data_7HEB
# 
_entry.id   7HEB 
# 
_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   7HEB         pdb_00007heb 10.2210/pdb7heb/pdb 
WWPDB D_1001407365 ?            ?                   
# 
_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                        7HEB 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                            18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 
'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                114.023   1   ?                      ? ? ? 
3 non-polymer syn '(3R)-2-methyl-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-2-ol' 234.298   1   ?                      ? ? ? 
4 water       nat water                                                                 18.015    421 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                TFA   
3 '(3R)-2-methyl-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-2-ol' A1A9N 
4 water                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A9N non-polymer         . '(3R)-2-methyl-3-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pentan-2-ol' ? 'C12 H18 N4 O'   234.298 
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 
TFA   non-polymer         . 'trifluoroacetic acid'                                                ? 'C2 H F3 O2'     114.023 
THR   'L-peptide linking' y THREONINE                                                             ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                              ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A9N 1   202 201  A1A9N LA1 A . 
E 4 HOH   1   301 292  HOH   HOH A . 
E 4 HOH   2   302 196  HOH   HOH A . 
E 4 HOH   3   303 625  HOH   HOH A . 
E 4 HOH   4   304 493  HOH   HOH A . 
E 4 HOH   5   305 1289 HOH   HOH A . 
E 4 HOH   6   306 281  HOH   HOH A . 
E 4 HOH   7   307 11   HOH   HOH A . 
E 4 HOH   8   308 229  HOH   HOH A . 
E 4 HOH   9   309 136  HOH   HOH A . 
E 4 HOH   10  310 153  HOH   HOH A . 
E 4 HOH   11  311 209  HOH   HOH A . 
E 4 HOH   12  312 409  HOH   HOH A . 
E 4 HOH   13  313 109  HOH   HOH A . 
E 4 HOH   14  314 236  HOH   HOH A . 
E 4 HOH   15  315 76   HOH   HOH A . 
E 4 HOH   16  316 1301 HOH   HOH A . 
E 4 HOH   17  317 124  HOH   HOH A . 
E 4 HOH   18  318 1275 HOH   HOH A . 
E 4 HOH   19  319 661  HOH   HOH A . 
E 4 HOH   20  320 337  HOH   HOH A . 
E 4 HOH   21  321 4    HOH   HOH A . 
E 4 HOH   22  322 1283 HOH   HOH A . 
E 4 HOH   23  323 151  HOH   HOH A . 
E 4 HOH   24  324 1295 HOH   HOH A . 
E 4 HOH   25  325 21   HOH   HOH A . 
E 4 HOH   26  326 192  HOH   HOH A . 
E 4 HOH   27  327 662  HOH   HOH A . 
E 4 HOH   28  328 15   HOH   HOH A . 
E 4 HOH   29  329 225  HOH   HOH A . 
E 4 HOH   30  330 39   HOH   HOH A . 
E 4 HOH   31  331 8    HOH   HOH A . 
E 4 HOH   32  332 405  HOH   HOH A . 
E 4 HOH   33  333 1300 HOH   HOH A . 
E 4 HOH   34  334 241  HOH   HOH A . 
E 4 HOH   35  335 140  HOH   HOH A . 
E 4 HOH   36  336 164  HOH   HOH A . 
E 4 HOH   37  337 18   HOH   HOH A . 
E 4 HOH   38  338 17   HOH   HOH A . 
E 4 HOH   39  339 1290 HOH   HOH A . 
E 4 HOH   40  340 165  HOH   HOH A . 
E 4 HOH   41  341 964  HOH   HOH A . 
E 4 HOH   42  342 105  HOH   HOH A . 
E 4 HOH   43  343 320  HOH   HOH A . 
E 4 HOH   44  344 57   HOH   HOH A . 
E 4 HOH   45  345 469  HOH   HOH A . 
E 4 HOH   46  346 24   HOH   HOH A . 
E 4 HOH   47  347 630  HOH   HOH A . 
E 4 HOH   48  348 393  HOH   HOH A . 
E 4 HOH   49  349 155  HOH   HOH A . 
E 4 HOH   50  350 93   HOH   HOH A . 
E 4 HOH   51  351 92   HOH   HOH A . 
E 4 HOH   52  352 354  HOH   HOH A . 
E 4 HOH   53  353 86   HOH   HOH A . 
E 4 HOH   54  354 33   HOH   HOH A . 
E 4 HOH   55  355 42   HOH   HOH A . 
E 4 HOH   56  356 36   HOH   HOH A . 
E 4 HOH   57  357 247  HOH   HOH A . 
E 4 HOH   58  358 2    HOH   HOH A . 
E 4 HOH   59  359 169  HOH   HOH A . 
E 4 HOH   60  360 26   HOH   HOH A . 
E 4 HOH   61  361 396  HOH   HOH A . 
E 4 HOH   62  362 66   HOH   HOH A . 
E 4 HOH   63  363 19   HOH   HOH A . 
E 4 HOH   64  364 139  HOH   HOH A . 
E 4 HOH   65  365 49   HOH   HOH A . 
E 4 HOH   66  366 939  HOH   HOH A . 
E 4 HOH   67  367 162  HOH   HOH A . 
E 4 HOH   68  368 159  HOH   HOH A . 
E 4 HOH   69  369 5    HOH   HOH A . 
E 4 HOH   70  370 102  HOH   HOH A . 
E 4 HOH   71  371 45   HOH   HOH A . 
E 4 HOH   72  372 138  HOH   HOH A . 
E 4 HOH   73  373 46   HOH   HOH A . 
E 4 HOH   74  374 56   HOH   HOH A . 
E 4 HOH   75  375 81   HOH   HOH A . 
E 4 HOH   76  376 134  HOH   HOH A . 
E 4 HOH   77  377 154  HOH   HOH A . 
E 4 HOH   78  378 186  HOH   HOH A . 
E 4 HOH   79  379 34   HOH   HOH A . 
E 4 HOH   80  380 148  HOH   HOH A . 
E 4 HOH   81  381 218  HOH   HOH A . 
E 4 HOH   82  382 1    HOH   HOH A . 
E 4 HOH   83  383 296  HOH   HOH A . 
E 4 HOH   84  384 27   HOH   HOH A . 
E 4 HOH   85  385 140  HOH   HOH A . 
E 4 HOH   86  386 461  HOH   HOH A . 
E 4 HOH   87  387 35   HOH   HOH A . 
E 4 HOH   88  388 115  HOH   HOH A . 
E 4 HOH   89  389 366  HOH   HOH A . 
E 4 HOH   90  390 58   HOH   HOH A . 
E 4 HOH   91  391 1308 HOH   HOH A . 
E 4 HOH   92  392 116  HOH   HOH A . 
E 4 HOH   93  393 6    HOH   HOH A . 
E 4 HOH   94  394 83   HOH   HOH A . 
E 4 HOH   95  395 132  HOH   HOH A . 
E 4 HOH   96  396 96   HOH   HOH A . 
E 4 HOH   97  397 85   HOH   HOH A . 
E 4 HOH   98  398 74   HOH   HOH A . 
E 4 HOH   99  399 351  HOH   HOH A . 
E 4 HOH   100 400 67   HOH   HOH A . 
E 4 HOH   101 401 303  HOH   HOH A . 
E 4 HOH   102 402 12   HOH   HOH A . 
E 4 HOH   103 403 199  HOH   HOH A . 
E 4 HOH   104 404 1315 HOH   HOH A . 
E 4 HOH   105 405 3    HOH   HOH A . 
E 4 HOH   106 406 195  HOH   HOH A . 
E 4 HOH   107 407 1068 HOH   HOH A . 
E 4 HOH   108 408 3    HOH   HOH A . 
E 4 HOH   109 409 25   HOH   HOH A . 
E 4 HOH   110 410 156  HOH   HOH A . 
E 4 HOH   111 411 68   HOH   HOH A . 
E 4 HOH   112 412 123  HOH   HOH A . 
E 4 HOH   113 413 121  HOH   HOH A . 
E 4 HOH   114 414 125  HOH   HOH A . 
E 4 HOH   115 415 53   HOH   HOH A . 
E 4 HOH   116 416 278  HOH   HOH A . 
E 4 HOH   117 417 122  HOH   HOH A . 
E 4 HOH   118 418 397  HOH   HOH A . 
E 4 HOH   119 419 4    HOH   HOH A . 
E 4 HOH   120 420 95   HOH   HOH A . 
E 4 HOH   121 421 381  HOH   HOH A . 
E 4 HOH   122 422 582  HOH   HOH A . 
E 4 HOH   123 423 1310 HOH   HOH A . 
E 4 HOH   124 424 1279 HOH   HOH A . 
E 4 HOH   125 425 51   HOH   HOH A . 
E 4 HOH   126 426 1313 HOH   HOH A . 
E 4 HOH   127 427 333  HOH   HOH A . 
E 4 HOH   128 428 1309 HOH   HOH A . 
E 4 HOH   129 429 70   HOH   HOH A . 
E 4 HOH   130 430 1222 HOH   HOH A . 
E 4 HOH   131 431 78   HOH   HOH A . 
E 4 HOH   132 432 7    HOH   HOH A . 
E 4 HOH   133 433 1189 HOH   HOH A . 
E 4 HOH   134 434 71   HOH   HOH A . 
E 4 HOH   135 435 6    HOH   HOH A . 
E 4 HOH   136 436 212  HOH   HOH A . 
E 4 HOH   137 437 80   HOH   HOH A . 
E 4 HOH   138 438 7    HOH   HOH A . 
E 4 HOH   139 439 73   HOH   HOH A . 
E 4 HOH   140 440 40   HOH   HOH A . 
E 4 HOH   141 441 952  HOH   HOH A . 
E 4 HOH   142 442 1286 HOH   HOH A . 
E 4 HOH   143 443 94   HOH   HOH A . 
E 4 HOH   144 444 944  HOH   HOH A . 
E 4 HOH   145 445 1238 HOH   HOH A . 
E 4 HOH   146 446 97   HOH   HOH A . 
E 4 HOH   147 447 188  HOH   HOH A . 
E 4 HOH   148 448 79   HOH   HOH A . 
E 4 HOH   149 449 1296 HOH   HOH A . 
E 4 HOH   150 450 104  HOH   HOH A . 
E 4 HOH   151 451 576  HOH   HOH A . 
E 4 HOH   152 452 16   HOH   HOH A . 
E 4 HOH   153 453 1134 HOH   HOH A . 
E 4 HOH   154 454 330  HOH   HOH A . 
E 4 HOH   155 455 1119 HOH   HOH A . 
E 4 HOH   156 456 1094 HOH   HOH A . 
E 4 HOH   157 457 509  HOH   HOH A . 
E 4 HOH   158 458 107  HOH   HOH A . 
E 4 HOH   159 459 163  HOH   HOH A . 
E 4 HOH   160 460 726  HOH   HOH A . 
E 4 HOH   161 461 408  HOH   HOH A . 
E 4 HOH   162 462 2    HOH   HOH A . 
E 4 HOH   163 463 756  HOH   HOH A . 
E 4 HOH   164 464 361  HOH   HOH A . 
E 4 HOH   165 465 126  HOH   HOH A . 
E 4 HOH   166 466 319  HOH   HOH A . 
E 4 HOH   167 467 280  HOH   HOH A . 
E 4 HOH   168 468 556  HOH   HOH A . 
E 4 HOH   169 469 801  HOH   HOH A . 
E 4 HOH   170 470 250  HOH   HOH A . 
E 4 HOH   171 471 1307 HOH   HOH A . 
E 4 HOH   172 472 63   HOH   HOH A . 
E 4 HOH   173 473 1276 HOH   HOH A . 
E 4 HOH   174 474 267  HOH   HOH A . 
E 4 HOH   175 475 342  HOH   HOH A . 
E 4 HOH   176 476 370  HOH   HOH A . 
E 4 HOH   177 477 135  HOH   HOH A . 
E 4 HOH   178 478 224  HOH   HOH A . 
E 4 HOH   179 479 1306 HOH   HOH A . 
E 4 HOH   180 480 521  HOH   HOH A . 
E 4 HOH   181 481 1287 HOH   HOH A . 
E 4 HOH   182 482 695  HOH   HOH A . 
E 4 HOH   183 483 326  HOH   HOH A . 
E 4 HOH   184 484 5    HOH   HOH A . 
E 4 HOH   185 485 919  HOH   HOH A . 
E 4 HOH   186 486 674  HOH   HOH A . 
E 4 HOH   187 487 202  HOH   HOH A . 
E 4 HOH   188 488 1314 HOH   HOH A . 
E 4 HOH   189 489 309  HOH   HOH A . 
E 4 HOH   190 490 318  HOH   HOH A . 
E 4 HOH   191 491 315  HOH   HOH A . 
E 4 HOH   192 492 1299 HOH   HOH A . 
E 4 HOH   193 493 805  HOH   HOH A . 
E 4 HOH   194 494 331  HOH   HOH A . 
E 4 HOH   195 495 711  HOH   HOH A . 
E 4 HOH   196 496 12   HOH   HOH A . 
E 4 HOH   197 497 941  HOH   HOH A . 
E 4 HOH   198 498 356  HOH   HOH A . 
E 4 HOH   199 499 263  HOH   HOH A . 
E 4 HOH   200 500 152  HOH   HOH A . 
E 4 HOH   201 501 208  HOH   HOH A . 
E 4 HOH   202 502 1071 HOH   HOH A . 
E 4 HOH   203 503 1284 HOH   HOH A . 
E 4 HOH   204 504 180  HOH   HOH A . 
E 4 HOH   205 505 350  HOH   HOH A . 
E 4 HOH   206 506 363  HOH   HOH A . 
E 4 HOH   207 507 313  HOH   HOH A . 
E 4 HOH   208 508 371  HOH   HOH A . 
E 4 HOH   209 509 8    HOH   HOH A . 
E 4 HOH   210 510 9    HOH   HOH A . 
E 4 HOH   211 511 185  HOH   HOH A . 
E 4 HOH   212 512 429  HOH   HOH A . 
E 4 HOH   213 513 70   HOH   HOH A . 
E 4 HOH   214 514 376  HOH   HOH A . 
E 4 HOH   215 515 772  HOH   HOH A . 
E 4 HOH   216 516 1074 HOH   HOH A . 
E 4 HOH   217 517 10   HOH   HOH A . 
E 4 HOH   218 518 346  HOH   HOH A . 
E 4 HOH   219 519 1292 HOH   HOH A . 
E 4 HOH   220 520 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 549  HOH   HOH B . 
F 4 HOH   3   203 358  HOH   HOH B . 
F 4 HOH   4   204 900  HOH   HOH B . 
F 4 HOH   5   205 654  HOH   HOH B . 
F 4 HOH   6   206 758  HOH   HOH B . 
F 4 HOH   7   207 364  HOH   HOH B . 
F 4 HOH   8   208 398  HOH   HOH B . 
F 4 HOH   9   209 531  HOH   HOH B . 
F 4 HOH   10  210 240  HOH   HOH B . 
F 4 HOH   11  211 1249 HOH   HOH B . 
F 4 HOH   12  212 743  HOH   HOH B . 
F 4 HOH   13  213 232  HOH   HOH B . 
F 4 HOH   14  214 120  HOH   HOH B . 
F 4 HOH   15  215 50   HOH   HOH B . 
F 4 HOH   16  216 452  HOH   HOH B . 
F 4 HOH   17  217 264  HOH   HOH B . 
F 4 HOH   18  218 353  HOH   HOH B . 
F 4 HOH   19  219 332  HOH   HOH B . 
F 4 HOH   20  220 343  HOH   HOH B . 
F 4 HOH   21  221 444  HOH   HOH B . 
F 4 HOH   22  222 131  HOH   HOH B . 
F 4 HOH   23  223 1140 HOH   HOH B . 
F 4 HOH   24  224 282  HOH   HOH B . 
F 4 HOH   25  225 1278 HOH   HOH B . 
F 4 HOH   26  226 75   HOH   HOH B . 
F 4 HOH   27  227 54   HOH   HOH B . 
F 4 HOH   28  228 300  HOH   HOH B . 
F 4 HOH   29  229 110  HOH   HOH B . 
F 4 HOH   30  230 276  HOH   HOH B . 
F 4 HOH   31  231 272  HOH   HOH B . 
F 4 HOH   32  232 1312 HOH   HOH B . 
F 4 HOH   33  233 82   HOH   HOH B . 
F 4 HOH   34  234 60   HOH   HOH B . 
F 4 HOH   35  235 205  HOH   HOH B . 
F 4 HOH   36  236 723  HOH   HOH B . 
F 4 HOH   37  237 1    HOH   HOH B . 
F 4 HOH   38  238 166  HOH   HOH B . 
F 4 HOH   39  239 127  HOH   HOH B . 
F 4 HOH   40  240 14   HOH   HOH B . 
F 4 HOH   41  241 325  HOH   HOH B . 
F 4 HOH   42  242 181  HOH   HOH B . 
F 4 HOH   43  243 69   HOH   HOH B . 
F 4 HOH   44  244 128  HOH   HOH B . 
F 4 HOH   45  245 9    HOH   HOH B . 
F 4 HOH   46  246 30   HOH   HOH B . 
F 4 HOH   47  247 52   HOH   HOH B . 
F 4 HOH   48  248 133  HOH   HOH B . 
F 4 HOH   49  249 144  HOH   HOH B . 
F 4 HOH   50  250 252  HOH   HOH B . 
F 4 HOH   51  251 172  HOH   HOH B . 
F 4 HOH   52  252 129  HOH   HOH B . 
F 4 HOH   53  253 231  HOH   HOH B . 
F 4 HOH   54  254 391  HOH   HOH B . 
F 4 HOH   55  255 103  HOH   HOH B . 
F 4 HOH   56  256 31   HOH   HOH B . 
F 4 HOH   57  257 271  HOH   HOH B . 
F 4 HOH   58  258 143  HOH   HOH B . 
F 4 HOH   59  259 47   HOH   HOH B . 
F 4 HOH   60  260 41   HOH   HOH B . 
F 4 HOH   61  261 62   HOH   HOH B . 
F 4 HOH   62  262 150  HOH   HOH B . 
F 4 HOH   63  263 72   HOH   HOH B . 
F 4 HOH   64  264 61   HOH   HOH B . 
F 4 HOH   65  265 10   HOH   HOH B . 
F 4 HOH   66  266 347  HOH   HOH B . 
F 4 HOH   67  267 302  HOH   HOH B . 
F 4 HOH   68  268 1277 HOH   HOH B . 
F 4 HOH   69  269 117  HOH   HOH B . 
F 4 HOH   70  270 11   HOH   HOH B . 
F 4 HOH   71  271 242  HOH   HOH B . 
F 4 HOH   72  272 59   HOH   HOH B . 
F 4 HOH   73  273 20   HOH   HOH B . 
F 4 HOH   74  274 147  HOH   HOH B . 
F 4 HOH   75  275 287  HOH   HOH B . 
F 4 HOH   76  276 84   HOH   HOH B . 
F 4 HOH   77  277 243  HOH   HOH B . 
F 4 HOH   78  278 221  HOH   HOH B . 
F 4 HOH   79  279 114  HOH   HOH B . 
F 4 HOH   80  280 43   HOH   HOH B . 
F 4 HOH   81  281 77   HOH   HOH B . 
F 4 HOH   82  282 1106 HOH   HOH B . 
F 4 HOH   83  283 299  HOH   HOH B . 
F 4 HOH   84  284 175  HOH   HOH B . 
F 4 HOH   85  285 1305 HOH   HOH B . 
F 4 HOH   86  286 22   HOH   HOH B . 
F 4 HOH   87  287 216  HOH   HOH B . 
F 4 HOH   88  288 387  HOH   HOH B . 
F 4 HOH   89  289 1066 HOH   HOH B . 
F 4 HOH   90  290 13   HOH   HOH B . 
F 4 HOH   91  291 106  HOH   HOH B . 
F 4 HOH   92  292 89   HOH   HOH B . 
F 4 HOH   93  293 137  HOH   HOH B . 
F 4 HOH   94  294 311  HOH   HOH B . 
F 4 HOH   95  295 235  HOH   HOH B . 
F 4 HOH   96  296 99   HOH   HOH B . 
F 4 HOH   97  297 88   HOH   HOH B . 
F 4 HOH   98  298 416  HOH   HOH B . 
F 4 HOH   99  299 220  HOH   HOH B . 
F 4 HOH   100 300 635  HOH   HOH B . 
F 4 HOH   101 301 160  HOH   HOH B . 
F 4 HOH   102 302 142  HOH   HOH B . 
F 4 HOH   103 303 112  HOH   HOH B . 
F 4 HOH   104 304 316  HOH   HOH B . 
F 4 HOH   105 305 297  HOH   HOH B . 
F 4 HOH   106 306 118  HOH   HOH B . 
F 4 HOH   107 307 101  HOH   HOH B . 
F 4 HOH   108 308 32   HOH   HOH B . 
F 4 HOH   109 309 48   HOH   HOH B . 
F 4 HOH   110 310 215  HOH   HOH B . 
F 4 HOH   111 311 341  HOH   HOH B . 
F 4 HOH   112 312 37   HOH   HOH B . 
F 4 HOH   113 313 170  HOH   HOH B . 
F 4 HOH   114 314 38   HOH   HOH B . 
F 4 HOH   115 315 1274 HOH   HOH B . 
F 4 HOH   116 316 1285 HOH   HOH B . 
F 4 HOH   117 317 23   HOH   HOH B . 
F 4 HOH   118 318 1291 HOH   HOH B . 
F 4 HOH   119 319 177  HOH   HOH B . 
F 4 HOH   120 320 91   HOH   HOH B . 
F 4 HOH   121 321 704  HOH   HOH B . 
F 4 HOH   122 322 1294 HOH   HOH B . 
F 4 HOH   123 323 28   HOH   HOH B . 
F 4 HOH   124 324 161  HOH   HOH B . 
F 4 HOH   125 325 44   HOH   HOH B . 
F 4 HOH   126 326 197  HOH   HOH B . 
F 4 HOH   127 327 29   HOH   HOH B . 
F 4 HOH   128 328 100  HOH   HOH B . 
F 4 HOH   129 329 141  HOH   HOH B . 
F 4 HOH   130 330 182  HOH   HOH B . 
F 4 HOH   131 331 334  HOH   HOH B . 
F 4 HOH   132 332 1126 HOH   HOH B . 
F 4 HOH   133 333 207  HOH   HOH B . 
F 4 HOH   134 334 55   HOH   HOH B . 
F 4 HOH   135 335 98   HOH   HOH B . 
F 4 HOH   136 336 717  HOH   HOH B . 
F 4 HOH   137 337 445  HOH   HOH B . 
F 4 HOH   138 338 339  HOH   HOH B . 
