 3 .   ? 32.782 -9.251  5.933   1.00 20.31 ?  405 HOH   A O    1 
HETATM 6692 O O    . HOH   D 3 .   ? 30.700 1.874   16.689  1.00 21.19 ?  406 HOH   A O    1 
HETATM 6693 O O    . HOH   D 3 .   ? 28.596 -10.559 -14.044 1.00 43.15 ?  407 HOH   A O    1 
HETATM 6694 O O    . HOH   D 3 .   ? 14.466 -24.709 11.543  1.00 36.10 ?  408 HOH   A O    1 
HETATM 6695 O O    . HOH   D 3 .   ? 20.542 -20.002 2.737   1.00 16.80 ?  409 HOH   A O    1 
HETATM 6696 O O    B HOH   D 3 .   ? 23.684 3.707   -1.918  0.26 16.25 ?  410 HOH   A O    1 
HETATM 6697 O O    . HOH   D 3 .   ? 11.092 1.709   12.786  1.00 24.79 ?  411 HOH   A O    1 
HETATM 6698 O O    . HOH   D 3 .   ? 31.055 6.206   -12.308 1.00 29.72 ?  412 HOH   A O    1 
HETATM 6699 O O    A HOH   D 3 .   ? 18.988 -0.633  -1.620  0.74 10.80 ?  413 HOH   A O    1 
HETATM 6700 O O    . HOH   D 3 .   ? 6.716  -3.416  13.139  1.00 32.14 ?  414 HOH   A O    1 
HETATM 6701 O O    . HOH   D 3 .   ? 26.970 4.218   -0.687  1.00 12.50 ?  415 HOH   A O    1 
HETATM 6702 O O    . HOH   D 3 .   ? 15.895 2.224   24.740  1.00 47.75 ?  416 HOH   A O    1 
HETATM 6703 O O    . HOH   D 3 .   ? 21.794 -13.720 -8.166  1.00 39.30 ?  417 HOH   A O    1 
HETATM 6704 O O    . HOH   D 3 .   ? 23.998 -15.666 -9.228  1.00 33.43 ?  418 HOH   A O    1 
HETATM 6705 O O    . HOH   D 3 .   ? 41.664 1.554   4.944   1.00 36.92 ?  419 HOH   A O    1 
HETATM 6706 O O    A HOH   D 3 .   ? 21.383 3.186   -0.338  0.74 11.43 ?  420 HOH   A O    1 
HETATM 6707 O O    . HOH   D 3 .   ? 23.911 -20.264 -1.386  1.00 15.88 ?  421 HOH   A O    1 
HETATM 6708 O O    A HOH   D 3 .   ? 14.039 -23.031 7.331   0.74 14.96 ?  422 HOH   A O    1 
HETATM 6709 O O    . HOH   D 3 .   ? 30.063 -10.133 13.027  1.00 20.53 ?  423 HOH   A O    1 
HETATM 6710 O O    . HOH   D 3 .   ? 38.187 -1.351  -1.938  1.00 19.04 ?  424 HOH   A O    1 
HETATM 6711 O O    . HOH   D 3 .   ? 40.939 -8.324  -6.687  1.00 36.45 ?  425 HOH   A O    1 
HETATM 6712 O O    B HOH   D 3 .   ? 21.214 3.044   -0.359  0.26 16.53 ?  426 HOH   A O    1 
HETATM 6713 O O    . HOH   D 3 .   ? 10.413 -13.628 -1.700  1.00 17.44 ?  427 HOH   A O    1 
HETATM 6714 O O    . HOH   D 3 .   ? 27.998 0.851   -7.160  1.00 13.58 ?  428 HOH   A O    1 
HETATM 6715 O O    . HOH   D 3 .   ? 45.009 -0.667  2.966   1.00 37.76 ?  429 HOH   A O    1 
HETATM 6716 O O    . HOH   D 3 .   ? 30.338 -12.944 13.481  1.00 19.28 ?  430 HOH   A O    1 
HETATM 6717 O O    . HOH   D 3 .   ? 16.250 16.704  8.644   1.00 30.82 ?  431 HOH   A O    1 
HETATM 6718 O O    . HOH   D 3 .   ? 16.250 -14.163 20.296  1.00 46.77 ?  432 HOH   A O    1 
HETATM 6719 O O    . HOH   D 3 .   ? 32.679 -4.203  -9.935  1.00 29.35 ?  433 HOH   A O    1 
HETATM 6720 O O    . HOH   D 3 .   ? 36.734 -4.983  5.394   1.00 24.60 ?  434 HOH   A O    1 
HETATM 6721 O O    . HOH   D 3 .   ? 35.114 -5.220  -3.110  1.00 17.90 ?  435 HOH   A O    1 
HETATM 6722 O O    . HOH   D 3 .   ? 24.100 3.918   -4.819  1.00 17.90 ?  436 HOH   A O    1 
HETATM 6723 O O    A HOH   D 3 .   ? 16.057 6.990   3.004   0.74 16.36 ?  437 HOH   A O    1 
HETATM 6724 O O    . HOH   D 3 .   ? 22.724 8.168   18.395  1.00 46.44 ?  438 HOH   A O    1 
HETATM 6725 O O    . HOH   D 3 .   ? 11.766 -10.746 17.059  1.00 22.81 ?  439 HOH   A O    1 
HETATM 6726 O O    . HOH   D 3 .   ? 32.584 -10.639 3.209   1.00 30.71 ?  440 HOH   A O    1 
HETATM 6727 O O    . HOH   D 3 .   ? 27.173 -3.208  19.365  1.00 35.65 ?  441 HOH   A O    1 
HETATM 6728 O O    . HOH   D 3 .   ? 21.354 -9.251  21.281  1.00 46.74 ?  442 HOH   A O    1 
HETATM 6729 O O    . HOH   D 3 .   ? 9.503  -16.269 -2.022  1.00 38.02 ?  443 HOH   A O    1 
HETATM 6730 O O    A HOH   D 3 .   ? 11.095 -0.335  1.936   0.74 25.70 ?  444 HOH   A O    1 
HETATM 6731 O O    . HOH   D 3 .   ? 20.614 -17.720 24.796  1.00 47.81 ?  445 HOH   A O    1 
HETATM 6732 O O    . HOH   D 3 .   ? 37.752 -8.837  -3.516  1.00 23.12 ?  446 HOH   A O    1 
HETATM 6733 O O    A HOH   D 3 .   ? 18.896 2.068   -0.742  0.74 11.76 ?  447 HOH   A O    1 
HETATM 6734 O O    A HOH   D 3 .   ? 16.293 2.988   -1.432  0.74 17.09 ?  448 HOH   A O    1 
HETATM 6735 O O    . HOH   D 3 .   ? 19.539 -11.040 24.053  1.00 62.06 ?  449 HOH   A O    1 
HETATM 6736 O O    B HOH   D 3 .   ? 17.997 9.195   8.954   0.26 18.01 ?  450 HOH   A O    1 
HETATM 6737 O O    . HOH   D 3 .   ? 18.443 4.905   -15.078 1.00 49.53 ?  451 HOH   A O    1 
HETATM 6738 O O    . HOH   D 3 .   ? 23.545 -8.036  17.089  1.00 20.89 ?  452 HOH   A O    1 
HETATM 6739 O O    . HOH   D 3 .   ? 23.302 -20.940 1.269   1.00 17.55 ?  453 HOH   A O    1 
HETATM 6740 O O    . HOH   D 3 .   ? 21.556 -14.682 17.989  1.00 50.44 ?  454 HOH   A O    1 
HETATM 6741 O O    . HOH   D 3 .   ? 34.406 -8.080  -0.562  1.00 25.21 ?  455 HOH   A O    1 
HETATM 6742 O O    . HOH   D 3 .   ? 18.412 -16.036 16.361  1.00 37.20 ?  456 HOH   A O    1 
HETATM 6743 O O    B HOH   D 3 .   ? 5.349  -1.169  -1.733  0.26 21.87 ?  457 HOH   A O    1 
HETATM 6744 O O    . HOH   D 3 .   ? 30.632 14.767  2.782   1.00 18.80 ?  458 HOH   A O    1 
HETATM 6745 O O    A HOH   D 3 .   ? -1.411 -4.883  7.637   0.74 34.83 ?  459 HOH   A O    1 
HETATM 6746 O O    . HOH   D 3 .   ? 31.331 -12.754 -0.035  1.00 19.42 ?  460 HOH   A O    1 
HETATM 6747 O O    A HOH   D 3 .   ? 23.244 7.543   -3.219  0.74 24.65 ?  461 HOH   A O    1 
HETATM 6748 O O    . HOH   D 3 .   ? 29.801 -16.048 10.621  1.00 33.93 ?  462 HOH   A O    1 
HETATM 6749 O O    B HOH   D 3 .   ? 16.462 10.349  6.788   0.26 16.58 ?  463 HOH   A O    1 
HETATM 6750 O O    A HOH   D 3 .   ? 14.055 -0.300  3.466   0.74 34.04 ?  464 HOH   A O    1 
HETATM 6751 O O    . HOH   D 3 .   ? 27.822 7.025   -6.486  1.00 42.68 ?  465 HOH   A O    1 
HETATM 6752 O O    . HOH   D 3 .   ? 29.862 -1.877  -12.728 1.00 42.01 ?  466 HOH   A O    1 
HETATM 6753 O O    . HOH   D 3 .   ? 25.432 8.243   -4.798  1.00 28.56 ?  467 HOH   A O    1 
HETATM 6754 O O    . HOH   D 3 .   ? 32.463 -15.942 10.794  1.00 36.49 ?  468 HOH   A O    1 
HETATM 6755 O O    B HOH   D 3 .   ? 20.878 9.486   -4.258  0.26 22.80 ?  469 HOH   A O    1 
HETATM 6756 O O    . HOH   D 3 .   ? 19.845 -17.250 -5.106  1.00 24.22 ?  470 HOH   A O    1 
HETATM 6757 O O    B HOH   D 3 .   ? 7.718  0.179   -1.459  0.26 20.65 ?  471 HOH   A O    1 
HETATM 6758 O O    B HOH   D 3 .   ? 19.199 1.439   -0.880  0.26 10.81 ?  472 HOH   A O    1 
HETATM 6759 O O    . HOH   D 3 .   ? 24.866 5.745   20.704  1.00 51.28 ?  473 HOH   A O    1 
HETATM 6760 O O    . HOH   D 3 .   ? 23.157 -22.335 -3.318  1.00 34.44 ?  474 HOH   A O    1 
HETATM 6761 O O    . HOH   D 3 .   ? 24.654 14.636  7.825   1.00 37.96 ?  475 HOH   A O    1 
HETATM 6762 O O    . HOH   D 3 .   ? 39.585 -7.054  -3.613  1.00 47.21 ?  476 HOH   A O    1 
HETATM 6763 O O    . HOH   D 3 .   ? 22.108 5.301   -6.060  1.00 26.75 ?  477 HOH   A O    1 
HETATM 6764 O O    . HOH   D 3 .   ? 12.101 -13.382 16.404  1.00 49.68 ?  478 HOH   A O    1 
HETATM 6765 O O    . HOH   D 3 .   ? 27.424 -11.356 16.550  1.00 34.93 ?  479 HOH   A O    1 
HETATM 6766 O O    B HOH   D 3 .   ? 22.571 7.415   -4.332  0.26 14.93 ?  480 HOH   A O    1 
HETATM 6767 O O    . HOH   D 3 .   ? 18.740 10.891  11.202  1.00 30.95 ?  481 HOH   A O    1 
HETATM 6768 O O    A HOH   D 3 .   ? 26.954 11.681  -1.302  0.74 27.36 ?  482 HOH   A O    1 
HETATM 6769 O O    . HOH   D 3 .   ? 15.669 -21.458 3.653   1.00 22.72 ?  483 HOH   A O    1 
HETATM 6770 O O    . HOH   D 3 .   ? 23.517 13.744  5.480   1.00 18.13 ?  484 HOH   A O    1 
HETATM 6771 O O    . HOH   D 3 .   ? 10.949 -14.842 -6.179  1.00 34.02 ?  485 HOH   A O    1 
HETATM 6772 O O    B HOH   D 3 .   ? 26.648 12.158  -2.175  0.26 21.42 ?  486 HOH   A O    1 
HETATM 6773 O O    . HOH   D 3 .   ? 12.333 1.614   17.309  1.00 39.75 ?  487 HOH   A O    1 
HETATM 6774 O O    B HOH   D 3 .   ? 22.661 13.856  -2.493  0.26 22.46 ?  488 HOH   A O    1 
HETATM 6775 O O    . HOH   D 3 .   ? 15.662 -16.918 -7.041  1.00 29.44 ?  489 HOH   A O    1 
HETATM 6776 O O    . HOH   D 3 .   ? 13.997 -10.279 -10.890 1.00 33.07 ?  490 HOH   A O    1 
HETATM 6777 O O    . HOH   D 3 .   ? 25.771 10.851  -3.920  1.00 27.93 ?  491 HOH   A O    1 
HETATM 6778 O O    . HOH   D 3 .   ? 18.028 -16.146 -8.823  1.00 36.38 ?  492 HOH   A O    1 
HETATM 6779 O O    B HOH   D 3 .   ? 11.491 0.940   -2.470  0.26 12.96 ?  493 HOH   A O    1 
HETATM 6780 O O    . HOH   D 3 .   ? 35.201 7.410   12.260  1.00 50.58 ?  494 HOH   A O    1 
HETATM 6781 O O    . HOH   D 3 .   ? 28.887 8.967   17.500  1.00 38.14 ?  495 HOH   A O    1 
HETATM 6782 O O    B HOH   D 3 .   ? 22.675 11.606  -3.986  0.26 20.18 ?  496 HOH   A O    1 
HETATM 6783 O O    . HOH   D 3 .   ? 16.825 -20.595 16.130  1.00 27.58 ?  497 HOH   A O    1 
HETATM 6784 O O    A HOH   D 3 .   ? 23.213 11.853  -4.096  0.74 17.82 ?  498 HOH   A O    1 
HETATM 6785 O O    . HOH   D 3 .   ? 17.441 -18.770 19.798  1.00 45.72 ?  499 HOH   A O    1 
HETATM 6786 O O    . HOH   D 3 .   ? 30.832 0.732   19.220  1.00 37.77 ?  500 HOH   A O    1 
HETATM 6787 O O    . HOH   D 3 .   ? 40.979 -3.986  -0.375  1.00 39.21 ?  501 HOH   A O    1 
HETATM 6788 O O    . HOH   D 3 .   ? 44.584 10.460  -1.566  1.00 28.30 ?  502 HOH   A O    1 
HETATM 6789 O O    . HOH   D 3 .   ? 28.711 -7.877  -15.299 1.00 45.52 ?  503 HOH   A O    1 
HETATM 6790 O O    . HOH   D 3 .   ? 28.622 -4.576  -12.312 1.00 38.10 ?  504 HOH   A O    1 
HETATM 6791 O O    B HOH   D 3 .   ? 9.518  3.585   0.676   0.26 14.21 ?  505 HOH   A O    1 
HETATM 6792 O O    . HOH   D 3 .   ? 41.772 9.321   -4.080  1.00 31.10 ?  506 HOH   A O    1 
HETATM 6793 O O    B HOH   D 3 .   ? 24.751 13.814  -0.826  0.26 31.05 ?  507 HOH   A O    1 
HETATM 6794 O O    . HOH   D 3 .   ? 23.254 -12.942 19.292  1.00 48.75 ?  508 HOH   A O    1 
HETATM 6795 O O    . HOH   D 3 .   ? 31.539 -0.537  -10.585 1.00 29.09 ?  509 HOH   A O    1 
HETATM 6796 O O    . HOH   D 3 .   ? 16.051 -6.636  -11.856 1.00 38.10 ?  510 HOH   A O    1 
HETATM 6797 O O    . HOH   D 3 .   ? 40.612 -0.200  -7.784  1.00 34.30 ?  511 HOH   A O    1 
HETATM 6798 O O    . HOH   D 3 .   ? 39.202 2.361   7.577   1.00 31.09 ?  512 HOH   A O    1 
HETATM 6799 O O    . HOH   D 3 .   ? 18.463 -23.208 1.838   1.00 39.19 ?  513 HOH   A O    1 
HETATM 6800 O O    . HOH   D 3 .   ? 19.961 -22.312 4.094   1.00 27.58 ?  514 HOH   A O    1 
HETATM 6801 O O    A HOH   D 3 .   ? 14.012 -25.304 8.823   0.74 25.34 ?  515 HOH   A O    1 
HETATM 6802 O O    B HOH   D 3 .   ? 1.613  3.859   1.087   0.26 18.47 ?  516 HOH   A O    1 
HETATM 6803 O O    . HOH   D 3 .   ? 8.074  -3.025  -5.632  1.00 42.79 ?  517 HOH   A O    1 
HETATM 6804 O O    . HOH   D 3 .   ? 16.150 -23.342 5.698   1.00 28.52 ?  518 HOH   A O    1 
HETATM 6805 O O    . HOH   D 3 .   ? 30.780 -5.785  -11.852 1.00 45.06 ?  519 HOH   A O    1 
HETATM 6806 O O    . HOH   D 3 .   ? 37.393 -6.657  7.520   1.00 25.66 ?  520 HOH   A O    1 
HETATM 6807 O O    . HOH   D 3 .   ? 23.075 -23.757 1.660   1.00 30.42 ?  521 HOH   A O    1 
HETATM 6808 O O    . HOH   D 3 .   ? 30.781 5.848   -14.685 1.00 36.28 ?  522 HOH   A O    1 
HETATM 6809 O O    . HOH   D 3 .   ? 39.553 -0.047  6.581   1.00 30.97 ?  523 HOH   A O    1 
HETATM 6810 O O    . HOH   D 3 .   ? 20.468 -16.001 -7.410  1.00 28.33 ?  524 HOH   A O    1 
HETATM 6811 O O    . HOH   D 3 .   ? 29.044 14.446  0.861   1.00 46.80 ?  525 HOH   A O    1 
HETATM 6812 O O    . HOH   D 3 .   ? 38.060 13.934  6.734   1.00 41.34 ?  526 HOH   A O    1 
HETATM 6813 O O    B HOH   D 3 .   ? 9.989  7.026   8.965   0.26 24.75 ?  527 HOH   A O    1 
HETATM 6814 O O    B HOH   D 3 .   ? 7.842  6.771   2.356   0.26 13.55 ?  528 HOH   A O    1 
HETATM 6815 O O    . HOH   D 3 .   ? 36.511 -6.479  10.173  1.00 41.37 ?  529 HOH   A O    1 
HETATM 6816 O O    . HOH   D 3 .   ? 21.962 -24.041 4.389   1.00 24.81 ?  530 HOH   A O    1 
HETATM 6817 O O    B HOH   D 3 .   ? 9.882  0.952   -5.003  0.26 14.40 ?  531 HOH   A O    1 
HETATM 6818 O O    A HOH   D 3 .   ? 14.892 8.686   4.904   0.74 37.69 ?  532 HOH   A O    1 
HETATM 6819 O O    . HOH   D 3 .   ? 17.390 -6.603  -14.226 1.00 35.54 ?  533 HOH   A O    1 
HETATM 6820 O O    . HOH   D 3 .   ? 24.107 9.008   -7.266  1.00 38.21 ?  534 HOH   A O    1 
HETATM 6821 O O    . HOH   D 3 .   ? 16.389 -21.196 18.781  1.00 37.73 ?  535 HOH   A O    1 
HETATM 6822 O O    . HOH   D 3 .   ? 15.885 -12.218 27.532  1.00 41.51 ?  536 HOH   A O    1 
HETATM 6823 O O    . HOH   D 3 .   ? 14.720 -22.838 19.812  1.00 33.77 ?  537 HOH   A O    1 
HETATM 6824 O O    . HOH   E 3 .   ? 29.783 -22.411 5.428   1.00 19.10 ?  201 HOH   B O    1 
HETATM 6825 O O    . HOH   E 3 .   ? 47.414 -7.455  -3.990  1.00 40.55 ?  202 HOH   B O    1 
HETATM 6826 O O    . HOH   E 3 .   ? 48.114 -6.897  15.585  1.00 33.15 ?  203 HOH   B O    1 
HETATM 6827 O O    . HOH   E 3 .   ? 49.389 -22.638 -19.729 1.00 48.23 ?  204 HOH   B O    1 
HETATM 6828 O O    . HOH   E 3 .   ? 41.846 -35.974 -17.308 1.00 29.54 ?  205 HOH   B O    1 
HETATM 6829 O O    . HOH   E 3 .   ? 41.362 -7.796  5.505   1.00 37.24 ?  206 HOH   B O    1 
HETATM 6830 O O    . HOH   E 3 .   ? 27.822 -41.796 -15.171 1.00 37.41 ?  207 HOH   B O    1 
HETATM 6831 O O    . HOH   E 3 .   ? 37.917 -39.504 -0.237  1.00 38.00 ?  208 HOH   B O    1 
HETATM 6832 O O    . HOH   E 3 .   ? 58.202 -12.933 8.436   1.00 34.27 ?  209 HOH   B O    1 
HETATM 6833 O O    . HOH   E 3 .   ? 59.179 -18.771 6.821   1.00 35.87 ?  210 HOH   B O    1 
HETATM 6834 O O    . HOH   E 3 .   ? 27.680 -29.208 -1.847  1.00 39.78 ?  211 HOH   B O    1 
HETATM 6835 O O    . HOH   E 3 .   ? 50.226 -3.375  7.200   1.00 36.58 ?  212 HOH   B O    1 
HETATM 6836 O O    . HOH   E 3 .   ? 56.351 -19.740 7.356   1.00 33.30 ?  213 HOH   B O    1 
HETATM 6837 O O    . HOH   E 3 .   ? 52.966 -13.493 -20.424 1.00 36.06 ?  214 HOH   B O    1 
HETATM 6838 O O    . HOH   E 3 .   ? 55.342 -16.481 -14.344 1.00 33.80 ?  215 HOH   B O    1 
HETATM 6839 O O    . HOH   E 3 .   ? 35.941 -43.237 -8.540  1.00 30.47 ?  216 HOH   B O    1 
HETATM 6840 O O    . HOH   E 3 .   ? 30.222 -41.060 -8.155  1.00 15.93 ?  217 HOH   B O    1 
HETATM 6841 O O    . HOH   E 3 .   ? 37.145 -19.865 -18.105 1.00 37.94 ?  218 HOH   B O    1 
HETATM 6842 O O    . HOH   E 3 .   ? 54.495 -9.340  -8.800  1.00 18.99 ?  219 HOH   B O    1 
HETATM 6843 O O    . HOH   E 3 .   ? 29.839 -26.312 3.921   1.00 26.99 ?  220 HOH   B O    1 
HETATM 6844 O O    . HOH   E 3 .   ? 44.485 -7.353  2.163   1.00 32.66 ?  221 HOH   B O    1 
HETATM 6845 O O    . HOH   E 3 .   ? 57.781 -24.499 5.005   1.00 32.32 ?  222 HOH   B O    1 
HETATM 6846 O O    . HOH   E 3 .   ? 56.697 -30.762 -7.770  1.00 36.38 ?  223 HOH   B O    1 
HETATM 6847 O O    . HOH   E 3 .   ? 39.304 -10.908 6.081   1.00 28.94 ?  224 HOH   B O    1 
HETATM 6848 O O    . HOH   E 3 .   ? 45.148 -34.941 6.842   1.00 40.31 ?  225 HOH   B O    1 
HETATM 6849 O O    . HOH   E 3 .   ? 34.561 -36.368 -7.206  1.00 16.74 ?  226 HOH   B O    1 
HETATM 6850 O O    . HOH   E 3 .   ? 50.671 -6.118  0.246   1.00 27.28 ?  227 HOH   B O    1 
HETATM 6851 O O    . HOH   E 3 .   ? 29.731 -34.201 -0.458  1.00 34.87 ?  228 HOH   B O    1 
HETATM 6852 O O    . HOH   E 3 .   ? 41.517 -39.211 -14.901 1.00 21.15 ?  229 HOH   B O    1 
HETATM 6853 O O    . HOH   E 3 .   ? 30.826 -28.762 4.271   1.00 23.55 ?  230 HOH   B O    1 
HETATM 6854 O O    . HOH   E 3 .   ? 57.208 -26.825 -7.588  1.00 41.26 ?  231 HOH   B O    1 
HETATM 6855 O O    . HOH   E 3 .   ? 57.381 -16.226 -12.266 1.00 18.32 ?  232 HOH   B O    1 
HETATM 6856 O O    . HOH   E 3 .   ? 32.862 -43.839 -11.332 1.00 18.90 ?  233 HOH   B O    1 
HETATM 6857 O O    . HOH   E 3 .   ? 44.493 -27.834 -0.730  1.00 22.64 ?  234 HOH   B O    1 
HETATM 6858 O O    . HOH   E 3 .   ? 44.988 -43.573 -10.531 1.00 27.86 ?  235 HOH   B O    1 
HETATM 6859 O O    . HOH   E 3 .   ? 40.634 -16.071 14.135  1.00 23.89 ?  236 HOH   B O    1 
HETATM 6860 O O    . HOH   E 3 .   ? 35.134 -7.991  -3.069  1.00 17.64 ?  237 HOH   B O    1 
HETATM 6861 O O    . HOH   E 3 .   ? 50.727 -12.987 -0.481  1.00 12.14 ?  238 HOH   B O    1 
HETATM 6862 O O    . HOH   E 3 .   ? 41.321 -9.650  13.069  1.00 22.01 ?  239 HOH   B O    1 
HETATM 6863 O O    . HOH   E 3 .   ? 42.626 -22.887 3.823   1.00 11.10 ?  240 HOH   B O    1 
HETATM 6864 O O    . HOH   E 3 .   ? 46.368 -1.590  13.277  1.00 29.20 ?  241 HOH   B O    1 
HETATM 6865 O O    . HOH   E 3 .   ? 51.542 -13.868 10.949  1.00 29.85 ?  242 HOH   B O    1 
HETATM 6866 O O    . HOH   E 3 .   ? 25.389 -25.955 -1.397  1.00 32.04 ?  243 HOH   B O    1 
HETATM 6867 O O    . HOH   E 3 .   ? 42.562 -25.393 2.607   1.00 14.83 ?  244 HOH   B O    1 
HETATM 6868 O O    . HOH   E 3 .   ? 28.395 -19.702 -13.155 1.00 23.72 ?  245 HOH   B O    1 
HETATM 6869 O O    . HOH   E 3 .   ? 51.674 -6.519  4.394   1.00 19.73 ?  246 HOH   B O    1 
HETATM 6870 O O    . HOH   E 3 .   ? 43.122 -43.269 -8.257  1.00 27.69 ?  247 HOH   B O    1 
HETATM 6871 O O    . HOH   E 3 .   ? 49.772 -0.571  10.263  1.00 30.73 ?  248 HOH   B O    1 
HETATM 6872 O O    . HOH   E 3 .   ? 39.503 -11.132 0.293   1.00 16.29 ?  249 HOH   B O    1 
HETATM 6873 O O    . HOH   E 3 .   ? 48.477 -36.525 -15.538 1.00 43.61 ?  250 HOH   B O    1 
HETATM 6874 O O    . HOH   E 3 .   ? 34.823 -24.660 13.843  1.00 29.75 ?  251 HOH   B O    1 
HETATM 6875 O O    . HOH   E 3 .   ? 34.211 -18.561 11.402  1.00 22.27 ?  252 HOH   B O    1 
HETATM 6876 O O    . HOH   E 3 .   ? 50.995 -39.954 -8.190  1.00 31.75 ?  253 HOH   B O    1 
HETATM 6877 O O    . HOH   E 3 .   ? 30.846 -15.735 2.618   1.00 12.87 ?  254 HOH   B O    1 
HETATM 6878 O O    . HOH   E 3 .   ? 40.327 -12.754 -11.544 1.00 14.43 ?  255 HOH   B O    1 
HETATM 6879 O O    . HOH   E 3 .   ? 57.612 -24.439 -3.859  1.00 21.69 ?  256 HOH   B O    1 
HETATM 6880 O O    . HOH   E 3 .   ? 38.908 -12.050 12.340  1.00 34.62 ?  257 HOH   B O    1 
HETATM 6881 O O    . HOH   E 3 .   ? 43.216 -32.411 -17.118 1.00 22.57 ?  258 HOH   B O    1 
HETATM 6882 O O    . HOH   E 3 .   ? 57.500 -9.268  1.440   1.00 18.82 ?  259 HOH   B O    1 
HETATM 6883 O O    . HOH   E 3 .   ? 29.733 -25.244 -10.852 1.00 15.80 ?  260 HOH   B O    1 
HETATM 6884 O O    . HOH   E 3 .   ? 41.871 -23.527 9.278   1.00 16.15 ?  261 HOH   B O    1 
HETATM 6885 O O    . HOH   E 3 .   ? 43.366 -15.800 -12.195 1.00 13.35 ?  262 HOH   B O    1 
HETATM 6886 O O    . HOH   E 3 .   ? 27.175 -31.869 -10.025 1.00 20.02 ?  263 HOH   B O    1 
HETATM 6887 O O    . HOH   E 3 .   ? 48.077 -24.520 -17.814 1.00 29.76 ?  264 HOH   B O    1 
HETATM 6888 O O    . HOH   E 3 .   ? 38.448 -11.082 -2.254  1.00 18.07 ?  265 HOH   B O    1 
HETATM 6889 O O    . HOH   E 3 .   ? 34.934 -33.374 -19.227 1.00 29.03 ?  266 HOH   B O    1 
HETATM 6890 O O    . HOH   E 3 .   ? 28.275 -34.388 -9.450  1.00 19.53 ?  267 HOH   B O    1 
HETATM 6891 O O    . HOH   E 3 .   ? 48.016 -22.780 5.819   1.00 16.65 ?  268 HOH   B O    1 
HETATM 6892 O O    . HOH   E 3 .   ? 28.493 -30.872 -14.786 1.00 29.31 ?  269 HOH   B O    1 
HETATM 6893 O O    . HOH   E 3 .   ? 49.317 -28.706 -6.911  1.00 14.88 ?  270 HOH   B O    1 
HETATM 6894 O O    . HOH   E 3 .   ? 58.194 -10.646 -4.114  1.00 21.00 ?  271 HOH   B O    1 
HETATM 6895 O O    . HOH   E 3 .   ? 27.965 -22.917 -8.067  1.00 16.85 ?  272 HOH   B O    1 
HETATM 6896 O O    . HOH   E 3 .   ? 34.460 -12.786 2.567   1.00 26.75 ?  273 HOH   B O    1 
HETATM 6897 O O    . HOH   E 3 .   ? 56.929 -8.671  8.450   1.00 18.90 ?  274 HOH   B O    1 
HETATM 6898 O O    . HOH   E 3 .   ? 42.313 -9.936  9.360   1.00 20.73 ?  275 HOH   B O    1 
HETATM 6899 O O    . HOH   E 3 .   ? 56.200 -23.496 -14.741 1.00 25.75 ?  276 HOH   B O    1 
HETATM 6900 O O    . HOH   E 3 .   ? 41.195 -5.527  11.544  1.00 46.89 ?  277 HOH   B O    1 
HETATM 6901 O O    . HOH   E 3 .   ? 30.589 -42.322 -10.626 1.00 29.14 ?  278 HOH   B O    1 
HETATM 6902 O O    . HOH   E 3 .   ? 49.955 -24.719 5.785   1.00 33.18 ?  279 HOH   B O    1 
HETATM 6903 O O    . HOH   E 3 .   ? 59.770 -15.381 8.145   1.00 31.91 ?  280 HOH   B O    1 
HETATM 6904 O O    . HOH   E 3 .   ? 46.627 -31.275 -4.774  1.00 22.33 ?  281 HOH   B O    1 
HETATM 6905 O O    . HOH   E 3 .   ? 48.395 -25.074 3.098   1.00 12.75 ?  282 HOH   B O    1 
HETATM 6906 O O    . HOH   E 3 .   ? 33.538 -15.324 -13.997 1.00 20.17 ?  283 HOH   B O    1 
HETATM 6907 O O    . HOH   E 3 .   ? 31.859 -17.960 -14.619 1.00 32.49 ?  284 HOH   B O    1 
HETATM 6908 O O    . HOH   E 3 .   ? 46.857 -29.606 9.825   1.00 31.80 ?  285 HOH   B O    1 
HETATM 6909 O O    . HOH   E 3 .   ? 48.718 -20.057 5.930   1.00 13.66 ?  286 HOH   B O    1 
HETATM 6910 O O    . HOH   E 3 .   ? 42.406 -34.719 3.732   1.00 25.58 ?  287 HOH   B O    1 
HETATM 6911 O O    . HOH   E 3 .   ? 36.782 -12.787 -1.511  1.00 26.16 ?  288 HOH   B O    1 
HETATM 6912 O O    . HOH   E 3 .   ? 47.090 -33.978 -4.621  1.00 16.94 ?  289 HOH   B O    1 
HETATM 6913 O O    . HOH   E 3 .   ? 27.567 -26.726 -15.681 1.00 31.63 ?  290 HOH   B O    1 
HETATM 6914 O O    . HOH   E 3 .   ? 51.260 -37.626 -9.556  1.00 24.10 ?  291 HOH   B O    1 
HETATM 6915 O O    . HOH   E 3 .   ? 52.518 -10.432 13.025  1.00 21.94 ?  292 HOH   B O    1 
HETATM 6916 O O    . HOH   E 3 .   ? 45.379 -33.448 -15.936 1.00 22.18 ?  293 HOH   B O    1 
HETATM 6917 O O    . HOH   E 3 .   ? 42.282 -9.987  -14.944 1.00 32.72 ?  294 HOH   B O    1 
HETATM 6918 O O    . HOH   E 3 .   ? 37.323 -35.686 7.177   1.00 32.95 ?  295 HOH   B O    1 
HETATM 6919 O O    . HOH   E 3 .   ? 45.934 -40.410 -3.606  1.00 28.24 ?  296 HOH   B O    1 
HETATM 6920 O O    . HOH   E 3 .   ? 57.686 -22.136 3.055   1.00 25.37 ?  297 HOH   B O    1 
HETATM 6921 O O    . HOH   E 3 .   ? 44.615 -27.468 1.970   1.00 15.10 ?  298 HOH   B O    1 
HETATM 6922 O O    . HOH   E 3 .   ? 42.870 -20.343 -20.785 1.00 33.39 ?  299 HOH   B O    1 
HETATM 6923 O O    . HOH   E 3 .   ? 44.034 -29.378 -4.699  1.00 24.18 ?  300 HOH   B O    1 
HETATM 6924 O O    . HOH   E 3 .   ? 52.622 -35.691 -8.532  1.00 26.81 ?  301 HOH   B O    1 
HETATM 6925 O O    . HOH   E 3 .   ? 32.808 -34.602 -5.921  1.00 15.74 ?  302 HOH   B O    1 
HETATM 6926 O O    . HOH   E 3 .   ? 53.069 -16.046 -12.766 1.00 28.45 ?  303 HOH   B O    1 
HETATM 6927 O O    . HOH   E 3 .   ? 57.138 -12.098 12.398  1.00 37.87 ?  304 HOH   B O    1 
HETATM 6928 O O    . HOH   E 3 .   ? 37.481 -18.241 13.109  1.00 26.82 ?  305 HOH   B O    1 
HETATM 6929 O O    . HOH   E 3 .   ? 42.666 -12.284 -18.530 1.00 28.48 ?  306 HOH   B O    1 
HETATM 6930 O O    . HOH   E 3 .   ? 43.533 -15.419 18.231  1.00 30.39 ?  307 HOH   B O    1 
HETATM 6931 O O    . HOH   E 3 .   ? 35.020 -33.555 4.478   1.00 27.65 ?  308 HOH   B O    1 
HETATM 6932 O O    . HOH   E 3 .   ? 37.841 -10.267 -10.797 1.00 16.04 ?  309 HOH   B O    1 
HETATM 6933 O O    . HOH   E 3 .   ? 25.938 -21.478 -3.563  1.00 15.40 ?  310 HOH   B O    1 
HETATM 6934 O O    . HOH   E 3 .   ? 41.150 -24.483 15.822  1.00 40.15 ?  311 HOH   B O    1 
HETATM 6935 O O    . HOH   E 3 .   ? 53.491 -30.199 4.541   1.00 18.01 ?  312 HOH   B O    1 
HETATM 6936 O O    . HOH   E 3 .   ? 40.255 -10.839 -9.597  1.00 16.40 ?  313 HOH   B O    1 
HETATM 6937 O O    . HOH   E 3 .   ? 52.585 -29.251 -13.014 1.00 23.42 ?  314 HOH   B O    1 
HETATM 6938 O O    . HOH   E 3 .   ? 62.828 -20.237 -0.799  1.00 36.61 ?  315 HOH   B O    1 
HETATM 6939 O O    . HOH   E 3 .   ? 59.992 -17.080 -10.426 1.00 32.55 ?  316 HOH   B O    1 
HETATM 6940 O O    . HOH   E 3 .   ? 62.654 -13.577 4.678   1.00 27.27 ?  317 HOH   B O    1 
HETATM 6941 O O    . HOH   E 3 .   ? 48.169 -32.677 -16.600 1.00 43.99 ?  318 HOH   B O    1 
HETATM 6942 O O    . HOH   E 3 .   ? 41.672 -8.124  1.316   1.00 24.42 ?  319 HOH   B O    1 
HETATM 6943 O O    . HOH   E 3 .   ? 43.185 -21.470 10.647  1.00 15.24 ?  320 HOH   B O    1 
HETATM 6944 O O    . HOH   E 3 .   ? 44.563 -24.672 9.558   1.00 18.69 ?  321 HOH   B O    1 
HETATM 6945 O O    . HOH   E 3 .   ? 38.338 -12.799 7.917   1.00 18.23 ?  322 HOH   B O    1 
HETATM 6946 O O    . HOH   E 3 .   ? 51.398 -32.954 -10.772 1.00 38.51 ?  323 HOH   B O    1 
HETATM 6947 O O    . HOH   E 3 .   ? 26.336 -21.022 -6.291  1.00 15.84 ?  324 HOH   B O    1 
HETATM 6948 O O    . HOH   E 3 .   ? 37.288 -30.646 -21.082 1.00 30.16 ?  325 HOH   B O    1 
HETATM 6949 O O    . HOH   E 3 .   ? 53.649 -12.596 -22.301 1.00 32.42 ?  326 HOH   B O    1 
HETATM 6950 O O    . HOH   E 3 .   ? 36.688 -12.439 4.261   1.00 18.38 ?  327 HOH   B O    1 
HETATM 6951 O O    . HOH   E 3 .   ? 27.994 -14.793 -9.448  1.00 32.17 ?  328 HOH   B O    1 
HETATM 6952 O O    . HOH   E 3 .   ? 33.530 -31.180 11.034  1.00 31.89 ?  329 HOH   B O    1 
HETATM 6953 O O    . HOH   E 3 .   ? 47.140 -24.499 8.123   1.00 23.40 ?  330 HOH   B O    1 
HETATM 6954 O O    . HOH   E 3 .   ? 38.371 -9.361  -13.314 1.00 25.59 ?  331 HOH   B O    1 
HETATM 6955 O O    . HOH   E 3 .   ? 44.253 -1.778  7.542   1.00 45.80 ?  332 HOH   B O    1 
HETATM 6956 O O    . HOH   E 3 .   ? 51.811 -5.860  -7.845  1.00 46.16 ?  333 HOH   B O    1 
HETATM 6957 O O    . HOH   E 3 .   ? 39.464 -23.604 -20.298 1.00 35.27 ?  334 HOH   B O    1 
HETATM 6958 O O    . HOH   E 3 .   ? 43.111 -34.700 0.088   1.00 19.79 ?  335 HOH   B O    1 
HETATM 6959 O O    . HOH   E 3 .   ? 47.469 -27.467 1.976   1.00 14.07 ?  336 HOH   B O    1 
HETATM 6960 O O    . HOH   E 3 .   ? 45.762 -36.272 -16.155 1.00 32.52 ?  337 HOH   B O    1 
HETATM 6961 O O    . HOH   E 3 .   ? 48.595 -11.929 -14.049 1.00 26.78 ?  338 HOH   B O    1 
HETATM 6962 O O    . HOH   E 3 .   ? 46.816 -19.923 12.284  1.00 29.28 ?  339 HOH   B O    1 
HETATM 6963 O O    . HOH   E 3 .   ? 42.839 -43.569 -14.355 1.00 44.39 ?  340 HOH   B O    1 
HETATM 6964 O O    . HOH   E 3 .   ? 37.020 -15.108 -16.548 1.00 39.57 ?  341 HOH   B O    1 
HETATM 6965 O O    . HOH   E 3 .   ? 37.088 -45.243 -9.811  1.00 36.45 ?  342 HOH   B O    1 
HETATM 6966 O O    . HOH   E 3 .   ? 28.898 -42.964 -12.393 1.00 38.40 ?  343 HOH   B O    1 
HETATM 6967 O O    . HOH   E 3 .   ? 33.006 -14.687 1.002   1.00 19.29 ?  344 HOH   B O    1 
HETATM 6968 O O    . HOH   E 3 .   ? 38.458 -12.278 -16.285 1.00 41.70 ?  345 HOH   B O    1 
HETATM 6969 O O    . HOH   E 3 .   ? 39.804 -44.322 -11.218 1.00 36.33 ?  346 HOH   B O    1 
HETATM 6970 O O    . HOH   E 3 .   ? 33.796 -9.302  -8.829  1.00 31.90 ?  347 HOH   B O    1 
HETATM 6971 O O    . HOH   E 3 .   ? 40.419 -43.536 -9.122  1.00 26.28 ?  348 HOH   B O    1 
HETATM 6972 O O    . HOH   E 3 .   ? 62.549 -20.124 -4.837  1.00 44.96 ?  349 HOH   B O    1 
HETATM 6973 O O    . HOH   E 3 .   ? 27.745 -26.640 -0.624  1.00 30.32 ?  350 HOH   B O    1 
HETATM 6974 O O    . HOH   E 3 .   ? 38.481 -22.285 15.021  1.00 42.42 ?  351 HOH   B O    1 
HETATM 6975 O O    . HOH   E 3 .   ? 44.167 -37.352 -17.728 1.00 32.90 ?  352 HOH   B O    1 
HETATM 6976 O O    . HOH   E 3 .   ? 55.628 -8.278  10.859  1.00 24.69 ?  353 HOH   B O    1 
HETATM 6977 O O    . HOH   E 3 .   ? 36.076 -8.604  -9.737  1.00 33.73 ?  354 HOH   B O    1 
HETATM 6978 O O    . HOH   E 3 .   ? 23.169 -23.704 6.770   1.00 31.83 ?  355 HOH   B O    1 
HETATM 6979 O O    . HOH   E 3 .   ? 56.520 -7.284  3.130   1.00 27.96 ?  356 HOH   B O    1 
HETATM 6980 O O    . HOH   E 3 .   ? 34.650 -10.328 7.479   1.00 23.28 ?  357 HOH   B O    1 
HETATM 6981 O O    . HOH   E 3 .   ? 43.160 -12.651 -21.190 1.00 37.78 ?  358 HOH   B O    1 
HETATM 6982 O O    . HOH   E 3 .   ? 61.522 -19.910 1.642   1.00 33.75 ?  359 HOH   B O    1 
HETATM 6983 O O    . HOH   E 3 .   ? 34.123 -7.744  11.486  1.00 39.69 ?  360 HOH   B O    1 
HETATM 6984 O O    . HOH   E 3 .   ? 56.984 -21.509 -16.399 1.00 39.13 ?  361 HOH   B O    1 
HETATM 6985 O O    . HOH   E 3 .   ? 40.214 -8.893  9.897   1.00 37.43 ?  362 HOH   B O    1 
HETATM 6986 O O    . HOH   E 3 .   ? 27.147 -25.984 -11.497 1.00 31.18 ?  363 HOH   B O    1 
HETATM 6987 O O    . HOH   E 3 .   ? 32.419 -23.625 14.052  1.00 38.85 ?  364 HOH   B O    1 
HETATM 6988 O O    . HOH   E 3 .   ? 54.228 -5.759  2.970   1.00 35.55 ?  365 HOH   B O    1 
HETATM 6989 O O    . HOH   E 3 .   ? 48.388 -26.572 8.855   1.00 36.81 ?  366 HOH   B O    1 
HETATM 6990 O O    . HOH   E 3 .   ? 58.973 -10.439 9.207   1.00 38.94 ?  367 HOH   B O    1 
HETATM 6991 O O    . HOH   E 3 .   ? 36.186 -8.707  8.959   1.00 40.86 ?  368 HOH   B O    1 
HETATM 6992 O O    . HOH   E 3 .   ? 56.137 -7.882  -0.617  1.00 35.67 ?  369 HOH   B O    1 
HETATM 6993 O O    . HOH   E 3 .   ? 39.853 -7.041  7.863   1.00 41.28 ?  370 HOH   B O    1 
HETATM 6994 O O    . HOH   E 3 .   ? 40.054 -11.376 -13.984 1.00 32.60 ?  371 HOH   B O    1 
HETATM 6995 O O    . HOH   E 3 .   ? 63.050 -12.473 6.897   1.00 37.70 ?  372 HOH   B O    1 
HETATM 6996 O O    . HOH   E 3 .   ? 41.799 -9.971  -17.424 1.00 54.21 ?  373 HOH   B O    1 
HETATM 6997 O O    . HOH   E 3 .   ? 52.007 -12.981 13.387  1.00 30.82 ?  374 HOH   B O    1 
HETATM 6998 O O    . HOH   E 3 .   ? 41.869 -6.799  -4.895  1.00 45.68 ?  375 HOH   B O    1 
HETATM 6999 O O    . HOH   E 3 .   ? 38.039 -10.648 10.078  1.00 28.86 ?  376 HOH   B O    1 
HETATM 7000 O O    . HOH   E 3 .   ? 36.518 -22.797 13.278  1.00 26.68 ?  377 HOH   B O    1 
HETATM 7001 O O    . HOH   E 3 .   ? 44.056 -5.626  -3.484  1.00 41.59 ?  378 HOH   B O    1 
HETATM 7002 O O    . HOH   E 3 .   ? 42.614 -17.173 -23.247 1.00 43.26 ?  379 HOH   B O    1 
HETATM 7003 O O    . HOH   E 3 .   ? 40.181 -7.629  3.209   1.00 38.31 ?  380 HOH   B O    1 
HETATM 7004 O O    . HOH   E 3 .   ? 39.734 -14.128 15.711  1.00 48.20 ?  381 HOH   B O    1 
HETATM 7005 O O    . HOH   E 3 .   ? 52.866 -29.887 7.164   1.00 22.49 ?  382 HOH   B O    1 
HETATM 7006 O O    . HOH   E 3 .   ? 60.475 -22.259 2.818   1.00 45.14 ?  383 HOH   B O    1 
HETATM 7007 O O    . HOH   E 3 .   ? 40.990 -9.808  15.768  1.00 43.35 ?  384 HOH   B O    1 
HETATM 7008 O O    . HOH   E 3 .   ? 25.747 -18.900 -11.919 1.00 37.71 ?  385 HOH   B O    1 
HETATM 7009 O O    . HOH   E 3 .   ? 35.321 -20.308 13.309  1.00 28.58 ?  386 HOH   B O    1 
HETATM 7010 O O    . HOH   E 3 .   ? 23.919 -20.860 -7.713  1.00 26.61 ?  387 HOH   B O    1 
HETATM 7011 O O    . HOH   E 3 .   ? 46.782 -5.344  2.943   1.00 39.92 ?  388 HOH   B O    1 
HETATM 7012 O O    . HOH   E 3 .   ? 35.286 -33.758 7.288   1.00 40.04 ?  389 HOH   B O    1 
HETATM 7013 O O    . HOH   E 3 .   ? 40.744 -6.622  -0.859  1.00 24.06 ?  390 HOH   B O    1 
HETATM 7014 O O    . HOH   E 3 .   ? 44.073 -31.769 -3.884  1.00 32.99 ?  391 HOH   B O    1 
HETATM 7015 O O    . HOH   E 3 .   ? 26.613 -27.983 -13.537 1.00 35.56 ?  392 HOH   B O    1 
HETATM 7016 O O    . HOH   E 3 .   ? 27.846 -27.115 2.171   1.00 30.53 ?  393 HOH   B O    1 
HETATM 7017 O O    . HOH   E 3 .   ? 24.611 -20.660 -10.514 1.00 37.66 ?  394 HOH   B O    1 
HETATM 7018 O O    . HOH   E 3 .   ? 34.405 -33.482 9.574   1.00 33.85 ?  395 HOH   B O    1 
HETATM 7019 O O    . HOH   E 3 .   ? 26.887 -30.711 -12.663 1.00 28.13 ?  396 HOH   B O    1 
HETATM 7020 O O    . HOH   E 3 .   ? 50.648 -30.807 8.657   1.00 27.16 ?  397 HOH   B O    1 
HETATM 7021 O O    . HOH   E 3 .   ? 45.760 -20.304 15.171  1.00 49.06 ?  398 HOH   B O    1 
HETATM 7022 O O    . HOH   E 3 .   ? 57.707 -6.504  -2.379  1.00 37.47 ?  399 HOH   B O    1 
HETATM 7023 O O    . HOH   E 3 .   ? 40.872 -11.774 -22.318 1.00 41.49 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.6123 0.5983 0.6640 0.0083  -0.0344 0.0830  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6029 0.5942 0.6322 0.0032  -0.0239 0.0559  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6097 0.5961 0.6528 0.0071  -0.0336 0.0818  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6008 0.5923 0.6262 0.0025  -0.0242 0.0576  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5959 0.5856 0.6234 0.0013  -0.0353 0.0835  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5912 0.5837 0.6086 -0.0011 -0.0294 0.0694  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5987 0.5876 0.6313 0.0032  -0.0373 0.0877  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5939 0.5858 0.6157 0.0001  -0.0303 0.0702  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6184 0.6025 0.6628 0.0106  -0.0290 0.0792  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6063 0.5974 0.6330 0.0048  -0.0194 0.0489  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6211 0.6045 0.6646 0.0117  -0.0270 0.0779  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6081 0.5990 0.6347 0.0055  -0.0176 0.0456  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6213 0.6045 0.6655 0.0123  -0.0270 0.0785  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6082 0.5989 0.6349 0.0058  -0.0176 0.0460  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.5767 0.5710 0.5763 -0.0062 -0.0329 0.0814  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5411 0.5421 0.4907 -0.0194 -0.0318 0.0888  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.4947 0.5100 0.4408 -0.0302 -0.0190 0.0643  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.4960 0.5109 0.4300 -0.0307 -0.0228 0.0670  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5500 0.5429 0.4510 -0.0213 -0.0428 0.1164  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5568 0.5420 0.4106 -0.0224 -0.0518 0.1438  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5599 0.5394 0.3892 -0.0227 -0.0545 0.1561  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5584 0.5424 0.3996 -0.0218 -0.0556 0.1550  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4438 0.4698 0.3941 -0.0411 -0.0045 0.0362  5   SER   A N   
47   C CA  . SER   A 5   ? 0.3924 0.4273 0.3527 -0.0504 0.0105  0.0071  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3367 0.3753 0.2891 -0.0518 0.0299  -0.0105 5   SER   A C   
49   O O   . SER   A 5   ? 0.3419 0.3862 0.2865 -0.0393 0.0345  -0.0268 5   SER   A O   
50   C CB  . SER   A 5   ? 0.3982 0.4403 0.3727 -0.0557 0.0077  -0.0012 5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4032 0.4525 0.3824 -0.0572 0.0106  -0.0041 5   SER   A OG  
57   N N   A PHE   A 6   ? 0.2968 0.3348 0.2451 -0.0682 0.0512  -0.0040 6   PHE   A N   
58   N N   B PHE   A 6   ? 0.3110 0.3495 0.2717 -0.0479 0.0269  -0.0090 6   PHE   A N   
59   C CA  A PHE   A 6   ? 0.2640 0.2952 0.2194 -0.0798 0.0681  0.0112  6   PHE   A CA  
60   C CA  B PHE   A 6   ? 0.2859 0.3208 0.2551 -0.0434 0.0240  -0.0035 6   PHE   A CA  
61   C C   A PHE   A 6   ? 0.2617 0.2900 0.2395 -0.0874 0.0838  0.0152  6   PHE   A C   
62   C C   B PHE   A 6   ? 0.2706 0.3053 0.2622 -0.0433 0.0267  -0.0030 6   PHE   A C   
63   O O   A PHE   A 6   ? 0.2725 0.2972 0.2632 -0.0844 0.0857  0.0255  6   PHE   A O   
64   O O   B PHE   A 6   ? 0.2723 0.3079 0.2706 -0.0440 0.0238  -0.0026 6   PHE   A O   
65   C CB  A PHE   A 6   ? 0.2455 0.2675 0.1946 -0.0736 0.0600  0.0190  6   PHE   A CB  
66   C CB  B PHE   A 6   ? 0.2779 0.3075 0.2357 -0.0386 0.0183  0.0011  6   PHE   A CB  
67   C CG  A PHE   A 6   ? 0.2292 0.2490 0.1785 -0.0665 0.0527  0.0249  6   PHE   A CG  
68   C CG  B PHE   A 6   ? 0.2702 0.2957 0.2187 -0.0352 0.0135  0.0070  6   PHE   A CG  
69   C CD1 A PHE   A 6   ? 0.2255 0.2411 0.1823 -0.0575 0.0429  0.0339  6   PHE   A CD1 
70   C CD1 B PHE   A 6   ? 0.2673 0.2907 0.2128 -0.0324 0.0102  0.0115  6   PHE   A CD1 
71   C CD2 A PHE   A 6   ? 0.2312 0.2510 0.1962 -0.0521 0.0463  0.0185  6   PHE   A CD2 
72   C CD2 B PHE   A 6   ? 0.2686 0.2923 0.2167 -0.0317 0.0123  0.0089  6   PHE   A CD2 
73   C CE1 A PHE   A 6   ? 0.2243 0.2400 0.1880 -0.0543 0.0435  0.0356  6   PHE   A CE1 
74   C CE1 B PHE   A 6   ? 0.2662 0.2882 0.2116 -0.0312 0.0090  0.0139  6   PHE   A CE1 
75   C CE2 A PHE   A 6   ? 0.2288 0.2502 0.2076 -0.0476 0.0467  0.0133  6   PHE   A CE2 
76   C CE2 B PHE   A 6   ? 0.2672 0.2902 0.2155 -0.0300 0.0117  0.0096  6   PHE   A CE2 
77   C CZ  A PHE   A 6   ? 0.2276 0.2433 0.1958 -0.0504 0.0395  0.0198  6   PHE   A CZ  
78   C CZ  B PHE   A 6   ? 0.2666 0.2884 0.2123 -0.0301 0.0085  0.0118  6   PHE   A CZ  
97   N N   A SER   A 7   ? 0.2497 0.2796 0.2345 -0.0911 0.0965  0.0114  7   SER   A N   
98   N N   B SER   A 7   ? 0.2533 0.2872 0.2603 -0.0421 0.0307  -0.0023 7   SER   A N   
99   C CA  A SER   A 7   ? 0.2504 0.2775 0.2512 -0.0786 0.0943  -0.0065 7   SER   A CA  
100  C CA  B SER   A 7   ? 0.2402 0.2706 0.2628 -0.0394 0.0344  -0.0030 7   SER   A CA  
101  C C   A SER   A 7   ? 0.2351 0.2490 0.2509 -0.0719 0.1026  -0.0062 7   SER   A C   
102  C C   B SER   A 7   ? 0.2263 0.2504 0.2495 -0.0356 0.0387  0.0013  7   SER   A C   
103  O O   A SER   A 7   ? 0.2431 0.2380 0.2475 -0.0758 0.0982  -0.0064 7   SER   A O   
104  O O   B SER   A 7   ? 0.2265 0.2498 0.2486 -0.0355 0.0399  0.0018  7   SER   A O   
105  C CB  A SER   A 7   ? 0.2680 0.3036 0.2688 -0.0646 0.0915  -0.0098 7   SER   A CB  
106  C CB  B SER   A 7   ? 0.2434 0.2741 0.2807 -0.0383 0.0349  -0.0087 7   SER   A CB  
107  O OG  A SER   A 7   ? 0.2846 0.3218 0.2987 -0.0518 0.0867  -0.0164 7   SER   A OG  
108  O OG  B SER   A 7   ? 0.2471 0.2794 0.2961 -0.0358 0.0346  -0.0110 7   SER   A OG  
119  N N   A GLY   A 8   ? 0.2191 0.2358 0.2650 -0.0600 0.0953  -0.0123 8   GLY   A N   
120  N N   B GLY   A 8   ? 0.2144 0.2311 0.2412 -0.0335 0.0393  0.0019  8   GLY   A N   
121  C CA  A GLY   A 8   ? 0.2035 0.2206 0.2775 -0.0419 0.0902  -0.0122 8   GLY   A CA  
122  C CA  B GLY   A 8   ? 0.2037 0.2134 0.2341 -0.0275 0.0406  0.0039  8   GLY   A CA  
123  C C   A GLY   A 8   ? 0.1828 0.2087 0.2719 -0.0327 0.0788  -0.0089 8   GLY   A C   
124  C C   B GLY   A 8   ? 0.1921 0.1978 0.2202 -0.0254 0.0397  0.0072  8   GLY   A C   
125  O O   A GLY   A 8   ? 0.1756 0.2112 0.2956 -0.0150 0.0745  -0.0302 8   GLY   A O   
126  O O   B GLY   A 8   ? 0.1925 0.1987 0.2276 -0.0214 0.0355  0.0024  8   GLY   A O   
133  N N   A TYR   A 9   ? 0.1652 0.1928 0.2454 -0.0293 0.0658  0.0029  9   TYR   A N   
134  N N   B TYR   A 9   ? 0.1787 0.1813 0.2023 -0.0229 0.0386  0.0121  9   TYR   A N   
135  C CA  A TYR   A 9   ? 0.1525 0.1782 0.2191 -0.0262 0.0521  0.0115  9   TYR   A CA  
136  C CA  B TYR   A 9   ? 0.1670 0.1649 0.1858 -0.0212 0.0386  0.0180  9   TYR   A CA  
137  C C   A TYR   A 9   ? 0.1502 0.1624 0.2166 -0.0172 0.0435  0.0292  9   TYR   A C   
138  C C   B TYR   A 9   ? 0.1608 0.1475 0.1838 -0.0174 0.0406  0.0229  9   TYR   A C   
139  O O   A TYR   A 9   ? 0.1518 0.1723 0.2352 -0.0148 0.0425  0.0330  9   TYR   A O   
140  O O   B TYR   A 9   ? 0.1613 0.1516 0.1940 -0.0165 0.0471  0.0175  9   TYR   A O   
141  C CB  A TYR   A 9   ? 0.1490 0.1864 0.2210 -0.0214 0.0388  0.0033  9   TYR   A CB  
142  C CB  B TYR   A 9   ? 0.1619 0.1697 0.1828 -0.0221 0.0373  0.0142  9   TYR   A CB  
143  C CG  A TYR   A 9   ? 0.1483 0.1846 0.2133 -0.0098 0.0391  0.0005  9   TYR   A CG  
144  C CG  B TYR   A 9   ? 0.1568 0.1706 0.1806 -0.0225 0.0395  0.0073  9   TYR   A CG  
145  C CD1 A TYR   A 9   ? 0.1486 0.1858 0.2185 -0.0112 0.0467  -0.0007 9   TYR   A CD1 
146  C CD1 B TYR   A 9   ? 0.1552 0.1703 0.1840 -0.0277 0.0448  0.0056  9   TYR   A CD1 
147  C CD2 A TYR   A 9   ? 0.1465 0.1782 0.2104 -0.0042 0.0314  0.0109  9   TYR   A CD2 
148  C CD2 B TYR   A 9   ? 0.1532 0.1661 0.1724 -0.0189 0.0364  0.0108  9   TYR   A CD2 
149  C CE1 A TYR   A 9   ? 0.1516 0.1871 0.2198 -0.0126 0.0422  -0.0024 9   TYR   A CE1 
150  C CE1 B TYR   A 9   ? 0.1515 0.1647 0.1819 -0.0276 0.0473  0.0047  9   TYR   A CE1 
151  C CE2 A TYR   A 9   ? 0.1458 0.1810 0.2163 -0.0054 0.0302  0.0073  9   TYR   A CE2 
152  C CE2 B TYR   A 9   ? 0.1471 0.1629 0.1696 -0.0181 0.0400  0.0110  9   TYR   A CE2 
153  C CZ  A TYR   A 9   ? 0.1502 0.1893 0.2291 -0.0193 0.0416  0.0044  9   TYR   A CZ  
154  C CZ  B TYR   A 9   ? 0.1426 0.1572 0.1753 -0.0238 0.0501  0.0092  9   TYR   A CZ  
155  O OH  A TYR   A 9   ? 0.1656 0.2002 0.2502 -0.0274 0.0357  0.0064  9   TYR   A OH  
156  O OH  B TYR   A 9   ? 0.1344 0.1555 0.1774 -0.0246 0.0537  0.0086  9   TYR   A OH  
175  N N   A LEU   A 10  ? 0.1524 0.1467 0.2049 -0.0135 0.0339  0.0313  10  LEU   A N   
176  N N   B LEU   A 10  ? 0.1543 0.1326 0.1717 -0.0137 0.0448  0.0302  10  LEU   A N   
177  C CA  A LEU   A 10  ? 0.1468 0.1427 0.2109 -0.0164 0.0252  0.0352  10  LEU   A CA  
178  C CA  B LEU   A 10  ? 0.1480 0.1229 0.1586 -0.0116 0.0427  0.0286  10  LEU   A CA  
179  C C   A LEU   A 10  ? 0.1393 0.1388 0.1942 -0.0141 0.0257  0.0379  10  LEU   A C   
180  C C   B LEU   A 10  ? 0.1488 0.1159 0.1786 -0.0086 0.0418  0.0306  10  LEU   A C   
181  O O   A LEU   A 10  ? 0.1425 0.1363 0.2091 -0.0146 0.0357  0.0408  10  LEU   A O   
182  O O   B LEU   A 10  ? 0.1519 0.1119 0.1959 -0.0094 0.0424  0.0355  10  LEU   A O   
183  C CB  A LEU   A 10  ? 0.1578 0.1576 0.2452 -0.0176 0.0144  0.0540  10  LEU   A CB  
184  C CB  B LEU   A 10  ? 0.1460 0.1190 0.1338 -0.0151 0.0318  0.0351  10  LEU   A CB  
185  C CG  A LEU   A 10  ? 0.1840 0.1879 0.2881 -0.0098 -0.0169 0.0669  10  LEU   A CG  
186  C CG  B LEU   A 10  ? 0.1444 0.1190 0.1025 -0.0145 0.0157  0.0401  10  LEU   A CG  
187  C CD1 A LEU   A 10  ? 0.2040 0.2058 0.3185 -0.0108 -0.0208 0.0691  10  LEU   A CD1 
188  C CD1 B LEU   A 10  ? 0.1469 0.1282 0.1083 -0.0118 0.0108  0.0371  10  LEU   A CD1 
189  C CD2 A LEU   A 10  ? 0.2039 0.2103 0.3162 -0.0148 -0.0142 0.0561  10  LEU   A CD2 
190  C CD2 B LEU   A 10  ? 0.1451 0.1172 0.0925 -0.0133 0.0129  0.0406  10  LEU   A CD2 
213  N N   A LYS   A 11  ? 0.1358 0.1435 0.1861 -0.0150 0.0260  0.0377  11  LYS   A N   
214  N N   B LYS   A 11  ? 0.1470 0.1159 0.1734 -0.0017 0.0448  0.0298  11  LYS   A N   
215  C CA  A LYS   A 11  ? 0.1453 0.1429 0.1886 -0.0198 0.0162  0.0365  11  LYS   A CA  
216  C CA  B LYS   A 11  ? 0.1402 0.1188 0.1725 -0.0010 0.0404  0.0310  11  LYS   A CA  
217  C C   A LYS   A 11  ? 0.1382 0.1427 0.1800 -0.0253 0.0123  0.0358  11  LYS   A C   
218  C C   B LYS   A 11  ? 0.1423 0.1185 0.1718 0.0044  0.0371  0.0371  11  LYS   A C   
219  O O   A LYS   A 11  ? 0.1493 0.1632 0.2074 -0.0477 0.0190  0.0248  11  LYS   A O   
220  O O   B LYS   A 11  ? 0.1395 0.1135 0.1780 0.0099  0.0369  0.0274  11  LYS   A O   
221  C CB  A LYS   A 11  ? 0.1479 0.1337 0.1717 -0.0182 0.0131  0.0293  11  LYS   A CB  
222  C CB  B LYS   A 11  ? 0.1383 0.1189 0.1615 -0.0050 0.0334  0.0278  11  LYS   A CB  
223  C CG  A LYS   A 11  ? 0.1577 0.1344 0.1718 -0.0184 0.0182  0.0286  11  LYS   A CG  
224  C CG  B LYS   A 11  ? 0.1360 0.1241 0.1542 -0.0040 0.0267  0.0296  11  LYS   A CG  
225  C CD  A LYS   A 11  ? 0.1604 0.1410 0.1737 -0.0196 0.0129  0.0282  11  LYS   A CD  
226  C CD  B LYS   A 11  ? 0.1367 0.1342 0.1592 0.0024  0.0236  0.0309  11  LYS   A CD  
227  C CE  A LYS   A 11  ? 0.1642 0.1387 0.1751 -0.0165 0.0082  0.0289  11  LYS   A CE  
228  C CE  B LYS   A 11  ? 0.1367 0.1359 0.1560 0.0053  0.0188  0.0325  11  LYS   A CE  
229  N NZ  A LYS   A 11  ? 0.1635 0.1390 0.1783 0.0002  0.0110  0.0212  11  LYS   A NZ  
230  N NZ  B LYS   A 11  ? 0.1352 0.1385 0.1578 0.0041  0.0236  0.0250  11  LYS   A NZ  
257  N N   A LEU   A 12  ? 0.1250 0.1361 0.1635 -0.0191 0.0180  0.0309  12  LEU   A N   
258  N N   B LEU   A 12  ? 0.1452 0.1350 0.1727 0.0072  0.0315  0.0357  12  LEU   A N   
259  C CA  A LEU   A 12  ? 0.1308 0.1452 0.1683 -0.0159 0.0123  0.0373  12  LEU   A CA  
260  C CA  B LEU   A 12  ? 0.1464 0.1462 0.1625 0.0084  0.0314  0.0403  12  LEU   A CA  
261  C C   A LEU   A 12  ? 0.1363 0.1351 0.1654 -0.0200 0.0105  0.0364  12  LEU   A C   
262  C C   B LEU   A 12  ? 0.1435 0.1485 0.1585 0.0069  0.0346  0.0347  12  LEU   A C   
263  O O   A LEU   A 12  ? 0.1428 0.1404 0.1750 -0.0191 0.0049  0.0264  12  LEU   A O   
264  O O   B LEU   A 12  ? 0.1470 0.1451 0.1620 0.0089  0.0371  0.0387  12  LEU   A O   
265  C CB  A LEU   A 12  ? 0.1438 0.1456 0.1872 -0.0138 0.0023  0.0511  12  LEU   A CB  
266  C CB  B LEU   A 12  ? 0.1497 0.1586 0.1679 0.0071  0.0319  0.0420  12  LEU   A CB  
267  C CG  A LEU   A 12  ? 0.1503 0.1600 0.2035 -0.0060 0.0066  0.0686  12  LEU   A CG  
268  C CG  B LEU   A 12  ? 0.1488 0.1667 0.1819 0.0062  0.0356  0.0384  12  LEU   A CG  
269  C CD1 A LEU   A 12  ? 0.1601 0.1640 0.2187 0.0075  0.0202  0.0779  12  LEU   A CD1 
270  C CD1 B LEU   A 12  ? 0.1494 0.1728 0.1800 0.0111  0.0368  0.0381  12  LEU   A CD1 
271  C CD2 A LEU   A 12  ? 0.1489 0.1760 0.2116 -0.0143 0.0055  0.0522  12  LEU   A CD2 
272  C CD2 B LEU   A 12  ? 0.1497 0.1705 0.1926 -0.0004 0.0324  0.0355  12  LEU   A CD2 
295  N N   A THR   A 13  ? 0.1330 0.1286 0.1705 -0.0163 0.0079  0.0335  13  THR   A N   
296  N N   B THR   A 13  ? 0.1411 0.1477 0.1616 0.0047  0.0342  0.0292  13  THR   A N   
297  C CA  A THR   A 13  ? 0.1341 0.1314 0.1763 -0.0167 0.0175  0.0237  13  THR   A CA  
298  C CA  B THR   A 13  ? 0.1424 0.1508 0.1663 0.0019  0.0335  0.0265  13  THR   A CA  
299  C C   A THR   A 13  ? 0.1344 0.1211 0.1750 -0.0171 0.0133  0.0285  13  THR   A C   
300  C C   B THR   A 13  ? 0.1455 0.1523 0.1630 0.0034  0.0337  0.0202  13  THR   A C   
301  O O   A THR   A 13  ? 0.1292 0.1291 0.1724 -0.0112 0.0098  0.0260  13  THR   A O   
302  O O   B THR   A 13  ? 0.1499 0.1540 0.1692 0.0050  0.0294  0.0189  13  THR   A O   
303  C CB  A THR   A 13  ? 0.1385 0.1497 0.1857 -0.0172 0.0134  0.0289  13  THR   A CB  
304  C CB  B THR   A 13  ? 0.1384 0.1538 0.1707 0.0025  0.0365  0.0273  13  THR   A CB  
305  O OG1 A THR   A 13  ? 0.1415 0.1468 0.1945 -0.0186 -0.0014 0.0281  13  THR   A OG1 