F 4 HOH   139 339 234  HOH   HOH B . 
F 4 HOH   140 340 65   HOH   HOH B . 
F 4 HOH   141 341 619  HOH   HOH B . 
F 4 HOH   142 342 1293 HOH   HOH B . 
F 4 HOH   143 343 362  HOH   HOH B . 
F 4 HOH   144 344 178  HOH   HOH B . 
F 4 HOH   145 345 90   HOH   HOH B . 
F 4 HOH   146 346 960  HOH   HOH B . 
F 4 HOH   147 347 335  HOH   HOH B . 
F 4 HOH   148 348 1304 HOH   HOH B . 
F 4 HOH   149 349 623  HOH   HOH B . 
F 4 HOH   150 350 463  HOH   HOH B . 
F 4 HOH   151 351 191  HOH   HOH B . 
F 4 HOH   152 352 1046 HOH   HOH B . 
F 4 HOH   153 353 87   HOH   HOH B . 
F 4 HOH   154 354 304  HOH   HOH B . 
F 4 HOH   155 355 1280 HOH   HOH B . 
F 4 HOH   156 356 203  HOH   HOH B . 
F 4 HOH   157 357 541  HOH   HOH B . 
F 4 HOH   158 358 290  HOH   HOH B . 
F 4 HOH   159 359 479  HOH   HOH B . 
F 4 HOH   160 360 389  HOH   HOH B . 
F 4 HOH   161 361 1077 HOH   HOH B . 
F 4 HOH   162 362 718  HOH   HOH B . 
F 4 HOH   163 363 1072 HOH   HOH B . 
F 4 HOH   164 364 283  HOH   HOH B . 
F 4 HOH   165 365 1316 HOH   HOH B . 
F 4 HOH   166 366 291  HOH   HOH B . 
F 4 HOH   167 367 898  HOH   HOH B . 
F 4 HOH   168 368 373  HOH   HOH B . 
F 4 HOH   169 369 615  HOH   HOH B . 
F 4 HOH   170 370 340  HOH   HOH B . 
F 4 HOH   171 371 190  HOH   HOH B . 
F 4 HOH   172 372 667  HOH   HOH B . 
F 4 HOH   173 373 1303 HOH   HOH B . 
F 4 HOH   174 374 310  HOH   HOH B . 
F 4 HOH   175 375 431  HOH   HOH B . 
F 4 HOH   176 376 149  HOH   HOH B . 
F 4 HOH   177 377 1173 HOH   HOH B . 
F 4 HOH   178 378 183  HOH   HOH B . 
F 4 HOH   179 379 1000 HOH   HOH B . 
F 4 HOH   180 380 1163 HOH   HOH B . 
F 4 HOH   181 381 418  HOH   HOH B . 
F 4 HOH   182 382 1311 HOH   HOH B . 
F 4 HOH   183 383 176  HOH   HOH B . 
F 4 HOH   184 384 424  HOH   HOH B . 
F 4 HOH   185 385 981  HOH   HOH B . 
F 4 HOH   186 386 491  HOH   HOH B . 
F 4 HOH   187 387 470  HOH   HOH B . 
F 4 HOH   188 388 248  HOH   HOH B . 
F 4 HOH   189 389 1298 HOH   HOH B . 
F 4 HOH   190 390 265  HOH   HOH B . 
F 4 HOH   191 391 184  HOH   HOH B . 
F 4 HOH   192 392 360  HOH   HOH B . 
F 4 HOH   193 393 355  HOH   HOH B . 
F 4 HOH   194 394 410  HOH   HOH B . 
F 4 HOH   195 395 274  HOH   HOH B . 
F 4 HOH   196 396 566  HOH   HOH B . 
F 4 HOH   197 397 314  HOH   HOH B . 
F 4 HOH   198 398 157  HOH   HOH B . 
F 4 HOH   199 399 321  HOH   HOH B . 
F 4 HOH   200 400 792  HOH   HOH B . 
F 4 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HEB 
_cell.length_a           88.762 
_cell.length_b           88.762 
_cell.length_c           39.563 
_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                         7HEB 
_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          7HEB 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.71 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HEB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.380 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165601 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.041 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.000 
_reflns.B_iso_Wilson_estimate        11.830 
_reflns.pdbx_redundancy              6.300 
_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     1049503 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 34863 7639 ? 1.145 ? ? ? 4.600 ? 0.900  ? ? ? ? ? ? 92.800 1.294 0.585 0.671 
1 2 5.480 44.380 ? 7494  1096 ? 0.024 ? ? ? 6.800 ? 59.000 ? ? ? ? ? ? 99.900 0.026 0.010 1.000 
# 
_refine.entry_id                                 7HEB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3800 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5400 
_refine.ls_number_reflns_obs                     165500 
_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                          0.1472 
_refine.ls_R_factor_R_work                       0.1465 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1611 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7986 
_refine.ls_number_reflns_R_work                  157514 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.9622 
_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                            0.1000 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                63.580 
_refine.B_iso_min                                8.580 
_refine.pdbx_overall_phase_error                 18.1500 
_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                        44.3800 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             421 
_refine_hist.number_atoms_total               3005 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           20.16 
_refine_hist.pdbx_B_iso_mean_solvent          29.92 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 91.0000  4779 . 0.3888 0.3346 . 249 0.0000 5028 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 98.0000  5191 . 0.3253 0.3310 . 232 0.0000 5423 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5218 . 0.2827 0.3093 . 252 0.0000 5470 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5198 . 0.2513 0.2527 . 277 0.0000 5475 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5200 . 0.2280 0.2498 . 319 0.0000 5519 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5253 . 0.2178 0.2339 . 256 0.0000 5509 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5275 . 0.1929 0.2136 . 262 0.0000 5537 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5239 . 0.1786 0.1951 . 255 0.0000 5494 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5227 . 0.1656 0.1864 . 280 0.0000 5507 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5273 . 0.1514 0.1670 . 239 0.0000 5512 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5273 . 0.1440 0.1661 . 252 0.0000 5525 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5270 . 0.1370 0.1501 . 280 0.0000 5550 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5178 . 0.1297 0.1675 . 287 0.0000 5465 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5325 . 0.1268 0.1453 . 235 0.0000 5560 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5188 . 0.1283 0.1428 . 262 0.0000 5450 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5288 . 0.1286 0.1547 . 272 0.0000 5560 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5258 . 0.1277 0.1457 . 284 0.0000 5542 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5213 . 0.1342 0.1474 . 274 0.0000 5487 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5284 . 0.1315 0.1677 . 252 0.0000 5536 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5261 . 0.1298 0.1590 . 266 0.0000 5527 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5308 . 0.1236 0.1310 . 255 0.0000 5563 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5220 . 0.1188 0.1292 . 278 0.0000 5498 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5294 . 0.1200 0.1354 . 259 0.0000 5553 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5320 . 0.1264 0.1463 . 272 0.0000 5592 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5281 . 0.1374 0.1459 . 250 0.0000 5531 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5278 . 0.1358 0.1428 . 281 0.0000 5559 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5297 . 0.1405 0.1449 . 285 0.0000 5582 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5305 . 0.1393 0.1457 . 291 0.0000 5596 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5330 . 0.1514 0.1727 . 260 0.0000 5590 . 'X-RAY DIFFRACTION' 
3.1100 44.3800 30 100.0000 5490 . 0.1516 0.1706 . 270 0.0000 5760 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEB 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003667' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEB 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HEB A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEB 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 7HEB SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEB MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEB SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEB MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    209 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    326 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.60 
# 
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  ? ? 55.57 -133.18 
2 1 SER A 128 ? B 70.78 -5.27   
3 1 HIS B 86  ? ? 57.49 -127.52 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O B A HOH 517 ? 5.83 . 
2 1 O ? A HOH 518 ? 5.98 . 
3 1 O ? A HOH 519 ? 5.98 . 
4 1 O ? A HOH 520 ? 7.60 . 
5 1 O ? B HOH 401 ? 6.29 . 
# 
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 
A1A9N N2   N Y N 1   
A1A9N C3   C N R 2   
A1A9N C6   C Y N 3   
A1A9N C9   C Y N 4   
A1A9N C12  C N N 5   
A1A9N C1   C N N 6   
A1A9N C10  C N N 7   
A1A9N C11  C N N 8   
A1A9N C2   C N N 9   
A1A9N C4   C Y N 10  
A1A9N C5   C Y N 11  
A1A9N C7   C Y N 12  
A1A9N C8   C Y N 13  
A1A9N N1   N N N 14  
A1A9N N3   N Y N 15  
A1A9N N4   N Y N 16  
A1A9N O1   O N N 17  
A1A9N H1   H N N 18  
A1A9N H10  H N N 19  
A1A9N H17  H N N 20  
A1A9N H15  H N N 21  
A1A9N H16  H N N 22  
A1A9N H2   H N N 23  
A1A9N H3   H N N 24  
A1A9N H4   H N N 25  
A1A9N H14  H N N 26  
A1A9N H13  H N N 27  
A1A9N H12  H N N 28  
A1A9N H5   H N N 29  
A1A9N H6   H N N 30  
A1A9N H8   H N N 31  
A1A9N H9   H N N 32  
A1A9N H7   H N N 33  
A1A9N H11  H N N 34  
A1A9N H18  H N N 35  
ALA   N    N N N 36  
ALA   CA   C N S 37  
ALA   C    C N N 38  
ALA   O    O N N 39  
ALA   CB   C N N 40  
ALA   OXT  O N N 41  
ALA   H    H N N 42  
ALA   H2   H N N 43  
ALA   HA   H N N 44  
ALA   HB1  H N N 45  
ALA   HB2  H N N 46  
ALA   HB3  H N N 47  
ALA   HXT  H N N 48  
ARG   N    N N N 49  
ARG   CA   C N S 50  
ARG   C    C N N 51  
ARG   O    O N N 52  
ARG   CB   C N N 53  
ARG   CG   C N N 54  
ARG   CD   C N N 55  
ARG   NE   N N N 56  
ARG   CZ   C N N 57  
ARG   NH1  N N N 58  
ARG   NH2  N N N 59  
ARG   OXT  O N N 60  
ARG   H    H N N 61  
ARG   H2   H N N 62  
ARG   HA   H N N 63  
ARG   HB2  H N N 64  
ARG   HB3  H N N 65  
ARG   HG2  H N N 66  
ARG   HG3  H N N 67  
ARG   HD2  H N N 68  
ARG   HD3  H N N 69  
ARG   HE   H N N 70  
ARG   HH11 H N N 71  
ARG   HH12 H N N 72  
ARG   HH21 H N N 73  
ARG   HH22 H N N 74  
ARG   HXT  H N N 75  
ASN   N    N N N 76  
ASN   CA   C N S 77  
ASN   C    C N N 78  
ASN   O    O N N 79  
ASN   CB   C N N 80  
ASN   CG   C N N 81  
ASN   OD1  O N N 82  
ASN   ND2  N N N 83  
ASN   OXT  O N N 84  
ASN   H    H N N 85  
ASN   H2   H N N 86  
ASN   HA   H N N 87  
ASN   HB2  H N N 88  
ASN   HB3  H N N 89  
ASN   HD21 H N N 90  
ASN   HD22 H N N 91  
ASN   HXT  H N N 92  
ASP   N    N N N 93  
ASP   CA   C N S 94  
ASP   C    C N N 95  
ASP   O    O N N 96  
ASP   CB   C N N 97  
ASP   CG   C N N 98  
ASP   OD1  O N N 99  
ASP   OD2  O N N 100 
ASP   OXT  O N N 101 
ASP   H    H N N 102 
ASP   H2   H N N 103 
ASP   HA   H N N 104 
ASP   HB2  H N N 105 
ASP   HB3  H N N 106 
ASP   HD2  H N N 107 
ASP   HXT  H N N 108 
CYS   N    N N N 109 
CYS   CA   C N R 110 
CYS   C    C N N 111 
CYS   O    O N N 112 
CYS   CB   C N N 113 
CYS   SG   S N N 114 
CYS   OXT  O N N 115 
CYS   H    H N N 116 
CYS   H2   H N N 117 
CYS   HA   H N N 118 
CYS   HB2  H N N 119 
CYS   HB3  H N N 120 
CYS   HG   H N N 121 
CYS   HXT  H N N 122 
GLN   N    N N N 123 
GLN   CA   C N S 124 
GLN   C    C N N 125 
GLN   O    O N N 126 
GLN   CB   C N N 127 
GLN   CG   C N N 128 
GLN   CD   C N N 129 
GLN   OE1  O N N 130 
GLN   NE2  N N N 131 
GLN   OXT  O N N 132 
GLN   H    H N N 133 
GLN   H2   H N N 134 
GLN   HA   H N N 135 
GLN   HB2  H N N 136 
GLN   HB3  H N N 137 
GLN   HG2  H N N 138 
GLN   HG3  H N N 139 
GLN   HE21 H N N 140 
GLN   HE22 H N N 141 
GLN   HXT  H N N 142 
GLU   N    N N N 143 
GLU   CA   C N S 144 
GLU   C    C N N 145 
GLU   O    O N N 146 
GLU   CB   C N N 147 
GLU   CG   C N N 148 
GLU   CD   C N N 149 
GLU   OE1  O N N 150 
GLU   OE2  O N N 151 
GLU   OXT  O N N 152 
GLU   H    H N N 153 
GLU   H2   H N N 154 
GLU   HA   H N N 155 
GLU   HB2  H N N 156 
GLU   HB3  H N N 157 
GLU   HG2  H N N 158 
GLU   HG3  H N N 159 
GLU   HE2  H N N 160 
GLU   HXT  H N N 161 
GLY   N    N N N 162 
GLY   CA   C N N 163 
GLY   C    C N N 164 
GLY   O    O N N 165 
GLY   OXT  O N N 166 
GLY   H    H N N 167 
GLY   H2   H N N 168 
GLY   HA2  H N N 169 
GLY   HA3  H N N 170 
GLY   HXT  H N N 171 
HIS   N    N N N 172 
HIS   CA   C N S 173 
HIS   C    C N N 174 
HIS   O    O N N 175 
HIS   CB   C N N 176 
HIS   CG   C Y N 177 
HIS   ND1  N Y N 178 
HIS   CD2  C Y N 179 
HIS   CE1  C Y N 180 
HIS   NE2  N Y N 181 
HIS   OXT  O N N 182 
HIS   H    H N N 183 
HIS   H2   H N N 184 
HIS   HA   H N N 185 
HIS   HB2  H N N 186 
HIS   HB3  H N N 187 
HIS   HD1  H N N 188 
HIS   HD2  H N N 189 
HIS   HE1  H N N 190 
HIS   HE2  H N N 191 
HIS   HXT  H N N 192 
HOH   O    O N N 193 
HOH   H1   H N N 194 
HOH   H2   H N N 195 
ILE   N    N N N 196 
ILE   CA   C N S 197 
ILE   C    C N N 198 
ILE   O    O N N 199 
ILE   CB   C N S 200 
ILE   CG1  C N N 201 
ILE   CG2  C N N 202 
ILE   CD1  C N N 203 
ILE   OXT  O N N 204 
ILE   H    H N N 205 
ILE   H2   H N N 206 
ILE   HA   H N N 207 
ILE   HB   H N N 208 
ILE   HG12 H N N 209 
ILE   HG13 H N N 210 
ILE   HG21 H N N 211 
ILE   HG22 H N N 212 
ILE   HG23 H N N 213 
ILE   HD11 H N N 214 
ILE   HD12 H N N 215 
ILE   HD13 H N N 216 
ILE   HXT  H N N 217 
LEU   N    N N N 218 
LEU   CA   C N S 219 
LEU   C    C N N 220 
LEU   O    O N N 221 
LEU   CB   C N N 222 
LEU   CG   C N N 223 
LEU   CD1  C N N 224 
LEU   CD2  C N N 225 
LEU   OXT  O N N 226 
LEU   H    H N N 227 
LEU   H2   H N N 228 
LEU   HA   H N N 229 
LEU   HB2  H N N 230 
LEU   HB3  H N N 231 
LEU   HG   H N N 232 
LEU   HD11 H N N 233 
LEU   HD12 H N N 234 
LEU   HD13 H N N 235 
LEU   HD21 H N N 236 
LEU   HD22 H N N 237 
LEU   HD23 H N N 238 
LEU   HXT  H N N 239 
LYS   N    N N N 240 
LYS   CA   C N S 241 
LYS   C    C N N 242 
LYS   O    O N N 243 
LYS   CB   C N N 244 
LYS   CG   C N N 245 
LYS   CD   C N N 246 
LYS   CE   C N N 247 
LYS   NZ   N N N 248 
LYS   OXT  O N N 249 
LYS   H    H N N 250 
LYS   H2   H N N 251 
LYS   HA   H N N 252 
LYS   HB2  H N N 253 
LYS   HB3  H N N 254 
LYS   HG2  H N N 255 
LYS   HG3  H N N 256 
LYS   HD2  H N N 257 
LYS   HD3  H N N 258 
LYS   HE2  H N N 259 
LYS   HE3  H N N 260 
LYS   HZ1  H N N 261 
LYS   HZ2  H N N 262 
LYS   HZ3  H N N 263 
LYS   HXT  H N N 264 
MET   N    N N N 265 
MET   CA   C N S 266 
MET   C    C N N 267 
MET   O    O N N 268 
MET   CB   C N N 269 
MET   CG   C N N 270 
MET   SD   S N N 271 
MET   CE   C N N 272 
MET   OXT  O N N 273 
MET   H    H N N 274 
MET   H2   H N N 275 
MET   HA   H N N 276 
MET   HB2  H N N 277 
MET   HB3  H N N 278 
MET   HG2  H N N 279 
MET   HG3  H N N 280 
MET   HE1  H N N 281 
MET   HE2  H N N 282 
MET   HE3  H N N 283 
MET   HXT  H N N 284 
PHE   N    N N N 285 
PHE   CA   C N S 286 
PHE   C    C N N 287 
PHE   O    O N N 288 
PHE   CB   C N N 289 
PHE   CG   C Y N 290 
PHE   CD1  C Y N 291 
PHE   CD2  C Y N 292 
PHE   CE1  C Y N 293 
PHE   CE2  C Y N 294 
PHE   CZ   C Y N 295 
PHE   OXT  O N N 296 
PHE   H    H N N 297 
PHE   H2   H N N 298 
PHE   HA   H N N 299 
PHE   HB2  H N N 300 
PHE   HB3  H N N 301 
PHE   HD1  H N N 302 
PHE   HD2  H N N 303 
PHE   HE1  H N N 304 
PHE   HE2  H N N 305 
PHE   HZ   H N N 306 
PHE   HXT  H N N 307 
PRO   N    N N N 308 
PRO   CA   C N S 309 
PRO   C    C N N 310 
PRO   O    O N N 311 
PRO   CB   C N N 312 
PRO   CG   C N N 313 
PRO   CD   C N N 314 
PRO   OXT  O N N 315 
PRO   H    H N N 316 
PRO   HA   H N N 317 
PRO   HB2  H N N 318 
PRO   HB3  H N N 319 
PRO   HG2  H N N 320 
PRO   HG3  H N N 321 
PRO   HD2  H N N 322 
PRO   HD3  H N N 323 
PRO   HXT  H N N 324 
SER   N    N N N 325 
SER   CA   C N S 326 
SER   C    C N N 327 
SER   O    O N N 328 
SER   CB   C N N 329 
SER   OG   O N N 330 
SER   OXT  O N N 331 
SER   H    H N N 332 
SER   H2   H N N 333 
SER   HA   H N N 334 
SER   HB2  H N N 335 
SER   HB3  H N N 336 
SER   HG   H N N 337 
SER   HXT  H N N 338 
TFA   C1   C N N 339 
TFA   C2   C N N 340 
TFA   O    O N N 341 
TFA   F1   F N N 342 
TFA   F2   F N N 343 
TFA   F3   F N N 344 
TFA   OXT  O N N 345 
TFA   HXT  H N N 346 
THR   N    N N N 347 
THR   CA   C N S 348 
THR   C    C N N 349 
THR   O    O N N 350 
THR   CB   C N R 351 
THR   OG1  O N N 352 
THR   CG2  C N N 353 
THR   OXT  O N N 354 
THR   H    H N N 355 
THR   H2   H N N 356 
THR   HA   H N N 357 
THR   HB   H N N 358 
THR   HG1  H N N 359 
THR   HG21 H N N 360 
THR   HG22 H N N 361 
THR   HG23 H N N 362 
THR   HXT  H N N 363 
TYR   N    N N N 364 
TYR   CA   C N S 365 
TYR   C    C N N 366 
TYR   O    O N N 367 
TYR   CB   C N N 368 
TYR   CG   C Y N 369 
TYR   CD1  C Y N 370 
TYR   CD2  C Y N 371 
TYR   CE1  C Y N 372 
TYR   CE2  C Y N 373 
TYR   CZ   C Y N 374 
TYR   OH   O N N 375 
TYR   OXT  O N N 376 
TYR   H    H N N 377 
TYR   H2   H N N 378 
TYR   HA   H N N 379 
TYR   HB2  H N N 380 
TYR   HB3  H N N 381 
TYR   HD1  H N N 382 
TYR   HD2  H N N 383 
TYR   HE1  H N N 384 
TYR   HE2  H N N 385 
TYR   HH   H N N 386 
TYR   HXT  H N N 387 
VAL   N    N N N 388 
VAL   CA   C N S 389 
VAL   C    C N N 390 
VAL   O    O N N 391 
VAL   CB   C N N 392 
VAL   CG1  C N N 393 
VAL   CG2  C N N 394 
VAL   OXT  O N N 395 
VAL   H    H N N 396 
VAL   H2   H N N 397 
VAL   HA   H N N 398 
VAL   HB   H N N 399 
VAL   HG11 H N N 400 
VAL   HG12 H N N 401 
VAL   HG13 H N N 402 
VAL   HG21 H N N 403 
VAL   HG22 H N N 404 
VAL   HG23 H N N 405 
VAL   HXT  H N N 406 
# 
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 
A1A9N O1  C10  sing N N 1   
A1A9N C2  C1   sing N N 2   
A1A9N C2  C3   sing N N 3   
A1A9N C10 C12  sing N N 4   
A1A9N C10 C3   sing N N 5   
A1A9N C10 C11  sing N N 6   
A1A9N C3  N1   sing N N 7   
A1A9N N1  C4   sing N N 8   
A1A9N C4  C7   doub Y N 9   
A1A9N C4  N2   sing Y N 10  
A1A9N C8  C7   sing Y N 11  
A1A9N C8  C9   doub Y N 12  
A1A9N C7  C6   sing Y N 13  
A1A9N N2  C5   doub Y N 14  
A1A9N C9  N4   sing Y N 15  
A1A9N C6  N4   sing Y N 16  
A1A9N C6  N3   doub Y N 17  
A1A9N C5  N3   sing Y N 18  
A1A9N C3  H1   sing N N 19  
A1A9N C9  H10  sing N N 20  
A1A9N C12 H17  sing N N 21  
A1A9N C12 H15  sing N N 22  
A1A9N C12 H16  sing N N 23  
A1A9N C1  H2   sing N N 24  
A1A9N C1  H3   sing N N 25  
A1A9N C1  H4   sing N N 26  
A1A9N C11 H14  sing N N 27  
A1A9N C11 H13  sing N N 28  
A1A9N C11 H12  sing N N 29  
A1A9N C2  H5   sing N N 30  
A1A9N C2  H6   sing N N 31  
A1A9N C5  H8   sing N N 32  
A1A9N C8  H9   sing N N 33  
A1A9N N1  H7   sing N N 34  
A1A9N N4  H11  sing N N 35  
A1A9N O1  H18  sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
GLN   N   CA   sing N N 119 
GLN   N   H    sing N N 120 
GLN   N   H2   sing N N 121 
GLN   CA  C    sing N N 122 
GLN   CA  CB   sing N N 123 
GLN   CA  HA   sing N N 124 
GLN   C   O    doub N N 125 
GLN   C   OXT  sing N N 126 
GLN   CB  CG   sing N N 127 
GLN   CB  HB2  sing N N 128 
GLN   CB  HB3  sing N N 129 
GLN   CG  CD   sing N N 130 
GLN   CG  HG2  sing N N 131 
GLN   CG  HG3  sing N N 132 
GLN   CD  OE1  doub N N 133 
GLN   CD  NE2  sing N N 134 
GLN   NE2 HE21 sing N N 135 
GLN   NE2 HE22 sing N N 136 
GLN   OXT HXT  sing N N 137 
GLU   N   CA   sing N N 138 
GLU   N   H    sing N N 139 
GLU   N   H2   sing N N 140 
GLU   CA  C    sing N N 141 
GLU   CA  CB   sing N N 142 
GLU   CA  HA   sing N N 143 
GLU   C   O    doub N N 144 
GLU   C   OXT  sing N N 145 
GLU   CB  CG   sing N N 146 
GLU   CB  HB2  sing N N 147 
GLU   CB  HB3  sing N N 148 
GLU   CG  CD   sing N N 149 
GLU   CG  HG2  sing N N 150 
GLU   CG  HG3  sing N N 151 
GLU   CD  OE1  doub N N 152 
GLU   CD  OE2  sing N N 153 
GLU   OE2 HE2  sing N N 154 
GLU   OXT HXT  sing N N 155 
GLY   N   CA   sing N N 156 
GLY   N   H    sing N N 157 
GLY   N   H2   sing N N 158 
GLY   CA  C    sing N N 159 
GLY   CA  HA2  sing N N 160 
GLY   CA  HA3  sing N N 161 
GLY   C   O    doub N N 162 
GLY   C   OXT  sing N N 163 
GLY   OXT HXT  sing N N 164 
HIS   N   CA   sing N N 165 
HIS   N   H    sing N N 166 
HIS   N   H2   sing N N 167 
HIS   CA  C    sing N N 168 
HIS   CA  CB   sing N N 169 
HIS   CA  HA   sing N N 170 
HIS   C   O    doub N N 171 
HIS   C   OXT  sing N N 172 
HIS   CB  CG   sing N N 173 
HIS   CB  HB2  sing N N 174 
HIS   CB  HB3  sing N N 175 
HIS   CG  ND1  sing Y N 176 
HIS   CG  CD2  doub Y N 177 
HIS   ND1 CE1  doub Y N 178 
HIS   ND1 HD1  sing N N 179 
HIS   CD2 NE2  sing Y N 180 
HIS   CD2 HD2  sing N N 181 
HIS   CE1 NE2  sing Y N 182 
HIS   CE1 HE1  sing N N 183 
HIS   NE2 HE2  sing N N 184 
HIS   OXT HXT  sing N N 185 
HOH   O   H1   sing N N 186 
HOH   O   H2   sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
TFA   C1  C2   sing N N 326 
TFA   C1  O    doub N N 327 
TFA   C1  OXT  sing N N 328 
TFA   C2  F1   sing N N 329 
TFA   C2  F2   sing N N 330 
TFA   C2  F3   sing N N 331 
TFA   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                    7HEB 
_atom_sites.fract_transf_matrix[1][1]   0.011266 
_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]   0.011266 
_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]   0.025276 
_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 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.635 -16.217 22.262  0.72 50.85 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.570 -16.207 22.343  0.28 49.82 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.656 -15.149 22.426  0.72 50.48 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.625 -15.109 22.504  0.28 49.58 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.299 -13.795 22.139  0.72 49.12 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.293 -13.783 22.158  0.28 48.61 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.411 -13.518 22.590  0.72 49.51 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.416 -13.513 22.583  0.28 48.95 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.020 -15.185 23.831  0.72 51.18 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.043 -15.076 23.932  0.28 50.08 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.996 -14.069 23.984  0.72 51.37 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.030 -13.947 24.069  0.28 50.22 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.378 -16.541 24.093  0.72 51.38 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.408 -16.413 24.284  0.28 50.22 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.944 -15.279 21.783  0.72 60.59 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.886 -15.238 21.891  0.28 59.51 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.712 -15.051 24.496  0.72 61.44 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.761 -14.912 24.562  0.28 60.12 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.487 -14.219 24.796  0.72 61.66 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.559 -14.048 24.911  0.28 60.28 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.459 -13.219 24.036  0.72 61.66 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.497 -13.097 24.052  0.28 60.28 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.402 -14.079 23.217  0.72 61.66 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.402 -13.996 23.332  0.28 60.28 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.926 -16.515 24.951  0.72 61.68 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.977 -16.339 25.150  0.28 60.29 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.739 -16.729 23.388  0.72 61.68 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.752 -16.639 23.606  0.28 60.29 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.069 -17.222 24.103  0.72 61.68 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.099 -17.093 24.316  0.28 60.29 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.595 -12.959 21.378  1.00 47.04 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.040 -11.608 21.050  1.00 43.12 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 17.892 -10.633 21.298  1.00 40.01 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.788 -11.027 21.687  1.00 39.92 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.590 -11.507 19.619  1.00 42.05 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.575 -11.897 18.566  1.00 40.94 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.466 -11.365 18.529  1.00 40.44 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 18.953 -12.832 17.699  1.00 40.60 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.835 -13.163 21.032  0.72 56.46 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.840 -13.169 21.025  0.28 56.46 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.760 -11.369 21.647  1.00 51.77 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.858 -10.587 19.448  1.00 50.48 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.355 -12.094 19.529  1.00 50.48 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.417 -13.089 17.077  1.00 48.74 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.738 -13.181 17.760  1.00 48.74 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.158 -9.346  21.070  1.00 36.80 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.240 -8.280  21.453  1.00 33.69 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.355 -7.796  20.306  1.00 30.06 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.626 -6.814  20.477  1.00 30.29 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.012 -7.106  22.061  1.00 34.48 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 18.877 -6.515  21.108  1.00 34.96 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 18.877 -9.064  20.688  1.00 44.18 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.654 -8.619  22.142  1.00 40.45 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.380 -6.437  22.371  1.00 41.40 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.542 -7.427  22.811  1.00 41.40 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.294 -5.871  21.458  1.00 41.97 ?  5   SER   A HG   1 
ATOM   57   N N    . PHE   A 1 6   ? 16.390 -8.456  19.152  1.00 25.88 ?  6   PHE   A N    1 
ATOM   58   C CA   . PHE   A 1 6   ? 15.487 -8.094  18.066  1.00 22.25 ?  6   PHE   A CA   1 
ATOM   59   C C    . PHE   A 1 6   ? 14.057 -8.471  18.442  1.00 22.02 ?  6   PHE   A C    1 
ATOM   60   O O    . PHE   A 1 6   ? 13.801 -9.587  18.902  1.00 23.30 ?  6   PHE   A O    1 
ATOM   61   C CB   . PHE   A 1 6   ? 15.900 -8.809  16.786  1.00 20.38 ?  6   PHE   A CB   1 
ATOM   62   C CG   . PHE   A 1 6   ? 17.184 -8.292  16.194  1.00 18.97 ?  6   PHE   A CG   1 
ATOM   63   C CD1  . PHE   A 1 6   ? 17.207 -7.094  15.505  1.00 18.39 ?  6   PHE   A CD1  1 
ATOM   64   C CD2  . PHE   A 1 6   ? 18.359 -9.011  16.318  1.00 19.26 ?  6   PHE   A CD2  1 
ATOM   65   C CE1  . PHE   A 1 6   ? 18.380 -6.615  14.955  1.00 18.44 ?  6   PHE   A CE1  1 
ATOM   66   C CE2  . PHE   A 1 6   ? 19.534 -8.542  15.769  1.00 19.45 ?  6   PHE   A CE2  1 
ATOM   67   C CZ   . PHE   A 1 6   ? 19.545 -7.340  15.087  1.00 18.85 ?  6   PHE   A CZ   1 
ATOM   68   H H    . PHE   A 1 6   ? 16.917 -9.113  18.977  1.00 31.08 ?  6   PHE   A H    1 
ATOM   69   H HA   . PHE   A 1 6   ? 15.523 -7.141  17.919  1.00 26.73 ?  6   PHE   A HA   1 
ATOM   70   H HB2  . PHE   A 1 6   ? 16.018 -9.754  16.981  1.00 24.48 ?  6   PHE   A HB2  1 
ATOM   71   H HB3  . PHE   A 1 6   ? 15.198 -8.698  16.127  1.00 24.48 ?  6   PHE   A HB3  1 
ATOM   72   H HD1  . PHE   A 1 6   ? 16.422 -6.602  15.415  1.00 22.08 ?  6   PHE   A HD1  1 
ATOM   73   H HD2  . PHE   A 1 6   ? 18.355 -9.822  16.779  1.00 23.13 ?  6   PHE   A HD2  1 
ATOM   74   H HE1  . PHE   A 1 6   ? 18.384 -5.806  14.496  1.00 22.15 ?  6   PHE   A HE1  1 
ATOM   75   H HE2  . PHE   A 1 6   ? 20.320 -9.031  15.863  1.00 23.36 ?  6   PHE   A HE2  1 
ATOM   76   H HZ   . PHE   A 1 6   ? 20.336 -7.018  14.718  1.00 22.64 ?  6   PHE   A HZ   1 
ATOM   77   N N    A SER   A 1 7   ? 13.121 -7.551  18.208  0.72 21.24 ?  7   SER   A N    1 
ATOM   78   N N    B SER   A 1 7   ? 13.123 -7.537  18.265  0.28 21.75 ?  7   SER   A N    1 
ATOM   79   C CA   A SER   A 1 7   ? 11.748 -7.684  18.678  0.72 21.47 ?  7   SER   A CA   1 
ATOM   80   C CA   B SER   A 1 7   ? 11.762 -7.715  18.752  0.28 21.74 ?  7   SER   A CA   1 
ATOM   81   C C    A SER   A 1 7   ? 10.763 -7.481  17.533  0.72 19.37 ?  7   SER   A C    1 
ATOM   82   C C    B SER   A 1 7   ? 10.765 -7.259  17.695  0.28 20.25 ?  7   SER   A C    1 
ATOM   83   O O    A SER   A 1 7   ? 10.954 -6.607  16.682  0.72 19.52 ?  7   SER   A O    1 
ATOM   84   O O    B SER   A 1 7   ? 11.029 -6.331  16.927  0.28 20.51 ?  7   SER   A O    1 
ATOM   85   C CB   A SER   A 1 7   ? 11.467 -6.647  19.775  0.72 23.67 ?  7   SER   A CB   1 
ATOM   86   C CB   B SER   A 1 7   ? 11.532 -6.937  20.057  0.28 23.08 ?  7   SER   A CB   1 
ATOM   87   O OG   A SER   A 1 7   ? 10.129 -6.727  20.224  0.72 25.40 ?  7   SER   A OG   1 
ATOM   88   O OG   B SER   A 1 7   ? 10.185 -7.036  20.482  0.28 24.14 ?  7   SER   A OG   1 
ATOM   89   H H    A SER   A 1 7   ? 13.266 -6.831  17.764  0.72 25.51 ?  7   SER   A H    1 
ATOM   90   H H    B SER   A 1 7   ? 13.255 -6.793  17.857  0.28 26.12 ?  7   SER   A H    1 
ATOM   91   H HA   A SER   A 1 7   ? 11.615 -8.570  19.050  0.72 25.78 ?  7   SER   A HA   1 
ATOM   92   H HA   B SER   A 1 7   ? 11.599 -8.652  18.931  0.28 26.11 ?  7   SER   A HA   1 
ATOM   93   H HB2  A SER   A 1 7   ? 12.070 -6.806  20.521  0.72 28.42 ?  7   SER   A HB2  1 
ATOM   94   H HB2  B SER   A 1 7   ? 12.099 -7.310  20.751  0.28 27.72 ?  7   SER   A HB2  1 
ATOM   95   H HB3  A SER   A 1 7   ? 11.614 -5.760  19.416  0.72 28.42 ?  7   SER   A HB3  1 
ATOM   96   H HB3  B SER   A 1 7   ? 11.757 -6.004  19.914  0.28 27.72 ?  7   SER   A HB3  1 
ATOM   97   H HG   A SER   A 1 7   ? 9.994  -6.170  20.838  0.72 30.50 ?  7   SER   A HG   1 
ATOM   98   H HG   B SER   A 1 7   ? 10.072 -6.594  21.189  0.28 28.98 ?  7   SER   A HG   1 
ATOM   99   N N    A GLY   A 1 8   ? 9.702  -8.290  17.522  0.72 17.91 ?  8   GLY   A N    1 
ATOM   100  N N    B GLY   A 1 8   ? 9.611  -7.929  17.668  0.28 18.61 ?  8   GLY   A N    1 
ATOM   101  C CA   A GLY   A 1 8   ? 8.607  -8.073  16.599  0.72 16.98 ?  8   GLY   A CA   1 
ATOM   102  C CA   B GLY   A 1 8   ? 8.546  -7.588  16.748  0.28 17.16 ?  8   GLY   A CA   1 
ATOM   103  C C    A GLY   A 1 8   ? 8.831  -8.553  15.186  0.72 15.73 ?  8   GLY   A C    1 