306  O OG1 B THR   A 13  ? 0.1262 0.1528 0.1744 0.0001  0.0521  0.0307  13  THR   A OG1 
307  C CG2 A THR   A 13  ? 0.1419 0.1714 0.2082 -0.0166 0.0203  0.0200  13  THR   A CG2 
308  C CG2 B THR   A 13  ? 0.1452 0.1621 0.1777 0.0085  0.0323  0.0208  13  THR   A CG2 
323  N N   A ASP   A 14  ? 0.1418 0.1185 0.1908 -0.0210 0.0130  0.0275  14  ASP   A N   
324  N N   B ASP   A 14  ? 0.1528 0.1567 0.1715 0.0034  0.0275  0.0174  14  ASP   A N   
325  C CA  A ASP   A 14  ? 0.1409 0.1298 0.2031 -0.0097 0.0044  0.0432  14  ASP   A CA  
326  C CA  B ASP   A 14  ? 0.1615 0.1663 0.1820 0.0019  0.0186  0.0253  14  ASP   A CA  
327  C C   A ASP   A 14  ? 0.1374 0.1334 0.1912 -0.0131 0.0016  0.0349  14  ASP   A C   
328  C C   B ASP   A 14  ? 0.1502 0.1541 0.1671 0.0016  0.0121  0.0379  14  ASP   A C   
329  O O   A ASP   A 14  ? 0.1505 0.1497 0.1965 -0.0189 -0.0020 0.0429  14  ASP   A O   
330  O O   B ASP   A 14  ? 0.1479 0.1498 0.1683 -0.0028 0.0069  0.0481  14  ASP   A O   
331  C CB  A ASP   A 14  ? 0.1565 0.1528 0.2596 -0.0161 -0.0027 0.0486  14  ASP   A CB  
332  C CB  B ASP   A 14  ? 0.1806 0.1869 0.2135 0.0037  0.0077  0.0184  14  ASP   A CB  
333  C CG  A ASP   A 14  ? 0.1757 0.1926 0.3505 -0.0157 0.0075  0.0476  14  ASP   A CG  
334  C CG  B ASP   A 14  ? 0.1964 0.2124 0.2515 0.0014  0.0028  0.0093  14  ASP   A CG  
335  O OD1 A ASP   A 14  ? 0.1956 0.1943 0.3741 -0.0098 -0.0035 0.0470  14  ASP   A OD1 
336  O OD1 B ASP   A 14  ? 0.2085 0.2209 0.2664 0.0051  -0.0007 0.0045  14  ASP   A OD1 
337  O OD2 A ASP   A 14  ? 0.1989 0.2296 0.3981 -0.0214 -0.0035 0.0318  14  ASP   A OD2 
338  O OD2 B ASP   A 14  ? 0.2014 0.2244 0.2668 -0.0044 -0.0065 0.0033  14  ASP   A OD2 
347  N N   A ASN   A 15  ? 0.1330 0.1216 0.1870 -0.0149 0.0091  0.0411  15  ASN   A N   
348  N N   B ASN   A 15  ? 0.1423 0.1443 0.1590 0.0039  0.0157  0.0399  15  ASN   A N   
349  C CA  A ASN   A 15  ? 0.1311 0.1281 0.1923 -0.0136 0.0022  0.0279  15  ASN   A CA  
350  C CA  B ASN   A 15  ? 0.1370 0.1399 0.1585 0.0077  0.0102  0.0315  15  ASN   A CA  
351  C C   A ASN   A 15  ? 0.1276 0.1226 0.2165 -0.0120 0.0073  0.0295  15  ASN   A C   
352  C C   B ASN   A 15  ? 0.1364 0.1352 0.1739 0.0016  0.0130  0.0273  15  ASN   A C   
353  O O   A ASN   A 15  ? 0.1330 0.1239 0.2696 -0.0057 -0.0172 0.0300  15  ASN   A O   
354  O O   B ASN   A 15  ? 0.1450 0.1413 0.2055 -0.0066 0.0059  0.0155  15  ASN   A O   
355  C CB  A ASN   A 15  ? 0.1329 0.1303 0.1882 -0.0094 0.0151  0.0274  15  ASN   A CB  
356  C CB  B ASN   A 15  ? 0.1406 0.1435 0.1562 0.0072  0.0066  0.0309  15  ASN   A CB  
357  C CG  A ASN   A 15  ? 0.1395 0.1416 0.1911 -0.0063 0.0184  0.0164  15  ASN   A CG  
358  C CG  B ASN   A 15  ? 0.1424 0.1495 0.1569 0.0057  0.0101  0.0270  15  ASN   A CG  
359  O OD1 A ASN   A 15  ? 0.1449 0.1459 0.1975 -0.0163 0.0167  0.0083  15  ASN   A OD1 
360  O OD1 B ASN   A 15  ? 0.1397 0.1479 0.1656 0.0070  0.0174  0.0271  15  ASN   A OD1 
361  N ND2 A ASN   A 15  ? 0.1413 0.1574 0.1844 -0.0135 0.0146  0.0252  15  ASN   A ND2 
362  N ND2 B ASN   A 15  ? 0.1434 0.1559 0.1496 -0.0002 0.0043  0.0305  15  ASN   A ND2 
375  N N   A VAL   A 16  ? 0.1324 0.1250 0.2024 -0.0133 0.0061  0.0343  16  VAL   A N   
376  N N   B VAL   A 16  ? 0.1311 0.1313 0.1627 0.0024  0.0189  0.0345  16  VAL   A N   
377  C CA  A VAL   A 16  ? 0.1317 0.1342 0.1920 -0.0087 0.0082  0.0381  16  VAL   A CA  
378  C CA  B VAL   A 16  ? 0.1361 0.1345 0.1601 0.0020  0.0225  0.0364  16  VAL   A CA  
379  C C   A VAL   A 16  ? 0.1295 0.1284 0.1906 -0.0159 0.0040  0.0345  16  VAL   A C   
380  C C   B VAL   A 16  ? 0.1341 0.1311 0.1621 0.0003  0.0243  0.0362  16  VAL   A C   
381  O O   A VAL   A 16  ? 0.1210 0.1265 0.1990 -0.0087 0.0158  0.0272  16  VAL   A O   
382  O O   B VAL   A 16  ? 0.1300 0.1273 0.1632 0.0060  0.0263  0.0450  16  VAL   A O   
383  C CB  A VAL   A 16  ? 0.1362 0.1591 0.1859 0.0062  0.0237  0.0522  16  VAL   A CB  
384  C CB  B VAL   A 16  ? 0.1443 0.1474 0.1626 0.0065  0.0315  0.0339  16  VAL   A CB  
385  C CG1 A VAL   A 16  ? 0.1502 0.1754 0.1869 0.0103  0.0210  0.0549  16  VAL   A CG1 
386  C CG1 B VAL   A 16  ? 0.1432 0.1525 0.1664 0.0070  0.0306  0.0316  16  VAL   A CG1 
387  C CG2 A VAL   A 16  ? 0.1416 0.1758 0.2110 0.0085  0.0348  0.0456  16  VAL   A CG2 
388  C CG2 B VAL   A 16  ? 0.1479 0.1536 0.1690 0.0072  0.0350  0.0364  16  VAL   A CG2 
407  N N   A TYR   A 17  ? 0.1310 0.1309 0.1909 -0.0106 0.0149  0.0329  17  TYR   A N   
408  N N   B TYR   A 17  ? 0.1394 0.1289 0.1674 -0.0066 0.0299  0.0303  17  TYR   A N   
409  C CA  A TYR   A 17  ? 0.1280 0.1336 0.1831 -0.0111 0.0149  0.0422  17  TYR   A CA  
410  C CA  B TYR   A 17  ? 0.1399 0.1275 0.1623 -0.0118 0.0312  0.0263  17  TYR   A CA  
411  C C   A TYR   A 17  ? 0.1337 0.1280 0.1982 -0.0082 0.0182  0.0382  17  TYR   A C   
412  C C   B TYR   A 17  ? 0.1361 0.1293 0.1638 -0.0166 0.0364  0.0307  17  TYR   A C   
413  O O   A TYR   A 17  ? 0.1351 0.1183 0.1978 -0.0093 0.0290  0.0298  17  TYR   A O   
414  O O   B TYR   A 17  ? 0.1351 0.1279 0.1639 -0.0247 0.0393  0.0307  17  TYR   A O   
415  C CB  A TYR   A 17  ? 0.1367 0.1375 0.1796 -0.0043 0.0151  0.0316  17  TYR   A CB  
416  C CB  B TYR   A 17  ? 0.1508 0.1217 0.1577 -0.0181 0.0266  0.0228  17  TYR   A CB  
417  C CG  A TYR   A 17  ? 0.1499 0.1509 0.1872 -0.0035 0.0115  0.0286  17  TYR   A CG  
418  C CG  B TYR   A 17  ? 0.1602 0.1256 0.1579 -0.0140 0.0174  0.0164  17  TYR   A CG  
419  C CD1 A TYR   A 17  ? 0.1571 0.1596 0.1912 0.0075  0.0047  0.0319  17  TYR   A CD1 
420  C CD1 B TYR   A 17  ? 0.1639 0.1313 0.1622 -0.0131 0.0146  0.0159  17  TYR   A CD1 
421  C CD2 A TYR   A 17  ? 0.1562 0.1523 0.1816 -0.0099 0.0108  0.0321  17  TYR   A CD2 
422  C CD2 B TYR   A 17  ? 0.1636 0.1273 0.1522 -0.0188 0.0129  0.0155  17  TYR   A CD2 
423  C CE1 A TYR   A 17  ? 0.1628 0.1582 0.1974 0.0010  0.0019  0.0298  17  TYR   A CE1 
424  C CE1 B TYR   A 17  ? 0.1653 0.1323 0.1608 -0.0157 0.0075  0.0171  17  TYR   A CE1 
425  C CE2 A TYR   A 17  ? 0.1688 0.1527 0.1842 -0.0098 0.0064  0.0244  17  TYR   A CE2 
426  C CE2 B TYR   A 17  ? 0.1629 0.1256 0.1458 -0.0217 0.0055  0.0123  17  TYR   A CE2 
427  C CZ  A TYR   A 17  ? 0.1705 0.1458 0.1860 -0.0112 -0.0041 0.0311  17  TYR   A CZ  
428  C CZ  B TYR   A 17  ? 0.1634 0.1240 0.1580 -0.0209 0.0042  0.0107  17  TYR   A CZ  
429  O OH  A TYR   A 17  ? 0.1813 0.1471 0.1917 -0.0019 0.0013  0.0325  17  TYR   A OH  
430  O OH  B TYR   A 17  ? 0.1659 0.1185 0.1652 -0.0182 -0.0006 0.0053  17  TYR   A OH  
449  N N   A ILE   A 18  ? 0.1318 0.1364 0.2030 -0.0140 0.0145  0.0496  18  ILE   A N   
450  N N   B ILE   A 18  ? 0.1309 0.1310 0.1555 -0.0129 0.0342  0.0407  18  ILE   A N   
451  C CA  A ILE   A 18  ? 0.1355 0.1396 0.2036 -0.0111 0.0153  0.0551  18  ILE   A CA  
452  C CA  B ILE   A 18  ? 0.1308 0.1359 0.1675 -0.0121 0.0341  0.0354  18  ILE   A CA  
453  C C   A ILE   A 18  ? 0.1312 0.1464 0.2193 -0.0225 0.0202  0.0484  18  ILE   A C   
454  C C   B ILE   A 18  ? 0.1363 0.1434 0.1840 -0.0145 0.0338  0.0274  18  ILE   A C   
455  O O   A ILE   A 18  ? 0.1290 0.1592 0.2121 -0.0238 0.0208  0.0522  18  ILE   A O   
456  O O   B ILE   A 18  ? 0.1265 0.1474 0.2001 -0.0225 0.0363  0.0256  18  ILE   A O   
457  C CB  A ILE   A 18  ? 0.1350 0.1442 0.1951 -0.0030 0.0099  0.0711  18  ILE   A CB  
458  C CB  B ILE   A 18  ? 0.1287 0.1403 0.1679 -0.0112 0.0324  0.0338  18  ILE   A CB  
459  C CG1 A ILE   A 18  ? 0.1397 0.1502 0.2012 0.0082  0.0092  0.0759  18  ILE   A CG1 
460  C CG1 B ILE   A 18  ? 0.1287 0.1480 0.1719 -0.0138 0.0239  0.0364  18  ILE   A CG1 
461  C CG2 A ILE   A 18  ? 0.1448 0.1559 0.2138 -0.0068 0.0034  0.0653  18  ILE   A CG2 
462  C CG2 B ILE   A 18  ? 0.1380 0.1452 0.1765 -0.0203 0.0296  0.0301  18  ILE   A CG2 
463  C CD1 A ILE   A 18  ? 0.1569 0.1610 0.2311 0.0146  -0.0017 0.0791  18  ILE   A CD1 
464  C CD1 B ILE   A 18  ? 0.1332 0.1590 0.1831 -0.0042 0.0218  0.0252  18  ILE   A CD1 
487  N N   A LYS   A 19  ? 0.1368 0.1453 0.2423 -0.0146 0.0477  0.0448  19  LYS   A N   
488  N N   B LYS   A 19  ? 0.1458 0.1504 0.1734 -0.0011 0.0314  0.0224  19  LYS   A N   
489  C CA  A LYS   A 19  ? 0.1469 0.1561 0.2645 -0.0153 0.0609  0.0485  19  LYS   A CA  
490  C CA  B LYS   A 19  ? 0.1564 0.1618 0.1728 0.0086  0.0238  0.0190  19  LYS   A CA  
491  C C   A LYS   A 19  ? 0.1376 0.1454 0.2770 -0.0101 0.0537  0.0449  19  LYS   A C   
492  C C   B LYS   A 19  ? 0.1507 0.1554 0.1585 0.0164  0.0153  0.0165  19  LYS   A C   
493  O O   A LYS   A 19  ? 0.1325 0.1420 0.2686 -0.0106 0.0393  0.0430  19  LYS   A O   
494  O O   B LYS   A 19  ? 0.1538 0.1537 0.1609 0.0140  0.0120  0.0139  19  LYS   A O   
495  C CB  A LYS   A 19  ? 0.1620 0.1751 0.2741 -0.0185 0.0824  0.0455  19  LYS   A CB  
496  C CB  B LYS   A 19  ? 0.1723 0.1766 0.1869 0.0093  0.0264  0.0120  19  LYS   A CB  
497  C CG  A LYS   A 19  ? 0.2025 0.2054 0.2795 -0.0167 0.0930  0.0334  19  LYS   A CG  
498  C CG  B LYS   A 19  ? 0.1904 0.1878 0.2057 0.0099  0.0251  0.0063  19  LYS   A CG  
499  C CD  A LYS   A 19  ? 0.2350 0.2251 0.2700 -0.0242 0.1010  0.0324  19  LYS   A CD  
500  C CD  B LYS   A 19  ? 0.2075 0.1971 0.2203 0.0089  0.0201  0.0039  19  LYS   A CD  
501  C CE  A LYS   A 19  ? 0.2637 0.2419 0.2787 -0.0276 0.0914  0.0206  19  LYS   A CE  
502  C CE  B LYS   A 19  ? 0.2190 0.2067 0.2354 0.0074  0.0178  0.0018  19  LYS   A CE  
503  N NZ  A LYS   A 19  ? 0.2814 0.2481 0.2717 -0.0412 0.0940  0.0108  19  LYS   A NZ  
504  N NZ  B LYS   A 19  ? 0.2282 0.2108 0.2411 0.0009  0.0197  -0.0029 19  LYS   A NZ  
531  N N   A ASN   A 20  ? 0.1424 0.1494 0.3017 -0.0125 0.0618  0.0457  20  ASN   A N   
532  N N   B ASN   A 20  ? 0.1513 0.1556 0.1551 0.0215  0.0104  0.0168  20  ASN   A N   
533  C CA  A ASN   A 20  ? 0.1563 0.1673 0.3207 0.0042  0.0757  0.0406  20  ASN   A CA  
534  C CA  B ASN   A 20  ? 0.1558 0.1595 0.1462 0.0212  0.0092  0.0159  20  ASN   A CA  
535  C C   A ASN   A 20  ? 0.1776 0.1750 0.3224 -0.0046 0.0852  0.0274  20  ASN   A C   
536  C C   B ASN   A 20  ? 0.1607 0.1648 0.1279 0.0189  0.0104  0.0185  20  ASN   A C   
537  O O   A ASN   A 20  ? 0.2036 0.1952 0.3242 -0.0208 0.0787  0.0242  20  ASN   A O   
538  O O   B ASN   A 20  ? 0.1672 0.1732 0.1152 0.0131  0.0121  0.0256  20  ASN   A O   
539  C CB  A ASN   A 20  ? 0.1628 0.1822 0.3371 0.0139  0.0696  0.0475  20  ASN   A CB  
540  C CB  B ASN   A 20  ? 0.1606 0.1626 0.1589 0.0185  0.0045  0.0135  20  ASN   A CB  
541  C CG  A ASN   A 20  ? 0.1680 0.1893 0.3455 0.0261  0.0651  0.0462  20  ASN   A CG  
542  C CG  B ASN   A 20  ? 0.1676 0.1642 0.1743 0.0132  0.0039  0.0084  20  ASN   A CG  
543  O OD1 A ASN   A 20  ? 0.1873 0.1977 0.3572 0.0370  0.0719  0.0329  20  ASN   A OD1 
544  O OD1 B ASN   A 20  ? 0.1776 0.1709 0.1898 0.0068  0.0001  0.0031  20  ASN   A OD1 
545  N ND2 A ASN   A 20  ? 0.1787 0.1927 0.3556 0.0281  0.0427  0.0560  20  ASN   A ND2 
546  N ND2 B ASN   A 20  ? 0.1664 0.1607 0.1727 0.0165  0.0047  0.0052  20  ASN   A ND2 
559  N N   A ALA   A 21  ? 0.1818 0.1676 0.3198 -0.0111 0.0835  0.0173  21  ALA   A N   
560  N N   B ALA   A 21  ? 0.1686 0.1689 0.1497 0.0127  0.0073  0.0158  21  ALA   A N   
561  C CA  A ALA   A 21  ? 0.1872 0.1675 0.3112 -0.0146 0.0774  0.0149  21  ALA   A CA  
562  C CA  B ALA   A 21  ? 0.1776 0.1753 0.1658 0.0058  0.0056  0.0138  21  ALA   A CA  
563  C C   A ALA   A 21  ? 0.1720 0.1610 0.2929 -0.0180 0.0722  0.0259  21  ALA   A C   
564  C C   B ALA   A 21  ? 0.1754 0.1798 0.1658 0.0107  0.0096  0.0152  21  ALA   A C   
565  O O   A ALA   A 21  ? 0.1640 0.1626 0.2843 -0.0118 0.0564  0.0273  21  ALA   A O   
566  O O   B ALA   A 21  ? 0.1755 0.1825 0.1549 0.0194  0.0105  0.0174  21  ALA   A O   
567  C CB  A ALA   A 21  ? 0.2142 0.1807 0.3129 -0.0212 0.0706  0.0218  21  ALA   A CB  
568  C CB  B ALA   A 21  ? 0.1909 0.1771 0.1804 -0.0017 0.0030  0.0130  21  ALA   A CB  
579  N N   A ASP   A 22  ? 0.1773 0.1604 0.2902 -0.0198 0.0695  0.0242  22  ASP   A N   
580  N N   B ASP   A 22  ? 0.1778 0.1845 0.1758 0.0034  0.0167  0.0134  22  ASP   A N   
581  C CA  A ASP   A 22  ? 0.1875 0.1628 0.2748 -0.0188 0.0518  0.0223  22  ASP   A CA  
582  C CA  B ASP   A 22  ? 0.1804 0.1945 0.1836 -0.0014 0.0187  0.0118  22  ASP   A CA  
583  C C   A ASP   A 22  ? 0.1785 0.1697 0.2246 -0.0192 0.0519  0.0264  22  ASP   A C   
584  C C   B ASP   A 22  ? 0.1767 0.2000 0.1688 -0.0022 0.0182  0.0069  22  ASP   A C   
585  O O   A ASP   A 22  ? 0.1896 0.1930 0.2394 -0.0158 0.0552  0.0284  22  ASP   A O   
586  O O   B ASP   A 22  ? 0.1801 0.2100 0.1748 -0.0011 0.0218  0.0066  22  ASP   A O   
587  C CB  A ASP   A 22  ? 0.2115 0.1649 0.3233 -0.0166 0.0401  0.0090  22  ASP   A CB  
588  C CB  B ASP   A 22  ? 0.1867 0.2009 0.2124 -0.0049 0.0233  0.0112  22  ASP   A CB  
589  C CG  A ASP   A 22  ? 0.2267 0.1699 0.3715 -0.0205 0.0234  0.0109  22  ASP   A CG  
590  C CG  B ASP   A 22  ? 0.1896 0.2086 0.2407 -0.0083 0.0271  0.0126  22  ASP   A CG  
591  O OD1 A ASP   A 22  ? 0.2204 0.1733 0.3795 -0.0356 0.0107  0.0281  22  ASP   A OD1 
592  O OD1 B ASP   A 22  ? 0.1893 0.2124 0.2397 -0.0111 0.0299  0.0182  22  ASP   A OD1 
593  O OD2 A ASP   A 22  ? 0.2474 0.1786 0.4072 -0.0062 0.0228  0.0002  22  ASP   A OD2 
594  O OD2 B ASP   A 22  ? 0.1926 0.2154 0.2650 -0.0118 0.0249  0.0147  22  ASP   A OD2 
603  N N   A ILE   A 23  ? 0.1740 0.1693 0.2036 -0.0151 0.0560  0.0208  23  ILE   A N   
604  N N   B ILE   A 23  ? 0.1750 0.1984 0.1656 -0.0024 0.0182  0.0036  23  ILE   A N   
605  C CA  A ILE   A 23  ? 0.1697 0.1594 0.1968 -0.0178 0.0463  0.0203  23  ILE   A CA  
606  C CA  B ILE   A 23  ? 0.1766 0.1992 0.1740 -0.0066 0.0100  0.0050  23  ILE   A CA  
607  C C   A ILE   A 23  ? 0.1651 0.1725 0.1816 -0.0191 0.0597  0.0115  23  ILE   A C   
608  C C   B ILE   A 23  ? 0.1845 0.2044 0.1730 -0.0117 0.0161  -0.0003 23  ILE   A C   
609  O O   A ILE   A 23  ? 0.1744 0.1841 0.1879 -0.0106 0.0517  0.0102  23  ILE   A O   
610  O O   B ILE   A 23  ? 0.1868 0.2070 0.1738 -0.0073 0.0139  -0.0016 23  ILE   A O   
611  C CB  A ILE   A 23  ? 0.1749 0.1551 0.1710 -0.0115 0.0430  0.0216  23  ILE   A CB  
612  C CB  B ILE   A 23  ? 0.1754 0.1975 0.1690 -0.0040 0.0012  0.0056  23  ILE   A CB  
613  C CG1 A ILE   A 23  ? 0.1852 0.1620 0.1639 -0.0004 0.0323  0.0103  23  ILE   A CG1 
614  C CG1 B ILE   A 23  ? 0.1745 0.1998 0.1622 -0.0005 -0.0085 0.0058  23  ILE   A CG1 
615  C CG2 A ILE   A 23  ? 0.1707 0.1541 0.1712 -0.0134 0.0388  0.0226  23  ILE   A CG2 
616  C CG2 B ILE   A 23  ? 0.1739 0.1949 0.1744 -0.0050 -0.0008 0.0013  23  ILE   A CG2 
617  C CD1 A ILE   A 23  ? 0.1899 0.1616 0.1679 -0.0009 0.0162  0.0009  23  ILE   A CD1 
618  C CD1 B ILE   A 23  ? 0.1724 0.1995 0.1598 -0.0015 -0.0178 0.0041  23  ILE   A CD1 
641  N N   A VAL   A 24  ? 0.1774 0.1758 0.1887 -0.0321 0.0533  0.0041  24  VAL   A N   
642  N N   B VAL   A 24  ? 0.1968 0.2067 0.1804 -0.0219 0.0141  -0.0004 24  VAL   A N   
643  C CA  A VAL   A 24  ? 0.2032 0.1929 0.2085 -0.0370 0.0492  -0.0084 24  VAL   A CA  
644  C CA  B VAL   A 24  ? 0.2122 0.2089 0.1861 -0.0274 0.0161  -0.0009 24  VAL   A CA  
645  C C   A VAL   A 24  ? 0.2161 0.2175 0.2141 -0.0365 0.0500  -0.0149 24  VAL   A C   
646  C C   B VAL   A 24  ? 0.2233 0.2171 0.1994 -0.0199 0.0142  -0.0005 24  VAL   A C   
647  O O   A VAL   A 24  ? 0.2309 0.2166 0.2085 -0.0296 0.0491  -0.0195 24  VAL   A O   
648  O O   B VAL   A 24  ? 0.2284 0.2155 0.2068 -0.0161 0.0124  -0.0027 24  VAL   A O   
649  C CB  A VAL   A 24  ? 0.2138 0.1981 0.2300 -0.0364 0.0534  -0.0097 24  VAL   A CB  
650  C CB  B VAL   A 24  ? 0.2171 0.2069 0.1845 -0.0380 0.0173  0.0004  24  VAL   A CB  
651  C CG1 A VAL   A 24  ? 0.2254 0.2050 0.2405 -0.0321 0.0596  -0.0115 24  VAL   A CG1 
652  C CG1 B VAL   A 24  ? 0.2246 0.2091 0.1889 -0.0395 0.0179  0.0030  24  VAL   A CG1 
653  C CG2 A VAL   A 24  ? 0.2210 0.2103 0.2410 -0.0322 0.0563  -0.0016 24  VAL   A CG2 
654  C CG2 B VAL   A 24  ? 0.2156 0.2038 0.1772 -0.0460 0.0184  -0.0040 24  VAL   A CG2 
673  N N   A GLU   A 25  ? 0.2239 0.2529 0.2235 -0.0317 0.0707  -0.0219 25  GLU   A N   
674  N N   B GLU   A 25  ? 0.2323 0.2323 0.2086 -0.0128 0.0176  -0.0019 25  GLU   A N   
675  C CA  A GLU   A 25  ? 0.2437 0.2869 0.2388 -0.0209 0.0910  -0.0215 25  GLU   A CA  
676  C CA  B GLU   A 25  ? 0.2454 0.2493 0.2242 -0.0053 0.0179  -0.0037 25  GLU   A CA  
677  C C   A GLU   A 25  ? 0.2374 0.2889 0.2126 -0.0312 0.1007  -0.0167 25  GLU   A C   
678  C C   B GLU   A 25  ? 0.2409 0.2502 0.2072 -0.0096 0.0213  -0.0066 25  GLU   A C   
679  O O   A GLU   A 25  ? 0.2453 0.2964 0.2104 -0.0319 0.1008  -0.0138 25  GLU   A O   
680  O O   B GLU   A 25  ? 0.2428 0.2512 0.2082 -0.0076 0.0221  -0.0074 25  GLU   A O   
681  C CB  A GLU   A 25  ? 0.2694 0.3158 0.2917 -0.0101 0.0988  -0.0141 25  GLU   A CB  
682  C CB  B GLU   A 25  ? 0.2624 0.2664 0.2655 0.0010  0.0141  -0.0032 25  GLU   A CB  
683  C CG  A GLU   A 25  ? 0.2963 0.3405 0.3569 -0.0060 0.0892  -0.0052 25  GLU   A CG  
684  C CG  B GLU   A 25  ? 0.2781 0.2811 0.3070 0.0041  0.0070  -0.0044 25  GLU   A CG  
685  C CD  A GLU   A 25  ? 0.3187 0.3651 0.4157 0.0005  0.0812  -0.0028 25  GLU   A CD  
686  C CD  B GLU   A 25  ? 0.2922 0.2943 0.3435 0.0080  0.0019  -0.0047 25  GLU   A CD  
687  O OE1 A GLU   A 25  ? 0.3282 0.3763 0.4353 0.0030  0.0750  -0.0053 25  GLU   A OE1 
688  O OE1 B GLU   A 25  ? 0.2996 0.3019 0.3572 0.0093  -0.0029 -0.0077 25  GLU   A OE1 
689  O OE2 A GLU   A 25  ? 0.3227 0.3718 0.4447 0.0034  0.0800  -0.0068 25  GLU   A OE2 
690  O OE2 B GLU   A 25  ? 0.2941 0.2985 0.3574 0.0098  0.0024  -0.0050 25  GLU   A OE2 
703  N N   A GLU   A 26  ? 0.2236 0.2771 0.2134 -0.0447 0.1079  -0.0211 26  GLU   A N   
704  N N   B GLU   A 26  ? 0.2341 0.2494 0.1975 -0.0176 0.0223  -0.0119 26  GLU   A N   
705  C CA  A GLU   A 26  ? 0.2315 0.2664 0.2019 -0.0574 0.0989  -0.0099 26  GLU   A CA  
706  C CA  B GLU   A 26  ? 0.2327 0.2512 0.1907 -0.0271 0.0210  -0.0163 26  GLU   A CA  
707  C C   A GLU   A 26  ? 0.2217 0.2457 0.1725 -0.0585 0.0810  -0.0115 26  GLU   A C   
708  C C   B GLU   A 26  ? 0.2232 0.2417 0.1674 -0.0399 0.0372  -0.0172 26  GLU   A C   
709  O O   A GLU   A 26  ? 0.2253 0.2382 0.1776 -0.0686 0.0730  -0.0061 26  GLU   A O   
710  O O   B GLU   A 26  ? 0.2269 0.2420 0.1589 -0.0420 0.0344  -0.0201 26  GLU   A O   
711  C CB  A GLU   A 26  ? 0.2549 0.2623 0.2412 -0.0755 0.0884  -0.0014 26  GLU   A CB  
712  C CB  B GLU   A 26  ? 0.2428 0.2609 0.2178 -0.0242 0.0076  -0.0195 26  GLU   A CB  
713  C CG  A GLU   A 26  ? 0.2829 0.2590 0.2913 -0.0868 0.0895  -0.0124 26  GLU   A CG  
714  C CG  B GLU   A 26  ? 0.2577 0.2736 0.2603 -0.0198 0.0008  -0.0217 26  GLU   A CG  
715  C CD  A GLU   A 26  ? 0.2986 0.2494 0.3130 -0.1035 0.1103  -0.0180 26  GLU   A CD  
716  C CD  B GLU   A 26  ? 0.2699 0.2824 0.2924 -0.0168 -0.0010 -0.0238 26  GLU   A CD  
717  O OE1 A GLU   A 26  ? 0.2939 0.2648 0.3073 -0.0937 0.1366  -0.0642 26  GLU   A OE1 
718  O OE1 B GLU   A 26  ? 0.2779 0.2856 0.3047 -0.0161 -0.0006 -0.0305 26  GLU   A OE1 
719  O OE2 A GLU   A 26  ? 0.3206 0.2493 0.3204 -0.0957 0.1056  -0.0077 26  GLU   A OE2 
720  O OE2 B GLU   A 26  ? 0.2739 0.2904 0.3078 -0.0104 -0.0037 -0.0214 26  GLU   A OE2 
733  N N   . ALA   A 27  ? 0.2075 0.2281 0.1562 -0.0541 0.0552  -0.0155 27  ALA   A N   
734  C CA  . ALA   A 27  ? 0.2113 0.2269 0.1490 -0.0502 0.0446  -0.0209 27  ALA   A CA  
735  C C   . ALA   A 27  ? 0.2422 0.2465 0.1611 -0.0532 0.0428  -0.0375 27  ALA   A C   
736  O O   . ALA   A 27  ? 0.2418 0.2425 0.1605 -0.0607 0.0364  -0.0230 27  ALA   A O   
737  C CB  . ALA   A 27  ? 0.1957 0.2162 0.1582 -0.0469 0.0402  -0.0107 27  ALA   A CB  
744  N N   . LYS   A 28  ? 0.2848 0.2761 0.1862 -0.0433 0.0427  -0.0676 28  LYS   A N   
745  C CA  . LYS   A 28  ? 0.3326 0.3239 0.2337 -0.0337 0.0461  -0.0803 28  LYS   A CA  
746  C C   . LYS   A 28  ? 0.3514 0.3676 0.2280 -0.0366 0.0678  -0.0536 28  LYS   A C   
747  O O   . LYS   A 28  ? 0.3588 0.3768 0.2589 -0.0352 0.0480  -0.0479 28  LYS   A O   
748  C CB  . LYS   A 28  ? 0.3610 0.3373 0.2880 -0.0174 0.0351  -0.1024 28  LYS   A CB  
749  C CG  . LYS   A 28  ? 0.3822 0.3519 0.3474 -0.0061 0.0270  -0.1084 28  LYS   A CG  
750  C CD  . LYS   A 28  ? 0.3974 0.3711 0.4242 0.0002  0.0170  -0.1013 28  LYS   A CD  
751  C CE  . LYS   A 28  ? 0.4144 0.3860 0.4806 0.0031  0.0075  -0.0983 28  LYS   A CE  
752  N NZ  . LYS   A 28  ? 0.4296 0.3948 0.5153 0.0063  0.0047  -0.0951 28  LYS   A NZ  
766  N N   A LYS   A 29  ? 0.3553 0.3898 0.2015 -0.0418 0.0993  -0.0336 29  LYS   A N   
767  N N   B LYS   A 29  ? 0.3575 0.3826 0.2445 -0.0390 0.0726  -0.0359 29  LYS   A N   
768  C CA  A LYS   A 29  ? 0.3660 0.4141 0.2241 -0.0460 0.1131  -0.0181 29  LYS   A CA  
769  C CA  B LYS   A 29  ? 0.3647 0.3966 0.2706 -0.0417 0.0745  -0.0205 29  LYS   A CA  
770  C C   A LYS   A 29  ? 0.3609 0.4048 0.2121 -0.0549 0.0978  -0.0085 29  LYS   A C   
771  C C   B LYS   A 29  ? 0.3579 0.3936 0.2403 -0.0528 0.0788  -0.0103 29  LYS   A C   
772  O O   A LYS   A 29  ? 0.3682 0.4118 0.2266 -0.0492 0.0915  -0.0069 29  LYS   A O   
773  O O   B LYS   A 29  ? 0.3607 0.3964 0.2495 -0.0502 0.0764  -0.0088 29  LYS   A O   
774  C CB  A LYS   A 29  ? 0.3794 0.4447 0.2820 -0.0400 0.1321  -0.0112 29  LYS   A CB  
775  C CB  B LYS   A 29  ? 0.3764 0.4112 0.3257 -0.0341 0.0709  -0.0152 29  LYS   A CB  
776  C CG  A LYS   A 29  ? 0.3934 0.4698 0.3516 -0.0347 0.1412  -0.0103 29  LYS   A CG  
777  C CG  B LYS   A 29  ? 0.3869 0.4229 0.3768 -0.0278 0.0668  -0.0118 29  LYS   A CG  
778  C CD  A LYS   A 29  ? 0.4064 0.4905 0.4198 -0.0298 0.1440  -0.0135 29  LYS   A CD  
779  C CD  B LYS   A 29  ? 0.3958 0.4327 0.4205 -0.0229 0.0629  -0.0098 29  LYS   A CD  
780  C CE  A LYS   A 29  ? 0.4151 0.5044 0.4666 -0.0262 0.1464  -0.0162 29  LYS   A CE  
781  C CE  B LYS   A 29  ? 0.4018 0.4394 0.4502 -0.0195 0.0606  -0.0086 29  LYS   A CE  
782  N NZ  A LYS   A 29  ? 0.4192 0.5118 0.4945 -0.0245 0.1473  -0.0188 29  LYS   A NZ  
783  N NZ  B LYS   A 29  ? 0.4046 0.4427 0.4664 -0.0178 0.0593  -0.0080 29  LYS   A NZ  
810  N N   . VAL   A 30  ? 0.3460 0.3855 0.2026 -0.0663 0.0854  -0.0025 30  VAL   A N   
811  C CA  . VAL   A 30  ? 0.3295 0.3600 0.1750 -0.0867 0.0583  0.0230  30  VAL   A CA  
812  C C   . VAL   A 30  ? 0.3280 0.3399 0.1291 -0.0902 0.0429  0.0299  30  VAL   A C   
813  O O   . VAL   A 30  ? 0.3346 0.3407 0.1281 -0.0837 0.0337  0.0352  30  VAL   A O   
814  C CB  . VAL   A 30  ? 0.3194 0.3528 0.2157 -0.1004 0.0341  0.0322  30  VAL   A CB  
815  C CG1 . VAL   A 30  ? 0.3235 0.3541 0.2373 -0.1025 0.0190  0.0346  30  VAL   A CG1 
816  C CG2 . VAL   A 30  ? 0.3143 0.3516 0.2440 -0.1042 0.0358  0.0350  30  VAL   A CG2 
827  N N   . LYS   A 31  ? 0.3175 0.3156 0.1111 -0.0996 0.0206  0.0155  31  LYS   A N   
828  C CA  . LYS   A 31  ? 0.3291 0.3084 0.1378 -0.0902 -0.0039 0.0064  31  LYS   A CA  
829  C C   . LYS   A 31  ? 0.3065 0.2805 0.1144 -0.0757 0.0011  0.0404  31  LYS   A C   
830  O O   . LYS   A 31  ? 0.3126 0.2927 0.1304 -0.0711 -0.0153 0.0542  31  LYS   A O   
831  C CB  . LYS   A 31  ? 0.3718 0.3363 0.2429 -0.0848 -0.0264 -0.0196 31  LYS   A CB  
832  C CG  . LYS   A 31  ? 0.4175 0.3670 0.3780 -0.0722 -0.0437 -0.0315 31  LYS   A CG  
833  C CD  . LYS   A 31  ? 0.4529 0.3909 0.4810 -0.0627 -0.0601 -0.0411 31  LYS   A CD  
834  C CE  . LYS   A 31  ? 0.4754 0.4116 0.5446 -0.0564 -0.0739 -0.0494 31  LYS   A CE  
835  N NZ  . LYS   A 31  ? 0.4870 0.4222 0.5764 -0.0542 -0.0803 -0.0541 31  LYS   A NZ  
849  N N   . PRO   A 32  ? 0.2741 0.2469 0.1046 -0.0727 0.0089  0.0286  32  PRO   A N   
850  C CA  . PRO   A 32  ? 0.2654 0.2317 0.1357 -0.0660 -0.0063 0.0340  32  PRO   A CA  
851  C C   . PRO   A 32  ? 0.2629 0.2226 0.1412 -0.0527 -0.0187 0.0435  32  PRO   A C   
852  O O   . PRO   A 32  ? 0.2541 0.2138 0.1526 -0.0541 -0.0364 0.0452  32  PRO   A O   
853  C CB  . PRO   A 32  ? 0.2562 0.2380 0.1510 -0.0699 -0.0050 0.0253  32  PRO   A CB  
854  C CG  . PRO   A 32  ? 0.2501 0.2413 0.1083 -0.0621 -0.0039 0.0176  32  PRO   A CG  
855  C CD  . PRO   A 32  ? 0.2565 0.2433 0.0975 -0.0629 0.0045  0.0216  32  PRO   A CD  
863  N N   . THR   A 33  ? 0.2703 0.2192 0.1365 -0.0474 -0.0195 0.0456  33  THR   A N   
864  C CA  . THR   A 33  ? 0.2677 0.2204 0.1422 -0.0347 -0.0314 0.0451  33  THR   A CA  
865  C C   . THR   A 33  ? 0.2354 0.2022 0.1350 -0.0377 -0.0306 0.0309  33  THR   A C   
866  O O   . THR   A 33  ? 0.2338 0.2049 0.1415 -0.0366 -0.0399 0.0362  33  THR   A O   
867  C CB  . THR   A 33  ? 0.2943 0.2391 0.1524 -0.0229 -0.0407 0.0646  33  THR   A CB  
868  O OG1 . THR   A 33  ? 0.3160 0.2543 0.1847 -0.0139 -0.0303 0.0738  33  THR   A OG1 
869  C CG2 . THR   A 33  ? 0.2990 0.2498 0.1817 -0.0129 -0.0472 0.0634  33  THR   A CG2 
877  N N   . VAL   A 34  ? 0.2053 0.1844 0.1236 -0.0349 -0.0234 0.0355  34  VAL   A N   
878  C CA  . VAL   A 34  ? 0.1833 0.1663 0.1166 -0.0262 -0.0089 0.0287  34  VAL   A CA  
879  C C   . VAL   A 34  ? 0.1709 0.1574 0.1083 -0.0239 0.0001  0.0162  34  VAL   A C   
880  O O   . VAL   A 34  ? 0.1732 0.1623 0.1305 -0.0311 0.0014  0.0271  34  VAL   A O   
881  C CB  . VAL   A 34  ? 0.1890 0.1636 0.1408 -0.0263 -0.0074 0.0186  34  VAL   A CB  
882  C CG1 . VAL   A 34  ? 0.1915 0.1664 0.1354 -0.0228 0.0005  0.0085  34  VAL   A CG1 
883  C CG2 . VAL   A 34  ? 0.1956 0.1796 0.1715 -0.0168 -0.0206 0.0185  34  VAL   A CG2 
893  N N   . VAL   A 35  ? 0.1553 0.1479 0.1100 -0.0287 -0.0049 0.0219  35  VAL   A N   
894  C CA  . VAL   A 35  ? 0.1459 0.1497 0.1085 -0.0246 -0.0050 0.0172  35  VAL   A CA  
895  C C   . VAL   A 35  ? 0.1347 0.1389 0.1046 -0.0197 0.0028  0.0174  35  VAL   A C   
896  O O   . VAL   A 35  ? 0.1346 0.1488 0.1222 -0.0208 0.0101  0.0081  35  VAL   A O   
897  C CB  . VAL   A 35  ? 0.1539 0.1540 0.1224 -0.0101 0.0117  0.0050  35  VAL   A CB  
898  C CG1 . VAL   A 35  ? 0.1599 0.1558 0.1313 -0.0082 0.0002  -0.0022 35  VAL   A CG1 
899  C CG2 . VAL   A 35  ? 0.1516 0.1549 0.1511 -0.0115 0.0174  0.0004  35  VAL   A CG2 
909  N N   . VAL   A 36  ? 0.1268 0.1388 0.1050 -0.0134 0.0072  0.0175  36  VAL   A N   
910  C CA  . VAL   A 36  ? 0.1212 0.1231 0.1030 -0.0078 0.0073  0.0102  36  VAL   A CA  
911  C C   . VAL   A 36  ? 0.1202 0.1187 0.1127 -0.0047 0.0093  0.0150  36  VAL   A C   
912  O O   . VAL   A 36  ? 0.1266 0.1238 0.1339 -0.0009 0.0169  0.0141  36  VAL   A O   
913  C CB  . VAL   A 36  ? 0.1231 0.1168 0.1154 -0.0079 0.0068  0.0154  36  VAL   A CB  
914  C CG1 . VAL   A 36  ? 0.1290 0.1208 0.1329 -0.0121 0.0053  0.0033  36  VAL   A CG1 
915  C CG2 . VAL   A 36  ? 0.1355 0.1179 0.1319 -0.0056 -0.0010 0.0169  36  VAL   A CG2 
925  N N   . ASN   A 37  ? 0.1162 0.1161 0.1153 -0.0015 0.0084  0.0156  37  ASN   A N   
926  C CA  . ASN   A 37  ? 0.1183 0.1109 0.1089 0.0047  0.0101  0.0155  37  ASN   A CA  
927  C C   . ASN   A 37  ? 0.1206 0.1119 0.1107 0.0006  0.0170  0.0214  37  ASN   A C   
928  O O   . ASN   A 37  ? 0.1339 0.1234 0.1173 0.0105  0.0184  0.0108  37  ASN   A O   
929  C CB  . ASN   A 37  ? 0.1214 0.1176 0.1161 0.0048  0.0058  0.0108  37  ASN   A CB  
930  C CG  . ASN   A 37  ? 0.1204 0.1137 0.1208 0.0004  0.0082  0.0115  37  ASN   A CG  
931  O OD1 . ASN   A 37  ? 0.1190 0.1184 0.1459 0.0019  0.0038  0.0160  37  ASN   A OD1 
932  N ND2 . ASN   A 37  ? 0.1259 0.1206 0.1359 -0.0022 0.0015  0.0306  37  ASN   A ND2 
939  N N   A ALA   A 38  ? 0.1165 0.1192 0.1161 0.0055  0.0127  0.0070  38  ALA   A N   
940  N N   B ALA   A 38  ? 0.1268 0.1210 0.1190 -0.0044 0.0077  0.0138  38  ALA   A N   
941  C CA  A ALA   A 38  ? 0.1285 0.1187 0.1139 -0.0011 0.0034  0.0010  38  ALA   A CA  
942  C CA  B ALA   A 38  ? 0.1375 0.1274 0.1293 -0.0117 -0.0017 0.0072  38  ALA   A CA  
943  C C   A ALA   A 38  ? 0.1247 0.1180 0.1079 0.0045  -0.0042 -0.0015 38  ALA   A C   
944  C C   B ALA   A 38  ? 0.1327 0.1286 0.1291 -0.0052 -0.0097 0.0165  38  ALA   A C   
945  O O   A ALA   A 38  ? 0.1220 0.1157 0.1286 0.0026  -0.0018 -0.0005 38  ALA   A O   
946  O O   B ALA   A 38  ? 0.1244 0.1298 0.1392 -0.0066 -0.0200 0.0190  38  ALA   A O   
947  C CB  A ALA   A 38  ? 0.1331 0.1347 0.1234 -0.0069 -0.0036 0.0010  38  ALA   A CB  
948  C CB  B ALA   A 38  ? 0.1467 0.1311 0.1395 -0.0180 -0.0046 -0.0108 38  ALA   A CB  
959  N N   A ALA   A 39  ? 0.1211 0.1108 0.1246 0.0048  -0.0024 0.0072  39  ALA   A N   
960  N N   B ALA   A 39  ? 0.1360 0.1280 0.1299 -0.0029 -0.0050 0.0292  39  ALA   A N   
961  C CA  A ALA   A 39  ? 0.1210 0.1082 0.1212 0.0070  0.0006  0.0067  39  ALA   A CA  
962  C CA  B ALA   A 39  ? 0.1411 0.1342 0.1284 0.0012  0.0008  0.0305  39  ALA   A CA  
963  C C   A ALA   A 39  ? 0.1204 0.1103 0.1246 0.0035  -0.0002 -0.0021 39  ALA   A C   
964  C C   B ALA   A 39  ? 0.1348 0.1298 0.1220 0.0008  0.0058  0.0195  39  ALA   A C   
965  O O   A ALA   A 39  ? 0.1278 0.1159 0.1216 0.0052  0.0030  0.0043  39  ALA   A O   
966  O O   B ALA   A 39  ? 0.1280 0.1325 0.1116 -0.0038 0.0092  0.0141  39  ALA   A O   
967  C CB  A ALA   A 39  ? 0.1202 0.1074 0.1333 0.0091  -0.0062 -0.0065 39  ALA   A CB  
968  C CB  B ALA   A 39  ? 0.1521 0.1409 0.1364 0.0072  -0.0035 0.0287  39  ALA   A CB  
979  N N   A ASN   A 40  ? 0.1285 0.1221 0.1297 -0.0093 0.0191  -0.0017 40  ASN   A N   
980  N N   B ASN   A 40  ? 0.1373 0.1264 0.1210 -0.0000 0.0170  0.0190  40  ASN   A N   
981  C CA  A ASN   A 40  ? 0.1408 0.1163 0.1304 0.0003  0.0169  0.0031  40  ASN   A CA  
982  C CA  B ASN   A 40  ? 0.1404 0.1235 0.1260 0.0008  0.0230  0.0130  40  ASN   A CA  
983  C C   A ASN   A 40  ? 0.1453 0.1077 0.1223 -0.0081 0.0287  0.0145  40  ASN   A C   
984  C C   B ASN   A 40  ? 0.1453 0.1179 0.1180 0.0002  0.0291  0.0133  40  ASN   A C   
985  O O   A ASN   A 40  ? 0.1370 0.1127 0.1371 -0.0085 0.0204  0.0194  40  ASN   A O   
986  O O   B ASN   A 40  ? 0.1413 0.1211 0.1146 0.0061  0.0318  0.0130  40  ASN   A O   
987  C CB  A ASN   A 40  ? 0.1561 0.1248 0.1413 0.0081  -0.0068 0.0103  40  ASN   A CB  
988  C CB  B ASN   A 40  ? 0.1418 0.1280 0.1355 -0.0010 0.0232  0.0105  40  ASN   A CB  
989  C CG  A ASN   A 40  ? 0.1636 0.1271 0.1654 0.0060  -0.0193 0.0112  40  ASN   A CG  
990  C CG  B ASN   A 40  ? 0.1387 0.1297 0.1399 -0.0103 0.0361  0.0078  40  ASN   A CG  
991  O OD1 A ASN   A 40  ? 0.1724 0.1279 0.1972 0.0044  -0.0220 0.0059  40  ASN   A OD1 
992  O OD1 B ASN   A 40  ? 0.1347 0.1284 0.1349 -0.0187 0.0533  0.0131  40  ASN   A OD1 
993  N ND2 A ASN   A 40  ? 0.1685 0.1351 0.1904 0.0074  -0.0165 0.0091  40  ASN   A ND2 
994  N ND2 B ASN   A 40  ? 0.1423 0.1358 0.1561 -0.0092 0.0320  0.0019  40  ASN   A ND2 
1007 N N   . VAL   A 41  ? 0.1551 0.1162 0.1232 -0.0029 0.0271  0.0147  41  VAL   A N   
1008 C CA  . VAL   A 41  ? 0.1626 0.1197 0.1407 -0.0032 0.0402  0.0096  41  VAL   A CA  
1009 C C   . VAL   A 41  ? 0.1530 0.1179 0.1425 0.0036  0.0313  0.0098  41  VAL   A C   
1010 O O   . VAL   A 41  ? 0.1582 0.1151 0.1686 0.0042  0.0282  0.0066  41  VAL   A O   
1011 C CB  . VAL   A 41  ? 0.1824 0.1336 0.1472 -0.0162 0.0526  0.0038  41  VAL   A CB  
1012 C CG1 . VAL   A 41  ? 0.1900 0.1397 0.1571 -0.0134 0.0537  -0.0045 41  VAL   A CG1 
1013 C CG2 . VAL   A 41  ? 0.2083 0.1467 0.1418 -0.0253 0.0546  0.0052  41  VAL   A CG2 
1024 N N   . TYR   A 42  ? 0.1433 0.1150 0.1598 -0.0037 0.0322  0.0202  42  TYR   A N   
1025 C CA  . TYR   A 42  ? 0.1385 0.1095 0.1615 -0.0036 0.0353  0.0212  42  TYR   A CA  
1026 C C   . TYR   A 42  ? 0.1303 0.1114 0.1647 -0.0020 0.0250  0.0230  42  TYR   A C   
1027 O O   . TYR   A 42  ? 0.1344 0.1158 0.1739 -0.0140 0.0195  0.0063  42  TYR   A O   
1028 C CB  . TYR   A 42  ? 0.1586 0.1202 0.1618 -0.0023 0.0373  0.0207  42  TYR   A CB  
1029 C CG  . TYR   A 42  ? 0.1790 0.1288 0.1574 -0.0068 0.0295  0.0303  42  TYR   A CG  
1030 C CD1 . TYR   A 42  ? 0.1946 0.1441 0.1597 -0.0131 0.0420  0.0243  42  TYR   A CD1 
1031 C CD2 . TYR   A 42  ? 0.1928 0.1542 0.1689 -0.0088 0.0214  0.0249  42  TYR   A CD2 
1032 C CE1 . TYR   A 42  ? 0.2051 0.1609 0.1658 -0.0165 0.0408  0.0263  42  TYR   A CE1 
1033 C CE2 . TYR   A 42  ? 0.2103 0.1687 0.1789 -0.0217 0.0212  0.0331  42  TYR   A CE2 
1034 C CZ  . TYR   A 42  ? 0.2197 0.1766 0.1704 -0.0235 0.0397  0.0283  42  TYR   A CZ  
1035 O OH  . TYR   A 42  ? 0.2362 0.2025 0.1917 -0.0356 0.0346  0.0133  42  TYR   A OH  
1045 N N   . LEU   A 43  ? 0.1294 0.1138 0.1446 -0.0050 0.0181  0.0065  43  LEU   A N   
1046 C CA  . LEU   A 43  ? 0.1254 0.1145 0.1455 -0.0049 0.0177  0.0067  43  LEU   A CA  
1047 C C   . LEU   A 43  ? 0.1281 0.1173 0.1420 -0.0054 0.0101  0.0067  43  LEU   A C   
1048 O O   . LEU   A 43  ? 0.1443 0.1203 0.1628 0.0019  -0.0027 0.0045  43  LEU   A O   
1049 C CB  . LEU   A 43  ? 0.1308 0.1104 0.1537 -0.0055 0.0181  0.0077  43  LEU   A CB  
1050 C CG  . LEU   A 43  ? 0.1365 0.1144 0.1663 -0.0014 0.0076  0.0062  43  LEU   A CG  
1051 C CD1 . LEU   A 43  ? 0.1471 0.1286 0.1786 -0.0001 -0.0023 0.0172  43  LEU   A CD1 
1052 C CD2 . LEU   A 43  ? 0.1516 0.1142 0.1674 -0.0017 0.0152  0.0095  43  LEU   A CD2 
1064 N N   A LYS   A 44  ? 0.1309 0.1144 0.1394 -0.0003 0.0021  0.0124  44  LYS   A N   
1065 N N   B LYS   A 44  ? 0.1424 0.1309 0.1481 -0.0052 0.0100  0.0050  44  LYS   A N   
1066 C CA  A LYS   A 44  ? 0.1431 0.1104 0.1425 -0.0033 0.0135  0.0175  44  LYS   A CA  
1067 C CA  B LYS   A 44  ? 0.1590 0.1456 0.1607 -0.0070 0.0150  0.0024  44  LYS   A CA  
1068 C C   A LYS   A 44  ? 0.1348 0.1120 0.1383 0.0051  0.0003  0.0111  44  LYS   A C   
1069 C C   B LYS   A 44  ? 0.1536 0.1442 0.1396 -0.0066 0.0138  -0.0019 44  LYS   A C   
1070 O O   A LYS   A 44  ? 0.1423 0.1295 0.1458 0.0036  -0.0019 0.0027  44  LYS   A O   
1071 O O   B LYS   A 44  ? 0.1546 0.1463 0.1344 -0.0096 0.0237  -0.0028 44  LYS   A O   
1072 C CB  A LYS   A 44  ? 0.1710 0.1218 0.1886 0.0001  0.0271  0.0292  44  LYS   A CB  
1073 C CB  B LYS   A 44  ? 0.1803 0.1652 0.2005 -0.0064 0.0211  0.0042  44  LYS   A CB  
1074 C CG  A LYS   A 44  ? 0.2031 0.1591 0.2694 -0.0092 0.0398  0.0345  44  LYS   A CG  
1075 C CG  B LYS   A 44  ? 0.2018 0.1885 0.2479 -0.0058 0.0261  0.0063  44  LYS   A CG  
1076 C CD  A LYS   A 44  ? 0.2419 0.2146 0.3772 -0.0131 0.0282  0.0273  44  LYS   A CD  
1077 C CD  B LYS   A 44  ? 0.2232 0.2134 0.3021 -0.0068 0.0205  0.0039  44  LYS   A CD  
1078 C CE  A LYS   A 44  ? 0.2607 0.2467 0.4470 -0.0162 0.0234  0.0223  44  LYS   A CE  
1079 C CE  B LYS   A 44  ? 0.2334 0.2280 0.3372 -0.0079 0.0188  0.0023  44  LYS   A CE  
1080 N NZ  A LYS   A 44  ? 0.2682 0.2675 0.4820 -0.0170 0.0274  0.0236  44  LYS   A NZ  
1081 N NZ  B LYS   A 44  ? 0.2359 0.2333 0.3523 -0.0108 0.0204  0.0005  44  LYS   A NZ  
1108 N N   A HIS   A 45  ? 0.1192 0.1110 0.1401 0.0044  -0.0007 0.0167  45  HIS   A N   
1109 N N   B HIS   A 45  ? 0.1479 0.1455 0.1417 -0.0049 0.0071  -0.0022 45  HIS   A N   
1110 C CA  A HIS   A 45  ? 0.1176 0.1110 0.1426 0.0030  -0.0067 0.0109  45  HIS   A CA  
1111 C CA  B HIS   A 45  ? 0.1465 0.1451 0.1448 -0.0065 -0.0045 -0.0095 45  HIS   A CA  
1112 C C   A HIS   A 45  ? 0.1218 0.1157 0.1597 0.0017  -0.0030 0.0021  45  HIS   A C   
1113 C C   B HIS   A 45  ? 0.1487 0.1470 0.1579 -0.0020 -0.0104 -0.0182 45  HIS   A C   
1114 O O   A HIS   A 45  ? 0.1296 0.1223 0.1817 0.0088  -0.0170 -0.0140 45  HIS   A O   
1115 O O   B HIS   A 45  ? 0.1534 0.1485 0.1790 -0.0026 -0.0237 -0.0333 45  HIS   A O   
1116 C CB  A HIS   A 45  ? 0.1214 0.1106 0.1459 0.0036  0.0039  0.0045  45  HIS   A CB  
1117 C CB  B HIS   A 45  ? 0.1445 0.1455 0.1396 -0.0061 -0.0052 -0.0051 45  HIS   A CB  
1118 C CG  A HIS   A 45  ? 0.1158 0.1104 0.1358 -0.0070 0.0024  0.0083  45  HIS   A CG  
1119 C CG  B HIS   A 45  ? 0.1411 0.1465 0.1338 -0.0066 -0.0045 0.0070  45  HIS   A CG  
1120 N ND1 A HIS   A 45  ? 0.1115 0.1151 0.1427 -0.0012 0.0032  0.0070  45  HIS   A ND1 
1121 N ND1 B HIS   A 45  ? 0.1397 0.1497 0.1422 -0.0041 -0.0041 0.0142  45  HIS   A ND1 
1122 C CD2 A HIS   A 45  ? 0.1212 0.1174 0.1357 -0.0121 -0.0023 0.0171  45  HIS   A CD2 
1123 C CD2 B HIS   A 45  ? 0.1410 0.1471 0.1321 -0.0087 -0.0057 0.0127  45  HIS   A CD2 
1124 C CE1 A HIS   A 45  ? 0.1149 0.1194 0.1250 -0.0020 0.0047  0.0153  45  HIS   A CE1 
1125 C CE1 B HIS   A 45  ? 0.1388 0.1489 0.1315 -0.0041 -0.0042 0.0162  45  HIS   A CE1 
1126 N NE2 A HIS   A 45  ? 0.1190 0.1230 0.1305 -0.0021 -0.0007 0.0206  45  HIS   A NE2 
1127 N NE2 B HIS   A 45  ? 0.1396 0.1486 0.1312 -0.0051 -0.0054 0.0176  45  HIS   A NE2 
1142 N N   A GLY   A 46  ? 0.1379 0.1240 0.1791 0.0167  -0.0175 0.0086  46  GLY   A N   
1143 N N   B GLY   A 46  ? 0.1507 0.1446 0.1573 0.0056  -0.0112 -0.0074 46  GLY   A N   
1144 C CA  A GLY   A 46  ? 0.1470 0.1345 0.1795 0.0156  -0.0218 0.0132  46  GLY   A CA  
1145 C CA  B GLY   A 46  ? 0.1467 0.1426 0.1461 0.0082  -0.0109 0.0064  46  GLY   A CA  
1146 C C   A GLY   A 46  ? 0.1517 0.1343 0.1818 0.0244  -0.0318 0.0304  46  GLY   A C   
1147 C C   B GLY   A 46  ? 0.1424 0.1452 0.1326 0.0120  -0.0089 0.0119  46  GLY   A C   
1148 O O   A GLY   A 46  ? 0.1576 0.1527 0.2041 0.0311  -0.0325 0.0229  46  GLY   A O   
1149 O O   B GLY   A 46  ? 0.1485 0.1525 0.1336 0.0169  0.0016  0.0063  46  GLY   A O   
1156 N N   A GLY   A 47  ? 0.1491 0.1327 0.1696 0.0176  -0.0151 0.0347  47  GLY   A N   
1157 N N   B GLY   A 47  ? 0.1298 0.1461 0.1379 0.0071  -0.0026 0.0238  47  GLY   A N   
1158 C CA  A GLY   A 47  ? 0.1473 0.1501 0.1726 0.0153  -0.0264 0.0238  47  GLY   A CA  
1159 C CA  B GLY   A 47  ? 0.1253 0.1519 0.1301 0.0045  0.0004  0.0331  47  GLY   A CA  
1160 C C   A GLY   A 47  ? 0.1370 0.1414 0.1592 0.0172  -0.0317 0.0026  47  GLY   A C   
1161 C C   B GLY   A 47  ? 0.1150 0.1561 0.1455 0.0008  0.0042  0.0265  47  GLY   A C   
1162 O O   A GLY   A 47  ? 0.1329 0.1356 0.1628 0.0144  -0.0278 0.0139  47  GLY   A O   
1163 O O   B GLY   A 47  ? 0.1135 0.1607 0.1622 0.0027  0.0070  0.0283  47  GLY   A O   
1170 N N   A GLY   A 48  ? 0.1368 0.1483 0.1643 0.0166  -0.0356 0.0016  48  GLY   A N   
1171 N N   B GLY   A 48  ? 0.1131 0.1559 0.1512 -0.0010 0.0111  0.0146  48  GLY   A N   
1172 C CA  A GLY   A 48  ? 0.1336 0.1327 0.1737 0.0062  -0.0351 -0.0107 48  GLY   A CA  
1173 C CA  B GLY   A 48  ? 0.1174 0.1517 0.1491 -0.0089 0.0197  0.0067  48  GLY   A CA  
1174 C C   A GLY   A 48  ? 0.1360 0.1284 0.1633 -0.0017 -0.0161 -0.0123 48  GLY   A C   
1175 C C   B GLY   A 48  ? 0.1187 0.1442 0.1394 -0.0053 0.0188  -0.0053 48  GLY   A C   
1176 O O   A GLY   A 48  ? 0.1509 0.1252 0.1641 0.0016  -0.0140 -0.0118 48  GLY   A O   
1177 O O   B GLY   A 48  ? 0.1120 0.1396 0.1409 -0.0082 0.0173  0.0013  48  GLY   A O   
1184 N N   A VAL   A 49  ? 0.1329 0.1199 0.1683 -0.0034 -0.0133 -0.0048 49  VAL   A N   
1185 N N   B VAL   A 49  ? 0.1282 0.1385 0.1321 -0.0108 0.0082  -0.0176 49  VAL   A N   
1186 C CA  A VAL   A 49  ? 0.1486 0.1172 0.1591 -0.0096 0.0064  -0.0059 49  VAL   A CA  
1187 C CA  B VAL   A 49  ? 0.1386 0.1354 0.1370 -0.0070 0.0197  -0.0086 49  VAL   A CA  
1188 C C   A VAL   A 49  ? 0.1330 0.1108 0.1383 -0.0011 0.0026  0.0034  49  VAL   A C   
1189 C C   B VAL   A 49  ? 0.1298 0.1236 0.1215 0.0039  0.0129  -0.0117 49  VAL   A C   
1190 O O   A VAL   A 49  ? 0.1330 0.1192 0.1337 -0.0062 0.0051  0.0020  49  VAL   A O   
1191 O O   B VAL   A 49  ? 0.1319 0.1218 0.1161 0.0159  0.0124  -0.0123 49  VAL   A O   
1192 C CB  A VAL   A 49  ? 0.1737 0.1140 0.1710 -0.0079 0.0200  -0.0069 49  VAL   A CB  
1193 C CB  B VAL   A 49  ? 0.1546 0.1489 0.1607 -0.0116 0.0253  -0.0005 49  VAL   A CB  
1194 C CG1 A VAL   A 49  ? 0.1808 0.1117 0.1634 0.0041  0.0273  0.0041  49  VAL   A CG1 
1195 C CG1 B VAL   A 49  ? 0.1571 0.1520 0.1702 -0.0095 0.0179  0.0009  49  VAL   A CG1 
1196 C CG2 A VAL   A 49  ? 0.1880 0.1222 0.2056 -0.0319 0.0183  -0.0034 49  VAL   A CG2 
1197 C CG2 B VAL   A 49  ? 0.1664 0.1553 0.1798 -0.0174 0.0305  0.0054  49  VAL   A CG2 
1216 N N   A ALA   A 50  ? 0.1264 0.1108 0.1321 -0.0007 -0.0103 0.0114  50  ALA   A N   
1217 N N   B ALA   A 50  ? 0.1268 0.1231 0.1196 0.0032  0.0053  -0.0102 50  ALA   A N   
1218 C CA  A ALA   A 50  ? 0.1177 0.1094 0.1288 -0.0058 -0.0082 0.0135  50  ALA   A CA  
1219 C CA  B ALA   A 50  ? 0.1230 0.1214 0.1222 0.0016  -0.0027 -0.0050 50  ALA   A CA  
1220 C C   A ALA   A 50  ? 0.1114 0.1156 0.1320 -0.0035 -0.0079 0.0068  50  ALA   A C   
1221 C C   B ALA   A 50  ? 0.1144 0.1203 0.1185 0.0048  -0.0019 -0.0078 50  ALA   A C   
1222 O O   A ALA   A 50  ? 0.1215 0.1192 0.1376 -0.0013 -0.0074 0.0048  50  ALA   A O   
1223 O O   B ALA   A 50  ? 0.1072 0.1218 0.1258 0.0068  0.0033  -0.0131 50  ALA   A O   
1224 C CB  A ALA   A 50  ? 0.1280 0.1091 0.1279 -0.0062 -0.0029 0.0026  50  ALA   A CB  
1225 C CB  B ALA   A 50  ? 0.1272 0.1216 0.1228 0.0014  -0.0026 -0.0031 50  ALA   A CB  
1236 N N   A GLY   A 51  ? 0.1123 0.1038 0.1448 0.0009  -0.0106 -0.0001 51  GLY   A N   
1237 N N   B GLY   A 51  ? 0.1126 0.1167 0.1143 0.0052  -0.0094 -0.0062 51  GLY   A N   
1238 C CA  A GLY   A 51  ? 0.1254 0.1028 0.1571 0.0000  -0.0102 0.0035  51  GLY   A CA  
1239 C CA  B GLY   A 51  ? 0.1104 0.1157 0.1093 0.0052  -0.0087 0.0071  51  GLY   A CA  
1240 C C   A GLY   A 51  ? 0.1248 0.1111 0.1506 0.0027  -0.0035 -0.0055 51  GLY   A C   
1241 C C   B GLY   A 51  ? 0.1135 0.1152 0.1049 0.0071  -0.0056 0.0168  51  GLY   A C   
1242 O O   A GLY   A 51  ? 0.1336 0.1161 0.1646 0.0006  -0.0050 -0.0096 51  GLY   A O   
1243 O O   B GLY   A 51  ? 0.1132 0.1190 0.1125 0.0054  -0.0080 0.0116  51  GLY   A O   
1250 N N   A ALA   A 52  ? 0.1234 0.1225 0.1397 0.0022  0.0016  -0.0167 52  ALA   A N   
1251 N N   B ALA   A 52  ? 0.1225 0.1160 0.1148 0.0059  0.0014  0.0151  52  ALA   A N   
1252 C CA  A ALA   A 52  ? 0.1227 0.1345 0.1454 0.0033  0.0009  -0.0171 52  ALA   A CA  
1253 C CA  B ALA   A 52  ? 0.1240 0.1194 0.1206 0.0025  0.0022  0.0096  52  ALA   A CA  
1254 C C   A ALA   A 52  ? 0.1138 0.1270 0.1280 -0.0066 0.0046  -0.0133 52  ALA   A C   
1255 C C   B ALA   A 52  ? 0.1247 0.1187 0.1131 0.0008  -0.0014 0.0118  52  ALA   A C   
1256 O O   A ALA   A 52  ? 0.1265 0.1316 0.1403 -0.0031 0.0077  -0.0118 52  ALA   A O   
1257 O O   B ALA   A 52  ? 0.1257 0.1232 0.1070 0.0007  -0.0121 0.0175  52  ALA   A O   
1258 C CB  A ALA   A 52  ? 0.1267 0.1647 0.1549 -0.0070 -0.0038 -0.0121 52  ALA   A CB  
1259 C CB  B ALA   A 52  ? 0.1256 0.1268 0.1226 -0.0019 0.0049  0.0113  52  ALA   A CB  
1270 N N   A LEU   A 53  ? 0.1135 0.1239 0.1301 -0.0000 -0.0012 -0.0085 53  LEU   A N   
1271 N N   B LEU   A 53  ? 0.1280 0.1148 0.1061 -0.0020 -0.0015 0.0108  53  LEU   A N   
1272 C CA  A LEU   A 53  ? 0.1224 0.1300 0.1278 0.0046  0.0028  -0.0006 53  LEU   A CA  
1273 C CA  B LEU   A 53  ? 0.1359 0.1226 0.1030 -0.0017 -0.0011 0.0037  53  LEU   A CA  
1274 C C   A LEU   A 53  ? 0.1200 0.1319 0.1182 0.0086  0.0017  0.0010  53  LEU   A C   
1275 C C   B LEU   A 53  ? 0.1309 0.1262 0.0935 0.0002  -0.0069 0.0059  53  LEU   A C   
1276 O O   A LEU   A 53  ? 0.1340 0.1479 0.1277 -0.0012 0.0004  0.0016  53  LEU   A O   
1277 O O   B LEU   A 53  ? 0.1337 0.1288 0.0862 0.0026  -0.0157 0.0033  53  LEU   A O   
1278 C CB  A LEU   A 53  ? 0.1327 0.1337 0.1283 0.0040  0.0035  0.0001  53  LEU   A CB  
1279 C CB  B LEU   A 53  ? 0.1441 0.1274 0.1059 -0.0042 0.0008  -0.0009 53  LEU   A CB  
1280 C CG  A LEU   A 53  ? 0.1563 0.1317 0.1361 -0.0045 0.0099  0.0027  53  LEU   A CG  
1281 C CG  B LEU   A 53  ? 0.1475 0.1276 0.1201 -0.0025 0.0049  -0.0015 53  LEU   A CG  
1282 C CD1 A LEU   A 53  ? 0.1726 0.1430 0.1460 0.0046  0.0173  0.0025  53  LEU   A CD1 
1283 C CD1 B LEU   A 53  ? 0.1515 0.1321 0.1241 0.0036  0.0066  0.0016  53  LEU   A CD1 
1284 C CD2 A LEU   A 53  ? 0.1770 0.1379 0.1467 -0.0100 0.0154  0.0031  53  LEU   A CD2 
1285 C CD2 B LEU   A 53  ? 0.1506 0.1323 0.1369 -0.0039 0.0095  0.0026  53  LEU   A CD2 
1308 N N   A ASN   A 54  ? 0.1135 0.1265 0.1159 0.0025  -0.0037 0.0018  54  ASN   A N   
1309 N N   B ASN   A 54  ? 0.1264 0.1298 0.1039 -0.0015 -0.0014 0.0036  54  ASN   A N   
1310 C CA  A ASN   A 54  ? 0.1091 0.1230 0.1246 -0.0010 -0.0083 -0.0017 54  ASN   A CA  
1311 C CA  B ASN   A 54  ? 0.1229 0.1324 0.1193 -0.0019 0.0016  -0.0002 54  ASN   A CA  
1312 C C   A ASN   A 54  ? 0.1186 0.1257 0.1262 -0.0080 0.0004  -0.0068 54  ASN   A C   
1313 C C   B ASN   A 54  ? 0.1244 0.1290 0.1280 -0.0020 -0.0020 -0.0004 54  ASN   A C   
1314 O O   A ASN   A 54  ? 0.1181 0.1278 0.1287 -0.0076 -0.0042 -0.0138 54  ASN   A O   
1315 O O   B ASN   A 54  ? 0.1263 0.1268 0.1357 -0.0016 -0.0080 0.0074  54  ASN   A O   
1316 C CB  A ASN   A 54  ? 0.1061 0.1216 0.1445 -0.0030 -0.0149 -0.0017 54  ASN   A CB  
1317 C CB  B ASN   A 54  ? 0.1250 0.1367 0.1314 -0.0006 0.0094  -0.0024 54  ASN   A CB  
1318 C CG  A ASN   A 54  ? 0.1148 0.1203 0.1439 0.0014  -0.0088 0.0000  54  ASN   A CG  
1319 C CG  B ASN   A 54  ? 0.1250 0.1391 0.1359 0.0043  0.0113  -0.0037 54  ASN   A CG  
1320 O OD1 A ASN   A 54  ? 0.1110 0.1161 0.1379 -0.0041 -0.0075 0.0082  54  ASN   A OD1 
1321 O OD1 B ASN   A 54  ? 0.1225 0.1401 0.1416 0.0006  0.0113  -0.0055 54  ASN   A OD1 
1322 N ND2 A ASN   A 54  ? 0.1218 0.1335 0.1737 -0.0106 -0.0257 0.0100  54  ASN   A ND2 
1323 N ND2 B ASN   A 54  ? 0.1276 0.1423 0.1458 0.0053  0.0068  -0.0014 54  ASN   A ND2 
1336 N N   . LYS   A 55  ? 0.1202 0.1249 0.1387 0.0005  -0.0054 -0.0134 55  LYS   A N   
1337 C CA  . LYS   A 55  ? 0.1302 0.1344 0.1463 0.0056  -0.0106 -0.0231 55  LYS   A CA  
1338 C C   . LYS   A 55  ? 0.1279 0.1414 0.1485 -0.0009 -0.0050 -0.0218 55  LYS   A C   