ATOM   104  C C    B GLY   A 1 8   ? 8.702  -8.143  15.351  0.28 15.49 ?  8   GLY   A C    1 
ATOM   105  O O    A GLY   A 1 8   ? 8.097  -8.134  14.285  0.72 16.29 ?  8   GLY   A O    1 
ATOM   106  O O    B GLY   A 1 8   ? 7.926  -7.770  14.465  0.28 15.73 ?  8   GLY   A O    1 
ATOM   107  H H    A GLY   A 1 8   ? 9.602  -8.969  18.042  0.72 21.51 ?  8   GLY   A H    1 
ATOM   108  H H    B GLY   A 1 8   ? 9.426  -8.597  18.178  0.28 22.35 ?  8   GLY   A H    1 
ATOM   109  H HA2  A GLY   A 1 8   ? 7.818  -8.516  16.948  0.72 20.40 ?  8   GLY   A HA2  1 
ATOM   110  H HA2  B GLY   A 1 8   ? 7.705  -7.921  17.101  0.28 20.61 ?  8   GLY   A HA2  1 
ATOM   111  H HA3  A GLY   A 1 8   ? 8.424  -7.126  16.552  0.72 20.40 ?  8   GLY   A HA3  1 
ATOM   112  H HA3  B GLY   A 1 8   ? 8.480  -6.622  16.685  0.28 20.61 ?  8   GLY   A HA3  1 
ATOM   113  N N    A TYR   A 1 9   ? 9.817  -9.422  14.958  0.72 14.49 ?  9   TYR   A N    1 
ATOM   114  N N    B TYR   A 1 9   ? 9.675  -9.022  15.126  0.28 14.40 ?  9   TYR   A N    1 
ATOM   115  C CA   A TYR   A 1 9   ? 10.088 -9.948  13.628  0.72 13.33 ?  9   TYR   A CA   1 
ATOM   116  C CA   B TYR   A 1 9   ? 9.927  -9.582  13.806  0.28 13.42 ?  9   TYR   A CA   1 
ATOM   117  C C    A TYR   A 1 9   ? 9.230  -11.172 13.338  0.72 12.75 ?  9   TYR   A C    1 
ATOM   118  C C    B TYR   A 1 9   ? 9.049  -10.800 13.556  0.28 12.69 ?  9   TYR   A C    1 
ATOM   119  O O    A TYR   A 1 9   ? 8.983  -12.004 14.217  0.72 13.70 ?  9   TYR   A O    1 
ATOM   120  O O    B TYR   A 1 9   ? 8.762  -11.579 14.470  0.28 13.28 ?  9   TYR   A O    1 
ATOM   121  C CB   A TYR   A 1 9   ? 11.570 -10.319 13.468  0.72 13.73 ?  9   TYR   A CB   1 
ATOM   122  C CB   B TYR   A 1 9   ? 11.394 -9.998  13.674  0.28 13.82 ?  9   TYR   A CB   1 
ATOM   123  C CG   A TYR   A 1 9   ? 12.478 -9.111  13.358  0.72 14.11 ?  9   TYR   A CG   1 
ATOM   124  C CG   B TYR   A 1 9   ? 12.335 -8.856  13.388  0.28 14.34 ?  9   TYR   A CG   1 
ATOM   125  C CD1  A TYR   A 1 9   ? 12.805 -8.367  14.482  0.72 14.52 ?  9   TYR   A CD1  1 
ATOM   126  C CD1  B TYR   A 1 9   ? 12.639 -7.927  14.369  0.28 14.64 ?  9   TYR   A CD1  1 
ATOM   127  C CD2  A TYR   A 1 9   ? 12.974 -8.696  12.129  0.72 14.46 ?  9   TYR   A CD2  1 
ATOM   128  C CD2  B TYR   A 1 9   ? 12.918 -8.708  12.137  0.28 14.27 ?  9   TYR   A CD2  1 
ATOM   129  C CE1  A TYR   A 1 9   ? 13.613 -7.252  14.391  0.72 15.18 ?  9   TYR   A CE1  1 
ATOM   130  C CE1  B TYR   A 1 9   ? 13.494 -6.877  14.114  0.28 14.88 ?  9   TYR   A CE1  1 
ATOM   131  C CE2  A TYR   A 1 9   ? 13.784 -7.579  12.026  0.72 14.74 ?  9   TYR   A CE2  1 
ATOM   132  C CE2  B TYR   A 1 9   ? 13.775 -7.662  11.870  0.28 14.30 ?  9   TYR   A CE2  1 
ATOM   133  C CZ   A TYR   A 1 9   ? 14.093 -6.860  13.160  0.72 15.44 ?  9   TYR   A CZ   1 
ATOM   134  C CZ   B TYR   A 1 9   ? 14.059 -6.749  12.861  0.28 14.63 ?  9   TYR   A CZ   1 
ATOM   135  O OH   A TYR   A 1 9   ? 14.895 -5.749  13.054  0.72 16.68 ?  9   TYR   A OH   1 
ATOM   136  O OH   B TYR   A 1 9   ? 14.912 -5.704  12.598  0.28 14.96 ?  9   TYR   A OH   1 
ATOM   137  H H    A TYR   A 1 9   ? 10.340 -9.737  15.566  0.72 17.41 ?  9   TYR   A H    1 
ATOM   138  H H    B TYR   A 1 9   ? 10.207 -9.312  15.730  0.28 17.31 ?  9   TYR   A H    1 
ATOM   139  H HA   A TYR   A 1 9   ? 9.879  -9.276  12.967  0.72 16.01 ?  9   TYR   A HA   1 
ATOM   140  H HA   B TYR   A 1 9   ? 9.735  -8.915  13.124  0.28 16.13 ?  9   TYR   A HA   1 
ATOM   141  H HB2  A TYR   A 1 9   ? 11.854 -10.843 14.235  0.72 16.50 ?  9   TYR   A HB2  1 
ATOM   142  H HB2  B TYR   A 1 9   ? 11.681 -10.424 14.496  0.28 16.60 ?  9   TYR   A HB2  1 
ATOM   143  H HB3  A TYR   A 1 9   ? 11.674 -10.845 12.656  0.72 16.50 ?  9   TYR   A HB3  1 
ATOM   144  H HB3  B TYR   A 1 9   ? 11.460 -10.623 12.938  0.28 16.60 ?  9   TYR   A HB3  1 
ATOM   145  H HD1  A TYR   A 1 9   ? 12.473 -8.627  15.313  0.72 17.45 ?  9   TYR   A HD1  1 
ATOM   146  H HD1  B TYR   A 1 9   ? 12.257 -8.016  15.213  0.28 17.59 ?  9   TYR   A HD1  1 
ATOM   147  H HD2  A TYR   A 1 9   ? 12.761 -9.179  11.363  0.72 17.37 ?  9   TYR   A HD2  1 
ATOM   148  H HD2  B TYR   A 1 9   ? 12.727 -9.323  11.466  0.28 17.15 ?  9   TYR   A HD2  1 
ATOM   149  H HE1  A TYR   A 1 9   ? 13.826 -6.762  15.154  0.72 18.24 ?  9   TYR   A HE1  1 
ATOM   150  H HE1  B TYR   A 1 9   ? 13.690 -6.264  14.784  0.28 17.88 ?  9   TYR   A HE1  1 
ATOM   151  H HE2  A TYR   A 1 9   ? 14.116 -7.313  11.197  0.72 17.71 ?  9   TYR   A HE2  1 
ATOM   152  H HE2  B TYR   A 1 9   ? 14.160 -7.574  11.029  0.28 17.18 ?  9   TYR   A HE2  1 
ATOM   153  H HH   A TYR   A 1 9   ? 15.023 -5.403  13.809  0.72 20.03 ?  9   TYR   A HH   1 
ATOM   154  H HH   B TYR   A 1 9   ? 15.000 -5.237  13.291  0.28 17.98 ?  9   TYR   A HH   1 
ATOM   155  N N    A LEU   A 1 10  ? 8.804  -11.287 12.085  0.72 12.67 ?  10  LEU   A N    1 
ATOM   156  N N    B LEU   A 1 10  ? 8.619  -10.947 12.306  0.28 12.16 ?  10  LEU   A N    1 
ATOM   157  C CA   A LEU   A 1 10  ? 8.211  -12.515 11.581  0.72 12.53 ?  10  LEU   A CA   1 
ATOM   158  C CA   B LEU   A 1 10  ? 8.003  -12.180 11.845  0.28 11.62 ?  10  LEU   A CA   1 
ATOM   159  C C    A LEU   A 1 10  ? 9.336  -13.449 11.153  0.72 12.15 ?  10  LEU   A C    1 
ATOM   160  C C    B LEU   A 1 10  ? 9.108  -13.137 11.417  0.28 11.28 ?  10  LEU   A C    1 
ATOM   161  O O    A LEU   A 1 10  ? 10.301 -13.023 10.511  0.72 12.68 ?  10  LEU   A O    1 
ATOM   162  O O    B LEU   A 1 10  ? 10.048 -12.744 10.720  0.28 11.26 ?  10  LEU   A O    1 
ATOM   163  C CB   A LEU   A 1 10  ? 7.340  -12.191 10.369  0.72 13.95 ?  10  LEU   A CB   1 
ATOM   164  C CB   B LEU   A 1 10  ? 7.065  -11.904 10.668  0.28 11.64 ?  10  LEU   A CB   1 
ATOM   165  C CG   A LEU   A 1 10  ? 6.601  -13.348 9.701   0.72 16.33 ?  10  LEU   A CG   1 
ATOM   166  C CG   B LEU   A 1 10  ? 6.420  -13.161 10.065  0.28 12.11 ?  10  LEU   A CG   1 
ATOM   167  C CD1  A LEU   A 1 10  ? 5.519  -13.880 10.623  0.72 17.30 ?  10  LEU   A CD1  1 
ATOM   168  C CD1  B LEU   A 1 10  ? 4.948  -12.957 9.774   0.28 12.39 ?  10  LEU   A CD1  1 
ATOM   169  C CD2  A LEU   A 1 10  ? 6.009  -12.901 8.375   0.72 17.47 ?  10  LEU   A CD2  1 
ATOM   170  C CD2  B LEU   A 1 10  ? 7.125  -13.616 8.796   0.28 12.27 ?  10  LEU   A CD2  1 
ATOM   171  H H    A LEU   A 1 10  ? 8.857  -10.665 11.491  0.72 15.23 ?  10  LEU   A H    1 
ATOM   172  H H    B LEU   A 1 10  ? 8.674  -10.336 11.706  0.28 14.61 ?  10  LEU   A H    1 
ATOM   173  H HA   A LEU   A 1 10  ? 7.673  -12.944 12.271  0.72 15.06 ?  10  LEU   A HA   1 
ATOM   174  H HA   B LEU   A 1 10  ? 7.489  -12.584 12.565  0.28 13.96 ?  10  LEU   A HA   1 
ATOM   175  H HB2  A LEU   A 1 10  ? 6.671  -11.555 10.645  0.72 16.75 ?  10  LEU   A HB2  1 
ATOM   176  H HB2  B LEU   A 1 10  ? 6.347  -11.319 10.966  0.28 13.99 ?  10  LEU   A HB2  1 
ATOM   177  H HB3  A LEU   A 1 10  ? 7.909  -11.799 9.694   0.72 16.75 ?  10  LEU   A HB3  1 
ATOM   178  H HB3  B LEU   A 1 10  ? 7.568  -11.464 9.965   0.28 13.99 ?  10  LEU   A HB3  1 
ATOM   179  H HG   A LEU   A 1 10  ? 7.224  -14.075 9.525   0.72 19.62 ?  10  LEU   A HG   1 
ATOM   180  H HG   B LEU   A 1 10  ? 6.490  -13.879 10.710  0.28 14.55 ?  10  LEU   A HG   1 
ATOM   181  H HD11 A LEU   A 1 10  ? 5.074  -14.631 10.195  0.72 20.78 ?  10  LEU   A HD11 1 
ATOM   182  H HD11 B LEU   A 1 10  ? 4.600  -13.758 9.347   0.28 14.88 ?  10  LEU   A HD11 1 
ATOM   183  H HD12 A LEU   A 1 10  ? 5.922  -14.172 11.457  0.72 20.78 ?  10  LEU   A HD12 1 
ATOM   184  H HD12 B LEU   A 1 10  ? 4.481  -12.799 10.609  0.28 14.88 ?  10  LEU   A HD12 1 
ATOM   185  H HD13 A LEU   A 1 10  ? 4.876  -13.175 10.798  0.72 20.78 ?  10  LEU   A HD13 1 
ATOM   186  H HD13 B LEU   A 1 10  ? 4.847  -12.197 9.185   0.28 14.88 ?  10  LEU   A HD13 1 
ATOM   187  H HD21 A LEU   A 1 10  ? 5.540  -13.649 7.971   0.72 20.98 ?  10  LEU   A HD21 1 
ATOM   188  H HD21 B LEU   A 1 10  ? 6.670  -14.398 8.447   0.28 14.74 ?  10  LEU   A HD21 1 
ATOM   189  H HD22 A LEU   A 1 10  ? 5.392  -12.172 8.539   0.72 20.98 ?  10  LEU   A HD22 1 
ATOM   190  H HD22 B LEU   A 1 10  ? 7.094  -12.898 8.144   0.28 14.74 ?  10  LEU   A HD22 1 
ATOM   191  H HD23 A LEU   A 1 10  ? 6.727  -12.608 7.796   0.72 20.98 ?  10  LEU   A HD23 1 
ATOM   192  H HD23 B LEU   A 1 10  ? 8.045  -13.833 9.006   0.28 14.74 ?  10  LEU   A HD23 1 
ATOM   193  N N    A LYS   A 1 11  ? 9.224  -14.720 11.529  0.72 12.02 ?  11  LYS   A N    1 
ATOM   194  N N    B LYS   A 1 11  ? 9.004  -14.387 11.848  0.28 11.35 ?  11  LYS   A N    1 
ATOM   195  C CA   A LYS   A 1 11  ? 10.231 -15.719 11.199  0.72 12.17 ?  11  LYS   A CA   1 
ATOM   196  C CA   B LYS   A 1 11  ? 9.987  -15.398 11.494  0.28 11.08 ?  11  LYS   A CA   1 
ATOM   197  C C    A LYS   A 1 11  ? 9.893  -16.326 9.845   0.72 12.32 ?  11  LYS   A C    1 
ATOM   198  C C    B LYS   A 1 11  ? 9.650  -15.939 10.109  0.28 10.83 ?  11  LYS   A C    1 
ATOM   199  O O    A LYS   A 1 11  ? 8.848  -16.961 9.697   0.72 14.10 ?  11  LYS   A O    1 
ATOM   200  O O    B LYS   A 1 11  ? 8.543  -16.439 9.889   0.28 10.91 ?  11  LYS   A O    1 
ATOM   201  C CB   A LYS   A 1 11  ? 10.271 -16.790 12.290  0.72 12.00 ?  11  LYS   A CB   1 
ATOM   202  C CB   B LYS   A 1 11  ? 9.963  -16.511 12.539  0.28 11.00 ?  11  LYS   A CB   1 
ATOM   203  C CG   A LYS   A 1 11  ? 11.281 -17.906 12.079  0.72 12.41 ?  11  LYS   A CG   1 
ATOM   204  C CG   B LYS   A 1 11  ? 11.043 -17.560 12.375  0.28 11.18 ?  11  LYS   A CG   1 
ATOM   205  C CD   A LYS   A 1 11  ? 11.358 -18.763 13.346  0.72 13.06 ?  11  LYS   A CD   1 
ATOM   206  C CD   B LYS   A 1 11  ? 11.143 -18.435 13.616  0.28 11.64 ?  11  LYS   A CD   1 
ATOM   207  C CE   A LYS   A 1 11  ? 12.343 -19.916 13.241  0.72 13.21 ?  11  LYS   A CE   1 
ATOM   208  C CE   B LYS   A 1 11  ? 12.168 -19.546 13.440  0.28 12.03 ?  11  LYS   A CE   1 
ATOM   209  N NZ   A LYS   A 1 11  ? 13.708 -19.432 12.938  0.72 12.95 ?  11  LYS   A NZ   1 
ATOM   210  N NZ   B LYS   A 1 11  ? 13.559 -19.026 13.318  0.28 12.24 ?  11  LYS   A NZ   1 
ATOM   211  H H    A LYS   A 1 11  ? 8.560  -15.034 11.982  0.72 14.44 ?  11  LYS   A H    1 
ATOM   212  H H    B LYS   A 1 11  ? 8.363  -14.674 12.342  0.28 13.64 ?  11  LYS   A H    1 
ATOM   213  H HA   A LYS   A 1 11  ? 11.102 -15.302 11.142  0.72 14.63 ?  11  LYS   A HA   1 
ATOM   214  H HA   B LYS   A 1 11  ? 10.874 -15.001 11.472  0.28 13.32 ?  11  LYS   A HA   1 
ATOM   215  H HB2  A LYS   A 1 11  ? 10.493 -16.363 13.132  0.72 14.42 ?  11  LYS   A HB2  1 
ATOM   216  H HB2  B LYS   A 1 11  ? 10.070 -16.112 13.417  0.28 13.22 ?  11  LYS   A HB2  1 
ATOM   217  H HB3  A LYS   A 1 11  ? 9.398  -17.203 12.355  0.72 14.42 ?  11  LYS   A HB3  1 
ATOM   218  H HB3  B LYS   A 1 11  ? 9.105  -16.960 12.489  0.28 13.22 ?  11  LYS   A HB3  1 
ATOM   219  H HG2  A LYS   A 1 11  ? 10.997 -18.472 11.342  0.72 14.92 ?  11  LYS   A HG2  1 
ATOM   220  H HG2  B LYS   A 1 11  ? 10.826 -18.127 11.619  0.28 13.44 ?  11  LYS   A HG2  1 
ATOM   221  H HG3  A LYS   A 1 11  ? 12.157 -17.532 11.906  0.72 14.92 ?  11  LYS   A HG3  1 
ATOM   222  H HG3  B LYS   A 1 11  ? 11.897 -17.124 12.239  0.28 13.44 ?  11  LYS   A HG3  1 
ATOM   223  H HD2  A LYS   A 1 11  ? 11.634 -18.206 14.088  0.72 15.70 ?  11  LYS   A HD2  1 
ATOM   224  H HD2  B LYS   A 1 11  ? 11.412 -17.888 14.372  0.28 13.99 ?  11  LYS   A HD2  1 
ATOM   225  H HD3  A LYS   A 1 11  ? 10.482 -19.143 13.524  0.72 15.70 ?  11  LYS   A HD3  1 
ATOM   226  H HD3  B LYS   A 1 11  ? 10.279 -18.843 13.792  0.28 13.99 ?  11  LYS   A HD3  1 
ATOM   227  H HE2  A LYS   A 1 11  ? 12.372 -20.392 14.089  0.72 15.87 ?  11  LYS   A HE2  1 
ATOM   228  H HE2  B LYS   A 1 11  ? 12.135 -20.136 14.208  0.28 14.46 ?  11  LYS   A HE2  1 
ATOM   229  H HE3  A LYS   A 1 11  ? 12.067 -20.514 12.532  0.72 15.87 ?  11  LYS   A HE3  1 
ATOM   230  H HE3  B LYS   A 1 11  ? 11.962 -20.041 12.631  0.28 14.46 ?  11  LYS   A HE3  1 
ATOM   231  H HZ1  A LYS   A 1 11  ? 14.270 -20.117 12.879  0.72 15.56 ?  11  LYS   A HZ1  1 
ATOM   232  H HZ1  B LYS   A 1 11  ? 14.131 -19.701 13.216  0.28 14.71 ?  11  LYS   A HZ1  1 
ATOM   233  H HZ2  A LYS   A 1 11  ? 13.708 -18.989 12.164  0.72 15.56 ?  11  LYS   A HZ2  1 
ATOM   234  H HZ2  B LYS   A 1 11  ? 13.623 -18.485 12.613  0.28 14.71 ?  11  LYS   A HZ2  1 
ATOM   235  H HZ3  A LYS   A 1 11  ? 13.987 -18.882 13.582  0.72 15.56 ?  11  LYS   A HZ3  1 
ATOM   236  H HZ3  B LYS   A 1 11  ? 13.780 -18.570 14.051  0.28 14.71 ?  11  LYS   A HZ3  1 
ATOM   237  N N    A LEU   A 1 12  ? 10.773 -16.152 8.860   0.72 11.50 ?  12  LEU   A N    1 
ATOM   238  N N    B LEU   A 1 12  ? 10.579 -15.800 9.164   0.28 11.17 ?  12  LEU   A N    1 
ATOM   239  C CA   A LEU   A 1 12  ? 10.517 -16.740 7.548   0.72 11.82 ?  12  LEU   A CA   1 
ATOM   240  C CA   B LEU   A 1 12  ? 10.357 -16.305 7.812   0.28 11.64 ?  12  LEU   A CA   1 
ATOM   241  C C    A LEU   A 1 12  ? 11.106 -18.138 7.411   0.72 11.92 ?  12  LEU   A C    1 
ATOM   242  C C    B LEU   A 1 12  ? 10.912 -17.714 7.630   0.28 11.50 ?  12  LEU   A C    1 
ATOM   243  O O    A LEU   A 1 12  ? 10.478 -19.017 6.812   0.72 12.20 ?  12  LEU   A O    1 
ATOM   244  O O    B LEU   A 1 12  ? 10.244 -18.585 7.062   0.28 11.43 ?  12  LEU   A O    1 
ATOM   245  C CB   A LEU   A 1 12  ? 11.070 -15.848 6.431   0.72 12.02 ?  12  LEU   A CB   1 
ATOM   246  C CB   B LEU   A 1 12  ? 10.985 -15.361 6.780   0.28 12.69 ?  12  LEU   A CB   1 
ATOM   247  C CG   A LEU   A 1 12  ? 10.425 -14.471 6.279   0.72 13.31 ?  12  LEU   A CG   1 
ATOM   248  C CG   B LEU   A 1 12  ? 10.222 -14.071 6.471   0.28 13.65 ?  12  LEU   A CG   1 
ATOM   249  C CD1  A LEU   A 1 12  ? 11.109 -13.708 5.157   0.72 13.94 ?  12  LEU   A CD1  1 
ATOM   250  C CD1  B LEU   A 1 12  ? 11.084 -13.130 5.649   0.28 14.07 ?  12  LEU   A CD1  1 
ATOM   251  C CD2  A LEU   A 1 12  ? 8.930  -14.600 6.020   0.72 14.62 ?  12  LEU   A CD2  1 
ATOM   252  C CD2  B LEU   A 1 12  ? 8.920  -14.371 5.737   0.28 14.25 ?  12  LEU   A CD2  1 
ATOM   253  H H    A LEU   A 1 12  ? 11.512 -15.705 8.922   0.72 13.82 ?  12  LEU   A H    1 
ATOM   254  H H    B LEU   A 1 12  ? 11.334 -15.398 9.277   0.28 13.42 ?  12  LEU   A H    1 
ATOM   255  H HA   A LEU   A 1 12  ? 9.560  -16.813 7.424   0.72 14.21 ?  12  LEU   A HA   1 
ATOM   256  H HA   B LEU   A 1 12  ? 9.402  -16.330 7.646   0.28 13.98 ?  12  LEU   A HA   1 
ATOM   257  H HB2  A LEU   A 1 12  ? 12.014 -15.711 6.590   0.72 14.44 ?  12  LEU   A HB2  1 
ATOM   258  H HB2  B LEU   A 1 12  ? 11.864 -15.104 7.097   0.28 15.25 ?  12  LEU   A HB2  1 
ATOM   259  H HB3  A LEU   A 1 12  ? 10.951 -16.316 5.587   0.72 14.44 ?  12  LEU   A HB3  1 
ATOM   260  H HB3  B LEU   A 1 12  ? 11.074 -15.847 5.946   0.28 15.25 ?  12  LEU   A HB3  1 
ATOM   261  H HG   A LEU   A 1 12  ? 10.549 -13.970 7.099   0.72 15.99 ?  12  LEU   A HG   1 
ATOM   262  H HG   B LEU   A 1 12  ? 10.001 -13.623 7.303   0.28 16.40 ?  12  LEU   A HG   1 
ATOM   263  H HD11 A LEU   A 1 12  ? 10.699 -12.836 5.068   0.72 16.75 ?  12  LEU   A HD11 1 
ATOM   264  H HD11 B LEU   A 1 12  ? 10.575 -12.328 5.448   0.28 16.90 ?  12  LEU   A HD11 1 