1339 O O   . LYS   A 55  ? 0.1369 0.1517 0.1586 0.0049  -0.0011 -0.0316 55  LYS   A O   
1340 C CB  . LYS   A 55  ? 0.1374 0.1391 0.1652 0.0132  -0.0124 -0.0221 55  LYS   A CB  
1341 C CG  . LYS   A 55  ? 0.1470 0.1676 0.1811 0.0232  -0.0188 -0.0288 55  LYS   A CG  
1342 C CD  . LYS   A 55  ? 0.1589 0.2016 0.1929 0.0388  -0.0147 -0.0283 55  LYS   A CD  
1343 C CE  . LYS   A 55  ? 0.1799 0.2407 0.2152 0.0508  -0.0229 -0.0341 55  LYS   A CE  
1344 N NZ  . LYS   A 55  ? 0.1863 0.2500 0.2147 0.0570  -0.0236 -0.0291 55  LYS   A NZ  
1359 N N   . ALA   A 56  ? 0.1318 0.1508 0.1504 -0.0058 0.0013  -0.0247 56  ALA   A N   
1360 C CA  . ALA   A 56  ? 0.1426 0.1730 0.1536 -0.0087 0.0106  -0.0236 56  ALA   A CA  
1361 C C   . ALA   A 56  ? 0.1482 0.1800 0.1349 -0.0074 0.0106  -0.0259 56  ALA   A C   
1362 O O   . ALA   A 56  ? 0.1494 0.2155 0.1499 0.0013  0.0092  -0.0266 56  ALA   A O   
1363 C CB  . ALA   A 56  ? 0.1506 0.1920 0.1649 -0.0179 0.0078  -0.0148 56  ALA   A CB  
1369 N N   . THR   A 57  ? 0.1339 0.1615 0.1232 -0.0074 0.0082  -0.0187 57  THR   A N   
1370 C CA  . THR   A 57  ? 0.1377 0.1549 0.1321 -0.0076 -0.0060 -0.0144 57  THR   A CA  
1371 C C   . THR   A 57  ? 0.1393 0.1601 0.1392 -0.0017 -0.0093 -0.0202 57  THR   A C   
1372 O O   . THR   A 57  ? 0.1348 0.1614 0.1621 -0.0056 -0.0160 -0.0265 57  THR   A O   
1373 C CB  . THR   A 57  ? 0.1358 0.1531 0.1353 -0.0072 -0.0012 -0.0062 57  THR   A CB  
1374 O OG1 . THR   A 57  ? 0.1246 0.1431 0.1444 -0.0035 0.0008  -0.0125 57  THR   A OG1 
1375 C CG2 . THR   A 57  ? 0.1408 0.1556 0.1270 -0.0062 -0.0015 0.0000  57  THR   A CG2 
1383 N N   . ASN   A 58  ? 0.1380 0.1598 0.1515 -0.0050 0.0012  -0.0321 58  ASN   A N   
1384 C CA  . ASN   A 58  ? 0.1560 0.1499 0.1766 -0.0113 0.0074  -0.0398 58  ASN   A CA  
1385 C C   . ASN   A 58  ? 0.1367 0.1411 0.1721 0.0030  -0.0096 -0.0259 58  ASN   A C   
1386 O O   . ASN   A 58  ? 0.1367 0.1521 0.1804 -0.0113 -0.0087 -0.0350 58  ASN   A O   
1387 C CB  . ASN   A 58  ? 0.2041 0.1681 0.2152 -0.0247 0.0313  -0.0559 58  ASN   A CB  
1388 C CG  . ASN   A 58  ? 0.2438 0.1887 0.2886 -0.0213 0.0332  -0.0440 58  ASN   A CG  
1389 O OD1 . ASN   A 58  ? 0.2684 0.1865 0.3229 0.0159  0.0581  -0.0391 58  ASN   A OD1 
1390 N ND2 . ASN   A 58  ? 0.2545 0.2013 0.3135 -0.0276 0.0204  -0.0469 58  ASN   A ND2 
1397 N N   . ASN   A 59  ? 0.1226 0.1334 0.1593 -0.0027 -0.0170 -0.0204 59  ASN   A N   
1398 C CA  . ASN   A 59  ? 0.1247 0.1240 0.1591 0.0004  -0.0115 -0.0129 59  ASN   A CA  
1399 C C   . ASN   A 59  ? 0.1235 0.1249 0.1567 -0.0042 -0.0087 -0.0110 59  ASN   A C   
1400 O O   . ASN   A 59  ? 0.1244 0.1303 0.1564 -0.0064 -0.0017 -0.0043 59  ASN   A O   
1401 C CB  . ASN   A 59  ? 0.1366 0.1240 0.1664 0.0052  -0.0195 -0.0200 59  ASN   A CB  
1402 C CG  . ASN   A 59  ? 0.1355 0.1294 0.1620 -0.0018 -0.0258 -0.0021 59  ASN   A CG  
1403 O OD1 . ASN   A 59  ? 0.1515 0.1356 0.1587 -0.0119 -0.0272 0.0004  59  ASN   A OD1 
1404 N ND2 . ASN   A 59  ? 0.1380 0.1335 0.1804 -0.0119 -0.0184 -0.0007 59  ASN   A ND2 
1411 N N   . ALA   A 60  ? 0.1193 0.1316 0.1492 -0.0016 -0.0035 -0.0049 60  ALA   A N   
1412 C CA  . ALA   A 60  ? 0.1227 0.1349 0.1552 -0.0004 -0.0109 -0.0033 60  ALA   A CA  
1413 C C   . ALA   A 60  ? 0.1213 0.1258 0.1548 -0.0021 -0.0072 -0.0100 60  ALA   A C   
1414 O O   . ALA   A 60  ? 0.1210 0.1277 0.1706 0.0026  -0.0113 -0.0115 60  ALA   A O   
1415 C CB  . ALA   A 60  ? 0.1360 0.1455 0.1600 0.0021  -0.0185 -0.0131 60  ALA   A CB  
1421 N N   . MET   A 61  ? 0.1195 0.1210 0.1542 -0.0035 -0.0067 -0.0079 61  MET   A N   
1422 C CA  . MET   A 61  ? 0.1218 0.1167 0.1477 -0.0040 -0.0020 -0.0011 61  MET   A CA  
1423 C C   . MET   A 61  ? 0.1146 0.1166 0.1457 -0.0049 -0.0040 0.0003  61  MET   A C   
1424 O O   . MET   A 61  ? 0.1187 0.1185 0.1580 -0.0023 0.0054  -0.0003 61  MET   A O   
1425 C CB  . MET   A 61  ? 0.1272 0.1208 0.1336 -0.0056 0.0007  -0.0030 61  MET   A CB  
1426 C CG  . MET   A 61  ? 0.1284 0.1321 0.1500 0.0005  -0.0041 -0.0067 61  MET   A CG  
1427 S SD  . MET   A 61  ? 0.1301 0.1328 0.1869 -0.0115 0.0005  -0.0202 61  MET   A SD  
1428 C CE  . MET   A 61  ? 0.1567 0.1460 0.2137 -0.0146 0.0218  -0.0189 61  MET   A CE  
1438 N N   . GLN   A 62  ? 0.1194 0.1159 0.1414 -0.0012 0.0005  -0.0032 62  GLN   A N   
1439 C CA  . GLN   A 62  ? 0.1213 0.1133 0.1504 -0.0034 0.0013  0.0024  62  GLN   A CA  
1440 C C   . GLN   A 62  ? 0.1219 0.1084 0.1604 -0.0002 0.0095  0.0073  62  GLN   A C   
1441 O O   . GLN   A 62  ? 0.1243 0.1225 0.1624 -0.0011 0.0033  -0.0038 62  GLN   A O   
1442 C CB  . GLN   A 62  ? 0.1237 0.1105 0.1606 -0.0017 0.0005  -0.0001 62  GLN   A CB  
1443 C CG  . GLN   A 62  ? 0.1300 0.1095 0.1601 -0.0043 0.0023  0.0127  62  GLN   A CG  
1444 C CD  . GLN   A 62  ? 0.1375 0.1180 0.1533 -0.0016 0.0008  0.0129  62  GLN   A CD  
1445 O OE1 . GLN   A 62  ? 0.1447 0.1285 0.1572 -0.0009 -0.0058 0.0011  62  GLN   A OE1 
1446 N NE2 . GLN   A 62  ? 0.1435 0.1163 0.1644 0.0024  -0.0008 -0.0034 62  GLN   A NE2 
1455 N N   . VAL   A 63  ? 0.1159 0.1178 0.1713 -0.0021 0.0040  -0.0150 63  VAL   A N   
1456 C CA  . VAL   A 63  ? 0.1208 0.1278 0.1924 -0.0123 0.0021  -0.0153 63  VAL   A CA  
1457 C C   . VAL   A 63  ? 0.1109 0.1291 0.1734 -0.0114 -0.0033 -0.0167 63  VAL   A C   
1458 O O   . VAL   A 63  ? 0.1142 0.1288 0.1924 -0.0110 -0.0007 -0.0080 63  VAL   A O   
1459 C CB  . VAL   A 63  ? 0.1336 0.1433 0.2139 -0.0117 0.0008  -0.0345 63  VAL   A CB  
1460 C CG1 . VAL   A 63  ? 0.1465 0.1654 0.2440 -0.0153 -0.0088 -0.0531 63  VAL   A CG1 
1461 C CG2 . VAL   A 63  ? 0.1466 0.1383 0.2303 -0.0120 0.0165  -0.0347 63  VAL   A CG2 
1471 N N   . GLU   A 64  ? 0.1145 0.1386 0.1599 -0.0021 -0.0008 -0.0087 64  GLU   A N   
1472 C CA  . GLU   A 64  ? 0.1169 0.1316 0.1731 -0.0031 -0.0043 -0.0046 64  GLU   A CA  
1473 C C   . GLU   A 64  ? 0.1160 0.1261 0.1707 -0.0031 0.0007  0.0030  64  GLU   A C   
1474 O O   . GLU   A 64  ? 0.1181 0.1330 0.1750 0.0027  0.0032  -0.0021 64  GLU   A O   
1475 C CB  . GLU   A 64  ? 0.1298 0.1407 0.1783 -0.0069 0.0014  -0.0079 64  GLU   A CB  
1476 C CG  . GLU   A 64  ? 0.1395 0.1452 0.1800 -0.0094 0.0056  -0.0004 64  GLU   A CG  
1477 C CD  . GLU   A 64  ? 0.1544 0.1554 0.1889 -0.0149 0.0133  -0.0067 64  GLU   A CD  
1478 O OE1 . GLU   A 64  ? 0.1507 0.1696 0.2134 -0.0200 0.0178  -0.0027 64  GLU   A OE1 
1479 O OE2 . GLU   A 64  ? 0.1772 0.1552 0.1836 -0.0250 0.0015  0.0082  64  GLU   A OE2 
1486 N N   . SER   A 65  ? 0.1125 0.1220 0.1612 0.0049  -0.0003 -0.0006 65  SER   A N   
1487 C CA  . SER   A 65  ? 0.1195 0.1174 0.1608 -0.0011 0.0007  -0.0043 65  SER   A CA  
1488 C C   . SER   A 65  ? 0.1206 0.1256 0.1627 -0.0042 0.0017  0.0042  65  SER   A C   
1489 O O   . SER   A 65  ? 0.1283 0.1302 0.1774 0.0032  0.0156  -0.0063 65  SER   A O   
1490 C CB  . SER   A 65  ? 0.1173 0.1178 0.1610 -0.0055 0.0076  0.0091  65  SER   A CB  
1491 O OG  . SER   A 65  ? 0.1195 0.1296 0.1659 -0.0052 -0.0026 0.0104  65  SER   A OG  
1497 N N   . ASP   A 66  ? 0.1227 0.1225 0.1636 -0.0013 0.0119  0.0083  66  ASP   A N   
1498 C CA  . ASP   A 66  ? 0.1338 0.1341 0.1756 0.0009  0.0092  0.0140  66  ASP   A CA  
1499 C C   . ASP   A 66  ? 0.1320 0.1296 0.1833 -0.0020 0.0192  0.0161  66  ASP   A C   
1500 O O   . ASP   A 66  ? 0.1392 0.1387 0.2012 -0.0022 0.0331  0.0236  66  ASP   A O   
1501 C CB  . ASP   A 66  ? 0.1447 0.1425 0.2022 0.0083  0.0115  0.0278  66  ASP   A CB  
1502 C CG  . ASP   A 66  ? 0.1667 0.1594 0.2388 0.0066  0.0046  0.0424  66  ASP   A CG  
1503 O OD1 . ASP   A 66  ? 0.1679 0.1899 0.2211 -0.0034 0.0002  0.0480  66  ASP   A OD1 
1504 O OD2 . ASP   A 66  ? 0.1839 0.1719 0.3254 0.0231  -0.0191 0.0223  66  ASP   A OD2 
1509 N N   . ASP   A 67  ? 0.1188 0.1325 0.1878 0.0002  0.0177  0.0160  67  ASP   A N   
1510 C CA  . ASP   A 67  ? 0.1274 0.1492 0.1992 0.0026  0.0111  0.0230  67  ASP   A CA  
1511 C C   . ASP   A 67  ? 0.1276 0.1471 0.2019 0.0034  0.0137  0.0246  67  ASP   A C   
1512 O O   . ASP   A 67  ? 0.1275 0.1555 0.2145 0.0051  0.0300  0.0313  67  ASP   A O   
1513 C CB  . ASP   A 67  ? 0.1372 0.1613 0.2342 -0.0008 -0.0112 0.0247  67  ASP   A CB  
1514 C CG  . ASP   A 67  ? 0.1321 0.1742 0.2735 -0.0024 -0.0180 0.0311  67  ASP   A CG  
1515 O OD1 . ASP   A 67  ? 0.1363 0.1938 0.3495 -0.0093 -0.0303 0.0443  67  ASP   A OD1 
1516 O OD2 . ASP   A 67  ? 0.1347 0.1778 0.2600 0.0073  -0.0120 0.0244  67  ASP   A OD2 
1521 N N   . TYR   A 68  ? 0.1267 0.1311 0.1899 0.0026  0.0216  0.0207  68  TYR   A N   
1522 C CA  . TYR   A 68  ? 0.1385 0.1339 0.1926 0.0012  0.0224  0.0263  68  TYR   A CA  
1523 C C   . TYR   A 68  ? 0.1300 0.1335 0.1860 0.0022  0.0266  0.0170  68  TYR   A C   
1524 O O   . TYR   A 68  ? 0.1380 0.1371 0.1977 0.0105  0.0392  0.0175  68  TYR   A O   
1525 C CB  . TYR   A 68  ? 0.1392 0.1289 0.2125 0.0087  0.0426  0.0254  68  TYR   A CB  
1526 C CG  . TYR   A 68  ? 0.1475 0.1456 0.2435 0.0058  0.0531  0.0337  68  TYR   A CG  
1527 C CD1 . TYR   A 68  ? 0.1614 0.1556 0.2813 -0.0188 0.0455  -0.0003 68  TYR   A CD1 
1528 C CD2 . TYR   A 68  ? 0.1744 0.1498 0.2806 0.0127  0.0583  0.0427  68  TYR   A CD2 
1529 C CE1 . TYR   A 68  ? 0.1702 0.1680 0.3219 -0.0182 0.0543  -0.0122 68  TYR   A CE1 
1530 C CE2 . TYR   A 68  ? 0.1696 0.1543 0.3133 0.0023  0.0673  0.0179  68  TYR   A CE2 
1531 C CZ  . TYR   A 68  ? 0.1714 0.1618 0.3363 -0.0201 0.0588  -0.0157 68  TYR   A CZ  
1532 O OH  . TYR   A 68  ? 0.1944 0.1657 0.3652 -0.0171 0.0333  -0.0505 68  TYR   A OH  
1542 N N   . ILE   A 69  ? 0.1244 0.1263 0.1911 0.0027  0.0214  0.0144  69  ILE   A N   
1543 C CA  . ILE   A 69  ? 0.1341 0.1326 0.1794 0.0034  0.0186  0.0064  69  ILE   A CA  
1544 C C   . ILE   A 69  ? 0.1336 0.1332 0.1677 0.0039  0.0251  0.0187  69  ILE   A C   
1545 O O   . ILE   A 69  ? 0.1475 0.1431 0.1653 -0.0034 0.0265  0.0173  69  ILE   A O   
1546 C CB  . ILE   A 69  ? 0.1413 0.1540 0.1750 0.0053  0.0132  -0.0025 69  ILE   A CB  
1547 C CG1 . ILE   A 69  ? 0.1405 0.1663 0.1867 0.0070  0.0176  -0.0161 69  ILE   A CG1 
1548 C CG2 . ILE   A 69  ? 0.1638 0.1750 0.1903 0.0146  -0.0008 -0.0079 69  ILE   A CG2 
1549 C CD1 . ILE   A 69  ? 0.1389 0.1753 0.2052 -0.0021 0.0186  -0.0206 69  ILE   A CD1 
1561 N N   . ALA   A 70  ? 0.1416 0.1348 0.1819 -0.0065 0.0291  0.0147  70  ALA   A N   
1562 C CA  . ALA   A 70  ? 0.1476 0.1447 0.2060 -0.0174 0.0344  0.0174  70  ALA   A CA  
1563 C C   . ALA   A 70  ? 0.1427 0.1600 0.1997 -0.0110 0.0373  0.0188  70  ALA   A C   
1564 O O   . ALA   A 70  ? 0.1599 0.1935 0.2245 0.0089  0.0536  0.0365  70  ALA   A O   
1565 C CB  . ALA   A 70  ? 0.1494 0.1399 0.2232 -0.0179 0.0294  0.0073  70  ALA   A CB  
1571 N N   . THR   A 71  ? 0.1378 0.1584 0.1834 -0.0026 0.0231  0.0210  71  THR   A N   
1572 C CA  . THR   A 71  ? 0.1489 0.1732 0.2180 0.0073  0.0229  0.0250  71  THR   A CA  
1573 C C   . THR   A 71  ? 0.1379 0.1666 0.2300 0.0130  0.0401  0.0180  71  THR   A C   
1574 O O   . THR   A 71  ? 0.1422 0.1941 0.2772 0.0110  0.0460  -0.0060 71  THR   A O   
1575 C CB  . THR   A 71  ? 0.1738 0.1969 0.2446 0.0172  -0.0120 0.0294  71  THR   A CB  
1576 O OG1 . THR   A 71  ? 0.1974 0.2159 0.2507 0.0116  -0.0333 0.0267  71  THR   A OG1 
1577 C CG2 . THR   A 71  ? 0.1830 0.2082 0.2716 0.0233  -0.0141 0.0380  71  THR   A CG2 
1585 N N   . ASN   A 72  ? 0.1442 0.1496 0.2098 0.0111  0.0313  0.0186  72  ASN   A N   
1586 C CA  . ASN   A 72  ? 0.1484 0.1509 0.2168 0.0145  0.0451  0.0183  72  ASN   A CA  
1587 C C   . ASN   A 72  ? 0.1628 0.1470 0.2108 0.0110  0.0521  0.0111  72  ASN   A C   
1588 O O   . ASN   A 72  ? 0.1758 0.1476 0.2415 0.0173  0.0459  0.0011  72  ASN   A O   
1589 C CB  . ASN   A 72  ? 0.1646 0.1527 0.2180 0.0179  0.0407  0.0164  72  ASN   A CB  
1590 C CG  . ASN   A 72  ? 0.1865 0.1661 0.2223 0.0290  0.0338  0.0243  72  ASN   A CG  
1591 O OD1 . ASN   A 72  ? 0.2048 0.2039 0.2426 0.0306  0.0377  0.0316  72  ASN   A OD1 
1592 N ND2 . ASN   A 72  ? 0.2028 0.1682 0.2266 0.0505  0.0168  0.0143  72  ASN   A ND2 
1599 N N   . GLY   A 73  ? 0.1590 0.1467 0.1943 0.0035  0.0487  0.0087  73  GLY   A N   
1600 C CA  . GLY   A 73  ? 0.1645 0.1476 0.1792 -0.0071 0.0411  0.0005  73  GLY   A CA  
1601 C C   . GLY   A 73  ? 0.1605 0.1366 0.1677 -0.0006 0.0542  0.0155  73  GLY   A C   
1602 O O   . GLY   A 73  ? 0.1611 0.1408 0.1833 0.0105  0.0408  0.0261  73  GLY   A O   
1606 N N   . PRO   A 74  ? 0.1708 0.1391 0.1727 -0.0153 0.0492  0.0140  74  PRO   A N   
1607 C CA  . PRO   A 74  ? 0.1665 0.1360 0.1832 -0.0047 0.0464  0.0190  74  PRO   A CA  
1608 C C   . PRO   A 74  ? 0.1545 0.1229 0.1795 -0.0012 0.0323  0.0034  74  PRO   A C   
1609 O O   . PRO   A 74  ? 0.1649 0.1280 0.2016 0.0053  0.0411  -0.0002 74  PRO   A O   
1610 C CB  . PRO   A 74  ? 0.1877 0.1619 0.2078 -0.0030 0.0466  0.0294  74  PRO   A CB  
1611 C CG  . PRO   A 74  ? 0.2121 0.1939 0.2392 -0.0176 0.0369  0.0143  74  PRO   A CG  
1612 C CD  . PRO   A 74  ? 0.1926 0.1715 0.1871 -0.0249 0.0385  0.0011  74  PRO   A CD  
1620 N N   . LEU   A 75  ? 0.1501 0.1189 0.1554 -0.0028 0.0291  0.0072  75  LEU   A N   
1621 C CA  . LEU   A 75  ? 0.1558 0.1156 0.1437 -0.0008 0.0140  0.0070  75  LEU   A CA  
1622 C C   . LEU   A 75  ? 0.1700 0.1324 0.1425 -0.0006 0.0188  0.0123  75  LEU   A C   
1623 O O   . LEU   A 75  ? 0.1990 0.1460 0.1450 0.0121  0.0108  0.0083  75  LEU   A O   
1624 C CB  . LEU   A 75  ? 0.1620 0.1227 0.1432 -0.0078 0.0108  0.0177  75  LEU   A CB  
1625 C CG  . LEU   A 75  ? 0.1799 0.1529 0.1635 -0.0387 0.0143  0.0138  75  LEU   A CG  
1626 C CD1 . LEU   A 75  ? 0.1932 0.2040 0.1741 -0.0417 0.0147  -0.0018 75  LEU   A CD1 
1627 C CD2 . LEU   A 75  ? 0.2077 0.1948 0.2097 -0.0135 0.0136  0.0173  75  LEU   A CD2 
1639 N N   . LYS   A 76  ? 0.1720 0.1292 0.1594 -0.0096 0.0198  -0.0028 76  LYS   A N   
1640 C CA  . LYS   A 76  ? 0.1699 0.1480 0.1637 -0.0061 0.0199  -0.0130 76  LYS   A CA  
1641 C C   . LYS   A 76  ? 0.1609 0.1325 0.1429 -0.0002 0.0213  0.0080  76  LYS   A C   
1642 O O   . LYS   A 76  ? 0.1625 0.1261 0.1377 0.0001  0.0196  0.0133  76  LYS   A O   
1643 C CB  . LYS   A 76  ? 0.1738 0.1711 0.2009 0.0069  0.0205  -0.0384 76  LYS   A CB  
1644 C CG  . LYS   A 76  ? 0.1830 0.1672 0.2564 0.0079  0.0156  -0.0378 76  LYS   A CG  
1645 C CD  . LYS   A 76  ? 0.1896 0.1672 0.3049 0.0112  0.0090  -0.0452 76  LYS   A CD  
1646 C CE  . LYS   A 76  ? 0.2066 0.1869 0.3605 0.0061  0.0054  -0.0474 76  LYS   A CE  
1647 N NZ  . LYS   A 76  ? 0.2079 0.1835 0.3971 -0.0093 0.0001  -0.0553 76  LYS   A NZ  
1661 N N   . VAL   A 77  ? 0.1720 0.1352 0.1438 -0.0015 0.0315  0.0136  77  VAL   A N   
1662 C CA  . VAL   A 77  ? 0.1702 0.1354 0.1378 0.0103  0.0236  0.0138  77  VAL   A CA  
1663 C C   . VAL   A 77  ? 0.1592 0.1342 0.1300 0.0103  0.0188  0.0081  77  VAL   A C   
1664 O O   . VAL   A 77  ? 0.1663 0.1404 0.1306 0.0131  0.0333  -0.0021 77  VAL   A O   
1665 C CB  . VAL   A 77  ? 0.1898 0.1538 0.1449 0.0061  0.0161  0.0203  77  VAL   A CB  
1666 C CG1 . VAL   A 77  ? 0.1843 0.1679 0.1638 0.0159  0.0030  0.0096  77  VAL   A CG1 
1667 C CG2 . VAL   A 77  ? 0.2149 0.1676 0.1746 0.0044  -0.0012 0.0266  77  VAL   A CG2 
1677 N N   . GLY   A 78  ? 0.1590 0.1268 0.1245 0.0055  0.0257  0.0062  78  GLY   A N   
1678 C CA  . GLY   A 78  ? 0.1574 0.1266 0.1404 0.0036  0.0251  0.0102  78  GLY   A CA  
1679 C C   . GLY   A 78  ? 0.1408 0.1164 0.1403 0.0075  0.0299  0.0071  78  GLY   A C   
1680 O O   . GLY   A 78  ? 0.1381 0.1299 0.1630 0.0002  0.0212  0.0230  78  GLY   A O   
1684 N N   . GLY   A 79  ? 0.1493 0.1183 0.1385 0.0079  0.0200  0.0136  79  GLY   A N   
1685 C CA  . GLY   A 79  ? 0.1453 0.1291 0.1420 0.0020  0.0245  0.0125  79  GLY   A CA  
1686 C C   . GLY   A 79  ? 0.1328 0.1208 0.1385 0.0020  0.0175  0.0043  79  GLY   A C   
1687 O O   . GLY   A 79  ? 0.1352 0.1311 0.1473 0.0202  0.0159  0.0029  79  GLY   A O   
1691 N N   . SER   A 80  ? 0.1247 0.1345 0.1604 0.0008  0.0198  -0.0065 80  SER   A N   
1692 C CA  . SER   A 80  ? 0.1284 0.1278 0.1505 0.0020  0.0116  0.0069  80  SER   A CA  
1693 C C   . SER   A 80  ? 0.1227 0.1255 0.1477 0.0000  0.0082  0.0118  80  SER   A C   
1694 O O   . SER   A 80  ? 0.1219 0.1538 0.1791 0.0113  0.0101  -0.0066 80  SER   A O   
1695 C CB  . SER   A 80  ? 0.1405 0.1279 0.1776 -0.0018 0.0069  0.0063  80  SER   A CB  
1696 O OG  . SER   A 80  ? 0.1638 0.1314 0.2138 0.0025  -0.0005 0.0188  80  SER   A OG  
1702 N N   . CYS   A 81  ? 0.1192 0.1250 0.1515 0.0032  -0.0021 0.0071  81  CYS   A N   
1703 C CA  . CYS   A 81  ? 0.1190 0.1336 0.1491 -0.0042 -0.0094 0.0148  81  CYS   A CA  
1704 C C   . CYS   A 81  ? 0.1192 0.1259 0.1470 -0.0029 -0.0021 0.0223  81  CYS   A C   
1705 O O   . CYS   A 81  ? 0.1199 0.1560 0.1574 0.0046  0.0026  0.0312  81  CYS   A O   
1706 C CB  . CYS   A 81  ? 0.1332 0.1366 0.1628 -0.0093 -0.0008 0.0224  81  CYS   A CB  
1707 S SG  . CYS   A 81  ? 0.1438 0.1281 0.1641 -0.0106 0.0013  0.0118  81  CYS   A SG  
1713 N N   . VAL   A 82  ? 0.1196 0.1337 0.1528 0.0033  -0.0104 0.0177  82  VAL   A N   
1714 C CA  . VAL   A 82  ? 0.1328 0.1419 0.1512 0.0044  -0.0073 0.0271  82  VAL   A CA  
1715 C C   . VAL   A 82  ? 0.1341 0.1465 0.1580 0.0000  -0.0123 0.0242  82  VAL   A C   
1716 O O   . VAL   A 82  ? 0.1284 0.1547 0.1836 -0.0000 -0.0098 -0.0040 82  VAL   A O   
1717 C CB  . VAL   A 82  ? 0.1676 0.1560 0.1637 0.0038  -0.0026 0.0266  82  VAL   A CB  
1718 C CG1 . VAL   A 82  ? 0.1909 0.1716 0.1793 0.0056  0.0019  0.0250  82  VAL   A CG1 
1719 C CG2 . VAL   A 82  ? 0.1746 0.1585 0.1918 -0.0013 0.0002  0.0280  82  VAL   A CG2 
1729 N N   . LEU   A 83  ? 0.1288 0.1398 0.1471 -0.0074 -0.0071 0.0089  83  LEU   A N   
1730 C CA  . LEU   A 83  ? 0.1324 0.1439 0.1437 -0.0116 -0.0058 0.0093  83  LEU   A CA  
1731 C C   . LEU   A 83  ? 0.1360 0.1434 0.1460 -0.0103 -0.0137 0.0099  83  LEU   A C   
1732 O O   . LEU   A 83  ? 0.1460 0.1492 0.1462 -0.0168 -0.0102 0.0193  83  LEU   A O   
1733 C CB  . LEU   A 83  ? 0.1435 0.1497 0.1503 -0.0098 -0.0124 0.0131  83  LEU   A CB  
1734 C CG  . LEU   A 83  ? 0.1517 0.1610 0.1557 -0.0124 0.0040  0.0043  83  LEU   A CG  
1735 C CD1 . LEU   A 83  ? 0.1641 0.1650 0.1633 -0.0276 0.0006  0.0181  83  LEU   A CD1 
1736 C CD2 . LEU   A 83  ? 0.1512 0.1766 0.1699 -0.0126 0.0193  0.0135  83  LEU   A CD2 
1748 N N   . SER   A 84  ? 0.1477 0.1457 0.1477 -0.0145 -0.0081 0.0124  84  SER   A N   
1749 C CA  . SER   A 84  ? 0.1578 0.1535 0.1344 -0.0091 -0.0090 0.0083  84  SER   A CA  
1750 C C   . SER   A 84  ? 0.1618 0.1502 0.1298 -0.0142 0.0000  0.0067  84  SER   A C   
1751 O O   . SER   A 84  ? 0.1530 0.1650 0.1345 -0.0126 -0.0057 0.0020  84  SER   A O   
1752 C CB  . SER   A 84  ? 0.1711 0.1792 0.1418 -0.0126 -0.0097 -0.0025 84  SER   A CB  
1753 O OG  . SER   A 84  ? 0.1755 0.1999 0.1559 -0.0094 -0.0185 -0.0178 84  SER   A OG  
1759 N N   . GLY   A 85  ? 0.1787 0.1598 0.1314 -0.0136 0.0048  0.0020  85  GLY   A N   
1760 C CA  . GLY   A 85  ? 0.1809 0.1667 0.1469 -0.0208 0.0089  -0.0093 85  GLY   A CA  
1761 C C   . GLY   A 85  ? 0.1722 0.1768 0.1265 -0.0163 0.0013  -0.0035 85  GLY   A C   
1762 O O   . GLY   A 85  ? 0.1684 0.1878 0.1361 -0.0262 0.0099  -0.0150 85  GLY   A O   
1766 N N   . HIS   A 86  ? 0.1720 0.1675 0.1228 -0.0182 -0.0048 -0.0020 86  HIS   A N   
1767 C CA  . HIS   A 86  ? 0.1917 0.1758 0.1157 -0.0198 -0.0054 -0.0013 86  HIS   A CA  
1768 C C   . HIS   A 86  ? 0.2162 0.1862 0.1237 -0.0186 -0.0100 -0.0037 86  HIS   A C   
1769 O O   . HIS   A 86  ? 0.2221 0.2083 0.1343 -0.0122 0.0000  0.0001  86  HIS   A O   
1770 C CB  . HIS   A 86  ? 0.1876 0.1675 0.1310 -0.0114 -0.0018 -0.0025 86  HIS   A CB  
1771 C CG  . HIS   A 86  ? 0.1819 0.1694 0.1403 -0.0063 0.0062  0.0063  86  HIS   A CG  
1772 N ND1 . HIS   A 86  ? 0.1866 0.1726 0.1815 -0.0166 0.0013  0.0072  86  HIS   A ND1 
1773 C CD2 . HIS   A 86  ? 0.1826 0.1619 0.1422 -0.0014 0.0079  0.0076  86  HIS   A CD2 
1774 C CE1 . HIS   A 86  ? 0.1867 0.1698 0.1831 -0.0080 0.0149  0.0109  86  HIS   A CE1 
1775 N NE2 . HIS   A 86  ? 0.1832 0.1652 0.1578 0.0038  0.0180  0.0216  86  HIS   A NE2 
1783 N N   . ASN   A 87  ? 0.2274 0.1923 0.1310 -0.0153 0.0168  -0.0137 87  ASN   A N   
1784 C CA  . ASN   A 87  ? 0.2453 0.2086 0.1452 -0.0063 0.0396  -0.0252 87  ASN   A CA  
1785 C C   . ASN   A 87  ? 0.2453 0.2246 0.1732 -0.0099 0.0587  -0.0095 87  ASN   A C   
1786 O O   . ASN   A 87  ? 0.2684 0.2427 0.2239 -0.0175 0.0941  -0.0109 87  ASN   A O   
1787 C CB  . ASN   A 87  ? 0.2623 0.2212 0.1536 0.0031  0.0433  -0.0218 87  ASN   A CB  
1788 C CG  . ASN   A 87  ? 0.2752 0.2315 0.1556 0.0142  0.0518  -0.0100 87  ASN   A CG  
1789 O OD1 . ASN   A 87  ? 0.2954 0.2327 0.1716 0.0339  0.0508  -0.0015 87  ASN   A OD1 
1790 N ND2 . ASN   A 87  ? 0.2770 0.2541 0.1753 0.0134  0.0506  -0.0022 87  ASN   A ND2 
1797 N N   . LEU   A 88  ? 0.2169 0.2167 0.1535 -0.0238 0.0297  0.0082  88  LEU   A N   
1798 C CA  . LEU   A 88  ? 0.2019 0.2159 0.1786 -0.0369 0.0205  0.0254  88  LEU   A CA  
1799 C C   . LEU   A 88  ? 0.1952 0.2152 0.1641 -0.0343 0.0206  0.0349  88  LEU   A C   
1800 O O   . LEU   A 88  ? 0.1990 0.2243 0.2076 -0.0298 0.0262  0.0509  88  LEU   A O   
1801 C CB  . LEU   A 88  ? 0.2081 0.2253 0.1984 -0.0514 -0.0098 0.0418  88  LEU   A CB  
1802 C CG  . LEU   A 88  ? 0.2277 0.2427 0.2398 -0.0516 -0.0224 0.0457  88  LEU   A CG  
1803 C CD1 . LEU   A 88  ? 0.2433 0.2510 0.2388 -0.0493 -0.0325 0.0337  88  LEU   A CD1 
1804 C CD2 . LEU   A 88  ? 0.2388 0.2519 0.2754 -0.0428 -0.0248 0.0409  88  LEU   A CD2 
1816 N N   . ALA   A 89  ? 0.1960 0.2020 0.1406 -0.0310 0.0119  0.0071  89  ALA   A N   
1817 C CA  . ALA   A 89  ? 0.2042 0.1985 0.1246 -0.0257 0.0054  0.0167  89  ALA   A CA  
1818 C C   . ALA   A 89  ? 0.2110 0.2051 0.1326 -0.0217 -0.0125 0.0160  89  ALA   A C   
1819 O O   . ALA   A 89  ? 0.2068 0.1972 0.1732 -0.0260 -0.0188 -0.0114 89  ALA   A O   
1820 C CB  . ALA   A 89  ? 0.1989 0.1993 0.1263 -0.0235 0.0058  0.0168  89  ALA   A CB  
1826 N N   . LYS   A 90  ? 0.2180 0.2192 0.1310 -0.0283 -0.0273 0.0214  90  LYS   A N   
1827 C CA  . LYS   A 90  ? 0.2265 0.2341 0.1411 -0.0243 -0.0383 0.0175  90  LYS   A CA  
1828 C C   . LYS   A 90  ? 0.2021 0.2140 0.1419 -0.0249 -0.0267 0.0092  90  LYS   A C   
1829 O O   . LYS   A 90  ? 0.2015 0.2263 0.1734 -0.0277 -0.0272 0.0022  90  LYS   A O   
1830 C CB  . LYS   A 90  ? 0.2575 0.2721 0.1816 -0.0230 -0.0418 0.0361  90  LYS   A CB  
1831 C CG  . LYS   A 90  ? 0.2916 0.3047 0.2831 -0.0256 -0.0334 0.0450  90  LYS   A CG  
1832 C CD  . LYS   A 90  ? 0.3237 0.3311 0.3865 -0.0303 -0.0184 0.0487  90  LYS   A CD  
1833 C CE  . LYS   A 90  ? 0.3540 0.3597 0.4655 -0.0332 -0.0081 0.0463  90  LYS   A CE  
1834 N NZ  . LYS   A 90  ? 0.3672 0.3775 0.5158 -0.0331 -0.0026 0.0413  90  LYS   A NZ  
1848 N N   . HIS   A 91  ? 0.1877 0.1887 0.1160 -0.0210 -0.0286 0.0151  91  HIS   A N   
1849 C CA  . HIS   A 91  ? 0.1732 0.1706 0.1292 -0.0142 -0.0258 0.0223  91  HIS   A CA  
1850 C C   . HIS   A 91  ? 0.1523 0.1538 0.1197 -0.0165 -0.0094 0.0133  91  HIS   A C   
1851 O O   . HIS   A 91  ? 0.1542 0.1724 0.1185 -0.0216 -0.0021 0.0145  91  HIS   A O   
1852 C CB  . HIS   A 91  ? 0.1889 0.1995 0.1817 0.0056  -0.0414 0.0245  91  HIS   A CB  
1853 C CG  . HIS   A 91  ? 0.2274 0.2483 0.2556 0.0185  -0.0746 0.0146  91  HIS   A CG  
1854 N ND1 . HIS   A 91  ? 0.2377 0.2764 0.2920 0.0208  -0.0866 -0.0040 91  HIS   A ND1 
1855 C CD2 . HIS   A 91  ? 0.2511 0.2681 0.2822 0.0234  -0.0843 0.0211  91  HIS   A CD2 
1856 C CE1 . HIS   A 91  ? 0.2476 0.2832 0.3045 0.0251  -0.0869 0.0081  91  HIS   A CE1 
1857 N NE2 . HIS   A 91  ? 0.2605 0.2826 0.3012 0.0288  -0.0885 0.0154  91  HIS   A NE2 
1865 N N   . CYS   A 92  ? 0.1406 0.1484 0.1247 -0.0167 -0.0071 0.0161  92  CYS   A N   
1866 C CA  . CYS   A 92  ? 0.1323 0.1424 0.1310 -0.0118 -0.0034 0.0154  92  CYS   A CA  
1867 C C   . CYS   A 92  ? 0.1301 0.1382 0.1250 -0.0093 -0.0024 0.0158  92  CYS   A C   
1868 O O   . CYS   A 92  ? 0.1316 0.1429 0.1395 -0.0127 -0.0047 0.0071  92  CYS   A O   
1869 C CB  . CYS   A 92  ? 0.1420 0.1440 0.1400 -0.0031 -0.0064 0.0066  92  CYS   A CB  
1870 S SG  . CYS   A 92  ? 0.1367 0.1314 0.1414 -0.0083 -0.0029 0.0102  92  CYS   A SG  
1876 N N   . LEU   A 93  ? 0.1296 0.1249 0.1242 -0.0076 0.0043  0.0120  93  LEU   A N   
1877 C CA  . LEU   A 93  ? 0.1217 0.1211 0.1241 -0.0049 0.0009  0.0151  93  LEU   A CA  
1878 C C   . LEU   A 93  ? 0.1204 0.1135 0.1227 0.0008  -0.0015 0.0117  93  LEU   A C   
1879 O O   . LEU   A 93  ? 0.1139 0.1268 0.1192 0.0007  0.0014  0.0116  93  LEU   A O   
1880 C CB  . LEU   A 93  ? 0.1246 0.1225 0.1380 -0.0046 -0.0034 0.0219  93  LEU   A CB  
1881 C CG  . LEU   A 93  ? 0.1344 0.1249 0.1454 -0.0012 0.0032  0.0232  93  LEU   A CG  
1882 C CD1 . LEU   A 93  ? 0.1380 0.1316 0.1717 0.0023  0.0062  0.0102  93  LEU   A CD1 
1883 C CD2 . LEU   A 93  ? 0.1470 0.1279 0.1574 -0.0059 -0.0036 0.0173  93  LEU   A CD2 
1895 N N   . HIS   A 94  ? 0.1146 0.1108 0.1285 -0.0023 0.0042  0.0162  94  HIS   A N   
1896 C CA  . HIS   A 94  ? 0.1147 0.1106 0.1279 -0.0045 -0.0026 0.0125  94  HIS   A CA  
1897 C C   . HIS   A 94  ? 0.1158 0.1116 0.1214 -0.0005 -0.0012 0.0070  94  HIS   A C   
1898 O O   . HIS   A 94  ? 0.1145 0.1334 0.1586 0.0020  0.0022  -0.0091 94  HIS   A O   
1899 C CB  . HIS   A 94  ? 0.1097 0.1103 0.1373 0.0003  -0.0065 0.0122  94  HIS   A CB  
1900 C CG  . HIS   A 94  ? 0.1157 0.1146 0.1290 -0.0040 -0.0065 0.0146  94  HIS   A CG  
1901 N ND1 . HIS   A 94  ? 0.1170 0.1161 0.1344 -0.0030 -0.0003 0.0131  94  HIS   A ND1 
1902 C CD2 . HIS   A 94  ? 0.1253 0.1244 0.1376 0.0029  -0.0076 0.0080  94  HIS   A CD2 
1903 C CE1 . HIS   A 94  ? 0.1209 0.1164 0.1321 -0.0085 -0.0075 0.0031  94  HIS   A CE1 
1904 N NE2 . HIS   A 94  ? 0.1293 0.1198 0.1424 -0.0057 -0.0086 -0.0007 94  HIS   A NE2 
1912 N N   . VAL   A 95  ? 0.1115 0.1075 0.1121 -0.0028 0.0048  0.0038  95  VAL   A N   
1913 C CA  . VAL   A 95  ? 0.1212 0.1126 0.1143 -0.0005 0.0071  0.0075  95  VAL   A CA  
1914 C C   . VAL   A 95  ? 0.1188 0.1134 0.1055 -0.0084 0.0069  0.0101  95  VAL   A C   
1915 O O   . VAL   A 95  ? 0.1230 0.1230 0.1215 0.0103  0.0106  0.0052  95  VAL   A O   
1916 C CB  . VAL   A 95  ? 0.1231 0.1121 0.1356 -0.0068 0.0050  0.0103  95  VAL   A CB  
1917 C CG1 . VAL   A 95  ? 0.1345 0.1185 0.1489 -0.0116 0.0035  0.0008  95  VAL   A CG1 
1918 C CG2 . VAL   A 95  ? 0.1295 0.1156 0.1374 -0.0095 0.0101  0.0197  95  VAL   A CG2 
1928 N N   . VAL   A 96  ? 0.1220 0.1127 0.1088 -0.0056 0.0108  0.0097  96  VAL   A N   
1929 C CA  . VAL   A 96  ? 0.1328 0.1115 0.1224 0.0003  0.0156  0.0183  96  VAL   A CA  
1930 C C   . VAL   A 96  ? 0.1368 0.1186 0.1090 0.0014  0.0170  0.0198  96  VAL   A C   
1931 O O   . VAL   A 96  ? 0.1443 0.1245 0.1402 -0.0031 0.0197  -0.0001 96  VAL   A O   
1932 C CB  . VAL   A 96  ? 0.1353 0.1190 0.1304 -0.0020 0.0249  0.0134  96  VAL   A CB  
1933 C CG1 . VAL   A 96  ? 0.1433 0.1287 0.1193 0.0003  0.0181  0.0140  96  VAL   A CG1 
1934 C CG2 . VAL   A 96  ? 0.1326 0.1275 0.1405 -0.0104 0.0210  0.0134  96  VAL   A CG2 
1944 N N   . GLY   A 97  ? 0.1354 0.1212 0.1226 -0.0029 0.0112  0.0076  97  GLY   A N   
1945 C CA  . GLY   A 97  ? 0.1444 0.1305 0.1197 0.0003  0.0059  0.0116  97  GLY   A CA  
1946 C C   . GLY   A 97  ? 0.1506 0.1424 0.1124 -0.0049 0.0086  0.0057  97  GLY   A C   
1947 O O   . GLY   A 97  ? 0.1608 0.1414 0.1299 -0.0044 0.0028  0.0158  97  GLY   A O   
1951 N N   A PRO   A 98  ? 0.1527 0.1475 0.1006 0.0010  0.0013  0.0160  98  PRO   A N   
1952 N N   B PRO   A 98  ? 0.1561 0.1410 0.1134 0.0017  0.0089  0.0147  98  PRO   A N   
1953 C CA  A PRO   A 98  ? 0.1668 0.1668 0.1148 -0.0016 0.0009  0.0063  98  PRO   A CA  
1954 C CA  B PRO   A 98  ? 0.1655 0.1475 0.1260 -0.0010 0.0054  0.0157  98  PRO   A CA  
1955 C C   A PRO   A 98  ? 0.1732 0.1732 0.1025 -0.0098 0.0025  0.0113  98  PRO   A C   
1956 C C   B PRO   A 98  ? 0.1802 0.1498 0.1338 -0.0060 -0.0035 0.0285  98  PRO   A C   
1957 O O   A PRO   A 98  ? 0.1663 0.1571 0.1105 -0.0053 0.0091  0.0086  98  PRO   A O   
1958 O O   B PRO   A 98  ? 0.1789 0.1446 0.1427 -0.0041 -0.0046 0.0264  98  PRO   A O   
1959 C CB  A PRO   A 98  ? 0.1768 0.1786 0.1108 0.0082  -0.0071 -0.0038 98  PRO   A CB  
1960 C CB  B PRO   A 98  ? 0.1649 0.1499 0.1206 0.0076  0.0069  0.0087  98  PRO   A CB  
1961 C CG  A PRO   A 98  ? 0.1692 0.1710 0.1202 0.0084  -0.0081 -0.0099 98  PRO   A CG  
1962 C CG  B PRO   A 98  ? 0.1649 0.1480 0.1219 0.0080  0.0082  0.0069  98  PRO   A CG  
1963 C CD  A PRO   A 98  ? 0.1569 0.1551 0.1092 0.0050  -0.0061 0.0072  98  PRO   A CD  
1964 C CD  B PRO   A 98  ? 0.1571 0.1412 0.1147 0.0059  0.0072  0.0129  98  PRO   A CD  
1979 N N   A ASN   A 99  ? 0.1822 0.1981 0.1157 -0.0093 -0.0000 0.0309  99  ASN   A N   
1980 N N   B ASN   A 99  ? 0.1964 0.1600 0.1370 -0.0087 -0.0066 0.0459  99  ASN   A N   
1981 C CA  A ASN   A 99  ? 0.2046 0.2102 0.1292 -0.0116 -0.0051 0.0438  99  ASN   A CA  
1982 C CA  B ASN   A 99  ? 0.2146 0.1692 0.1441 -0.0062 -0.0149 0.0634  99  ASN   A CA  
1983 C C   A ASN   A 99  ? 0.2259 0.2398 0.1208 -0.0257 -0.0054 0.0498  99  ASN   A C   
1984 C C   B ASN   A 99  ? 0.2243 0.1834 0.1406 0.0011  -0.0171 0.0666  99  ASN   A C   
1985 O O   A ASN   A 99  ? 0.2304 0.2615 0.1316 -0.0150 -0.0113 0.0391  99  ASN   A O   
1986 O O   B ASN   A 99  ? 0.2243 0.1775 0.1350 0.0139  -0.0187 0.0686  99  ASN   A O   
1987 C CB  A ASN   A 99  ? 0.2046 0.1992 0.1359 -0.0140 -0.0123 0.0451  99  ASN   A CB  
1988 C CB  B ASN   A 99  ? 0.2217 0.1710 0.1715 -0.0120 -0.0241 0.0720  99  ASN   A CB  
1989 C CG  A ASN   A 99  ? 0.2043 0.1919 0.1535 -0.0126 -0.0239 0.0298  99  ASN   A CG  
1990 C CG  B ASN   A 99  ? 0.2271 0.1764 0.1913 -0.0137 -0.0282 0.0756  99  ASN   A CG  
1991 O OD1 A ASN   A 99  ? 0.2152 0.2043 0.1451 -0.0027 -0.0205 0.0242  99  ASN   A OD1 
1992 O OD1 B ASN   A 99  ? 0.2298 0.1784 0.1809 -0.0167 -0.0260 0.0848  99  ASN   A OD1 
1993 N ND2 A ASN   A 99  ? 0.2012 0.1827 0.1909 -0.0149 -0.0271 0.0236  99  ASN   A ND2 
1994 N ND2 B ASN   A 99  ? 0.2290 0.1842 0.2096 -0.0078 -0.0292 0.0683  99  ASN   A ND2 
2007 N N   A VAL   A 100 ? 0.2493 0.2475 0.1158 -0.0469 -0.0296 0.0375  100 VAL   A N   
2008 N N   B VAL   A 100 ? 0.2343 0.2086 0.1507 -0.0026 -0.0275 0.0579  100 VAL   A N   
2009 C CA  A VAL   A 100 ? 0.2800 0.2649 0.1461 -0.0499 -0.0436 0.0374  100 VAL   A CA  
2010 C CA  B VAL   A 100 ? 0.2484 0.2392 0.1845 -0.0047 -0.0359 0.0480  100 VAL   A CA  
2011 C C   A VAL   A 100 ? 0.2917 0.2727 0.1343 -0.0534 -0.0469 0.0647  100 VAL   A C   
2012 C C   B VAL   A 100 ? 0.2549 0.2632 0.2009 -0.0072 -0.0393 0.0570  100 VAL   A C   
2013 O O   A VAL   A 100 ? 0.3018 0.2753 0.1561 -0.0497 -0.0287 0.0663  100 VAL   A O   
2014 O O   B VAL   A 100 ? 0.2575 0.2724 0.2117 -0.0027 -0.0306 0.0499  100 VAL   A O   
2015 C CB  A VAL   A 100 ? 0.2999 0.2692 0.1851 -0.0508 -0.0527 0.0302  100 VAL   A CB  
2016 C CB  B VAL   A 100 ? 0.2550 0.2424 0.2042 -0.0026 -0.0402 0.0351  100 VAL   A CB  
2017 C CG1 A VAL   A 100 ? 0.3012 0.2736 0.2025 -0.0523 -0.0468 0.0308  100 VAL   A CG1 
2018 C CG1 B VAL   A 100 ? 0.2562 0.2435 0.2159 -0.0045 -0.0386 0.0314  100 VAL   A CG1 
2019 C CG2 A VAL   A 100 ? 0.3132 0.2748 0.2058 -0.0508 -0.0507 0.0269  100 VAL   A CG2 
2020 C CG2 B VAL   A 100 ? 0.2574 0.2447 0.2131 -0.0009 -0.0415 0.0301  100 VAL   A CG2 
2039 N N   A ASN   A 101 ? 0.2968 0.2857 0.1625 -0.0591 -0.0518 0.0893  101 ASN   A N   
2040 N N   B ASN   A 101 ? 0.2613 0.2721 0.2145 -0.0150 -0.0459 0.0721  101 ASN   A N   
2041 C CA  A ASN   A 101 ? 0.3150 0.3038 0.1892 -0.0642 -0.0543 0.1079  101 ASN   A CA  
2042 C CA  B ASN   A 101 ? 0.2717 0.2792 0.2291 -0.0205 -0.0510 0.0804  101 ASN   A CA  
2043 C C   A ASN   A 101 ? 0.3375 0.3337 0.2143 -0.0698 -0.0209 0.1431  101 ASN   A C   
2044 C C   B ASN   A 101 ? 0.2832 0.2960 0.2356 -0.0254 -0.0395 0.0893  101 ASN   A C   
2045 O O   A ASN   A 101 ? 0.3499 0.3347 0.2487 -0.0695 -0.0153 0.1424  101 ASN   A O   
2046 O O   B ASN   A 101 ? 0.2854 0.2926 0.2253 -0.0221 -0.0416 0.1037  101 ASN   A O   
2047 C CB  A ASN   A 101 ? 0.3132 0.2921 0.1949 -0.0563 -0.0771 0.0888  101 ASN   A CB  
2048 C CB  B ASN   A 101 ? 0.2723 0.2676 0.2325 -0.0217 -0.0615 0.0776  101 ASN   A CB  
2049 C CG  A ASN   A 101 ? 0.3118 0.2792 0.1886 -0.0503 -0.0929 0.0685  101 ASN   A CG  
2050 C CG  B ASN   A 101 ? 0.2738 0.2563 0.2341 -0.0243 -0.0666 0.0709  101 ASN   A CG  
2051 O OD1 A ASN   A 101 ? 0.3104 0.2826 0.2027 -0.0389 -0.0902 0.0342  101 ASN   A OD1 
2052 O OD1 B ASN   A 101 ? 0.2762 0.2548 0.2434 -0.0281 -0.0615 0.0665  101 ASN   A OD1 
2053 N ND2 A ASN   A 101 ? 0.3125 0.2713 0.1977 -0.0540 -0.0933 0.0660  101 ASN   A ND2 
2054 N ND2 B ASN   A 101 ? 0.2750 0.2496 0.2392 -0.0261 -0.0681 0.0630  101 ASN   A ND2 
2067 N N   A LYS   A 102 ? 0.3494 0.3763 0.2419 -0.0780 -0.0076 0.1434  102 LYS   A N   
2068 N N   B LYS   A 102 ? 0.2924 0.3155 0.2643 -0.0368 -0.0257 0.0712  102 LYS   A N   
2069 C CA  A LYS   A 102 ? 0.3639 0.4142 0.2551 -0.0732 -0.0085 0.1312  102 LYS   A CA  
2070 C CA  B LYS   A 102 ? 0.3039 0.3340 0.2876 -0.0448 -0.0139 0.0509  102 LYS   A CA  
2071 C C   A LYS   A 102 ? 0.3667 0.4363 0.2318 -0.0632 -0.0085 0.1241  102 LYS   A C   
2072 C C   B LYS   A 102 ? 0.3091 0.3454 0.2930 -0.0471 -0.0090 0.0419  102 LYS   A C   
2073 O O   A LYS   A 102 ? 0.3699 0.4482 0.2405 -0.0592 -0.0033 0.1184  102 LYS   A O   
2074 O O   B LYS   A 102 ? 0.3118 0.3488 0.2980 -0.0470 -0.0093 0.0382  102 LYS   A O   
2075 C CB  A LYS   A 102 ? 0.3778 0.4296 0.3054 -0.0763 -0.0183 0.1046  102 LYS   A CB  
2076 C CB  B LYS   A 102 ? 0.3115 0.3405 0.3064 -0.0486 -0.0116 0.0354  102 LYS   A CB  
2077 C CG  A LYS   A 102 ? 0.3890 0.4413 0.3485 -0.0772 -0.0268 0.0753  102 LYS   A CG  
2078 C CG  B LYS   A 102 ? 0.3185 0.3460 0.3227 -0.0511 -0.0092 0.0215  102 LYS   A CG  
2079 C CD  A LYS   A 102 ? 0.4007 0.4519 0.3849 -0.0767 -0.0382 0.0471  102 LYS   A CD  
2080 C CD  B LYS   A 102 ? 0.3258 0.3505 0.3345 -0.0525 -0.0089 0.0088  102 LYS   A CD  
2081 C CE  A LYS   A 102 ? 0.4105 0.4598 0.4135 -0.0761 -0.0451 0.0266  102 LYS   A CE  
2082 C CE  B LYS   A 102 ? 0.3315 0.3534 0.3432 -0.0529 -0.0075 -0.0008 102 LYS   A CE  
2083 N NZ  A LYS   A 102 ? 0.4157 0.4635 0.4285 -0.0780 -0.0456 0.0134  102 LYS   A NZ  
2084 N NZ  B LYS   A 102 ? 0.3343 0.3543 0.3473 -0.0544 -0.0053 -0.0068 102 LYS   A NZ  
2111 N N   A GLY   A 103 ? 0.3625 0.4474 0.2303 -0.0541 -0.0158 0.0984  103 GLY   A N   
2112 N N   B GLY   A 103 ? 0.3100 0.3525 0.2940 -0.0487 -0.0054 0.0336  103 GLY   A N   
2113 C CA  A GLY   A 103 ? 0.3577 0.4522 0.2157 -0.0467 -0.0152 0.0765  103 GLY   A CA  
2114 C CA  B GLY   A 103 ? 0.3105 0.3580 0.2876 -0.0505 -0.0025 0.0263  103 GLY   A CA  
2115 C C   A GLY   A 103 ? 0.3495 0.4562 0.2090 -0.0434 -0.0056 0.0509  103 GLY   A C   
2116 C C   B GLY   A 103 ? 0.3119 0.3643 0.2859 -0.0499 -0.0004 0.0193  103 GLY   A C   
2117 O O   A GLY   A 103 ? 0.3555 0.4614 0.2291 -0.0403 -0.0031 0.0355  103 GLY   A O   
2118 O O   B GLY   A 103 ? 0.3138 0.3660 0.2930 -0.0517 -0.0017 0.0149  103 GLY   A O   
2125 N N   A GLU   A 104 ? 0.3316 0.4495 0.1640 -0.0459 0.0071  0.0392  104 GLU   A N   
2126 N N   B GLU   A 104 ? 0.3111 0.3665 0.2660 -0.0469 0.0036  0.0181  104 GLU   A N   
2127 C CA  A GLU   A 104 ? 0.3087 0.4370 0.1463 -0.0537 0.0131  0.0243  104 GLU   A CA  
2128 C CA  B GLU   A 104 ? 0.3105 0.3674 0.2526 -0.0444 0.0042  0.0131  104 GLU   A CA  
2129 C C   A GLU   A 104 ? 0.3055 0.4436 0.1360 -0.0554 0.0175  -0.0022 104 GLU   A C   
2130 C C   B GLU   A 104 ? 0.3171 0.3727 0.2546 -0.0382 0.0080  0.0058  104 GLU   A C   
2131 O O   A GLU   A 104 ? 0.2999 0.4468 0.1615 -0.0555 0.0041  -0.0155 104 GLU   A O   
2132 O O   B GLU   A 104 ? 0.3167 0.3734 0.2536 -0.0374 0.0054  0.0045  104 GLU   A O   
2133 C CB  A GLU   A 104 ? 0.2848 0.4168 0.1327 -0.0622 0.0184  0.0455  104 GLU   A CB  
2134 C CB  B GLU   A 104 ? 0.3032 0.3631 0.2409 -0.0467 0.0008  0.0159  104 GLU   A CB  
2135 C CG  A GLU   A 104 ? 0.2657 0.3970 0.1447 -0.0655 0.0116  0.0653  104 GLU   A CG  
2136 C CG  B GLU   A 104 ? 0.2975 0.3591 0.2378 -0.0475 -0.0040 0.0187  104 GLU   A CG  
2137 C CD  A GLU   A 104 ? 0.2442 0.3777 0.1397 -0.0705 0.0088  0.0827  104 GLU   A CD  
2138 C CD  B GLU   A 104 ? 0.2917 0.3547 0.2347 -0.0490 -0.0075 0.0213  104 GLU   A CD  
2139 O OE1 A GLU   A 104 ? 0.2280 0.3553 0.1311 -0.0684 -0.0010 0.0807  104 GLU   A OE1 
2140 O OE1 B GLU   A 104 ? 0.2886 0.3518 0.2275 -0.0501 -0.0106 0.0240  104 GLU   A OE1 
2141 O OE2 A GLU   A 104 ? 0.2490 0.3755 0.1657 -0.0715 0.0128  0.0978  104 GLU   A OE2 
2142 O OE2 B GLU   A 104 ? 0.2929 0.3545 0.2427 -0.0478 -0.0068 0.0215  104 GLU   A OE2 
2155 N N   A ASP   A 105 ? 0.3092 0.4461 0.1509 -0.0540 0.0339  -0.0220 105 ASP   A N   
2156 N N   B ASP   A 105 ? 0.3262 0.3780 0.2716 -0.0325 0.0135  -0.0021 105 ASP   A N   
2157 C CA  A ASP   A 105 ? 0.3069 0.4409 0.1987 -0.0477 0.0417  -0.0456 105 ASP   A CA  
2158 C CA  B ASP   A 105 ? 0.3325 0.3818 0.2937 -0.0276 0.0196  -0.0122 105 ASP   A CA  
2159 C C   A ASP   A 105 ? 0.2712 0.4156 0.1694 -0.0540 0.0280  -0.0543 105 ASP   A C   
2160 C C   B ASP   A 105 ? 0.3257 0.3747 0.2757 -0.0310 0.0162  -0.0157 105 ASP   A C   
2161 O O   A ASP   A 105 ? 0.2453 0.3845 0.1267 -0.0511 0.0228  -0.0757 105 ASP   A O   
2162 O O   B ASP   A 105 ? 0.3240 0.3738 0.2604 -0.0298 0.0188  -0.0171 105 ASP   A O   
2163 C CB  A ASP   A 105 ? 0.3359 0.4644 0.2808 -0.0379 0.0578  -0.0616 105 ASP   A CB  
2164 C CB  B ASP   A 105 ? 0.3441 0.3907 0.3354 -0.0210 0.0298  -0.0200 105 ASP   A CB  
2165 C CG  A ASP   A 105 ? 0.3628 0.4798 0.3533 -0.0281 0.0631  -0.0767 105 ASP   A CG  
2166 C CG  B ASP   A 105 ? 0.3530 0.3978 0.3743 -0.0160 0.0369  -0.0276 105 ASP   A CG  
2167 O OD1 A ASP   A 105 ? 0.3701 0.4852 0.3628 -0.0279 0.0639  -0.0887 105 ASP   A OD1 
2168 O OD1 B ASP   A 105 ? 0.3559 0.4006 0.3848 -0.0164 0.0379  -0.0322 105 ASP   A OD1 
2169 O OD2 A ASP   A 105 ? 0.3775 0.4865 0.3995 -0.0249 0.0659  -0.0746 105 ASP   A OD2 
2170 O OD2 B ASP   A 105 ? 0.3570 0.4007 0.3919 -0.0143 0.0430  -0.0282 105 ASP   A OD2 
2179 N N   A ILE   A 106 ? 0.2554 0.4059 0.1934 -0.0607 0.0043  -0.0496 106 ILE   A N   
2180 N N   B ILE   A 106 ? 0.3190 0.3669 0.2766 -0.0364 0.0075  -0.0207 106 ILE   A N   
2181 C CA  A ILE   A 106 ? 0.2302 0.3931 0.2182 -0.0723 -0.0151 -0.0561 106 ILE   A CA  
2182 C CA  B ILE   A 106 ? 0.3094 0.3568 0.2809 -0.0428 0.0014  -0.0291 106 ILE   A CA  
2183 C C   A ILE   A 106 ? 0.2149 0.3690 0.2196 -0.0863 -0.0125 -0.0838 106 ILE   A C   
2184 C C   B ILE   A 106 ? 0.3007 0.3424 0.2801 -0.0475 0.0102  -0.0453 106 ILE   A C   
2185 O O   A ILE   A 106 ? 0.1933 0.3580 0.2194 -0.0901 0.0012  -0.0884 106 ILE   A O   
2186 O O   B ILE   A 106 ? 0.2975 0.3389 0.2726 -0.0480 0.0116  -0.0502 106 ILE   A O   
2187 C CB  A ILE   A 106 ? 0.2270 0.4000 0.2619 -0.0624 -0.0331 -0.0256 106 ILE   A CB  
2188 C CB  B ILE   A 106 ? 0.3096 0.3601 0.2936 -0.0423 -0.0111 -0.0190 106 ILE   A CB  
2189 C CG1 A ILE   A 106 ? 0.2171 0.3985 0.2826 -0.0489 -0.0363 0.0003  106 ILE   A CG1 
2190 C CG1 B ILE   A 106 ? 0.3075 0.3586 0.3001 -0.0418 -0.0162 -0.0118 106 ILE   A CG1 
2191 C CG2 A ILE   A 106 ? 0.2340 0.4048 0.2774 -0.0610 -0.0405 -0.0228 106 ILE   A CG2 
2192 C CG2 B ILE   A 106 ? 0.3117 0.3625 0.2982 -0.0415 -0.0144 -0.0172 106 ILE   A CG2 
2193 C CD1 A ILE   A 106 ? 0.2156 0.3958 0.2958 -0.0354 -0.0269 0.0151  106 ILE   A CD1 
2194 C CD1 B ILE   A 106 ? 0.3070 0.3562 0.3036 -0.0408 -0.0163 -0.0078 106 ILE   A CD1 
2217 N N   A GLN   A 107 ? 0.2348 0.3548 0.2433 -0.0863 0.0018  -0.1021 107 GLN   A N   
2218 N N   B GLN   A 107 ? 0.2956 0.3303 0.2931 -0.0505 0.0208  -0.0548 107 GLN   A N   
2219 C CA  A GLN   A 107 ? 0.2616 0.3391 0.3232 -0.0719 0.0260  -0.0971 107 GLN   A CA  
2220 C CA  B GLN   A 107 ? 0.2899 0.3157 0.3191 -0.0500 0.0310  -0.0613 107 GLN   A CA  
2221 C C   A GLN   A 107 ? 0.2395 0.2873 0.3051 -0.0623 0.0493  -0.0755 107 GLN   A C   
2222 C C   B GLN   A 107 ? 0.2533 0.2787 0.2851 -0.0528 0.0449  -0.0633 107 GLN   A C   
2223 O O   A GLN   A 107 ? 0.2474 0.2775 0.3649 -0.0551 0.0588  -0.0712 107 GLN   A O   
2224 O O   B GLN   A 107 ? 0.2581 0.2770 0.3099 -0.0499 0.0506  -0.0597 107 GLN   A O   
2225 C CB  A GLN   A 107 ? 0.3015 0.3690 0.4291 -0.0750 0.0159  -0.0967 107 GLN   A CB  
2226 C CB  B GLN   A 107 ? 0.3169 0.3353 0.3825 -0.0487 0.0235  -0.0576 107 GLN   A CB  
2227 C CG  A GLN   A 107 ? 0.3396 0.3983 0.5409 -0.0727 0.0075  -0.0868 107 GLN   A CG  
2228 C CG  B GLN   A 107 ? 0.3408 0.3537 0.4472 -0.0461 0.0163  -0.0521 107 GLN   A CG  
2229 C CD  A GLN   A 107 ? 0.3719 0.4239 0.6364 -0.0712 0.0033  -0.0736 107 GLN   A CD  
2230 C CD  B GLN   A 107 ? 0.3606 0.3690 0.5020 -0.0439 0.0114  -0.0449 107 GLN   A CD  
2231 O OE1 A GLN   A 107 ? 0.3848 0.4310 0.6740 -0.0703 0.0016  -0.0703 107 GLN   A OE1 
2232 O OE1 B GLN   A 107 ? 0.3673 0.3733 0.5235 -0.0431 0.0103  -0.0425 107 GLN   A OE1 
2233 N NE2 A GLN   A 107 ? 0.3819 0.4348 0.6694 -0.0730 0.0001  -0.0714 107 GLN   A NE2 
2234 N NE2 B GLN   A 107 ? 0.3679 0.3754 0.5205 -0.0442 0.0099  -0.0438 107 GLN   A NE2 
2251 N N   . LEU   A 108 ? 0.2113 0.2413 0.2389 -0.0572 0.0477  -0.0703 108 LEU   A N   
2252 C CA  . LEU   A 108 ? 0.1781 0.1828 0.1994 -0.0200 0.0402  -0.0207 108 LEU   A CA  
2253 C C   . LEU   A 108 ? 0.1579 0.1461 0.1884 -0.0059 0.0277  0.0143  108 LEU   A C   
2254 O O   . LEU   A 108 ? 0.1528 0.1443 0.2062 0.0017  0.0377  0.0144  108 LEU   A O   
2255 C CB  . LEU   A 108 ? 0.1806 0.1881 0.1796 -0.0247 0.0394  -0.0132 108 LEU   A CB  
2256 C CG  . LEU   A 108 ? 0.1980 0.2109 0.1998 -0.0187 0.0564  -0.0119 108 LEU   A CG  
2257 C CD1 . LEU   A 108 ? 0.2178 0.2181 0.2003 -0.0281 0.0646  -0.0095 108 LEU   A CD1 
2258 C CD2 . LEU   A 108 ? 0.1999 0.2310 0.2455 -0.0110 0.0471  0.0047  108 LEU   A CD2 
2271 N N   . LEU   A 109 ? 0.1454 0.1455 0.1800 0.0074  0.0260  0.0258  109 LEU   A N   
2272 C CA  . LEU   A 109 ? 0.1374 0.1390 0.1686 0.0049  0.0124  0.0284  109 LEU   A CA  
2273 C C   . LEU   A 109 ? 0.1274 0.1328 0.1654 -0.0033 0.0121  0.0147  109 LEU   A C   
2274 O O   . LEU   A 109 ? 0.1349 0.1211 0.1791 0.0011  0.0016  0.0087  109 LEU   A O   
2275 C CB  . LEU   A 109 ? 0.1443 0.1556 0.1911 0.0110  0.0065  0.0446  109 LEU   A CB  
2276 C CG  . LEU   A 109 ? 0.1403 0.1599 0.1955 0.0132  0.0156  0.0480  109 LEU   A CG  
2277 C CD1 . LEU   A 109 ? 0.1465 0.1466 0.2088 0.0151  0.0278  0.0302  109 LEU   A CD1 
2278 C CD2 . LEU   A 109 ? 0.1458 0.1822 0.2102 0.0139  0.0124  0.0461  109 LEU   A CD2 
2290 N N   . LYS   A 110 ? 0.1293 0.1317 0.1582 -0.0007 0.0017  0.0080  110 LYS   A N   
2291 C CA  . LYS   A 110 ? 0.1256 0.1231 0.1598 -0.0045 -0.0038 0.0138  110 LYS   A CA  
2292 C C   . LYS   A 110 ? 0.1308 0.1218 0.1455 -0.0025 0.0030  0.0045  110 LYS   A C   
2293 O O   . LYS   A 110 ? 0.1254 0.1201 0.1591 -0.0053 0.0074  0.0014  110 LYS   A O   
2294 C CB  . LYS   A 110 ? 0.1323 0.1338 0.1725 -0.0079 -0.0062 0.0030  110 LYS   A CB  
2295 C CG  . LYS   A 110 ? 0.1381 0.1318 0.1823 -0.0026 0.0003  -0.0029 110 LYS   A CG  
2296 C CD  . LYS   A 110 ? 0.1400 0.1347 0.1970 -0.0094 -0.0029 -0.0005 110 LYS   A CD  
2297 C CE  . LYS   A 110 ? 0.1504 0.1401 0.2232 -0.0069 0.0141  -0.0059 110 LYS   A CE  
2298 N NZ  . LYS   A 110 ? 0.1523 0.1431 0.2246 -0.0112 0.0224  -0.0012 110 LYS   A NZ  
2312 N N   . SER   A 111 ? 0.1279 0.1274 0.1493 -0.0015 0.0017  0.0107  111 SER   A N   
2313 C CA  . SER   A 111 ? 0.1230 0.1311 0.1604 -0.0016 0.0069  0.0054  111 SER   A CA  
2314 C C   . SER   A 111 ? 0.1151 0.1220 0.1569 -0.0034 0.0069  0.0088  111 SER   A C   
2315 O O   . SER   A 111 ? 0.1279 0.1159 0.1741 -0.0007 0.0088  0.0124  111 SER   A O   
2316 C CB  . SER   A 111 ? 0.1432 0.1511 0.1748 -0.0065 0.0239  -0.0046 111 SER   A CB  
2317 O OG  . SER   A 111 ? 0.1834 0.1746 0.1883 -0.0050 0.0307  -0.0133 111 SER   A OG  
2323 N N   . ALA   A 112 ? 0.1200 0.1183 0.1616 -0.0001 0.0130  0.0089  112 ALA   A N   
2324 C CA  . ALA   A 112 ? 0.1249 0.1164 0.1577 -0.0018 0.0140  0.0083  112 ALA   A CA  
2325 C C   . ALA   A 112 ? 0.1177 0.1099 0.1645 0.0019  0.0124  0.0067  112 ALA   A C   
2326 O O   . ALA   A 112 ? 0.1239 0.1086 0.1645 -0.0077 0.0140  0.0129  112 ALA   A O   
2327 C CB  . ALA   A 112 ? 0.1337 0.1199 0.1559 -0.0040 0.0137  0.0095  112 ALA   A CB  
2333 N N   . TYR   A 113 ? 0.1113 0.1154 0.1672 -0.0028 0.0095  0.0198  113 TYR   A N   
2334 C CA  . TYR   A 113 ? 0.1090 0.1172 0.1587 0.0032  0.0114  0.0160  113 TYR   A CA  
2335 C C   . TYR   A 113 ? 0.1055 0.1149 0.1459 -0.0089 0.0095  0.0111  113 TYR   A C   
2336 O O   . TYR   A 113 ? 0.1166 0.1185 0.1584 -0.0064 0.0115  0.0074  113 TYR   A O   
2337 C CB  . TYR   A 113 ? 0.1109 0.1363 0.1664 -0.0036 -0.0005 0.0227  113 TYR   A CB  
2338 C CG  . TYR   A 113 ? 0.1138 0.1469 0.1558 -0.0068 0.0140  0.0369  113 TYR   A CG  
2339 C CD1 . TYR   A 113 ? 0.1191 0.1593 0.1585 0.0065  0.0124  0.0411  113 TYR   A CD1 
2340 C CD2 . TYR   A 113 ? 0.1206 0.1534 0.1595 -0.0052 0.0065  0.0354  113 TYR   A CD2 
2341 C CE1 . TYR   A 113 ? 0.1209 0.1743 0.1645 0.0104  0.0151  0.0440  113 TYR   A CE1 
2342 C CE2 . TYR   A 113 ? 0.1206 0.1711 0.1646 -0.0010 0.0052  0.0445  113 TYR   A CE2 
2343 C CZ  . TYR   A 113 ? 0.1188 0.1814 0.1568 0.0156  0.0145  0.0531  113 TYR   A CZ  
2344 O OH  . TYR   A 113 ? 0.1249 0.1995 0.1755 0.0272  0.0210  0.0598  113 TYR   A OH  
2354 N N   . GLU   A 114 ? 0.1143 0.1146 0.1464 -0.0055 0.0107  0.0156  114 GLU   A N   
2355 C CA  . GLU   A 114 ? 0.1167 0.1067 0.1594 0.0033  0.0029  0.0138  114 GLU   A CA  
2356 C C   . GLU   A 114 ? 0.1109 0.1139 0.1593 0.0017  0.0106  0.0084  114 GLU   A C   
2357 O O   . GLU   A 114 ? 0.1224 0.1156 0.1604 0.0004  -0.0005 0.0118  114 GLU   A O   
2358 C CB  . GLU   A 114 ? 0.1169 0.1121 0.1587 -0.0022 0.0044  0.0132  114 GLU   A CB  
2359 C CG  . GLU   A 114 ? 0.1231 0.1156 0.1704 0.0034  0.0080  0.0059  114 GLU   A CG  
2360 C CD  . GLU   A 114 ? 0.1318 0.1175 0.1785 -0.0059 0.0049  0.0057  114 GLU   A CD  
2361 O OE1 . GLU   A 114 ? 0.1369 0.1201 0.1780 -0.0095 0.0155  -0.0037 114 GLU   A OE1 
2362 O OE2 . GLU   A 114 ? 0.1491 0.1201 0.1964 -0.0082 0.0077  -0.0065 114 GLU   A OE2 
2369 N N   . ASN   A 115 ? 0.1160 0.1140 0.1466 -0.0062 0.0040  0.0052  115 ASN   A N   
2370 C CA  . ASN   A 115 ? 0.1189 0.1197 0.1574 -0.0062 0.0078  0.0075  115 ASN   A CA  
2371 C C   . ASN   A 115 ? 0.1219 0.1141 0.1398 -0.0075 0.0005  0.0082  115 ASN   A C   
2372 O O   . ASN   A 115 ? 0.1262 0.1256 0.1461 -0.0057 0.0072  0.0150  115 ASN   A O   
2373 C CB  . ASN   A 115 ? 0.1252 0.1209 0.1472 -0.0111 0.0139  0.0096  115 ASN   A CB  
2374 C CG  . ASN   A 115 ? 0.1266 0.1399 0.1619 -0.0137 0.0177  0.0112  115 ASN   A CG  
2375 O OD1 . ASN   A 115 ? 0.1355 0.2372 0.1875 -0.0110 0.0238  0.0261  115 ASN   A OD1 
2376 N ND2 . ASN   A 115 ? 0.1312 0.1240 0.1632 -0.0087 0.0256  0.0174  115 ASN   A ND2 
2383 N N   . PHE   A 116 ? 0.1170 0.1164 0.1472 0.0004  0.0119  0.0145  116 PHE   A N   
2384 C CA  . PHE   A 116 ? 0.1206 0.1216 0.1417 0.0012  0.0096  0.0122  116 PHE   A CA  
2385 C C   . PHE   A 116 ? 0.1193 0.1254 0.1452 -0.0037 0.0129  0.0211  116 PHE   A C   
2386 O O   . PHE   A 116 ? 0.1280 0.1322 0.1548 0.0061  0.0100  0.0265  116 PHE   A O   
2387 C CB  . PHE   A 116 ? 0.1220 0.1137 0.1542 0.0006  0.0146  0.0128  116 PHE   A CB  
2388 C CG  . PHE   A 116 ? 0.1177 0.1152 0.1438 0.0003  0.0143  0.0112  116 PHE   A CG  
2389 C CD1 . PHE   A 116 ? 0.1232 0.1171 0.1435 -0.0009 0.0148  0.0122  116 PHE   A CD1 
2390 C CD2 . PHE   A 116 ? 0.1244 0.1228 0.1594 0.0014  0.0157  0.0159  116 PHE   A CD2 
2391 C CE1 . PHE   A 116 ? 0.1269 0.1151 0.1540 -0.0075 0.0101  0.0162  116 PHE   A CE1 
2392 C CE2 . PHE   A 116 ? 0.1254 0.1237 0.1698 0.0034  0.0138  0.0125  116 PHE   A CE2 
2393 C CZ  . PHE   A 116 ? 0.1276 0.1093 0.1589 0.0039  0.0085  0.0166  116 PHE   A CZ  
2403 N N   . ASN   A 117 ? 0.1235 0.1169 0.1575 -0.0005 0.0104  0.0207  117 ASN   A N   
2404 C CA  . ASN   A 117 ? 0.1239 0.1194 0.1633 0.0033  0.0117  0.0252  117 ASN   A CA  
2405 C C   . ASN   A 117 ? 0.1257 0.1267 0.1668 0.0009  0.0096  0.0251  117 ASN   A C   
2406 O O   . ASN   A 117 ? 0.1354 0.1342 0.1862 -0.0027 -0.0089 0.0339  117 ASN   A O   
2407 C CB  . ASN   A 117 ? 0.1213 0.1239 0.1694 0.0046  0.0079  0.0253  117 ASN   A CB  
2408 C CG  . ASN   A 117 ? 0.1181 0.1258 0.1631 0.0007  0.0118  0.0216  117 ASN   A CG  
2409 O OD1 . ASN   A 117 ? 0.1269 0.1495 0.1749 -0.0099 0.0130  0.0157  117 ASN   A OD1 
2410 N ND2 . ASN   A 117 ? 0.1149 0.1221 0.1720 0.0010  0.0103  0.0172  117 ASN   A ND2 
2417 N N   . GLN   A 118 ? 0.1201 0.1251 0.1751 0.0019  -0.0033 0.0237  118 GLN   A N   
2418 C CA  . GLN   A 118 ? 0.1281 0.1382 0.1794 0.0015  -0.0079 0.0138  118 GLN   A CA  
2419 C C   . GLN   A 118 ? 0.1368 0.1433 0.1640 -0.0000 -0.0116 0.0224  118 GLN   A C   
2420 O O   . GLN   A 118 ? 0.1415 0.1788 0.1950 0.0063  -0.0250 -0.0055 118 GLN   A O   
2421 C CB  . GLN   A 118 ? 0.1214 0.1430 0.1934 -0.0015 -0.0007 0.0214  118 GLN   A CB  
2422 C CG  . GLN   A 118 ? 0.1216 0.1481 0.1992 -0.0032 0.0048  0.0250  118 GLN   A CG  
2423 C CD  . GLN   A 118 ? 0.1126 0.1498 0.2097 -0.0023 0.0039  0.0188  118 GLN   A CD  
2424 O OE1 . GLN   A 118 ? 0.1256 0.1593 0.2220 0.0084  -0.0036 0.0087  118 GLN   A OE1 
2425 N NE2 . GLN   A 118 ? 0.1277 0.1478 0.2019 0.0028  -0.0030 0.0194  118 GLN   A NE2 
2434 N N   . HIS   A 119 ? 0.1430 0.1362 0.1615 -0.0015 -0.0071 0.0269  119 HIS   A N   
2435 C CA  . HIS   A 119 ? 0.1465 0.1491 0.1617 -0.0038 -0.0068 0.0349  119 HIS   A CA  
2436 C C   . HIS   A 119 ? 0.1517 0.1517 0.1573 -0.0066 -0.0002 0.0297  119 HIS   A C   
2437 O O   . HIS   A 119 ? 0.1614 0.1636 0.1574 -0.0261 -0.0012 0.0254  119 HIS   A O   
2438 C CB  . HIS   A 119 ? 0.1493 0.1460 0.1902 -0.0054 0.0106  0.0328  119 HIS   A CB  
2439 C CG  . HIS   A 119 ? 0.1493 0.1528 0.2375 0.0007  0.0135  0.0417  119 HIS   A CG  
2440 N ND1 . HIS   A 119 ? 0.1623 0.1729 0.2837 -0.0104 0.0096  0.0289  119 HIS   A ND1 
2441 C CD2 . HIS   A 119 ? 0.1626 0.1597 0.2530 0.0135  0.0375  0.0589  119 HIS   A CD2 
2442 C CE1 . HIS   A 119 ? 0.1655 0.1723 0.3069 -0.0088 0.0250  0.0444  119 HIS   A CE1 
2443 N NE2 . HIS   A 119 ? 0.1746 0.1649 0.2956 0.0067  0.0456  0.0640  119 HIS   A NE2 
2451 N N   . GLU   A 120 ? 0.1639 0.1725 0.1554 -0.0040 -0.0023 0.0502  120 GLU   A N   
2452 C CA  . GLU   A 120 ? 0.1921 0.2055 0.1791 0.0101  -0.0099 0.0852  120 GLU   A CA  
2453 C C   . GLU   A 120 ? 0.1731 0.1864 0.1647 -0.0079 -0.0036 0.0737  120 GLU   A C   
2454 O O   . GLU   A 120 ? 0.1738 0.1768 0.1730 -0.0143 -0.0014 0.0681  120 GLU   A O   
2455 C CB  . GLU   A 120 ? 0.2715 0.2837 0.2513 0.0317  -0.0138 0.1277  120 GLU   A CB  
2456 C CG  . GLU   A 120 ? 0.3754 0.3750 0.3825 0.0502  -0.0142 0.1226  120 GLU   A CG  
2457 C CD  . GLU   A 120 ? 0.4570 0.4502 0.5124 0.0604  -0.0045 0.1029  120 GLU   A CD  
2458 O OE1 . GLU   A 120 ? 0.4784 0.4709 0.5537 0.0613  -0.0018 0.0963  120 GLU   A OE1 
2459 O OE2 . GLU   A 120 ? 0.5134 0.5134 0.5633 0.0636  -0.0000 0.0956  120 GLU   A OE2 
2466 N N   . VAL   A 121 ? 0.1661 0.1852 0.1463 -0.0093 0.0028  0.0552  121 VAL   A N   
2467 C CA  . VAL   A 121 ? 0.1741 0.1906 0.1405 -0.0144 0.0213  0.0451  121 VAL   A CA  
2468 C C   . VAL   A 121 ? 0.1625 0.1710 0.1233 -0.0153 0.0061  0.0325  121 VAL   A C   
2469 O O   . VAL   A 121 ? 0.1664 0.1733 0.1453 -0.0224 -0.0063 0.0282  121 VAL   A O   
2470 C CB  . VAL   A 121 ? 0.2123 0.2260 0.1725 -0.0014 0.0273  0.0587  121 VAL   A CB  
2471 C CG1 . VAL   A 121 ? 0.2191 0.2422 0.1711 0.0033  0.0368  0.0634  121 VAL   A CG1 
2472 C CG2 . VAL   A 121 ? 0.2341 0.2441 0.2157 -0.0030 0.0275  0.0445  121 VAL   A CG2 
2482 N N   . LEU   A 122 ? 0.1490 0.1526 0.1411 -0.0192 0.0100  0.0307  122 LEU   A N   
2483 C CA  . LEU   A 122 ? 0.1562 0.1395 0.1394 -0.0180 0.0289  0.0259  122 LEU   A CA  
2484 C C   . LEU   A 122 ? 0.1486 0.1403 0.1369 -0.0240 0.0123  0.0173  122 LEU   A C   
2485 O O   . LEU   A 122 ? 0.1515 0.1502 0.1719 -0.0248 0.0112  0.0225  122 LEU   A O   
2486 C CB  . LEU   A 122 ? 0.1737 0.1463 0.1747 -0.0054 0.0215  0.0366  122 LEU   A CB  
2487 C CG  . LEU   A 122 ? 0.1779 0.1483 0.1575 -0.0063 0.0250  0.0256  122 LEU   A CG  
2488 C CD1 . LEU   A 122 ? 0.1999 0.1533 0.1691 -0.0170 0.0282  0.0271  122 LEU   A CD1 
2489 C CD2 . LEU   A 122 ? 0.1699 0.1473 0.1584 -0.0024 0.0309  0.0196  122 LEU   A CD2 
2501 N N   . LEU   A 123 ? 0.1404 0.1415 0.1264 -0.0228 0.0057  0.0203  123 LEU   A N   
2502 C CA  . LEU   A 123 ? 0.1402 0.1443 0.1226 -0.0182 0.0128  0.0159  123 LEU   A CA  
2503 C C   . LEU   A 123 ? 0.1353 0.1354 0.1145 -0.0129 0.0110  0.0249  123 LEU   A C   
2504 O O   . LEU   A 123 ? 0.1357 0.1499 0.1294 -0.0241 0.0047  0.0258  123 LEU   A O   
2505 C CB  . LEU   A 123 ? 0.1485 0.1545 0.1317 -0.0205 0.0205  0.0132  123 LEU   A CB  
2506 C CG  . LEU   A 123 ? 0.1524 0.1632 0.1466 -0.0166 0.0225  0.0051  123 LEU   A CG  
2507 C CD1 . LEU   A 123 ? 0.1573 0.1678 0.1705 -0.0094 0.0202  -0.0044 123 LEU   A CD1 
2508 C CD2 . LEU   A 123 ? 0.1661 0.1676 0.1535 -0.0170 0.0129  -0.0023 123 LEU   A CD2 
2520 N N   A ALA   A 124 ? 0.1335 0.1257 0.1204 -0.0127 0.0142  0.0165  124 ALA   A N   
2521 N N   B ALA   A 124 ? 0.1330 0.1332 0.1076 -0.0071 0.0067  0.0157  124 ALA   A N   
2522 C CA  A ALA   A 124 ? 0.1252 0.1244 0.1342 -0.0141 0.0092  0.0194  124 ALA   A CA  
2523 C CA  B ALA   A 124 ? 0.1270 0.1355 0.1047 -0.0044 0.0006  0.0153  124 ALA   A CA  
2524 C C   A ALA   A 124 ? 0.1215 0.1271 0.1429 -0.0133 0.0194  0.0242  124 ALA   A C   
2525 C C   B ALA   A 124 ? 0.1267 0.1367 0.0995 -0.0028 0.0068  0.0159  124 ALA   A C   
2526 O O   A ALA   A 124 ? 0.1238 0.1371 0.1650 -0.0092 0.0214  0.0338  124 ALA   A O   
2527 O O   B ALA   A 124 ? 0.1292 0.1437 0.1089 0.0011  0.0065  0.0154  124 ALA   A O   
2528 C CB  A ALA   A 124 ? 0.1249 0.1264 0.1534 -0.0150 0.0103  0.0204  124 ALA   A CB  
2529 C CB  B ALA   A 124 ? 0.1228 0.1358 0.1064 0.0008  -0.0038 0.0153  124 ALA   A CB  
2540 N N   A PRO   A 125 ? 0.1196 0.1222 0.1440 -0.0106 0.0081  0.0281  125 PRO   A N   
2541 N N   B PRO   A 125 ? 0.1279 0.1333 0.0915 -0.0016 0.0035  0.0220  125 PRO   A N   
2542 C CA  A PRO   A 125 ? 0.1290 0.1298 0.1418 -0.0063 0.0052  0.0160  125 PRO   A CA  
2543 C CA  B PRO   A 125 ? 0.1304 0.1293 0.0925 -0.0001 0.0065  0.0154  125 PRO   A CA  
2544 C C   A PRO   A 125 ? 0.1172 0.1420 0.1414 -0.0020 0.0039  0.0190  125 PRO   A C   
2545 C C   B PRO   A 125 ? 0.1289 0.1294 0.0876 0.0079  0.0012  0.0166  125 PRO   A C   
2546 O O   A PRO   A 125 ? 0.1131 0.1388 0.1577 0.0053  0.0076  0.0129  125 PRO   A O   
2547 O O   B PRO   A 125 ? 0.1301 0.1263 0.1016 0.0100  -0.0012 0.0147  125 PRO   A O   
2548 C CB  A PRO   A 125 ? 0.1434 0.1282 0.1374 -0.0024 0.0146  0.0136  125 PRO   A CB  
2549 C CB  B PRO   A 125 ? 0.1356 0.1335 0.0914 -0.0023 0.0013  0.0162  125 PRO   A CB  
2550 C CG  A PRO   A 125 ? 0.1373 0.1134 0.1383 -0.0079 0.0174  0.0166  125 PRO   A CG  
2551 C CG  B PRO   A 125 ? 0.1367 0.1374 0.1013 -0.0023 0.0040  0.0168  125 PRO   A CG  
2552 C CD  A PRO   A 125 ? 0.1242 0.1195 0.1466 -0.0141 0.0131  0.0187  125 PRO   A CD  
2553 C CD  B PRO   A 125 ? 0.1297 0.1378 0.0978 -0.0030 0.0035  0.0173  125 PRO   A CD  
2568 N N   A LEU   A 126 ? 0.1205 0.1650 0.1407 -0.0008 0.0090  0.0234  126 LEU   A N   
2569 N N   B LEU   A 126 ? 0.1308 0.1320 0.1012 0.0036  -0.0056 0.0080  126 LEU   A N   
2570 C CA  A LEU   A 126 ? 0.1198 0.1698 0.1379 -0.0042 0.0106  0.0260  126 LEU   A CA  
2571 C CA  B LEU   A 126 ? 0.1259 0.1398 0.1110 -0.0036 0.0010  0.0121  126 LEU   A CA  
2572 C C   A LEU   A 126 ? 0.1304 0.1544 0.1397 0.0053  -0.0027 0.0186  126 LEU   A C   
2573 C C   B LEU   A 126 ? 0.1200 0.1361 0.1139 0.0021  0.0114  0.0151  126 LEU   A C   
2574 O O   A LEU   A 126 ? 0.1351 0.1444 0.1594 0.0061  0.0095  0.0092  126 LEU   A O   
2575 O O   B LEU   A 126 ? 0.1245 0.1369 0.1188 0.0062  0.0265  0.0180  126 LEU   A O   
2576 C CB  A LEU   A 126 ? 0.1301 0.1914 0.1456 -0.0098 0.0094  0.0221  126 LEU   A CB  
2577 C CB  B LEU   A 126 ? 0.1291 0.1516 0.1275 -0.0131 0.0028  0.0206  126 LEU   A CB  
2578 C CG  A LEU   A 126 ? 0.1358 0.2113 0.1827 -0.0167 0.0125  0.0198  126 LEU   A CG  
2579 C CG  B LEU   A 126 ? 0.1356 0.1674 0.1604 -0.0188 0.0037  0.0215  126 LEU   A CG  
2580 C CD1 A LEU   A 126 ? 0.1388 0.2285 0.2128 -0.0174 0.0075  0.0186  126 LEU   A CD1 
2581 C CD1 B LEU   A 126 ? 0.1396 0.1813 0.1805 -0.0166 0.0053  0.0279  126 LEU   A CD1 
2582 C CD2 A LEU   A 126 ? 0.1362 0.2109 0.1856 -0.0196 0.0118  0.0285  126 LEU   A CD2 
2583 C CD2 B LEU   A 126 ? 0.1431 0.1686 0.1753 -0.0208 0.0062  0.0172  126 LEU   A CD2 
2606 N N   A LEU   A 127 ? 0.1279 0.1466 0.1478 0.0072  0.0058  0.0268  127 LEU   A N   
2607 N N   B LEU   A 127 ? 0.1115 0.1314 0.1012 0.0024  0.0130  0.0204  127 LEU   A N   
2608 C CA  A LEU   A 127 ? 0.1276 0.1428 0.1294 0.0040  0.0002  0.0185  127 LEU   A CA  
2609 C CA  B LEU   A 127 ? 0.1098 0.1319 0.1077 0.0058  0.0085  0.0250  127 LEU   A CA  
2610 C C   A LEU   A 127 ? 0.1229 0.1301 0.1224 0.0041  -0.0070 0.0115  127 LEU   A C   
2611 C C   B LEU   A 127 ? 0.1133 0.1300 0.1195 0.0086  0.0106  0.0180  127 LEU   A C   
2612 O O   A LEU   A 127 ? 0.1308 0.1258 0.1332 -0.0093 -0.0118 0.0152  127 LEU   A O   
2613 O O   B LEU   A 127 ? 0.1171 0.1327 0.1239 0.0033  0.0227  0.0258  127 LEU   A O   
2614 C CB  A LEU   A 127 ? 0.1316 0.1495 0.1331 0.0124  0.0076  0.0191  127 LEU   A CB  
2615 C CB  B LEU   A 127 ? 0.1118 0.1412 0.1108 0.0060  -0.0060 0.0207  127 LEU   A CB  
2616 C CG  A LEU   A 127 ? 0.1390 0.1561 0.1389 0.0115  -0.0025 0.0181  127 LEU   A CG  
2617 C CG  B LEU   A 127 ? 0.1173 0.1491 0.1100 0.0111  -0.0131 0.0121  127 LEU   A CG  
2618 C CD1 A LEU   A 127 ? 0.1387 0.1514 0.1533 0.0109  -0.0002 0.0122  127 LEU   A CD1 
2619 C CD1 B LEU   A 127 ? 0.1142 0.1538 0.1229 0.0189  -0.0065 0.0080  127 LEU   A CD1 
2620 C CD2 A LEU   A 127 ? 0.1522 0.1587 0.1588 0.0137  -0.0151 0.0159  127 LEU   A CD2 
2621 C CD2 B LEU   A 127 ? 0.1286 0.1549 0.1013 0.0068  -0.0225 -0.0024 127 LEU   A CD2 
2644 N N   A SER   A 128 ? 0.1244 0.1315 0.1186 -0.0073 -0.0069 0.0129  128 SER   A N   
2645 N N   B SER   A 128 ? 0.1224 0.1322 0.1282 0.0068  0.0007  0.0152  128 SER   A N   
2646 C CA  A SER   A 128 ? 0.1398 0.1253 0.1204 0.0003  -0.0077 0.0117  128 SER   A CA  
2647 C CA  B SER   A 128 ? 0.1253 0.1288 0.1230 0.0099  -0.0114 0.0117  128 SER   A CA  
2648 C C   A SER   A 128 ? 0.1434 0.1295 0.1289 0.0044  -0.0078 0.0090  128 SER   A C   
2649 C C   B SER   A 128 ? 0.1252 0.1262 0.1150 0.0072  -0.0215 0.0273  128 SER   A C   
2650 O O   A SER   A 128 ? 0.1537 0.1481 0.1455 0.0062  -0.0094 0.0049  128 SER   A O   
2651 O O   B SER   A 128 ? 0.1210 0.1277 0.1173 0.0060  -0.0233 0.0302  128 SER   A O   
2652 C CB  A SER   A 128 ? 0.1438 0.1212 0.1211 -0.0044 -0.0055 0.0189  128 SER   A CB  
2653 C CB  B SER   A 128 ? 0.1307 0.1315 0.1276 0.0100  -0.0091 0.0067  128 SER   A CB  
2654 O OG  A SER   A 128 ? 0.1463 0.1278 0.1286 0.0021  -0.0032 0.0079  128 SER   A OG  
2655 O OG  B SER   A 128 ? 0.1344 0.1331 0.1320 0.0074  0.0044  0.0066  128 SER   A OG  
2666 N N   A ALA   A 129 ? 0.1296 0.1347 0.1511 0.0024  -0.0073 0.0129  129 ALA   A N   
2667 N N   B ALA   A 129 ? 0.1264 0.1325 0.1172 0.0083  -0.0258 0.0265  129 ALA   A N   
2668 C CA  A ALA   A 129 ? 0.1279 0.1416 0.1528 0.0049  -0.0018 0.0123  129 ALA   A CA  
2669 C CA  B ALA   A 129 ? 0.1339 0.1342 0.1186 0.0113  -0.0184 0.0229  129 ALA   A CA  
2670 C C   A ALA   A 129 ? 0.1341 0.1385 0.1405 -0.0014 -0.0069 -0.0043 129 ALA   A C   
2671 C C   B ALA   A 129 ? 0.1365 0.1349 0.1203 0.0084  -0.0179 0.0202  129 ALA   A C   
2672 O O   A ALA   A 129 ? 0.1362 0.1431 0.1327 -0.0054 -0.0006 0.0113  129 ALA   A O   
2673 O O   B ALA   A 129 ? 0.1322 0.1367 0.1259 0.0094  -0.0158 0.0173  129 ALA   A O   
2674 C CB  A ALA   A 129 ? 0.1354 0.1585 0.1814 0.0117  0.0066  0.0256  129 ALA   A CB  
2675 C CB  B ALA   A 129 ? 0.1410 0.1426 0.1101 0.0159  -0.0138 0.0189  129 ALA   A CB  
2686 N N   A GLY   A 130 ? 0.1450 0.1354 0.1777 0.0024  0.0003  -0.0101 130 GLY   A N   
2687 N N   B GLY   A 130 ? 0.1400 0.1366 0.1152 0.0121  -0.0179 0.0244  130 GLY   A N   
2688 C CA  A GLY   A 130 ? 0.1588 0.1352 0.1870 0.0079  0.0048  -0.0164 130 GLY   A CA  
2689 C CA  B GLY   A 130 ? 0.1418 0.1357 0.1224 0.0144  -0.0155 0.0223  130 GLY   A CA  
2690 C C   A GLY   A 130 ? 0.1584 0.1310 0.1841 0.0145  -0.0025 -0.0235 130 GLY   A C   
2691 C C   B GLY   A 130 ? 0.1443 0.1390 0.1207 0.0166  -0.0230 0.0203  130 GLY   A C   
2692 O O   A GLY   A 130 ? 0.1555 0.1272 0.1891 0.0075  -0.0221 -0.0262 130 GLY   A O   
2693 O O   B GLY   A 130 ? 0.1443 0.1423 0.1219 0.0223  -0.0281 0.0175  130 GLY   A O   
2700 N N   A ILE   A 131 ? 0.1614 0.1310 0.1649 0.0103  -0.0115 -0.0094 131 ILE   A N   
2701 N N   B ILE   A 131 ? 0.1471 0.1416 0.1277 0.0103  -0.0220 0.0171  131 ILE   A N   
2702 C CA  A ILE   A 131 ? 0.1735 0.1321 0.1483 0.0051  -0.0234 -0.0044 131 ILE   A CA  
2703 C CA  B ILE   A 131 ? 0.1502 0.1405 0.1249 0.0071  -0.0122 0.0142  131 ILE   A CA  
2704 C C   A ILE   A 131 ? 0.1755 0.1335 0.1296 0.0040  -0.0184 0.0085  131 ILE   A C   
2705 C C   B ILE   A 131 ? 0.1569 0.1453 0.1240 0.0076  -0.0039 0.0198  131 ILE   A C   
2706 O O   A ILE   A 131 ? 0.1846 0.1359 0.1455 0.0036  -0.0136 0.0133  131 ILE   A O   
2707 O O   B ILE   A 131 ? 0.1615 0.1489 0.1283 0.0048  0.0215  0.0236  131 ILE   A O   
2708 C CB  A ILE   A 131 ? 0.1800 0.1427 0.1560 -0.0009 -0.0229 -0.0143 131 ILE   A CB  
2709 C CB  B ILE   A 131 ? 0.1472 0.1393 0.1274 0.0067  -0.0120 0.0044  131 ILE   A CB  
2710 C CG1 A ILE   A 131 ? 0.1910 0.1764 0.1731 -0.0048 -0.0273 -0.0218 131 ILE   A CG1 
2711 C CG1 B ILE   A 131 ? 0.1417 0.1437 0.1274 0.0039  -0.0099 -0.0044 131 ILE   A CG1 
2712 C CG2 A ILE   A 131 ? 0.1871 0.1334 0.1840 0.0017  -0.0103 -0.0226 131 ILE   A CG2 
2713 C CG2 B ILE   A 131 ? 0.1496 0.1370 0.1321 0.0029  -0.0079 -0.0029 131 ILE   A CG2 
2714 C CD1 A ILE   A 131 ? 0.1962 0.1895 0.2127 -0.0094 -0.0266 -0.0352 131 ILE   A CD1 
2715 C CD1 B ILE   A 131 ? 0.1429 0.1481 0.1381 0.0040  -0.0050 -0.0150 131 ILE   A CD1 
2738 N N   A PHE   A 132 ? 0.1698 0.1338 0.1161 0.0094  -0.0118 0.0031  132 PHE   A N   
2739 N N   B PHE   A 132 ? 0.1553 0.1438 0.1215 0.0107  -0.0139 0.0188  132 PHE   A N   
2740 C CA  A PHE   A 132 ? 0.1702 0.1418 0.1107 0.0018  -0.0032 0.0058  132 PHE   A CA  
2741 C CA  B PHE   A 132 ? 0.1565 0.1384 0.1240 0.0083  -0.0200 0.0191  132 PHE   A CA  
2742 C C   A PHE   A 132 ? 0.1735 0.1592 0.1132 0.0038  -0.0054 0.0052  132 PHE   A C   
2743 C C   B PHE   A 132 ? 0.1609 0.1422 0.1363 0.0129  -0.0189 0.0172  132 PHE   A C   
2744 O O   A PHE   A 132 ? 0.1840 0.1732 0.1325 -0.0069 -0.0032 0.0058  132 PHE   A O   
2745 O O   B PHE   A 132 ? 0.1652 0.1483 0.1385 0.0096  -0.0146 0.0149  132 PHE   A O   
2746 C CB  A PHE   A 132 ? 0.1667 0.1344 0.1132 0.0048  -0.0024 0.0005  132 PHE   A CB  
2747 C CB  B PHE   A 132 ? 0.1502 0.1346 0.1109 0.0068  -0.0214 0.0307  132 PHE   A CB  
2748 C CG  A PHE   A 132 ? 0.1681 0.1332 0.1186 0.0054  -0.0144 0.0048  132 PHE   A CG  
2749 C CG  B PHE   A 132 ? 0.1549 0.1345 0.1206 0.0078  -0.0231 0.0237  132 PHE   A CG  
2750 C CD1 A PHE   A 132 ? 0.1663 0.1400 0.1324 0.0029  -0.0151 -0.0001 132 PHE   A CD1 
2751 C CD1 B PHE   A 132 ? 0.1553 0.1402 0.1309 0.0101  -0.0139 0.0165  132 PHE   A CD1 
2752 C CD2 A PHE   A 132 ? 0.1701 0.1511 0.1452 0.0066  -0.0095 0.0031  132 PHE   A CD2 
2753 C CD2 B PHE   A 132 ? 0.1575 0.1394 0.1298 0.0076  -0.0269 0.0129  132 PHE   A CD2 
2754 C CE1 A PHE   A 132 ? 0.1635 0.1428 0.1366 -0.0012 -0.0209 -0.0108 132 PHE   A CE1 
2755 C CE1 B PHE   A 132 ? 0.1561 0.1422 0.1239 0.0099  -0.0135 0.0118  132 PHE   A CE1 
2756 C CE2 A PHE   A 132 ? 0.1680 0.1580 0.1561 0.0134  -0.0171 -0.0024 132 PHE   A CE2 
2757 C CE2 B PHE   A 132 ? 0.1547 0.1425 0.1249 0.0100  -0.0251 0.0057  132 PHE   A CE2 
2758 C CZ  A PHE   A 132 ? 0.1658 0.1527 0.1483 0.0054  -0.0205 -0.0067 132 PHE   A CZ  
2759 C CZ  B PHE   A 132 ? 0.1542 0.1404 0.1163 0.0083  -0.0192 0.0102  132 PHE   A CZ  
2778 N N   A GLY   A 133 ? 0.1699 0.1631 0.1116 0.0085  -0.0269 0.0028  133 GLY   A N   
2779 N N   B GLY   A 133 ? 0.1610 0.1417 0.1306 0.0150  -0.0182 0.0204  133 GLY   A N   
2780 C CA  A GLY   A 133 ? 0.1786 0.1755 0.1284 0.0034  -0.0255 -0.0023 133 GLY   A CA  
2781 C CA  B GLY   A 133 ? 0.1643 0.1468 0.1326 0.0112  -0.0190 0.0143  133 GLY   A CA  
2782 C C   A GLY   A 133 ? 0.1801 0.1874 0.1202 -0.0013 -0.0317 -0.0104 133 GLY   A C   
2783 C C   B GLY   A 133 ? 0.1652 0.1539 0.1293 0.0059  -0.0292 0.0058  133 GLY   A C   
2784 O O   A GLY   A 133 ? 0.1937 0.2047 0.1419 0.0021  -0.0346 -0.0296 133 GLY   A O   
2785 O O   B GLY   A 133 ? 0.1692 0.1618 0.1018 0.0010  -0.0271 0.0027  133 GLY   A O   
2792 N N   A ALA   A 134 ? 0.1777 0.1784 0.1302 -0.0099 -0.0268 -0.0092 134 ALA   A N   
2793 N N   B ALA   A 134 ? 0.1657 0.1513 0.1416 0.0058  -0.0332 -0.0074 134 ALA   A N   
2794 C CA  A ALA   A 134 ? 0.1727 0.1798 0.1638 -0.0124 -0.0228 -0.0039 134 ALA   A CA  
2795 C CA  B ALA   A 134 ? 0.1629 0.1463 0.1453 0.0060  -0.0308 -0.0186 134 ALA   A CA  
2796 C C   A ALA   A 134 ? 0.1730 0.1922 0.1688 -0.0078 -0.0220 0.0170  134 ALA   A C   
2797 C C   B ALA   A 134 ? 0.1626 0.1412 0.1362 0.0072  -0.0301 -0.0190 134 ALA   A C   
2798 O O   A ALA   A 134 ? 0.1808 0.1983 0.1903 0.0009  -0.0064 0.0230  134 ALA   A O   
2799 O O   B ALA   A 134 ? 0.1616 0.1380 0.1533 0.0065  -0.0257 -0.0160 134 ALA   A O   
2800 C CB  A ALA   A 134 ? 0.1814 0.1749 0.1994 -0.0076 -0.0254 -0.0037 134 ALA   A CB  
2801 C CB  B ALA   A 134 ? 0.1660 0.1454 0.1657 0.0098  -0.0316 -0.0224 134 ALA   A CB  
2812 N N   A ASP   A 135 ? 0.1797 0.1975 0.1793 -0.0166 -0.0255 0.0350  135 ASP   A N   
2813 N N   B ASP   A 135 ? 0.1720 0.1466 0.1337 0.0039  -0.0293 -0.0149 135 ASP   A N   
2814 C CA  A ASP   A 135 ? 0.1781 0.2127 0.2029 -0.0217 -0.0390 0.0482  135 ASP   A CA  
2815 C CA  B ASP   A 135 ? 0.1745 0.1532 0.1440 0.0013  -0.0303 -0.0090 135 ASP   A CA  
2816 C C   A ASP   A 135 ? 0.1652 0.2092 0.2033 -0.0114 -0.0253 0.0564  135 ASP   A C   
2817 C C   B ASP   A 135 ? 0.1652 0.1400 0.1467 0.0057  -0.0252 -0.0101 135 ASP   A C   
2818 O O   A ASP   A 135 ? 0.1622 0.1948 0.2032 -0.0111 -0.0242 0.0621  135 ASP   A O   
2819 O O   B ASP   A 135 ? 0.1662 0.1360 0.1520 0.0070  -0.0189 -0.0068 135 ASP   A O   
2820 C CB  A ASP   A 135 ? 0.2029 0.2450 0.2409 -0.0398 -0.0581 0.0372  135 ASP   A CB  
2821 C CB  B ASP   A 135 ? 0.1851 0.1695 0.1496 -0.0005 -0.0355 -0.0093 135 ASP   A CB  
2822 C CG  A ASP   A 135 ? 0.2185 0.2749 0.2885 -0.0537 -0.0667 0.0280  135 ASP   A CG  
2823 C CG  B ASP   A 135 ? 0.1907 0.1848 0.1667 -0.0002 -0.0368 -0.0109 135 ASP   A CG  
2824 O OD1 A ASP   A 135 ? 0.2104 0.2819 0.2930 -0.0612 -0.0698 0.0416  135 ASP   A OD1 
2825 O OD1 B ASP   A 135 ? 0.1925 0.1849 0.1735 0.0000  -0.0362 -0.0208 135 ASP   A OD1 
2826 O OD2 A ASP   A 135 ? 0.2455 0.2953 0.3368 -0.0548 -0.0463 0.0254  135 ASP   A OD2 
2827 O OD2 B ASP   A 135 ? 0.1923 0.1975 0.1777 -0.0017 -0.0374 -0.0110 135 ASP   A OD2 
2836 N N   A PRO   A 136 ? 0.1560 0.2099 0.2092 0.0002  -0.0140 0.0590  136 PRO   A N   
2837 N N   B PRO   A 136 ? 0.1562 0.1298 0.1511 0.0078  -0.0188 -0.0117 136 PRO   A N   
2838 C CA  A PRO   A 136 ? 0.1495 0.2131 0.2151 0.0010  -0.0028 0.0559  136 PRO   A CA  
2839 C CA  B PRO   A 136 ? 0.1522 0.1349 0.1530 -0.0005 -0.0195 -0.0128 136 PRO   A CA  
2840 C C   A PRO   A 136 ? 0.1280 0.2107 0.2145 0.0035  -0.0053 0.0548  136 PRO   A C   
2841 C C   B PRO   A 136 ? 0.1435 0.1383 0.1462 -0.0038 -0.0253 -0.0102 136 PRO   A C   
2842 O O   A PRO   A 136 ? 0.1211 0.2098 0.2168 0.0026  0.0014  0.0569  136 PRO   A O   
2843 O O   B PRO   A 136 ? 0.1447 0.1340 0.1433 0.0015  -0.0218 -0.0045 136 PRO   A O   
2844 C CB  A PRO   A 136 ? 0.1674 0.2115 0.2334 0.0092  -0.0037 0.0514  136 PRO   A CB  
2845 C CB  B PRO   A 136 ? 0.1602 0.1321 0.1651 -0.0004 -0.0157 -0.0170 136 PRO   A CB  
2846 C CG  A PRO   A 136 ? 0.1802 0.2164 0.2551 0.0133  -0.0078 0.0446  136 PRO   A CG  
2847 C CG  B PRO   A 136 ? 0.1672 0.1286 0.1736 0.0056  -0.0120 -0.0161 136 PRO   A CG  
2848 C CD  A PRO   A 136 ? 0.1675 0.2104 0.2370 0.0112  -0.0062 0.0578  136 PRO   A CD  
2849 C CD  B PRO   A 136 ? 0.1602 0.1255 0.1690 0.0099  -0.0123 -0.0147 136 PRO   A CD  
2864 N N   A ILE   A 137 ? 0.1216 0.2073 0.2204 0.0038  -0.0143 0.0582  137 ILE   A N   
2865 N N   B ILE   A 137 ? 0.1377 0.1410 0.1495 -0.0101 -0.0235 -0.0092 137 ILE   A N   
2866 C CA  A ILE   A 137 ? 0.1285 0.2103 0.2369 -0.0059 -0.0175 0.0578  137 ILE   A CA  
2867 C CA  B ILE   A 137 ? 0.1391 0.1495 0.1658 -0.0044 -0.0182 -0.0064 137 ILE   A CA  
2868 C C   A ILE   A 137 ? 0.1329 0.2025 0.2155 -0.0100 -0.0207 0.0511  137 ILE   A C   
2869 C C   B ILE   A 137 ? 0.1422 0.1466 0.1510 -0.0007 -0.0139 -0.0158 137 ILE   A C   
2870 O O   A ILE   A 137 ? 0.1367 0.1950 0.2196 -0.0093 -0.0079 0.0482  137 ILE   A O   
2871 O O   B ILE   A 137 ? 0.1426 0.1504 0.1568 -0.0036 -0.0016 -0.0159 137 ILE   A O   
2872 C CB  A ILE   A 137 ? 0.1348 0.2211 0.2731 -0.0085 -0.0294 0.0633  137 ILE   A CB  
2873 C CB  B ILE   A 137 ? 0.1449 0.1619 0.1925 -0.0051 -0.0256 0.0053  137 ILE   A CB  
2874 C CG1 A ILE   A 137 ? 0.1452 0.2356 0.3083 -0.0053 -0.0352 0.0697  137 ILE   A CG1 
2875 C CG1 B ILE   A 137 ? 0.1524 0.1743 0.2157 0.0051  -0.0359 0.0159  137 ILE   A CG1 
2876 C CG2 A ILE   A 137 ? 0.1428 0.2235 0.2853 -0.0141 -0.0342 0.0626  137 ILE   A CG2 
2877 C CG2 B ILE   A 137 ? 0.1471 0.1608 0.1977 -0.0066 -0.0293 0.0074  137 ILE   A CG2 
2878 C CD1 A ILE   A 137 ? 0.1630 0.2493 0.3373 -0.0020 -0.0266 0.0692  137 ILE   A CD1 
2879 C CD1 B ILE   A 137 ? 0.1598 0.1791 0.2349 0.0084  -0.0349 0.0214  137 ILE   A CD1 
2902 N N   A HIS   A 138 ? 0.1347 0.2027 0.2054 -0.0146 -0.0149 0.0413  138 HIS   A N   
2903 N N   B HIS   A 138 ? 0.1433 0.1415 0.1447 0.0007  -0.0076 -0.0233 138 HIS   A N   
2904 C CA  A HIS   A 138 ? 0.1413 0.2009 0.1851 -0.0123 -0.0119 0.0326  138 HIS   A CA  
2905 C CA  B HIS   A 138 ? 0.1438 0.1372 0.1424 -0.0030 -0.0093 -0.0183 138 HIS   A CA  
2906 C C   A HIS   A 138 ? 0.1320 0.1913 0.1716 -0.0078 -0.0089 0.0332  138 HIS   A C   
2907 C C   B HIS   A 138 ? 0.1363 0.1247 0.1324 0.0028  -0.0118 -0.0141 138 HIS   A C   
2908 O O   A HIS   A 138 ? 0.1440 0.1883 0.1745 -0.0155 -0.0052 0.0355  138 HIS   A O   
2909 O O   B HIS   A 138 ? 0.1417 0.1235 0.1329 0.0024  -0.0121 -0.0116 138 HIS   A O   
2910 C CB  A HIS   A 138 ? 0.1592 0.2139 0.1859 -0.0116 -0.0140 0.0199  138 HIS   A CB  
2911 C CB  B HIS   A 138 ? 0.1532 0.1497 0.1505 -0.0034 -0.0072 -0.0217 138 HIS   A CB  
2912 C CG  A HIS   A 138 ? 0.1735 0.2191 0.1924 -0.0173 -0.0157 0.0111  138 HIS   A CG  
2913 C CG  B HIS   A 138 ? 0.1640 0.1627 0.1690 0.0016  -0.0066 -0.0226 138 HIS   A CG  
2914 N ND1 A HIS   A 138 ? 0.1828 0.2299 0.2144 -0.0195 -0.0141 0.0006  138 HIS   A ND1 
2915 N ND1 B HIS   A 138 ? 0.1700 0.1684 0.1804 0.0050  -0.0076 -0.0280 138 HIS   A ND1 
2916 C CD2 A HIS   A 138 ? 0.1810 0.2209 0.1972 -0.0128 -0.0092 0.0166  138 HIS   A CD2 
2917 C CD2 B HIS   A 138 ? 0.1684 0.1666 0.1789 0.0037  -0.0054 -0.0208 138 HIS   A CD2 
2918 C CE1 A HIS   A 138 ? 0.1908 0.2356 0.2191 -0.0090 -0.0089 0.0015  138 HIS   A CE1 
2919 C CE1 B HIS   A 138 ? 0.1714 0.1699 0.1828 0.0064  -0.0050 -0.0280 138 HIS   A CE1 
2920 N NE2 A HIS   A 138 ? 0.1863 0.2323 0.1968 -0.0090 -0.0069 0.0101  138 HIS   A NE2 
2921 N NE2 B HIS   A 138 ? 0.1706 0.1698 0.1814 0.0055  -0.0030 -0.0242 138 HIS   A NE2 
2936 N N   A SER   A 139 ? 0.1243 0.1833 0.1669 -0.0031 -0.0022 0.0362  139 SER   A N   
2937 N N   B SER   A 139 ? 0.1304 0.1201 0.1320 0.0024  -0.0113 -0.0060 139 SER   A N   
2938 C CA  A SER   A 139 ? 0.1223 0.1759 0.1663 -0.0049 -0.0037 0.0361  139 SER   A CA  
2939 C CA  B SER   A 139 ? 0.1228 0.1245 0.1270 0.0046  -0.0101 -0.0026 139 SER   A CA  
2940 C C   A SER   A 139 ? 0.1147 0.1704 0.1672 -0.0027 0.0050  0.0249  139 SER   A C   
2941 C C   B SER   A 139 ? 0.1174 0.1250 0.1274 0.0066  -0.0065 -0.0010 139 SER   A C   
2942 O O   A SER   A 139 ? 0.1094 0.1585 0.1721 -0.0037 0.0122  0.0296  139 SER   A O   
2943 O O   B SER   A 139 ? 0.1172 0.1235 0.1407 -0.0001 -0.0212 0.0013  139 SER   A O   
2944 C CB  A SER   A 139 ? 0.1186 0.1743 0.1650 -0.0033 -0.0016 0.0418  139 SER   A CB  
2945 C CB  B SER   A 139 ? 0.1272 0.1248 0.1358 0.0038  -0.0104 0.0055  139 SER   A CB  
2946 O OG  A SER   A 139 ? 0.1260 0.1659 0.1616 -0.0072 -0.0035 0.0457  139 SER   A OG  
2947 O OG  B SER   A 139 ? 0.1296 0.1300 0.1343 0.0022  -0.0094 0.0091  139 SER   A OG  
2958 N N   A LEU   A 140 ? 0.1129 0.1720 0.1677 -0.0029 -0.0026 0.0335  140 LEU   A N   
2959 N N   B LEU   A 140 ? 0.1120 0.1238 0.1208 0.0056  0.0031  0.0073  140 LEU   A N   
2960 C CA  A LEU   A 140 ? 0.1148 0.1646 0.1620 -0.0037 0.0035  0.0355  140 LEU   A CA  
2961 C CA  B LEU   A 140 ? 0.1116 0.1231 0.1132 -0.0018 0.0087  0.0078  140 LEU   A CA  
2962 C C   A LEU   A 140 ? 0.1089 0.1715 0.1542 -0.0036 0.0059  0.0352  140 LEU   A C   
2963 C C   B LEU   A 140 ? 0.1127 0.1310 0.1149 -0.0038 -0.0030 0.0028  140 LEU   A C   
2964 O O   A LEU   A 140 ? 0.1184 0.1741 0.1619 0.0086  0.0056  0.0237  140 LEU   A O   
2965 O O   B LEU   A 140 ? 0.1176 0.1324 0.1184 0.0000  0.0020  0.0011  140 LEU   A O   
2966 C CB  A LEU   A 140 ? 0.1207 0.1669 0.1811 -0.0046 0.0020  0.0315  140 LEU   A CB  
2967 C CB  B LEU   A 140 ? 0.1036 0.1202 0.1073 -0.0002 0.0137  0.0104  140 LEU   A CB  
2968 C CG  A LEU   A 140 ? 0.1228 0.1804 0.1893 -0.0034 0.0152  0.0364  140 LEU   A CG  
2969 C CG  B LEU   A 140 ? 0.1029 0.1237 0.1096 0.0045  0.0133  0.0220  140 LEU   A CG  
2970 C CD1 A LEU   A 140 ? 0.1261 0.1811 0.1979 0.0077  0.0131  0.0312  140 LEU   A CD1 
2971 C CD1 B LEU   A 140 ? 0.1038 0.1261 0.0949 0.0086  0.0171  0.0173  140 LEU   A CD1 
2972 C CD2 A LEU   A 140 ? 0.1314 0.1977 0.2112 0.0007  0.0230  0.0427  140 LEU   A CD2 
2973 C CD2 B LEU   A 140 ? 0.1053 0.1313 0.1290 0.0108  0.0108  0.0334  140 LEU   A CD2 
2996 N N   A ARG   A 141 ? 0.1142 0.1818 0.1662 -0.0086 -0.0091 0.0399  141 ARG   A N   
2997 N N   B ARG   A 141 ? 0.1162 0.1359 0.1236 -0.0059 -0.0106 0.0082  141 ARG   A N   
2998 C CA  A ARG   A 141 ? 0.1368 0.1969 0.1856 -0.0165 -0.0063 0.0236  141 ARG   A CA  
2999 C CA  B ARG   A 141 ? 0.1243 0.1523 0.1357 -0.0061 -0.0118 0.0013  141 ARG   A CA  
3000 C C   A ARG   A 141 ? 0.1350 0.1843 0.1607 -0.0109 -0.0053 0.0226  141 ARG   A C   
3001 C C   B ARG   A 141 ? 0.1288 0.1623 0.1332 -0.0062 -0.0000 0.0156  141 ARG   A C   
3002 O O   A ARG   A 141 ? 0.1310 0.1766 0.1553 -0.0140 0.0065  -0.0010 141 ARG   A O   
3003 O O   B ARG   A 141 ? 0.1323 0.1572 0.1136 -0.0096 0.0173  0.0078  141 ARG   A O   
3004 C CB  A ARG   A 141 ? 0.1520 0.2197 0.2182 -0.0266 -0.0185 0.0077  141 ARG   A CB  
3005 C CB  B ARG   A 141 ? 0.1304 0.1623 0.1612 -0.0056 -0.0183 -0.0026 141 ARG   A CB  
3006 C CG  A ARG   A 141 ? 0.1851 0.2506 0.2562 -0.0278 -0.0115 0.0026  141 ARG   A CG  
3007 C CG  B ARG   A 141 ? 0.1395 0.1759 0.1876 -0.0104 -0.0180 0.0009  141 ARG   A CG  
3008 C CD  A ARG   A 141 ? 0.2071 0.2728 0.2751 -0.0350 -0.0090 0.0012  141 ARG   A CD  
3009 C CD  B ARG   A 141 ? 0.1449 0.1879 0.2062 -0.0161 -0.0176 0.0100  141 ARG   A CD  
3010 N NE  A ARG   A 141 ? 0.2094 0.2945 0.2888 -0.0401 -0.0125 0.0014  141 ARG   A NE  
3011 N NE  B ARG   A 141 ? 0.1399 0.1925 0.2155 -0.0233 -0.0235 0.0202  141 ARG   A NE  
3012 C CZ  A ARG   A 141 ? 0.2097 0.3126 0.2926 -0.0481 -0.0029 0.0076  141 ARG   A CZ  
3013 C CZ  B ARG   A 141 ? 0.1505 0.2110 0.2336 -0.0201 -0.0111 0.0329  141 ARG   A CZ  
3014 N NH1 A ARG   A 141 ? 0.2026 0.3189 0.2889 -0.0569 0.0078  -0.0011 141 ARG   A NH1 
3015 N NH1 B ARG   A 141 ? 0.1552 0.2231 0.2475 -0.0193 -0.0048 0.0332  141 ARG   A NH1 
3016 N NH2 A ARG   A 141 ? 0.2138 0.3199 0.3030 -0.0432 -0.0147 0.0144  141 ARG   A NH2 
3017 N NH2 B ARG   A 141 ? 0.1546 0.2151 0.2403 -0.0143 -0.0176 0.0377  141 ARG   A NH2 
3044 N N   . VAL   A 142 ? 0.1270 0.1830 0.1662 -0.0067 -0.0029 0.0230  142 VAL   A N   
3045 C CA  . VAL   A 142 ? 0.1272 0.1782 0.1783 -0.0089 0.0125  0.0263  142 VAL   A CA  
3046 C C   . VAL   A 142 ? 0.1147 0.1727 0.1771 -0.0065 0.0091  0.0291  142 VAL   A C   
3047 O O   . VAL   A 142 ? 0.1174 0.1670 0.1751 0.0029  0.0075  0.0247  142 VAL   A O   
3048 C CB  . VAL   A 142 ? 0.1364 0.1834 0.1762 -0.0050 0.0107  0.0295  142 VAL   A CB  
3049 C CG1 . VAL   A 142 ? 0.1387 0.1751 0.1732 -0.0045 0.0177  0.0155  142 VAL   A CG1 
3050 C CG2 . VAL   A 142 ? 0.1515 0.1987 0.1887 -0.0013 0.0104  0.0398  142 VAL   A CG2 
3061 N N   . CYS   A 143 ? 0.1219 0.1712 0.1668 -0.0019 0.0070  0.0354  143 CYS   A N   
3062 C CA  . CYS   A 143 ? 0.1214 0.1652 0.1705 -0.0038 0.0087  0.0336  143 CYS   A CA  
3063 C C   . CYS   A 143 ? 0.1165 0.1583 0.1658 -0.0027 0.0061  0.0271  143 CYS   A C   
3064 O O   . CYS   A 143 ? 0.1142 0.1523 0.1666 -0.0022 0.0061  0.0305  143 CYS   A O   
3065 C CB  . CYS   A 143 ? 0.1283 0.1655 0.1831 0.0027  0.0142  0.0325  143 CYS   A CB  
3066 S SG  . CYS   A 143 ? 0.1531 0.1670 0.1618 0.0159  0.0182  0.0278  143 CYS   A SG  
3072 N N   . VAL   A 144 ? 0.1148 0.1709 0.1856 -0.0041 0.0119  0.0346  144 VAL   A N   
3073 C CA  . VAL   A 144 ? 0.1242 0.1753 0.2094 -0.0108 0.0145  0.0341  144 VAL   A CA  
3074 C C   . VAL   A 144 ? 0.1259 0.1686 0.2068 -0.0184 -0.0053 0.0262  144 VAL   A C   
3075 O O   . VAL   A 144 ? 0.1415 0.1710 0.2093 -0.0043 -0.0083 0.0321  144 VAL   A O   
3076 C CB  . VAL   A 144 ? 0.1449 0.2025 0.2630 -0.0064 0.0303  0.0317  144 VAL   A CB  
3077 C CG1 . VAL   A 144 ? 0.1534 0.2193 0.2986 -0.0162 0.0058  0.0289  144 VAL   A CG1 
3078 C CG2 . VAL   A 144 ? 0.1271 0.2070 0.2707 -0.0039 0.0368  0.0466  144 VAL   A CG2 
3088 N N   . ASP   A 145 ? 0.1326 0.1684 0.2108 -0.0169 0.0071  0.0226  145 ASP   A N   
3089 C CA  . ASP   A 145 ? 0.1422 0.1753 0.2130 -0.0236 -0.0013 0.0132  145 ASP   A CA  
3090 C C   . ASP   A 145 ? 0.1416 0.1569 0.2130 -0.0161 0.0059  0.0041  145 ASP   A C   
3091 O O   . ASP   A 145 ? 0.1576 0.1654 0.2645 -0.0187 -0.0013 -0.0301 145 ASP   A O   
3092 C CB  . ASP   A 145 ? 0.1561 0.2001 0.2299 -0.0306 -0.0174 0.0182  145 ASP   A CB  
3093 C CG  . ASP   A 145 ? 0.1723 0.2364 0.2519 -0.0444 -0.0309 0.0228  145 ASP   A CG  
3094 O OD1 . ASP   A 145 ? 0.1649 0.2472 0.2681 -0.0527 -0.0188 0.0247  145 ASP   A OD1 
3095 O OD2 . ASP   A 145 ? 0.1910 0.2565 0.2617 -0.0512 -0.0428 0.0163  145 ASP   A OD2 
3100 N N   . THR   A 146 ? 0.1240 0.1431 0.1818 -0.0106 0.0072  0.0123  146 THR   A N   
3101 C CA  . THR   A 146 ? 0.1186 0.1378 0.1689 -0.0065 0.0037  0.0097  146 THR   A CA  
3102 C C   . THR   A 146 ? 0.1172 0.1301 0.1721 0.0007  0.0111  0.0176  146 THR   A C   
3103 O O   . THR   A 146 ? 0.1308 0.1451 0.1892 0.0095  -0.0029 0.0126  146 THR   A O   
3104 C CB  . THR   A 146 ? 0.1194 0.1442 0.1716 -0.0024 0.0044  0.0162  146 THR   A CB  
3105 O OG1 . THR   A 146 ? 0.1194 0.1624 0.1731 0.0017  0.0013  0.0096  146 THR   A OG1 
3106 C CG2 . THR   A 146 ? 0.1218 0.1443 0.1884 -0.0079 0.0088  0.0154  146 THR   A CG2 
3114 N N   . VAL   A 147 ? 0.1148 0.1339 0.1724 0.0028  0.0086  0.0168  147 VAL   A N   
3115 C CA  . VAL   A 147 ? 0.1175 0.1382 0.1706 -0.0018 0.0197  0.0212  147 VAL   A CA  
3116 C C   . VAL   A 147 ? 0.1181 0.1315 0.1807 -0.0085 0.0121  0.0237  147 VAL   A C   
3117 O O   . VAL   A 147 ? 0.1246 0.1382 0.1967 -0.0140 0.0108  0.0201  147 VAL   A O   
3118 C CB  . VAL   A 147 ? 0.1368 0.1330 0.1653 -0.0086 0.0188  0.0251  147 VAL   A CB  
3119 C CG1 . VAL   A 147 ? 0.1664 0.1376 0.1686 -0.0063 0.0205  0.0330  147 VAL   A CG1 
3120 C CG2 . VAL   A 147 ? 0.1458 0.1342 0.1718 -0.0068 0.0091  0.0221  147 VAL   A CG2 
3130 N N   . ARG   A 148 ? 0.1202 0.1318 0.1878 -0.0111 0.0138  0.0370  148 ARG   A N   
3131 C CA  . ARG   A 148 ? 0.1320 0.1347 0.1872 -0.0140 0.0065  0.0391  148 ARG   A CA  
3132 C C   . ARG   A 148 ? 0.1458 0.1344 0.1858 -0.0147 0.0078  0.0532  148 ARG   A C   
3133 O O   . ARG   A 148 ? 0.1760 0.1458 0.2011 -0.0241 0.0127  0.0475  148 ARG   A O   
3134 C CB  . ARG   A 148 ? 0.1412 0.1301 0.2022 -0.0069 0.0125  0.0315  148 ARG   A CB  
3135 C CG  . ARG   A 148 ? 0.1568 0.1320 0.2290 -0.0104 0.0214  0.0185  148 ARG   A CG  
3136 C CD  . ARG   A 148 ? 0.1729 0.1320 0.2451 -0.0076 0.0287  0.0339  148 ARG   A CD  
3137 N NE  . ARG   A 148 ? 0.1657 0.1436 0.2399 0.0107  0.0388  0.0398  148 ARG   A NE  
3138 C CZ  . ARG   A 148 ? 0.1627 0.1316 0.2306 0.0030  0.0371  0.0372  148 ARG   A CZ  
3139 N NH1 . ARG   A 148 ? 0.1751 0.1326 0.2370 -0.0060 0.0388  0.0160  148 ARG   A NH1 
3140 N NH2 . ARG   A 148 ? 0.1550 0.1478 0.2379 0.0130  0.0381  0.0391  148 ARG   A NH2 
3154 N N   . THR   A 149 ? 0.1449 0.1388 0.1708 -0.0155 -0.0011 0.0403  149 THR   A N   
3155 C CA  . THR   A 149 ? 0.1510 0.1447 0.1679 -0.0123 0.0005  0.0397  149 THR   A CA  
3156 C C   . THR   A 149 ? 0.1480 0.1434 0.1578 -0.0161 0.0060  0.0490  149 THR   A C   
3157 O O   . THR   A 149 ? 0.1445 0.1522 0.1752 -0.0144 0.0098  0.0415  149 THR   A O   
3158 C CB  . THR   A 149 ? 0.1509 0.1590 0.1736 -0.0130 0.0002  0.0316  149 THR   A CB  
3159 O OG1 . THR   A 149 ? 0.1489 0.1479 0.1826 -0.0186 0.0029  0.0341  149 THR   A OG1 
3160 C CG2 . THR   A 149 ? 0.1443 0.1687 0.1878 -0.0044 -0.0088 0.0326  149 THR   A CG2 
3168 N N   . ASN   A 150 ? 0.1494 0.1469 0.1709 -0.0102 0.0024  0.0486  150 ASN   A N   
3169 C CA  . ASN   A 150 ? 0.1660 0.1525 0.1711 -0.0146 0.0115  0.0396  150 ASN   A CA  
3170 C C   . ASN   A 150 ? 0.1468 0.1419 0.1755 -0.0172 0.0116  0.0369  150 ASN   A C   
3171 O O   . ASN   A 150 ? 0.1575 0.1508 0.2146 -0.0144 -0.0083 0.0297  150 ASN   A O   
3172 C CB  . ASN   A 150 ? 0.2110 0.1797 0.1966 -0.0210 0.0316  0.0583  150 ASN   A CB  
3173 C CG  . ASN   A 150 ? 0.2626 0.2133 0.2678 -0.0180 0.0116  0.0621  150 ASN   A CG  
3174 O OD1 . ASN   A 150 ? 0.2875 0.2167 0.2828 -0.0235 0.0076  0.0775  150 ASN   A OD1 
3175 N ND2 . ASN   A 150 ? 0.2883 0.2390 0.3066 -0.0111 -0.0004 0.0560  150 ASN   A ND2 
3182 N N   . VAL   A 151 ? 0.1489 0.1355 0.1663 -0.0164 0.0108  0.0315  151 VAL   A N   
3183 C CA  . VAL   A 151 ? 0.1576 0.1389 0.1651 -0.0208 0.0182  0.0313  151 VAL   A CA  
3184 C C   . VAL   A 151 ? 0.1451 0.1315 0.1792 -0.0266 0.0169  0.0320  151 VAL   A C   
3185 O O   . VAL   A 151 ? 0.1556 0.1431 0.2101 -0.0221 0.0158  0.0286  151 VAL   A O   
3186 C CB  . VAL   A 151 ? 0.1859 0.1560 0.1648 -0.0073 0.0168  0.0289  151 VAL   A CB  
3187 C CG1 . VAL   A 151 ? 0.1794 0.1810 0.1904 -0.0081 0.0063  0.0239  151 VAL   A CG1 
3188 C CG2 . VAL   A 151 ? 0.2007 0.1497 0.1658 -0.0036 0.0301  0.0247  151 VAL   A CG2 
3198 N N   . TYR   A 152 ? 0.1426 0.1363 0.1726 -0.0222 0.0186  0.0270  152 TYR   A N   
3199 C CA  . TYR   A 152 ? 0.1395 0.1406 0.1578 -0.0204 0.0178  0.0300  152 TYR   A CA  
3200 C C   . TYR   A 152 ? 0.1348 0.1363 0.1468 -0.0151 0.0221  0.0333  152 TYR   A C   
3201 O O   . TYR   A 152 ? 0.1451 0.1370 0.1529 -0.0245 0.0200  0.0254  152 TYR   A O   
3202 C CB  . TYR   A 152 ? 0.1583 0.1417 0.1637 -0.0130 0.0273  0.0323  152 TYR   A CB  
3203 C CG  . TYR   A 152 ? 0.1755 0.1660 0.1550 -0.0146 0.0357  0.0316  152 TYR   A CG  
3204 C CD1 . TYR   A 152 ? 0.1916 0.1882 0.1694 -0.0046 0.0312  0.0466  152 TYR   A CD1 
3205 C CD2 . TYR   A 152 ? 0.1852 0.1814 0.1423 -0.0305 0.0311  0.0290  152 TYR   A CD2 
3206 C CE1 . TYR   A 152 ? 0.2216 0.2057 0.1856 -0.0029 0.0131  0.0521  152 TYR   A CE1 
3207 C CE2 . TYR   A 152 ? 0.2088 0.2034 0.1605 -0.0357 0.0268  0.0365  152 TYR   A CE2 
3208 C CZ  . TYR   A 152 ? 0.2346 0.2068 0.1701 -0.0204 0.0109  0.0600  152 TYR   A CZ  
3209 O OH  . TYR   A 152 ? 0.2631 0.2280 0.2035 -0.0140 0.0096  0.0786  152 TYR   A OH  
3219 N N   A LEU   A 153 ? 0.1319 0.1296 0.1607 -0.0162 0.0293  0.0321  153 LEU   A N   
3220 N N   B LEU   A 153 ? 0.1335 0.1377 0.1388 -0.0098 0.0126  0.0341  153 LEU   A N   
3221 C CA  A LEU   A 153 ? 0.1290 0.1331 0.1845 -0.0101 0.0302  0.0317  153 LEU   A CA  
3222 C CA  B LEU   A 153 ? 0.1301 0.1402 0.1316 -0.0012 0.0074  0.0312  153 LEU   A CA  
3223 C C   A LEU   A 153 ? 0.1311 0.1375 0.1925 -0.0160 0.0384  0.0266  153 LEU   A C   
3224 C C   B LEU   A 153 ? 0.1300 0.1445 0.1254 0.0019  0.0063  0.0231  153 LEU   A C   
3225 O O   A LEU   A 153 ? 0.1376 0.1422 0.2235 -0.0183 0.0526  0.0226  153 LEU   A O   
3226 O O   B LEU   A 153 ? 0.1339 0.1508 0.1394 0.0006  0.0178  0.0248  153 LEU   A O   
3227 C CB  A LEU   A 153 ? 0.1285 0.1321 0.1982 -0.0133 0.0209  0.0311  153 LEU   A CB  
3228 C CB  B LEU   A 153 ? 0.1312 0.1414 0.1395 0.0032  0.0035  0.0337  153 LEU   A CB  
3229 C CG  A LEU   A 153 ? 0.1346 0.1405 0.1876 -0.0128 0.0254  0.0202  153 LEU   A CG  
3230 C CG  B LEU   A 153 ? 0.1387 0.1466 0.1434 0.0044  0.0012  0.0303  153 LEU   A CG  
3231 C CD1 A LEU   A 153 ? 0.1467 0.1401 0.1912 -0.0101 0.0059  0.0321  153 LEU   A CD1 
3232 C CD1 B LEU   A 153 ? 0.1445 0.1482 0.1535 0.0042  0.0001  0.0279  153 LEU   A CD1 
3233 C CD2 A LEU   A 153 ? 0.1434 0.1469 0.1908 -0.0126 0.0397  0.0030  153 LEU   A CD2 
3234 C CD2 B LEU   A 153 ? 0.1412 0.1508 0.1448 0.0062  0.0009  0.0228  153 LEU   A CD2 
3257 N N   A ALA   A 154 ? 0.1255 0.1321 0.1853 -0.0185 0.0327  0.0281  154 ALA   A N   
3258 N N   B ALA   A 154 ? 0.1258 0.1418 0.1044 0.0032  -0.0043 0.0133  154 ALA   A N   
3259 C CA  A ALA   A 154 ? 0.1390 0.1349 0.1904 -0.0115 0.0299  0.0320  154 ALA   A CA  
3260 C CA  B ALA   A 154 ? 0.1274 0.1379 0.0953 0.0089  -0.0061 0.0095  154 ALA   A CA  
3261 C C   A ALA   A 154 ? 0.1397 0.1352 0.1844 -0.0101 0.0248  0.0364  154 ALA   A C   
3262 C C   B ALA   A 154 ? 0.1270 0.1386 0.0866 0.0068  -0.0103 0.0118  154 ALA   A C   
3263 O O   A ALA   A 154 ? 0.1477 0.1644 0.1873 -0.0097 0.0300  0.0325  154 ALA   A O   
3264 O O   B ALA   A 154 ? 0.1292 0.1369 0.0810 0.0010  -0.0095 0.0122  154 ALA   A O   
3265 C CB  A ALA   A 154 ? 0.1453 0.1450 0.1908 -0.0001 0.0213  0.0249  154 ALA   A CB  
3266 C CB  B ALA   A 154 ? 0.1333 0.1392 0.1044 0.0091  -0.0164 0.0029  154 ALA   A CB  
3277 N N   A VAL   A 155 ? 0.1398 0.1341 0.1885 -0.0062 0.0297  0.0380  155 VAL   A N   
3278 N N   B VAL   A 155 ? 0.1253 0.1369 0.0878 0.0083  -0.0144 0.0056  155 VAL   A N   
3279 C CA  A VAL   A 155 ? 0.1469 0.1370 0.2210 -0.0049 0.0246  0.0407  155 VAL   A CA  
3280 C CA  B VAL   A 155 ? 0.1303 0.1367 0.0870 0.0020  -0.0127 0.0089  155 VAL   A CA  
3281 C C   A VAL   A 155 ? 0.1563 0.1427 0.2763 0.0013  0.0191  0.0491  155 VAL   A C   
3282 C C   B VAL   A 155 ? 0.1343 0.1359 0.1107 0.0061  -0.0182 0.0108  155 VAL   A C   
3283 O O   A VAL   A 155 ? 0.1556 0.1370 0.2905 0.0110  0.0390  0.0372  155 VAL   A O   
3284 O O   B VAL   A 155 ? 0.1311 0.1379 0.1197 0.0060  -0.0208 -0.0017 155 VAL   A O   
3285 C CB  A VAL   A 155 ? 0.1524 0.1398 0.2074 0.0034  0.0102  0.0386  155 VAL   A CB  
3286 C CB  B VAL   A 155 ? 0.1351 0.1364 0.0846 -0.0016 -0.0123 -0.0028 155 VAL   A CB  
3287 C CG1 A VAL   A 155 ? 0.1671 0.1471 0.2170 0.0096  0.0080  0.0388  155 VAL   A CG1 
3288 C CG1 B VAL   A 155 ? 0.1375 0.1366 0.0871 -0.0021 -0.0110 -0.0076 155 VAL   A CG1 
3289 C CG2 A VAL   A 155 ? 0.1641 0.1519 0.2016 0.0131  0.0038  0.0271  155 VAL   A CG2 
3290 C CG2 B VAL   A 155 ? 0.1429 0.1433 0.1022 -0.0019 -0.0073 -0.0021 155 VAL   A CG2 
3309 N N   A PHE   A 156 ? 0.1706 0.1479 0.3187 -0.0069 0.0198  0.0729  156 PHE   A N   
3310 N N   B PHE   A 156 ? 0.1360 0.1329 0.1179 0.0080  -0.0193 0.0202  156 PHE   A N   
3311 C CA  A PHE   A 156 ? 0.1865 0.1521 0.3600 0.0004  0.0158  0.0775  156 PHE   A CA  
3312 C CA  B PHE   A 156 ? 0.1488 0.1344 0.1513 0.0151  -0.0109 0.0220  156 PHE   A CA  
3313 C C   A PHE   A 156 ? 0.1789 0.1558 0.3756 0.0088  0.0233  0.0801  156 PHE   A C   
3314 C C   B PHE   A 156 ? 0.1477 0.1415 0.1490 0.0233  -0.0139 0.0275  156 PHE   A C   
3315 O O   A PHE   A 156 ? 0.1840 0.1673 0.4033 0.0146  0.0292  0.0530  156 PHE   A O   
3316 O O   B PHE   A 156 ? 0.1565 0.1513 0.1584 0.0264  -0.0160 0.0271  156 PHE   A O   
3317 C CB  A PHE   A 156 ? 0.2159 0.1578 0.3687 -0.0072 0.0067  0.0886  156 PHE   A CB  
3318 C CB  B PHE   A 156 ? 0.1563 0.1358 0.1806 0.0044  -0.0080 0.0368  156 PHE   A CB  
3319 C CG  A PHE   A 156 ? 0.2548 0.1726 0.3792 0.0089  -0.0177 0.0813  156 PHE   A CG  
3320 C CG  B PHE   A 156 ? 0.1629 0.1361 0.2023 0.0032  -0.0132 0.0416  156 PHE   A CG  
3321 C CD1 A PHE   A 156 ? 0.2743 0.1822 0.3936 0.0223  -0.0228 0.0671  156 PHE   A CD1 
3322 C CD1 B PHE   A 156 ? 0.1577 0.1313 0.2155 -0.0019 -0.0137 0.0390  156 PHE   A CD1 
3323 C CD2 A PHE   A 156 ? 0.2749 0.1851 0.3864 0.0191  -0.0279 0.0835  156 PHE   A CD2 
3324 C CD2 B PHE   A 156 ? 0.1677 0.1418 0.2159 0.0008  -0.0197 0.0450  156 PHE   A CD2 
3325 C CE1 A PHE   A 156 ? 0.2898 0.1909 0.4064 0.0272  -0.0238 0.0553  156 PHE   A CE1 
3326 C CE1 B PHE   A 156 ? 0.1578 0.1338 0.2267 -0.0055 -0.0156 0.0332  156 PHE   A CE1 
3327 C CE2 A PHE   A 156 ? 0.2914 0.1984 0.4009 0.0285  -0.0320 0.0606  156 PHE   A CE2 
3328 C CE2 B PHE   A 156 ? 0.1699 0.1433 0.2289 -0.0012 -0.0212 0.0355  156 PHE   A CE2 
3329 C CZ  A PHE   A 156 ? 0.2951 0.2006 0.4083 0.0318  -0.0287 0.0463  156 PHE   A CZ  
3330 C CZ  B PHE   A 156 ? 0.1587 0.1341 0.2302 -0.0101 -0.0181 0.0340  156 PHE   A CZ  
3349 N N   A ASP   A 157 ? 0.1775 0.1644 0.3569 0.0076  0.0211  0.0949  157 ASP   A N   
3350 N N   B ASP   A 157 ? 0.1416 0.1367 0.1437 0.0241  -0.0075 0.0217  157 ASP   A N   
3351 C CA  A ASP   A 157 ? 0.1919 0.1847 0.3542 0.0149  0.0121  0.1024  157 ASP   A CA  
3352 C CA  B ASP   A 157 ? 0.1472 0.1444 0.1561 0.0249  -0.0023 0.0271  157 ASP   A CA  
3353 C C   A ASP   A 157 ? 0.1743 0.1901 0.3620 0.0213  0.0211  0.1041  157 ASP   A C   
3354 C C   B ASP   A 157 ? 0.1474 0.1527 0.1752 0.0305  0.0015  0.0237  157 ASP   A C   
3355 O O   A ASP   A 157 ? 0.1683 0.1810 0.3374 0.0163  0.0172  0.1130  157 ASP   A O   
3356 O O   B ASP   A 157 ? 0.1520 0.1499 0.1662 0.0265  0.0019  0.0270  157 ASP   A O   
3357 C CB  A ASP   A 157 ? 0.2232 0.2062 0.3625 0.0158  0.0120  0.0988  157 ASP   A CB  
3358 C CB  B ASP   A 157 ? 0.1518 0.1465 0.1547 0.0205  -0.0029 0.0258  157 ASP   A CB  
3359 C CG  A ASP   A 157 ? 0.2561 0.2250 0.3739 0.0257  -0.0020 0.1020  157 ASP   A CG  
3360 C CG  B ASP   A 157 ? 0.1538 0.1491 0.1531 0.0200  -0.0026 0.0303  157 ASP   A CG  
3361 O OD1 A ASP   A 157 ? 0.2838 0.2363 0.3977 0.0296  -0.0213 0.0936  157 ASP   A OD1 
3362 O OD1 B ASP   A 157 ? 0.1545 0.1579 0.1507 0.0176  0.0029  0.0447  157 ASP   A OD1 
3363 O OD2 A ASP   A 157 ? 0.2491 0.2288 0.3756 0.0270  0.0016  0.1120  157 ASP   A OD2 