ATOM   265  H HD12 A LEU   A 1 12  ? 12.053 -13.610 5.372   0.72 16.75 ?  12  LEU   A HD12 1 
ATOM   266  H HD12 B LEU   A 1 12  ? 11.875 -12.898 6.161   0.28 16.90 ?  12  LEU   A HD12 1 
ATOM   267  H HD13 A LEU   A 1 12  ? 11.013 -14.207 4.330   0.72 16.75 ?  12  LEU   A HD13 1 
ATOM   268  H HD13 B LEU   A 1 12  ? 11.340 -13.574 4.826   0.28 16.90 ?  12  LEU   A HD13 1 
ATOM   269  H HD21 A LEU   A 1 12  ? 8.579  -13.735 5.762   0.72 17.56 ?  12  LEU   A HD21 1 
ATOM   270  H HD21 B LEU   A 1 12  ? 8.514  -13.535 5.457   0.28 17.12 ?  12  LEU   A HD21 1 
ATOM   271  H HD22 A LEU   A 1 12  ? 8.789  -15.242 5.306   0.72 17.56 ?  12  LEU   A HD22 1 
ATOM   272  H HD22 B LEU   A 1 12  ? 9.116  -14.919 4.960   0.28 17.12 ?  12  LEU   A HD22 1 
ATOM   273  H HD23 A LEU   A 1 12  ? 8.496  -14.907 6.831   0.72 17.56 ?  12  LEU   A HD23 1 
ATOM   274  H HD23 B LEU   A 1 12  ? 8.322  -14.846 6.334   0.28 17.12 ?  12  LEU   A HD23 1 
ATOM   275  N N    A THR   A 1 13  ? 12.312 -18.349 7.932   0.72 12.12 ?  13  THR   A N    1 
ATOM   276  N N    B THR   A 1 13  ? 12.142 -17.942 8.078   0.28 11.53 ?  13  THR   A N    1 
ATOM   277  C CA   A THR   A 1 13  ? 13.006 -19.627 7.839   0.72 12.22 ?  13  THR   A CA   1 
ATOM   278  C CA   B THR   A 1 13  ? 12.774 -19.249 8.007   0.28 11.49 ?  13  THR   A CA   1 
ATOM   279  C C    A THR   A 1 13  ? 13.785 -19.841 9.129   0.72 12.38 ?  13  THR   A C    1 
ATOM   280  C C    B THR   A 1 13  ? 13.520 -19.484 9.313   0.28 11.81 ?  13  THR   A C    1 
ATOM   281  O O    A THR   A 1 13  ? 13.689 -19.057 10.079  0.72 12.13 ?  13  THR   A O    1 
ATOM   282  O O    B THR   A 1 13  ? 13.381 -18.733 10.283  0.28 12.22 ?  13  THR   A O    1 
ATOM   283  C CB   A THR   A 1 13  ? 13.987 -19.674 6.658   0.72 13.25 ?  13  THR   A CB   1 
ATOM   284  C CB   B THR   A 1 13  ? 13.728 -19.334 6.808   0.28 11.68 ?  13  THR   A CB   1 
ATOM   285  O OG1  A THR   A 1 13  ? 15.063 -18.768 6.908   0.72 13.45 ?  13  THR   A OG1  1 
ATOM   286  O OG1  B THR   A 1 13  ? 14.785 -18.385 6.979   0.28 11.38 ?  13  THR   A OG1  1 
ATOM   287  C CG2  A THR   A 1 13  ? 13.316 -19.321 5.344   0.72 14.53 ?  13  THR   A CG2  1 
ATOM   288  C CG2  B THR   A 1 13  ? 12.996 -19.059 5.496   0.28 12.34 ?  13  THR   A CG2  1 
ATOM   289  H H    A THR   A 1 13  ? 12.763 -17.751 8.350   0.72 14.57 ?  13  THR   A H    1 
ATOM   290  H H    B THR   A 1 13  ? 12.640 -17.333 8.420   0.28 13.85 ?  13  THR   A H    1 
ATOM   291  H HA   A THR   A 1 13  ? 12.359 -20.350 7.734   0.72 14.69 ?  13  THR   A HA   1 
ATOM   292  H HA   B THR   A 1 13  ? 12.092 -19.933 7.909   0.28 13.81 ?  13  THR   A HA   1 
ATOM   293  H HB   A THR   A 1 13  ? 14.346 -20.572 6.576   0.72 15.92 ?  13  THR   A HB   1 
ATOM   294  H HB   B THR   A 1 13  ? 14.106 -20.225 6.760   0.28 14.04 ?  13  THR   A HB   1 
ATOM   295  H HG1  A THR   A 1 13  ? 15.600 -18.777 6.259   0.72 16.16 ?  13  THR   A HG1  1 
ATOM   296  H HG1  B THR   A 1 13  ? 15.309 -18.417 6.324   0.28 13.67 ?  13  THR   A HG1  1 
ATOM   297  H HG21 A THR   A 1 13  ? 13.925 -19.493 4.608   0.72 17.46 ?  13  THR   A HG21 1 
ATOM   298  H HG21 B THR   A 1 13  ? 13.604 -19.175 4.747   0.28 14.83 ?  13  THR   A HG21 1 
ATOM   299  H HG22 A THR   A 1 13  ? 12.519 -19.862 5.224   0.72 17.46 ?  13  THR   A HG22 1 
ATOM   300  H HG22 B THR   A 1 13  ? 12.254 -19.678 5.394   0.28 14.83 ?  13  THR   A HG22 1 
ATOM   301  H HG23 A THR   A 1 13  ? 13.067 -18.386 5.339   0.72 17.46 ?  13  THR   A HG23 1 
ATOM   302  H HG23 B THR   A 1 13  ? 12.654 -18.153 5.487   0.28 14.83 ?  13  THR   A HG23 1 
ATOM   303  N N    A ASP   A 1 14  ? 14.592 -20.903 9.147   0.72 13.23 ?  14  ASP   A N    1 
ATOM   304  N N    B ASP   A 1 14  ? 14.330 -20.539 9.321   0.28 11.91 ?  14  ASP   A N    1 
ATOM   305  C CA   A ASP   A 1 14  ? 15.441 -21.168 10.300  0.72 13.89 ?  14  ASP   A CA   1 
ATOM   306  C CA   B ASP   A 1 14  ? 15.156 -20.846 10.479  0.28 12.48 ?  14  ASP   A CA   1 
ATOM   307  C C    A ASP   A 1 14  ? 16.260 -19.946 10.696  0.72 13.65 ?  14  ASP   A C    1 
ATOM   308  C C    B ASP   A 1 14  ? 16.037 -19.666 10.875  0.28 12.08 ?  14  ASP   A C    1 
ATOM   309  O O    A ASP   A 1 14  ? 16.483 -19.704 11.887  0.72 15.04 ?  14  ASP   A O    1 
ATOM   310  O O    B ASP   A 1 14  ? 16.303 -19.467 12.066  0.28 12.41 ?  14  ASP   A O    1 
ATOM   311  C CB   A ASP   A 1 14  ? 16.387 -22.328 9.992   0.72 16.57 ?  14  ASP   A CB   1 
ATOM   312  C CB   B ASP   A 1 14  ? 16.010 -22.070 10.162  0.28 13.95 ?  14  ASP   A CB   1 
ATOM   313  C CG   A ASP   A 1 14  ? 17.307 -22.636 11.145  0.72 20.65 ?  14  ASP   A CG   1 
ATOM   314  C CG   B ASP   A 1 14  ? 16.914 -22.453 11.303  0.28 15.70 ?  14  ASP   A CG   1 
ATOM   315  O OD1  A ASP   A 1 14  ? 16.814 -22.871 12.268  0.72 22.47 ?  14  ASP   A OD1  1 
ATOM   316  O OD1  B ASP   A 1 14  ? 16.444 -23.143 12.236  0.28 16.39 ?  14  ASP   A OD1  1 
ATOM   317  O OD2  A ASP   A 1 14  ? 18.529 -22.641 10.923  0.72 22.76 -1 14  ASP   A OD2  1 
ATOM   318  O OD2  B ASP   A 1 14  ? 18.095 -22.051 11.264  0.28 16.49 -1 14  ASP   A OD2  1 
ATOM   319  H H    A ASP   A 1 14  ? 14.675 -21.478 8.506   0.72 15.89 ?  14  ASP   A H    1 
ATOM   320  H H    B ASP   A 1 14  ? 14.418 -21.083 8.668   0.28 14.31 ?  14  ASP   A H    1 
ATOM   321  H HA   A ASP   A 1 14  ? 14.895 -21.427 11.054  0.72 16.69 ?  14  ASP   A HA   1 
ATOM   322  H HA   B ASP   A 1 14  ? 14.587 -21.058 11.234  0.28 15.00 ?  14  ASP   A HA   1 
ATOM   323  H HB2  A ASP   A 1 14  ? 15.869 -23.131 9.795   0.72 19.90 ?  14  ASP   A HB2  1 
ATOM   324  H HB2  B ASP   A 1 14  ? 15.419 -22.815 9.945   0.28 16.77 ?  14  ASP   A HB2  1 
ATOM   325  H HB3  A ASP   A 1 14  ? 16.948 -22.108 9.232   0.72 19.90 ?  14  ASP   A HB3  1 
ATOM   326  H HB3  B ASP   A 1 14  ? 16.579 -21.873 9.402   0.28 16.77 ?  14  ASP   A HB3  1 
ATOM   327  N N    A ASN   A 1 15  ? 16.733 -19.169 9.714   0.72 12.61 ?  15  ASN   A N    1 
ATOM   328  N N    B ASN   A 1 15  ? 16.471 -18.854 9.901   0.28 11.74 ?  15  ASN   A N    1 
ATOM   329  C CA   A ASN   A 1 15  ? 17.722 -18.131 9.977   0.72 13.26 ?  15  ASN   A CA   1 
ATOM   330  C CA   B ASN   A 1 15  ? 17.482 -17.835 10.162  0.28 11.98 ?  15  ASN   A CA   1 
ATOM   331  C C    A ASN   A 1 15  ? 17.323 -16.727 9.531   0.72 13.64 ?  15  ASN   A C    1 
ATOM   332  C C    B ASN   A 1 15  ? 17.196 -16.498 9.482   0.28 12.30 ?  15  ASN   A C    1 
ATOM   333  O O    A ASN   A 1 15  ? 18.032 -15.774 9.880   0.72 14.20 ?  15  ASN   A O    1 
ATOM   334  O O    B ASN   A 1 15  ? 18.112 -15.676 9.361   0.28 13.05 ?  15  ASN   A O    1 
ATOM   335  C CB   A ASN   A 1 15  ? 19.083 -18.504 9.352   0.72 12.93 ?  15  ASN   A CB   1 
ATOM   336  C CB   B ASN   A 1 15  ? 18.857 -18.299 9.677   0.28 11.91 ?  15  ASN   A CB   1 
ATOM   337  C CG   A ASN   A 1 15  ? 19.037 -18.577 7.837   0.72 13.64 ?  15  ASN   A CG   1 
ATOM   338  C CG   B ASN   A 1 15  ? 18.917 -18.453 8.172   0.28 12.04 ?  15  ASN   A CG   1 
ATOM   339  O OD1  A ASN   A 1 15  ? 18.346 -19.422 7.264   0.72 14.67 ?  15  ASN   A OD1  1 
ATOM   340  O OD1  B ASN   A 1 15  ? 18.153 -19.223 7.586   0.28 12.24 ?  15  ASN   A OD1  1 
ATOM   341  N ND2  A ASN   A 1 15  ? 19.790 -17.699 7.177   0.72 13.83 ?  15  ASN   A ND2  1 
ATOM   342  N ND2  B ASN   A 1 15  ? 19.804 -17.692 7.532   0.28 12.27 ?  15  ASN   A ND2  1 
ATOM   343  H H    A ASN   A 1 15  ? 16.507 -19.239 8.887   0.72 15.15 ?  15  ASN   A H    1 
ATOM   344  H H    B ASN   A 1 15  ? 16.180 -18.864 9.096   0.28 14.11 ?  15  ASN   A H    1 
ATOM   345  H HA   A ASN   A 1 15  ? 17.873 -18.095 10.931  0.72 15.94 ?  15  ASN   A HA   1 
ATOM   346  H HA   B ASN   A 1 15  ? 17.537 -17.677 11.119  0.28 14.39 ?  15  ASN   A HA   1 
ATOM   347  H HB2  A ASN   A 1 15  ? 19.746 -17.833 9.600   0.72 15.54 ?  15  ASN   A HB2  1 
ATOM   348  H HB2  B ASN   A 1 15  ? 19.521 -17.642 9.942   0.28 14.31 ?  15  ASN   A HB2  1 
ATOM   349  H HB3  A ASN   A 1 15  ? 19.368 -19.374 9.688   0.72 15.54 ?  15  ASN   A HB3  1 
ATOM   350  H HB3  B ASN   A 1 15  ? 19.054 -19.156 10.071  0.28 14.31 ?  15  ASN   A HB3  1 
ATOM   351  H HD21 A ASN   A 1 15  ? 19.797 -17.703 6.318   0.72 16.62 ?  15  ASN   A HD21 1 
ATOM   352  H HD21 B ASN   A 1 15  ? 19.867 -17.731 6.675   0.28 14.75 ?  15  ASN   A HD21 1 
ATOM   353  H HD22 A ASN   A 1 15  ? 20.261 -17.120 7.608   0.72 16.62 ?  15  ASN   A HD22 1 
ATOM   354  H HD22 B ASN   A 1 15  ? 20.317 -17.160 7.975   0.28 14.75 ?  15  ASN   A HD22 1 
ATOM   355  N N    A VAL   A 1 16  ? 16.221 -16.565 8.794   0.72 13.01 ?  16  VAL   A N    1 
ATOM   356  N N    B VAL   A 1 16  ? 15.971 -16.252 9.021   0.28 11.68 ?  16  VAL   A N    1 
ATOM   357  C CA   A VAL   A 1 16  ? 15.819 -15.282 8.221   0.72 12.60 ?  16  VAL   A CA   1 
ATOM   358  C CA   B VAL   A 1 16  ? 15.610 -14.984 8.396   0.28 11.49 ?  16  VAL   A CA   1 
ATOM   359  C C    A VAL   A 1 16  ? 14.540 -14.788 8.888   0.72 12.36 ?  16  VAL   A C    1 
ATOM   360  C C    B VAL   A 1 16  ? 14.342 -14.464 9.060   0.28 11.40 ?  16  VAL   A C    1 
ATOM   361  O O    A VAL   A 1 16  ? 13.543 -15.519 8.984   0.72 12.50 ?  16  VAL   A O    1 
ATOM   362  O O    B VAL   A 1 16  ? 13.331 -15.173 9.122   0.28 11.43 ?  16  VAL   A O    1 
ATOM   363  C CB   A VAL   A 1 16  ? 15.649 -15.360 6.694   0.72 13.42 ?  16  VAL   A CB   1 
ATOM   364  C CB   B VAL   A 1 16  ? 15.427 -15.123 6.871   0.28 11.94 ?  16  VAL   A CB   1 
ATOM   365  C CG1  A VAL   A 1 16  ? 15.227 -14.000 6.136   0.72 14.61 ?  16  VAL   A CG1  1 
ATOM   366  C CG1  B VAL   A 1 16  ? 14.995 -13.793 6.247   0.28 12.28 ?  16  VAL   A CG1  1 
ATOM   367  C CG2  A VAL   A 1 16  ? 16.927 -15.844 6.029   0.72 14.28 ?  16  VAL   A CG2  1 
ATOM   368  C CG2  B VAL   A 1 16  ? 16.711 -15.631 6.220   0.28 12.54 ?  16  VAL   A CG2  1 
ATOM   369  H H    A VAL   A 1 16  ? 15.689 -17.212 8.605   0.72 15.63 ?  16  VAL   A H    1 
ATOM   370  H H    B VAL   A 1 16  ? 15.318 -16.810 9.053   0.28 14.04 ?  16  VAL   A H    1 
ATOM   371  H HA   A VAL   A 1 16  ? 16.519 -14.636 8.403   0.72 15.14 ?  16  VAL   A HA   1 
ATOM   372  H HA   B VAL   A 1 16  ? 16.312 -14.333 8.552   0.28 13.80 ?  16  VAL   A HA   1 
ATOM   373  H HB   A VAL   A 1 16  ? 14.948 -15.999 6.493   0.72 16.13 ?  16  VAL   A HB   1 
ATOM   374  H HB   B VAL   A 1 16  ? 14.730 -15.773 6.698   0.28 14.35 ?  16  VAL   A HB   1 
ATOM   375  H HG11 A VAL   A 1 16  ? 15.315 -14.018 5.171   0.72 17.55 ?  16  VAL   A HG11 1 
ATOM   376  H HG11 B VAL   A 1 16  ? 15.062 -13.864 5.280   0.28 14.76 ?  16  VAL   A HG11 1 
ATOM   377  H HG12 A VAL   A 1 16  ? 14.301 -13.832 6.379   0.72 17.55 ?  16  VAL   A HG12 1 
ATOM   378  H HG12 B VAL   A 1 16  ? 14.077 -13.606 6.498   0.28 14.76 ?  16  VAL   A HG12 1 
ATOM   379  H HG13 A VAL   A 1 16  ? 15.798 -13.314 6.510   0.72 17.55 ?  16  VAL   A HG13 1 
ATOM   380  H HG13 B VAL   A 1 16  ? 15.578 -13.088 6.566   0.28 14.76 ?  16  VAL   A HG13 1 
ATOM   381  H HG21 A VAL   A 1 16  ? 16.812 -15.806 5.068   0.72 17.15 ?  16  VAL   A HG21 1 
ATOM   382  H HG21 B VAL   A 1 16  ? 16.590 -15.655 5.258   0.28 15.07 ?  16  VAL   A HG21 1 
ATOM   383  H HG22 A VAL   A 1 16  ? 17.659 -15.272 6.300   0.72 17.15 ?  16  VAL   A HG22 1 
ATOM   384  H HG22 B VAL   A 1 16  ? 17.440 -15.035 6.447   0.28 15.07 ?  16  VAL   A HG22 1 
ATOM   385  H HG23 A VAL   A 1 16  ? 17.099 -16.758 6.307   0.72 17.15 ?  16  VAL   A HG23 1 
ATOM   386  H HG23 B VAL   A 1 16  ? 16.901 -16.524 6.552   0.28 15.07 ?  16  VAL   A HG23 1 
ATOM   387  N N    A TYR   A 1 17  ? 14.565 -13.519 9.289   0.72 12.34 ?  17  TYR   A N    1 
ATOM   388  N N    B TYR   A 1 17  ? 14.406 -13.227 9.558   0.28 11.39 ?  17  TYR   A N    1 
ATOM   389  C CA   A TYR   A 1 17  ? 13.491 -12.836 9.990   0.72 11.98 ?  17  TYR   A CA   1 
ATOM   390  C CA   B TYR   A 1 17  ? 13.299 -12.560 10.227  0.28 11.61 ?  17  TYR   A CA   1 
ATOM   391  C C    A TYR   A 1 17  ? 13.215 -11.516 9.278   0.72 12.22 ?  17  TYR   A C    1 
ATOM   392  C C    B TYR   A 1 17  ? 13.069 -11.220 9.550   0.28 11.16 ?  17  TYR   A C    1 
ATOM   393  O O    A TYR   A 1 17  ? 14.109 -10.958 8.638   0.72 11.95 ?  17  TYR   A O    1 
ATOM   394  O O    B TYR   A 1 17  ? 14.005 -10.615 9.021   0.28 10.95 ?  17  TYR   A O    1 
ATOM   395  C CB   A TYR   A 1 17  ? 13.935 -12.569 11.432  0.72 12.33 ?  17  TYR   A CB   1 
ATOM   396  C CB   B TYR   A 1 17  ? 13.618 -12.314 11.705  0.28 12.38 ?  17  TYR   A CB   1 
ATOM   397  C CG   A TYR   A 1 17  ? 14.114 -13.829 12.252  0.72 13.34 ?  17  TYR   A CG   1 
ATOM   398  C CG   B TYR   A 1 17  ? 13.913 -13.571 12.488  0.28 13.37 ?  17  TYR   A CG   1 
ATOM   399  C CD1  A TYR   A 1 17  ? 15.280 -14.586 12.185  0.72 13.78 ?  17  TYR   A CD1  1 
ATOM   400  C CD1  B TYR   A 1 17  ? 15.134 -14.222 12.362  0.28 14.16 ?  17  TYR   A CD1  1 
ATOM   401  C CD2  A TYR   A 1 17  ? 13.104 -14.272 13.089  0.72 13.73 ?  17  TYR   A CD2  1 
ATOM   402  C CD2  B TYR   A 1 17  ? 12.973 -14.102 13.356  0.28 14.04 ?  17  TYR   A CD2  1 
ATOM   403  C CE1  A TYR   A 1 17  ? 15.424 -15.756 12.936  0.72 14.31 ?  17  TYR   A CE1  1 
ATOM   404  C CE1  B TYR   A 1 17  ? 15.406 -15.372 13.075  0.28 14.92 ?  17  TYR   A CE1  1 
ATOM   405  C CE2  A TYR   A 1 17  ? 13.238 -15.432 13.838  0.72 14.24 ?  17  TYR   A CE2  1 
ATOM   406  C CE2  B TYR   A 1 17  ? 13.237 -15.255 14.074  0.28 14.86 ?  17  TYR   A CE2  1 
ATOM   407  C CZ   A TYR   A 1 17  ? 14.399 -16.169 13.764  0.72 14.52 ?  17  TYR   A CZ   1 
ATOM   408  C CZ   B TYR   A 1 17  ? 14.456 -15.885 13.932  0.28 15.38 ?  17  TYR   A CZ   1 
ATOM   409  O OH   A TYR   A 1 17  ? 14.524 -17.317 14.513  0.72 15.36 ?  17  TYR   A OH   1 
ATOM   410  O OH   B TYR   A 1 17  ? 14.728 -17.030 14.645  0.28 16.26 ?  17  TYR   A OH   1 
ATOM   411  H H    A TYR   A 1 17  ? 15.245 -13.008 9.149   0.72 14.83 ?  17  TYR   A H    1 
ATOM   412  H H    B TYR   A 1 17  ? 15.109 -12.727 9.508   0.28 13.68 ?  17  TYR   A H    1 
ATOM   413  H HA   A TYR   A 1 17  ? 12.692 -13.392 9.991   0.72 14.39 ?  17  TYR   A HA   1 
ATOM   414  H HA   B TYR   A 1 17  ? 12.489 -13.084 10.158  0.28 13.95 ?  17  TYR   A HA   1 
ATOM   415  H HB2  A TYR   A 1 17  ? 14.785 -12.110 11.414  0.72 14.82 ?  17  TYR   A HB2  1 
ATOM   416  H HB2  B TYR   A 1 17  ? 14.390 -11.733 11.764  0.28 14.88 ?  17  TYR   A HB2  1 
ATOM   417  H HB3  A TYR   A 1 17  ? 13.267 -12.033 11.866  0.72 14.82 ?  17  TYR   A HB3  1 
ATOM   418  H HB3  B TYR   A 1 17  ? 12.853 -11.885 12.118  0.28 14.88 ?  17  TYR   A HB3  1 
ATOM   419  H HD1  A TYR   A 1 17  ? 15.978 -14.321 11.625  0.72 16.56 ?  17  TYR   A HD1  1 
ATOM   420  H HD1  B TYR   A 1 17  ? 15.776 -13.877 11.782  0.28 17.01 ?  17  TYR   A HD1  1 
ATOM   421  H HD2  A TYR   A 1 17  ? 12.317 -13.790 13.144  0.72 16.49 ?  17  TYR   A HD2  1 
ATOM   422  H HD2  B TYR   A 1 17  ? 12.149 -13.678 13.453  0.28 16.87 ?  17  TYR   A HD2  1 
ATOM   423  H HE1  A TYR   A 1 17  ? 16.214 -16.255 12.887  0.72 17.20 ?  17  TYR   A HE1  1 
ATOM   424  H HE1  B TYR   A 1 17  ? 16.230 -15.792 12.978  0.28 17.93 ?  17  TYR   A HE1  1 
ATOM   425  H HE2  A TYR   A 1 17  ? 12.548 -15.707 14.397  0.72 17.11 ?  17  TYR   A HE2  1 