3364 O OD2 B ASP   A 157 ? 0.1484 0.1344 0.1694 0.0195  -0.0035 0.0250  157 ASP   A OD2 
3373 N N   A LYS   A 158 ? 0.1774 0.2026 0.3940 0.0266  0.0309  0.1034  158 LYS   A N   
3374 N N   B LYS   A 158 ? 0.1517 0.1627 0.2037 0.0361  0.0099  0.0246  158 LYS   A N   
3375 C CA  A LYS   A 158 ? 0.1831 0.2266 0.4053 0.0293  0.0463  0.1123  158 LYS   A CA  
3376 C CA  B LYS   A 158 ? 0.1557 0.1807 0.2271 0.0364  0.0150  0.0323  158 LYS   A CA  
3377 C C   A LYS   A 158 ? 0.1660 0.2360 0.3911 0.0296  0.0487  0.1346  158 LYS   A C   
3378 C C   B LYS   A 158 ? 0.1545 0.1831 0.2234 0.0384  0.0086  0.0278  158 LYS   A C   
3379 O O   A LYS   A 158 ? 0.1606 0.2324 0.3930 0.0185  0.0459  0.1426  158 LYS   A O   
3380 O O   B LYS   A 158 ? 0.1594 0.1894 0.2365 0.0391  0.0144  0.0254  158 LYS   A O   
3381 C CB  A LYS   A 158 ? 0.2069 0.2490 0.4347 0.0316  0.0702  0.1074  158 LYS   A CB  
3382 C CB  B LYS   A 158 ? 0.1634 0.1957 0.2581 0.0343  0.0313  0.0405  158 LYS   A CB  
3383 C CG  A LYS   A 158 ? 0.2229 0.2688 0.4671 0.0339  0.0949  0.1060  158 LYS   A CG  
3384 C CG  B LYS   A 158 ? 0.1679 0.2074 0.2859 0.0323  0.0442  0.0473  158 LYS   A CG  
3385 C CD  A LYS   A 158 ? 0.2327 0.2850 0.4883 0.0311  0.1202  0.1128  158 LYS   A CD  
3386 C CD  B LYS   A 158 ? 0.1731 0.2174 0.3064 0.0286  0.0543  0.0559  158 LYS   A CD  
3387 C CE  A LYS   A 158 ? 0.2393 0.2972 0.5117 0.0285  0.1389  0.1191  158 LYS   A CE  
3388 C CE  B LYS   A 158 ? 0.1777 0.2271 0.3284 0.0265  0.0619  0.0590  158 LYS   A CE  
3389 N NZ  A LYS   A 158 ? 0.2421 0.3005 0.5215 0.0237  0.1489  0.1268  158 LYS   A NZ  
3390 N NZ  B LYS   A 158 ? 0.1817 0.2304 0.3388 0.0242  0.0638  0.0632  158 LYS   A NZ  
3417 N N   A ASN   A 159 ? 0.1742 0.2530 0.3988 0.0395  0.0352  0.1347  159 ASN   A N   
3418 N N   B ASN   A 159 ? 0.1523 0.1762 0.2077 0.0330  -0.0083 0.0196  159 ASN   A N   
3419 C CA  A ASN   A 159 ? 0.1798 0.2663 0.3997 0.0450  0.0160  0.1436  159 ASN   A CA  
3420 C CA  B ASN   A 159 ? 0.1497 0.1742 0.1952 0.0266  -0.0280 0.0164  159 ASN   A CA  
3421 C C   A ASN   A 159 ? 0.1638 0.2582 0.3563 0.0270  0.0123  0.1365  159 ASN   A C   
3422 C C   B ASN   A 159 ? 0.1432 0.1686 0.1831 0.0196  -0.0220 0.0093  159 ASN   A C   
3423 O O   A ASN   A 159 ? 0.1514 0.2709 0.3581 0.0245  -0.0028 0.1274  159 ASN   A O   
3424 O O   B ASN   A 159 ? 0.1331 0.1659 0.1841 0.0230  -0.0303 -0.0016 159 ASN   A O   
3425 C CB  A ASN   A 159 ? 0.2059 0.2861 0.4499 0.0553  0.0194  0.1534  159 ASN   A CB  
3426 C CB  B ASN   A 159 ? 0.1571 0.1861 0.2023 0.0192  -0.0409 0.0193  159 ASN   A CB  
3427 C CG  A ASN   A 159 ? 0.2390 0.3040 0.4993 0.0529  0.0310  0.1515  159 ASN   A CG  
3428 C CG  B ASN   A 159 ? 0.1686 0.2016 0.2172 0.0104  -0.0413 0.0206  159 ASN   A CG  
3429 O OD1 A ASN   A 159 ? 0.2478 0.3122 0.5167 0.0512  0.0410  0.1510  159 ASN   A OD1 
3430 O OD1 B ASN   A 159 ? 0.1819 0.2193 0.2450 0.0182  -0.0279 0.0108  159 ASN   A OD1 
3431 N ND2 A ASN   A 159 ? 0.2559 0.3115 0.5213 0.0510  0.0338  0.1436  159 ASN   A ND2 
3432 N ND2 B ASN   A 159 ? 0.1701 0.2008 0.2154 0.0027  -0.0443 0.0283  159 ASN   A ND2 
3445 N N   A LEU   A 160 ? 0.1524 0.2427 0.3178 0.0149  -0.0006 0.1274  160 LEU   A N   
3446 N N   B LEU   A 160 ? 0.1411 0.1608 0.1652 0.0127  -0.0127 0.0018  160 LEU   A N   
3447 C CA  A LEU   A 160 ? 0.1502 0.2269 0.2880 0.0048  0.0050  0.1155  160 LEU   A CA  
3448 C CA  B LEU   A 160 ? 0.1375 0.1490 0.1354 0.0100  -0.0150 0.0090  160 LEU   A CA  
3449 C C   A LEU   A 160 ? 0.1369 0.2180 0.2744 0.0056  0.0127  0.1067  160 LEU   A C   
3450 C C   B LEU   A 160 ? 0.1333 0.1423 0.1275 0.0095  -0.0038 0.0139  160 LEU   A C   
3451 O O   A LEU   A 160 ? 0.1365 0.2230 0.2905 0.0000  0.0062  0.0962  160 LEU   A O   
3452 O O   B LEU   A 160 ? 0.1354 0.1425 0.1333 0.0082  0.0012  0.0070  160 LEU   A O   
3453 C CB  A LEU   A 160 ? 0.1634 0.2301 0.2609 -0.0045 -0.0007 0.1064  160 LEU   A CB  
3454 C CB  B LEU   A 160 ? 0.1413 0.1464 0.1252 0.0028  -0.0083 0.0100  160 LEU   A CB  
3455 C CG  A LEU   A 160 ? 0.1686 0.2372 0.2517 -0.0161 0.0030  0.0791  160 LEU   A CG  
3456 C CG  B LEU   A 160 ? 0.1416 0.1462 0.1220 -0.0078 -0.0042 0.0078  160 LEU   A CG  
3457 C CD1 A LEU   A 160 ? 0.1825 0.2449 0.2518 -0.0147 0.0044  0.0640  160 LEU   A CD1 
3458 C CD1 B LEU   A 160 ? 0.1466 0.1472 0.1264 -0.0136 -0.0063 0.0060  160 LEU   A CD1 
3459 C CD2 A LEU   A 160 ? 0.1641 0.2394 0.2541 -0.0162 0.0073  0.0656  160 LEU   A CD2 
3460 C CD2 B LEU   A 160 ? 0.1381 0.1456 0.1177 -0.0081 0.0027  0.0046  160 LEU   A CD2 
3483 N N   A TYR   A 161 ? 0.1308 0.2065 0.2616 0.0055  0.0267  0.0981  161 TYR   A N   
3484 N N   B TYR   A 161 ? 0.1347 0.1391 0.1297 0.0139  0.0001  0.0191  161 TYR   A N   
3485 C CA  A TYR   A 161 ? 0.1326 0.1975 0.2626 0.0072  0.0272  0.0973  161 TYR   A CA  
3486 C CA  B TYR   A 161 ? 0.1396 0.1433 0.1326 0.0150  0.0077  0.0212  161 TYR   A CA  
3487 C C   A TYR   A 161 ? 0.1275 0.2111 0.2764 0.0128  0.0161  0.0974  161 TYR   A C   
3488 C C   B TYR   A 161 ? 0.1450 0.1561 0.1477 0.0138  0.0119  0.0281  161 TYR   A C   
3489 O O   A TYR   A 161 ? 0.1201 0.2071 0.2576 0.0069  0.0151  0.0935  161 TYR   A O   
3490 O O   B TYR   A 161 ? 0.1437 0.1564 0.1385 0.0091  0.0142  0.0210  161 TYR   A O   
3491 C CB  A TYR   A 161 ? 0.1441 0.1889 0.2600 0.0092  0.0302  0.0770  161 TYR   A CB  
3492 C CB  B TYR   A 161 ? 0.1411 0.1417 0.1381 0.0161  0.0090  0.0115  161 TYR   A CB  
3493 C CG  A TYR   A 161 ? 0.1494 0.1856 0.2534 0.0043  0.0299  0.0576  161 TYR   A CG  
3494 C CG  B TYR   A 161 ? 0.1427 0.1421 0.1418 0.0190  0.0087  0.0079  161 TYR   A CG  
3495 C CD1 A TYR   A 161 ? 0.1450 0.1787 0.2571 0.0012  0.0296  0.0453  161 TYR   A CD1 
3496 C CD1 B TYR   A 161 ? 0.1398 0.1370 0.1442 0.0158  0.0102  0.0037  161 TYR   A CD1 
3497 C CD2 A TYR   A 161 ? 0.1540 0.1955 0.2502 0.0154  0.0268  0.0453  161 TYR   A CD2 
3498 C CD2 B TYR   A 161 ? 0.1454 0.1509 0.1476 0.0264  0.0045  0.0112  161 TYR   A CD2 
3499 C CE1 A TYR   A 161 ? 0.1530 0.1724 0.2542 0.0013  0.0243  0.0453  161 TYR   A CE1 
3500 C CE1 B TYR   A 161 ? 0.1456 0.1428 0.1560 0.0153  0.0059  0.0089  161 TYR   A CE1 
3501 C CE2 A TYR   A 161 ? 0.1556 0.1879 0.2491 0.0092  0.0250  0.0447  161 TYR   A CE2 
3502 C CE2 B TYR   A 161 ? 0.1507 0.1552 0.1570 0.0214  0.0054  0.0189  161 TYR   A CE2 
3503 C CZ  A TYR   A 161 ? 0.1579 0.1752 0.2546 -0.0061 0.0247  0.0515  161 TYR   A CZ  
3504 C CZ  B TYR   A 161 ? 0.1518 0.1542 0.1627 0.0146  0.0046  0.0238  161 TYR   A CZ  
3505 O OH  A TYR   A 161 ? 0.1730 0.1797 0.2652 -0.0110 0.0249  0.0582  161 TYR   A OH  
3506 O OH  B TYR   A 161 ? 0.1583 0.1661 0.1721 0.0148  -0.0037 0.0369  161 TYR   A OH  
3525 N N   A ASP   A 162 ? 0.1276 0.2285 0.3155 0.0140  0.0194  0.1110  162 ASP   A N   
3526 N N   B ASP   A 162 ? 0.1501 0.1731 0.1797 0.0147  0.0177  0.0409  162 ASP   A N   
3527 C CA  A ASP   A 162 ? 0.1257 0.2585 0.3315 0.0033  0.0238  0.1234  162 ASP   A CA  
3528 C CA  B ASP   A 162 ? 0.1560 0.1966 0.2068 0.0101  0.0210  0.0504  162 ASP   A CA  
3529 C C   A ASP   A 162 ? 0.1156 0.2744 0.3259 -0.0026 0.0231  0.1347  162 ASP   A C   
3530 C C   B ASP   A 162 ? 0.1627 0.2131 0.2163 0.0079  0.0157  0.0496  162 ASP   A C   
3531 O O   A ASP   A 162 ? 0.1186 0.2747 0.3438 -0.0070 0.0257  0.1289  162 ASP   A O   
3532 O O   B ASP   A 162 ? 0.1666 0.2126 0.2182 0.0095  0.0180  0.0445  162 ASP   A O   
3533 C CB  A ASP   A 162 ? 0.1330 0.2717 0.3632 0.0044  0.0309  0.1110  162 ASP   A CB  
3534 C CB  B ASP   A 162 ? 0.1546 0.2024 0.2213 0.0081  0.0288  0.0571  162 ASP   A CB  
3535 C CG  A ASP   A 162 ? 0.1450 0.2889 0.3912 0.0104  0.0410  0.0930  162 ASP   A CG  
3536 C CG  B ASP   A 162 ? 0.1535 0.2100 0.2361 0.0055  0.0341  0.0619  162 ASP   A CG  
3537 O OD1 A ASP   A 162 ? 0.1616 0.2992 0.4065 0.0004  0.0333  0.0819  162 ASP   A OD1 
3538 O OD1 B ASP   A 162 ? 0.1621 0.2165 0.2486 -0.0018 0.0250  0.0559  162 ASP   A OD1 
3539 O OD2 A ASP   A 162 ? 0.1606 0.2964 0.4125 0.0208  0.0546  0.0800  162 ASP   A OD2 
3540 O OD2 B ASP   A 162 ? 0.1498 0.2121 0.2386 0.0053  0.0520  0.0673  162 ASP   A OD2 
3549 N N   A LYS   A 163 ? 0.1249 0.2962 0.3298 0.0055  0.0005  0.1358  163 LYS   A N   
3550 N N   B LYS   A 163 ? 0.1736 0.2309 0.2271 0.0089  0.0037  0.0556  163 LYS   A N   
3551 C CA  A LYS   A 163 ? 0.1420 0.3134 0.3276 0.0040  -0.0050 0.1366  163 LYS   A CA  
3552 C CA  B LYS   A 163 ? 0.1845 0.2458 0.2438 0.0043  0.0004  0.0559  163 LYS   A CA  
3553 C C   A LYS   A 163 ? 0.1329 0.2959 0.3120 -0.0007 0.0084  0.1340  163 LYS   A C   
3554 C C   B LYS   A 163 ? 0.1723 0.2366 0.2304 -0.0003 0.0054  0.0587  163 LYS   A C   
3555 O O   A LYS   A 163 ? 0.1260 0.3075 0.3286 -0.0131 0.0114  0.1226  163 LYS   A O   
3556 O O   B LYS   A 163 ? 0.1722 0.2440 0.2341 -0.0040 0.0086  0.0538  163 LYS   A O   
3557 C CB  A LYS   A 163 ? 0.1864 0.3447 0.3566 0.0209  -0.0253 0.1353  163 LYS   A CB  
3558 C CB  B LYS   A 163 ? 0.2118 0.2677 0.2832 0.0099  -0.0073 0.0518  163 LYS   A CB  
3559 C CG  A LYS   A 163 ? 0.2309 0.3758 0.4052 0.0212  -0.0169 0.1237  163 LYS   A CG  
3560 C CG  B LYS   A 163 ? 0.2374 0.2869 0.3228 0.0109  -0.0068 0.0462  163 LYS   A CG  
3561 C CD  A LYS   A 163 ? 0.2684 0.4020 0.4554 0.0220  -0.0155 0.1149  163 LYS   A CD  
3562 C CD  B LYS   A 163 ? 0.2590 0.3038 0.3627 0.0110  -0.0058 0.0413  163 LYS   A CD  
3563 C CE  A LYS   A 163 ? 0.2964 0.4184 0.4975 0.0209  -0.0103 0.1091  163 LYS   A CE  
3564 C CE  B LYS   A 163 ? 0.2753 0.3153 0.3944 0.0103  -0.0022 0.0380  163 LYS   A CE  
3565 N NZ  A LYS   A 163 ? 0.3073 0.4273 0.5228 0.0204  -0.0084 0.1063  163 LYS   A NZ  
3566 N NZ  B LYS   A 163 ? 0.2842 0.3211 0.4128 0.0100  -0.0018 0.0361  163 LYS   A NZ  
3593 N N   A LEU   A 164 ? 0.1213 0.2624 0.2890 -0.0064 0.0077  0.1263  164 LEU   A N   
3594 N N   B LEU   A 164 ? 0.1557 0.2140 0.2162 -0.0054 0.0041  0.0614  164 LEU   A N   
3595 C CA  A LEU   A 164 ? 0.1232 0.2356 0.2756 -0.0067 0.0175  0.1003  164 LEU   A CA  
3596 C CA  B LEU   A 164 ? 0.1430 0.1932 0.1995 -0.0105 0.0123  0.0600  164 LEU   A CA  
3597 C C   A LEU   A 164 ? 0.1350 0.2189 0.2729 -0.0003 0.0195  0.0823  164 LEU   A C   
3598 C C   B LEU   A 164 ? 0.1400 0.1858 0.1918 -0.0075 0.0197  0.0526  164 LEU   A C   
3599 O O   A LEU   A 164 ? 0.1410 0.2280 0.2701 -0.0103 0.0418  0.0565  164 LEU   A O   
3600 O O   B LEU   A 164 ? 0.1386 0.1906 0.1840 -0.0089 0.0336  0.0445  164 LEU   A O   
3601 C CB  A LEU   A 164 ? 0.1246 0.2225 0.2573 -0.0003 0.0227  0.1011  164 LEU   A CB  
3602 C CB  B LEU   A 164 ? 0.1395 0.1819 0.1887 -0.0150 0.0138  0.0675  164 LEU   A CB  
3603 C CG  A LEU   A 164 ? 0.1348 0.2173 0.2684 0.0052  0.0219  0.0916  164 LEU   A CG  
3604 C CG  B LEU   A 164 ? 0.1415 0.1785 0.1938 -0.0141 0.0088  0.0574  164 LEU   A CG  
3605 C CD1 A LEU   A 164 ? 0.1298 0.2038 0.2665 0.0107  0.0110  0.0995  164 LEU   A CD1 
3606 C CD1 B LEU   A 164 ? 0.1418 0.1805 0.2069 -0.0129 0.0098  0.0486  164 LEU   A CD1 
3607 C CD2 A LEU   A 164 ? 0.1486 0.2188 0.2718 0.0033  0.0196  0.0868  164 LEU   A CD2 
3608 C CD2 B LEU   A 164 ? 0.1463 0.1751 0.1881 -0.0121 0.0006  0.0513  164 LEU   A CD2 
3631 N N   A VAL   A 165 ? 0.1239 0.1962 0.2678 -0.0058 0.0124  0.0817  165 VAL   A N   
3632 N N   B VAL   A 165 ? 0.1332 0.1729 0.1917 -0.0081 0.0192  0.0468  165 VAL   A N   
3633 C CA  A VAL   A 165 ? 0.1378 0.1915 0.2631 -0.0074 0.0181  0.0782  165 VAL   A CA  
3634 C CA  B VAL   A 165 ? 0.1330 0.1612 0.1801 -0.0102 0.0230  0.0429  165 VAL   A CA  
3635 C C   A VAL   A 165 ? 0.1295 0.1988 0.2566 -0.0039 0.0233  0.0797  165 VAL   A C   
3636 C C   B VAL   A 165 ? 0.1253 0.1615 0.1809 -0.0065 0.0185  0.0495  165 VAL   A C   
3637 O O   A VAL   A 165 ? 0.1304 0.2027 0.2565 -0.0064 0.0217  0.0737  165 VAL   A O   
3638 O O   B VAL   A 165 ? 0.1225 0.1488 0.1834 -0.0048 0.0141  0.0537  165 VAL   A O   
3639 C CB  A VAL   A 165 ? 0.1519 0.1844 0.2601 -0.0067 0.0256  0.0698  165 VAL   A CB  
3640 C CB  B VAL   A 165 ? 0.1396 0.1536 0.1783 -0.0118 0.0241  0.0341  165 VAL   A CB  
3641 C CG1 A VAL   A 165 ? 0.1562 0.1880 0.2629 0.0010  0.0272  0.0635  165 VAL   A CG1 
3642 C CG1 B VAL   A 165 ? 0.1456 0.1543 0.1810 -0.0165 0.0274  0.0380  165 VAL   A CG1 
3643 C CG2 A VAL   A 165 ? 0.1672 0.1850 0.2661 -0.0027 0.0256  0.0636  165 VAL   A CG2 
3644 C CG2 B VAL   A 165 ? 0.1462 0.1503 0.1754 -0.0127 0.0284  0.0254  165 VAL   A CG2 
3663 N N   A SER   A 166 ? 0.1196 0.2089 0.2745 0.0003  0.0270  0.0733  166 SER   A N   
3664 N N   B SER   A 166 ? 0.1224 0.1747 0.1961 -0.0086 0.0182  0.0480  166 SER   A N   
3665 C CA  A SER   A 166 ? 0.1262 0.2303 0.2920 -0.0008 0.0190  0.0641  166 SER   A CA  
3666 C CA  B SER   A 166 ? 0.1253 0.1892 0.2066 -0.0128 0.0146  0.0475  166 SER   A CA  
3667 C C   A SER   A 166 ? 0.1390 0.2492 0.2798 -0.0014 0.0038  0.0554  166 SER   A C   
3668 C C   B SER   A 166 ? 0.1305 0.1978 0.2153 -0.0181 0.0129  0.0296  166 SER   A C   
3669 O O   A SER   A 166 ? 0.1668 0.2624 0.3114 -0.0036 0.0128  0.0351  166 SER   A O   
3670 O O   B SER   A 166 ? 0.1349 0.1968 0.2384 -0.0173 0.0146  0.0191  166 SER   A O   
3671 C CB  A SER   A 166 ? 0.1468 0.2507 0.3460 0.0074  0.0068  0.0431  166 SER   A CB  
3672 C CB  B SER   A 166 ? 0.1359 0.2017 0.2156 -0.0077 0.0176  0.0559  166 SER   A CB  
3673 O OG  A SER   A 166 ? 0.1623 0.2754 0.3900 -0.0036 0.0174  0.0506  166 SER   A OG  
3674 O OG  B SER   A 166 ? 0.1460 0.2174 0.2384 -0.0054 0.0274  0.0510  166 SER   A OG  
3685 N N   A SER   A 167 ? 0.1409 0.2627 0.2515 0.0083  -0.0115 0.0571  167 SER   A N   
3686 N N   B SER   A 167 ? 0.1434 0.2042 0.1990 -0.0190 0.0082  0.0180  167 SER   A N   
3687 C CA  A SER   A 167 ? 0.1614 0.2734 0.2386 0.0077  -0.0145 0.0477  167 SER   A CA  
3688 C CA  B SER   A 167 ? 0.1689 0.2160 0.1891 -0.0111 0.0052  0.0028  167 SER   A CA  
3689 C C   A SER   A 167 ? 0.1646 0.2771 0.2313 0.0113  0.0005  0.0491  167 SER   A C   
3690 C C   B SER   A 167 ? 0.1886 0.2231 0.1897 -0.0063 0.0096  -0.0083 167 SER   A C   
3691 O O   A SER   A 167 ? 0.1860 0.2804 0.2459 0.0137  -0.0142 0.0498  167 SER   A O   
3692 O O   B SER   A 167 ? 0.1969 0.2278 0.1877 -0.0025 0.0049  -0.0136 167 SER   A O   
3693 C CB  A SER   A 167 ? 0.1752 0.2793 0.2430 0.0092  -0.0090 0.0497  167 SER   A CB  
3694 C CB  B SER   A 167 ? 0.1700 0.2180 0.1769 -0.0052 0.0084  0.0008  167 SER   A CB  
3695 O OG  A SER   A 167 ? 0.1822 0.2802 0.2343 0.0059  0.0044  0.0491  167 SER   A OG  
3696 O OG  B SER   A 167 ? 0.1673 0.2172 0.1677 -0.0016 0.0221  -0.0015 167 SER   A OG  
3707 N N   A PHE   A 168 ? 0.1485 0.2754 0.2169 0.0180  0.0113  0.0440  168 PHE   A N   
3708 N N   B PHE   A 168 ? 0.2010 0.2274 0.2022 -0.0072 0.0066  -0.0088 168 PHE   A N   
3709 C CA  A PHE   A 168 ? 0.1441 0.2782 0.2304 0.0171  0.0201  0.0343  168 PHE   A CA  
3710 C CA  B PHE   A 168 ? 0.2175 0.2309 0.2257 -0.0088 0.0037  -0.0131 168 PHE   A CA  
3711 C C   A PHE   A 168 ? 0.1541 0.3080 0.2631 0.0059  0.0590  0.0103  168 PHE   A C   
3712 C C   B PHE   A 168 ? 0.2466 0.2581 0.2792 -0.0129 0.0072  -0.0103 168 PHE   A C   
3713 O O   A PHE   A 168 ? 0.1645 0.3053 0.2917 -0.0100 0.0620  0.0157  168 PHE   A O   
3714 O O   B PHE   A 168 ? 0.2503 0.2601 0.2883 -0.0143 0.0107  -0.0065 168 PHE   A O   
3715 C CB  A PHE   A 168 ? 0.1438 0.2574 0.2179 0.0141  0.0001  0.0359  168 PHE   A CB  
3716 C CB  B PHE   A 168 ? 0.2070 0.2120 0.2065 -0.0119 -0.0016 -0.0172 168 PHE   A CB  
3717 C CG  A PHE   A 168 ? 0.1376 0.2408 0.2026 0.0097  0.0006  0.0420  168 PHE   A CG  
3718 C CG  B PHE   A 168 ? 0.1953 0.1946 0.1884 -0.0147 -0.0072 -0.0209 168 PHE   A CG  
3719 C CD1 A PHE   A 168 ? 0.1448 0.2412 0.2081 -0.0037 -0.0019 0.0476  168 PHE   A CD1 
3720 C CD1 B PHE   A 168 ? 0.1886 0.1876 0.1816 -0.0193 -0.0148 -0.0247 168 PHE   A CD1 
3721 C CD2 A PHE   A 168 ? 0.1342 0.2376 0.2007 0.0100  0.0130  0.0367  168 PHE   A CD2 
3722 C CD2 B PHE   A 168 ? 0.1901 0.1857 0.1815 -0.0132 -0.0041 -0.0248 168 PHE   A CD2 
3723 C CE1 A PHE   A 168 ? 0.1357 0.2403 0.2026 -0.0026 -0.0010 0.0482  168 PHE   A CE1 
3724 C CE1 B PHE   A 168 ? 0.1829 0.1863 0.1768 -0.0204 -0.0184 -0.0278 168 PHE   A CE1 
3725 C CE2 A PHE   A 168 ? 0.1388 0.2305 0.2074 0.0073  0.0112  0.0437  168 PHE   A CE2 
3726 C CE2 B PHE   A 168 ? 0.1870 0.1855 0.1804 -0.0152 -0.0067 -0.0254 168 PHE   A CE2 
3727 C CZ  A PHE   A 168 ? 0.1382 0.2342 0.2093 0.0033  0.0048  0.0428  168 PHE   A CZ  
3728 C CZ  B PHE   A 168 ? 0.1839 0.1875 0.1764 -0.0173 -0.0143 -0.0265 168 PHE   A CZ  
3747 N N   A LEU   A 169 ? 0.1912 0.3415 0.3062 -0.0018 0.0707  -0.0121 169 LEU   A N   
3748 N N   B LEU   A 169 ? 0.2725 0.2834 0.3263 -0.0144 0.0104  -0.0114 169 LEU   A N   
3749 C CA  A LEU   A 169 ? 0.2468 0.3774 0.3832 0.0011  0.0464  -0.0339 169 LEU   A CA  
3750 C CA  B LEU   A 169 ? 0.3018 0.3086 0.3730 -0.0143 0.0076  -0.0111 169 LEU   A CA  
3751 C C   A LEU   A 169 ? 0.2497 0.3833 0.4163 0.0037  0.0432  -0.0287 169 LEU   A C   
3752 C C   B LEU   A 169 ? 0.3094 0.3149 0.3897 -0.0184 0.0062  -0.0025 169 LEU   A C   
3753 O O   A LEU   A 169 ? 0.2582 0.3855 0.4273 0.0053  0.0403  -0.0304 169 LEU   A O   
3754 O O   B LEU   A 169 ? 0.3120 0.3171 0.3971 -0.0228 0.0058  0.0029  169 LEU   A O   
3755 C CB  A LEU   A 169 ? 0.2890 0.4017 0.4169 -0.0022 0.0253  -0.0543 169 LEU   A CB  
3756 C CB  B LEU   A 169 ? 0.3189 0.3245 0.3969 -0.0110 0.0067  -0.0180 169 LEU   A CB  
3757 C CG  A LEU   A 169 ? 0.3258 0.4209 0.4446 -0.0070 0.0083  -0.0739 169 LEU   A CG  
3758 C CG  B LEU   A 169 ? 0.3325 0.3370 0.4170 -0.0098 0.0067  -0.0260 169 LEU   A CG  
3759 C CD1 A LEU   A 169 ? 0.3377 0.4259 0.4589 -0.0081 0.0016  -0.0797 169 LEU   A CD1 
3760 C CD1 B LEU   A 169 ? 0.3370 0.3402 0.4250 -0.0079 0.0072  -0.0273 169 LEU   A CD1 
3761 C CD2 A LEU   A 169 ? 0.3385 0.4288 0.4500 -0.0094 0.0039  -0.0796 169 LEU   A CD2 
3762 C CD2 B LEU   A 169 ? 0.3367 0.3413 0.4228 -0.0101 0.0070  -0.0299 169 LEU   A CD2 
3763 O OXT A LEU   A 169 ? 0.2360 0.3850 0.4187 0.0060  0.0450  -0.0245 169 LEU   A OXT 
3764 O OXT B LEU   A 169 ? 0.3112 0.3166 0.3941 -0.0172 0.0070  -0.0008 169 LEU   A OXT 
3787 N N   A SER   B 1   ? 0.3459 0.3296 0.3582 -0.1035 -0.0770 0.0416  1   SER   B N   
3788 N N   B SER   B 1   ? 0.3455 0.3427 0.3399 -0.0504 -0.0426 0.0204  1   SER   B N   
3789 C CA  A SER   B 1   ? 0.3340 0.3290 0.3567 -0.1114 -0.0837 0.0361  1   SER   B CA  
3790 C CA  B SER   B 1   ? 0.3417 0.3430 0.3411 -0.0511 -0.0429 0.0197  1   SER   B CA  
3791 C C   A SER   B 1   ? 0.3078 0.3333 0.3339 -0.1106 -0.0901 0.0578  1   SER   B C   
3792 C C   B SER   B 1   ? 0.3335 0.3433 0.3345 -0.0483 -0.0460 0.0274  1   SER   B C   
3793 O O   A SER   B 1   ? 0.3146 0.3309 0.3001 -0.1051 -0.0896 0.0560  1   SER   B O   
3794 O O   B SER   B 1   ? 0.3353 0.3425 0.3220 -0.0481 -0.0481 0.0256  1   SER   B O   
3795 C CB  A SER   B 1   ? 0.3445 0.3239 0.3840 -0.1144 -0.0763 0.0096  1   SER   B CB  
3796 C CB  B SER   B 1   ? 0.3443 0.3426 0.3520 -0.0527 -0.0382 0.0104  1   SER   B CB  
3797 O OG  A SER   B 1   ? 0.3595 0.3310 0.4265 -0.1122 -0.0627 0.0007  1   SER   B OG  
3798 O OG  B SER   B 1   ? 0.3482 0.3460 0.3675 -0.0534 -0.0340 0.0063  1   SER   B OG  
3813 N N   A MET   B 2   ? 0.2826 0.3383 0.3483 -0.1063 -0.0827 0.0972  2   MET   B N   
3814 N N   B MET   B 2   ? 0.3245 0.3435 0.3420 -0.0438 -0.0443 0.0409  2   MET   B N   
3815 C CA  A MET   B 2   ? 0.2616 0.3386 0.3724 -0.0893 -0.0799 0.1201  2   MET   B CA  
3816 C CA  B MET   B 2   ? 0.3135 0.3405 0.3495 -0.0370 -0.0420 0.0517  2   MET   B CA  
3817 C C   A MET   B 2   ? 0.2209 0.3105 0.3404 -0.0760 -0.0916 0.1543  2   MET   B C   
3818 C C   B MET   B 2   ? 0.2900 0.3197 0.3197 -0.0352 -0.0422 0.0614  2   MET   B C   
3819 O O   A MET   B 2   ? 0.2129 0.3244 0.3406 -0.0627 -0.1062 0.1574  2   MET   B O   
3820 O O   B MET   B 2   ? 0.2914 0.3250 0.3222 -0.0329 -0.0411 0.0619  2   MET   B O   
3821 C CB  A MET   B 2   ? 0.2929 0.3741 0.4578 -0.0699 -0.0556 0.0927  2   MET   B CB  
3822 C CB  B MET   B 2   ? 0.3268 0.3584 0.3938 -0.0295 -0.0378 0.0498  2   MET   B CB  
3823 C CG  A MET   B 2   ? 0.3208 0.4057 0.5324 -0.0514 -0.0362 0.0755  2   MET   B CG  
3824 C CG  B MET   B 2   ? 0.3385 0.3738 0.4317 -0.0227 -0.0354 0.0504  2   MET   B CG  
3825 S SD  A MET   B 2   ? 0.3463 0.4340 0.6010 -0.0352 -0.0233 0.0614  2   MET   B SD  
3826 S SD  B MET   B 2   ? 0.3479 0.3870 0.4647 -0.0163 -0.0362 0.0516  2   MET   B SD  
3827 C CE  A MET   B 2   ? 0.3484 0.4418 0.6089 -0.0334 -0.0128 0.0588  2   MET   B CE  
3828 C CE  B MET   B 2   ? 0.3487 0.3890 0.4726 -0.0165 -0.0334 0.0499  2   MET   B CE  
3847 N N   A VAL   B 3   ? 0.1955 0.2695 0.3138 -0.0805 -0.0842 0.1639  3   VAL   B N   
3848 N N   B VAL   B 3   ? 0.2642 0.2920 0.2890 -0.0372 -0.0442 0.0679  3   VAL   B N   
3849 C CA  A VAL   B 3   ? 0.1988 0.2335 0.3086 -0.0731 -0.0739 0.1403  3   VAL   B CA  
3850 C CA  B VAL   B 3   ? 0.2407 0.2632 0.2655 -0.0376 -0.0448 0.0677  3   VAL   B CA  
3851 C C   A VAL   B 3   ? 0.1875 0.2249 0.2662 -0.0597 -0.0680 0.1147  3   VAL   B C   
3852 C C   B VAL   B 3   ? 0.2124 0.2371 0.2346 -0.0405 -0.0509 0.0737  3   VAL   B C   
3853 O O   A VAL   B 3   ? 0.1867 0.2325 0.2751 -0.0613 -0.0699 0.1222  3   VAL   B O   
3854 O O   B VAL   B 3   ? 0.2111 0.2400 0.2215 -0.0324 -0.0539 0.0757  3   VAL   B O   
3855 C CB  A VAL   B 3   ? 0.2220 0.2287 0.3664 -0.0674 -0.0693 0.1160  3   VAL   B CB  
3856 C CB  B VAL   B 3   ? 0.2471 0.2622 0.2802 -0.0355 -0.0387 0.0605  3   VAL   B CB  
3857 C CG1 A VAL   B 3   ? 0.2283 0.2228 0.3863 -0.0666 -0.0665 0.1103  3   VAL   B CG1 
3858 C CG1 B VAL   B 3   ? 0.2486 0.2612 0.2871 -0.0357 -0.0368 0.0575  3   VAL   B CG1 
3859 C CG2 A VAL   B 3   ? 0.2306 0.2357 0.3874 -0.0658 -0.0598 0.1121  3   VAL   B CG2 
3860 C CG2 B VAL   B 3   ? 0.2502 0.2634 0.2854 -0.0344 -0.0356 0.0604  3   VAL   B CG2 
3879 N N   . ASN   B 4   ? 0.1871 0.2067 0.2265 -0.0530 -0.0575 0.0775  4   ASN   B N   
3880 C CA  . ASN   B 4   ? 0.1831 0.1970 0.1899 -0.0528 -0.0440 0.0399  4   ASN   B CA  
3881 C C   . ASN   B 4   ? 0.1913 0.2068 0.1822 -0.0512 -0.0301 0.0250  4   ASN   B C   
3882 O O   . ASN   B 4   ? 0.1934 0.2135 0.1996 -0.0477 -0.0250 0.0125  4   ASN   B O   
3883 C CB  . ASN   B 4   ? 0.1809 0.1944 0.1715 -0.0397 -0.0482 0.0341  4   ASN   B CB  
3884 C CG  . ASN   B 4   ? 0.1755 0.1792 0.1598 -0.0408 -0.0482 0.0274  4   ASN   B CG  
3885 O OD1 . ASN   B 4   ? 0.1756 0.1680 0.1704 -0.0372 -0.0435 0.0273  4   ASN   B OD1 
3886 N ND2 . ASN   B 4   ? 0.1938 0.1880 0.1712 -0.0235 -0.0323 0.0204  4   ASN   B ND2 
3894 N N   . SER   B 5   ? 0.2100 0.2212 0.1834 -0.0501 -0.0106 0.0290  5   SER   B N   
3895 C CA  . SER   B 5   ? 0.2349 0.2542 0.2179 -0.0398 0.0112  0.0325  5   SER   B CA  
3896 C C   . SER   B 5   ? 0.2483 0.2616 0.2496 -0.0599 0.0294  0.0326  5   SER   B C   
3897 O O   . SER   B 5   ? 0.2614 0.2625 0.3154 -0.0506 0.0546  0.0295  5   SER   B O   
3898 C CB  . SER   B 5   ? 0.2481 0.2786 0.2518 -0.0300 0.0118  0.0404  5   SER   B CB  
3899 O OG  . SER   B 5   ? 0.2704 0.3120 0.3111 -0.0209 0.0060  0.0479  5   SER   B OG  
3905 N N   . PHE   B 6   ? 0.2657 0.2817 0.2257 -0.0656 0.0429  0.0344  6   PHE   B N   
3906 C CA  . PHE   B 6   ? 0.2753 0.2867 0.1960 -0.0830 0.0505  0.0153  6   PHE   B CA  
3907 C C   . PHE   B 6   ? 0.3317 0.3167 0.2479 -0.0834 0.0697  -0.0126 6   PHE   B C   
3908 O O   . PHE   B 6   ? 0.3450 0.3451 0.2753 -0.0723 0.0517  -0.0282 6   PHE   B O   
3909 C CB  . PHE   B 6   ? 0.2426 0.2655 0.1730 -0.0750 0.0217  0.0103  6   PHE   B CB  
3910 C CG  . PHE   B 6   ? 0.2114 0.2319 0.1695 -0.0684 0.0062  0.0088  6   PHE   B CG  
3911 C CD1 . PHE   B 6   ? 0.2063 0.2035 0.1545 -0.0609 -0.0093 0.0029  6   PHE   B CD1 
3912 C CD2 . PHE   B 6   ? 0.1935 0.2312 0.1786 -0.0547 0.0075  0.0358  6   PHE   B CD2 
3913 C CE1 . PHE   B 6   ? 0.2022 0.1861 0.1661 -0.0497 -0.0125 0.0029  6   PHE   B CE1 
3914 C CE2 . PHE   B 6   ? 0.1958 0.2144 0.2056 -0.0430 0.0079  0.0334  6   PHE   B CE2 
3915 C CZ  . PHE   B 6   ? 0.1973 0.1925 0.1821 -0.0452 0.0056  0.0159  6   PHE   B CZ  
3925 N N   A SER   B 7   ? 0.3592 0.3024 0.2464 -0.1013 0.0966  -0.0358 7   SER   B N   
3926 N N   B SER   B 7   ? 0.3452 0.3129 0.2707 -0.0881 0.0719  -0.0159 7   SER   B N   
3927 C CA  A SER   B 7   ? 0.3859 0.3053 0.2842 -0.1021 0.1193  -0.0435 7   SER   B CA  
3928 C CA  B SER   B 7   ? 0.3579 0.3136 0.3041 -0.0866 0.0740  -0.0159 7   SER   B CA  
3929 C C   A SER   B 7   ? 0.3835 0.2929 0.2702 -0.1054 0.1347  -0.0538 7   SER   B C   
3930 C C   B SER   B 7   ? 0.3583 0.3034 0.2996 -0.0885 0.0773  -0.0209 7   SER   B C   
3931 O O   A SER   B 7   ? 0.3906 0.2972 0.2936 -0.1048 0.1350  -0.0487 7   SER   B O   
3932 O O   B SER   B 7   ? 0.3613 0.3062 0.3074 -0.0884 0.0764  -0.0169 7   SER   B O   
3933 C CB  A SER   B 7   ? 0.4073 0.3192 0.3485 -0.0975 0.1277  -0.0413 7   SER   B CB  
3934 C CB  B SER   B 7   ? 0.3665 0.3226 0.3403 -0.0827 0.0734  -0.0132 7   SER   B CB  
3935 O OG  A SER   B 7   ? 0.4211 0.3331 0.3982 -0.0950 0.1288  -0.0410 7   SER   B OG  
3936 O OG  B SER   B 7   ? 0.3715 0.3297 0.3648 -0.0800 0.0714  -0.0131 7   SER   B OG  
3947 N N   A GLY   B 8   ? 0.3763 0.2803 0.2717 -0.0978 0.1382  -0.0645 8   GLY   B N   
3948 N N   B GLY   B 8   ? 0.3554 0.2894 0.2950 -0.0872 0.0805  -0.0307 8   GLY   B N   
3949 C CA  A GLY   B 8   ? 0.3645 0.2650 0.2740 -0.0901 0.1364  -0.0716 8   GLY   B CA  
3950 C CA  B GLY   B 8   ? 0.3503 0.2727 0.2869 -0.0856 0.0850  -0.0407 8   GLY   B CA  
3951 C C   A GLY   B 8   ? 0.3484 0.2464 0.2704 -0.0891 0.1334  -0.0620 8   GLY   B C   
3952 C C   B GLY   B 8   ? 0.3430 0.2535 0.2739 -0.0854 0.0939  -0.0483 8   GLY   B C   
3953 O O   A GLY   B 8   ? 0.3564 0.2470 0.3029 -0.0826 0.1352  -0.0654 8   GLY   B O   
3954 O O   B GLY   B 8   ? 0.3469 0.2563 0.2844 -0.0826 0.0886  -0.0486 8   GLY   B O   
3961 N N   . TYR   B 9   ? 0.3348 0.2333 0.2525 -0.0828 0.1027  -0.0609 9   TYR   B N   
3962 C CA  . TYR   B 9   ? 0.3131 0.2001 0.2210 -0.0670 0.0761  -0.0448 9   TYR   B CA  
3963 C C   . TYR   B 9   ? 0.3060 0.2016 0.2052 -0.0604 0.0392  -0.0340 9   TYR   B C   
3964 O O   . TYR   B 9   ? 0.3179 0.2245 0.2435 -0.0578 0.0330  -0.0198 9   TYR   B O   
3965 C CB  . TYR   B 9   ? 0.3079 0.1792 0.2271 -0.0530 0.0781  -0.0392 9   TYR   B CB  
3966 C CG  . TYR   B 9   ? 0.3024 0.1569 0.2235 -0.0576 0.0746  -0.0388 9   TYR   B CG  
3967 C CD1 . TYR   B 9   ? 0.3094 0.1594 0.2406 -0.0708 0.0741  -0.0376 9   TYR   B CD1 
3968 C CD2 . TYR   B 9   ? 0.2879 0.1510 0.2137 -0.0482 0.0762  -0.0441 9   TYR   B CD2 
3969 C CE1 . TYR   B 9   ? 0.3053 0.1670 0.2526 -0.0749 0.0743  -0.0482 9   TYR   B CE1 
3970 C CE2 . TYR   B 9   ? 0.2893 0.1516 0.2299 -0.0476 0.0684  -0.0458 9   TYR   B CE2 
3971 C CZ  . TYR   B 9   ? 0.2939 0.1676 0.2524 -0.0664 0.0699  -0.0610 9   TYR   B CZ  
3972 O OH  . TYR   B 9   ? 0.2860 0.1856 0.2714 -0.0809 0.0669  -0.0776 9   TYR   B OH  
3983 N N   . LEU   B 10  ? 0.2844 0.1770 0.1784 -0.0555 0.0169  -0.0371 10  LEU   B N   
3984 C CA  . LEU   B 10  ? 0.2797 0.1749 0.1799 -0.0612 -0.0101 -0.0343 10  LEU   B CA  
3985 C C   . LEU   B 10  ? 0.2569 0.1712 0.1755 -0.0589 -0.0190 -0.0295 10  LEU   B C   
3986 O O   . LEU   B 10  ? 0.2431 0.1722 0.1796 -0.0469 -0.0118 -0.0247 10  LEU   B O   
3987 C CB  . LEU   B 10  ? 0.2963 0.1729 0.1956 -0.0655 -0.0262 -0.0192 10  LEU   B CB  
3988 C CG  . LEU   B 10  ? 0.3162 0.1825 0.2362 -0.0613 -0.0456 -0.0072 10  LEU   B CG  
3989 C CD1 . LEU   B 10  ? 0.3292 0.1976 0.2646 -0.0563 -0.0452 -0.0053 10  LEU   B CD1 
3990 C CD2 . LEU   B 10  ? 0.3270 0.1896 0.2690 -0.0601 -0.0366 0.0145  10  LEU   B CD2 
4002 N N   . LYS   B 11  ? 0.2675 0.2012 0.1776 -0.0542 -0.0257 -0.0291 11  LYS   B N   
4003 C CA  . LYS   B 11  ? 0.2826 0.2272 0.2007 -0.0426 -0.0391 -0.0300 11  LYS   B CA  
4004 C C   . LYS   B 11  ? 0.2636 0.2105 0.2094 -0.0620 -0.0402 -0.0396 11  LYS   B C   
4005 O O   . LYS   B 11  ? 0.2791 0.2318 0.2479 -0.0739 -0.0351 -0.0723 11  LYS   B O   
4006 C CB  . LYS   B 11  ? 0.3187 0.2767 0.2629 -0.0122 -0.0398 -0.0213 11  LYS   B CB  
4007 C CG  . LYS   B 11  ? 0.3485 0.3112 0.3295 0.0039  -0.0419 -0.0222 11  LYS   B CG  
4008 C CD  . LYS   B 11  ? 0.3713 0.3380 0.3929 0.0147  -0.0403 -0.0290 11  LYS   B CD  
4009 C CE  . LYS   B 11  ? 0.3884 0.3557 0.4410 0.0200  -0.0366 -0.0313 11  LYS   B CE  
4010 N NZ  . LYS   B 11  ? 0.3979 0.3652 0.4700 0.0224  -0.0353 -0.0311 11  LYS   B NZ  
4024 N N   . LEU   B 12  ? 0.2319 0.1848 0.2114 -0.0560 -0.0348 -0.0383 12  LEU   B N   
4025 C CA  . LEU   B 12  ? 0.2186 0.1702 0.2291 -0.0511 -0.0297 -0.0286 12  LEU   B CA  
4026 C C   . LEU   B 12  ? 0.2083 0.1693 0.2383 -0.0516 -0.0449 -0.0245 12  LEU   B C   
4027 O O   . LEU   B 12  ? 0.2111 0.1728 0.2702 -0.0625 -0.0563 -0.0181 12  LEU   B O   
4028 C CB  . LEU   B 12  ? 0.2212 0.1554 0.2311 -0.0445 -0.0170 -0.0271 12  LEU   B CB  
4029 C CG  . LEU   B 12  ? 0.2209 0.1530 0.2360 -0.0433 -0.0150 -0.0241 12  LEU   B CG  
4030 C CD1 . LEU   B 12  ? 0.2294 0.1530 0.2336 -0.0282 -0.0140 -0.0102 12  LEU   B CD1 
4031 C CD2 . LEU   B 12  ? 0.2288 0.1599 0.2561 -0.0454 -0.0123 -0.0300 12  LEU   B CD2 
4043 N N   . THR   B 13  ? 0.2006 0.1734 0.2455 -0.0484 -0.0396 -0.0367 13  THR   B N   
4044 C CA  . THR   B 13  ? 0.2009 0.1819 0.2370 -0.0500 -0.0480 -0.0277 13  THR   B CA  
4045 C C   . THR   B 13  ? 0.2342 0.1950 0.2519 -0.0589 -0.0644 -0.0178 13  THR   B C   
4046 O O   . THR   B 13  ? 0.2509 0.1938 0.2652 -0.0570 -0.0306 -0.0128 13  THR   B O   
4047 C CB  . THR   B 13  ? 0.1803 0.1811 0.2429 -0.0480 -0.0432 -0.0208 13  THR   B CB  
4048 O OG1 . THR   B 13  ? 0.1708 0.1758 0.2501 -0.0378 -0.0334 -0.0242 13  THR   B OG1 
4049 C CG2 . THR   B 13  ? 0.1923 0.1889 0.2485 -0.0427 -0.0350 -0.0065 13  THR   B CG2 
4057 N N   A ASP   B 14  ? 0.2470 0.2122 0.2621 -0.0650 -0.1010 -0.0064 14  ASP   B N   
4058 N N   B ASP   B 14  ? 0.2419 0.2042 0.2638 -0.0587 -0.0728 -0.0092 14  ASP   B N   
4059 C CA  A ASP   B 14  ? 0.2597 0.2288 0.2936 -0.0627 -0.1071 0.0119  14  ASP   B CA  
4060 C CA  B ASP   B 14  ? 0.2479 0.2135 0.2794 -0.0565 -0.0740 0.0022  14  ASP   B CA  
4061 C C   A ASP   B 14  ? 0.2466 0.2128 0.2559 -0.0650 -0.0856 0.0193  14  ASP   B C   
4062 C C   B ASP   B 14  ? 0.2333 0.1996 0.2482 -0.0575 -0.0741 0.0092  14  ASP   B C   
4063 O O   A ASP   B 14  ? 0.2709 0.2307 0.2576 -0.0641 -0.0863 0.0274  14  ASP   B O   
4064 O O   B ASP   B 14  ? 0.2423 0.2020 0.2442 -0.0573 -0.0767 0.0088  14  ASP   B O   
4065 C CB  A ASP   B 14  ? 0.2863 0.2662 0.3755 -0.0552 -0.1189 0.0104  14  ASP   B CB  
4066 C CB  B ASP   B 14  ? 0.2679 0.2372 0.3275 -0.0518 -0.0705 0.0032  14  ASP   B CB  
4067 C CG  A ASP   B 14  ? 0.3159 0.3021 0.4573 -0.0477 -0.1157 -0.0034 14  ASP   B CG  
4068 C CG  B ASP   B 14  ? 0.2866 0.2550 0.3703 -0.0470 -0.0657 -0.0013 14  ASP   B CG  
4069 O OD1 A ASP   B 14  ? 0.3328 0.3144 0.4732 -0.0475 -0.1147 -0.0203 14  ASP   B OD1 
4070 O OD1 B ASP   B 14  ? 0.2924 0.2624 0.3793 -0.0459 -0.0622 -0.0054 14  ASP   B OD1 
4071 O OD2 A ASP   B 14  ? 0.3213 0.3173 0.4954 -0.0459 -0.1137 -0.0010 14  ASP   B OD2 
4072 O OD2 B ASP   B 14  ? 0.2932 0.2598 0.3871 -0.0484 -0.0665 -0.0020 14  ASP   B OD2 
4081 N N   . ASN   B 15  ? 0.2103 0.1834 0.2226 -0.0532 -0.0758 0.0127  15  ASN   B N   
4082 C CA  . ASN   B 15  ? 0.1719 0.1579 0.2021 -0.0346 -0.0463 0.0044  15  ASN   B CA  
4083 C C   . ASN   B 15  ? 0.1595 0.1429 0.1905 -0.0244 -0.0342 -0.0022 15  ASN   B C   
4084 O O   . ASN   B 15  ? 0.1612 0.1371 0.2190 -0.0221 -0.0424 -0.0150 15  ASN   B O   
4085 C CB  . ASN   B 15  ? 0.1681 0.1505 0.2193 -0.0135 -0.0437 0.0019  15  ASN   B CB  
4086 C CG  . ASN   B 15  ? 0.1595 0.1498 0.2273 -0.0192 -0.0215 0.0009  15  ASN   B CG  
4087 O OD1 . ASN   B 15  ? 0.1674 0.1782 0.2532 -0.0421 -0.0277 0.0108  15  ASN   B OD1 
4088 N ND2 . ASN   B 15  ? 0.1587 0.1328 0.2162 -0.0172 0.0005  -0.0150 15  ASN   B ND2 
4096 N N   . VAL   B 16  ? 0.1623 0.1335 0.1877 -0.0321 -0.0413 -0.0013 16  VAL   B N   
4097 C CA  . VAL   B 16  ? 0.1625 0.1369 0.1830 -0.0269 -0.0326 -0.0197 16  VAL   B CA  
4098 C C   . VAL   B 16  ? 0.1606 0.1469 0.1774 -0.0324 -0.0312 -0.0150 16  VAL   B C   
4099 O O   . VAL   B 16  ? 0.1634 0.1635 0.2032 -0.0335 -0.0208 -0.0346 16  VAL   B O   
4100 C CB  . VAL   B 16  ? 0.1676 0.1373 0.1953 -0.0166 -0.0208 -0.0148 16  VAL   B CB  
4101 C CG1 . VAL   B 16  ? 0.1743 0.1349 0.1951 -0.0037 -0.0118 -0.0143 16  VAL   B CG1 
4102 C CG2 . VAL   B 16  ? 0.1645 0.1448 0.2193 -0.0142 -0.0111 -0.0168 16  VAL   B CG2 
4112 N N   . TYR   B 17  ? 0.1638 0.1482 0.1848 -0.0270 -0.0284 -0.0215 17  TYR   B N   
4113 C CA  . TYR   B 17  ? 0.1718 0.1611 0.1773 -0.0397 -0.0304 -0.0071 17  TYR   B CA  
4114 C C   . TYR   B 17  ? 0.1672 0.1398 0.1793 -0.0352 -0.0213 -0.0106 17  TYR   B C   
4115 O O   . TYR   B 17  ? 0.1608 0.1503 0.1858 -0.0261 -0.0298 -0.0315 17  TYR   B O   
4116 C CB  . TYR   B 17  ? 0.2036 0.2040 0.1925 -0.0272 -0.0272 0.0264  17  TYR   B CB  
4117 C CG  . TYR   B 17  ? 0.2304 0.2542 0.2252 -0.0154 -0.0314 0.0309  17  TYR   B CG  
4118 C CD1 . TYR   B 17  ? 0.2420 0.2655 0.2422 -0.0125 -0.0416 0.0440  17  TYR   B CD1 
4119 C CD2 . TYR   B 17  ? 0.2497 0.2818 0.2524 -0.0063 -0.0379 0.0248  17  TYR   B CD2 
4120 C CE1 . TYR   B 17  ? 0.2618 0.2861 0.2623 -0.0038 -0.0522 0.0391  17  TYR   B CE1 
4121 C CE2 . TYR   B 17  ? 0.2646 0.2982 0.2712 0.0022  -0.0569 0.0314  17  TYR   B CE2 
4122 C CZ  . TYR   B 17  ? 0.2749 0.3059 0.2745 0.0054  -0.0639 0.0400  17  TYR   B CZ  
4123 O OH  . TYR   B 17  ? 0.2902 0.3290 0.3013 0.0135  -0.0715 0.0429  17  TYR   B OH  
4133 N N   . ILE   B 18  ? 0.1780 0.1381 0.1666 -0.0328 -0.0109 -0.0168 18  ILE   B N   
4134 C CA  . ILE   B 18  ? 0.1809 0.1369 0.1571 -0.0320 -0.0145 -0.0216 18  ILE   B CA  
4135 C C   . ILE   B 18  ? 0.1979 0.1388 0.1591 -0.0365 -0.0021 -0.0281 18  ILE   B C   
4136 O O   . ILE   B 18  ? 0.2156 0.1538 0.1782 -0.0294 0.0074  -0.0374 18  ILE   B O   
4137 C CB  . ILE   B 18  ? 0.1864 0.1406 0.1788 -0.0381 -0.0081 -0.0110 18  ILE   B CB  
4138 C CG1 . ILE   B 18  ? 0.1853 0.1500 0.1834 -0.0404 -0.0084 -0.0003 18  ILE   B CG1 
4139 C CG2 . ILE   B 18  ? 0.1887 0.1477 0.1898 -0.0381 -0.0121 -0.0093 18  ILE   B CG2 
4140 C CD1 . ILE   B 18  ? 0.1932 0.1788 0.2077 -0.0378 -0.0271 0.0191  18  ILE   B CD1 
4152 N N   . LYS   B 19  ? 0.1961 0.1410 0.1737 -0.0244 0.0247  -0.0334 19  LYS   B N   
4153 C CA  . LYS   B 19  ? 0.2032 0.1457 0.1865 -0.0246 0.0250  -0.0314 19  LYS   B CA  
4154 C C   . LYS   B 19  ? 0.1831 0.1449 0.2005 -0.0227 0.0302  -0.0386 19  LYS   B C   
4155 O O   . LYS   B 19  ? 0.1745 0.1513 0.1953 -0.0103 0.0182  -0.0376 19  LYS   B O   
4156 C CB  . LYS   B 19  ? 0.2272 0.1637 0.2048 -0.0301 0.0391  -0.0242 19  LYS   B CB  
4157 C CG  . LYS   B 19  ? 0.2487 0.1871 0.2257 -0.0332 0.0445  -0.0285 19  LYS   B CG  
4158 C CD  . LYS   B 19  ? 0.2708 0.2209 0.2380 -0.0404 0.0474  -0.0212 19  LYS   B CD  
4159 C CE  . LYS   B 19  ? 0.2965 0.2482 0.2529 -0.0435 0.0464  -0.0190 19  LYS   B CE  
4160 N NZ  . LYS   B 19  ? 0.3174 0.2649 0.2602 -0.0496 0.0513  -0.0134 19  LYS   B NZ  
4174 N N   . ASN   B 20  ? 0.1817 0.1577 0.2339 -0.0175 0.0384  -0.0543 20  ASN   B N   
4175 C CA  . ASN   B 20  ? 0.1806 0.1733 0.2615 -0.0107 0.0385  -0.0646 20  ASN   B CA  
4176 C C   . ASN   B 20  ? 0.1799 0.1880 0.2653 -0.0184 0.0520  -0.0746 20  ASN   B C   
4177 O O   . ASN   B 20  ? 0.1992 0.2196 0.2844 -0.0322 0.0514  -0.0720 20  ASN   B O   
4178 C CB  . ASN   B 20  ? 0.2055 0.1763 0.2867 0.0094  0.0311  -0.0645 20  ASN   B CB  
4179 C CG  . ASN   B 20  ? 0.2294 0.1851 0.3111 0.0356  0.0286  -0.0752 20  ASN   B CG  
4180 O OD1 . ASN   B 20  ? 0.2557 0.2125 0.3385 0.0497  0.0254  -0.0769 20  ASN   B OD1 
4181 N ND2 . ASN   B 20  ? 0.2214 0.1832 0.3078 0.0353  0.0192  -0.0766 20  ASN   B ND2 
4188 N N   . ALA   B 21  ? 0.1800 0.1729 0.2713 -0.0278 0.0515  -0.0574 21  ALA   B N   
4189 C CA  . ALA   B 21  ? 0.1897 0.1769 0.2827 -0.0329 0.0379  -0.0449 21  ALA   B CA  
4190 C C   . ALA   B 21  ? 0.1892 0.1544 0.2685 -0.0201 0.0392  -0.0345 21  ALA   B C   
4191 O O   . ALA   B 21  ? 0.1934 0.1502 0.2655 -0.0291 0.0335  -0.0276 21  ALA   B O   
4192 C CB  . ALA   B 21  ? 0.2037 0.2047 0.2976 -0.0434 0.0293  -0.0296 21  ALA   B CB  
4198 N N   . ASP   B 22  ? 0.1824 0.1456 0.2661 -0.0187 0.0352  -0.0298 22  ASP   B N   
4199 C CA  . ASP   B 22  ? 0.1775 0.1427 0.2581 -0.0116 0.0232  -0.0253 22  ASP   B CA  
4200 C C   . ASP   B 22  ? 0.1708 0.1396 0.2114 -0.0142 0.0156  -0.0109 22  ASP   B C   
4201 O O   . ASP   B 22  ? 0.1755 0.1448 0.2098 -0.0106 0.0096  -0.0037 22  ASP   B O   
4202 C CB  . ASP   B 22  ? 0.1818 0.1536 0.3037 -0.0074 0.0194  -0.0090 22  ASP   B CB  
4203 C CG  . ASP   B 22  ? 0.1842 0.1718 0.3471 0.0005  -0.0046 -0.0054 22  ASP   B CG  
4204 O OD1 . ASP   B 22  ? 0.1962 0.1702 0.3467 0.0054  -0.0219 -0.0087 22  ASP   B OD1 
4205 O OD2 . ASP   B 22  ? 0.1950 0.1972 0.3926 0.0121  -0.0233 -0.0100 22  ASP   B OD2 
4210 N N   . ILE   B 23  ? 0.1675 0.1367 0.1884 -0.0084 -0.0000 0.0135  23  ILE   B N   
4211 C CA  . ILE   B 23  ? 0.1616 0.1348 0.1737 -0.0086 -0.0026 0.0095  23  ILE   B CA  
4212 C C   . ILE   B 23  ? 0.1532 0.1353 0.1697 -0.0055 -0.0070 0.0072  23  ILE   B C   
4213 O O   . ILE   B 23  ? 0.1457 0.1389 0.1695 -0.0066 0.0007  0.0054  23  ILE   B O   
4214 C CB  . ILE   B 23  ? 0.1613 0.1431 0.1885 -0.0184 -0.0011 0.0121  23  ILE   B CB  
4215 C CG1 . ILE   B 23  ? 0.1639 0.1522 0.2003 -0.0112 0.0050  0.0264  23  ILE   B CG1 
4216 C CG2 . ILE   B 23  ? 0.1713 0.1609 0.1952 -0.0128 -0.0042 0.0027  23  ILE   B CG2 
4217 C CD1 . ILE   B 23  ? 0.1666 0.1624 0.2110 -0.0079 0.0096  0.0164  23  ILE   B CD1 
4229 N N   . VAL   B 24  ? 0.1564 0.1321 0.1896 -0.0062 -0.0136 0.0025  24  VAL   B N   
4230 C CA  . VAL   B 24  ? 0.1513 0.1362 0.2121 -0.0043 -0.0163 -0.0061 24  VAL   B CA  
4231 C C   . VAL   B 24  ? 0.1459 0.1441 0.2163 -0.0101 -0.0115 0.0020  24  VAL   B C   
4232 O O   . VAL   B 24  ? 0.1481 0.1507 0.2309 -0.0153 -0.0100 0.0147  24  VAL   B O   
4233 C CB  . VAL   B 24  ? 0.1632 0.1609 0.2198 0.0037  -0.0283 -0.0036 24  VAL   B CB  
4234 C CG1 . VAL   B 24  ? 0.1633 0.1669 0.2432 -0.0090 -0.0245 -0.0009 24  VAL   B CG1 
4235 C CG2 . VAL   B 24  ? 0.1743 0.1842 0.2217 0.0108  -0.0258 -0.0099 24  VAL   B CG2 
4245 N N   . GLU   B 25  ? 0.1655 0.1603 0.2150 -0.0086 -0.0035 0.0063  25  GLU   B N   
4246 C CA  . GLU   B 25  ? 0.1741 0.1849 0.2342 0.0059  0.0139  -0.0031 25  GLU   B CA  
4247 C C   . GLU   B 25  ? 0.1691 0.1711 0.2059 -0.0073 0.0119  -0.0003 25  GLU   B C   
4248 O O   . GLU   B 25  ? 0.1787 0.1896 0.2217 -0.0082 0.0142  0.0101  25  GLU   B O   
4249 C CB  . GLU   B 25  ? 0.2114 0.2283 0.3013 0.0279  0.0248  -0.0113 25  GLU   B CB  
4250 C CG  . GLU   B 25  ? 0.2593 0.2846 0.4006 0.0360  0.0171  -0.0229 25  GLU   B CG  
4251 C CD  . GLU   B 25  ? 0.2963 0.3415 0.4841 0.0303  0.0140  -0.0317 25  GLU   B CD  
4252 O OE1 . GLU   B 25  ? 0.3169 0.3634 0.5146 0.0327  0.0194  -0.0306 25  GLU   B OE1 
4253 O OE2 . GLU   B 25  ? 0.3145 0.3541 0.5163 0.0280  0.0108  -0.0399 25  GLU   B OE2 
4260 N N   . GLU   B 26  ? 0.1696 0.1627 0.1878 -0.0193 0.0062  -0.0020 26  GLU   B N   
4261 C CA  . GLU   B 26  ? 0.1696 0.1748 0.1885 -0.0284 -0.0031 0.0016  26  GLU   B CA  
4262 C C   . GLU   B 26  ? 0.1581 0.1696 0.1786 -0.0174 0.0062  0.0176  26  GLU   B C   
4263 O O   . GLU   B 26  ? 0.1808 0.1942 0.1883 -0.0229 0.0066  0.0269  26  GLU   B O   
4264 C CB  . GLU   B 26  ? 0.1969 0.1941 0.2028 -0.0384 -0.0058 0.0080  26  GLU   B CB  
4265 C CG  . GLU   B 26  ? 0.2439 0.2304 0.2533 -0.0444 0.0019  -0.0175 26  GLU   B CG  
4266 C CD  . GLU   B 26  ? 0.2779 0.2532 0.2788 -0.0691 0.0193  -0.0494 26  GLU   B CD  
4267 O OE1 . GLU   B 26  ? 0.3010 0.2327 0.2810 -0.0839 0.0638  -0.0419 26  GLU   B OE1 
4268 O OE2 . GLU   B 26  ? 0.2800 0.2948 0.3150 -0.0646 0.0218  -0.0347 26  GLU   B OE2 
4275 N N   . ALA   B 27  ? 0.1412 0.1569 0.1860 -0.0203 0.0090  0.0215  27  ALA   B N   
4276 C CA  . ALA   B 27  ? 0.1462 0.1555 0.1952 -0.0143 0.0041  0.0297  27  ALA   B CA  
4277 C C   . ALA   B 27  ? 0.1513 0.1621 0.2209 -0.0095 0.0154  0.0446  27  ALA   B C   
4278 O O   . ALA   B 27  ? 0.1636 0.1666 0.2312 -0.0010 0.0175  0.0487  27  ALA   B O   
4279 C CB  . ALA   B 27  ? 0.1586 0.1446 0.2010 -0.0128 0.0016  0.0223  27  ALA   B CB  
4285 N N   . LYS   B 28  ? 0.1428 0.1795 0.2631 -0.0143 0.0205  0.0630  28  LYS   B N   
4286 C CA  . LYS   B 28  ? 0.1637 0.2233 0.2973 -0.0010 0.0508  0.0909  28  LYS   B CA  
4287 C C   . LYS   B 28  ? 0.1849 0.2409 0.2867 0.0076  0.0647  0.0779  28  LYS   B C   
4288 O O   . LYS   B 28  ? 0.2117 0.2475 0.2994 0.0030  0.0654  0.0781  28  LYS   B O   
4289 C CB  . LYS   B 28  ? 0.1861 0.2643 0.3461 0.0136  0.0707  0.1123  28  LYS   B CB  
4290 C CG  . LYS   B 28  ? 0.2142 0.3067 0.3839 0.0261  0.0760  0.1290  28  LYS   B CG  
4291 C CD  . LYS   B 28  ? 0.2627 0.3600 0.4369 0.0344  0.0862  0.1331  28  LYS   B CD  
4292 C CE  . LYS   B 28  ? 0.3037 0.4035 0.4812 0.0431  0.0843  0.1383  28  LYS   B CE  
4293 N NZ  . LYS   B 28  ? 0.3152 0.4069 0.5038 0.0502  0.0805  0.1452  28  LYS   B NZ  
4307 N N   . LYS   B 29  ? 0.1993 0.2671 0.2835 0.0270  0.0687  0.0653  29  LYS   B N   
4308 C CA  . LYS   B 29  ? 0.2421 0.3017 0.2977 0.0269  0.0690  0.0621  29  LYS   B CA  
4309 C C   . LYS   B 29  ? 0.2349 0.3017 0.2530 0.0270  0.0532  0.0747  29  LYS   B C   
4310 O O   . LYS   B 29  ? 0.2525 0.3222 0.2554 0.0315  0.0550  0.0803  29  LYS   B O   
4311 C CB  . LYS   B 29  ? 0.3019 0.3393 0.3804 0.0233  0.0689  0.0507  29  LYS   B CB  
4312 C CG  . LYS   B 29  ? 0.3479 0.3695 0.4644 0.0194  0.0738  0.0482  29  LYS   B CG  
4313 C CD  . LYS   B 29  ? 0.3827 0.3913 0.5321 0.0136  0.0821  0.0438  29  LYS   B CD  
4314 C CE  . LYS   B 29  ? 0.4107 0.4067 0.5784 0.0093  0.0898  0.0406  29  LYS   B CE  
4315 N NZ  . LYS   B 29  ? 0.4213 0.4161 0.6042 0.0088  0.0927  0.0384  29  LYS   B NZ  
4329 N N   . VAL   B 30  ? 0.2055 0.2819 0.2368 0.0179  0.0407  0.0702  30  VAL   B N   
4330 C CA  . VAL   B 30  ? 0.1946 0.2677 0.2581 0.0017  0.0063  0.0694  30  VAL   B CA  
4331 C C   . VAL   B 30  ? 0.1730 0.2584 0.2456 -0.0058 0.0058  0.0860  30  VAL   B C   
4332 O O   . VAL   B 30  ? 0.1877 0.2692 0.2525 0.0024  0.0063  0.0949  30  VAL   B O   
4333 C CB  . VAL   B 30  ? 0.2026 0.2618 0.2962 -0.0153 -0.0198 0.0612  30  VAL   B CB  
4334 C CG1 . VAL   B 30  ? 0.2075 0.2719 0.2950 -0.0156 -0.0145 0.0541  30  VAL   B CG1 
4335 C CG2 . VAL   B 30  ? 0.2101 0.2565 0.3135 -0.0261 -0.0298 0.0551  30  VAL   B CG2 
4345 N N   . LYS   B 31  ? 0.1622 0.2232 0.2735 -0.0224 0.0024  0.0998  31  LYS   B N   
4346 C CA  . LYS   B 31  ? 0.1582 0.2162 0.3003 -0.0318 -0.0074 0.1010  31  LYS   B CA  
4347 C C   . LYS   B 31  ? 0.1512 0.1735 0.2733 -0.0306 -0.0258 0.0792  31  LYS   B C   
4348 O O   . LYS   B 31  ? 0.1622 0.1871 0.2897 -0.0209 -0.0192 0.0880  31  LYS   B O   
4349 C CB  . LYS   B 31  ? 0.1793 0.2642 0.3555 -0.0309 0.0195  0.1139  31  LYS   B CB  
4350 C CG  . LYS   B 31  ? 0.2121 0.3158 0.4044 -0.0252 0.0284  0.1040  31  LYS   B CG  
4351 C CD  . LYS   B 31  ? 0.2459 0.3675 0.4486 -0.0214 0.0227  0.0920  31  LYS   B CD  
4352 C CE  . LYS   B 31  ? 0.2778 0.3969 0.4899 -0.0190 0.0135  0.0784  31  LYS   B CE  
4353 N NZ  . LYS   B 31  ? 0.2816 0.4147 0.5069 -0.0135 0.0033  0.0663  31  LYS   B NZ  
4367 N N   . PRO   B 32  ? 0.1580 0.1449 0.2283 -0.0268 -0.0384 0.0440  32  PRO   B N   
4368 C CA  . PRO   B 32  ? 0.1664 0.1446 0.1810 -0.0280 -0.0418 0.0301  32  PRO   B CA  
4369 C C   . PRO   B 32  ? 0.1752 0.1378 0.1814 -0.0316 -0.0517 0.0370  32  PRO   B C   
4370 O O   . PRO   B 32  ? 0.1840 0.1399 0.2111 -0.0353 -0.0714 0.0326  32  PRO   B O   
4371 C CB  . PRO   B 32  ? 0.1835 0.1379 0.1800 -0.0334 -0.0342 0.0164  32  PRO   B CB  
4372 C CG  . PRO   B 32  ? 0.1970 0.1261 0.1872 -0.0288 -0.0481 0.0165  32  PRO   B CG  
4373 C CD  . PRO   B 32  ? 0.1844 0.1315 0.2076 -0.0218 -0.0519 0.0215  32  PRO   B CD  
4381 N N   . THR   B 33  ? 0.1757 0.1287 0.1636 -0.0259 -0.0473 0.0211  33  THR   B N   
4382 C CA  . THR   B 33  ? 0.1831 0.1338 0.1611 -0.0318 -0.0436 0.0249  33  THR   B CA  
4383 C C   . THR   B 33  ? 0.1864 0.1266 0.1557 -0.0289 -0.0426 0.0180  33  THR   B C   
4384 O O   . THR   B 33  ? 0.2079 0.1292 0.1662 -0.0376 -0.0510 0.0173  33  THR   B O   
4385 C CB  . THR   B 33  ? 0.1943 0.1454 0.1662 -0.0156 -0.0502 0.0285  33  THR   B CB  
4386 O OG1 . THR   B 33  ? 0.1839 0.1528 0.1770 -0.0200 -0.0457 0.0352  33  THR   B OG1 
4387 C CG2 . THR   B 33  ? 0.2179 0.1498 0.1835 -0.0032 -0.0489 0.0169  33  THR   B CG2 
4395 N N   . VAL   B 34  ? 0.1691 0.1235 0.1478 -0.0324 -0.0369 0.0138  34  VAL   B N   
4396 C CA  . VAL   B 34  ? 0.1561 0.1218 0.1395 -0.0243 -0.0245 0.0095  34  VAL   B CA  
4397 C C   . VAL   B 34  ? 0.1437 0.1182 0.1259 -0.0252 -0.0162 0.0072  34  VAL   B C   
4398 O O   . VAL   B 34  ? 0.1619 0.1186 0.1349 -0.0254 -0.0333 0.0052  34  VAL   B O   
4399 C CB  . VAL   B 34  ? 0.1637 0.1345 0.1737 -0.0086 -0.0274 -0.0022 34  VAL   B CB  
4400 C CG1 . VAL   B 34  ? 0.1646 0.1459 0.1775 -0.0107 -0.0146 -0.0046 34  VAL   B CG1 
4401 C CG2 . VAL   B 34  ? 0.1731 0.1390 0.1964 -0.0043 -0.0224 -0.0022 34  VAL   B CG2 
4411 N N   . VAL   B 35  ? 0.1353 0.1150 0.1233 -0.0226 -0.0107 0.0072  35  VAL   B N   
4412 C CA  . VAL   B 35  ? 0.1342 0.1142 0.1268 -0.0168 -0.0064 0.0080  35  VAL   B CA  
4413 C C   . VAL   B 35  ? 0.1213 0.1086 0.1352 -0.0144 -0.0164 0.0064  35  VAL   B C   
4414 O O   . VAL   B 35  ? 0.1291 0.1127 0.1373 -0.0225 -0.0044 -0.0023 35  VAL   B O   
4415 C CB  . VAL   B 35  ? 0.1360 0.1308 0.1279 -0.0141 0.0016  0.0063  35  VAL   B CB  
4416 C CG1 . VAL   B 35  ? 0.1308 0.1418 0.1523 -0.0172 -0.0034 0.0041  35  VAL   B CG1 
4417 C CG2 . VAL   B 35  ? 0.1319 0.1322 0.1564 -0.0053 -0.0004 -0.0017 35  VAL   B CG2 
4427 N N   . VAL   B 36  ? 0.1289 0.1088 0.1265 -0.0129 -0.0156 0.0093  36  VAL   B N   
4428 C CA  . VAL   B 36  ? 0.1199 0.1085 0.1256 -0.0113 -0.0120 0.0052  36  VAL   B CA  
4429 C C   . VAL   B 36  ? 0.1150 0.1103 0.1228 -0.0131 -0.0079 0.0021  36  VAL   B C   
4430 O O   . VAL   B 36  ? 0.1256 0.1188 0.1420 -0.0077 -0.0051 -0.0066 36  VAL   B O   
4431 C CB  . VAL   B 36  ? 0.1237 0.1133 0.1326 -0.0128 -0.0052 0.0034  36  VAL   B CB  
4432 C CG1 . VAL   B 36  ? 0.1223 0.1288 0.1455 -0.0191 -0.0095 0.0023  36  VAL   B CG1 
4433 C CG2 . VAL   B 36  ? 0.1288 0.1150 0.1304 -0.0124 -0.0110 0.0079  36  VAL   B CG2 
4443 N N   . ASN   B 37  ? 0.1192 0.1168 0.1224 -0.0032 -0.0108 0.0043  37  ASN   B N   
4444 C CA  . ASN   B 37  ? 0.1196 0.1175 0.1358 0.0020  -0.0160 0.0045  37  ASN   B CA  
4445 C C   . ASN   B 37  ? 0.1194 0.1181 0.1318 0.0014  -0.0071 0.0035  37  ASN   B C   
4446 O O   . ASN   B 37  ? 0.1293 0.1260 0.1305 0.0037  -0.0008 0.0093  37  ASN   B O   
4447 C CB  . ASN   B 37  ? 0.1251 0.1236 0.1231 0.0010  -0.0173 0.0043  37  ASN   B CB  
4448 C CG  . ASN   B 37  ? 0.1307 0.1232 0.1386 -0.0017 -0.0153 -0.0009 37  ASN   B CG  
4449 O OD1 . ASN   B 37  ? 0.1358 0.1287 0.1505 0.0081  -0.0162 0.0012  37  ASN   B OD1 
4450 N ND2 . ASN   B 37  ? 0.1381 0.1198 0.1381 0.0009  -0.0229 0.0073  37  ASN   B ND2 
4457 N N   . ALA   B 38  ? 0.1288 0.1188 0.1292 0.0055  0.0023  0.0048  38  ALA   B N   
4458 C CA  . ALA   B 38  ? 0.1390 0.1203 0.1359 -0.0013 0.0015  0.0057  38  ALA   B CA  
4459 C C   . ALA   B 38  ? 0.1348 0.1164 0.1351 0.0009  -0.0037 0.0023  38  ALA   B C   
4460 O O   . ALA   B 38  ? 0.1468 0.1277 0.1442 0.0073  -0.0063 0.0027  38  ALA   B O   
4461 C CB  . ALA   B 38  ? 0.1632 0.1298 0.1463 -0.0144 0.0085  0.0056  38  ALA   B CB  
4467 N N   . ALA   B 39  ? 0.1324 0.1192 0.1378 0.0035  -0.0098 0.0016  39  ALA   B N   
4468 C CA  . ALA   B 39  ? 0.1436 0.1262 0.1329 0.0015  -0.0086 0.0057  39  ALA   B CA  
4469 C C   . ALA   B 39  ? 0.1439 0.1309 0.1222 0.0046  -0.0074 0.0016  39  ALA   B C   
4470 O O   . ALA   B 39  ? 0.1478 0.1370 0.1450 0.0029  -0.0037 0.0076  39  ALA   B O   
4471 C CB  . ALA   B 39  ? 0.1492 0.1300 0.1541 -0.0028 -0.0006 -0.0011 39  ALA   B CB  
4477 N N   . ASN   B 40  ? 0.1476 0.1535 0.1261 -0.0050 0.0021  -0.0076 40  ASN   B N   
4478 C CA  . ASN   B 40  ? 0.1528 0.1593 0.1332 -0.0024 -0.0057 -0.0081 40  ASN   B CA  
4479 C C   . ASN   B 40  ? 0.1585 0.1582 0.1172 0.0058  -0.0108 -0.0037 40  ASN   B C   
4480 O O   . ASN   B 40  ? 0.1554 0.1480 0.1356 0.0088  -0.0196 -0.0052 40  ASN   B O   
4481 C CB  . ASN   B 40  ? 0.1709 0.1613 0.1437 0.0043  -0.0153 0.0053  40  ASN   B CB  
4482 C CG  . ASN   B 40  ? 0.1731 0.1629 0.1775 0.0016  -0.0295 0.0200  40  ASN   B CG  
4483 O OD1 . ASN   B 40  ? 0.1720 0.1601 0.2536 0.0037  -0.0357 0.0193  40  ASN   B OD1 
4484 N ND2 . ASN   B 40  ? 0.1740 0.1632 0.1821 0.0002  -0.0226 0.0178  40  ASN   B ND2 
4491 N N   . VAL   B 41  ? 0.1685 0.1634 0.1247 0.0111  -0.0025 -0.0030 41  VAL   B N   
4492 C CA  . VAL   B 41  ? 0.1760 0.1727 0.1301 0.0091  -0.0067 -0.0152 41  VAL   B CA  
4493 C C   . VAL   B 41  ? 0.1774 0.1725 0.1283 0.0156  -0.0139 -0.0153 41  VAL   B C   
4494 O O   . VAL   B 41  ? 0.1775 0.1706 0.1406 0.0133  -0.0142 -0.0183 41  VAL   B O   
4495 C CB  . VAL   B 41  ? 0.1887 0.1887 0.1518 0.0004  0.0123  -0.0258 41  VAL   B CB  
4496 C CG1 . VAL   B 41  ? 0.1850 0.1934 0.1695 -0.0033 0.0210  -0.0259 41  VAL   B CG1 
4497 C CG2 . VAL   B 41  ? 0.2014 0.2085 0.1544 -0.0052 0.0108  -0.0260 41  VAL   B CG2 
4507 N N   . TYR   B 42  ? 0.1796 0.1728 0.1339 0.0127  -0.0266 -0.0038 42  TYR   B N   
4508 C CA  . TYR   B 42  ? 0.1826 0.1804 0.1504 0.0126  -0.0296 -0.0132 42  TYR   B CA  
4509 C C   . TYR   B 42  ? 0.1653 0.1543 0.1595 0.0185  -0.0291 -0.0215 42  TYR   B C   
4510 O O   . TYR   B 42  ? 0.1669 0.1620 0.1886 0.0102  -0.0335 -0.0235 42  TYR   B O   
4511 C CB  . TYR   B 42  ? 0.2091 0.2141 0.1649 0.0090  -0.0369 0.0058  42  TYR   B CB  
4512 C CG  . TYR   B 42  ? 0.2092 0.2375 0.1540 -0.0011 -0.0312 0.0175  42  TYR   B CG  
4513 C CD1 . TYR   B 42  ? 0.2005 0.2368 0.1275 -0.0083 -0.0240 -0.0008 42  TYR   B CD1 
4514 C CD2 . TYR   B 42  ? 0.2219 0.2526 0.1968 0.0051  -0.0142 0.0210  42  TYR   B CD2 
4515 C CE1 . TYR   B 42  ? 0.2141 0.2509 0.1375 -0.0018 -0.0224 0.0043  42  TYR   B CE1 
4516 C CE2 . TYR   B 42  ? 0.2271 0.2628 0.1888 0.0079  0.0035  0.0347  42  TYR   B CE2 
4517 C CZ  . TYR   B 42  ? 0.2332 0.2719 0.1759 0.0168  0.0093  0.0188  42  TYR   B CZ  
4518 O OH  . TYR   B 42  ? 0.2661 0.2945 0.2231 0.0302  0.0252  0.0305  42  TYR   B OH  
4528 N N   . LEU   B 43  ? 0.1579 0.1387 0.1468 0.0093  -0.0221 -0.0200 43  LEU   B N   
4529 C CA  . LEU   B 43  ? 0.1543 0.1433 0.1370 0.0042  -0.0175 -0.0078 43  LEU   B CA  
4530 C C   . LEU   B 43  ? 0.1596 0.1481 0.1369 0.0037  -0.0196 -0.0045 43  LEU   B C   
4531 O O   . LEU   B 43  ? 0.1539 0.1556 0.1645 0.0035  -0.0271 0.0095  43  LEU   B O   
4532 C CB  . LEU   B 43  ? 0.1532 0.1394 0.1424 0.0021  -0.0252 -0.0120 43  LEU   B CB  
4533 C CG  . LEU   B 43  ? 0.1614 0.1356 0.1484 0.0016  -0.0314 -0.0075 43  LEU   B CG  
4534 C CD1 . LEU   B 43  ? 0.1651 0.1362 0.1903 -0.0010 -0.0385 -0.0064 43  LEU   B CD1 
4535 C CD2 . LEU   B 43  ? 0.1609 0.1353 0.1634 -0.0011 -0.0332 -0.0050 43  LEU   B CD2 
4547 N N   . LYS   B 44  ? 0.1564 0.1452 0.1368 0.0093  -0.0131 -0.0089 44  LYS   B N   
4548 C CA  . LYS   B 44  ? 0.1710 0.1528 0.1438 0.0097  -0.0215 0.0058  44  LYS   B CA  
4549 C C   . LYS   B 44  ? 0.1552 0.1473 0.1477 0.0078  -0.0207 -0.0002 44  LYS   B C   
4550 O O   . LYS   B 44  ? 0.1747 0.1455 0.1761 0.0016  -0.0112 0.0040  44  LYS   B O   
4551 C CB  . LYS   B 44  ? 0.1993 0.1715 0.1595 0.0200  -0.0307 0.0032  44  LYS   B CB  
4552 C CG  . LYS   B 44  ? 0.2424 0.2023 0.1978 0.0105  -0.0546 -0.0022 44  LYS   B CG  
4553 C CD  . LYS   B 44  ? 0.2783 0.2284 0.2531 -0.0052 -0.0670 0.0001  44  LYS   B CD  
4554 C CE  . LYS   B 44  ? 0.3110 0.2556 0.3002 -0.0122 -0.0669 0.0109  44  LYS   B CE  
4555 N NZ  . LYS   B 44  ? 0.3244 0.2667 0.3256 -0.0122 -0.0688 0.0237  44  LYS   B NZ  
4569 N N   . HIS   B 45  ? 0.1541 0.1455 0.1437 0.0046  -0.0189 0.0080  45  HIS   B N   
4570 C CA  . HIS   B 45  ? 0.1571 0.1407 0.1536 0.0071  -0.0112 -0.0032 45  HIS   B CA  
4571 C C   . HIS   B 45  ? 0.1849 0.1623 0.1918 0.0158  -0.0191 -0.0049 45  HIS   B C   
4572 O O   . HIS   B 45  ? 0.1918 0.1933 0.2340 0.0414  0.0018  0.0003  45  HIS   B O   
4573 C CB  . HIS   B 45  ? 0.1475 0.1466 0.1476 -0.0003 -0.0108 -0.0053 45  HIS   B CB  
4574 C CG  . HIS   B 45  ? 0.1510 0.1424 0.1411 -0.0037 -0.0151 0.0007  45  HIS   B CG  
4575 N ND1 . HIS   B 45  ? 0.1597 0.1419 0.1525 -0.0003 -0.0212 -0.0089 45  HIS   B ND1 
4576 C CD2 . HIS   B 45  ? 0.1549 0.1474 0.1601 -0.0093 -0.0176 0.0006  45  HIS   B CD2 
4577 C CE1 . HIS   B 45  ? 0.1667 0.1319 0.1502 0.0028  -0.0295 -0.0046 45  HIS   B CE1 
4578 N NE2 . HIS   B 45  ? 0.1645 0.1398 0.1554 -0.0031 -0.0240 -0.0067 45  HIS   B NE2 
4586 N N   A GLY   B 46  ? 0.1969 0.1548 0.2163 0.0183  -0.0369 0.0039  46  GLY   B N   
4587 N N   B GLY   B 46  ? 0.1917 0.1679 0.2066 0.0164  -0.0287 0.0025  46  GLY   B N   
4588 C CA  A GLY   B 46  ? 0.2055 0.1651 0.2586 0.0193  -0.0471 0.0078  46  GLY   B CA  
4589 C CA  B GLY   B 46  ? 0.1969 0.1779 0.2287 0.0163  -0.0356 0.0092  46  GLY   B CA  
4590 C C   A GLY   B 46  ? 0.1970 0.1818 0.2995 0.0275  -0.0413 0.0039  46  GLY   B C   
4591 C C   B GLY   B 46  ? 0.1963 0.1889 0.2517 0.0182  -0.0348 0.0134  46  GLY   B C   
4592 O O   A GLY   B 46  ? 0.2041 0.2024 0.3891 0.0324  -0.0138 -0.0216 46  GLY   B O   
4593 O O   B GLY   B 46  ? 0.2007 0.1976 0.2643 0.0221  -0.0319 0.0242  46  GLY   B O   
4600 N N   . GLY   B 47  ? 0.1930 0.1947 0.2634 0.0116  -0.0270 0.0053  47  GLY   B N   
4601 C CA  . GLY   B 47  ? 0.1839 0.1691 0.2265 0.0046  -0.0198 0.0065  47  GLY   B CA  
4602 C C   . GLY   B 47  ? 0.1618 0.1453 0.1985 0.0054  -0.0022 0.0165  47  GLY   B C   
4603 O O   . GLY   B 47  ? 0.1706 0.1350 0.2005 0.0076  -0.0117 0.0144  47  GLY   B O   
4608 N N   . GLY   B 48  ? 0.1434 0.1377 0.1952 0.0063  -0.0117 0.0199  48  GLY   B N   
4609 C CA  . GLY   B 48  ? 0.1461 0.1346 0.2012 -0.0000 -0.0067 0.0081  48  GLY   B CA  
4610 C C   . GLY   B 48  ? 0.1400 0.1274 0.1840 0.0003  0.0035  0.0043  48  GLY   B C   
4611 O O   . GLY   B 48  ? 0.1428 0.1325 0.2011 0.0063  -0.0111 0.0078  48  GLY   B O   
4615 N N   . VAL   B 49  ? 0.1456 0.1392 0.1662 0.0158  -0.0037 0.0032  49  VAL   B N   
4616 C CA  . VAL   B 49  ? 0.1457 0.1465 0.1560 0.0117  -0.0135 -0.0035 49  VAL   B CA  
4617 C C   . VAL   B 49  ? 0.1326 0.1386 0.1356 0.0144  -0.0049 0.0038  49  VAL   B C   
4618 O O   . VAL   B 49  ? 0.1411 0.1445 0.1486 0.0074  -0.0050 0.0030  49  VAL   B O   
4619 C CB  . VAL   B 49  ? 0.1469 0.1623 0.1869 0.0058  -0.0268 -0.0013 49  VAL   B CB  
4620 C CG1 . VAL   B 49  ? 0.1447 0.1740 0.1803 0.0084  -0.0295 0.0061  49  VAL   B CG1 
4621 C CG2 . VAL   B 49  ? 0.1670 0.1727 0.2144 -0.0086 -0.0374 -0.0003 49  VAL   B CG2 
4631 N N   . ALA   B 50  ? 0.1298 0.1362 0.1509 0.0044  -0.0053 0.0084  50  ALA   B N   
4632 C CA  . ALA   B 50  ? 0.1296 0.1254 0.1466 0.0052  -0.0110 0.0081  50  ALA   B CA  
4633 C C   . ALA   B 50  ? 0.1421 0.1258 0.1470 0.0075  -0.0061 0.0080  50  ALA   B C   
4634 O O   . ALA   B 50  ? 0.1372 0.1302 0.1474 0.0073  -0.0042 -0.0017 50  ALA   B O   
4635 C CB  . ALA   B 50  ? 0.1329 0.1323 0.1567 0.0004  -0.0074 0.0101  50  ALA   B CB  
4641 N N   . GLY   B 51  ? 0.1390 0.1408 0.1588 0.0101  -0.0119 0.0099  51  GLY   B N   
4642 C CA  . GLY   B 51  ? 0.1318 0.1450 0.1799 0.0146  -0.0176 0.0094  51  GLY   B CA  
4643 C C   . GLY   B 51  ? 0.1358 0.1431 0.1791 0.0183  -0.0075 0.0083  51  GLY   B C   
4644 O O   . GLY   B 51  ? 0.1378 0.1570 0.1992 0.0078  -0.0147 0.0016  51  GLY   B O   
4648 N N   . ALA   B 52  ? 0.1413 0.1338 0.1772 0.0154  -0.0034 0.0161  52  ALA   B N   
4649 C CA  . ALA   B 52  ? 0.1428 0.1442 0.1711 0.0186  0.0035  0.0045  52  ALA   B CA  
4650 C C   . ALA   B 52  ? 0.1362 0.1472 0.1573 0.0105  -0.0020 0.0023  52  ALA   B C   
4651 O O   . ALA   B 52  ? 0.1381 0.1509 0.1774 0.0148  0.0011  0.0029  52  ALA   B O   
4652 C CB  . ALA   B 52  ? 0.1639 0.1487 0.1772 0.0114  0.0043  0.0018  52  ALA   B CB  
4658 N N   . LEU   B 53  ? 0.1319 0.1398 0.1478 0.0151  -0.0024 0.0046  53  LEU   B N   
4659 C CA  . LEU   B 53  ? 0.1287 0.1435 0.1582 0.0133  -0.0068 0.0096  53  LEU   B CA  
4660 C C   . LEU   B 53  ? 0.1343 0.1370 0.1571 0.0099  -0.0031 0.0106  53  LEU   B C   
4661 O O   . LEU   B 53  ? 0.1392 0.1474 0.1684 0.0002  -0.0033 0.0153  53  LEU   B O   
4662 C CB  . LEU   B 53  ? 0.1339 0.1515 0.1623 0.0117  -0.0060 0.0128  53  LEU   B CB  
4663 C CG  . LEU   B 53  ? 0.1284 0.1640 0.1665 0.0038  -0.0022 0.0229  53  LEU   B CG  
4664 C CD1 . LEU   B 53  ? 0.1328 0.1902 0.2039 0.0153  -0.0074 0.0072  53  LEU   B CD1 
4665 C CD2 . LEU   B 53  ? 0.1468 0.1906 0.1949 -0.0067 -0.0100 -0.0102 53  LEU   B CD2 
4677 N N   . ASN   B 54  ? 0.1354 0.1349 0.1527 0.0022  -0.0071 0.0090  54  ASN   B N   
4678 C CA  . ASN   B 54  ? 0.1417 0.1434 0.1640 0.0035  -0.0050 0.0056  54  ASN   B CA  
4679 C C   . ASN   B 54  ? 0.1398 0.1439 0.1797 0.0038  -0.0055 0.0112  54  ASN   B C   
4680 O O   . ASN   B 54  ? 0.1376 0.1496 0.1830 -0.0001 -0.0007 0.0078  54  ASN   B O   
4681 C CB  . ASN   B 54  ? 0.1476 0.1562 0.1691 0.0053  0.0004  0.0086  54  ASN   B CB  
4682 C CG  . ASN   B 54  ? 0.1406 0.1618 0.1655 0.0008  -0.0088 0.0063  54  ASN   B CG  
4683 O OD1 . ASN   B 54  ? 0.1374 0.1651 0.1784 -0.0016 -0.0167 -0.0090 54  ASN   B OD1 
4684 N ND2 . ASN   B 54  ? 0.1510 0.1819 0.1908 -0.0033 -0.0343 0.0154  54  ASN   B ND2 
4691 N N   . LYS   B 55  ? 0.1357 0.1540 0.1935 0.0116  -0.0068 0.0092  55  LYS   B N   
4692 C CA  . LYS   B 55  ? 0.1388 0.1668 0.2112 0.0197  -0.0070 0.0134  55  LYS   B CA  
4693 C C   . LYS   B 55  ? 0.1359 0.1684 0.2054 0.0148  0.0027  0.0058  55  LYS   B C   
4694 O O   . LYS   B 55  ? 0.1297 0.1814 0.2160 0.0116  0.0059  -0.0008 55  LYS   B O   
4695 C CB  . LYS   B 55  ? 0.1497 0.1841 0.2415 0.0267  0.0040  0.0235  55  LYS   B CB  
4696 C CG  . LYS   B 55  ? 0.1894 0.2089 0.3229 0.0334  0.0139  0.0300  55  LYS   B CG  
4697 C CD  . LYS   B 55  ? 0.2295 0.2303 0.3960 0.0422  0.0318  0.0403  55  LYS   B CD  
4698 C CE  . LYS   B 55  ? 0.2609 0.2534 0.4618 0.0458  0.0452  0.0389  55  LYS   B CE  
4699 N NZ  . LYS   B 55  ? 0.2724 0.2670 0.4942 0.0492  0.0329  0.0455  55  LYS   B NZ  
4713 N N   . ALA   B 56  ? 0.1338 0.1703 0.1839 0.0122  0.0020  0.0026  56  ALA   B N   
4714 C CA  . ALA   B 56  ? 0.1473 0.1831 0.1875 0.0066  0.0018  -0.0025 56  ALA   B CA  
4715 C C   . ALA   B 56  ? 0.1477 0.1783 0.1796 0.0044  0.0076  0.0096  56  ALA   B C   
4716 O O   . ALA   B 56  ? 0.1606 0.1891 0.1952 0.0076  0.0188  0.0159  56  ALA   B O   
4717 C CB  . ALA   B 56  ? 0.1602 0.2037 0.1923 -0.0043 0.0027  -0.0112 56  ALA   B CB  
4723 N N   . THR   B 57  ? 0.1419 0.1673 0.1865 0.0015  0.0114  0.0162  57  THR   B N   
4724 C CA  . THR   B 57  ? 0.1472 0.1684 0.1789 -0.0014 0.0166  0.0217  57  THR   B CA  
4725 C C   . THR   B 57  ? 0.1413 0.1775 0.1994 0.0005  0.0162  0.0158  57  THR   B C   
4726 O O   . THR   B 57  ? 0.1516 0.1802 0.2091 -0.0133 0.0126  0.0102  57  THR   B O   
4727 C CB  . THR   B 57  ? 0.1515 0.1545 0.1725 -0.0000 0.0090  0.0206  57  THR   B CB  
4728 O OG1 . THR   B 57  ? 0.1505 0.1494 0.1842 -0.0026 0.0126  0.0090  57  THR   B OG1 
4729 C CG2 . THR   B 57  ? 0.1454 0.1553 0.1729 0.0002  0.0076  0.0138  57  THR   B CG2 
4737 N N   . ASN   B 58  ? 0.1278 0.1960 0.2201 -0.0102 0.0009  0.0071  58  ASN   B N   
4738 C CA  . ASN   B 58  ? 0.1518 0.2359 0.2723 -0.0230 0.0218  0.0162  58  ASN   B CA  
4739 C C   . ASN   B 58  ? 0.1357 0.2148 0.2330 -0.0138 -0.0066 0.0109  58  ASN   B C   
4740 O O   . ASN   B 58  ? 0.1438 0.2264 0.2412 -0.0175 -0.0057 -0.0007 58  ASN   B O   
4741 C CB  . ASN   B 58  ? 0.2410 0.3093 0.4096 -0.0333 0.0596  0.0295  58  ASN   B CB  
4742 C CG  . ASN   B 58  ? 0.3466 0.3833 0.5560 -0.0355 0.0807  0.0516  58  ASN   B CG  
4743 O OD1 . ASN   B 58  ? 0.3672 0.4070 0.6096 -0.0362 0.0845  0.0578  58  ASN   B OD1 
4744 N ND2 . ASN   B 58  ? 0.4396 0.4396 0.6067 -0.0373 0.0886  0.0582  58  ASN   B ND2 
4751 N N   . ASN   B 59  ? 0.1350 0.1949 0.2118 -0.0109 -0.0098 0.0189  59  ASN   B N   
4752 C CA  . ASN   B 59  ? 0.1350 0.1956 0.2084 -0.0115 -0.0167 0.0228  59  ASN   B CA  
4753 C C   . ASN   B 59  ? 0.1329 0.1867 0.1947 -0.0144 -0.0143 0.0076  59  ASN   B C   
4754 O O   . ASN   B 59  ? 0.1388 0.1932 0.1927 -0.0120 -0.0144 0.0022  59  ASN   B O   
4755 C CB  . ASN   B 59  ? 0.1470 0.2110 0.2244 -0.0078 -0.0285 0.0256  59  ASN   B CB  
4756 C CG  . ASN   B 59  ? 0.1643 0.2260 0.2369 -0.0026 -0.0396 0.0243  59  ASN   B CG  
4757 O OD1 . ASN   B 59  ? 0.1734 0.2297 0.2322 -0.0003 -0.0295 0.0366  59  ASN   B OD1 
4758 N ND2 . ASN   B 59  ? 0.1669 0.2341 0.2518 -0.0081 -0.0386 0.0138  59  ASN   B ND2 
4765 N N   . ALA   B 60  ? 0.1350 0.1742 0.1995 -0.0133 -0.0084 0.0059  60  ALA   B N   
4766 C CA  . ALA   B 60  ? 0.1453 0.1628 0.2008 -0.0169 -0.0055 0.0081  60  ALA   B CA  
4767 C C   . ALA   B 60  ? 0.1443 0.1526 0.1765 -0.0109 -0.0098 0.0087  60  ALA   B C   
4768 O O   . ALA   B 60  ? 0.1491 0.1564 0.1910 -0.0144 -0.0054 -0.0008 60  ALA   B O   
4769 C CB  . ALA   B 60  ? 0.1602 0.1615 0.2274 -0.0186 0.0010  0.0154  60  ALA   B CB  
4775 N N   . MET   B 61  ? 0.1352 0.1444 0.1750 -0.0037 -0.0060 0.0056  61  MET   B N   
4776 C CA  . MET   B 61  ? 0.1331 0.1436 0.1777 -0.0030 -0.0092 0.0042  61  MET   B CA  
4777 C C   . MET   B 61  ? 0.1419 0.1349 0.1775 -0.0068 -0.0151 0.0064  61  MET   B C   
4778 O O   . MET   B 61  ? 0.1446 0.1372 0.1643 -0.0005 -0.0138 -0.0079 61  MET   B O   
4779 C CB  . MET   B 61  ? 0.1328 0.1460 0.1707 -0.0003 -0.0109 0.0023  61  MET   B CB  
4780 C CG  . MET   B 61  ? 0.1359 0.1474 0.1538 -0.0011 -0.0043 -0.0018 61  MET   B CG  
4781 S SD  . MET   B 61  ? 0.1378 0.1500 0.1807 -0.0048 -0.0102 -0.0097 61  MET   B SD  
4782 C CE  . MET   B 61  ? 0.1447 0.1720 0.1983 -0.0022 -0.0076 -0.0268 61  MET   B CE  
4792 N N   . GLN   B 62  ? 0.1420 0.1388 0.1617 -0.0046 -0.0189 0.0032  62  GLN   B N   
4793 C CA  . GLN   B 62  ? 0.1431 0.1467 0.1646 -0.0018 -0.0218 0.0015  62  GLN   B CA  
4794 C C   . GLN   B 62  ? 0.1434 0.1532 0.1760 -0.0068 -0.0256 0.0028  62  GLN   B C   
4795 O O   . GLN   B 62  ? 0.1606 0.1509 0.1735 -0.0074 -0.0368 -0.0113 62  GLN   B O   
4796 C CB  . GLN   B 62  ? 0.1469 0.1547 0.1722 -0.0032 -0.0238 0.0047  62  GLN   B CB  
4797 C CG  . GLN   B 62  ? 0.1475 0.1631 0.1703 -0.0022 -0.0284 -0.0001 62  GLN   B CG  
4798 C CD  . GLN   B 62  ? 0.1465 0.1592 0.1622 -0.0010 -0.0326 0.0059  62  GLN   B CD  
4799 O OE1 . GLN   B 62  ? 0.1502 0.1519 0.1805 -0.0040 -0.0288 -0.0020 62  GLN   B OE1 
4800 N NE2 . GLN   B 62  ? 0.1511 0.1612 0.1756 -0.0016 -0.0273 -0.0070 62  GLN   B NE2 
4809 N N   . VAL   B 63  ? 0.1479 0.1598 0.1871 -0.0111 -0.0267 -0.0058 63  VAL   B N   
4810 C CA  . VAL   B 63  ? 0.1571 0.1600 0.1990 -0.0184 -0.0354 -0.0056 63  VAL   B CA  
4811 C C   . VAL   B 63  ? 0.1591 0.1507 0.1921 -0.0199 -0.0403 -0.0145 63  VAL   B C   
4812 O O   . VAL   B 63  ? 0.1712 0.1504 0.2030 -0.0159 -0.0504 -0.0101 63  VAL   B O   
4813 C CB  . VAL   B 63  ? 0.1617 0.1761 0.2338 -0.0232 -0.0292 -0.0027 63  VAL   B CB  
4814 C CG1 . VAL   B 63  ? 0.1745 0.1797 0.2442 -0.0337 -0.0212 -0.0030 63  VAL   B CG1 
4815 C CG2 . VAL   B 63  ? 0.1571 0.1940 0.2493 -0.0181 -0.0338 -0.0020 63  VAL   B CG2 
4825 N N   . GLU   B 64  ? 0.1596 0.1440 0.1844 -0.0138 -0.0302 -0.0111 64  GLU   B N   
4826 C CA  . GLU   B 64  ? 0.1587 0.1383 0.1716 -0.0113 -0.0334 -0.0046 64  GLU   B CA  
4827 C C   . GLU   B 64  ? 0.1514 0.1356 0.1670 -0.0067 -0.0316 -0.0126 64  GLU   B C   
4828 O O   . GLU   B 64  ? 0.1639 0.1478 0.1694 -0.0093 -0.0289 -0.0105 64  GLU   B O   
4829 C CB  . GLU   B 64  ? 0.1560 0.1465 0.1773 -0.0144 -0.0244 -0.0020 64  GLU   B CB  
4830 C CG  . GLU   B 64  ? 0.1637 0.1496 0.1771 -0.0210 -0.0289 -0.0091 64  GLU   B CG  
4831 C CD  . GLU   B 64  ? 0.1708 0.1633 0.1919 -0.0274 -0.0345 -0.0052 64  GLU   B CD  
4832 O OE1 . GLU   B 64  ? 0.1752 0.1781 0.2006 -0.0323 -0.0259 -0.0185 64  GLU   B OE1 
4833 O OE2 . GLU   B 64  ? 0.1860 0.1763 0.2009 -0.0348 -0.0508 -0.0043 64  GLU   B OE2 
4840 N N   . SER   B 65  ? 0.1502 0.1302 0.1716 -0.0098 -0.0202 -0.0137 65  SER   B N   
4841 C CA  . SER   B 65  ? 0.1526 0.1313 0.1716 -0.0026 -0.0229 -0.0146 65  SER   B CA  
4842 C C   . SER   B 65  ? 0.1554 0.1355 0.1701 0.0009  -0.0248 -0.0205 65  SER   B C   
4843 O O   . SER   B 65  ? 0.1549 0.1430 0.1724 -0.0040 -0.0246 -0.0257 65  SER   B O   
4844 C CB  . SER   B 65  ? 0.1511 0.1365 0.1636 -0.0102 -0.0168 -0.0121 65  SER   B CB  
4845 O OG  . SER   B 65  ? 0.1561 0.1416 0.1739 -0.0089 -0.0234 -0.0241 65  SER   B OG  
4851 N N   . ASP   B 66  ? 0.1659 0.1411 0.1668 -0.0029 -0.0288 -0.0187 66  ASP   B N   
4852 C CA  . ASP   B 66  ? 0.1726 0.1473 0.1632 -0.0009 -0.0382 -0.0110 66  ASP   B CA  
4853 C C   . ASP   B 66  ? 0.1753 0.1512 0.1605 -0.0044 -0.0316 -0.0155 66  ASP   B C   
4854 O O   . ASP   B 66  ? 0.1811 0.1551 0.1709 0.0039  -0.0309 -0.0205 66  ASP   B O   
4855 C CB  . ASP   B 66  ? 0.1919 0.1650 0.1870 0.0103  -0.0492 -0.0179 66  ASP   B CB  
4856 C CG  . ASP   B 66  ? 0.2244 0.1817 0.2140 0.0214  -0.0584 0.0003  66  ASP   B CG  
4857 O OD1 . ASP   B 66  ? 0.2484 0.1797 0.2191 0.0106  -0.0540 0.0082  66  ASP   B OD1 
4858 O OD2 . ASP   B 66  ? 0.2412 0.2026 0.2683 0.0364  -0.0570 -0.0042 66  ASP   B OD2 
4863 N N   . ASP   B 67  ? 0.1715 0.1465 0.1619 -0.0085 -0.0300 -0.0169 67  ASP   B N   
4864 C CA  . ASP   B 67  ? 0.1858 0.1421 0.1712 -0.0080 -0.0332 -0.0089 67  ASP   B CA  
4865 C C   . ASP   B 67  ? 0.1833 0.1428 0.1846 -0.0022 -0.0307 -0.0154 67  ASP   B C   
4866 O O   . ASP   B 67  ? 0.1871 0.1511 0.1931 -0.0042 -0.0267 -0.0217 67  ASP   B O   
4867 C CB  . ASP   B 67  ? 0.2066 0.1537 0.1920 -0.0158 -0.0423 -0.0101 67  ASP   B CB  
4868 C CG  . ASP   B 67  ? 0.2402 0.1618 0.2008 -0.0144 -0.0611 -0.0096 67  ASP   B CG  
4869 O OD1 . ASP   B 67  ? 0.2605 0.1685 0.2160 -0.0149 -0.0614 -0.0023 67  ASP   B OD1 
4870 O OD2 . ASP   B 67  ? 0.2587 0.1702 0.2140 -0.0029 -0.0665 -0.0096 67  ASP   B OD2 
4875 N N   . TYR   B 68  ? 0.1732 0.1448 0.1792 -0.0022 -0.0400 -0.0213 68  TYR   B N   
4876 C CA  . TYR   B 68  ? 0.1742 0.1599 0.1912 0.0042  -0.0505 -0.0327 68  TYR   B CA  
4877 C C   . TYR   B 68  ? 0.1646 0.1611 0.1800 0.0018  -0.0414 -0.0320 68  TYR   B C   
4878 O O   . TYR   B 68  ? 0.1689 0.1674 0.1878 0.0090  -0.0316 -0.0449 68  TYR   B O   
4879 C CB  . TYR   B 68  ? 0.1767 0.1806 0.1916 0.0151  -0.0528 -0.0453 68  TYR   B CB  
4880 C CG  . TYR   B 68  ? 0.1896 0.1982 0.2049 0.0161  -0.0483 -0.0656 68  TYR   B CG  
4881 C CD1 . TYR   B 68  ? 0.1932 0.1991 0.2312 -0.0017 -0.0405 -0.0750 68  TYR   B CD1 
4882 C CD2 . TYR   B 68  ? 0.1924 0.2182 0.2291 0.0280  -0.0529 -0.0609 68  TYR   B CD2 
4883 C CE1 . TYR   B 68  ? 0.1957 0.2180 0.2580 0.0031  -0.0423 -0.0693 68  TYR   B CE1 
4884 C CE2 . TYR   B 68  ? 0.1971 0.2231 0.2489 0.0241  -0.0405 -0.0720 68  TYR   B CE2 
4885 C CZ  . TYR   B 68  ? 0.1883 0.2222 0.2647 0.0093  -0.0463 -0.0751 68  TYR   B CZ  
4886 O OH  . TYR   B 68  ? 0.1829 0.2382 0.2952 0.0055  -0.0426 -0.0568 68  TYR   B OH  
4896 N N   . ILE   B 69  ? 0.1640 0.1493 0.1750 0.0036  -0.0392 -0.0314 69  ILE   B N   
4897 C CA  . ILE   B 69  ? 0.1705 0.1545 0.1835 -0.0019 -0.0286 -0.0333 69  ILE   B CA  
4898 C C   . ILE   B 69  ? 0.1701 0.1528 0.1802 0.0032  -0.0331 -0.0232 69  ILE   B C   
4899 O O   . ILE   B 69  ? 0.1756 0.1642 0.1808 0.0026  -0.0234 -0.0327 69  ILE   B O   
4900 C CB  . ILE   B 69  ? 0.1765 0.1599 0.2017 -0.0037 -0.0077 -0.0263 69  ILE   B CB  
4901 C CG1 . ILE   B 69  ? 0.1734 0.1579 0.2161 -0.0041 -0.0003 -0.0335 69  ILE   B CG1 
4902 C CG2 . ILE   B 69  ? 0.1918 0.1723 0.2137 -0.0068 -0.0092 -0.0180 69  ILE   B CG2 
4903 C CD1 . ILE   B 69  ? 0.1687 0.1651 0.2360 -0.0207 0.0049  -0.0305 69  ILE   B CD1 
4915 N N   . ALA   B 70  ? 0.1684 0.1519 0.1815 0.0033  -0.0358 -0.0237 70  ALA   B N   
4916 C CA  . ALA   B 70  ? 0.1762 0.1555 0.1685 -0.0019 -0.0472 -0.0193 70  ALA   B CA  
4917 C C   . ALA   B 70  ? 0.1842 0.1527 0.1797 -0.0011 -0.0541 -0.0335 70  ALA   B C   
4918 O O   . ALA   B 70  ? 0.1967 0.1533 0.1859 0.0005  -0.0426 -0.0367 70  ALA   B O   
4919 C CB  . ALA   B 70  ? 0.1793 0.1722 0.1689 -0.0104 -0.0460 -0.0178 70  ALA   B CB  
4925 N N   . THR   B 71  ? 0.1888 0.1532 0.1898 0.0043  -0.0621 -0.0344 71  THR   B N   
4926 C CA  . THR   B 71  ? 0.2018 0.1641 0.2059 0.0083  -0.0709 -0.0383 71  THR   B CA  
4927 C C   . THR   B 71  ? 0.1933 0.1673 0.2254 0.0272  -0.0657 -0.0543 71  THR   B C   
4928 O O   . THR   B 71  ? 0.2028 0.1760 0.2720 0.0249  -0.0568 -0.0653 71  THR   B O   
4929 C CB  . THR   B 71  ? 0.2287 0.1849 0.2320 -0.0025 -0.0784 -0.0144 71  THR   B CB  
4930 O OG1 . THR   B 71  ? 0.2388 0.2104 0.2663 -0.0192 -0.0797 0.0112  71  THR   B OG1 
4931 C CG2 . THR   B 71  ? 0.2449 0.1870 0.2520 0.0019  -0.0689 -0.0004 71  THR   B CG2 
4939 N N   . ASN   B 72  ? 0.1773 0.1736 0.2169 0.0183  -0.0633 -0.0680 72  ASN   B N   
4940 C CA  . ASN   B 72  ? 0.1807 0.1884 0.2252 0.0163  -0.0546 -0.0713 72  ASN   B CA  
4941 C C   . ASN   B 72  ? 0.1827 0.1989 0.2359 0.0019  -0.0345 -0.0732 72  ASN   B C   
4942 O O   . ASN   B 72  ? 0.1869 0.2161 0.2505 0.0073  -0.0150 -0.0751 72  ASN   B O   
4943 C CB  . ASN   B 72  ? 0.1906 0.2054 0.2370 0.0149  -0.0623 -0.0651 72  ASN   B CB  
4944 C CG  . ASN   B 72  ? 0.2102 0.2199 0.2446 0.0338  -0.0652 -0.0430 72  ASN   B CG  
4945 O OD1 . ASN   B 72  ? 0.2321 0.2376 0.2471 0.0235  -0.0487 -0.0434 72  ASN   B OD1 
4946 N ND2 . ASN   B 72  ? 0.2213 0.2256 0.2832 0.0495  -0.0558 -0.0114 72  ASN   B ND2 
4953 N N   . GLY   B 73  ? 0.1872 0.2021 0.2116 -0.0005 -0.0370 -0.0669 73  GLY   B N   
4954 C CA  . GLY   B 73  ? 0.1815 0.2051 0.1855 0.0023  -0.0290 -0.0536 73  GLY   B CA  
4955 C C   . GLY   B 73  ? 0.1747 0.1982 0.1490 0.0076  -0.0294 -0.0493 73  GLY   B C   
4956 O O   . GLY   B 73  ? 0.1701 0.1855 0.1658 0.0096  -0.0263 -0.0379 73  GLY   B O   
4960 N N   . PRO   B 74  ? 0.1761 0.2075 0.1462 0.0084  -0.0342 -0.0352 74  PRO   B N   
4961 C CA  . PRO   B 74  ? 0.1722 0.2062 0.1369 0.0109  -0.0282 -0.0247 74  PRO   B CA  
4962 C C   . PRO   B 74  ? 0.1612 0.1916 0.1368 0.0099  -0.0193 -0.0215 74  PRO   B C   
4963 O O   . PRO   B 74  ? 0.1615 0.1937 0.1865 0.0098  -0.0125 -0.0418 74  PRO   B O   
4964 C CB  . PRO   B 74  ? 0.1881 0.2238 0.1377 0.0083  -0.0213 -0.0217 74  PRO   B CB  
4965 C CG  . PRO   B 74  ? 0.2021 0.2338 0.1695 0.0067  -0.0178 -0.0180 74  PRO   B CG  
4966 C CD  . PRO   B 74  ? 0.1983 0.2219 0.1735 0.0092  -0.0207 -0.0313 74  PRO   B CD  
4974 N N   . LEU   B 75  ? 0.1568 0.1787 0.1303 0.0084  -0.0216 -0.0212 75  LEU   B N   
4975 C CA  . LEU   B 75  ? 0.1600 0.1780 0.1364 0.0052  -0.0163 -0.0047 75  LEU   B CA  
4976 C C   . LEU   B 75  ? 0.1673 0.1922 0.1301 0.0097  -0.0101 -0.0076 75  LEU   B C   
4977 O O   . LEU   B 75  ? 0.1829 0.2039 0.1444 0.0003  -0.0139 -0.0015 75  LEU   B O   
4978 C CB  . LEU   B 75  ? 0.1657 0.1751 0.1297 -0.0034 -0.0223 0.0087  75  LEU   B CB  
4979 C CG  . LEU   B 75  ? 0.1946 0.1939 0.1477 -0.0278 -0.0122 0.0013  75  LEU   B CG  
4980 C CD1 . LEU   B 75  ? 0.2207 0.2105 0.1531 -0.0445 0.0044  -0.0042 75  LEU   B CD1 
4981 C CD2 . LEU   B 75  ? 0.2258 0.2128 0.2079 -0.0203 0.0024  0.0075  75  LEU   B CD2 
4993 N N   . LYS   B 76  ? 0.1637 0.2111 0.1585 0.0044  -0.0096 -0.0050 76  LYS   B N   
4994 C CA  . LYS   B 76  ? 0.1719 0.2178 0.1858 -0.0082 0.0121  -0.0072 76  LYS   B CA  
4995 C C   . LYS   B 76  ? 0.1607 0.1974 0.1520 0.0008  0.0023  0.0126  76  LYS   B C   
4996 O O   . LYS   B 76  ? 0.1588 0.1860 0.1595 -0.0009 -0.0001 0.0137  76  LYS   B O   
4997 C CB  . LYS   B 76  ? 0.1902 0.2294 0.2556 -0.0089 0.0377  -0.0389 76  LYS   B CB  
4998 C CG  . LYS   B 76  ? 0.2004 0.2466 0.3064 0.0007  0.0262  -0.0516 76  LYS   B CG  
4999 C CD  . LYS   B 76  ? 0.2044 0.2564 0.3524 0.0084  0.0092  -0.0704 76  LYS   B CD  
5000 C CE  . LYS   B 76  ? 0.2096 0.2723 0.4045 0.0139  -0.0009 -0.0820 76  LYS   B CE  
5001 N NZ  . LYS   B 76  ? 0.2123 0.2778 0.4281 0.0144  -0.0198 -0.1025 76  LYS   B NZ  
5015 N N   . VAL   B 77  ? 0.1747 0.2039 0.1464 0.0136  0.0019  0.0153  77  VAL   B N   
5016 C CA  . VAL   B 77  ? 0.1700 0.1945 0.1594 0.0175  0.0141  0.0372  77  VAL   B CA  
5017 C C   . VAL   B 77  ? 0.1572 0.1780 0.1579 0.0186  0.0180  0.0303  77  VAL   B C   
5018 O O   . VAL   B 77  ? 0.1607 0.1808 0.1585 0.0246  0.0228  0.0201  77  VAL   B O   
5019 C CB  . VAL   B 77  ? 0.1813 0.2056 0.1854 0.0186  0.0260  0.0444  77  VAL   B CB  
5020 C CG1 . VAL   B 77  ? 0.1855 0.1962 0.2097 0.0106  0.0272  0.0571  77  VAL   B CG1 
5021 C CG2 . VAL   B 77  ? 0.1964 0.2257 0.2075 0.0180  0.0103  0.0515  77  VAL   B CG2 
5031 N N   . GLY   B 78  ? 0.1569 0.1677 0.1490 0.0139  0.0155  0.0221  78  GLY   B N   
5032 C CA  . GLY   B 78  ? 0.1504 0.1614 0.1425 0.0116  0.0133  0.0070  78  GLY   B CA  
5033 C C   . GLY   B 78  ? 0.1434 0.1538 0.1372 0.0116  0.0090  0.0110  78  GLY   B C   
5034 O O   . GLY   B 78  ? 0.1502 0.1509 0.1546 0.0189  0.0121  0.0123  78  GLY   B O   
5038 N N   . GLY   B 79  ? 0.1427 0.1552 0.1432 0.0104  0.0137  0.0049  79  GLY   B N   
5039 C CA  . GLY   B 79  ? 0.1427 0.1495 0.1506 0.0149  0.0066  0.0052  79  GLY   B CA  
5040 C C   . GLY   B 79  ? 0.1335 0.1415 0.1510 0.0162  0.0072  0.0000  79  GLY   B C   
5041 O O   . GLY   B 79  ? 0.1406 0.1404 0.1551 0.0116  0.0162  0.0138  79  GLY   B O   
5045 N N   . SER   B 80  ? 0.1346 0.1340 0.1542 0.0090  0.0157  -0.0035 80  SER   B N   
5046 C CA  . SER   B 80  ? 0.1330 0.1318 0.1540 0.0069  0.0051  0.0008  80  SER   B CA  
5047 C C   . SER   B 80  ? 0.1373 0.1326 0.1564 0.0094  -0.0074 -0.0024 80  SER   B C   
5048 O O   . SER   B 80  ? 0.1421 0.1331 0.1968 0.0087  0.0035  -0.0084 80  SER   B O   
5049 C CB  . SER   B 80  ? 0.1393 0.1365 0.1579 -0.0036 -0.0019 0.0039  80  SER   B CB  
5050 O OG  . SER   B 80  ? 0.1427 0.1533 0.1922 -0.0025 -0.0179 0.0137  80  SER   B OG  
5056 N N   . CYS   B 81  ? 0.1336 0.1182 0.1594 0.0013  -0.0057 -0.0099 81  CYS   B N   
5057 C CA  . CYS   B 81  ? 0.1396 0.1174 0.1630 0.0016  -0.0169 -0.0078 81  CYS   B CA  
5058 C C   . CYS   B 81  ? 0.1362 0.1140 0.1445 0.0005  -0.0191 -0.0071 81  CYS   B C   
5059 O O   . CYS   B 81  ? 0.1586 0.1216 0.1518 0.0076  -0.0078 -0.0101 81  CYS   B O   
5060 C CB  . CYS   B 81  ? 0.1572 0.1346 0.1639 -0.0050 -0.0119 -0.0049 81  CYS   B CB  
5061 S SG  . CYS   B 81  ? 0.1572 0.1499 0.1568 -0.0043 -0.0285 -0.0128 81  CYS   B SG  
5067 N N   . VAL   B 82  ? 0.1415 0.1161 0.1502 -0.0026 -0.0097 -0.0089 82  VAL   B N   
5068 C CA  . VAL   B 82  ? 0.1400 0.1193 0.1512 -0.0068 -0.0156 0.0007  82  VAL   B CA  
5069 C C   . VAL   B 82  ? 0.1527 0.1121 0.1537 -0.0014 -0.0114 -0.0018 82  VAL   B C   
5070 O O   . VAL   B 82  ? 0.1620 0.1130 0.1888 -0.0009 -0.0135 -0.0162 82  VAL   B O   
5071 C CB  . VAL   B 82  ? 0.1563 0.1415 0.1681 -0.0035 -0.0204 0.0056  82  VAL   B CB  
5072 C CG1 . VAL   B 82  ? 0.1760 0.1669 0.1789 0.0070  -0.0174 0.0179  82  VAL   B CG1 
5073 C CG2 . VAL   B 82  ? 0.1610 0.1570 0.1790 -0.0059 -0.0323 0.0127  82  VAL   B CG2 
5083 N N   . LEU   B 83  ? 0.1398 0.1157 0.1533 -0.0113 -0.0203 -0.0093 83  LEU   B N   
5084 C CA  . LEU   B 83  ? 0.1416 0.1215 0.1484 -0.0127 -0.0251 -0.0006 83  LEU   B CA  
5085 C C   . LEU   B 83  ? 0.1409 0.1223 0.1434 -0.0214 -0.0186 0.0048  83  LEU   B C   
5086 O O   . LEU   B 83  ? 0.1441 0.1269 0.1417 -0.0214 -0.0163 0.0061  83  LEU   B O   
5087 C CB  . LEU   B 83  ? 0.1500 0.1386 0.1562 -0.0169 -0.0301 -0.0089 83  LEU   B CB  
5088 C CG  . LEU   B 83  ? 0.1692 0.1529 0.1599 -0.0172 -0.0137 -0.0107 83  LEU   B CG  
5089 C CD1 . LEU   B 83  ? 0.1802 0.1602 0.1673 -0.0137 -0.0255 -0.0119 83  LEU   B CD1 
5090 C CD2 . LEU   B 83  ? 0.1871 0.1643 0.1718 -0.0092 -0.0123 -0.0262 83  LEU   B CD2 
5102 N N   . SER   B 84  ? 0.1468 0.1344 0.1667 -0.0222 -0.0183 0.0033  84  SER   B N   
5103 C CA  . SER   B 84  ? 0.1462 0.1526 0.1610 -0.0293 -0.0230 0.0195  84  SER   B CA  
5104 C C   . SER   B 84  ? 0.1412 0.1677 0.1306 -0.0208 -0.0218 0.0198  84  SER   B C   
5105 O O   . SER   B 84  ? 0.1471 0.1533 0.1299 -0.0220 -0.0166 0.0030  84  SER   B O   
5106 C CB  . SER   B 84  ? 0.1705 0.1561 0.2108 -0.0269 0.0016  0.0190  84  SER   B CB  
5107 O OG  . SER   B 84  ? 0.1730 0.1671 0.2547 -0.0326 0.0124  0.0263  84  SER   B OG  
5113 N N   . GLY   B 85  ? 0.1445 0.1889 0.1404 -0.0258 -0.0172 0.0219  85  GLY   B N   
5114 C CA  . GLY   B 85  ? 0.1488 0.1973 0.1578 -0.0334 -0.0047 -0.0037 85  GLY   B CA  
5115 C C   . GLY   B 85  ? 0.1464 0.1762 0.1486 -0.0399 -0.0056 0.0102  85  GLY   B C   
5116 O O   . GLY   B 85  ? 0.1532 0.1794 0.1581 -0.0553 0.0131  -0.0088 85  GLY   B O   
5120 N N   . HIS   B 86  ? 0.1435 0.1616 0.1594 -0.0299 -0.0195 0.0211  86  HIS   B N   
5121 C CA  . HIS   B 86  ? 0.1414 0.1607 0.1578 -0.0275 -0.0161 0.0214  86  HIS   B CA  
5122 C C   . HIS   B 86  ? 0.1423 0.1707 0.1523 -0.0394 -0.0127 0.0373  86  HIS   B C   
5123 O O   . HIS   B 86  ? 0.1546 0.1838 0.1614 -0.0313 0.0000  0.0317  86  HIS   B O   
5124 C CB  . HIS   B 86  ? 0.1506 0.1618 0.1662 -0.0177 -0.0221 0.0125  86  HIS   B CB  
5125 C CG  . HIS   B 86  ? 0.1535 0.1672 0.1647 -0.0086 -0.0248 0.0160  86  HIS   B CG  
5126 N ND1 . HIS   B 86  ? 0.1693 0.1892 0.1814 -0.0187 -0.0298 0.0043  86  HIS   B ND1 
5127 C CD2 . HIS   B 86  ? 0.1569 0.1748 0.1686 -0.0059 -0.0231 0.0057  86  HIS   B CD2 
5128 C CE1 . HIS   B 86  ? 0.1743 0.1903 0.1781 -0.0113 -0.0140 -0.0142 86  HIS   B CE1 
5129 N NE2 . HIS   B 86  ? 0.1689 0.1837 0.1634 0.0049  -0.0145 -0.0015 86  HIS   B NE2 
5137 N N   . ASN   B 87  ? 0.1454 0.1750 0.1677 -0.0346 -0.0062 0.0291  87  ASN   B N   
5138 C CA  . ASN   B 87  ? 0.1529 0.1928 0.1681 -0.0302 0.0209  0.0225  87  ASN   B CA  
5139 C C   . ASN   B 87  ? 0.1658 0.1781 0.1574 -0.0221 0.0305  0.0186  87  ASN   B C   
5140 O O   . ASN   B 87  ? 0.1827 0.1898 0.1846 -0.0276 0.0448  0.0125  87  ASN   B O   
5141 C CB  . ASN   B 87  ? 0.1534 0.2270 0.1938 -0.0273 0.0218  0.0130  87  ASN   B CB  
5142 C CG  . ASN   B 87  ? 0.1582 0.2445 0.2088 0.0077  0.0287  0.0338  87  ASN   B CG  
5143 O OD1 . ASN   B 87  ? 0.1549 0.2297 0.1964 0.0136  0.0413  0.0535  87  ASN   B OD1 
5144 N ND2 . ASN   B 87  ? 0.1922 0.2526 0.2426 0.0066  0.0298  0.0302  87  ASN   B ND2 
5151 N N   . LEU   B 88  ? 0.1565 0.1655 0.1475 -0.0247 0.0165  0.0163  88  LEU   B N   
5152 C CA  . LEU   B 88  ? 0.1652 0.1562 0.1518 -0.0309 0.0053  0.0016  88  LEU   B CA  
5153 C C   . LEU   B 88  ? 0.1652 0.1415 0.1497 -0.0352 0.0038  -0.0009 88  LEU   B C   
5154 O O   . LEU   B 88  ? 0.1920 0.1570 0.1776 -0.0168 -0.0284 -0.0071 88  LEU   B O   
5155 C CB  . LEU   B 88  ? 0.1754 0.1668 0.1663 -0.0373 -0.0058 0.0205  88  LEU   B CB  
5156 C CG  . LEU   B 88  ? 0.2104 0.1994 0.1823 -0.0352 -0.0270 0.0351  88  LEU   B CG  
5157 C CD1 . LEU   B 88  ? 0.2208 0.2317 0.1960 -0.0485 -0.0229 0.0482  88  LEU   B CD1 
5158 C CD2 . LEU   B 88  ? 0.2438 0.2256 0.2340 0.0000  -0.0534 0.0181  88  LEU   B CD2 
5170 N N   . ALA   B 89  ? 0.1553 0.1460 0.1390 -0.0325 0.0140  0.0008  89  ALA   B N   
5171 C CA  . ALA   B 89  ? 0.1512 0.1412 0.1248 -0.0325 0.0039  0.0068  89  ALA   B CA  
5172 C C   . ALA   B 89  ? 0.1546 0.1447 0.1309 -0.0388 0.0155  0.0014  89  ALA   B C   
5173 O O   . ALA   B 89  ? 0.1431 0.1552 0.1703 -0.0374 0.0108  -0.0260 89  ALA   B O   
5174 C CB  . ALA   B 89  ? 0.1491 0.1431 0.1447 -0.0349 -0.0001 0.0159  89  ALA   B CB  
5180 N N   . LYS   B 90  ? 0.1898 0.1338 0.1410 -0.0412 -0.0041 0.0082  90  LYS   B N   
5181 C CA  . LYS   B 90  ? 0.2037 0.1332 0.1410 -0.0402 -0.0052 0.0076  90  LYS   B CA  
5182 C C   . LYS   B 90  ? 0.1908 0.1263 0.1567 -0.0432 -0.0067 -0.0057 90  LYS   B C   
5183 O O   . LYS   B 90  ? 0.2019 0.1453 0.1763 -0.0592 0.0012  -0.0006 90  LYS   B O   
5184 C CB  . LYS   B 90  ? 0.2261 0.1407 0.1670 -0.0337 -0.0004 0.0194  90  LYS   B CB  
5185 C CG  . LYS   B 90  ? 0.2334 0.1503 0.1756 -0.0201 0.0350  0.0232  90  LYS   B CG  
5186 C CD  . LYS   B 90  ? 0.2691 0.1764 0.2210 -0.0122 0.0566  -0.0006 90  LYS   B CD  
5187 C CE  . LYS   B 90  ? 0.2812 0.1929 0.2721 -0.0185 0.0620  -0.0071 90  LYS   B CE  
5188 N NZ  . LYS   B 90  ? 0.2832 0.1884 0.2763 -0.0283 0.0693  -0.0084 90  LYS   B NZ  
5202 N N   . HIS   B 91  ? 0.1607 0.1148 0.1405 -0.0316 -0.0151 0.0057  91  HIS   B N   
5203 C CA  . HIS   B 91  ? 0.1506 0.1211 0.1446 -0.0229 -0.0127 0.0036  91  HIS   B CA  
5204 C C   . HIS   B 91  ? 0.1416 0.1224 0.1317 -0.0240 -0.0143 0.0056  91  HIS   B C   
5205 O O   . HIS   B 91  ? 0.1562 0.1273 0.1313 -0.0248 -0.0198 0.0040  91  HIS   B O   
5206 C CB  . HIS   B 91  ? 0.1695 0.1271 0.1779 -0.0079 -0.0107 0.0103  91  HIS   B CB  
5207 C CG  . HIS   B 91  ? 0.2113 0.1464 0.2561 0.0061  0.0192  0.0293  91  HIS   B CG  
5208 N ND1 . HIS   B 91  ? 0.2419 0.1503 0.3108 0.0047  0.0260  0.0195  91  HIS   B ND1 
5209 C CD2 . HIS   B 91  ? 0.2273 0.1784 0.2923 0.0221  0.0049  0.0616  91  HIS   B CD2 
5210 C CE1 . HIS   B 91  ? 0.2481 0.1659 0.3267 0.0183  0.0238  0.0288  91  HIS   B CE1 
5211 N NE2 . HIS   B 91  ? 0.2396 0.1841 0.3185 0.0310  0.0188  0.0664  91  HIS   B NE2 
5219 N N   . CYS   B 92  ? 0.1356 0.1217 0.1296 -0.0231 -0.0192 0.0001  92  CYS   B N   
5220 C CA  . CYS   B 92  ? 0.1304 0.1170 0.1294 -0.0214 -0.0069 0.0036  92  CYS   B CA  
5221 C C   . CYS   B 92  ? 0.1323 0.1110 0.1258 -0.0111 -0.0105 0.0012  92  CYS   B C   
5222 O O   . CYS   B 92  ? 0.1380 0.1211 0.1457 -0.0138 -0.0069 -0.0051 92  CYS   B O   
5223 C CB  . CYS   B 92  ? 0.1309 0.1322 0.1362 -0.0143 -0.0120 0.0043  92  CYS   B CB  
5224 S SG  . CYS   B 92  ? 0.1343 0.1292 0.1487 -0.0103 -0.0149 0.0057  92  CYS   B SG  
5230 N N   . LEU   B 93  ? 0.1250 0.1147 0.1211 -0.0102 -0.0107 -0.0055 93  LEU   B N   
5231 C CA  . LEU   B 93  ? 0.1278 0.1181 0.1272 -0.0028 -0.0102 -0.0047 93  LEU   B CA  
5232 C C   . LEU   B 93  ? 0.1176 0.1096 0.1233 -0.0052 -0.0079 -0.0001 93  LEU   B C   
5233 O O   . LEU   B 93  ? 0.1256 0.1163 0.1305 -0.0069 -0.0043 -0.0013 93  LEU   B O   
5234 C CB  . LEU   B 93  ? 0.1250 0.1177 0.1421 -0.0007 -0.0086 0.0007  93  LEU   B CB  
5235 C CG  . LEU   B 93  ? 0.1268 0.1312 0.1571 -0.0019 -0.0017 0.0119  93  LEU   B CG  
5236 C CD1 . LEU   B 93  ? 0.1297 0.1400 0.1606 0.0104  -0.0038 -0.0076 93  LEU   B CD1 
5237 C CD2 . LEU   B 93  ? 0.1254 0.1328 0.1607 -0.0020 -0.0112 0.0059  93  LEU   B CD2 
5249 N N   . HIS   B 94  ? 0.1255 0.1083 0.1237 -0.0084 -0.0141 0.0017  94  HIS   B N   
5250 C CA  . HIS   B 94  ? 0.1256 0.1072 0.1257 0.0004  -0.0032 0.0004  94  HIS   B CA  
5251 C C   . HIS   B 94  ? 0.1204 0.1135 0.1363 -0.0016 -0.0035 0.0035  94  HIS   B C   
5252 O O   . HIS   B 94  ? 0.1294 0.1237 0.1785 -0.0051 0.0144  -0.0052 94  HIS   B O   
5253 C CB  . HIS   B 94  ? 0.1269 0.1197 0.1341 -0.0029 -0.0075 0.0031  94  HIS   B CB  
5254 C CG  . HIS   B 94  ? 0.1288 0.1173 0.1366 -0.0074 -0.0247 0.0075  94  HIS   B CG  
5255 N ND1 . HIS   B 94  ? 0.1315 0.1214 0.1400 -0.0067 -0.0220 -0.0003 94  HIS   B ND1 
5256 C CD2 . HIS   B 94  ? 0.1315 0.1189 0.1468 -0.0035 -0.0195 0.0046  94  HIS   B CD2 
5257 C CE1 . HIS   B 94  ? 0.1348 0.1243 0.1389 -0.0110 -0.0211 0.0036  94  HIS   B CE1 
5258 N NE2 . HIS   B 94  ? 0.1330 0.1243 0.1453 -0.0144 -0.0158 0.0087  94  HIS   B NE2 
5266 N N   . VAL   B 95  ? 0.1159 0.1121 0.1406 0.0001  -0.0001 0.0057  95  VAL   B N   
5267 C CA  . VAL   B 95  ? 0.1186 0.1203 0.1362 0.0019  -0.0009 0.0092  95  VAL   B CA  
5268 C C   . VAL   B 95  ? 0.1223 0.1208 0.1411 -0.0023 0.0065  0.0019  95  VAL   B C   
5269 O O   . VAL   B 95  ? 0.1277 0.1220 0.1550 0.0042  0.0031  0.0111  95  VAL   B O   
5270 C CB  . VAL   B 95  ? 0.1245 0.1188 0.1444 -0.0046 -0.0091 -0.0012 95  VAL   B CB  
5271 C CG1 . VAL   B 95  ? 0.1350 0.1344 0.1579 -0.0106 -0.0024 0.0123  95  VAL   B CG1 
5272 C CG2 . VAL   B 95  ? 0.1362 0.1193 0.1417 0.0016  -0.0095 0.0054  95  VAL   B CG2 
5282 N N   . VAL   B 96  ? 0.1330 0.1236 0.1463 0.0106  0.0031  0.0122  96  VAL   B N   
5283 C CA  . VAL   B 96  ? 0.1384 0.1358 0.1350 0.0080  -0.0002 0.0149  96  VAL   B CA  
5284 C C   . VAL   B 96  ? 0.1439 0.1412 0.1351 0.0083  0.0098  0.0093  96  VAL   B C   
5285 O O   . VAL   B 96  ? 0.1469 0.1454 0.1556 0.0048  0.0154  0.0015  96  VAL   B O   
5286 C CB  . VAL   B 96  ? 0.1484 0.1507 0.1367 0.0070  0.0000  0.0021  96  VAL   B CB  
5287 C CG1 . VAL   B 96  ? 0.1495 0.1677 0.1501 0.0118  0.0009  0.0058  96  VAL   B CG1 
5288 C CG2 . VAL   B 96  ? 0.1620 0.1613 0.1448 0.0064  -0.0002 0.0031  96  VAL   B CG2 
5298 N N   . GLY   B 97  ? 0.1475 0.1408 0.1417 0.0057  0.0024  0.0146  97  GLY   B N   
5299 C CA  . GLY   B 97  ? 0.1589 0.1356 0.1538 0.0047  0.0097  0.0166  97  GLY   B CA  
5300 C C   . GLY   B 97  ? 0.1737 0.1462 0.1519 0.0114  0.0021  0.0201  97  GLY   B C   
5301 O O   . GLY   B 97  ? 0.1817 0.1586 0.1542 0.0053  -0.0006 0.0160  97  GLY   B O   
5305 N N   . PRO   B 98  ? 0.1869 0.1490 0.1598 0.0083  0.0251  0.0278  98  PRO   B N   
5306 C CA  . PRO   B 98  ? 0.1970 0.1680 0.1612 0.0112  0.0341  0.0172  98  PRO   B CA  
5307 C C   . PRO   B 98  ? 0.2038 0.1650 0.1322 0.0200  0.0298  0.0364  98  PRO   B C   
5308 O O   . PRO   B 98  ? 0.1990 0.1645 0.1559 0.0211  0.0284  0.0337  98  PRO   B O   
5309 C CB  . PRO   B 98  ? 0.1873 0.1715 0.1878 0.0061  0.0408  0.0241  98  PRO   B CB  
5310 C CG  . PRO   B 98  ? 0.1819 0.1623 0.1865 0.0096  0.0250  0.0313  98  PRO   B CG  
5311 C CD  . PRO   B 98  ? 0.1703 0.1519 0.1759 0.0148  0.0227  0.0297  98  PRO   B CD  
5319 N N   . ASN   B 99  ? 0.2098 0.1816 0.1419 0.0335  0.0238  0.0220  99  ASN   B N   
5320 C CA  . ASN   B 99  ? 0.2264 0.1929 0.1470 0.0374  0.0207  0.0388  99  ASN   B CA  
5321 C C   . ASN   B 99  ? 0.2515 0.2186 0.1825 0.0327  0.0309  0.0621  99  ASN   B C   
5322 O O   . ASN   B 99  ? 0.2612 0.2216 0.1930 0.0341  0.0190  0.0615  99  ASN   B O   
5323 C CB  . ASN   B 99  ? 0.2374 0.1944 0.1629 0.0403  0.0085  0.0329  99  ASN   B CB  
5324 C CG  . ASN   B 99  ? 0.2393 0.2002 0.1899 0.0356  -0.0061 0.0287  99  ASN   B CG  
5325 O OD1 . ASN   B 99  ? 0.2435 0.2024 0.2191 0.0389  -0.0051 0.0343  99  ASN   B OD1 
5326 N ND2 . ASN   B 99  ? 0.2373 0.2030 0.2074 0.0381  -0.0260 0.0239  99  ASN   B ND2 
5333 N N   A VAL   B 100 ? 0.2702 0.2309 0.2199 0.0185  0.0352  0.0840  100 VAL   B N   
5334 N N   B VAL   B 100 ? 0.2753 0.2340 0.2178 0.0265  0.0272  0.0748  100 VAL   B N   
5335 C CA  A VAL   B 100 ? 0.3000 0.2472 0.2753 0.0110  0.0364  0.0920  100 VAL   B CA  
5336 C CA  B VAL   B 100 ? 0.3027 0.2500 0.2593 0.0213  0.0226  0.0806  100 VAL   B CA  
5337 C C   A VAL   B 100 ? 0.3223 0.2509 0.2641 0.0192  0.0357  0.1085  100 VAL   B C   
5338 C C   B VAL   B 100 ? 0.3221 0.2553 0.2605 0.0262  0.0230  0.0994  100 VAL   B C   
5339 O O   A VAL   B 100 ? 0.3311 0.2571 0.2630 0.0137  0.0423  0.1035  100 VAL   B O   
5340 O O   B VAL   B 100 ? 0.3261 0.2598 0.2609 0.0232  0.0243  0.0975  100 VAL   B O   
5341 C CB  A VAL   B 100 ? 0.3134 0.2661 0.3511 -0.0081 0.0338  0.0923  100 VAL   B CB  
5342 C CB  B VAL   B 100 ? 0.3117 0.2617 0.3013 0.0092  0.0176  0.0730  100 VAL   B CB  
5343 C CG1 A VAL   B 100 ? 0.3200 0.2728 0.3801 -0.0126 0.0357  0.0926  100 VAL   B CG1 
5344 C CG1 B VAL   B 100 ? 0.3159 0.2661 0.3173 0.0058  0.0171  0.0709  100 VAL   B CG1 
5345 C CG2 A VAL   B 100 ? 0.3165 0.2736 0.3703 -0.0141 0.0351  0.0972  100 VAL   B CG2 
5346 C CG2 B VAL   B 100 ? 0.3138 0.2656 0.3131 0.0048  0.0164  0.0722  100 VAL   B CG2 
5365 N N   . ASN   B 101 ? 0.3362 0.2577 0.2583 0.0354  0.0224  0.1135  101 ASN   B N   
5366 C CA  . ASN   B 101 ? 0.3742 0.2789 0.2732 0.0508  0.0048  0.1262  101 ASN   B CA  
5367 C C   . ASN   B 101 ? 0.4164 0.3187 0.2556 0.0542  -0.0130 0.1418  101 ASN   B C   
5368 O O   . ASN   B 101 ? 0.4228 0.3348 0.2841 0.0604  -0.0161 0.1163  101 ASN   B O   
5369 C CB  . ASN   B 101 ? 0.3715 0.2681 0.2881 0.0487  0.0172  0.1116  101 ASN   B CB  
5370 C CG  . ASN   B 101 ? 0.3674 0.2551 0.2920 0.0474  0.0276  0.1135  101 ASN   B CG  
5371 O OD1 . ASN   B 101 ? 0.3730 0.2580 0.3215 0.0368  0.0487  0.1041  101 ASN   B OD1 
5372 N ND2 . ASN   B 101 ? 0.3600 0.2485 0.2894 0.0522  0.0216  0.1037  101 ASN   B ND2 
5380 N N   . LYS   B 102 ? 0.4490 0.3534 0.2629 0.0429  -0.0040 0.1343  102 LYS   B N   
5381 C CA  . LYS   B 102 ? 0.4804 0.3954 0.2884 0.0317  0.0096  0.1089  102 LYS   B CA  
5382 C C   . LYS   B 102 ? 0.4749 0.3930 0.2792 0.0347  0.0213  0.1142  102 LYS   B C   
5383 O O   . LYS   B 102 ? 0.4848 0.3989 0.3003 0.0365  0.0107  0.1080  102 LYS   B O   
5384 C CB  . LYS   B 102 ? 0.5147 0.4368 0.3439 0.0200  0.0211  0.0685  102 LYS   B CB  
5385 C CG  . LYS   B 102 ? 0.5421 0.4699 0.4114 0.0131  0.0343  0.0262  102 LYS   B CG  
5386 C CD  . LYS   B 102 ? 0.5617 0.4952 0.4822 0.0075  0.0474  -0.0082 102 LYS   B CD  
5387 C CE  . LYS   B 102 ? 0.5777 0.5158 0.5423 0.0018  0.0581  -0.0312 102 LYS   B CE  
5388 N NZ  . LYS   B 102 ? 0.5884 0.5297 0.5784 -0.0013 0.0636  -0.0442 102 LYS   B NZ  
5402 N N   . GLY   B 103 ? 0.4561 0.3822 0.2735 0.0338  0.0454  0.1135  103 GLY   B N   
5403 C CA  . GLY   B 103 ? 0.4353 0.3701 0.2873 0.0322  0.0659  0.0983  103 GLY   B CA  
5404 C C   . GLY   B 103 ? 0.4102 0.3522 0.2826 0.0259  0.0832  0.0798  103 GLY   B C   
5405 O O   . GLY   B 103 ? 0.4148 0.3589 0.2906 0.0233  0.0869  0.0770  103 GLY   B O   
5409 N N   A GLU   B 104 ? 0.3920 0.3317 0.2606 0.0269  0.0989  0.0689  104 GLU   B N   
5410 N N   B GLU   B 104 ? 0.3964 0.3448 0.2901 0.0221  0.0678  0.0632  104 GLU   B N   
5411 C CA  A GLU   B 104 ? 0.3738 0.3137 0.2402 0.0313  0.1073  0.0525  104 GLU   B CA  
5412 C CA  B GLU   B 104 ? 0.3817 0.3365 0.2928 0.0196  0.0530  0.0435  104 GLU   B CA  
5413 C C   A GLU   B 104 ? 0.3814 0.3175 0.2517 0.0206  0.1376  0.0455  104 GLU   B C   
5414 C C   B GLU   B 104 ? 0.3765 0.3342 0.3035 0.0146  0.0586  0.0330  104 GLU   B C   
5415 O O   A GLU   B 104 ? 0.3832 0.3184 0.2853 0.0219  0.1362  0.0312  104 GLU   B O   
5416 O O   B GLU   B 104 ? 0.3772 0.3347 0.3126 0.0147  0.0589  0.0279  104 GLU   B O   
5417 C CB  A GLU   B 104 ? 0.3533 0.2906 0.2268 0.0450  0.0728  0.0302  104 GLU   B CB  
5418 C CB  B GLU   B 104 ? 0.3733 0.3294 0.2852 0.0212  0.0330  0.0316  104 GLU   B CB  
5419 C CG  A GLU   B 104 ? 0.3373 0.2767 0.2148 0.0528  0.0315  0.0047  104 GLU   B CG  