ATOM   426  H HE2  B TYR   A 1 17  ? 12.598 -15.597 14.654  0.28 17.85 ?  17  TYR   A HE2  1 
ATOM   427  H HH   A TYR   A 1 17  ? 13.793 -17.494 14.879  0.72 18.45 ?  17  TYR   A HH   1 
ATOM   428  H HH   B TYR   A 1 17  ? 15.502 -17.302 14.465  0.28 19.53 ?  17  TYR   A HH   1 
ATOM   429  N N    A ILE   A 1 18  ? 11.984 -11.002 9.381   0.72 12.59 ?  18  ILE   A N    1 
ATOM   430  N N    B ILE   A 1 18  ? 11.823 -10.746 9.569   0.28 10.75 ?  18  ILE   A N    1 
ATOM   431  C CA   A ILE   A 1 18  ? 11.604 -9.808  8.622   0.72 12.43 ?  18  ILE   A CA   1 
ATOM   432  C CA   B ILE   A 1 18  ? 11.462 -9.523  8.857   0.28 10.70 ?  18  ILE   A CA   1 
ATOM   433  C C    A ILE   A 1 18  ? 10.626 -8.950  9.420   0.72 12.70 ?  18  ILE   A C    1 
ATOM   434  C C    B ILE   A 1 18  ? 10.557 -8.663  9.729   0.28 10.67 ?  18  ILE   A C    1 
ATOM   435  O O    A ILE   A 1 18  ? 9.816  -9.463  10.199  0.72 13.44 ?  18  ILE   A O    1 
ATOM   436  O O    B ILE   A 1 18  ? 9.673  -9.174  10.427  0.28 10.97 ?  18  ILE   A O    1 
ATOM   437  C CB   A ILE   A 1 18  ? 11.055 -10.208 7.233   0.72 11.88 ?  18  ILE   A CB   1 
ATOM   438  C CB   B ILE   A 1 18  ? 10.820 -9.841  7.490   0.28 10.76 ?  18  ILE   A CB   1 
ATOM   439  C CG1  A ILE   A 1 18  ? 10.978 -8.999  6.304   0.72 11.98 ?  18  ILE   A CG1  1 
ATOM   440  C CG1  B ILE   A 1 18  ? 10.716 -8.576  6.633   0.28 11.91 ?  18  ILE   A CG1  1 
ATOM   441  C CG2  A ILE   A 1 18  ? 9.714  -10.924 7.363   0.72 12.23 ?  18  ILE   A CG2  1 
ATOM   442  C CG2  B ILE   A 1 18  ? 9.456  -10.494 7.672   0.28 11.02 ?  18  ILE   A CG2  1 
ATOM   443  C CD1  A ILE   A 1 18  ? 10.752 -9.380  4.864   0.72 13.30 ?  18  ILE   A CD1  1 
ATOM   444  C CD1  B ILE   A 1 18  ? 10.348 -8.843  5.184   0.28 12.76 ?  18  ILE   A CD1  1 
ATOM   445  H H    A ILE   A 1 18  ? 11.358 -11.339 9.867   0.72 15.12 ?  18  ILE   A H    1 
ATOM   446  H H    B ILE   A 1 18  ? 11.161 -11.118 9.981   0.28 12.92 ?  18  ILE   A H    1 
ATOM   447  H HA   A ILE   A 1 18  ? 12.408 -9.287  8.473   0.72 14.93 ?  18  ILE   A HA   1 
ATOM   448  H HA   B ILE   A 1 18  ? 12.269 -9.013  8.689   0.28 12.86 ?  18  ILE   A HA   1 
ATOM   449  H HB   A ILE   A 1 18  ? 11.681 -10.836 6.834   0.72 14.27 ?  18  ILE   A HB   1 
ATOM   450  H HB   B ILE   A 1 18  ? 11.397 -10.463 7.031   0.28 12.93 ?  18  ILE   A HB   1 
ATOM   451  H HG12 A ILE   A 1 18  ? 10.247 -8.430  6.584   0.72 14.40 ?  18  ILE   A HG12 1 
ATOM   452  H HG12 B ILE   A 1 18  ? 10.034 -7.995  7.004   0.28 14.31 ?  18  ILE   A HG12 1 
ATOM   453  H HG13 A ILE   A 1 18  ? 11.817 -8.509  6.353   0.72 14.40 ?  18  ILE   A HG13 1 
ATOM   454  H HG13 B ILE   A 1 18  ? 11.573 -8.119  6.637   0.28 14.31 ?  18  ILE   A HG13 1 
ATOM   455  H HG21 A ILE   A 1 18  ? 9.468  -11.302 6.501   0.72 14.70 ?  18  ILE   A HG21 1 
ATOM   456  H HG21 B ILE   A 1 18  ? 9.156  -10.839 6.816   0.28 13.25 ?  18  ILE   A HG21 1 
ATOM   457  H HG22 A ILE   A 1 18  ? 9.799  -11.638 8.018   0.72 14.70 ?  18  ILE   A HG22 1 
ATOM   458  H HG22 B ILE   A 1 18  ? 9.538  -11.220 8.310   0.28 13.25 ?  18  ILE   A HG22 1 
ATOM   459  H HG23 A ILE   A 1 18  ? 9.040  -10.292 7.650   0.72 14.70 ?  18  ILE   A HG23 1 
ATOM   460  H HG23 B ILE   A 1 18  ? 8.825  -9.835  8.002   0.28 13.25 ?  18  ILE   A HG23 1 
ATOM   461  H HD11 A ILE   A 1 18  ? 10.769 -8.573  4.319   0.72 15.97 ?  18  ILE   A HD11 1 
ATOM   462  H HD11 B ILE   A 1 18  ? 10.339 -8.001  4.698   0.28 15.34 ?  18  ILE   A HD11 1 
ATOM   463  H HD12 A ILE   A 1 18  ? 11.453 -9.983  4.580   0.72 15.97 ?  18  ILE   A HD12 1 
ATOM   464  H HD12 B ILE   A 1 18  ? 11.008 -9.439  4.794   0.28 15.34 ?  18  ILE   A HD12 1 
ATOM   465  H HD13 A ILE   A 1 18  ? 9.887  -9.810  4.783   0.72 15.97 ?  18  ILE   A HD13 1 
ATOM   466  H HD13 B ILE   A 1 18  ? 9.471  -9.253  5.148   0.28 15.34 ?  18  ILE   A HD13 1 
ATOM   467  N N    A LYS   A 1 19  ? 10.687 -7.632  9.193   0.72 12.11 ?  19  LYS   A N    1 
ATOM   468  N N    B LYS   A 1 19  ? 10.787 -7.347  9.688   0.28 10.81 ?  19  LYS   A N    1 
ATOM   469  C CA   A LYS   A 1 19  ? 9.861  -6.671  9.916   0.72 12.94 ?  19  LYS   A CA   1 
ATOM   470  C CA   B LYS   A 1 19  ? 10.012 -6.384  10.457  0.28 12.18 ?  19  LYS   A CA   1 
ATOM   471  C C    A LYS   A 1 19  ? 9.700  -5.403  9.080   0.72 12.64 ?  19  LYS   A C    1 
ATOM   472  C C    B LYS   A 1 19  ? 9.778  -5.146  9.608   0.28 13.07 ?  19  LYS   A C    1 
ATOM   473  O O    A LYS   A 1 19  ? 10.605 -5.018  8.335   0.72 12.36 ?  19  LYS   A O    1 
ATOM   474  O O    B LYS   A 1 19  ? 10.670 -4.716  8.872   0.28 13.12 ?  19  LYS   A O    1 
ATOM   475  C CB   A LYS   A 1 19  ? 10.530 -6.339  11.256  0.72 14.55 ?  19  LYS   A CB   1 
ATOM   476  C CB   B LYS   A 1 19  ? 10.762 -5.978  11.734  0.28 12.70 ?  19  LYS   A CB   1 
ATOM   477  C CG   A LYS   A 1 19  ? 9.794  -5.362  12.154  0.72 16.08 ?  19  LYS   A CG   1 
ATOM   478  C CG   B LYS   A 1 19  ? 10.004 -5.049  12.666  0.28 13.96 ?  19  LYS   A CG   1 
ATOM   479  C CD   A LYS   A 1 19  ? 10.655 -5.076  13.378  0.72 17.72 ?  19  LYS   A CD   1 
ATOM   480  C CD   B LYS   A 1 19  ? 10.830 -4.777  13.914  0.28 15.24 ?  19  LYS   A CD   1 
ATOM   481  C CE   A LYS   A 1 19  ? 9.987  -4.142  14.367  0.72 19.05 ?  19  LYS   A CE   1 
ATOM   482  C CE   B LYS   A 1 19  ? 10.177 -3.758  14.827  0.28 16.05 ?  19  LYS   A CE   1 
ATOM   483  N NZ   A LYS   A 1 19  ? 10.880 -3.887  15.534  0.72 19.63 ?  19  LYS   A NZ   1 
ATOM   484  N NZ   B LYS   A 1 19  ? 11.008 -3.525  16.039  0.28 16.62 ?  19  LYS   A NZ   1 
ATOM   485  H H    A LYS   A 1 19  ? 11.218 -7.278  8.621   0.72 14.55 ?  19  LYS   A H    1 
ATOM   486  H H    B LYS   A 1 19  ? 11.414 -6.974  9.216   0.28 12.99 ?  19  LYS   A H    1 
ATOM   487  H HA   A LYS   A 1 19  ? 8.986  -7.069  10.086  0.72 15.54 ?  19  LYS   A HA   1 
ATOM   488  H HA   B LYS   A 1 19  ? 9.159  -6.764  10.707  0.28 14.64 ?  19  LYS   A HA   1 
ATOM   489  H HB2  A LYS   A 1 19  ? 10.631 -7.169  11.759  0.72 17.48 ?  19  LYS   A HB2  1 
ATOM   490  H HB2  B LYS   A 1 19  ? 10.971 -6.777  12.240  0.28 15.26 ?  19  LYS   A HB2  1 
ATOM   491  H HB3  A LYS   A 1 19  ? 11.402 -5.970  11.073  0.72 17.48 ?  19  LYS   A HB3  1 
ATOM   492  H HB3  B LYS   A 1 19  ? 11.586 -5.527  11.486  0.28 15.26 ?  19  LYS   A HB3  1 
ATOM   493  H HG2  A LYS   A 1 19  ? 9.642  -4.531  11.676  0.72 19.31 ?  19  LYS   A HG2  1 
ATOM   494  H HG2  B LYS   A 1 19  ? 9.834  -4.204  12.223  0.28 16.78 ?  19  LYS   A HG2  1 
ATOM   495  H HG3  A LYS   A 1 19  ? 8.953  -5.749  12.445  0.72 19.31 ?  19  LYS   A HG3  1 
ATOM   496  H HG3  B LYS   A 1 19  ? 9.171  -5.466  12.937  0.28 16.78 ?  19  LYS   A HG3  1 
ATOM   497  H HD2  A LYS   A 1 19  ? 10.841 -5.911  13.835  0.72 21.29 ?  19  LYS   A HD2  1 
ATOM   498  H HD2  B LYS   A 1 19  ? 10.933 -5.603  14.413  0.28 18.31 ?  19  LYS   A HD2  1 
ATOM   499  H HD3  A LYS   A 1 19  ? 11.485 -4.664  13.090  0.72 21.29 ?  19  LYS   A HD3  1 
ATOM   500  H HD3  B LYS   A 1 19  ? 11.697 -4.435  13.652  0.28 18.31 ?  19  LYS   A HD3  1 
ATOM   501  H HE2  A LYS   A 1 19  ? 9.800  -3.294  13.934  0.72 22.88 ?  19  LYS   A HE2  1 
ATOM   502  H HE2  B LYS   A 1 19  ? 10.083 -2.916  14.353  0.28 19.28 ?  19  LYS   A HE2  1 
ATOM   503  H HE3  A LYS   A 1 19  ? 9.168  -4.545  14.691  0.72 22.88 ?  19  LYS   A HE3  1 
ATOM   504  H HE3  B LYS   A 1 19  ? 9.309  -4.086  15.108  0.28 19.28 ?  19  LYS   A HE3  1 
ATOM   505  H HZ1  A LYS   A 1 19  ? 10.480 -3.341  16.110  0.72 23.57 ?  19  LYS   A HZ1  1 
ATOM   506  H HZ1  B LYS   A 1 19  ? 10.614 -2.930  16.568  0.28 19.97 ?  19  LYS   A HZ1  1 
ATOM   507  H HZ2  A LYS   A 1 19  ? 11.070 -4.654  15.944  0.72 23.57 ?  19  LYS   A HZ2  1 
ATOM   508  H HZ2  B LYS   A 1 19  ? 11.112 -4.288  16.486  0.28 19.97 ?  19  LYS   A HZ2  1 
ATOM   509  H HZ3  A LYS   A 1 19  ? 11.639 -3.512  15.259  0.72 23.57 ?  19  LYS   A HZ3  1 
ATOM   510  H HZ3  B LYS   A 1 19  ? 11.810 -3.218  15.803  0.28 19.97 ?  19  LYS   A HZ3  1 
ATOM   511  N N    A ASN   A 1 20  ? 8.538  -4.757  9.208   0.72 13.55 ?  20  ASN   A N    1 
ATOM   512  N N    B ASN   A 1 20  ? 8.577  -4.581  9.703   0.28 14.25 ?  20  ASN   A N    1 
ATOM   513  C CA   A ASN   A 1 20  ? 8.332  -3.421  8.650   0.72 15.33 ?  20  ASN   A CA   1 
ATOM   514  C CA   B ASN   A 1 20  ? 8.280  -3.304  9.057   0.28 15.56 ?  20  ASN   A CA   1 
ATOM   515  C C    A ASN   A 1 20  ? 8.958  -2.423  9.620   0.72 16.35 ?  20  ASN   A C    1 
ATOM   516  C C    B ASN   A 1 20  ? 8.880  -2.193  9.905   0.28 15.95 ?  20  ASN   A C    1 
ATOM   517  O O    A ASN   A 1 20  ? 8.446  -2.222  10.726  0.72 17.56 ?  20  ASN   A O    1 
ATOM   518  O O    B ASN   A 1 20  ? 8.317  -1.799  10.930  0.28 16.40 ?  20  ASN   A O    1 
ATOM   519  C CB   A ASN   A 1 20  ? 6.836  -3.174  8.445   0.72 16.27 ?  20  ASN   A CB   1 
ATOM   520  C CB   B ASN   A 1 20  ? 6.777  -3.113  8.905   0.28 16.54 ?  20  ASN   A CB   1 
ATOM   521  C CG   A ASN   A 1 20  ? 6.506  -1.747  7.995   0.72 17.46 ?  20  ASN   A CG   1 
ATOM   522  C CG   B ASN   A 1 20  ? 6.396  -1.661  8.687   0.28 17.55 ?  20  ASN   A CG   1 
ATOM   523  O OD1  A ASN   A 1 20  ? 5.477  -1.193  8.385   0.72 19.52 ?  20  ASN   A OD1  1 
ATOM   524  O OD1  B ASN   A 1 20  ? 5.593  -1.098  9.432   0.28 18.32 ?  20  ASN   A OD1  1 
ATOM   525  N ND2  A ASN   A 1 20  ? 7.367  -1.159  7.167   0.72 17.56 ?  20  ASN   A ND2  1 
ATOM   526  N ND2  B ASN   A 1 20  ? 6.991  -1.040  7.675   0.28 17.53 ?  20  ASN   A ND2  1 
ATOM   527  H H    A ASN   A 1 20  ? 7.853  -5.086  9.618   0.72 16.28 ?  20  ASN   A H    1 
ATOM   528  H H    B ASN   A 1 20  ? 7.916  -4.927  10.126  0.28 17.12 ?  20  ASN   A H    1 
ATOM   529  H HA   A ASN   A 1 20  ? 8.781  -3.365  7.797   0.72 18.41 ?  20  ASN   A HA   1 
ATOM   530  H HA   B ASN   A 1 20  ? 8.693  -3.280  8.178   0.28 18.69 ?  20  ASN   A HA   1 
ATOM   531  H HB2  A ASN   A 1 20  ? 6.509  -3.786  7.766   0.72 19.55 ?  20  ASN   A HB2  1 
ATOM   532  H HB2  B ASN   A 1 20  ? 6.470  -3.623  8.140   0.28 19.87 ?  20  ASN   A HB2  1 
ATOM   533  H HB3  A ASN   A 1 20  ? 6.375  -3.345  9.284   0.72 19.55 ?  20  ASN   A HB3  1 
ATOM   534  H HB3  B ASN   A 1 20  ? 6.337  -3.425  9.711   0.28 19.87 ?  20  ASN   A HB3  1 
ATOM   535  H HD21 A ASN   A 1 20  ? 7.217  -0.360  6.896   0.72 21.09 ?  20  ASN   A HD21 1 
ATOM   536  H HD21 B ASN   A 1 20  ? 6.810  -0.216  7.513   0.28 21.06 ?  20  ASN   A HD21 1 
ATOM   537  H HD22 A ASN   A 1 20  ? 8.073  -1.579  6.908   0.72 21.09 ?  20  ASN   A HD22 1 
ATOM   538  H HD22 B ASN   A 1 20  ? 7.553  -1.464  7.179   0.28 21.06 ?  20  ASN   A HD22 1 
ATOM   539  N N    A ALA   A 1 21  ? 10.091 -1.833  9.241   0.72 16.53 ?  21  ALA   A N    1 
ATOM   540  N N    B ALA   A 1 21  ? 10.023 -1.674  9.471   0.28 16.10 ?  21  ALA   A N    1 
ATOM   541  C CA   A ALA   A 1 21  ? 10.795 -0.963  10.174  0.72 16.59 ?  21  ALA   A CA   1 
ATOM   542  C CA   B ALA   A 1 21  ? 10.709 -0.642  10.230  0.28 16.00 ?  21  ALA   A CA   1 
ATOM   543  C C    A ALA   A 1 21  ? 11.751 -0.043  9.431   0.72 16.07 ?  21  ALA   A C    1 
ATOM   544  C C    B ALA   A 1 21  ? 11.750 0.012   9.339   0.28 15.58 ?  21  ALA   A C    1 
ATOM   545  O O    A ALA   A 1 21  ? 12.215 -0.358  8.330   0.72 16.82 ?  21  ALA   A O    1 
ATOM   546  O O    B ALA   A 1 21  ? 12.219 -0.578  8.360   0.28 15.72 ?  21  ALA   A O    1 
ATOM   547  C CB   A ALA   A 1 21  ? 11.564 -1.775  11.221  0.72 17.35 ?  21  ALA   A CB   1 
ATOM   548  C CB   B ALA   A 1 21  ? 11.395 -1.223  11.467  0.28 16.39 ?  21  ALA   A CB   1 
ATOM   549  H H    A ALA   A 1 21  ? 10.462 -1.924  8.473   0.72 19.86 ?  21  ALA   A H    1 
ATOM   550  H H    B ALA   A 1 21  ? 10.415 -1.901  8.740   0.28 19.34 ?  21  ALA   A H    1 
ATOM   551  H HA   A ALA   A 1 21  ? 10.146 -0.414  10.640  0.72 19.93 ?  21  ALA   A HA   1 
ATOM   552  H HA   B ALA   A 1 21  ? 10.062 0.025   10.516  0.28 19.22 ?  21  ALA   A HA   1 
ATOM   553  H HB1  A ALA   A 1 21  ? 11.998 -1.165  11.835  0.72 20.84 ?  21  ALA   A HB1  1 
ATOM   554  H HB1  B ALA   A 1 21  ? 11.853 -0.507  11.934  0.28 19.69 ?  21  ALA   A HB1  1 
ATOM   555  H HB2  A ALA   A 1 21  ? 10.935 -2.339  11.707  0.72 20.84 ?  21  ALA   A HB2  1 
ATOM   556  H HB2  B ALA   A 1 21  ? 10.728 -1.623  12.042  0.28 19.69 ?  21  ALA   A HB2  1 
ATOM   557  H HB3  A ALA   A 1 21  ? 12.222 -2.327  10.775  0.72 20.84 ?  21  ALA   A HB3  1 
ATOM   558  H HB3  B ALA   A 1 21  ? 12.036 -1.894  11.182  0.28 19.69 ?  21  ALA   A HB3  1 
ATOM   559  N N    A ASP   A 1 22  ? 12.025 1.102   10.061  0.72 15.82 ?  22  ASP   A N    1 
ATOM   560  N N    B ASP   A 1 22  ? 12.099 1.243   9.696   0.28 15.52 ?  22  ASP   A N    1 
ATOM   561  C CA   A ASP   A 1 22  ? 13.054 2.040   9.619   0.72 15.40 ?  22  ASP   A CA   1 
ATOM   562  C CA   B ASP   A 1 22  ? 13.281 1.884   9.139   0.28 15.69 ?  22  ASP   A CA   1 
ATOM   563  C C    A ASP   A 1 22  ? 14.385 1.562   10.193  0.72 14.22 ?  22  ASP   A C    1 
ATOM   564  C C    B ASP   A 1 22  ? 14.514 1.239   9.759   0.28 14.93 ?  22  ASP   A C    1 
ATOM   565  O O    A ASP   A 1 22  ? 14.570 1.553   11.414  0.72 14.78 ?  22  ASP   A O    1 
ATOM   566  O O    B ASP   A 1 22  ? 14.625 1.148   10.985  0.28 15.13 ?  22  ASP   A O    1 
ATOM   567  C CB   A ASP   A 1 22  ? 12.692 3.440   10.116  0.72 17.16 ?  22  ASP   A CB   1 
ATOM   568  C CB   B ASP   A 1 22  ? 13.247 3.374   9.479   0.28 16.99 ?  22  ASP   A CB   1 
ATOM   569  C CG   A ASP   A 1 22  ? 13.704 4.505   9.700   0.72 19.48 ?  22  ASP   A CG   1 
ATOM   570  C CG   B ASP   A 1 22  ? 14.348 4.165   8.807   0.28 18.02 ?  22  ASP   A CG   1 
ATOM   571  O OD1  A ASP   A 1 22  ? 14.852 4.171   9.356   0.72 20.06 ?  22  ASP   A OD1  1 
ATOM   572  O OD1  B ASP   A 1 22  ? 15.245 3.550   8.200   0.28 18.35 ?  22  ASP   A OD1  1 
ATOM   573  O OD2  A ASP   A 1 22  ? 13.349 5.699   9.732   0.72 21.50 -1 22  ASP   A OD2  1 
ATOM   574  O OD2  B ASP   A 1 22  ? 14.314 5.412   8.892   0.28 18.77 -1 22  ASP   A OD2  1 
ATOM   575  H H    A ASP   A 1 22  ? 11.605 1.366   10.768  0.72 19.01 ?  22  ASP   A H    1 
ATOM   576  H H    B ASP   A 1 22  ? 11.663 1.726   10.261  0.28 18.65 ?  22  ASP   A H    1 
ATOM   577  H HA   A ASP   A 1 22  ? 13.104 2.047   8.654   0.72 18.50 ?  22  ASP   A HA   1 
ATOM   578  H HA   B ASP   A 1 22  ? 13.297 1.768   8.173   0.28 18.84 ?  22  ASP   A HA   1 
ATOM   579  H HB2  A ASP   A 1 22  ? 11.821 3.689   9.750   0.72 20.61 ?  22  ASP   A HB2  1 
ATOM   580  H HB2  B ASP   A 1 22  ? 12.402 3.747   9.201   0.28 20.41 ?  22  ASP   A HB2  1 
ATOM   581  H HB3  A ASP   A 1 22  ? 12.635 3.427   11.088  0.72 20.61 ?  22  ASP   A HB3  1 
ATOM   582  H HB3  B ASP   A 1 22  ? 13.366 3.471   10.432  0.28 20.41 ?  22  ASP   A HB3  1 
ATOM   583  N N    A ILE   A 1 23  ? 15.305 1.150   9.313   0.72 13.87 ?  23  ILE   A N    1 
ATOM   584  N N    B ILE   A 1 23  ? 15.436 0.775   8.911   0.28 14.44 ?  23  ILE   A N    1 
ATOM   585  C CA   A ILE   A 1 23  ? 16.558 0.534   9.748   0.72 13.42 ?  23  ILE   A CA   1 
ATOM   586  C CA   B ILE   A 1 23  ? 16.640 0.110   9.410   0.28 14.19 ?  23  ILE   A CA   1 
ATOM   587  C C    A ILE   A 1 23  ? 17.361 1.476   10.632  0.72 13.54 ?  23  ILE   A C    1 