5420 C CG  B GLU   B 104 ? 0.3665 0.3245 0.2780 0.0211  0.0134  0.0186  104 GLU   B CG  
5421 C CD  A GLU   B 104 ? 0.3226 0.2621 0.1934 0.0585  -0.0010 -0.0041 104 GLU   B CD  
5422 C CD  B GLU   B 104 ? 0.3611 0.3197 0.2716 0.0199  -0.0020 0.0100  104 GLU   B CD  
5423 O OE1 A GLU   B 104 ? 0.3026 0.2440 0.1611 0.0690  0.0058  -0.0001 104 GLU   B OE1 
5424 O OE1 B GLU   B 104 ? 0.3573 0.3158 0.2645 0.0193  -0.0029 0.0097  104 GLU   B OE1 
5425 O OE2 A GLU   B 104 ? 0.3291 0.2722 0.2101 0.0501  -0.0262 -0.0144 104 GLU   B OE2 
5426 O OE2 B GLU   B 104 ? 0.3611 0.3209 0.2758 0.0193  -0.0111 0.0035  104 GLU   B OE2 
5439 N N   A ASP   B 105 ? 0.3816 0.3241 0.2513 0.0063  0.1641  0.0489  105 ASP   B N   
5440 N N   B ASP   B 105 ? 0.3696 0.3322 0.3052 0.0085  0.0644  0.0280  105 ASP   B N   
5441 C CA  A ASP   B 105 ? 0.3861 0.3260 0.2752 -0.0063 0.1818  0.0358  105 ASP   B CA  
5442 C CA  B ASP   B 105 ? 0.3639 0.3291 0.3113 0.0025  0.0691  0.0199  105 ASP   B CA  
5443 C C   A ASP   B 105 ? 0.3688 0.2890 0.2556 -0.0189 0.1715  0.0317  105 ASP   B C   
5444 C C   B ASP   B 105 ? 0.3552 0.3201 0.2962 -0.0020 0.0667  0.0122  105 ASP   B C   
5445 O O   A ASP   B 105 ? 0.3528 0.2773 0.2471 -0.0168 0.1647  0.0337  105 ASP   B O   
5446 O O   B ASP   B 105 ? 0.3533 0.3173 0.2884 -0.0014 0.0684  0.0116  105 ASP   B O   
5447 C CB  A ASP   B 105 ? 0.4038 0.3569 0.3393 -0.0005 0.1966  0.0170  105 ASP   B CB  
5448 C CB  B ASP   B 105 ? 0.3650 0.3331 0.3331 0.0032  0.0755  0.0180  105 ASP   B CB  
5449 C CG  A ASP   B 105 ? 0.4150 0.3774 0.4036 0.0025  0.2121  0.0004  105 ASP   B CG  
5450 C CG  B ASP   B 105 ? 0.3652 0.3346 0.3548 0.0030  0.0814  0.0172  105 ASP   B CG  
5451 O OD1 A ASP   B 105 ? 0.4155 0.3840 0.4141 -0.0039 0.2243  0.0059  105 ASP   B OD1 
5452 O OD1 B ASP   B 105 ? 0.3643 0.3350 0.3604 0.0006  0.0832  0.0180  105 ASP   B OD1 
5453 O OD2 A ASP   B 105 ? 0.4212 0.3860 0.4476 0.0079  0.2053  -0.0133 105 ASP   B OD2 
5454 O OD2 B ASP   B 105 ? 0.3644 0.3352 0.3625 0.0034  0.0844  0.0187  105 ASP   B OD2 
5463 N N   A ILE   B 106 ? 0.3602 0.2631 0.2716 -0.0291 0.1517  0.0263  106 ILE   B N   
5464 N N   B ILE   B 106 ? 0.3476 0.3139 0.2937 -0.0053 0.0592  0.0063  106 ILE   B N   
5465 C CA  A ILE   B 106 ? 0.3399 0.2336 0.2838 -0.0448 0.1547  0.0207  106 ILE   B CA  
5466 C CA  B ILE   B 106 ? 0.3368 0.3076 0.2945 -0.0082 0.0568  0.0004  106 ILE   B CA  
5467 C C   A ILE   B 106 ? 0.3052 0.2306 0.2753 -0.0402 0.1460  -0.0018 106 ILE   B C   
5468 C C   B ILE   B 106 ? 0.3205 0.3056 0.2913 -0.0068 0.0538  -0.0061 106 ILE   B C   
5469 O O   A ILE   B 106 ? 0.2963 0.2030 0.2675 -0.0415 0.1357  -0.0121 106 ILE   B O   
5470 O O   B ILE   B 106 ? 0.3187 0.3022 0.2874 -0.0074 0.0490  -0.0081 106 ILE   B O   
5471 C CB  A ILE   B 106 ? 0.3605 0.2247 0.3158 -0.0543 0.1503  0.0293  106 ILE   B CB  
5472 C CB  B ILE   B 106 ? 0.3427 0.3064 0.3012 -0.0114 0.0561  0.0007  106 ILE   B CB  
5473 C CG1 A ILE   B 106 ? 0.3697 0.2251 0.3259 -0.0442 0.1440  0.0276  106 ILE   B CG1 
5474 C CG1 B ILE   B 106 ? 0.3449 0.3055 0.3026 -0.0102 0.0552  0.0020  106 ILE   B CG1 
5475 C CG2 A ILE   B 106 ? 0.3653 0.2276 0.3445 -0.0654 0.1543  0.0356  106 ILE   B CG2 
5476 C CG2 B ILE   B 106 ? 0.3450 0.3081 0.3097 -0.0133 0.0573  0.0006  106 ILE   B CG2 
5477 C CD1 A ILE   B 106 ? 0.3747 0.2299 0.3267 -0.0347 0.1414  0.0308  106 ILE   B CD1 
5478 C CD1 B ILE   B 106 ? 0.3461 0.3058 0.3034 -0.0085 0.0545  0.0036  106 ILE   B CD1 
5501 N N   A GLN   B 107 ? 0.2890 0.2631 0.2941 -0.0353 0.1313  -0.0046 107 GLN   B N   
5502 N N   B GLN   B 107 ? 0.3069 0.3079 0.2992 -0.0064 0.0523  -0.0082 107 GLN   B N   
5503 C CA  A GLN   B 107 ? 0.2708 0.2924 0.3149 -0.0316 0.1160  -0.0016 107 GLN   B CA  
5504 C CA  B GLN   B 107 ? 0.2923 0.3080 0.3099 -0.0056 0.0515  -0.0066 107 GLN   B CA  
5505 C C   A GLN   B 107 ? 0.2416 0.2724 0.2862 -0.0190 0.0838  -0.0090 107 GLN   B C   
5506 C C   B GLN   B 107 ? 0.2585 0.2842 0.2770 -0.0039 0.0553  -0.0096 107 GLN   B C   
5507 O O   A GLN   B 107 ? 0.2334 0.2683 0.3176 -0.0095 0.0622  -0.0170 107 GLN   B O   
5508 O O   B GLN   B 107 ? 0.2587 0.2861 0.2844 -0.0017 0.0474  -0.0130 107 GLN   B O   
5509 C CB  A GLN   B 107 ? 0.3001 0.3415 0.3898 -0.0306 0.1023  0.0063  107 GLN   B CB  
5510 C CB  B GLN   B 107 ? 0.3132 0.3314 0.3601 -0.0052 0.0429  -0.0025 107 GLN   B CB  
5511 C CG  A GLN   B 107 ? 0.3330 0.3843 0.4705 -0.0238 0.0673  0.0083  107 GLN   B CG  
5512 C CG  B GLN   B 107 ? 0.3327 0.3512 0.4100 -0.0035 0.0304  0.0008  107 GLN   B CG  
5513 C CD  A GLN   B 107 ? 0.3572 0.4202 0.5350 -0.0207 0.0428  0.0126  107 GLN   B CD  
5514 C CD  B GLN   B 107 ? 0.3476 0.3662 0.4507 -0.0028 0.0213  0.0042  107 GLN   B CD  
5515 O OE1 A GLN   B 107 ? 0.3647 0.4330 0.5600 -0.0161 0.0382  0.0120  107 GLN   B OE1 
5516 O OE1 B GLN   B 107 ? 0.3528 0.3719 0.4653 -0.0015 0.0199  0.0048  107 GLN   B OE1 
5517 N NE2 A GLN   B 107 ? 0.3682 0.4310 0.5571 -0.0194 0.0325  0.0175  107 GLN   B NE2 
5518 N NE2 B GLN   B 107 ? 0.3536 0.3706 0.4652 -0.0023 0.0176  0.0065  107 GLN   B NE2 
5535 N N   . LEU   B 108 ? 0.2240 0.2569 0.2467 -0.0005 0.0652  -0.0087 108 LEU   B N   
5536 C CA  . LEU   B 108 ? 0.2015 0.2250 0.2078 0.0185  0.0444  0.0021  108 LEU   B CA  
5537 C C   . LEU   B 108 ? 0.1764 0.1845 0.1981 0.0208  0.0193  0.0213  108 LEU   B C   
5538 O O   . LEU   B 108 ? 0.1800 0.1711 0.1949 0.0212  0.0187  0.0124  108 LEU   B O   
5539 C CB  . LEU   B 108 ? 0.2165 0.2392 0.1936 0.0137  0.0470  0.0072  108 LEU   B CB  
5540 C CG  . LEU   B 108 ? 0.2346 0.2656 0.2035 0.0189  0.0409  -0.0103 108 LEU   B CG  
5541 C CD1 . LEU   B 108 ? 0.2436 0.2797 0.1967 0.0098  0.0395  -0.0072 108 LEU   B CD1 
5542 C CD2 . LEU   B 108 ? 0.2548 0.2787 0.2216 0.0258  0.0327  -0.0190 108 LEU   B CD2 
5555 N N   . LEU   B 109 ? 0.1668 0.1626 0.1940 0.0182  0.0248  0.0164  109 LEU   B N   
5556 C CA  . LEU   B 109 ? 0.1493 0.1352 0.2070 0.0105  0.0252  0.0257  109 LEU   B CA  
5557 C C   . LEU   B 109 ? 0.1391 0.1237 0.2116 0.0089  0.0236  0.0163  109 LEU   B C   
5558 O O   . LEU   B 109 ? 0.1376 0.1277 0.2048 0.0035  0.0225  0.0285  109 LEU   B O   
5559 C CB  . LEU   B 109 ? 0.1623 0.1313 0.2083 0.0085  0.0175  0.0354  109 LEU   B CB  
5560 C CG  . LEU   B 109 ? 0.1582 0.1327 0.2053 0.0054  0.0120  0.0209  109 LEU   B CG  
5561 C CD1 . LEU   B 109 ? 0.1538 0.1450 0.1994 0.0156  0.0176  0.0135  109 LEU   B CD1 
5562 C CD2 . LEU   B 109 ? 0.1657 0.1397 0.2157 0.0101  0.0080  0.0236  109 LEU   B CD2 
5574 N N   . LYS   B 110 ? 0.1382 0.1253 0.1977 0.0024  0.0261  0.0217  110 LYS   B N   
5575 C CA  . LYS   B 110 ? 0.1353 0.1276 0.1865 0.0005  0.0177  0.0142  110 LYS   B CA  
5576 C C   . LYS   B 110 ? 0.1319 0.1273 0.1772 0.0008  0.0186  0.0146  110 LYS   B C   
5577 O O   . LYS   B 110 ? 0.1291 0.1287 0.1768 -0.0034 0.0114  0.0053  110 LYS   B O   
5578 C CB  . LYS   B 110 ? 0.1346 0.1296 0.2122 -0.0048 0.0191  0.0081  110 LYS   B CB  
5579 C CG  . LYS   B 110 ? 0.1384 0.1301 0.2219 -0.0038 0.0094  0.0132  110 LYS   B CG  
5580 C CD  . LYS   B 110 ? 0.1363 0.1316 0.2409 -0.0072 0.0169  0.0148  110 LYS   B CD  
5581 C CE  . LYS   B 110 ? 0.1385 0.1388 0.2582 0.0029  0.0118  0.0058  110 LYS   B CE  
5582 N NZ  . LYS   B 110 ? 0.1428 0.1622 0.2449 0.0018  0.0050  0.0020  110 LYS   B NZ  
5596 N N   . SER   B 111 ? 0.1420 0.1303 0.1765 -0.0036 0.0246  0.0150  111 SER   B N   
5597 C CA  . SER   B 111 ? 0.1452 0.1337 0.1784 0.0018  0.0198  0.0157  111 SER   B CA  
5598 C C   . SER   B 111 ? 0.1360 0.1292 0.1720 0.0023  0.0065  0.0049  111 SER   B C   
5599 O O   . SER   B 111 ? 0.1328 0.1305 0.1845 0.0029  0.0035  0.0083  111 SER   B O   
5600 C CB  . SER   B 111 ? 0.1568 0.1574 0.1878 0.0055  0.0292  0.0257  111 SER   B CB  
5601 O OG  . SER   B 111 ? 0.1765 0.1933 0.2068 0.0058  0.0365  0.0172  111 SER   B OG  
5607 N N   . ALA   B 112 ? 0.1275 0.1274 0.1834 0.0079  0.0135  0.0173  112 ALA   B N   
5608 C CA  . ALA   B 112 ? 0.1276 0.1350 0.1682 0.0013  0.0022  0.0057  112 ALA   B CA  
5609 C C   . ALA   B 112 ? 0.1179 0.1254 0.1636 0.0025  0.0015  0.0066  112 ALA   B C   
5610 O O   . ALA   B 112 ? 0.1204 0.1278 0.1728 -0.0021 -0.0001 0.0004  112 ALA   B O   
5611 C CB  . ALA   B 112 ? 0.1303 0.1440 0.1797 0.0091  0.0007  0.0156  112 ALA   B CB  
5617 N N   . TYR   B 113 ? 0.1181 0.1147 0.1747 -0.0007 0.0074  0.0065  113 TYR   B N   
5618 C CA  . TYR   B 113 ? 0.1185 0.1115 0.1661 -0.0017 0.0051  -0.0024 113 TYR   B CA  
5619 C C   . TYR   B 113 ? 0.1134 0.1047 0.1704 -0.0044 -0.0002 0.0080  113 TYR   B C   
5620 O O   . TYR   B 113 ? 0.1171 0.1123 0.1646 -0.0031 0.0002  -0.0011 113 TYR   B O   
5621 C CB  . TYR   B 113 ? 0.1234 0.1140 0.1756 -0.0044 0.0129  0.0046  113 TYR   B CB  
5622 C CG  . TYR   B 113 ? 0.1203 0.1140 0.1805 -0.0031 0.0064  0.0058  113 TYR   B CG  
5623 C CD1 . TYR   B 113 ? 0.1298 0.1185 0.1936 -0.0033 0.0103  0.0177  113 TYR   B CD1 
5624 C CD2 . TYR   B 113 ? 0.1281 0.1166 0.1890 -0.0042 0.0029  0.0087  113 TYR   B CD2 
5625 C CE1 . TYR   B 113 ? 0.1274 0.1210 0.1815 0.0016  0.0147  0.0053  113 TYR   B CE1 
5626 C CE2 . TYR   B 113 ? 0.1365 0.1126 0.1954 0.0035  0.0089  0.0113  113 TYR   B CE2 
5627 C CZ  . TYR   B 113 ? 0.1284 0.1167 0.1988 0.0055  0.0046  0.0040  113 TYR   B CZ  
5628 O OH  . TYR   B 113 ? 0.1324 0.1147 0.2113 0.0092  0.0106  0.0044  113 TYR   B OH  
5638 N N   . GLU   B 114 ? 0.1139 0.1072 0.1810 0.0014  0.0078  0.0061  114 GLU   B N   
5639 C CA  . GLU   B 114 ? 0.1158 0.1061 0.1810 0.0039  -0.0014 0.0055  114 GLU   B CA  
5640 C C   . GLU   B 114 ? 0.1179 0.1067 0.1665 0.0039  0.0017  0.0066  114 GLU   B C   
5641 O O   . GLU   B 114 ? 0.1196 0.1125 0.1737 0.0043  0.0047  0.0066  114 GLU   B O   
5642 C CB  . GLU   B 114 ? 0.1154 0.1125 0.1912 0.0026  0.0016  0.0062  114 GLU   B CB  
5643 C CG  . GLU   B 114 ? 0.1254 0.1171 0.1850 0.0012  0.0065  0.0078  114 GLU   B CG  
5644 C CD  . GLU   B 114 ? 0.1208 0.1226 0.1848 -0.0051 0.0100  0.0066  114 GLU   B CD  
5645 O OE1 . GLU   B 114 ? 0.1231 0.1346 0.1904 -0.0068 0.0105  0.0062  114 GLU   B OE1 
5646 O OE2 . GLU   B 114 ? 0.1234 0.1424 0.2025 -0.0158 0.0121  0.0108  114 GLU   B OE2 
5653 N N   . ASN   B 115 ? 0.1197 0.1057 0.1639 0.0033  -0.0033 0.0058  115 ASN   B N   
5654 C CA  . ASN   B 115 ? 0.1230 0.1128 0.1574 -0.0038 0.0010  0.0016  115 ASN   B CA  
5655 C C   . ASN   B 115 ? 0.1146 0.1082 0.1569 -0.0092 -0.0061 -0.0068 115 ASN   B C   
5656 O O   . ASN   B 115 ? 0.1279 0.1143 0.1666 -0.0108 -0.0030 -0.0015 115 ASN   B O   
5657 C CB  . ASN   B 115 ? 0.1290 0.1234 0.1576 -0.0100 0.0005  0.0037  115 ASN   B CB  
5658 C CG  . ASN   B 115 ? 0.1436 0.1266 0.1577 -0.0009 -0.0039 0.0019  115 ASN   B CG  
5659 O OD1 . ASN   B 115 ? 0.1892 0.1398 0.1820 0.0033  0.0126  -0.0110 115 ASN   B OD1 
5660 N ND2 . ASN   B 115 ? 0.1373 0.1396 0.1613 -0.0023 0.0014  0.0026  115 ASN   B ND2 
5667 N N   . PHE   B 116 ? 0.1137 0.1142 0.1473 -0.0031 -0.0005 0.0001  116 PHE   B N   
5668 C CA  . PHE   B 116 ? 0.1200 0.1147 0.1516 -0.0085 -0.0018 0.0033  116 PHE   B CA  
5669 C C   . PHE   B 116 ? 0.1251 0.1042 0.1481 -0.0070 -0.0060 0.0077  116 PHE   B C   
5670 O O   . PHE   B 116 ? 0.1276 0.1134 0.1546 -0.0003 -0.0034 0.0018  116 PHE   B O   
5671 C CB  . PHE   B 116 ? 0.1169 0.1139 0.1450 -0.0010 -0.0091 0.0011  116 PHE   B CB  
5672 C CG  . PHE   B 116 ? 0.1145 0.1116 0.1476 -0.0018 -0.0051 0.0001  116 PHE   B CG  
5673 C CD1 . PHE   B 116 ? 0.1206 0.1186 0.1715 -0.0022 0.0016  0.0010  116 PHE   B CD1 
5674 C CD2 . PHE   B 116 ? 0.1185 0.1189 0.1453 0.0032  -0.0029 -0.0078 116 PHE   B CD2 
5675 C CE1 . PHE   B 116 ? 0.1193 0.1204 0.1681 0.0001  -0.0104 0.0011  116 PHE   B CE1 
5676 C CE2 . PHE   B 116 ? 0.1210 0.1217 0.1566 0.0003  0.0020  -0.0012 116 PHE   B CE2 
5677 C CZ  . PHE   B 116 ? 0.1129 0.1209 0.1680 0.0018  -0.0022 -0.0023 116 PHE   B CZ  
5687 N N   . ASN   B 117 ? 0.1187 0.1041 0.1708 -0.0014 -0.0069 0.0054  117 ASN   B N   
5688 C CA  . ASN   B 117 ? 0.1225 0.1095 0.1755 0.0018  -0.0068 -0.0011 117 ASN   B CA  
5689 C C   . ASN   B 117 ? 0.1234 0.1086 0.1758 0.0049  -0.0018 -0.0003 117 ASN   B C   
5690 O O   . ASN   B 117 ? 0.1370 0.1152 0.1951 0.0014  -0.0195 0.0039  117 ASN   B O   
5691 C CB  . ASN   B 117 ? 0.1248 0.1195 0.1701 -0.0024 -0.0042 -0.0064 117 ASN   B CB  
5692 C CG  . ASN   B 117 ? 0.1251 0.1190 0.1701 -0.0023 0.0013  -0.0123 117 ASN   B CG  
5693 O OD1 . ASN   B 117 ? 0.1475 0.1166 0.1820 -0.0129 0.0081  -0.0038 117 ASN   B OD1 
5694 N ND2 . ASN   B 117 ? 0.1272 0.1198 0.1705 -0.0020 -0.0012 -0.0063 117 ASN   B ND2 
5701 N N   . GLN   B 118 ? 0.1235 0.1075 0.1714 -0.0073 -0.0116 -0.0042 118 GLN   B N   
5702 C CA  . GLN   B 118 ? 0.1345 0.1115 0.1836 -0.0004 -0.0090 -0.0019 118 GLN   B CA  
5703 C C   . GLN   B 118 ? 0.1392 0.1098 0.1813 -0.0001 -0.0064 -0.0038 118 GLN   B C   
5704 O O   . GLN   B 118 ? 0.1585 0.1120 0.2160 -0.0098 0.0023  0.0044  118 GLN   B O   
5705 C CB  . GLN   B 118 ? 0.1408 0.1174 0.1972 0.0011  -0.0144 -0.0062 118 GLN   B CB  
5706 C CG  . GLN   B 118 ? 0.1452 0.1191 0.1955 0.0062  -0.0071 -0.0094 118 GLN   B CG  
5707 C CD  . GLN   B 118 ? 0.1501 0.1159 0.1879 0.0006  -0.0040 -0.0153 118 GLN   B CD  
5708 O OE1 . GLN   B 118 ? 0.1620 0.1152 0.2027 0.0013  0.0096  0.0015  118 GLN   B OE1 
5709 N NE2 . GLN   B 118 ? 0.1553 0.1170 0.2004 0.0032  -0.0091 -0.0004 118 GLN   B NE2 
5718 N N   . HIS   B 119 ? 0.1365 0.1169 0.1517 -0.0049 -0.0080 0.0053  119 HIS   B N   
5719 C CA  . HIS   B 119 ? 0.1444 0.1251 0.1446 -0.0014 -0.0077 -0.0009 119 HIS   B CA  
5720 C C   . HIS   B 119 ? 0.1446 0.1234 0.1504 -0.0020 -0.0201 0.0062  119 HIS   B C   
5721 O O   . HIS   B 119 ? 0.1558 0.1236 0.1658 -0.0212 -0.0164 0.0085  119 HIS   B O   
5722 C CB  . HIS   B 119 ? 0.1485 0.1389 0.1545 -0.0019 -0.0131 -0.0061 119 HIS   B CB  
5723 C CG  . HIS   B 119 ? 0.1507 0.1600 0.1693 0.0108  -0.0310 -0.0209 119 HIS   B CG  
5724 N ND1 . HIS   B 119 ? 0.1666 0.1776 0.2022 0.0056  -0.0413 -0.0387 119 HIS   B ND1 
5725 C CD2 . HIS   B 119 ? 0.1664 0.1788 0.1787 0.0394  -0.0442 -0.0251 119 HIS   B CD2 
5726 C CE1 . HIS   B 119 ? 0.1861 0.1906 0.2105 0.0160  -0.0474 -0.0541 119 HIS   B CE1 
5727 N NE2 . HIS   B 119 ? 0.1858 0.2031 0.1946 0.0352  -0.0477 -0.0395 119 HIS   B NE2 
5735 N N   . GLU   B 120 ? 0.1594 0.1243 0.1515 -0.0076 -0.0266 0.0152  120 GLU   B N   
5736 C CA  . GLU   B 120 ? 0.1832 0.1383 0.1649 -0.0003 -0.0374 0.0223  120 GLU   B CA  
5737 C C   . GLU   B 120 ? 0.1649 0.1294 0.1456 -0.0092 -0.0268 0.0195  120 GLU   B C   
5738 O O   . GLU   B 120 ? 0.1604 0.1433 0.1449 -0.0114 -0.0223 0.0083  120 GLU   B O   
5739 C CB  . GLU   B 120 ? 0.2446 0.1712 0.2378 0.0196  -0.0630 0.0400  120 GLU   B CB  
5740 C CG  . GLU   B 120 ? 0.2992 0.2451 0.3443 0.0316  -0.0905 0.0652  120 GLU   B CG  
5741 C CD  . GLU   B 120 ? 0.3446 0.3132 0.4594 0.0300  -0.0972 0.0781  120 GLU   B CD  
5742 O OE1 . GLU   B 120 ? 0.3626 0.3339 0.5005 0.0217  -0.0931 0.0846  120 GLU   B OE1 
5743 O OE2 . GLU   B 120 ? 0.3651 0.3366 0.5179 0.0265  -0.0942 0.0743  120 GLU   B OE2 
5750 N N   . VAL   B 121 ? 0.1590 0.1232 0.1478 -0.0120 -0.0148 0.0163  121 VAL   B N   
5751 C CA  . VAL   B 121 ? 0.1544 0.1393 0.1387 -0.0141 -0.0164 0.0078  121 VAL   B CA  
5752 C C   . VAL   B 121 ? 0.1427 0.1304 0.1359 -0.0179 -0.0108 0.0067  121 VAL   B C   
5753 O O   . VAL   B 121 ? 0.1521 0.1270 0.1590 -0.0258 -0.0189 0.0007  121 VAL   B O   
5754 C CB  . VAL   B 121 ? 0.1781 0.1743 0.1469 -0.0031 -0.0162 0.0121  121 VAL   B CB  
5755 C CG1 . VAL   B 121 ? 0.1808 0.1824 0.1785 -0.0107 -0.0059 0.0082  121 VAL   B CG1 
5756 C CG2 . VAL   B 121 ? 0.2037 0.1982 0.1615 0.0031  -0.0105 0.0013  121 VAL   B CG2 
5766 N N   . LEU   B 122 ? 0.1353 0.1281 0.1338 -0.0147 -0.0205 0.0042  122 LEU   B N   
5767 C CA  . LEU   B 122 ? 0.1312 0.1345 0.1355 -0.0139 -0.0168 0.0056  122 LEU   B CA  
5768 C C   . LEU   B 122 ? 0.1309 0.1164 0.1359 -0.0193 -0.0107 0.0027  122 LEU   B C   
5769 O O   . LEU   B 122 ? 0.1411 0.1203 0.1686 -0.0237 -0.0203 -0.0008 122 LEU   B O   
5770 C CB  . LEU   B 122 ? 0.1569 0.1461 0.1680 -0.0048 -0.0138 0.0093  122 LEU   B CB  
5771 C CG  . LEU   B 122 ? 0.1441 0.1519 0.1645 -0.0128 -0.0012 0.0086  122 LEU   B CG  
5772 C CD1 . LEU   B 122 ? 0.1518 0.1715 0.1733 -0.0176 -0.0089 0.0042  122 LEU   B CD1 
5773 C CD2 . LEU   B 122 ? 0.1431 0.1525 0.1502 -0.0087 -0.0003 -0.0010 122 LEU   B CD2 
5785 N N   . LEU   B 123 ? 0.1341 0.1102 0.1316 -0.0174 -0.0088 0.0055  123 LEU   B N   
5786 C CA  . LEU   B 123 ? 0.1355 0.1137 0.1343 -0.0218 -0.0104 -0.0054 123 LEU   B CA  
5787 C C   . LEU   B 123 ? 0.1329 0.1126 0.1359 -0.0228 -0.0140 -0.0009 123 LEU   B C   
5788 O O   . LEU   B 123 ? 0.1459 0.1133 0.1423 -0.0315 -0.0146 -0.0001 123 LEU   B O   
5789 C CB  . LEU   B 123 ? 0.1385 0.1206 0.1453 -0.0183 -0.0075 -0.0114 123 LEU   B CB  
5790 C CG  . LEU   B 123 ? 0.1363 0.1257 0.1579 -0.0122 -0.0044 0.0044  123 LEU   B CG  
5791 C CD1 . LEU   B 123 ? 0.1511 0.1318 0.1708 -0.0118 0.0007  -0.0122 123 LEU   B CD1 
5792 C CD2 . LEU   B 123 ? 0.1418 0.1355 0.1775 -0.0112 0.0011  0.0129  123 LEU   B CD2 
5804 N N   . ALA   B 124 ? 0.1303 0.1113 0.1413 -0.0191 -0.0062 -0.0002 124 ALA   B N   
5805 C CA  . ALA   B 124 ? 0.1222 0.1139 0.1451 -0.0154 -0.0050 -0.0056 124 ALA   B CA  
5806 C C   . ALA   B 124 ? 0.1187 0.1106 0.1466 -0.0136 -0.0042 -0.0079 124 ALA   B C   
5807 O O   . ALA   B 124 ? 0.1310 0.1164 0.1522 -0.0104 -0.0091 -0.0023 124 ALA   B O   
5808 C CB  . ALA   B 124 ? 0.1332 0.1168 0.1511 -0.0085 0.0016  -0.0014 124 ALA   B CB  
5814 N N   . PRO   B 125 ? 0.1287 0.1159 0.1418 -0.0147 -0.0153 0.0089  125 PRO   B N   
5815 C CA  . PRO   B 125 ? 0.1360 0.1168 0.1564 -0.0137 -0.0141 0.0159  125 PRO   B CA  
5816 C C   . PRO   B 125 ? 0.1278 0.1119 0.1696 -0.0110 -0.0091 0.0026  125 PRO   B C   
5817 O O   . PRO   B 125 ? 0.1308 0.1161 0.1817 -0.0087 -0.0080 0.0132  125 PRO   B O   
5818 C CB  . PRO   B 125 ? 0.1414 0.1428 0.1693 -0.0165 -0.0111 0.0253  125 PRO   B CB  
5819 C CG  . PRO   B 125 ? 0.1475 0.1467 0.1603 -0.0251 -0.0191 0.0112  125 PRO   B CG  
5820 C CD  . PRO   B 125 ? 0.1411 0.1249 0.1428 -0.0237 -0.0107 0.0050  125 PRO   B CD  
5828 N N   . LEU   B 126 ? 0.1393 0.1121 0.1876 -0.0134 0.0068  0.0116  126 LEU   B N   
5829 C CA  . LEU   B 126 ? 0.1452 0.1208 0.1816 -0.0099 0.0161  0.0106  126 LEU   B CA  
5830 C C   . LEU   B 126 ? 0.1357 0.1286 0.1876 -0.0009 0.0164  0.0131  126 LEU   B C   
5831 O O   . LEU   B 126 ? 0.1540 0.1554 0.2105 0.0181  -0.0058 -0.0072 126 LEU   B O   
5832 C CB  . LEU   B 126 ? 0.1661 0.1236 0.2034 -0.0149 0.0270  0.0080  126 LEU   B CB  
5833 C CG  . LEU   B 126 ? 0.1822 0.1325 0.2106 -0.0196 0.0237  -0.0150 126 LEU   B CG  
5834 C CD1 . LEU   B 126 ? 0.1980 0.1381 0.2558 -0.0182 0.0194  -0.0123 126 LEU   B CD1 
5835 C CD2 . LEU   B 126 ? 0.1839 0.1394 0.2149 -0.0265 0.0142  -0.0128 126 LEU   B CD2 
5847 N N   . LEU   B 127 ? 0.1356 0.1172 0.1866 0.0008  0.0148  0.0121  127 LEU   B N   
5848 C CA  . LEU   B 127 ? 0.1401 0.1248 0.1915 -0.0052 0.0199  0.0195  127 LEU   B CA  
5849 C C   . LEU   B 127 ? 0.1340 0.1198 0.1961 -0.0006 0.0131  0.0214  127 LEU   B C   
5850 O O   . LEU   B 127 ? 0.1377 0.1231 0.1933 -0.0074 0.0035  0.0213  127 LEU   B O   
5851 C CB  . LEU   B 127 ? 0.1470 0.1273 0.1987 -0.0022 0.0139  0.0221  127 LEU   B CB  
5852 C CG  . LEU   B 127 ? 0.1565 0.1269 0.2180 0.0020  0.0131  0.0181  127 LEU   B CG  
5853 C CD1 . LEU   B 127 ? 0.1584 0.1286 0.2173 0.0036  0.0099  0.0099  127 LEU   B CD1 
5854 C CD2 . LEU   B 127 ? 0.1611 0.1353 0.2423 -0.0103 0.0143  0.0297  127 LEU   B CD2 
5866 N N   . SER   B 128 ? 0.1397 0.1242 0.1907 -0.0005 -0.0028 0.0177  128 SER   B N   
5867 C CA  . SER   B 128 ? 0.1538 0.1318 0.1931 0.0073  -0.0086 0.0159  128 SER   B CA  
5868 C C   . SER   B 128 ? 0.1627 0.1350 0.2071 0.0086  -0.0232 0.0103  128 SER   B C   
5869 O O   . SER   B 128 ? 0.1758 0.1381 0.2344 0.0044  -0.0156 0.0279  128 SER   B O   
5870 C CB  . SER   B 128 ? 0.1696 0.1329 0.1848 0.0085  -0.0042 0.0183  128 SER   B CB  
5871 O OG  . SER   B 128 ? 0.1776 0.1442 0.1902 0.0137  0.0053  0.0238  128 SER   B OG  
5877 N N   . ALA   B 129 ? 0.1726 0.1421 0.2273 0.0219  -0.0192 -0.0018 129 ALA   B N   
5878 C CA  . ALA   B 129 ? 0.1794 0.1458 0.2448 0.0247  -0.0200 -0.0147 129 ALA   B CA  
5879 C C   . ALA   B 129 ? 0.1661 0.1358 0.2324 0.0174  0.0039  0.0031  129 ALA   B C   
5880 O O   . ALA   B 129 ? 0.1612 0.1443 0.2316 0.0184  -0.0020 0.0158  129 ALA   B O   
5881 C CB  . ALA   B 129 ? 0.2031 0.1697 0.2771 0.0263  -0.0127 -0.0207 129 ALA   B CB  
5887 N N   . GLY   B 130 ? 0.1671 0.1356 0.2320 0.0225  0.0081  0.0015  130 GLY   B N   
5888 C CA  . GLY   B 130 ? 0.1804 0.1486 0.2484 0.0181  0.0242  -0.0062 130 GLY   B CA  
5889 C C   . GLY   B 130 ? 0.1822 0.1462 0.2401 0.0138  0.0117  0.0060  130 GLY   B C   
5890 O O   . GLY   B 130 ? 0.2021 0.1578 0.2538 0.0188  0.0131  0.0213  130 GLY   B O   
5894 N N   . ILE   B 131 ? 0.1735 0.1653 0.2504 0.0263  0.0042  0.0046  131 ILE   B N   
5895 C CA  . ILE   B 131 ? 0.1888 0.1812 0.2499 0.0256  -0.0106 0.0165  131 ILE   B CA  
5896 C C   . ILE   B 131 ? 0.2031 0.1711 0.2145 0.0187  -0.0081 0.0250  131 ILE   B C   
5897 O O   . ILE   B 131 ? 0.2340 0.1870 0.2218 0.0204  -0.0226 0.0229  131 ILE   B O   
5898 C CB  . ILE   B 131 ? 0.1909 0.2138 0.2893 0.0230  -0.0242 0.0257  131 ILE   B CB  
5899 C CG1 . ILE   B 131 ? 0.1943 0.2276 0.3056 0.0007  -0.0134 0.0266  131 ILE   B CG1 
5900 C CG2 . ILE   B 131 ? 0.1928 0.2320 0.3166 0.0307  -0.0196 0.0196  131 ILE   B CG2 
5901 C CD1 . ILE   B 131 ? 0.2072 0.2413 0.3218 -0.0151 -0.0149 0.0282  131 ILE   B CD1 
5913 N N   . PHE   B 132 ? 0.1812 0.1536 0.2035 0.0153  0.0055  0.0218  132 PHE   B N   
5914 C CA  . PHE   B 132 ? 0.1942 0.1521 0.1990 0.0107  0.0242  0.0162  132 PHE   B CA  
5915 C C   . PHE   B 132 ? 0.2127 0.1678 0.2177 0.0111  0.0294  0.0123  132 PHE   B C   
5916 O O   . PHE   B 132 ? 0.2283 0.1876 0.2430 0.0042  0.0487  0.0182  132 PHE   B O   
5917 C CB  . PHE   B 132 ? 0.1818 0.1537 0.1859 0.0116  0.0238  0.0204  132 PHE   B CB  
5918 C CG  . PHE   B 132 ? 0.1778 0.1585 0.1882 0.0167  0.0234  0.0178  132 PHE   B CG  
5919 C CD1 . PHE   B 132 ? 0.1818 0.1587 0.2203 0.0142  0.0283  0.0095  132 PHE   B CD1 
5920 C CD2 . PHE   B 132 ? 0.1793 0.1591 0.1667 0.0211  0.0219  0.0285  132 PHE   B CD2 
5921 C CE1 . PHE   B 132 ? 0.1850 0.1616 0.2325 0.0091  0.0216  0.0132  132 PHE   B CE1 
5922 C CE2 . PHE   B 132 ? 0.1846 0.1593 0.1757 0.0193  0.0156  0.0264  132 PHE   B CE2 
5923 C CZ  . PHE   B 132 ? 0.1850 0.1602 0.2159 0.0097  0.0044  0.0274  132 PHE   B CZ  
5933 N N   . GLY   B 133 ? 0.2101 0.1578 0.2105 0.0071  0.0178  0.0301  133 GLY   B N   
5934 C CA  . GLY   B 133 ? 0.2188 0.1670 0.2251 -0.0122 0.0153  0.0345  133 GLY   B CA  
5935 C C   . GLY   B 133 ? 0.2252 0.1751 0.2266 -0.0270 0.0221  0.0348  133 GLY   B C   
5936 O O   . GLY   B 133 ? 0.2486 0.1859 0.2604 -0.0355 0.0245  0.0523  133 GLY   B O   
5940 N N   . ALA   B 134 ? 0.2052 0.1760 0.2182 -0.0273 0.0189  0.0219  134 ALA   B N   
5941 C CA  . ALA   B 134 ? 0.1977 0.1728 0.2268 -0.0202 0.0258  0.0105  134 ALA   B CA  
5942 C C   . ALA   B 134 ? 0.2048 0.1644 0.2241 -0.0138 0.0233  0.0210  134 ALA   B C   
5943 O O   . ALA   B 134 ? 0.2106 0.1851 0.2422 -0.0028 0.0236  0.0122  134 ALA   B O   
5944 C CB  . ALA   B 134 ? 0.1964 0.1726 0.2440 -0.0104 0.0223  0.0033  134 ALA   B CB  
5950 N N   . ASP   B 135 ? 0.2192 0.1580 0.2235 -0.0191 0.0061  0.0338  135 ASP   B N   
5951 C CA  . ASP   B 135 ? 0.2329 0.1506 0.2455 -0.0156 -0.0078 0.0372  135 ASP   B CA  
5952 C C   . ASP   B 135 ? 0.2126 0.1432 0.2334 -0.0039 -0.0058 0.0247  135 ASP   B C   
5953 O O   . ASP   B 135 ? 0.2072 0.1369 0.2427 -0.0001 0.0003  0.0258  135 ASP   B O   
5954 C CB  . ASP   B 135 ? 0.2632 0.1596 0.2756 -0.0334 -0.0090 0.0378  135 ASP   B CB  
5955 C CG  . ASP   B 135 ? 0.2962 0.1615 0.3163 -0.0537 -0.0061 0.0299  135 ASP   B CG  
5956 O OD1 . ASP   B 135 ? 0.3097 0.1543 0.3120 -0.0365 -0.0154 0.0235  135 ASP   B OD1 
5957 O OD2 . ASP   B 135 ? 0.3196 0.1960 0.3721 -0.0661 -0.0038 0.0101  135 ASP   B OD2 
5962 N N   . PRO   B 136 ? 0.2029 0.1484 0.2423 0.0134  -0.0125 0.0236  136 PRO   B N   
5963 C CA  . PRO   B 136 ? 0.1852 0.1417 0.2469 0.0129  -0.0078 0.0123  136 PRO   B CA  
5964 C C   . PRO   B 136 ? 0.1657 0.1287 0.2412 0.0115  -0.0068 0.0060  136 PRO   B C   
5965 O O   . PRO   B 136 ? 0.1510 0.1290 0.2403 0.0105  0.0004  0.0113  136 PRO   B O   
5966 C CB  . PRO   B 136 ? 0.1946 0.1659 0.2588 0.0247  -0.0167 0.0025  136 PRO   B CB  
5967 C CG  . PRO   B 136 ? 0.2094 0.1710 0.2721 0.0344  -0.0094 0.0067  136 PRO   B CG  
5968 C CD  . PRO   B 136 ? 0.2088 0.1664 0.2651 0.0369  -0.0078 0.0167  136 PRO   B CD  
5976 N N   . ILE   B 137 ? 0.1729 0.1243 0.2516 0.0092  -0.0124 0.0025  137 ILE   B N   
5977 C CA  . ILE   B 137 ? 0.1839 0.1208 0.2654 -0.0050 0.0036  0.0012  137 ILE   B CA  
5978 C C   . ILE   B 137 ? 0.1751 0.1258 0.2518 -0.0086 0.0090  0.0077  137 ILE   B C   
5979 O O   . ILE   B 137 ? 0.1661 0.1248 0.2495 -0.0094 0.0034  0.0049  137 ILE   B O   
5980 C CB  . ILE   B 137 ? 0.2105 0.1275 0.3127 -0.0079 0.0013  -0.0027 137 ILE   B CB  
5981 C CG1 . ILE   B 137 ? 0.2366 0.1433 0.3697 0.0011  0.0093  -0.0146 137 ILE   B CG1 
5982 C CG2 . ILE   B 137 ? 0.2159 0.1345 0.3271 -0.0315 0.0010  0.0069  137 ILE   B CG2 
5983 C CD1 . ILE   B 137 ? 0.2598 0.1671 0.4085 0.0165  0.0041  -0.0055 137 ILE   B CD1 
5995 N N   . HIS   B 138 ? 0.1804 0.1203 0.2465 -0.0101 0.0159  0.0122  138 HIS   B N   
5996 C CA  . HIS   B 138 ? 0.1883 0.1338 0.2417 -0.0040 0.0238  0.0201  138 HIS   B CA  
5997 C C   . HIS   B 138 ? 0.1698 0.1294 0.2289 -0.0008 0.0224  0.0171  138 HIS   B C   
5998 O O   . HIS   B 138 ? 0.1637 0.1381 0.2529 0.0038  0.0266  0.0304  138 HIS   B O   
5999 C CB  . HIS   B 138 ? 0.2084 0.1455 0.2554 -0.0065 0.0383  0.0175  138 HIS   B CB  
6000 C CG  . HIS   B 138 ? 0.2274 0.1593 0.2630 -0.0073 0.0555  0.0342  138 HIS   B CG  
6001 N ND1 . HIS   B 138 ? 0.2362 0.1766 0.2922 -0.0032 0.0636  0.0218  138 HIS   B ND1 
6002 C CD2 . HIS   B 138 ? 0.2420 0.1724 0.2616 -0.0048 0.0595  0.0245  138 HIS   B CD2 
6003 C CE1 . HIS   B 138 ? 0.2393 0.1756 0.2881 -0.0054 0.0670  0.0252  138 HIS   B CE1 
6004 N NE2 . HIS   B 138 ? 0.2483 0.1675 0.2691 0.0000  0.0673  0.0209  138 HIS   B NE2 
6012 N N   . SER   B 139 ? 0.1702 0.1197 0.2261 0.0042  0.0218  0.0097  139 SER   B N   
6013 C CA  . SER   B 139 ? 0.1637 0.1152 0.2141 0.0008  0.0184  0.0017  139 SER   B CA  
6014 C C   . SER   B 139 ? 0.1404 0.1101 0.2124 -0.0002 0.0067  0.0040  139 SER   B C   
6015 O O   . SER   B 139 ? 0.1433 0.1123 0.2175 0.0006  -0.0045 0.0090  139 SER   B O   
6016 C CB  . SER   B 139 ? 0.1711 0.1178 0.2197 -0.0036 0.0012  0.0034  139 SER   B CB  
6017 O OG  . SER   B 139 ? 0.1704 0.1185 0.2338 -0.0032 -0.0110 0.0111  139 SER   B OG  
6023 N N   . LEU   B 140 ? 0.1396 0.1038 0.2104 -0.0035 0.0095  -0.0041 140 LEU   B N   
6024 C CA  . LEU   B 140 ? 0.1340 0.1072 0.2085 -0.0010 0.0081  0.0027  140 LEU   B CA  
6025 C C   . LEU   B 140 ? 0.1342 0.1066 0.2239 -0.0018 -0.0000 -0.0066 140 LEU   B C   
6026 O O   . LEU   B 140 ? 0.1323 0.1154 0.2222 -0.0010 -0.0027 -0.0008 140 LEU   B O   
6027 C CB  . LEU   B 140 ? 0.1339 0.1093 0.2227 -0.0109 0.0129  -0.0043 140 LEU   B CB  
6028 C CG  . LEU   B 140 ? 0.1457 0.1159 0.2116 -0.0153 0.0010  0.0004  140 LEU   B CG  
6029 C CD1 . LEU   B 140 ? 0.1560 0.1244 0.2213 -0.0148 0.0008  -0.0006 140 LEU   B CD1 
6030 C CD2 . LEU   B 140 ? 0.1665 0.1281 0.2128 -0.0134 -0.0038 -0.0117 140 LEU   B CD2 
6042 N N   . ARG   B 141 ? 0.1300 0.1077 0.2343 -0.0069 0.0068  -0.0053 141 ARG   B N   
6043 C CA  . ARG   B 141 ? 0.1341 0.1129 0.2700 -0.0133 0.0213  -0.0044 141 ARG   B CA  
6044 C C   . ARG   B 141 ? 0.1296 0.1166 0.2458 -0.0123 0.0095  -0.0028 141 ARG   B C   
6045 O O   . ARG   B 141 ? 0.1309 0.1209 0.2416 -0.0125 -0.0003 -0.0104 141 ARG   B O   
6046 C CB  . ARG   B 141 ? 0.1550 0.1257 0.3061 -0.0135 0.0306  0.0016  141 ARG   B CB  
6047 C CG  . ARG   B 141 ? 0.1871 0.1540 0.3234 -0.0167 0.0384  0.0035  141 ARG   B CG  
6048 C CD  . ARG   B 141 ? 0.2301 0.1773 0.3283 -0.0150 0.0284  -0.0074 141 ARG   B CD  
6049 N NE  . ARG   B 141 ? 0.2573 0.1752 0.3258 -0.0381 0.0321  -0.0150 141 ARG   B NE  
6050 C CZ  . ARG   B 141 ? 0.2752 0.1624 0.3159 -0.0348 0.0432  -0.0255 141 ARG   B CZ  
6051 N NH1 . ARG   B 141 ? 0.2874 0.1521 0.3083 -0.0376 0.0403  -0.0298 141 ARG   B NH1 
6052 N NH2 . ARG   B 141 ? 0.2839 0.1678 0.3215 -0.0211 0.0382  -0.0230 141 ARG   B NH2 
6066 N N   . VAL   B 142 ? 0.1355 0.1117 0.2344 -0.0047 0.0104  -0.0032 142 VAL   B N   
6067 C CA  . VAL   B 142 ? 0.1333 0.1135 0.2294 -0.0028 0.0141  -0.0083 142 VAL   B CA  
6068 C C   . VAL   B 142 ? 0.1278 0.1097 0.2276 0.0029  0.0069  -0.0039 142 VAL   B C   
6069 O O   . VAL   B 142 ? 0.1345 0.1129 0.2429 0.0006  0.0097  0.0000  142 VAL   B O   
6070 C CB  . VAL   B 142 ? 0.1465 0.1228 0.2351 0.0030  0.0192  0.0076  142 VAL   B CB  
6071 C CG1 . VAL   B 142 ? 0.1474 0.1249 0.2346 0.0084  0.0165  0.0019  142 VAL   B CG1 
6072 C CG2 . VAL   B 142 ? 0.1669 0.1267 0.2432 0.0043  0.0180  0.0099  142 VAL   B CG2 
6082 N N   . CYS   B 143 ? 0.1260 0.1112 0.2086 0.0024  0.0025  0.0027  143 CYS   B N   
6083 C CA  . CYS   B 143 ? 0.1259 0.1120 0.2136 -0.0045 -0.0008 0.0047  143 CYS   B CA  
6084 C C   . CYS   B 143 ? 0.1212 0.1124 0.2110 -0.0044 0.0038  0.0014  143 CYS   B C   
6085 O O   . CYS   B 143 ? 0.1286 0.1202 0.2157 -0.0050 -0.0003 0.0024  143 CYS   B O   
6086 C CB  . CYS   B 143 ? 0.1298 0.1248 0.2165 -0.0075 -0.0023 -0.0048 143 CYS   B CB  
6087 S SG  . CYS   B 143 ? 0.1353 0.1405 0.2077 -0.0049 0.0040  0.0004  143 CYS   B SG  
6093 N N   . VAL   B 144 ? 0.1269 0.1135 0.2201 -0.0058 0.0031  -0.0108 144 VAL   B N   
6094 C CA  . VAL   B 144 ? 0.1315 0.1278 0.2420 -0.0137 -0.0073 -0.0189 144 VAL   B CA  
6095 C C   . VAL   B 144 ? 0.1284 0.1265 0.2408 -0.0057 -0.0091 -0.0034 144 VAL   B C   
6096 O O   . VAL   B 144 ? 0.1433 0.1429 0.2598 0.0036  -0.0051 0.0131  144 VAL   B O   
6097 C CB  . VAL   B 144 ? 0.1547 0.1420 0.3041 -0.0128 -0.0150 -0.0311 144 VAL   B CB  
6098 C CG1 . VAL   B 144 ? 0.1754 0.1853 0.3378 -0.0073 -0.0276 -0.0302 144 VAL   B CG1 
6099 C CG2 . VAL   B 144 ? 0.1691 0.1397 0.2952 -0.0017 -0.0315 -0.0387 144 VAL   B CG2 
6109 N N   . ASP   B 145 ? 0.1315 0.1226 0.2518 -0.0039 -0.0064 -0.0121 145 ASP   B N   
6110 C CA  . ASP   B 145 ? 0.1307 0.1301 0.2777 -0.0044 0.0045  -0.0084 145 ASP   B CA  
6111 C C   . ASP   B 145 ? 0.1277 0.1282 0.2637 -0.0019 0.0076  -0.0073 145 ASP   B C   
6112 O O   . ASP   B 145 ? 0.1303 0.1400 0.3199 -0.0058 0.0117  -0.0243 145 ASP   B O   
6113 C CB  . ASP   B 145 ? 0.1463 0.1339 0.3209 -0.0147 0.0220  -0.0045 145 ASP   B CB  
6114 C CG  . ASP   B 145 ? 0.1589 0.1364 0.3703 -0.0245 0.0336  -0.0004 145 ASP   B CG  
6115 O OD1 . ASP   B 145 ? 0.1633 0.1407 0.3848 -0.0245 -0.0082 -0.0136 145 ASP   B OD1 
6116 O OD2 . ASP   B 145 ? 0.1869 0.1455 0.4126 -0.0283 0.0569  0.0058  145 ASP   B OD2 
6121 N N   . THR   B 146 ? 0.1207 0.1193 0.2229 -0.0091 0.0021  0.0038  146 THR   B N   
6122 C CA  . THR   B 146 ? 0.1258 0.1140 0.2076 -0.0049 0.0090  -0.0038 146 THR   B CA  
6123 C C   . THR   B 146 ? 0.1254 0.1135 0.1988 -0.0024 -0.0008 -0.0003 146 THR   B C   
6124 O O   . THR   B 146 ? 0.1333 0.1174 0.2117 -0.0009 0.0015  -0.0005 146 THR   B O   
6125 C CB  . THR   B 146 ? 0.1351 0.1184 0.2128 -0.0035 0.0129  -0.0001 146 THR   B CB  
6126 O OG1 . THR   B 146 ? 0.1364 0.1175 0.2120 -0.0029 0.0108  0.0079  146 THR   B OG1 
6127 C CG2 . THR   B 146 ? 0.1415 0.1261 0.2076 -0.0029 0.0085  0.0010  146 THR   B CG2 
6135 N N   . VAL   B 147 ? 0.1321 0.1125 0.1889 0.0005  0.0098  0.0023  147 VAL   B N   
6136 C CA  . VAL   B 147 ? 0.1315 0.1103 0.1851 -0.0073 -0.0016 0.0027  147 VAL   B CA  
6137 C C   . VAL   B 147 ? 0.1247 0.1152 0.1990 -0.0161 -0.0077 -0.0055 147 VAL   B C   
6138 O O   . VAL   B 147 ? 0.1378 0.1263 0.2014 -0.0165 -0.0233 -0.0097 147 VAL   B O   
6139 C CB  . VAL   B 147 ? 0.1344 0.1252 0.1825 -0.0068 -0.0112 0.0005  147 VAL   B CB  
6140 C CG1 . VAL   B 147 ? 0.1324 0.1380 0.1801 -0.0105 -0.0057 0.0077  147 VAL   B CG1 
6141 C CG2 . VAL   B 147 ? 0.1384 0.1260 0.1840 -0.0119 -0.0074 -0.0025 147 VAL   B CG2 
6151 N N   . ARG   B 148 ? 0.1297 0.1160 0.1910 -0.0085 -0.0149 -0.0076 148 ARG   B N   
6152 C CA  . ARG   B 148 ? 0.1329 0.1283 0.1887 -0.0093 -0.0260 -0.0087 148 ARG   B CA  
6153 C C   . ARG   B 148 ? 0.1370 0.1350 0.1747 -0.0075 -0.0213 -0.0032 148 ARG   B C   
6154 O O   . ARG   B 148 ? 0.1531 0.1652 0.1797 -0.0216 -0.0330 -0.0001 148 ARG   B O   
6155 C CB  . ARG   B 148 ? 0.1333 0.1392 0.1888 -0.0010 -0.0244 -0.0152 148 ARG   B CB  
6156 C CG  . ARG   B 148 ? 0.1362 0.1549 0.1996 -0.0104 -0.0163 -0.0274 148 ARG   B CG  
6157 C CD  . ARG   B 148 ? 0.1434 0.1675 0.2093 0.0055  -0.0192 -0.0280 148 ARG   B CD  
6158 N NE  . ARG   B 148 ? 0.1511 0.1643 0.2048 0.0224  -0.0195 -0.0270 148 ARG   B NE  
6159 C CZ  . ARG   B 148 ? 0.1391 0.1560 0.1946 0.0141  -0.0138 -0.0190 148 ARG   B CZ  
6160 N NH1 . ARG   B 148 ? 0.1379 0.1572 0.1896 0.0020  0.0030  -0.0072 148 ARG   B NH1 
6161 N NH2 . ARG   B 148 ? 0.1598 0.1473 0.1891 0.0196  -0.0065 -0.0137 148 ARG   B NH2 
6175 N N   . THR   B 149 ? 0.1427 0.1280 0.1719 -0.0111 -0.0259 0.0020  149 THR   B N   
6176 C CA  . THR   B 149 ? 0.1430 0.1331 0.1693 -0.0115 -0.0224 0.0106  149 THR   B CA  
6177 C C   . THR   B 149 ? 0.1434 0.1294 0.1562 -0.0134 -0.0303 0.0069  149 THR   B C   
6178 O O   . THR   B 149 ? 0.1506 0.1298 0.1707 -0.0216 -0.0117 0.0012  149 THR   B O   
6179 C CB  . THR   B 149 ? 0.1470 0.1331 0.1770 -0.0157 -0.0228 0.0003  149 THR   B CB  
6180 O OG1 . THR   B 149 ? 0.1472 0.1359 0.1684 -0.0212 -0.0207 -0.0045 149 THR   B OG1 
6181 C CG2 . THR   B 149 ? 0.1506 0.1315 0.1894 -0.0072 -0.0119 -0.0017 149 THR   B CG2 
6189 N N   . ASN   B 150 ? 0.1489 0.1267 0.1658 -0.0153 -0.0248 -0.0008 150 ASN   B N   
6190 C CA  . ASN   B 150 ? 0.1582 0.1405 0.1601 -0.0132 -0.0237 -0.0072 150 ASN   B CA  
6191 C C   . ASN   B 150 ? 0.1457 0.1350 0.1690 -0.0120 -0.0231 -0.0057 150 ASN   B C   
6192 O O   . ASN   B 150 ? 0.1546 0.1315 0.1915 -0.0238 -0.0415 -0.0057 150 ASN   B O   
6193 C CB  . ASN   B 150 ? 0.1753 0.1732 0.1663 -0.0146 -0.0335 0.0030  150 ASN   B CB  
6194 C CG  . ASN   B 150 ? 0.2004 0.2124 0.2019 -0.0178 -0.0344 0.0228  150 ASN   B CG  
6195 O OD1 . ASN   B 150 ? 0.2082 0.2304 0.2233 -0.0293 -0.0491 0.0198  150 ASN   B OD1 
6196 N ND2 . ASN   B 150 ? 0.2125 0.2282 0.2238 -0.0076 -0.0333 0.0519  150 ASN   B ND2 
6203 N N   . VAL   B 151 ? 0.1340 0.1338 0.1625 -0.0174 -0.0214 -0.0061 151 VAL   B N   
6204 C CA  . VAL   B 151 ? 0.1335 0.1389 0.1622 -0.0170 -0.0144 -0.0047 151 VAL   B CA  
6205 C C   . VAL   B 151 ? 0.1381 0.1290 0.1574 -0.0248 -0.0156 -0.0008 151 VAL   B C   
6206 O O   . VAL   B 151 ? 0.1503 0.1344 0.1772 -0.0261 -0.0120 -0.0109 151 VAL   B O   
6207 C CB  . VAL   B 151 ? 0.1550 0.1541 0.1787 -0.0057 -0.0116 -0.0060 151 VAL   B CB  
6208 C CG1 . VAL   B 151 ? 0.1666 0.1530 0.2006 -0.0170 0.0070  -0.0145 151 VAL   B CG1 
6209 C CG2 . VAL   B 151 ? 0.1721 0.1697 0.1749 0.0044  -0.0109 -0.0007 151 VAL   B CG2 
6219 N N   . TYR   B 152 ? 0.1363 0.1180 0.1576 -0.0206 -0.0120 -0.0069 152 TYR   B N   
6220 C CA  . TYR   B 152 ? 0.1395 0.1323 0.1477 -0.0254 -0.0086 -0.0109 152 TYR   B CA  
6221 C C   . TYR   B 152 ? 0.1375 0.1193 0.1466 -0.0146 -0.0084 -0.0078 152 TYR   B C   
6222 O O   . TYR   B 152 ? 0.1451 0.1234 0.1529 -0.0235 -0.0099 -0.0056 152 TYR   B O   
6223 C CB  . TYR   B 152 ? 0.1513 0.1452 0.1581 -0.0207 -0.0063 0.0065  152 TYR   B CB  
6224 C CG  . TYR   B 152 ? 0.1654 0.1533 0.1510 -0.0317 -0.0151 0.0065  152 TYR   B CG  
6225 C CD1 . TYR   B 152 ? 0.1771 0.1663 0.1432 -0.0269 -0.0181 0.0103  152 TYR   B CD1 
6226 C CD2 . TYR   B 152 ? 0.1817 0.1674 0.1640 -0.0305 -0.0071 -0.0003 152 TYR   B CD2 
6227 C CE1 . TYR   B 152 ? 0.1918 0.1802 0.1571 -0.0239 -0.0223 0.0245  152 TYR   B CE1 
6228 C CE2 . TYR   B 152 ? 0.1938 0.1899 0.1681 -0.0302 -0.0097 -0.0078 152 TYR   B CE2 
6229 C CZ  . TYR   B 152 ? 0.1987 0.2018 0.1502 -0.0275 -0.0396 0.0171  152 TYR   B CZ  
6230 O OH  . TYR   B 152 ? 0.2201 0.2377 0.1899 -0.0175 -0.0371 0.0192  152 TYR   B OH  
6240 N N   . LEU   B 153 ? 0.1401 0.1170 0.1561 -0.0240 -0.0158 -0.0115 153 LEU   B N   
6241 C CA  . LEU   B 153 ? 0.1465 0.1151 0.1508 -0.0228 -0.0065 -0.0106 153 LEU   B CA  
6242 C C   . LEU   B 153 ? 0.1441 0.1126 0.1729 -0.0224 -0.0062 -0.0170 153 LEU   B C   
6243 O O   . LEU   B 153 ? 0.1516 0.1351 0.1843 -0.0103 -0.0117 -0.0311 153 LEU   B O   
6244 C CB  . LEU   B 153 ? 0.1464 0.1111 0.1657 -0.0179 -0.0044 -0.0029 153 LEU   B CB  
6245 C CG  . LEU   B 153 ? 0.1436 0.1262 0.1837 -0.0195 -0.0002 0.0022  153 LEU   B CG  
6246 C CD1 . LEU   B 153 ? 0.1510 0.1421 0.1915 -0.0209 0.0054  0.0028  153 LEU   B CD1 
6247 C CD2 . LEU   B 153 ? 0.1485 0.1392 0.1945 -0.0231 0.0086  0.0012  153 LEU   B CD2 
6259 N N   . ALA   B 154 ? 0.1378 0.1185 0.1720 -0.0079 -0.0123 -0.0131 154 ALA   B N   
6260 C CA  . ALA   B 154 ? 0.1493 0.1307 0.1932 -0.0035 -0.0119 -0.0210 154 ALA   B CA  
6261 C C   . ALA   B 154 ? 0.1622 0.1279 0.1905 0.0032  -0.0183 -0.0294 154 ALA   B C   
6262 O O   . ALA   B 154 ? 0.1980 0.1355 0.2109 0.0030  -0.0014 -0.0182 154 ALA   B O   
6263 C CB  . ALA   B 154 ? 0.1466 0.1461 0.2143 -0.0051 -0.0056 -0.0265 154 ALA   B CB  
6269 N N   . VAL   B 155 ? 0.1359 0.1210 0.2013 -0.0036 0.0038  -0.0192 155 VAL   B N   
6270 C CA  . VAL   B 155 ? 0.1324 0.1232 0.2154 -0.0016 -0.0120 -0.0069 155 VAL   B CA  
6271 C C   . VAL   B 155 ? 0.1384 0.1258 0.2090 0.0006  -0.0093 -0.0098 155 VAL   B C   
6272 O O   . VAL   B 155 ? 0.1552 0.1438 0.2361 0.0040  -0.0054 -0.0308 155 VAL   B O   
6273 C CB  . VAL   B 155 ? 0.1390 0.1363 0.2378 -0.0046 -0.0177 0.0029  155 VAL   B CB  
6274 C CG1 . VAL   B 155 ? 0.1446 0.1324 0.2419 -0.0123 -0.0102 -0.0074 155 VAL   B CG1 
6275 C CG2 . VAL   B 155 ? 0.1343 0.1474 0.2710 -0.0036 -0.0175 0.0267  155 VAL   B CG2 
6285 N N   . PHE   B 156 ? 0.1267 0.1339 0.2221 0.0076  -0.0074 -0.0070 156 PHE   B N   
6286 C CA  . PHE   B 156 ? 0.1287 0.1406 0.2551 0.0075  -0.0126 -0.0104 156 PHE   B CA  
6287 C C   . PHE   B 156 ? 0.1232 0.1475 0.2787 0.0117  -0.0167 -0.0313 156 PHE   B C   
6288 O O   . PHE   B 156 ? 0.1481 0.1715 0.3018 0.0222  0.0032  -0.0409 156 PHE   B O   
6289 C CB  . PHE   B 156 ? 0.1348 0.1339 0.2573 0.0011  -0.0189 -0.0150 156 PHE   B CB  
6290 C CG  . PHE   B 156 ? 0.1357 0.1468 0.2627 -0.0033 -0.0138 0.0037  156 PHE   B CG  
6291 C CD1 . PHE   B 156 ? 0.1370 0.1766 0.2945 0.0043  -0.0037 0.0424  156 PHE   B CD1 
6292 C CD2 . PHE   B 156 ? 0.1436 0.1571 0.2624 0.0052  -0.0243 0.0121  156 PHE   B CD2 
6293 C CE1 . PHE   B 156 ? 0.1433 0.1954 0.3108 0.0065  -0.0039 0.0456  156 PHE   B CE1 
6294 C CE2 . PHE   B 156 ? 0.1499 0.1791 0.2855 0.0089  -0.0243 0.0214  156 PHE   B CE2 
6295 C CZ  . PHE   B 156 ? 0.1388 0.1919 0.3077 0.0128  -0.0219 0.0358  156 PHE   B CZ  
6305 N N   . ASP   B 157 ? 0.1290 0.1372 0.3050 0.0116  -0.0159 -0.0204 157 ASP   B N   
6306 C CA  . ASP   B 157 ? 0.1395 0.1425 0.3353 0.0070  -0.0198 -0.0263 157 ASP   B CA  
6307 C C   . ASP   B 157 ? 0.1405 0.1397 0.3448 0.0112  -0.0190 -0.0428 157 ASP   B C   
6308 O O   . ASP   B 157 ? 0.1313 0.1404 0.3306 0.0102  -0.0223 -0.0376 157 ASP   B O   
6309 C CB  . ASP   B 157 ? 0.1703 0.1647 0.3553 0.0049  -0.0433 -0.0037 157 ASP   B CB  
6310 C CG  . ASP   B 157 ? 0.2088 0.1748 0.3822 -0.0029 -0.0297 -0.0068 157 ASP   B CG  
6311 O OD1 . ASP   B 157 ? 0.2209 0.1743 0.3968 0.0042  -0.0226 -0.0034 157 ASP   B OD1 
6312 O OD2 . ASP   B 157 ? 0.2348 0.1916 0.4093 -0.0057 -0.0075 -0.0099 157 ASP   B OD2 
6317 N N   . LYS   B 158 ? 0.1457 0.1650 0.3585 0.0092  -0.0033 -0.0623 158 LYS   B N   
6318 C CA  . LYS   B 158 ? 0.1567 0.1788 0.3741 0.0067  0.0083  -0.0805 158 LYS   B CA  
6319 C C   . LYS   B 158 ? 0.1560 0.1646 0.3787 0.0098  0.0001  -0.0773 158 LYS   B C   
6320 O O   . LYS   B 158 ? 0.1621 0.1695 0.3820 -0.0039 -0.0010 -0.0805 158 LYS   B O   
6321 C CB  . LYS   B 158 ? 0.1770 0.2160 0.3798 0.0092  0.0121  -0.1029 158 LYS   B CB  
6322 C CG  . LYS   B 158 ? 0.2110 0.2608 0.3857 0.0148  0.0179  -0.1109 158 LYS   B CG  
6323 C CD  . LYS   B 158 ? 0.2434 0.3124 0.3966 0.0081  0.0177  -0.1034 158 LYS   B CD  
6324 C CE  . LYS   B 158 ? 0.2626 0.3385 0.4058 0.0088  0.0167  -0.1012 158 LYS   B CE  
6325 N NZ  . LYS   B 158 ? 0.2596 0.3560 0.3998 0.0064  0.0163  -0.1042 158 LYS   B NZ  
6339 N N   . ASN   B 159 ? 0.1611 0.1531 0.3948 0.0113  -0.0156 -0.0628 159 ASN   B N   
6340 C CA  . ASN   B 159 ? 0.1718 0.1491 0.4123 0.0196  -0.0357 -0.0439 159 ASN   B CA  
6341 C C   . ASN   B 159 ? 0.1597 0.1384 0.4034 0.0114  -0.0496 -0.0299 159 ASN   B C   
6342 O O   . ASN   B 159 ? 0.1638 0.1344 0.4118 -0.0047 -0.0526 -0.0204 159 ASN   B O   
6343 C CB  . ASN   B 159 ? 0.1925 0.1662 0.4475 0.0300  -0.0485 -0.0371 159 ASN   B CB  
6344 C CG  . ASN   B 159 ? 0.2213 0.1849 0.4809 0.0369  -0.0530 -0.0525 159 ASN   B CG  
6345 O OD1 . ASN   B 159 ? 0.2371 0.1996 0.4918 0.0384  -0.0525 -0.0633 159 ASN   B OD1 
6346 N ND2 . ASN   B 159 ? 0.2279 0.1976 0.4976 0.0462  -0.0533 -0.0458 159 ASN   B ND2 
6353 N N   . LEU   B 160 ? 0.1438 0.1363 0.3776 0.0025  -0.0488 -0.0265 160 LEU   B N   
6354 C CA  . LEU   B 160 ? 0.1431 0.1402 0.3277 0.0120  -0.0390 -0.0130 160 LEU   B CA  
6355 C C   . LEU   B 160 ? 0.1387 0.1305 0.3030 -0.0003 -0.0279 -0.0302 160 LEU   B C   
6356 O O   . LEU   B 160 ? 0.1315 0.1402 0.2890 -0.0021 -0.0283 -0.0232 160 LEU   B O   
6357 C CB  . LEU   B 160 ? 0.1423 0.1536 0.3112 0.0037  -0.0377 -0.0075 160 LEU   B CB  
6358 C CG  . LEU   B 160 ? 0.1455 0.1655 0.2859 0.0101  -0.0290 -0.0056 160 LEU   B CG  
6359 C CD1 . LEU   B 160 ? 0.1629 0.1813 0.2847 0.0014  -0.0196 -0.0083 160 LEU   B CD1 
6360 C CD2 . LEU   B 160 ? 0.1459 0.1650 0.2797 0.0141  -0.0271 -0.0132 160 LEU   B CD2 
6372 N N   . TYR   B 161 ? 0.1348 0.1397 0.3058 -0.0064 -0.0081 -0.0350 161 TYR   B N   
6373 C CA  . TYR   B 161 ? 0.1386 0.1418 0.2960 -0.0134 0.0072  -0.0509 161 TYR   B CA  
6374 C C   . TYR   B 161 ? 0.1466 0.1401 0.2865 -0.0089 0.0119  -0.0458 161 TYR   B C   
6375 O O   . TYR   B 161 ? 0.1516 0.1396 0.2753 -0.0128 -0.0009 -0.0359 161 TYR   B O   
6376 C CB  . TYR   B 161 ? 0.1536 0.1529 0.2980 -0.0179 0.0231  -0.0543 161 TYR   B CB  
6377 C CG  . TYR   B 161 ? 0.1796 0.1524 0.2924 -0.0251 0.0367  -0.0610 161 TYR   B CG  
6378 C CD1 . TYR   B 161 ? 0.1879 0.1486 0.2917 -0.0339 0.0403  -0.0533 161 TYR   B CD1 
6379 C CD2 . TYR   B 161 ? 0.2058 0.1591 0.2942 -0.0264 0.0334  -0.0562 161 TYR   B CD2 
6380 C CE1 . TYR   B 161 ? 0.2074 0.1701 0.3029 -0.0380 0.0335  -0.0481 161 TYR   B CE1 
6381 C CE2 . TYR   B 161 ? 0.2267 0.1798 0.3053 -0.0313 0.0349  -0.0483 161 TYR   B CE2 
6382 C CZ  . TYR   B 161 ? 0.2248 0.1841 0.3051 -0.0420 0.0304  -0.0368 161 TYR   B CZ  
6383 O OH  . TYR   B 161 ? 0.2515 0.2076 0.3194 -0.0412 0.0283  -0.0333 161 TYR   B OH  
6393 N N   . ASP   B 162 ? 0.1538 0.1378 0.3052 -0.0072 -0.0011 -0.0529 162 ASP   B N   
6394 C CA  . ASP   B 162 ? 0.1638 0.1433 0.3053 -0.0029 -0.0032 -0.0524 162 ASP   B CA  
6395 C C   . ASP   B 162 ? 0.1609 0.1369 0.2922 -0.0075 -0.0104 -0.0406 162 ASP   B C   
6396 O O   . ASP   B 162 ? 0.1630 0.1434 0.2924 -0.0116 -0.0256 -0.0313 162 ASP   B O   
6397 C CB  . ASP   B 162 ? 0.1833 0.1653 0.3279 0.0041  -0.0119 -0.0704 162 ASP   B CB  
6398 C CG  . ASP   B 162 ? 0.1850 0.1896 0.3533 0.0130  -0.0031 -0.0817 162 ASP   B CG  
6399 O OD1 . ASP   B 162 ? 0.1841 0.2139 0.3428 0.0128  0.0106  -0.0775 162 ASP   B OD1 
6400 O OD2 . ASP   B 162 ? 0.2039 0.2099 0.3884 0.0247  0.0070  -0.0758 162 ASP   B OD2 
6405 N N   A LYS   B 163 ? 0.1566 0.1167 0.2846 -0.0086 -0.0221 -0.0248 163 LYS   B N   
6406 N N   B LYS   B 163 ? 0.1673 0.1463 0.2881 -0.0083 -0.0149 -0.0259 163 LYS   B N   
6407 C CA  A LYS   B 163 ? 0.1652 0.1256 0.2795 -0.0213 -0.0247 -0.0038 163 LYS   B CA  
6408 C CA  B LYS   B 163 ? 0.1761 0.1622 0.2879 -0.0110 -0.0149 -0.0113 163 LYS   B CA  
6409 C C   A LYS   B 163 ? 0.1404 0.1270 0.2684 -0.0215 -0.0188 -0.0005 163 LYS   B C   
6410 C C   B LYS   B 163 ? 0.1517 0.1442 0.2708 -0.0136 -0.0153 -0.0052 163 LYS   B C   
6411 O O   A LYS   B 163 ? 0.1379 0.1381 0.2884 -0.0230 -0.0170 -0.0027 163 LYS   B O   
6412 O O   B LYS   B 163 ? 0.1509 0.1477 0.2770 -0.0142 -0.0169 -0.0037 163 LYS   B O   
6413 C CB  A LYS   B 163 ? 0.2049 0.1499 0.3113 -0.0159 -0.0307 0.0083  163 LYS   B CB  
6414 C CB  B LYS   B 163 ? 0.2083 0.1973 0.3171 -0.0084 -0.0159 -0.0046 163 LYS   B CB  
6415 C CG  A LYS   B 163 ? 0.2670 0.2177 0.3621 -0.0196 -0.0145 0.0184  163 LYS   B CG  
6416 C CG  B LYS   B 163 ? 0.2427 0.2348 0.3525 -0.0079 -0.0106 0.0009  163 LYS   B CG  
6417 C CD  A LYS   B 163 ? 0.3233 0.2565 0.4109 -0.0290 -0.0080 0.0113  163 LYS   B CD  
6418 C CD  B LYS   B 163 ? 0.2699 0.2624 0.3874 -0.0097 -0.0081 0.0009  163 LYS   B CD  
6419 C CE  A LYS   B 163 ? 0.3581 0.2860 0.4442 -0.0349 -0.0013 0.0108  163 LYS   B CE  
6420 C CE  B LYS   B 163 ? 0.2916 0.2867 0.4149 -0.0115 -0.0054 0.0012  163 LYS   B CE  
6421 N NZ  A LYS   B 163 ? 0.3742 0.3097 0.4669 -0.0374 0.0024  0.0084  163 LYS   B NZ  