ATOM   588  C C    B ILE   A 1 23  ? 17.422 1.038   10.327  0.28 14.54 ?  23  ILE   A C    1 
ATOM   589  O O    A ILE   A 1 23  ? 18.085 1.026   11.530  0.72 14.02 ?  23  ILE   A O    1 
ATOM   590  O O    B ILE   A 1 23  ? 18.075 0.584   11.275  0.28 14.27 ?  23  ILE   A O    1 
ATOM   591  C CB   A ILE   A 1 23  ? 17.361 0.028   8.529   0.72 13.19 ?  23  ILE   A CB   1 
ATOM   592  C CB   B ILE   A 1 23  ? 17.505 -0.434  8.250   0.28 13.69 ?  23  ILE   A CB   1 
ATOM   593  C CG1  A ILE   A 1 23  ? 18.495 -0.900  8.973   0.72 13.21 ?  23  ILE   A CG1  1 
ATOM   594  C CG1  B ILE   A 1 23  ? 18.601 -1.359  8.793   0.28 13.24 ?  23  ILE   A CG1  1 
ATOM   595  C CG2  A ILE   A 1 23  ? 17.872 1.197   7.678   0.72 13.37 ?  23  ILE   A CG2  1 
ATOM   596  C CG2  B ILE   A 1 23  ? 18.125 0.703   7.445   0.28 13.60 ?  23  ILE   A CG2  1 
ATOM   597  C CD1  A ILE   A 1 23  ? 19.174 -1.613  7.822   0.72 13.80 ?  23  ILE   A CD1  1 
ATOM   598  C CD1  B ILE   A 1 23  ? 19.482 -1.990  7.721   0.28 12.99 ?  23  ILE   A CD1  1 
ATOM   599  H H    A ILE   A 1 23  ? 15.217 1.216   8.464   0.72 16.67 ?  23  ILE   A H    1 
ATOM   600  H H    B ILE   A 1 23  ? 15.388 0.835   8.066   0.28 17.35 ?  23  ILE   A H    1 
ATOM   601  H HA   A ILE   A 1 23  ? 16.342 -0.238  10.287  0.72 16.13 ?  23  ILE   A HA   1 
ATOM   602  H HA   B ILE   A 1 23  ? 16.361 -0.653  9.937   0.28 17.05 ?  23  ILE   A HA   1 
ATOM   603  H HB   A ILE   A 1 23  ? 16.756 -0.487  7.978   0.72 15.84 ?  23  ILE   A HB   1 
ATOM   604  H HB   B ILE   A 1 23  ? 16.937 -0.952  7.660   0.28 16.44 ?  23  ILE   A HB   1 
ATOM   605  H HG12 A ILE   A 1 23  ? 19.170 -0.377  9.434   0.72 15.88 ?  23  ILE   A HG12 1 
ATOM   606  H HG12 B ILE   A 1 23  ? 19.179 -0.848  9.381   0.28 15.91 ?  23  ILE   A HG12 1 
ATOM   607  H HG13 A ILE   A 1 23  ? 18.135 -1.574  9.567   0.72 15.88 ?  23  ILE   A HG13 1 
ATOM   608  H HG13 B ILE   A 1 23  ? 18.184 -2.079  9.291   0.28 15.91 ?  23  ILE   A HG13 1 
ATOM   609  H HG21 A ILE   A 1 23  ? 18.229 0.851   6.845   0.72 16.06 ?  23  ILE   A HG21 1 
ATOM   610  H HG21 B ILE   A 1 23  ? 18.479 0.343   6.613   0.28 16.35 ?  23  ILE   A HG21 1 
ATOM   611  H HG22 A ILE   A 1 23  ? 17.131 1.800   7.489   0.72 16.06 ?  23  ILE   A HG22 1 
ATOM   612  H HG22 B ILE   A 1 23  ? 17.444 1.363   7.254   0.28 16.35 ?  23  ILE   A HG22 1 
ATOM   613  H HG23 A ILE   A 1 23  ? 18.563 1.671   8.164   0.72 16.06 ?  23  ILE   A HG23 1 
ATOM   614  H HG23 B ILE   A 1 23  ? 18.842 1.103   7.961   0.28 16.35 ?  23  ILE   A HG23 1 
ATOM   615  H HD11 A ILE   A 1 23  ? 19.828 -2.233  8.178   0.72 16.57 ?  23  ILE   A HD11 1 
ATOM   616  H HD11 B ILE   A 1 23  ? 20.070 -2.641  8.138   0.28 15.61 ?  23  ILE   A HD11 1 
ATOM   617  H HD12 A ILE   A 1 23  ? 18.503 -2.094  7.312   0.72 16.57 ?  23  ILE   A HD12 1 
ATOM   618  H HD12 B ILE   A 1 23  ? 18.917 -2.428  7.066   0.28 15.61 ?  23  ILE   A HD12 1 
ATOM   619  H HD13 A ILE   A 1 23  ? 19.611 -0.956  7.257   0.72 16.57 ?  23  ILE   A HD13 1 
ATOM   620  H HD13 B ILE   A 1 23  ? 20.009 -1.297  7.293   0.28 15.61 ?  23  ILE   A HD13 1 
ATOM   621  N N    A VAL   A 1 24  ? 17.236 2.787   10.413  0.72 14.16 ?  24  VAL   A N    1 
ATOM   622  N N    B VAL   A 1 24  ? 17.363 2.345   10.073  0.28 15.58 ?  24  VAL   A N    1 
ATOM   623  C CA   A VAL   A 1 24  ? 17.918 3.754   11.271  0.72 15.45 ?  24  VAL   A CA   1 
ATOM   624  C CA   B VAL   A 1 24  ? 18.011 3.306   10.960  0.28 16.70 ?  24  VAL   A CA   1 
ATOM   625  C C    A VAL   A 1 24  ? 17.391 3.658   12.695  0.72 15.97 ?  24  VAL   A C    1 
ATOM   626  C C    B VAL   A 1 24  ? 17.354 3.286   12.335  0.28 17.50 ?  24  VAL   A C    1 
ATOM   627  O O    A VAL   A 1 24  ? 18.159 3.549   13.661  0.72 16.75 ?  24  VAL   A O    1 
ATOM   628  O O    B VAL   A 1 24  ? 18.030 3.396   13.365  0.28 18.08 ?  24  VAL   A O    1 
ATOM   629  C CB   A VAL   A 1 24  ? 17.763 5.176   10.702  0.72 16.50 ?  24  VAL   A CB   1 
ATOM   630  C CB   B VAL   A 1 24  ? 17.989 4.709   10.326  0.28 17.06 ?  24  VAL   A CB   1 
ATOM   631  C CG1  A VAL   A 1 24  ? 18.267 6.213   11.698  0.72 17.19 ?  24  VAL   A CG1  1 
ATOM   632  C CG1  B VAL   A 1 24  ? 18.685 5.710   11.229  0.28 17.54 ?  24  VAL   A CG1  1 
ATOM   633  C CG2  A VAL   A 1 24  ? 18.494 5.300   9.371   0.72 17.37 ?  24  VAL   A CG2  1 
ATOM   634  C CG2  B VAL   A 1 24  ? 18.640 4.671   8.951   0.28 16.80 ?  24  VAL   A CG2  1 
ATOM   635  H H    A VAL   A 1 24  ? 16.769 3.140   9.780   0.72 17.01 ?  24  VAL   A H    1 
ATOM   636  H H    B VAL   A 1 24  ? 16.963 2.696   9.400   0.28 18.71 ?  24  VAL   A H    1 
ATOM   637  H HA   A VAL   A 1 24  ? 18.865 3.548   11.286  0.72 18.56 ?  24  VAL   A HA   1 
ATOM   638  H HA   B VAL   A 1 24  ? 18.938 3.049   11.074  0.28 20.06 ?  24  VAL   A HA   1 
ATOM   639  H HB   A VAL   A 1 24  ? 16.823 5.353   10.537  0.72 19.82 ?  24  VAL   A HB   1 
ATOM   640  H HB   B VAL   A 1 24  ? 17.067 4.992   10.214  0.28 20.50 ?  24  VAL   A HB   1 
ATOM   641  H HG11 A VAL   A 1 24  ? 18.444 7.042   11.227  0.72 20.65 ?  24  VAL   A HG11 1 
ATOM   642  H HG11 B VAL   A 1 24  ? 18.804 6.540   10.742  0.28 21.06 ?  24  VAL   A HG11 1 
ATOM   643  H HG12 A VAL   A 1 24  ? 17.588 6.355   12.373  0.72 20.65 ?  24  VAL   A HG12 1 
ATOM   644  H HG12 B VAL   A 1 24  ? 18.137 5.863   12.014  0.28 21.06 ?  24  VAL   A HG12 1 
ATOM   645  H HG13 A VAL   A 1 24  ? 19.084 5.885   12.107  0.72 20.65 ?  24  VAL   A HG13 1 
ATOM   646  H HG13 B VAL   A 1 24  ? 19.548 5.352   11.488  0.28 21.06 ?  24  VAL   A HG13 1 
ATOM   647  H HG21 A VAL   A 1 24  ? 18.261 6.147   8.957   0.72 20.86 ?  24  VAL   A HG21 1 
ATOM   648  H HG21 B VAL   A 1 24  ? 18.734 5.577   8.621   0.28 20.17 ?  24  VAL   A HG21 1 
ATOM   649  H HG22 A VAL   A 1 24  ? 19.451 5.268   9.531   0.72 20.86 ?  24  VAL   A HG22 1 
ATOM   650  H HG22 B VAL   A 1 24  ? 19.513 4.254   9.028   0.28 20.17 ?  24  VAL   A HG22 1 
ATOM   651  H HG23 A VAL   A 1 24  ? 18.231 4.568   8.791   0.72 20.86 ?  24  VAL   A HG23 1 
ATOM   652  H HG23 B VAL   A 1 24  ? 18.081 4.156   8.348   0.28 20.17 ?  24  VAL   A HG23 1 
ATOM   653  N N    A GLU   A 1 25  ? 16.066 3.699   12.845  0.72 16.45 ?  25  GLU   A N    1 
ATOM   654  N N    B GLU   A 1 25  ? 16.028 3.138   12.374  0.28 17.83 ?  25  GLU   A N    1 
ATOM   655  C CA   A GLU   A 1 25  ? 15.472 3.630   14.174  0.72 17.72 ?  25  GLU   A CA   1 
ATOM   656  C CA   B GLU   A 1 25  ? 15.332 3.068   13.655  0.28 18.49 ?  25  GLU   A CA   1 
ATOM   657  C C    A GLU   A 1 25  ? 15.710 2.268   14.812  0.72 16.80 ?  25  GLU   A C    1 
ATOM   658  C C    B GLU   A 1 25  ? 15.631 1.760   14.379  0.28 18.22 ?  25  GLU   A C    1 
ATOM   659  O O    A GLU   A 1 25  ? 15.940 2.176   16.023  0.72 17.63 ?  25  GLU   A O    1 
ATOM   660  O O    B GLU   A 1 25  ? 15.814 1.750   15.602  0.28 18.41 ?  25  GLU   A O    1 
ATOM   661  C CB   A GLU   A 1 25  ? 13.980 3.961   14.094  0.72 20.04 ?  25  GLU   A CB   1 
ATOM   662  C CB   B GLU   A 1 25  ? 13.829 3.255   13.447  0.28 19.63 ?  25  GLU   A CB   1 
ATOM   663  C CG   A GLU   A 1 25  ? 13.711 5.408   13.705  0.72 23.19 ?  25  GLU   A CG   1 
ATOM   664  C CG   B GLU   A 1 25  ? 13.458 4.630   12.910  0.28 21.20 ?  25  GLU   A CG   1 
ATOM   665  C CD   A GLU   A 1 25  ? 14.489 6.394   14.557  0.72 25.74 ?  25  GLU   A CD   1 
ATOM   666  C CD   B GLU   A 1 25  ? 13.881 5.755   13.837  0.28 22.49 ?  25  GLU   A CD   1 
ATOM   667  O OE1  A GLU   A 1 25  ? 14.517 6.222   15.795  0.72 26.50 ?  25  GLU   A OE1  1 
ATOM   668  O OE1  B GLU   A 1 25  ? 13.866 5.551   15.069  0.28 23.05 ?  25  GLU   A OE1  1 
ATOM   669  O OE2  A GLU   A 1 25  ? 15.090 7.326   13.985  0.72 26.95 -1 25  GLU   A OE2  1 
ATOM   670  O OE2  B GLU   A 1 25  ? 14.238 6.840   13.330  0.28 22.96 -1 25  GLU   A OE2  1 
ATOM   671  H H    A GLU   A 1 25  ? 15.499 3.775   12.201  0.72 19.75 ?  25  GLU   A H    1 
ATOM   672  H H    B GLU   A 1 25  ? 15.519 3.083   11.683  0.28 21.41 ?  25  GLU   A H    1 
ATOM   673  H HA   A GLU   A 1 25  ? 15.898 4.288   14.743  0.72 21.28 ?  25  GLU   A HA   1 
ATOM   674  H HA   B GLU   A 1 25  ? 15.645 3.791   14.216  0.28 22.21 ?  25  GLU   A HA   1 
ATOM   675  H HB2  A GLU   A 1 25  ? 13.562 3.396   13.424  0.72 24.07 ?  25  GLU   A HB2  1 
ATOM   676  H HB2  B GLU   A 1 25  ? 13.514 2.591   12.811  0.28 23.58 ?  25  GLU   A HB2  1 
ATOM   677  H HB3  A GLU   A 1 25  ? 13.569 3.807   14.959  0.72 24.07 ?  25  GLU   A HB3  1 
ATOM   678  H HB3  B GLU   A 1 25  ? 13.378 3.136   14.297  0.28 23.58 ?  25  GLU   A HB3  1 
ATOM   679  H HG2  A GLU   A 1 25  ? 13.974 5.545   12.783  0.72 27.85 ?  25  GLU   A HG2  1 
ATOM   680  H HG2  B GLU   A 1 25  ? 13.906 4.767   12.061  0.28 25.46 ?  25  GLU   A HG2  1 
ATOM   681  H HG3  A GLU   A 1 25  ? 12.765 5.598   13.814  0.72 27.85 ?  25  GLU   A HG3  1 
ATOM   682  H HG3  B GLU   A 1 25  ? 12.496 4.675   12.792  0.28 25.46 ?  25  GLU   A HG3  1 
ATOM   683  N N    A GLU   A 1 26  ? 15.675 1.201   14.009  0.72 16.66 ?  26  GLU   A N    1 
ATOM   684  N N    B GLU   A 1 26  ? 15.687 0.645   13.646  0.28 17.68 ?  26  GLU   A N    1 
ATOM   685  C CA   A GLU   A 1 26  ? 15.959 -0.130  14.535  0.72 16.56 ?  26  GLU   A CA   1 
ATOM   686  C CA   B GLU   A 1 26  ? 16.062 -0.620  14.267  0.28 17.56 ?  26  GLU   A CA   1 
ATOM   687  C C    A GLU   A 1 26  ? 17.389 -0.218  15.051  0.72 16.09 ?  26  GLU   A C    1 
ATOM   688  C C    B GLU   A 1 26  ? 17.468 -0.559  14.845  0.28 16.80 ?  26  GLU   A C    1 
ATOM   689  O O    A GLU   A 1 26  ? 17.636 -0.713  16.157  0.72 16.07 ?  26  GLU   A O    1 
ATOM   690  O O    B GLU   A 1 26  ? 17.757 -1.227  15.845  0.28 16.89 ?  26  GLU   A O    1 
ATOM   691  C CB   A GLU   A 1 26  ? 15.735 -1.172  13.441  0.72 18.06 ?  26  GLU   A CB   1 
ATOM   692  C CB   B GLU   A 1 26  ? 15.963 -1.764  13.253  0.28 18.00 ?  26  GLU   A CB   1 
ATOM   693  C CG   A GLU   A 1 26  ? 14.315 -1.655  13.322  0.72 21.52 ?  26  GLU   A CG   1 
ATOM   694  C CG   B GLU   A 1 26  ? 14.548 -2.218  12.954  0.28 17.83 ?  26  GLU   A CG   1 
ATOM   695  C CD   A GLU   A 1 26  ? 13.876 -2.444  14.539  0.72 23.75 ?  26  GLU   A CD   1 
ATOM   696  C CD   B GLU   A 1 26  ? 13.851 -2.820  14.157  0.28 17.26 ?  26  GLU   A CD   1 
ATOM   697  O OE1  A GLU   A 1 26  ? 14.474 -3.505  14.815  0.72 24.48 ?  26  GLU   A OE1  1 
ATOM   698  O OE1  B GLU   A 1 26  ? 14.230 -3.932  14.605  0.28 17.34 ?  26  GLU   A OE1  1 
ATOM   699  O OE2  A GLU   A 1 26  ? 12.949 -1.982  15.230  0.72 25.71 -1 26  GLU   A OE2  1 
ATOM   700  O OE2  B GLU   A 1 26  ? 12.912 -2.172  14.653  0.28 16.62 -1 26  GLU   A OE2  1 
ATOM   701  H H    A GLU   A 1 26  ? 15.492 1.227   13.169  0.72 20.01 ?  26  GLU   A H    1 
ATOM   702  H H    B GLU   A 1 26  ? 15.519 0.597   12.806  0.28 21.24 ?  26  GLU   A H    1 
ATOM   703  H HA   A GLU   A 1 26  ? 15.357 -0.317  15.268  0.72 19.89 ?  26  GLU   A HA   1 
ATOM   704  H HA   B GLU   A 1 26  ? 15.459 -0.810  14.998  0.28 21.10 ?  26  GLU   A HA   1 
ATOM   705  H HB2  A GLU   A 1 26  ? 15.987 -0.788  12.587  0.72 21.69 ?  26  GLU   A HB2  1 
ATOM   706  H HB2  B GLU   A 1 26  ? 16.358 -1.474  12.416  0.28 21.62 ?  26  GLU   A HB2  1 
ATOM   707  H HB3  A GLU   A 1 26  ? 16.294 -1.942  13.631  0.72 21.69 ?  26  GLU   A HB3  1 
ATOM   708  H HB3  B GLU   A 1 26  ? 16.449 -2.531  13.595  0.28 21.62 ?  26  GLU   A HB3  1 
ATOM   709  H HG2  A GLU   A 1 26  ? 13.724 -0.892  13.246  0.72 25.85 ?  26  GLU   A HG2  1 
ATOM   710  H HG2  B GLU   A 1 26  ? 14.027 -1.455  12.653  0.28 21.42 ?  26  GLU   A HG2  1 
ATOM   711  H HG3  A GLU   A 1 26  ? 14.235 -2.216  12.530  0.72 25.85 ?  26  GLU   A HG3  1 
ATOM   712  H HG3  B GLU   A 1 26  ? 14.567 -2.899  12.268  0.28 21.42 ?  26  GLU   A HG3  1 
ATOM   713  N N    . ALA   A 1 27  ? 18.350 0.244   14.249  1.00 15.93 ?  27  ALA   A N    1 
ATOM   714  C CA   . ALA   A 1 27  ? 19.743 0.235   14.683  1.00 16.58 ?  27  ALA   A CA   1 
ATOM   715  C C    . ALA   A 1 27  ? 19.930 1.035   15.968  1.00 18.79 ?  27  ALA   A C    1 
ATOM   716  O O    . ALA   A 1 27  ? 20.614 0.584   16.894  1.00 18.59 ?  27  ALA   A O    1 
ATOM   717  C CB   . ALA   A 1 27  ? 20.656 0.756   13.568  1.00 15.88 ?  27  ALA   A CB   1 
ATOM   718  H H    A ALA   A 1 27  ? 18.223 0.560   13.456  0.72 19.13 ?  27  ALA   A H    1 
ATOM   719  H H    B ALA   A 1 27  ? 18.168 0.796   13.613  0.28 19.13 ?  27  ALA   A H    1 
ATOM   720  H HA   . ALA   A 1 27  ? 20.003 -0.678  14.863  1.00 19.92 ?  27  ALA   A HA   1 
ATOM   721  H HB1  . ALA   A 1 27  ? 21.579 0.741   13.877  1.00 19.08 ?  27  ALA   A HB1  1 
ATOM   722  H HB2  . ALA   A 1 27  ? 20.567 0.183   12.786  1.00 19.08 ?  27  ALA   A HB2  1 
ATOM   723  H HB3  . ALA   A 1 27  ? 20.403 1.664   13.338  1.00 19.08 ?  27  ALA   A HB3  1 
ATOM   724  N N    A LYS   A 1 28  ? 19.326 2.223   16.046  0.72 20.57 ?  28  LYS   A N    1 
ATOM   725  N N    B LYS   A 1 28  ? 19.318 2.219   16.051  0.28 21.28 ?  28  LYS   A N    1 
ATOM   726  C CA   A LYS   A 1 28  ? 19.477 3.040   17.245  0.72 23.21 ?  28  LYS   A CA   1 
ATOM   727  C CA   B LYS   A 1 28  ? 19.453 3.032   17.256  0.28 24.10 ?  28  LYS   A CA   1 
ATOM   728  C C    A LYS   A 1 28  ? 18.915 2.342   18.476  0.72 24.05 ?  28  LYS   A C    1 
ATOM   729  C C    B LYS   A 1 28  ? 18.889 2.325   18.482  0.28 25.27 ?  28  LYS   A C    1 
ATOM   730  O O    A LYS   A 1 28  ? 19.445 2.513   19.580  0.72 25.38 ?  28  LYS   A O    1 
ATOM   731  O O    B LYS   A 1 28  ? 19.403 2.506   19.592  0.28 25.79 ?  28  LYS   A O    1 
ATOM   732  C CB   A LYS   A 1 28  ? 18.831 4.412   17.042  0.72 25.67 ?  28  LYS   A CB   1 
ATOM   733  C CB   B LYS   A 1 28  ? 18.780 4.393   17.058  0.28 25.86 ?  28  LYS   A CB   1 
ATOM   734  C CG   A LYS   A 1 28  ? 19.659 5.338   16.166  0.72 28.11 ?  28  LYS   A CG   1 
ATOM   735  C CG   B LYS   A 1 28  ? 19.542 5.321   16.125  0.28 27.55 ?  28  LYS   A CG   1 
ATOM   736  C CD   A LYS   A 1 28  ? 19.169 6.773   16.220  0.72 30.82 ?  28  LYS   A CD   1 
ATOM   737  C CD   B LYS   A 1 28  ? 19.077 6.766   16.248  0.28 29.25 ?  28  LYS   A CD   1 
ATOM   738  C CE   A LYS   A 1 28  ? 17.878 6.947   15.449  0.72 32.74 ?  28  LYS   A CE   1 
ATOM   739  C CE   B LYS   A 1 28  ? 17.740 6.992   15.564  0.28 30.45 ?  28  LYS   A CE   1 
ATOM   740  N NZ   A LYS   A 1 28  ? 17.467 8.376   15.397  0.72 33.96 ?  28  LYS   A NZ   1 
ATOM   741  N NZ   B LYS   A 1 28  ? 17.396 8.440   15.504  0.28 31.20 ?  28  LYS   A NZ   1 
ATOM   742  H H    A LYS   A 1 28  ? 18.837 2.568   15.432  0.72 24.70 ?  28  LYS   A H    1 
ATOM   743  H H    B LYS   A 1 28  ? 18.831 2.564   15.434  0.28 25.55 ?  28  LYS   A H    1 
ATOM   744  H HA   A LYS   A 1 28  ? 20.419 3.185   17.405  0.72 27.87 ?  28  LYS   A HA   1 
ATOM   745  H HA   B LYS   A 1 28  ? 20.393 3.192   17.418  0.28 28.94 ?  28  LYS   A HA   1 
ATOM   746  H HB2  A LYS   A 1 28  ? 17.967 4.298   16.617  0.72 30.82 ?  28  LYS   A HB2  1 
ATOM   747  H HB2  B LYS   A 1 28  ? 17.897 4.257   16.682  0.28 31.05 ?  28  LYS   A HB2  1 
ATOM   748  H HB3  A LYS   A 1 28  ? 18.721 4.842   17.905  0.72 30.82 ?  28  LYS   A HB3  1 