6422 N NZ  B LYS   B 163 ? 0.3034 0.2955 0.4322 -0.0120 -0.0037 0.0003  163 LYS   B NZ  
6449 N N   . LEU   B 164 ? 0.1327 0.1252 0.2530 -0.0135 -0.0152 -0.0028 164 LEU   B N   
6450 C CA  . LEU   B 164 ? 0.1283 0.1272 0.2380 -0.0097 -0.0253 0.0010  164 LEU   B CA  
6451 C C   . LEU   B 164 ? 0.1387 0.1311 0.2468 -0.0120 -0.0287 -0.0036 164 LEU   B C   
6452 O O   . LEU   B 164 ? 0.1396 0.1454 0.2677 -0.0111 -0.0282 -0.0066 164 LEU   B O   
6453 C CB  . LEU   B 164 ? 0.1313 0.1232 0.2362 -0.0088 -0.0179 -0.0021 164 LEU   B CB  
6454 C CG  . LEU   B 164 ? 0.1405 0.1354 0.2376 -0.0074 -0.0107 -0.0041 164 LEU   B CG  
6455 C CD1 . LEU   B 164 ? 0.1472 0.1369 0.2450 -0.0088 -0.0238 -0.0080 164 LEU   B CD1 
6456 C CD2 . LEU   B 164 ? 0.1561 0.1744 0.2542 -0.0000 0.0067  -0.0255 164 LEU   B CD2 
6469 N N   . VAL   B 165 ? 0.1646 0.1346 0.2613 -0.0139 -0.0294 -0.0156 165 VAL   B N   
6470 C CA  . VAL   B 165 ? 0.2013 0.1464 0.2638 -0.0200 -0.0417 -0.0154 165 VAL   B CA  
6471 C C   . VAL   B 165 ? 0.2221 0.1523 0.2897 -0.0321 -0.0730 -0.0151 165 VAL   B C   
6472 O O   . VAL   B 165 ? 0.2414 0.1663 0.2890 -0.0369 -0.0771 -0.0073 165 VAL   B O   
6473 C CB  . VAL   B 165 ? 0.2171 0.1639 0.2555 -0.0069 -0.0165 -0.0206 165 VAL   B CB  
6474 C CG1 . VAL   B 165 ? 0.2312 0.1719 0.2733 -0.0078 -0.0003 -0.0182 165 VAL   B CG1 
6475 C CG2 . VAL   B 165 ? 0.2074 0.1680 0.2529 -0.0066 -0.0137 -0.0118 165 VAL   B CG2 
6485 N N   . SER   B 166 ? 0.2298 0.1453 0.3235 -0.0291 -0.0796 -0.0307 166 SER   B N   
6486 C CA  . SER   B 166 ? 0.2309 0.1464 0.3737 -0.0337 -0.0787 -0.0374 166 SER   B CA  
6487 C C   . SER   B 166 ? 0.2166 0.1522 0.3899 -0.0371 -0.0756 -0.0193 166 SER   B C   
6488 O O   . SER   B 166 ? 0.2234 0.1799 0.4306 -0.0516 -0.0894 -0.0326 166 SER   B O   
6489 C CB  . SER   B 166 ? 0.2395 0.1558 0.4023 -0.0258 -0.0734 -0.0446 166 SER   B CB  
6490 O OG  . SER   B 166 ? 0.2279 0.1526 0.4224 -0.0188 -0.0744 -0.0219 166 SER   B OG  
6496 N N   . SER   B 167 ? 0.1937 0.1493 0.3622 -0.0359 -0.0742 0.0166  167 SER   B N   
6497 C CA  . SER   B 167 ? 0.1837 0.1562 0.3420 -0.0351 -0.0585 0.0219  167 SER   B CA  
6498 C C   . SER   B 167 ? 0.1772 0.1652 0.3281 -0.0456 -0.0592 0.0376  167 SER   B C   
6499 O O   . SER   B 167 ? 0.1840 0.1770 0.3232 -0.0519 -0.0455 0.0378  167 SER   B O   
6500 C CB  . SER   B 167 ? 0.1803 0.1652 0.3381 -0.0264 -0.0297 0.0243  167 SER   B CB  
6501 O OG  . SER   B 167 ? 0.1741 0.1736 0.3186 -0.0164 -0.0184 0.0219  167 SER   B OG  
6507 N N   . PHE   B 168 ? 0.1751 0.1610 0.3209 -0.0388 -0.0399 0.0465  168 PHE   B N   
6508 C CA  . PHE   B 168 ? 0.1821 0.1592 0.3018 -0.0441 -0.0322 0.0326  168 PHE   B CA  
6509 C C   . PHE   B 168 ? 0.1617 0.1521 0.2649 -0.0283 -0.0169 0.0161  168 PHE   B C   
6510 O O   . PHE   B 168 ? 0.1896 0.1437 0.2663 -0.0008 -0.0149 0.0013  168 PHE   B O   
6511 C CB  . PHE   B 168 ? 0.2003 0.1620 0.3031 -0.0467 -0.0435 0.0480  168 PHE   B CB  
6512 C CG  . PHE   B 168 ? 0.2273 0.1483 0.2929 -0.0458 -0.0505 0.0198  168 PHE   B CG  
6513 C CD1 . PHE   B 168 ? 0.2639 0.1513 0.2955 -0.0426 -0.0526 0.0115  168 PHE   B CD1 
6514 C CD2 . PHE   B 168 ? 0.2134 0.1424 0.2864 -0.0455 -0.0485 0.0209  168 PHE   B CD2 
6515 C CE1 . PHE   B 168 ? 0.2749 0.1636 0.2878 -0.0312 -0.0460 0.0109  168 PHE   B CE1 
6516 C CE2 . PHE   B 168 ? 0.2405 0.1506 0.2847 -0.0318 -0.0515 0.0117  168 PHE   B CE2 
6517 C CZ  . PHE   B 168 ? 0.2579 0.1519 0.2845 -0.0256 -0.0504 0.0190  168 PHE   B CZ  
6527 N N   . LEU   B 169 ? 0.1684 0.1733 0.2620 -0.0137 -0.0124 0.0018  169 LEU   B N   
6528 C CA  . LEU   B 169 ? 0.1963 0.1999 0.3048 -0.0143 -0.0123 -0.0256 169 LEU   B CA  
6529 C C   . LEU   B 169 ? 0.2196 0.2190 0.3580 0.0031  -0.0185 -0.0472 169 LEU   B C   
6530 O O   . LEU   B 169 ? 0.2417 0.2369 0.4057 0.0038  -0.0162 -0.0678 169 LEU   B O   
6531 C CB  . LEU   B 169 ? 0.2132 0.2372 0.3176 -0.0160 -0.0174 -0.0079 169 LEU   B CB  
6532 C CG  . LEU   B 169 ? 0.2534 0.2714 0.3569 -0.0038 -0.0146 -0.0028 169 LEU   B CG  
6533 C CD1 . LEU   B 169 ? 0.2684 0.2905 0.3663 -0.0028 -0.0220 0.0145  169 LEU   B CD1 
6534 C CD2 . LEU   B 169 ? 0.2513 0.2778 0.3617 0.0107  -0.0041 -0.0177 169 LEU   B CD2 
6535 O OXT . LEU   B 169 ? 0.2360 0.2340 0.3556 0.0276  -0.0103 -0.0476 169 LEU   B OXT 
6547 N N2  B A1A42 C .   ? 0.1203 0.1322 0.1437 -0.0109 -0.0060 0.0015  201 A1A42 A N2  
6548 C C3  B A1A42 C .   ? 0.1553 0.1440 0.1395 -0.0190 0.0176  0.0177  201 A1A42 A C3  
6549 C C6  B A1A42 C .   ? 0.1387 0.1236 0.1431 -0.0045 -0.0063 0.0215  201 A1A42 A C6  
6550 C C9  B A1A42 C .   ? 0.1173 0.1247 0.1181 0.0006  -0.0015 0.0092  201 A1A42 A C9  
6551 C C12 B A1A42 C .   ? 0.1049 0.1257 0.1274 -0.0205 -0.0037 -0.0000 201 A1A42 A C12 
6552 C C14 B A1A42 C .   ? 0.1390 0.1464 0.1519 -0.0025 -0.0194 0.0055  201 A1A42 A C14 
6553 C C1  B A1A42 C .   ? 0.1548 0.1497 0.1718 -0.0089 0.0208  0.0018  201 A1A42 A C1  
6554 C C10 B A1A42 C .   ? 0.1150 0.1198 0.1174 0.0005  0.0071  0.0098  201 A1A42 A C10 
6555 C C11 B A1A42 C .   ? 0.1145 0.1257 0.1258 -0.0031 0.0024  0.0075  201 A1A42 A C11 
6556 C C13 B A1A42 C .   ? 0.1409 0.1455 0.1533 -0.0047 -0.0139 0.0003  201 A1A42 A C13 
6557 C C15 B A1A42 C .   ? 0.1144 0.1282 0.1297 -0.0033 -0.0175 -0.0001 201 A1A42 A C15 
6558 C C16 B A1A42 C .   ? 0.1115 0.1297 0.1145 0.0036  -0.0091 0.0022  201 A1A42 A C16 
6559 C C2  B A1A42 C .   ? 0.1527 0.1418 0.1456 -0.0166 0.0180  0.0156  201 A1A42 A C2  
6560 C C4  B A1A42 C .   ? 0.1516 0.1385 0.1311 -0.0196 0.0099  0.0169  201 A1A42 A C4  
6561 C C5  B A1A42 C .   ? 0.1451 0.1289 0.1310 -0.0131 0.0040  0.0167  201 A1A42 A C5  
6562 C C7  B A1A42 C .   ? 0.1450 0.1302 0.1286 -0.0159 0.0106  0.0176  201 A1A42 A C7  
6563 C C8  B A1A42 C .   ? 0.1282 0.1241 0.1068 -0.0082 -0.0056 0.0192  201 A1A42 A C8  
6564 N N1  B A1A42 C .   ? 0.1370 0.1303 0.1219 -0.0128 0.0052  0.0205  201 A1A42 A N1  
6565 O O1  B A1A42 C .   ? 0.1387 0.1046 0.1424 0.0001  -0.0160 0.0253  201 A1A42 A O1  
6566 O O2  B A1A42 C .   ? 0.1367 0.1224 0.0979 -0.0204 -0.0055 0.0253  201 A1A42 A O2  
6567 O O3  B A1A42 C .   ? 0.1609 0.1626 0.1595 0.0018  -0.0179 -0.0009 201 A1A42 A O3  
6568 O O4  B A1A42 C .   ? 0.1273 0.1316 0.1413 -0.0046 -0.0297 0.0029  201 A1A42 A O4  
6569 O O5  B A1A42 C .   ? 0.1300 0.1296 0.1436 -0.0060 -0.0039 0.0275  201 A1A42 A O5  
6587 O O   . HOH   D .   ? 0.6110 0.4852 0.4019 0.2217  -0.1385 0.0640  301 HOH   A O   
6588 O O   . HOH   D .   ? 0.2071 0.2073 0.2480 -0.0217 -0.0173 0.0732  302 HOH   A O   
6589 O O   . HOH   D .   ? 0.3353 0.2083 0.3784 -0.0205 -0.0610 0.0582  303 HOH   A O   
6590 O O   . HOH   D .   ? 0.2443 0.1706 0.2489 0.0422  -0.0507 -0.0136 304 HOH   A O   
6591 O O   . HOH   D .   ? 0.4081 0.7595 0.4507 -0.1021 0.0658  0.0729  305 HOH   A O   
6592 O O   . HOH   D .   ? 0.1301 0.3603 0.2712 -0.0024 0.0105  0.0906  306 HOH   A O   
6593 O O   . HOH   D .   ? 0.6982 0.5209 0.5101 -0.1179 0.1685  0.2254  307 HOH   A O   
6594 O O   . HOH   D .   ? 0.2829 0.1929 0.2707 0.0188  -0.0406 0.0409  308 HOH   A O   
6595 O O   . HOH   D .   ? 0.2783 0.6847 0.5733 0.0184  -0.0858 0.2021  309 HOH   A O   
6596 O O   . HOH   D .   ? 0.2980 0.2298 0.4623 -0.0508 -0.1199 0.1039  310 HOH   A O   
6597 O O   . HOH   D .   ? 0.1874 0.1619 0.2188 0.0182  -0.0161 0.0294  311 HOH   A O   
6598 O O   . HOH   D .   ? 0.4565 0.3316 0.3480 -0.0307 -0.1137 -0.0158 312 HOH   A O   
6599 O O   . HOH   D .   ? 0.5304 0.3343 0.4518 -0.0664 0.1077  0.0943  313 HOH   A O   
6600 O O   . HOH   D .   ? 0.3165 0.3141 0.1638 -0.0454 0.0513  0.0356  314 HOH   A O   
6601 O O   A HOH   D .   ? 0.2806 0.4076 0.4755 -0.0622 0.1328  0.1428  315 HOH   A O   
6602 O O   . HOH   D .   ? 0.2061 0.1761 0.3612 -0.0388 0.0061  -0.0147 316 HOH   A O   
6603 O O   . HOH   D .   ? 0.5746 0.5289 0.5595 -0.0263 0.1355  0.0445  317 HOH   A O   
6604 O O   . HOH   D .   ? 0.5645 0.6157 0.4300 -0.1302 -0.1181 -0.0561 318 HOH   A O   
6605 O O   . HOH   D .   ? 0.4909 0.5502 0.5838 0.2021  0.1209  -0.0903 319 HOH   A O   
6606 O O   . HOH   D .   ? 0.3944 0.2894 0.2910 -0.1217 0.0106  0.0609  320 HOH   A O   
6607 O O   . HOH   D .   ? 0.4701 0.5205 0.2531 -0.0976 0.1093  0.0777  321 HOH   A O   
6608 O O   . HOH   D .   ? 0.8067 0.4996 0.3304 -0.0415 -0.0236 0.0702  322 HOH   A O   
6609 O O   . HOH   D .   ? 0.5543 0.1986 0.4699 0.0663  -0.0051 -0.0075 323 HOH   A O   
6610 O O   . HOH   D .   ? 0.2098 0.1888 0.3350 0.0301  -0.0988 -0.0696 324 HOH   A O   
6611 O O   . HOH   D .   ? 0.4763 0.2992 0.3722 -0.0826 0.2103  -0.0194 325 HOH   A O   
6612 O O   . HOH   D .   ? 0.2263 0.4511 0.4280 -0.0120 -0.0473 0.0997  326 HOH   A O   
6613 O O   B HOH   D .   ? 0.1691 0.1586 0.1427 0.0229  0.0105  0.0383  327 HOH   A O   
6614 O O   . HOH   D .   ? 0.4275 0.3316 0.4556 0.0212  0.1107  0.0115  328 HOH   A O   
6615 O O   . HOH   D .   ? 0.7128 0.4941 0.5423 -0.1285 -0.0246 0.2109  329 HOH   A O   
6616 O O   . HOH   D .   ? 0.1837 0.3141 0.3920 -0.0339 0.0376  -0.0777 330 HOH   A O   
6617 O O   . HOH   D .   ? 0.1624 0.3314 0.2771 0.0442  -0.0134 0.0100  331 HOH   A O   
6618 O O   . HOH   D .   ? 0.1486 0.1481 0.2233 -0.0193 0.0064  0.0036  332 HOH   A O   
6619 O O   . HOH   D .   ? 0.6052 0.5372 0.5173 0.0881  0.2544  -0.1397 333 HOH   A O   
6620 O O   . HOH   D .   ? 0.2869 0.2429 0.2344 0.0764  0.0214  0.0292  334 HOH   A O   
6621 O O   . HOH   D .   ? 0.6424 0.5995 0.4669 -0.0108 -0.1109 -0.0143 335 HOH   A O   
6622 O O   . HOH   D .   ? 0.3011 0.4433 0.3375 0.0024  0.0603  0.0638  336 HOH   A O   
6623 O O   . HOH   D .   ? 0.3648 0.6113 0.4032 -0.0547 0.0280  0.1355  337 HOH   A O   
6624 O O   B HOH   D .   ? 0.2127 0.2962 0.1793 0.0568  0.0040  0.0084  338 HOH   A O   
6625 O O   . HOH   D .   ? 0.2826 0.5592 0.6629 0.1104  0.0921  0.1169  339 HOH   A O   
6626 O O   . HOH   D .   ? 0.2561 0.5045 0.3970 0.0437  -0.0507 0.1728  340 HOH   A O   
6627 O O   A HOH   D .   ? 0.2321 0.1690 0.2023 -0.0286 0.0237  0.0018  341 HOH   A O   
6628 O O   B HOH   D .   ? 0.1766 0.1198 0.3047 0.0120  -0.0963 0.0062  342 HOH   A O   
6629 O O   B HOH   D .   ? 0.1636 0.1703 0.1283 0.0204  0.0037  -0.0438 343 HOH   A O   
6630 O O   . HOH   D .   ? 0.3155 0.3445 0.3399 -0.1122 -0.0165 0.0081  344 HOH   A O   
6631 O O   . HOH   D .   ? 0.3749 0.2508 0.6496 0.0636  0.1220  0.0168  345 HOH   A O   
6632 O O   . HOH   D .   ? 0.5802 0.4500 0.6378 0.0507  -0.1084 0.0005  346 HOH   A O   
6633 O O   . HOH   D .   ? 0.1335 0.1417 0.1918 -0.0006 -0.0151 0.0098  347 HOH   A O   
6634 O O   A HOH   D .   ? 0.6677 0.3385 0.5452 -0.1044 -0.1285 0.1039  348 HOH   A O   
6635 O O   . HOH   D .   ? 0.5541 0.3984 0.4009 -0.1946 -0.0903 0.1842  349 HOH   A O   
6636 O O   . HOH   D .   ? 0.3956 0.2722 0.5244 -0.0071 -0.1350 0.1637  350 HOH   A O   
6637 O O   . HOH   D .   ? 0.2586 0.4249 0.2864 -0.0438 0.0606  0.0271  351 HOH   A O   
6638 O O   . HOH   D .   ? 0.1502 0.2174 0.2138 0.0100  -0.0061 0.0454  352 HOH   A O   
6639 O O   B HOH   D .   ? 0.1404 0.1722 0.2520 0.0517  0.0162  0.0714  353 HOH   A O   
6640 O O   . HOH   D .   ? 0.3734 0.3464 0.2409 -0.0212 -0.1320 0.0474  354 HOH   A O   
6641 O O   . HOH   D .   ? 0.1920 0.1959 0.4077 0.0207  0.0988  -0.0194 355 HOH   A O   
6642 O O   . HOH   D .   ? 0.3203 0.4098 0.3682 -0.1074 -0.1162 -0.0182 356 HOH   A O   
6643 O O   . HOH   D .   ? 0.3861 0.3632 0.2272 -0.1080 -0.0523 -0.0595 357 HOH   A O   
6644 O O   A HOH   D .   ? 0.1667 0.3261 0.2571 0.0901  0.0755  0.1419  358 HOH   A O   
6645 O O   . HOH   D .   ? 0.4676 0.2758 0.6048 -0.1433 0.1059  -0.0322 359 HOH   A O   
6646 O O   . HOH   D .   ? 0.1365 0.1231 0.1349 0.0037  0.0039  0.0026  360 HOH   A O   
6647 O O   . HOH   D .   ? 0.2527 0.3713 0.3674 0.1051  -0.0761 -0.0341 361 HOH   A O   
6648 O O   . HOH   D .   ? 0.3614 0.6744 0.4805 -0.0584 -0.1302 0.1013  362 HOH   A O   
6649 O O   A HOH   D .   ? 0.1828 0.2761 0.2574 0.0139  0.0451  0.0176  363 HOH   A O   
6650 O O   . HOH   D .   ? 0.6209 0.4143 0.2706 0.0478  0.0240  0.1439  364 HOH   A O   
6651 O O   . HOH   D .   ? 0.1461 0.1891 0.2515 0.0093  -0.0136 0.0023  365 HOH   A O   
6652 O O   A HOH   D .   ? 0.3397 0.1606 0.1779 0.0355  0.0546  0.0077  366 HOH   A O   
6653 O O   . HOH   D .   ? 0.1510 0.1285 0.2149 -0.0101 0.0177  -0.0104 367 HOH   A O   
6654 O O   . HOH   D .   ? 0.3679 0.5753 0.4925 0.1448  -0.0220 0.1282  368 HOH   A O   
6655 O O   . HOH   D .   ? 0.3567 0.4085 0.4001 0.1739  0.0526  0.0547  369 HOH   A O   
6656 O O   . HOH   D .   ? 0.2971 0.2588 0.4044 -0.0886 0.1341  -0.0283 370 HOH   A O   
6657 O O   A HOH   D .   ? 0.1657 0.2118 0.3286 0.0183  0.0819  -0.0508 371 HOH   A O   
6658 O O   . HOH   D .   ? 0.4446 0.2360 0.4201 -0.1290 0.1488  -0.0429 372 HOH   A O   
6659 O O   . HOH   D .   ? 0.3908 0.2054 0.2057 0.1151  0.0467  0.0097  373 HOH   A O   
6660 O O   . HOH   D .   ? 0.1535 0.1472 0.1514 -0.0079 -0.0175 -0.0054 374 HOH   A O   
6661 O O   . HOH   D .   ? 0.1768 0.1693 0.2006 -0.0256 0.0092  0.0244  375 HOH   A O   
6662 O O   . HOH   D .   ? 0.3834 0.2200 0.4652 -0.1161 0.0819  0.0300  376 HOH   A O   
6663 O O   B HOH   D .   ? 0.1235 0.1296 0.1578 -0.0366 -0.0365 -0.0446 377 HOH   A O   
6664 O O   . HOH   D .   ? 0.1910 0.1881 0.2423 -0.0327 0.0040  0.0409  378 HOH   A O   
6665 O O   . HOH   D .   ? 0.2170 0.2077 0.2088 -0.0244 -0.0486 0.0266  379 HOH   A O   
6666 O O   . HOH   D .   ? 0.1552 0.2581 0.3598 -0.0124 0.0658  0.0730  380 HOH   A O   
6667 O O   . HOH   D .   ? 0.2982 0.3517 0.4705 -0.0621 -0.0962 -0.0704 381 HOH   A O   
6668 O O   . HOH   D .   ? 0.2853 0.4499 0.3472 -0.0680 -0.0315 0.1444  382 HOH   A O   
6669 O O   . HOH   D .   ? 0.2635 0.4448 0.3115 0.0494  0.0818  0.1948  383 HOH   A O   
6670 O O   A HOH   D .   ? 0.1353 0.1595 0.2604 0.0190  -0.0308 -0.0701 384 HOH   A O   
6671 O O   A HOH   D .   ? 0.2609 0.1960 0.3052 -0.0279 0.1024  0.0244  385 HOH   A O   
6672 O O   . HOH   D .   ? 0.3018 0.2870 0.2132 0.0277  0.0797  0.0126  386 HOH   A O   
6673 O O   B HOH   D .   ? 0.2265 0.2586 0.2668 -0.0069 -0.0045 -0.0192 387 HOH   A O   
6674 O O   A HOH   D .   ? 0.1653 0.1693 0.1621 0.0002  0.0083  0.0122  388 HOH   A O   
6675 O O   B HOH   D .   ? 0.1620 0.1683 0.1456 0.0075  0.0116  0.0288  389 HOH   A O   
6676 O O   . HOH   D .   ? 0.1781 0.2576 0.2583 0.0445  0.0397  0.0931  390 HOH   A O   
6677 O O   . HOH   D .   ? 0.6618 0.4052 0.5837 -0.1054 -0.0780 0.0545  391 HOH   A O   
6678 O O   . HOH   D .   ? 0.3963 0.2745 0.4391 -0.1158 0.0041  0.0203  392 HOH   A O   
6679 O O   . HOH   D .   ? 0.2090 0.1940 0.2656 -0.0013 -0.0399 0.0232  393 HOH   A O   
6680 O O   . HOH   D .   ? 0.2735 0.1811 0.1772 -0.0611 0.0268  0.0171  394 HOH   A O   
6681 O O   . HOH   D .   ? 0.3179 0.2293 0.3275 -0.0032 -0.0229 0.0875  395 HOH   A O   
6682 O O   B HOH   D .   ? 0.1075 0.1845 0.2392 0.0483  -0.0617 -0.0496 396 HOH   A O   
6683 O O   . HOH   D .   ? 0.1801 0.2011 0.1783 -0.0121 0.0067  0.0504  397 HOH   A O   
6684 O O   . HOH   D .   ? 0.5609 0.4950 0.5792 -0.0920 -0.0665 0.1410  398 HOH   A O   
6685 O O   . HOH   D .   ? 0.2554 0.2566 0.2931 -0.0053 -0.0214 -0.0503 399 HOH   A O   
6686 O O   B HOH   D .   ? 0.1820 0.1849 0.1090 -0.0628 -0.0288 0.0075  400 HOH   A O   
6687 O O   B HOH   D .   ? 0.2302 0.1478 0.0969 -0.0494 -0.0151 0.0062  401 HOH   A O   
6688 O O   . HOH   D .   ? 0.6004 0.3544 0.1989 -0.0444 0.1023  0.0397  402 HOH   A O   
6689 O O   . HOH   D .   ? 0.2895 0.6123 0.3819 0.0994  0.0652  -0.0994 403 HOH   A O   
6690 O O   . HOH   D .   ? 0.2528 0.3841 0.3811 -0.0409 0.1112  -0.0945 404 HOH   A O   
6691 O O   . HOH   D .   ? 0.1895 0.1899 0.3922 0.0425  0.1086  0.1073  405 HOH   A O   
6692 O O   . HOH   D .   ? 0.2998 0.2696 0.2359 -0.0652 -0.0963 0.0381  406 HOH   A O   
6693 O O   . HOH   D .   ? 0.6122 0.6337 0.3935 0.2204  -0.0904 -0.0466 407 HOH   A O   
6694 O O   . HOH   D .   ? 0.5502 0.3806 0.4408 0.0642  0.1768  -0.0828 408 HOH   A O   
6695 O O   . HOH   D .   ? 0.2108 0.1789 0.2488 0.0035  -0.0241 0.0069  409 HOH   A O   
6696 O O   B HOH   D .   ? 0.1542 0.3000 0.1634 -0.0157 0.0582  -0.0504 410 HOH   A O   
6697 O O   . HOH   D .   ? 0.3109 0.3083 0.3228 -0.0055 0.1292  -0.0085 411 HOH   A O   
6698 O O   . HOH   D .   ? 0.5359 0.2786 0.3148 -0.1178 0.1012  0.0336  412 HOH   A O   
6699 O O   A HOH   D .   ? 0.1397 0.1272 0.1434 -0.0210 -0.0310 -0.0090 413 HOH   A O   
6700 O O   . HOH   D .   ? 0.3288 0.3743 0.5181 -0.0096 0.0928  -0.0569 414 HOH   A O   
6701 O O   . HOH   D .   ? 0.1879 0.1312 0.1560 -0.0258 0.0148  0.0033  415 HOH   A O   
6702 O O   . HOH   D .   ? 0.6112 0.6736 0.5294 0.0662  0.0673  0.0810  416 HOH   A O   
6703 O O   . HOH   D .   ? 0.3723 0.6297 0.4913 -0.1315 0.0818  0.1047  417 HOH   A O   
6704 O O   . HOH   D .   ? 0.5734 0.2728 0.4240 0.1125  -0.0456 -0.0307 418 HOH   A O   
6705 O O   . HOH   D .   ? 0.4154 0.6344 0.3529 -0.0915 -0.0439 0.1683  419 HOH   A O   
6706 O O   A HOH   D .   ? 0.1229 0.1571 0.1545 -0.0166 -0.0115 -0.0112 420 HOH   A O   
6707 O O   . HOH   D .   ? 0.1470 0.1750 0.2815 -0.0005 0.0021  0.0168  421 HOH   A O   
6708 O O   A HOH   D .   ? 0.2087 0.1415 0.2182 -0.0072 0.0037  0.0137  422 HOH   A O   
6709 O O   . HOH   D .   ? 0.1959 0.2482 0.3359 -0.0214 -0.0376 0.0070  423 HOH   A O   
6710 O O   . HOH   D .   ? 0.2462 0.2241 0.2529 -0.0659 -0.0084 0.0648  424 HOH   A O   
6711 O O   . HOH   D .   ? 0.3022 0.3723 0.7105 -0.0254 0.1595  -0.0388 425 HOH   A O   
6712 O O   B HOH   D .   ? 0.2053 0.2391 0.1836 0.0924  -0.0444 -0.0784 426 HOH   A O   
6713 O O   . HOH   D .   ? 0.1518 0.2423 0.2683 0.0090  0.0054  0.0504  427 HOH   A O   
6714 O O   . HOH   D .   ? 0.2012 0.1619 0.1528 -0.0034 0.0173  0.0135  428 HOH   A O   
6715 O O   . HOH   D .   ? 0.6374 0.3591 0.4383 0.1449  -0.0818 0.1261  429 HOH   A O   
6716 O O   . HOH   D .   ? 0.2173 0.2748 0.2407 -0.0102 -0.0636 0.0386  430 HOH   A O   
6717 O O   . HOH   D .   ? 0.3384 0.4615 0.3711 0.1442  -0.0675 -0.1520 431 HOH   A O   
6718 O O   . HOH   D .   ? 0.6339 0.5736 0.5694 -0.1032 -0.1050 -0.1269 432 HOH   A O   
6719 O O   . HOH   D .   ? 0.2883 0.6425 0.1842 -0.0385 0.0516  0.0108  433 HOH   A O   
6720 O O   . HOH   D .   ? 0.2461 0.4451 0.2436 0.1803  0.0036  0.0282  434 HOH   A O   
6721 O O   . HOH   D .   ? 0.3351 0.1295 0.2153 -0.0044 -0.0510 0.0112  435 HOH   A O   
6722 O O   . HOH   D .   ? 0.1983 0.2140 0.2678 -0.0005 -0.0047 -0.0146 436 HOH   A O   
6723 O O   A HOH   D .   ? 0.1895 0.1553 0.2768 0.0265  -0.0414 0.0149  437 HOH   A O   
6724 O O   . HOH   D .   ? 0.6309 0.6896 0.4438 0.0807  0.2802  -0.0988 438 HOH   A O   
6725 O O   . HOH   D .   ? 0.3624 0.2668 0.2375 -0.0058 0.0043  0.0165  439 HOH   A O   
6726 O O   . HOH   D .   ? 0.4691 0.2184 0.4794 -0.0900 -0.2285 0.0975  440 HOH   A O   
6727 O O   . HOH   D .   ? 0.5825 0.4249 0.3473 -0.0144 -0.1440 0.0172  441 HOH   A O   
6728 O O   . HOH   D .   ? 0.5314 0.6234 0.6212 -0.1511 0.0218  -0.1271 442 HOH   A O   
6729 O O   . HOH   D .   ? 0.4521 0.4145 0.5782 0.1204  0.0255  -0.0212 443 HOH   A O   
6730 O O   A HOH   D .   ? 0.4298 0.2189 0.3276 0.0474  0.1397  0.1121  444 HOH   A O   
6731 O O   . HOH   D .   ? 0.6714 0.6033 0.5417 0.0998  -0.1270 0.0323  445 HOH   A O   
6732 O O   . HOH   D .   ? 0.1751 0.2167 0.4866 -0.0200 -0.0715 0.0546  446 HOH   A O   
6733 O O   A HOH   D .   ? 0.1830 0.1084 0.1555 0.0128  -0.0119 -0.0062 447 HOH   A O   
6734 O O   A HOH   D .   ? 0.2576 0.1511 0.2407 0.0297  -0.1078 -0.0283 448 HOH   A O   
6735 O O   . HOH   D .   ? 0.8261 0.8825 0.6492 -0.0289 0.0064  -0.0258 449 HOH   A O   
6736 O O   B HOH   D .   ? 0.2072 0.2610 0.2162 -0.0245 0.0423  -0.0668 450 HOH   A O   
6737 O O   . HOH   D .   ? 0.6767 0.7498 0.4555 0.2032  -0.1273 0.2186  451 HOH   A O   
6738 O O   . HOH   D .   ? 0.3622 0.2559 0.1756 -0.0894 0.0216  0.0372  452 HOH   A O   
6739 O O   . HOH   D .   ? 0.2586 0.1601 0.2482 -0.0008 -0.0005 0.0121  453 HOH   A O   
6740 O O   . HOH   D .   ? 0.6231 0.5624 0.7309 0.0766  -0.1338 0.1379  454 HOH   A O   
6741 O O   . HOH   D .   ? 0.3396 0.3339 0.2844 0.1827  -0.0582 -0.0638 455 HOH   A O   
6742 O O   . HOH   D .   ? 0.5266 0.4100 0.4769 -0.1323 -0.1169 -0.1209 456 HOH   A O   
6743 O O   B HOH   D .   ? 0.2578 0.2769 0.2961 0.0550  -0.0873 0.1182  457 HOH   A O   
6744 O O   . HOH   D .   ? 0.2407 0.1913 0.2822 0.0146  0.0307  0.0226  458 HOH   A O   
6745 O O   A HOH   D .   ? 0.5050 0.4313 0.3869 -0.0861 -0.0056 0.2242  459 HOH   A O   
6746 O O   . HOH   D .   ? 0.2138 0.2680 0.2560 0.0048  -0.0148 -0.0658 460 HOH   A O   
6747 O O   A HOH   D .   ? 0.2713 0.2769 0.3884 -0.0498 0.0891  -0.1166 461 HOH   A O   
6748 O O   . HOH   D .   ? 0.5891 0.2551 0.4450 0.0361  0.0520  0.0927  462 HOH   A O   
6749 O O   B HOH   D .   ? 0.2367 0.2213 0.1718 -0.0309 -0.0911 0.0125  463 HOH   A O   
6750 O O   A HOH   D .   ? 0.5351 0.3208 0.4375 0.1217  -0.0099 0.1832  464 HOH   A O   
6751 O O   . HOH   D .   ? 0.5606 0.5678 0.4931 -0.0140 -0.0034 0.1698  465 HOH   A O   
6752 O O   . HOH   D .   ? 0.6217 0.5061 0.4683 -0.0412 0.1042  0.1058  466 HOH   A O   
6753 O O   . HOH   D .   ? 0.2906 0.3502 0.4444 0.0954  -0.0206 0.1299  467 HOH   A O   
6754 O O   . HOH   D .   ? 0.5318 0.3179 0.5367 0.0433  0.0297  0.0485  468 HOH   A O   
6755 O O   B HOH   D .   ? 0.3104 0.2865 0.2695 0.0149  -0.0423 0.0199  469 HOH   A O   
6756 O O   . HOH   D .   ? 0.3105 0.3079 0.3020 -0.0953 0.0213  -0.0690 470 HOH   A O   
6757 O O   B HOH   D .   ? 0.2727 0.2855 0.2264 -0.0207 -0.1055 0.0320  471 HOH   A O   
6758 O O   B HOH   D .   ? 0.1352 0.0897 0.1858 0.0009  -0.0322 -0.0201 472 HOH   A O   
6759 O O   . HOH   D .   ? 0.6782 0.8076 0.4626 0.0219  -0.0365 -0.0501 473 HOH   A O   
6760 O O   . HOH   D .   ? 0.2944 0.5078 0.5065 -0.1353 0.0780  -0.1728 474 HOH   A O   
6761 O O   . HOH   D .   ? 0.4204 0.4884 0.5336 0.1175  0.0548  0.1788  475 HOH   A O   
6762 O O   . HOH   D .   ? 0.6174 0.3671 0.8094 -0.0052 -0.0067 0.2656  476 HOH   A O   
6763 O O   . HOH   D .   ? 0.2785 0.2376 0.5004 0.0572  -0.1121 -0.0506 477 HOH   A O   
6764 O O   . HOH   D .   ? 0.8381 0.5149 0.5345 0.2299  0.1934  0.1793  478 HOH   A O   
6765 O O   . HOH   D .   ? 0.3722 0.5800 0.3751 -0.0769 -0.0706 0.1858  479 HOH   A O   
6766 O O   B HOH   D .   ? 0.2264 0.1390 0.2018 -0.0198 -0.0665 -0.0292 480 HOH   A O   
6767 O O   . HOH   D .   ? 0.2850 0.3990 0.4921 0.0546  0.0343  -0.1711 481 HOH   A O   
6768 O O   A HOH   D .   ? 0.2854 0.3882 0.3660 -0.0361 -0.0607 0.0483  482 HOH   A O   
6769 O O   . HOH   D .   ? 0.2561 0.2802 0.3270 -0.0921 0.0539  -0.0304 483 HOH   A O   
6770 O O   . HOH   D .   ? 0.2701 0.1675 0.2512 0.0246  -0.0880 -0.0294 484 HOH   A O   
6771 O O   . HOH   D .   ? 0.3921 0.5424 0.3579 0.0054  -0.0323 -0.0672 485 HOH   A O   
6772 O O   B HOH   D .   ? 0.1874 0.3026 0.3239 -0.0230 0.0054  -0.0163 486 HOH   A O   
6773 O O   . HOH   D .   ? 0.6414 0.4459 0.4231 0.0812  0.1317  0.0497  487 HOH   A O   
6774 O O   B HOH   D .   ? 0.3359 0.2510 0.2663 -0.0306 0.0324  0.0601  488 HOH   A O   
6775 O O   . HOH   D .   ? 0.4391 0.4220 0.2574 -0.0731 0.0131  -0.0161 489 HOH   A O   
6776 O O   . HOH   D .   ? 0.4107 0.5281 0.3177 -0.0780 -0.0351 0.0260  490 HOH   A O   
6777 O O   . HOH   D .   ? 0.3693 0.2687 0.4232 -0.0243 0.1062  0.0036  491 HOH   A O   
6778 O O   . HOH   D .   ? 0.4710 0.5396 0.3717 0.0578  -0.0454 -0.0347 492 HOH   A O   
6779 O O   B HOH   D .   ? 0.1738 0.1425 0.1760 0.0055  -0.0296 0.0240  493 HOH   A O   
6780 O O   . HOH   D .   ? 0.6144 0.6729 0.6346 -0.1503 -0.1158 0.0796  494 HOH   A O   
6781 O O   . HOH   D .   ? 0.4749 0.4743 0.4998 -0.1580 -0.0823 -0.0256 495 HOH   A O   
6782 O O   B HOH   D .   ? 0.2486 0.2711 0.2470 0.0490  0.0864  0.0071  496 HOH   A O   
6783 O O   . HOH   D .   ? 0.4601 0.2489 0.3390 -0.0841 -0.1397 0.0520  497 HOH   A O   
6784 O O   A HOH   D .   ? 0.2035 0.2318 0.2419 0.0173  0.0228  -0.0071 498 HOH   A O   
6785 O O   . HOH   D .   ? 0.6149 0.5057 0.6166 -0.1124 0.0172  -0.0592 499 HOH   A O   
6786 O O   . HOH   D .   ? 0.7628 0.3503 0.3221 -0.0324 -0.1293 0.0123  500 HOH   A O   
6787 O O   . HOH   D .   ? 0.5894 0.4602 0.4403 -0.0455 0.0127  -0.1295 501 HOH   A O   
6788 O O   . HOH   D .   ? 0.2857 0.3527 0.4369 0.0074  0.1013  0.0721  502 HOH   A O   
6789 O O   . HOH   D .   ? 0.5437 0.5540 0.6320 0.0993  0.0893  -0.1194 503 HOH   A O   
6790 O O   . HOH   D .   ? 0.5924 0.4002 0.4550 0.0374  0.1211  0.0013  504 HOH   A O   
6791 O O   B HOH   D .   ? 0.2112 0.1587 0.1699 -0.0532 -0.0452 0.0849  505 HOH   A O   
6792 O O   . HOH   D .   ? 0.3004 0.5007 0.3806 0.1282  0.1272  0.2345  506 HOH   A O   
6793 O O   B HOH   D .   ? 0.4566 0.3378 0.3855 -0.0565 0.0124  0.0293  507 HOH   A O   
6794 O O   . HOH   D .   ? 0.6595 0.6999 0.4928 -0.1246 0.1779  0.1502  508 HOH   A O   
6795 O O   . HOH   D .   ? 0.4616 0.3765 0.2671 -0.1089 0.1459  -0.0531 509 HOH   A O   
6796 O O   . HOH   D .   ? 0.5651 0.4789 0.4036 -0.0650 -0.1042 -0.0455 510 HOH   A O   
6797 O O   . HOH   D .   ? 0.5344 0.3050 0.4638 -0.0438 0.2478  0.0102  511 HOH   A O   
6798 O O   . HOH   D .   ? 0.2682 0.2558 0.6572 -0.0066 -0.1248 0.0100  512 HOH   A O   
6799 O O   . HOH   D .   ? 0.4956 0.4761 0.5173 0.0836  -0.0826 0.0057  513 HOH   A O   
6800 O O   . HOH   D .   ? 0.2778 0.2174 0.5529 0.0041  0.0691  0.0940  514 HOH   A O   
6801 O O   A HOH   D .   ? 0.3335 0.2286 0.4008 -0.0546 0.0243  0.0750  515 HOH   A O   
6802 O O   B HOH   D .   ? 0.1715 0.2712 0.2590 -0.0041 -0.0143 0.0803  516 HOH   A O   
6803 O O   . HOH   D .   ? 0.5694 0.6284 0.4280 0.0375  -0.1338 -0.0449 517 HOH   A O   
6804 O O   . HOH   D .   ? 0.2671 0.3178 0.4989 -0.0454 0.1236  -0.0917 518 HOH   A O   
6805 O O   . HOH   D .   ? 0.3653 0.8135 0.5335 -0.1226 -0.0173 0.2330  519 HOH   A O   
6806 O O   . HOH   D .   ? 0.2530 0.3639 0.3581 0.0778  -0.0536 0.0433  520 HOH   A O   
6807 O O   . HOH   D .   ? 0.4480 0.2495 0.4582 -0.1233 0.0062  0.0330  521 HOH   A O   
6808 O O   . HOH   D .   ? 0.7029 0.2558 0.4198 -0.0377 -0.0632 0.0290  522 HOH   A O   
6809 O O   . HOH   D .   ? 0.2736 0.4072 0.4957 0.0517  -0.0410 0.0557  523 HOH   A O   
6810 O O   . HOH   D .   ? 0.3006 0.4673 0.3086 -0.0597 -0.0227 -0.0740 524 HOH   A O   
6811 O O   . HOH   D .   ? 0.5611 0.6937 0.5232 0.1254  -0.0602 0.0905  525 HOH   A O   
6812 O O   . HOH   D .   ? 0.5678 0.4551 0.5477 -0.0985 0.0235  0.0850  526 HOH   A O   
6813 O O   B HOH   D .   ? 0.3811 0.2977 0.2617 -0.0625 0.0722  -0.0554 527 HOH   A O   
6814 O O   B HOH   D .   ? 0.1886 0.1588 0.1676 -0.0132 0.0020  0.0549  528 HOH   A O   
6815 O O   . HOH   D .   ? 0.4816 0.6316 0.4585 0.2744  0.0086  0.0959  529 HOH   A O   
6816 O O   . HOH   D .   ? 0.3118 0.2298 0.4010 0.0161  0.0487  0.0651  530 HOH   A O   
6817 O O   B HOH   D .   ? 0.2014 0.1408 0.2048 0.0201  -0.0502 0.0387  531 HOH   A O   
6818 O O   A HOH   D .   ? 0.3706 0.6441 0.4174 0.0380  0.1721  0.0071  532 HOH   A O   
6819 O O   . HOH   D .   ? 0.4417 0.5038 0.4048 -0.0435 -0.0159 -0.1297 533 HOH   A O   
6820 O O   . HOH   D .   ? 0.2862 0.7301 0.4355 0.0214  0.0804  -0.0148 534 HOH   A O   
6821 O O   . HOH   D .   ? 0.4528 0.5219 0.4587 0.1822  -0.0404 0.1168  535 HOH   A O   
6822 O O   . HOH   D .   ? 0.4367 0.6093 0.5314 -0.0668 -0.0992 0.0155  536 HOH   A O   
6823 O O   . HOH   D .   ? 0.2575 0.4448 0.5810 -0.0335 -0.0982 0.2718  537 HOH   A O   
6824 O O   . HOH   E .   ? 0.2289 0.2110 0.2856 0.0210  0.0660  0.0268  201 HOH   B O   
6825 O O   . HOH   E .   ? 0.5076 0.4201 0.6130 0.0063  -0.1260 0.2699  202 HOH   B O   
6826 O O   . HOH   E .   ? 0.4593 0.5075 0.2929 0.0089  -0.0923 -0.1505 203 HOH   B O   
6827 O O   . HOH   E .   ? 0.7235 0.5509 0.5582 0.2440  0.0673  0.0077  204 HOH   B O   
6828 O O   . HOH   E .   ? 0.4744 0.2994 0.3485 -0.0434 0.0052  -0.1214 205 HOH   B O   
6829 O O   . HOH   E .   ? 0.4430 0.5700 0.4019 0.2681  -0.1131 -0.0203 206 HOH   B O   
6830 O O   . HOH   E .   ? 0.3961 0.5228 0.5024 -0.0483 0.2337  -0.1598 207 HOH   B O   
6831 O O   . HOH   E .   ? 0.6581 0.3112 0.4744 0.0875  0.1083  -0.0122 208 HOH   B O   
6832 O O   . HOH   E .   ? 0.5669 0.3744 0.3609 0.0014  -0.1357 0.0569  209 HOH   B O   
6833 O O   . HOH   E .   ? 0.3490 0.6584 0.3556 0.0876  0.0037  0.2311  210 HOH   B O   
6834 O O   . HOH   E .   ? 0.3029 0.5366 0.6718 -0.1167 0.0317  -0.0791 211 HOH   B O   
6835 O O   . HOH   E .   ? 0.4090 0.5448 0.4360 0.2472  -0.0385 0.0113  212 HOH   B O   
6836 O O   . HOH   E .   ? 0.2748 0.2933 0.6971 0.0724  -0.1224 0.0408  213 HOH   B O   
6837 O O   . HOH   E .   ? 0.4232 0.4038 0.5432 -0.1095 -0.0391 -0.1391 214 HOH   B O   
6838 O O   . HOH   E .   ? 0.5829 0.3068 0.3948 -0.1828 0.0401  0.0348  215 HOH   B O   
6839 O O   . HOH   E .   ? 0.2725 0.2761 0.6092 0.0088  0.0992  0.0524  216 HOH   B O   
6840 O O   . HOH   E .   ? 0.1542 0.1746 0.2766 -0.0110 -0.0020 0.0006  217 HOH   B O   
6841 O O   . HOH   E .   ? 0.3652 0.7468 0.3295 0.2095  0.0104  0.0164  218 HOH   B O   
6842 O O   . HOH   E .   ? 0.1938 0.2392 0.2886 0.0150  0.0147  -0.0278 219 HOH   B O   
6843 O O   . HOH   E .   ? 0.2979 0.1915 0.5359 0.0219  0.1825  0.0861  220 HOH   B O   
6844 O O   . HOH   E .   ? 0.3769 0.4610 0.4030 0.0413  0.0949  -0.1139 221 HOH   B O   
6845 O O   . HOH   E .   ? 0.3100 0.4643 0.4537 0.1647  0.0091  -0.0705 222 HOH   B O   
6846 O O   . HOH   E .   ? 0.3613 0.4750 0.5459 0.0296  -0.0973 0.0517  223 HOH   B O   
6847 O O   . HOH   E .   ? 0.2777 0.3871 0.4349 -0.1099 0.0387  -0.0401 224 HOH   B O   
6848 O O   . HOH   E .   ? 0.6013 0.6169 0.3135 0.1547  0.0145  0.0607  225 HOH   B O   
6849 O O   . HOH   E .   ? 0.1641 0.1881 0.2840 -0.0103 0.0111  -0.0026 226 HOH   B O   
6850 O O   . HOH   E .   ? 0.4701 0.2148 0.3518 -0.0272 -0.1172 0.0294  227 HOH   B O   
6851 O O   . HOH   E .   ? 0.3722 0.4480 0.5048 -0.1782 -0.0166 0.0480  228 HOH   B O   
6852 O O   . HOH   E .   ? 0.2279 0.2126 0.3631 -0.0377 -0.0112 -0.0547 229 HOH   B O   
6853 O O   . HOH   E .   ? 0.3020 0.2044 0.3883 0.0002  0.1364  0.0042  230 HOH   B O   
6854 O O   . HOH   E .   ? 0.4566 0.4034 0.7078 -0.0008 -0.1552 -0.0906 231 HOH   B O   
6855 O O   . HOH   E .   ? 0.2459 0.1763 0.2738 -0.0331 0.0994  -0.0027 232 HOH   B O   
6856 O O   . HOH   E .   ? 0.2124 0.2137 0.2920 -0.0399 0.0014  -0.0332 233 HOH   B O   
6857 O O   . HOH   E .   ? 0.1929 0.4278 0.2397 -0.0386 -0.0171 0.0521  234 HOH   B O   
6858 O O   . HOH   E .   ? 0.3843 0.2827 0.3917 0.1129  -0.0485 -0.0854 235 HOH   B O   
6859 O O   . HOH   E .   ? 0.3558 0.3024 0.2497 0.0348  0.0568  0.0426  236 HOH   B O   
6860 O O   . HOH   E .   ? 0.2061 0.1270 0.3371 0.0126  -0.0447 -0.0165 237 HOH   B O   
6861 O O   . HOH   E .   ? 0.1425 0.1426 0.1761 -0.0144 -0.0069 0.0031  238 HOH   B O   
6862 O O   . HOH   E .   ? 0.2630 0.2525 0.3207 0.0307  0.0300  -0.0935 239 HOH   B O   
6863 O O   . HOH   E .   ? 0.1386 0.1278 0.1554 -0.0036 -0.0084 0.0061  240 HOH   B O   
6864 O O   . HOH   E .   ? 0.3626 0.3533 0.3935 0.0793  -0.1300 -0.1768 241 HOH   B O   
6865 O O   . HOH   E .   ? 0.3128 0.4811 0.3401 -0.1377 -0.0107 -0.1044 242 HOH   B O   
6866 O O   . HOH   E .   ? 0.5383 0.2994 0.3798 -0.2203 -0.0278 0.0152  243 HOH   B O   
6867 O O   . HOH   E .   ? 0.1577 0.1451 0.2607 -0.0101 0.0089  -0.0141 244 HOH   B O   
6868 O O   . HOH   E .   ? 0.2134 0.3976 0.2904 -0.0395 -0.0558 -0.0622 245 HOH   B O   
6869 O O   . HOH   E .   ? 0.3595 0.1737 0.2163 0.0098  -0.0722 -0.0025 246 HOH   B O   
6870 O O   . HOH   E .   ? 0.3133 0.1649 0.5740 -0.0189 -0.1368 -0.0194 247 HOH   B O   
6871 O O   . HOH   E .   ? 0.3855 0.2974 0.4846 -0.0466 -0.1035 -0.0613 248 HOH   B O   
6872 O O   . HOH   E .   ? 0.2173 0.1843 0.2173 -0.0264 -0.0497 0.0130  249 HOH   B O   
6873 O O   . HOH   E .   ? 0.6814 0.4798 0.4955 0.2431  0.0060  -0.1417 250 HOH   B O   
6874 O O   . HOH   E .   ? 0.6363 0.2521 0.2421 -0.0290 0.0861  -0.0082 251 HOH   B O   
6875 O O   . HOH   E .   ? 0.3031 0.3416 0.2014 0.0359  0.0653  0.0201  252 HOH   B O   
6876 O O   . HOH   E .   ? 0.2568 0.4333 0.5163 0.1251  -0.0745 -0.0890 253 HOH   B O   
6877 O O   . HOH   E .   ? 0.1363 0.1506 0.2021 -0.0003 0.0073  0.0066  254 HOH   B O   
6878 O O   . HOH   E .   ? 0.2073 0.1380 0.2030 -0.0256 -0.0272 0.0225  255 HOH   B O   
6879 O O   . HOH   E .   ? 0.2895 0.2249 0.3100 0.0995  0.0960  0.0190  256 HOH   B O   
6880 O O   . HOH   E .   ? 0.2708 0.4798 0.5647 0.0039  0.0305  -0.1209 257 HOH   B O   
6881 O O   . HOH   E .   ? 0.3297 0.2307 0.2972 -0.0350 0.0281  -0.0477 258 HOH   B O   
6882 O O   . HOH   E .   ? 0.2522 0.1935 0.2695 -0.0552 0.0050  -0.0072 259 HOH   B O   
6883 O O   . HOH   E .   ? 0.1607 0.1654 0.2741 -0.0204 -0.0243 0.0066  260 HOH   B O   
6884 O O   . HOH   E .   ? 0.2259 0.2002 0.1875 0.0075  -0.0101 -0.0012 261 HOH   B O   
6885 O O   . HOH   E .   ? 0.1805 0.1734 0.1532 -0.0411 -0.0373 0.0020  262 HOH   B O   
6886 O O   . HOH   E .   ? 0.2158 0.1856 0.3593 0.0057  -0.0440 -0.0328 263 HOH   B O   
6887 O O   . HOH   E .   ? 0.4391 0.3420 0.3496 -0.1024 0.0631  -0.0973 264 HOH   B O   
6888 O O   . HOH   E .   ? 0.2293 0.2164 0.2409 0.0777  -0.0718 -0.0644 265 HOH   B O   
6889 O O   . HOH   E .   ? 0.2754 0.3300 0.4977 -0.0091 0.0025  -0.1091 266 HOH   B O   
6890 O O   . HOH   E .   ? 0.1682 0.1345 0.4395 -0.0095 -0.0241 -0.0004 267 HOH   B O   
6891 O O   . HOH   E .   ? 0.2297 0.2077 0.1953 0.0192  -0.0077 0.0010  268 HOH   B O   
6892 O O   . HOH   E .   ? 0.1998 0.4293 0.4845 -0.0566 -0.0250 -0.1768 269 HOH   B O   
6893 O O   . HOH   E .   ? 0.1969 0.1454 0.2230 -0.0207 -0.0131 0.0086  270 HOH   B O   
6894 O O   . HOH   E .   ? 0.2275 0.3355 0.2351 -0.0543 0.0177  0.0699  271 HOH   B O   
6895 O O   . HOH   E .   ? 0.1578 0.1599 0.3228 -0.0167 0.0101  0.0002  272 HOH   B O   
6896 O O   . HOH   E .   ? 0.2823 0.3752 0.3587 -0.1057 0.1033  -0.1581 273 HOH   B O   
6897 O O   . HOH   E .   ? 0.2282 0.2410 0.2491 -0.0327 -0.0741 -0.0306 274 HOH   B O   
6898 O O   . HOH   E .   ? 0.2602 0.2832 0.2443 -0.0416 -0.0940 0.0023  275 HOH   B O   
6899 O O   . HOH   E .   ? 0.2402 0.3611 0.3772 0.0170  0.1122  0.0119  276 HOH   B O   
6900 O O   . HOH   E .   ? 0.2965 0.7184 0.7669 0.1609  -0.0260 -0.1122 277 HOH   B O   
6901 O O   . HOH   E .   ? 0.4388 0.3964 0.2721 0.0374  -0.0016 -0.1190 278 HOH   B O   
6902 O O   . HOH   E .   ? 0.5842 0.3792 0.2974 0.2614  0.1101  0.0836  279 HOH   B O   
6903 O O   . HOH   E .   ? 0.2501 0.6964 0.2659 0.0505  -0.0345 -0.0632 280 HOH   B O   
6904 O O   . HOH   E .   ? 0.2387 0.3812 0.2284 0.1183  -0.0298 -0.0327 281 HOH   B O   
6905 O O   . HOH   E .   ? 0.1529 0.1505 0.1811 -0.0030 0.0002  -0.0010 282 HOH   B O   
6906 O O   . HOH   E .   ? 0.2308 0.2637 0.2720 0.0102  -0.0661 0.0120  283 HOH   B O   
6907 O O   . HOH   E .   ? 0.3140 0.5591 0.3613 -0.0367 -0.1076 0.1569  284 HOH   B O   
6908 O O   . HOH   E .   ? 0.3737 0.3588 0.4758 0.1282  -0.1019 -0.1130 285 HOH   B O   
6909 O O   . HOH   E .   ? 0.1541 0.2089 0.1559 -0.0140 -0.0212 0.0082  286 HOH   B O   
6910 O O   . HOH   E .   ? 0.2518 0.2181 0.5021 0.0040  0.0583  0.0294  287 HOH   B O   
6911 O O   . HOH   E .   ? 0.3736 0.2154 0.4048 -0.0895 -0.2040 0.0848  288 HOH   B O   
6912 O O   . HOH   E .   ? 0.1614 0.1925 0.2896 0.0202  -0.0125 0.0124  289 HOH   B O   
6913 O O   . HOH   E .   ? 0.2541 0.4552 0.4924 -0.0914 -0.1243 0.1104  290 HOH   B O   
6914 O O   . HOH   E .   ? 0.1531 0.3132 0.4495 0.0170  -0.0007 -0.1142 291 HOH   B O   
6915 O O   . HOH   E .   ? 0.3405 0.2714 0.2215 0.0079  -0.0717 -0.0144 292 HOH   B O   
6916 O O   . HOH   E .   ? 0.3018 0.2762 0.2648 -0.0239 0.0239  -0.1156 293 HOH   B O   
6917 O O   . HOH   E .   ? 0.3325 0.6525 0.2581 0.1657  -0.0388 0.0425  294 HOH   B O   
6918 O O   . HOH   E .   ? 0.4192 0.2899 0.5428 -0.0789 0.0076  0.0809  295 HOH   B O   
6919 O O   . HOH   E .   ? 0.2980 0.2639 0.5112 -0.0297 -0.0836 0.1283  296 HOH   B O   
6920 O O   . HOH   E .   ? 0.2347 0.3346 0.3947 -0.0423 -0.1156 0.0802  297 HOH   B O   
6921 O O   . HOH   E .   ? 0.1812 0.1472 0.2453 0.0057  -0.0039 0.0113  298 HOH   B O   
6922 O O   . HOH   E .   ? 0.4224 0.6050 0.2412 0.0458  -0.0305 0.1205  299 HOH   B O   
6923 O O   . HOH   E .   ? 0.3620 0.1781 0.3786 0.0755  0.1620  0.0504  300 HOH   B O   
6924 O O   . HOH   E .   ? 0.2004 0.2539 0.5645 0.0409  -0.0520 -0.0753 301 HOH   B O   
6925 O O   . HOH   E .   ? 0.1518 0.1791 0.2672 -0.0210 -0.0160 0.0035  302 HOH   B O   
6926 O O   . HOH   E .   ? 0.5406 0.3051 0.2352 -0.2022 0.0873  -0.0216 303 HOH   B O   
6927 O O   . HOH   E .   ? 0.4054 0.5160 0.5174 0.0067  -0.1319 -0.0521 304 HOH   B O   
6928 O O   . HOH   E .   ? 0.3847 0.4371 0.1973 -0.0187 0.0341  0.0406  305 HOH   B O   
6929 O O   . HOH   E .   ? 0.4420 0.3893 0.2508 0.1347  -0.0995 0.0352  306 HOH   B O   
6930 O O   . HOH   E .   ? 0.4684 0.4433 0.2431 0.1470  -0.0906 -0.0262 307 HOH   B O   
6931 O O   . HOH   E .   ? 0.2868 0.3814 0.3824 -0.1394 0.1190  -0.0885 308 HOH   B O   
6932 O O   . HOH   E .   ? 0.2301 0.1447 0.2346 -0.0185 -0.0091 0.0295  309 HOH   B O   
6933 O O   . HOH   E .   ? 0.1559 0.1469 0.2824 0.0094  -0.0019 -0.0065 310 HOH   B O   
6934 O O   . HOH   E .   ? 0.5853 0.4827 0.4575 -0.1128 -0.0229 0.0714  311 HOH   B O   
6935 O O   . HOH   E .   ? 0.2050 0.1514 0.3280 0.0383  -0.0905 -0.0090 312 HOH   B O   
6936 O O   . HOH   E .   ? 0.2079 0.1611 0.2543 -0.0254 -0.0218 -0.0066 313 HOH   B O   
6937 O O   . HOH   E .   ? 0.2514 0.2841 0.3542 -0.0415 0.0700  -0.0803 314 HOH   B O   
6938 O O   . HOH   E .   ? 0.3520 0.3722 0.6670 0.0557  -0.0076 0.1022  315 HOH   B O   
6939 O O   . HOH   E .   ? 0.4537 0.3055 0.4776 0.1024  0.2253  0.1553  316 HOH   B O   
6940 O O   . HOH   E .   ? 0.2304 0.3524 0.4532 -0.0233 -0.0492 -0.0304 317 HOH   B O   
6941 O O   . HOH   E .   ? 0.7085 0.4518 0.5113 0.1889  0.0732  -0.0033 318 HOH   B O   
6942 O O   . HOH   E .   ? 0.4097 0.2507 0.2675 0.1666  0.1060  0.0374  319 HOH   B O   
6943 O O   . HOH   E .   ? 0.2095 0.1858 0.1837 -0.0037 0.0130  0.0172  320 HOH   B O   
6944 O O   . HOH   E .   ? 0.2587 0.2089 0.2425 0.0120  -0.0236 0.0229  321 HOH   B O   
6945 O O   . HOH   E .   ? 0.1735 0.2753 0.2440 -0.0137 -0.0272 0.0707  322 HOH   B O   
6946 O O   . HOH   E .   ? 0.3338 0.3906 0.7388 -0.0140 -0.1047 0.2107  323 HOH   B O   
6947 O O   . HOH   E .   ? 0.1572 0.1616 0.2832 -0.0110 -0.0135 -0.0045 324 HOH   B O   
6948 O O   . HOH   E .   ? 0.4540 0.4455 0.2463 0.0432  -0.0447 -0.0517 325 HOH   B O   
6949 O O   . HOH   E .   ? 0.2129 0.5034 0.5156 -0.0129 0.0089  0.0444  326 HOH   B O   
6950 O O   . HOH   E .   ? 0.1993 0.2001 0.2989 0.0392  0.0414  0.0225  327 HOH   B O   
6951 O O   . HOH   E .   ? 0.7628 0.2051 0.2544 0.0384  -0.0285 0.0068  328 HOH   B O   
6952 O O   . HOH   E .   ? 0.5671 0.3204 0.3242 -0.0057 0.0935  0.1117  329 HOH   B O   
6953 O O   . HOH   E .   ? 0.2399 0.2015 0.4476 0.0094  -0.0017 0.0049  330 HOH   B O   
6954 O O   . HOH   E .   ? 0.4382 0.2507 0.2834 0.0205  0.0463  0.0868  331 HOH   B O   
6955 O O   . HOH   E .   ? 0.5818 0.5373 0.6209 0.0907  -0.1212 0.2558  332 HOH   B O   
6956 O O   . HOH   E .   ? 0.6596 0.6082 0.4861 0.2864  -0.0245 -0.0195 333 HOH   B O   
6957 O O   . HOH   E .   ? 0.4413 0.5878 0.3108 -0.0337 -0.1023 0.0338  334 HOH   B O   
6958 O O   . HOH   E .   ? 0.1730 0.2794 0.2996 0.0177  -0.0093 -0.0699 335 HOH   B O   
6959 O O   . HOH   E .   ? 0.1687 0.1394 0.2265 0.0089  -0.0262 0.0011  336 HOH   B O   
6960 O O   . HOH   E .   ? 0.5061 0.3437 0.3859 0.0234  0.0619  -0.1452 337 HOH   B O   
6961 O O   . HOH   E .   ? 0.2185 0.2323 0.5666 -0.0390 0.0136  0.1405  338 HOH   B O   
6962 O O   . HOH   E .   ? 0.4545 0.3676 0.2904 0.0827  -0.1187 -0.0786 339 HOH   B O   
6963 O O   . HOH   E .   ? 0.5497 0.4976 0.6393 -0.0945 -0.0475 -0.1069 340 HOH   B O   
6964 O O   . HOH   E .   ? 0.4093 0.7250 0.3694 -0.0786 -0.0485 0.2261  341 HOH   B O   
6965 O O   . HOH   E .   ? 0.4054 0.6033 0.3762 -0.0913 -0.0860 -0.0942 342 HOH   B O   
6966 O O   . HOH   E .   ? 0.2511 0.5757 0.6321 0.0333  -0.1234 0.0487  343 HOH   B O   
6967 O O   . HOH   E .   ? 0.2076 0.1956 0.3298 -0.0120 0.0535  -0.0066 344 HOH   B O   
6968 O O   . HOH   E .   ? 0.6512 0.6383 0.2951 -0.0441 -0.1013 0.1276  345 HOH   B O   
6969 O O   . HOH   E .   ? 0.4411 0.4796 0.4597 -0.0057 -0.0989 0.0798  346 HOH   B O   
6970 O O   . HOH   E .   ? 0.2445 0.5781 0.3894 0.1604  -0.0438 -0.1467 347 HOH   B O   
6971 O O   . HOH   E .   ? 0.2806 0.2172 0.5009 -0.0191 -0.1040 -0.0536 348 HOH   B O   
6972 O O   . HOH   E .   ? 0.4398 0.6151 0.6534 0.0497  0.0143  -0.0959 349 HOH   B O   
6973 O O   . HOH   E .   ? 0.2054 0.4318 0.5150 0.0416  0.0157  0.0441  350 HOH   B O   
6974 O O   . HOH   E .   ? 0.5366 0.5829 0.4925 -0.1272 0.0128  0.1285  351 HOH   B O   
6975 O O   . HOH   E .   ? 0.3333 0.4949 0.4219 -0.1746 0.0291  -0.0210 352 HOH   B O   
6976 O O   . HOH   E .   ? 0.3791 0.2289 0.3301 -0.0832 0.0025  -0.0806 353 HOH   B O   
6977 O O   . HOH   E .   ? 0.5051 0.3643 0.4121 0.0933  0.1153  -0.0393 354 HOH   B O   
6978 O O   . HOH   E .   ? 0.4155 0.2807 0.5132 -0.0944 0.0829  0.0891  355 HOH   B O   
6979 O O   . HOH   E .   ? 0.3854 0.2869 0.3901 -0.1157 -0.0237 -0.0496 356 HOH   B O   
6980 O O   . HOH   E .   ? 0.3200 0.1840 0.3806 0.0538  -0.1207 -0.0481 357 HOH   B O   
6981 O O   . HOH   E .   ? 0.4582 0.5277 0.4495 -0.0701 0.0078  -0.0238 358 HOH   B O   
6982 O O   . HOH   E .   ? 0.4864 0.3242 0.4719 0.0165  -0.1552 -0.0298 359 HOH   B O   
6983 O O   . HOH   E .   ? 0.4550 0.5149 0.5380 0.1769  -0.1246 0.1526  360 HOH   B O   
6984 O O   . HOH   E .   ? 0.4389 0.3617 0.6862 0.0239  0.0719  0.1044  361 HOH   B O   
6985 O O   . HOH   E .   ? 0.4511 0.6604 0.3106 0.1973  -0.0032 0.0755  362 HOH   B O   
6986 O O   . HOH   E .   ? 0.1989 0.3737 0.6122 -0.0590 -0.0644 -0.0943 363 HOH   B O   
6987 O O   . HOH   E .   ? 0.6342 0.4107 0.4313 0.0721  0.1183  0.0343  364 HOH   B O   
6988 O O   . HOH   E .   ? 0.5015 0.2861 0.5629 -0.1277 -0.0397 0.0147  365 HOH   B O   
6989 O O   . HOH   E .   ? 0.4591 0.4790 0.4606 -0.0054 -0.0784 -0.1136 366 HOH   B O   
6990 O O   . HOH   E .   ? 0.6322 0.5169 0.3305 0.1986  -0.1441 0.0301  367 HOH   B O   
6991 O O   . HOH   E .   ? 0.6055 0.4119 0.5351 0.0450  -0.1523 0.0327  368 HOH   B O   
6992 O O   . HOH   E .   ? 0.6544 0.3876 0.3133 -0.1344 -0.0922 -0.0484 369 HOH   B O   
6993 O O   . HOH   E .   ? 0.4966 0.5249 0.5470 0.2357  0.1250  0.1310  370 HOH   B O   
6994 O O   . HOH   E .   ? 0.6472 0.2155 0.3761 -0.0134 -0.0121 0.0730  371 HOH   B O   
6995 O O   . HOH   E .   ? 0.4660 0.4670 0.4995 -0.0790 -0.0831 0.0681  372 HOH   B O   
6996 O O   . HOH   E .   ? 0.7777 0.7522 0.5299 0.2234  -0.1374 0.1045  373 HOH   B O   
6997 O O   . HOH   E .   ? 0.3684 0.3604 0.4423 0.0781  -0.1359 -0.0820 374 HOH   B O   
6998 O O   . HOH   E .   ? 0.4959 0.6749 0.5647 0.1704  0.0919  0.2723  375 HOH   B O   
6999 O O   . HOH   E .   ? 0.2397 0.4143 0.4426 0.0382  -0.0776 -0.0733 376 HOH   B O   
7000 O O   . HOH   E .   ? 0.3244 0.4639 0.2253 0.0959  0.0388  0.0512  377 HOH   B O   
7001 O O   . HOH   E .   ? 0.6877 0.3499 0.5425 -0.0721 -0.0554 -0.0106 378 HOH   B O   
7002 O O   . HOH   E .   ? 0.5287 0.7343 0.3805 -0.1277 0.0130  -0.1417 379 HOH   B O   
7003 O O   . HOH   E .   ? 0.4268 0.5572 0.4716 0.0994  0.0421  0.0256  380 HOH   B O   
7004 O O   . HOH   E .   ? 0.5120 0.7101 0.6092 0.0308  0.2477  0.1398  381 HOH   B O   
7005 O O   . HOH   E .   ? 0.2938 0.2564 0.3043 -0.0061 0.0182  0.0487  382 HOH   B O   
7006 O O   . HOH   E .   ? 0.3935 0.7694 0.5522 0.1344  0.1548  0.1224  383 HOH   B O   
7007 O O   . HOH   E .   ? 0.6693 0.5767 0.4012 0.1879  0.0659  0.0985  384 HOH   B O   
7008 O O   . HOH   E .   ? 0.5619 0.4669 0.4040 -0.0151 -0.0513 -0.0186 385 HOH   B O   
7009 O O   . HOH   E .   ? 0.4375 0.3449 0.3036 -0.0111 0.0055  -0.0176 386 HOH   B O   
7010 O O   . HOH   E .   ? 0.2455 0.3987 0.3670 -0.0768 -0.1078 -0.0223 387 HOH   B O   
7011 O O   . HOH   E .   ? 0.7479 0.3388 0.4299 -0.0110 0.0621  -0.1176 388 HOH   B O   
7012 O O   . HOH   E .   ? 0.5719 0.4480 0.5013 -0.0962 0.0213  -0.0476 389 HOH   B O   
7013 O O   . HOH   E .   ? 0.3706 0.2207 0.3230 0.0700  -0.0397 0.0161  390 HOH   B O   
7014 O O   . HOH   E .   ? 0.5154 0.3823 0.3559 -0.0116 0.0518  0.0294  391 HOH   B O   
7015 O O   . HOH   E .   ? 0.2332 0.5122 0.6056 -0.1400 -0.0842 0.0037  392 HOH   B O   
7016 O O   . HOH   E .   ? 0.3971 0.2220 0.5409 -0.0177 0.0918  0.0413  393 HOH   B O   
7017 O O   . HOH   E .   ? 0.4821 0.5855 0.3632 0.1479  -0.0036 -0.1063 394 HOH   B O   
7018 O O   . HOH   E .   ? 0.3976 0.4853 0.4033 -0.0467 0.0734  0.0504  395 HOH   B O   
7019 O O   . HOH   E .   ? 0.2212 0.2881 0.5595 -0.0530 -0.1011 0.0029  396 HOH   B O   
7020 O O   . HOH   E .   ? 0.3077 0.3652 0.3590 0.0473  -0.0028 -0.0527 397 HOH   B O   
7021 O O   . HOH   E .   ? 0.5295 0.6028 0.7318 0.1265  -0.0960 0.2445  398 HOH   B O   
7022 O O   . HOH   E .   ? 0.6433 0.4502 0.3303 -0.1985 0.0060  0.1476  399 HOH   B O   
7023 O O   . HOH   E .   ? 0.5932 0.6123 0.3709 0.1988  -0.0536 0.0141  400 HOH   B O   
# 