ATOM   749  H HB3  B LYS   A 1 28  ? 18.707 4.834   17.919  0.28 31.05 ?  28  LYS   A HB3  1 
ATOM   750  H HG2  A LYS   A 1 28  ? 20.580 5.324   16.469  0.72 33.75 ?  28  LYS   A HG2  1 
ATOM   751  H HG2  B LYS   A 1 28  ? 20.486 5.289   16.344  0.28 33.08 ?  28  LYS   A HG2  1 
ATOM   752  H HG3  A LYS   A 1 28  ? 19.606 5.037   15.246  0.72 33.75 ?  28  LYS   A HG3  1 
ATOM   753  H HG3  B LYS   A 1 28  ? 19.402 5.037   15.208  0.28 33.08 ?  28  LYS   A HG3  1 
ATOM   754  H HD2  A LYS   A 1 28  ? 19.007 7.023   17.143  0.72 37.00 ?  28  LYS   A HD2  1 
ATOM   755  H HD2  B LYS   A 1 28  ? 18.978 6.991   17.187  0.28 35.12 ?  28  LYS   A HD2  1 
ATOM   756  H HD3  A LYS   A 1 28  ? 19.838 7.356   15.827  0.72 37.00 ?  28  LYS   A HD3  1 
ATOM   757  H HD3  B LYS   A 1 28  ? 19.732 7.348   15.833  0.28 35.12 ?  28  LYS   A HD3  1 
ATOM   758  H HE2  A LYS   A 1 28  ? 18.005 6.631   14.541  0.72 39.31 ?  28  LYS   A HE2  1 
ATOM   759  H HE2  B LYS   A 1 28  ? 17.783 6.652   14.657  0.28 36.56 ?  28  LYS   A HE2  1 
ATOM   760  H HE3  A LYS   A 1 28  ? 17.174 6.442   15.885  0.72 39.31 ?  28  LYS   A HE3  1 
ATOM   761  H HE3  B LYS   A 1 28  ? 17.044 6.535   16.061  0.28 36.56 ?  28  LYS   A HE3  1 
ATOM   762  H HZ1  A LYS   A 1 28  ? 16.708 8.458   14.940  0.72 40.78 ?  28  LYS   A HZ1  1 
ATOM   763  H HZ1  B LYS   A 1 28  ? 16.612 8.551   15.100  0.28 37.46 ?  28  LYS   A HZ1  1 
ATOM   764  H HZ2  A LYS   A 1 28  ? 17.344 8.687   16.222  0.72 40.78 ?  28  LYS   A HZ2  1 
ATOM   765  H HZ2  B LYS   A 1 28  ? 17.348 8.776   16.327  0.28 37.46 ?  28  LYS   A HZ2  1 
ATOM   766  H HZ3  A LYS   A 1 28  ? 18.099 8.859   14.997  0.72 40.78 ?  28  LYS   A HZ3  1 
ATOM   767  H HZ3  B LYS   A 1 28  ? 18.021 8.882   15.048  0.28 37.46 ?  28  LYS   A HZ3  1 
ATOM   768  N N    A LYS   A 1 29  ? 17.859 1.544   18.309  0.72 24.43 ?  29  LYS   A N    1 
ATOM   769  N N    B LYS   A 1 29  ? 17.842 1.517   18.307  0.28 26.10 ?  29  LYS   A N    1 
ATOM   770  C CA   A LYS   A 1 29  ? 17.263 0.840   19.440  0.72 25.96 ?  29  LYS   A CA   1 
ATOM   771  C CA   B LYS   A 1 29  ? 17.233 0.824   19.438  0.28 27.18 ?  29  LYS   A CA   1 
ATOM   772  C C    A LYS   A 1 29  ? 18.082 -0.387  19.827  0.72 25.57 ?  29  LYS   A C    1 
ATOM   773  C C    B LYS   A 1 29  ? 18.032 -0.414  19.832  0.28 26.17 ?  29  LYS   A C    1 
ATOM   774  O O    A LYS   A 1 29  ? 18.402 -0.584  21.006  0.72 26.49 ?  29  LYS   A O    1 
ATOM   775  O O    B LYS   A 1 29  ? 18.295 -0.641  21.018  0.28 26.51 ?  29  LYS   A O    1 
ATOM   776  C CB   A LYS   A 1 29  ? 15.828 0.430   19.095  0.72 28.32 ?  29  LYS   A CB   1 
ATOM   777  C CB   B LYS   A 1 29  ? 15.795 0.432   19.088  0.28 29.18 ?  29  LYS   A CB   1 
ATOM   778  C CG   A LYS   A 1 29  ? 15.080 -0.260  20.227  0.72 31.03 ?  29  LYS   A CG   1 
ATOM   779  C CG   B LYS   A 1 29  ? 15.010 -0.185  20.236  0.28 31.07 ?  29  LYS   A CG   1 
ATOM   780  C CD   A LYS   A 1 29  ? 14.748 0.713   21.345  0.72 33.75 ?  29  LYS   A CD   1 
ATOM   781  C CD   B LYS   A 1 29  ? 14.668 0.848   21.296  0.28 32.74 ?  29  LYS   A CD   1 
ATOM   782  C CE   A LYS   A 1 29  ? 13.871 0.063   22.403  0.72 35.65 ?  29  LYS   A CE   1 
ATOM   783  C CE   B LYS   A 1 29  ? 13.782 0.255   22.380  0.28 33.93 ?  29  LYS   A CE   1 
ATOM   784  N NZ   A LYS   A 1 29  ? 13.456 1.038   23.448  0.72 36.81 ?  29  LYS   A NZ   1 
ATOM   785  N NZ   B LYS   A 1 29  ? 13.399 1.271   23.399  0.28 34.61 ?  29  LYS   A NZ   1 
ATOM   786  H H    A LYS   A 1 29  ? 17.470 1.399   17.555  0.72 29.34 ?  29  LYS   A H    1 
ATOM   787  H H    B LYS   A 1 29  ? 17.465 1.362   17.549  0.28 31.34 ?  29  LYS   A H    1 
ATOM   788  H HA   A LYS   A 1 29  ? 17.229 1.434   20.204  0.72 31.17 ?  29  LYS   A HA   1 
ATOM   789  H HA   B LYS   A 1 29  ? 17.206 1.422   20.200  0.28 32.63 ?  29  LYS   A HA   1 
ATOM   790  H HB2  A LYS   A 1 29  ? 15.327 1.225   18.856  0.72 34.00 ?  29  LYS   A HB2  1 
ATOM   791  H HB2  B LYS   A 1 29  ? 15.318 1.226   18.801  0.28 35.03 ?  29  LYS   A HB2  1 
ATOM   792  H HB3  A LYS   A 1 29  ? 15.850 -0.181  18.343  0.72 34.00 ?  29  LYS   A HB3  1 
ATOM   793  H HB3  B LYS   A 1 29  ? 15.817 -0.215  18.366  0.28 35.03 ?  29  LYS   A HB3  1 
ATOM   794  H HG2  A LYS   A 1 29  ? 14.247 -0.622  19.885  0.72 37.26 ?  29  LYS   A HG2  1 
ATOM   795  H HG2  B LYS   A 1 29  ? 14.180 -0.553  19.894  0.28 37.30 ?  29  LYS   A HG2  1 
ATOM   796  H HG3  A LYS   A 1 29  ? 15.626 -0.973  20.596  0.72 37.26 ?  29  LYS   A HG3  1 
ATOM   797  H HG3  B LYS   A 1 29  ? 15.538 -0.885  20.653  0.28 37.30 ?  29  LYS   A HG3  1 
ATOM   798  H HD2  A LYS   A 1 29  ? 15.569 1.007   21.770  0.72 40.52 ?  29  LYS   A HD2  1 
ATOM   799  H HD2  B LYS   A 1 29  ? 15.485 1.166   21.711  0.28 39.31 ?  29  LYS   A HD2  1 
ATOM   800  H HD3  A LYS   A 1 29  ? 14.269 1.472   20.977  0.72 40.52 ?  29  LYS   A HD3  1 
ATOM   801  H HD3  B LYS   A 1 29  ? 14.192 1.586   20.883  0.28 39.31 ?  29  LYS   A HD3  1 
ATOM   802  H HE2  A LYS   A 1 29  ? 13.071 -0.290  21.981  0.72 42.80 ?  29  LYS   A HE2  1 
ATOM   803  H HE2  B LYS   A 1 29  ? 12.970 -0.090  21.976  0.28 40.73 ?  29  LYS   A HE2  1 
ATOM   804  H HE3  A LYS   A 1 29  ? 14.366 -0.652  22.833  0.72 42.80 ?  29  LYS   A HE3  1 
ATOM   805  H HE3  B LYS   A 1 29  ? 14.262 -0.459  22.829  0.28 40.73 ?  29  LYS   A HE3  1 
ATOM   806  H HZ1  A LYS   A 1 29  ? 12.945 0.635   24.054  0.72 44.19 ?  29  LYS   A HZ1  1 
ATOM   807  H HZ1  B LYS   A 1 29  ? 12.882 0.898   24.020  0.28 41.55 ?  29  LYS   A HZ1  1 
ATOM   808  H HZ2  A LYS   A 1 29  ? 14.174 1.374   23.853  0.72 44.19 ?  29  LYS   A HZ2  1 
ATOM   809  H HZ2  B LYS   A 1 29  ? 14.128 1.600   23.789  0.28 41.55 ?  29  LYS   A HZ2  1 
ATOM   810  H HZ3  A LYS   A 1 29  ? 12.995 1.703   23.077  0.72 44.19 ?  29  LYS   A HZ3  1 
ATOM   811  H HZ3  B LYS   A 1 29  ? 12.952 1.936   23.012  0.28 41.55 ?  29  LYS   A HZ3  1 
ATOM   812  N N    . VAL   A 1 30  ? 18.419 -1.228  18.849  1.00 24.84 ?  30  VAL   A N    1 
ATOM   813  C CA   . VAL   A 1 30  ? 19.067 -2.502  19.146  1.00 23.53 ?  30  VAL   A CA   1 
ATOM   814  C C    . VAL   A 1 30  ? 20.568 -2.342  19.374  1.00 22.25 ?  30  VAL   A C    1 
ATOM   815  O O    . VAL   A 1 30  ? 21.157 -3.065  20.185  1.00 22.72 ?  30  VAL   A O    1 
ATOM   816  C CB   . VAL   A 1 30  ? 18.768 -3.499  18.011  1.00 24.17 ?  30  VAL   A CB   1 
ATOM   817  C CG1  . VAL   A 1 30  ? 19.532 -4.801  18.213  1.00 24.58 ?  30  VAL   A CG1  1 
ATOM   818  C CG2  . VAL   A 1 30  ? 17.269 -3.762  17.910  1.00 24.75 ?  30  VAL   A CG2  1 
ATOM   819  H H    A VAL   A 1 30  ? 18.279 -1.087  18.013  0.72 29.82 ?  30  VAL   A H    1 
ATOM   820  H H    B VAL   A 1 30  ? 18.311 -1.070  18.012  0.28 29.82 ?  30  VAL   A H    1 
ATOM   821  H HA   . VAL   A 1 30  ? 18.675 -2.864  19.954  1.00 28.25 ?  30  VAL   A HA   1 
ATOM   822  H HB   . VAL   A 1 30  ? 19.056 -3.117  17.167  1.00 29.03 ?  30  VAL   A HB   1 
ATOM   823  H HG11 . VAL   A 1 30  ? 19.161 -5.480  17.625  1.00 29.51 ?  30  VAL   A HG11 1 
ATOM   824  H HG12 . VAL   A 1 30  ? 20.466 -4.658  17.999  1.00 29.51 ?  30  VAL   A HG12 1 
ATOM   825  H HG13 . VAL   A 1 30  ? 19.439 -5.080  19.137  1.00 29.51 ?  30  VAL   A HG13 1 
ATOM   826  H HG21 . VAL   A 1 30  ? 17.109 -4.427  17.220  1.00 29.72 ?  30  VAL   A HG21 1 
ATOM   827  H HG22 . VAL   A 1 30  ? 16.949 -4.089  18.764  1.00 29.72 ?  30  VAL   A HG22 1 
ATOM   828  H HG23 . VAL   A 1 30  ? 16.818 -2.935  17.681  1.00 29.72 ?  30  VAL   A HG23 1 
ATOM   829  N N    . LYS   A 1 31  ? 21.205 -1.408  18.679  1.00 21.35 ?  31  LYS   A N    1 
ATOM   830  C CA   . LYS   A 1 31  ? 22.659 -1.304  18.632  1.00 22.04 ?  31  LYS   A CA   1 
ATOM   831  C C    . LYS   A 1 31  ? 23.266 -2.666  18.288  1.00 19.63 ?  31  LYS   A C    1 
ATOM   832  O O    . LYS   A 1 31  ? 24.039 -3.228  19.072  1.00 20.57 ?  31  LYS   A O    1 
ATOM   833  C CB   . LYS   A 1 31  ? 23.236 -0.755  19.929  1.00 26.90 ?  31  LYS   A CB   1 
ATOM   834  C CG   . LYS   A 1 31  ? 22.555 0.515   20.417  1.00 32.33 ?  31  LYS   A CG   1 
ATOM   835  C CD   . LYS   A 1 31  ? 23.568 1.561   20.859  1.00 36.73 ?  31  LYS   A CD   1 
ATOM   836  C CE   . LYS   A 1 31  ? 22.932 2.616   21.753  1.00 39.67 ?  31  LYS   A CE   1 
ATOM   837  N NZ   . LYS   A 1 31  ? 21.754 3.280   21.127  1.00 41.15 ?  31  LYS   A NZ   1 
ATOM   838  H H    . LYS   A 1 31  ? 20.803 -0.812  18.211  1.00 25.64 ?  31  LYS   A H    1 
ATOM   839  H HA   . LYS   A 1 31  ? 22.890 -0.687  17.927  1.00 26.47 ?  31  LYS   A HA   1 
ATOM   840  H HB2  . LYS   A 1 31  ? 23.136 -1.428  20.612  1.00 32.29 ?  31  LYS   A HB2  1 
ATOM   841  H HB3  . LYS   A 1 31  ? 24.178 -0.558  19.792  1.00 32.29 ?  31  LYS   A HB3  1 
ATOM   842  H HG2  . LYS   A 1 31  ? 22.024 0.891   19.697  1.00 38.82 ?  31  LYS   A HG2  1 
ATOM   843  H HG3  . LYS   A 1 31  ? 21.988 0.302   21.175  1.00 38.82 ?  31  LYS   A HG3  1 
ATOM   844  H HD2  . LYS   A 1 31  ? 24.278 1.128   21.358  1.00 44.09 ?  31  LYS   A HD2  1 
ATOM   845  H HD3  . LYS   A 1 31  ? 23.931 2.005   20.075  1.00 44.09 ?  31  LYS   A HD3  1 
ATOM   846  H HE2  . LYS   A 1 31  ? 22.635 2.194   22.574  1.00 47.63 ?  31  LYS   A HE2  1 
ATOM   847  H HE3  . LYS   A 1 31  ? 23.591 3.300   21.952  1.00 47.63 ?  31  LYS   A HE3  1 
ATOM   848  H HZ1  . LYS   A 1 31  ? 21.424 3.896   21.679  1.00 49.40 ?  31  LYS   A HZ1  1 
ATOM   849  H HZ2  . LYS   A 1 31  ? 21.995 3.673   20.366  1.00 49.40 ?  31  LYS   A HZ2  1 
ATOM   850  H HZ3  . LYS   A 1 31  ? 21.121 2.678   20.956  1.00 49.40 ?  31  LYS   A HZ3  1 
ATOM   851  N N    . PRO   A 1 32  ? 22.932 -3.218  17.126  1.00 17.60 ?  32  PRO   A N    1 
ATOM   852  C CA   . PRO   A 1 32  ? 23.404 -4.557  16.779  1.00 17.55 ?  32  PRO   A CA   1 
ATOM   853  C C    . PRO   A 1 32  ? 24.905 -4.567  16.563  1.00 17.45 ?  32  PRO   A C    1 
ATOM   854  O O    . PRO   A 1 32  ? 25.547 -3.533  16.358  1.00 17.35 ?  32  PRO   A O    1 
ATOM   855  C CB   . PRO   A 1 32  ? 22.671 -4.851  15.467  1.00 17.88 ?  32  PRO   A CB   1 
ATOM   856  C CG   . PRO   A 1 32  ? 22.501 -3.499  14.848  1.00 16.70 ?  32  PRO   A CG   1 
ATOM   857  C CD   . PRO   A 1 32  ? 22.212 -2.588  16.007  1.00 16.70 ?  32  PRO   A CD   1 
ATOM   858  H HA   . PRO   A 1 32  ? 23.151 -5.203  17.458  1.00 21.08 ?  32  PRO   A HA   1 
ATOM   859  H HB2  . PRO   A 1 32  ? 23.215 -5.430  14.906  1.00 21.47 ?  32  PRO   A HB2  1 
ATOM   860  H HB3  . PRO   A 1 32  ? 21.810 -5.264  15.651  1.00 21.47 ?  32  PRO   A HB3  1 
ATOM   861  H HG2  . PRO   A 1 32  ? 23.319 -3.247  14.395  1.00 20.06 ?  32  PRO   A HG2  1 
ATOM   862  H HG3  . PRO   A 1 32  ? 21.755 -3.522  14.225  1.00 20.06 ?  32  PRO   A HG3  1 
ATOM   863  H HD2  . PRO   A 1 32  ? 22.569 -1.704  15.822  1.00 20.06 ?  32  PRO   A HD2  1 
ATOM   864  H HD3  . PRO   A 1 32  ? 21.262 -2.561  16.180  1.00 20.06 ?  32  PRO   A HD3  1 
ATOM   865  N N    . THR   A 1 33  ? 25.462 -5.776  16.593  1.00 17.37 ?  33  THR   A N    1 
ATOM   866  C CA   . THR   A 1 33  ? 26.876 -5.935  16.279  1.00 17.55 ?  33  THR   A CA   1 
ATOM   867  C C    . THR   A 1 33  ? 27.176 -5.470  14.859  1.00 15.87 ?  33  THR   A C    1 
ATOM   868  O O    . THR   A 1 33  ? 28.206 -4.825  14.612  1.00 16.32 ?  33  THR   A O    1 
ATOM   869  C CB   . THR   A 1 33  ? 27.283 -7.396  16.467  1.00 19.41 ?  33  THR   A CB   1 
ATOM   870  O OG1  . THR   A 1 33  ? 26.969 -7.808  17.801  1.00 20.81 ?  33  THR   A OG1  1 
ATOM   871  C CG2  . THR   A 1 33  ? 28.772 -7.573  16.221  1.00 20.33 ?  33  THR   A CG2  1 
ATOM   872  H H    . THR   A 1 33  ? 25.046 -6.506  16.786  1.00 20.86 ?  33  THR   A H    1 
ATOM   873  H HA   . THR   A 1 33  ? 27.398 -5.399  16.897  1.00 21.08 ?  33  THR   A HA   1 
ATOM   874  H HB   . THR   A 1 33  ? 26.797 -7.955  15.837  1.00 23.31 ?  33  THR   A HB   1 
ATOM   875  H HG1  . THR   A 1 33  ? 27.391 -7.341  18.358  1.00 24.99 ?  33  THR   A HG1  1 
ATOM   876  H HG21 . THR   A 1 33  ? 29.052 -8.456  16.506  1.00 24.42 ?  33  THR   A HG21 1 
ATOM   877  H HG22 . THR   A 1 33  ? 28.966 -7.471  15.277  1.00 24.42 ?  33  THR   A HG22 1 
ATOM   878  H HG23 . THR   A 1 33  ? 29.268 -6.908  16.721  1.00 24.42 ?  33  THR   A HG23 1 
ATOM   879  N N    . VAL   A 1 34  ? 26.289 -5.787  13.915  1.00 14.17 ?  34  VAL   A N    1 
ATOM   880  C CA   . VAL   A 1 34  ? 26.480 -5.451  12.507  1.00 12.89 ?  34  VAL   A CA   1 
ATOM   881  C C    . VAL   A 1 34  ? 25.179 -4.893  11.941  1.00 12.20 ?  34  VAL   A C    1 
ATOM   882  O O    . VAL   A 1 34  ? 24.139 -5.565  11.983  1.00 13.10 ?  34  VAL   A O    1 
ATOM   883  C CB   . VAL   A 1 34  ? 26.922 -6.665  11.671  1.00 13.65 ?  34  VAL   A CB   1 
ATOM   884  C CG1  . VAL   A 1 34  ? 27.110 -6.266  10.215  1.00 14.06 ?  34  VAL   A CG1  1 
ATOM   885  C CG2  . VAL   A 1 34  ? 28.197 -7.286  12.240  1.00 14.56 ?  34  VAL   A CG2  1 
ATOM   886  H H    . VAL   A 1 34  ? 25.555 -6.209  14.071  1.00 17.03 ?  34  VAL   A H    1 
ATOM   887  H HA   . VAL   A 1 34  ? 27.164 -4.763  12.431  1.00 15.49 ?  34  VAL   A HA   1 
ATOM   888  H HB   . VAL   A 1 34  ? 26.223 -7.337  11.710  1.00 16.40 ?  34  VAL   A HB   1 
ATOM   889  H HG11 . VAL   A 1 34  ? 27.596 -6.971  9.759   1.00 16.89 ?  34  VAL   A HG11 1 
ATOM   890  H HG12 . VAL   A 1 34  ? 26.243 -6.141  9.804   1.00 16.89 ?  34  VAL   A HG12 1 
ATOM   891  H HG13 . VAL   A 1 34  ? 27.620 -5.441  10.180  1.00 16.89 ?  34  VAL   A HG13 1 
ATOM   892  H HG21 . VAL   A 1 34  ? 28.472 -8.021  11.668  1.00 17.49 ?  34  VAL   A HG21 1 
ATOM   893  H HG22 . VAL   A 1 34  ? 28.893 -6.612  12.269  1.00 17.49 ?  34  VAL   A HG22 1 
ATOM   894  H HG23 . VAL   A 1 34  ? 28.019 -7.617  13.136  1.00 17.49 ?  34  VAL   A HG23 1 
ATOM   895  N N    . VAL   A 1 35  ? 25.239 -3.677  11.393  1.00 11.76 ?  35  VAL   A N    1 
ATOM   896  C CA   . VAL   A 1 35  ? 24.209 -3.163  10.499  1.00 11.45 ?  35  VAL   A CA   1 
ATOM   897  C C    . VAL   A 1 35  ? 24.764 -3.168  9.082   1.00 10.70 ?  35  VAL   A C    1 
ATOM   898  O O    . VAL   A 1 35  ? 25.909 -2.759  8.854   1.00 11.62 ?  35  VAL   A O    1 
ATOM   899  C CB   . VAL   A 1 35  ? 23.679 -1.770  10.904  1.00 12.03 ?  35  VAL   A CB   1 
ATOM   900  C CG1  . VAL   A 1 35  ? 24.755 -0.685  10.786  1.00 12.72 ?  35  VAL   A CG1  1 
ATOM   901  C CG2  . VAL   A 1 35  ? 22.448 -1.417  10.071  1.00 12.80 ?  35  VAL   A CG2  1 
ATOM   902  H H    . VAL   A 1 35  ? 25.879 -3.119  11.524  1.00 14.14 ?  35  VAL   A H    1 
ATOM   903  H HA   . VAL   A 1 35  ? 23.450 -3.773  10.518  1.00 13.76 ?  35  VAL   A HA   1 
ATOM   904  H HB   . VAL   A 1 35  ? 23.393 -1.802  11.828  1.00 14.45 ?  35  VAL   A HB   1 
ATOM   905  H HG11 . VAL   A 1 35  ? 24.408 0.146   11.151  1.00 15.28 ?  35  VAL   A HG11 1 
ATOM   906  H HG12 . VAL   A 1 35  ? 25.536 -0.964  11.287  1.00 15.28 ?  35  VAL   A HG12 1 
ATOM   907  H HG13 . VAL   A 1 35  ? 24.985 -0.562  9.852   1.00 15.28 ?  35  VAL   A HG13 1 
ATOM   908  H HG21 . VAL   A 1 35  ? 22.083 -0.576  10.380  1.00 15.38 ?  35  VAL   A HG21 1 
ATOM   909  H HG22 . VAL   A 1 35  ? 22.708 -1.341  9.136   1.00 15.38 ?  35  VAL   A HG22 1 
ATOM   910  H HG23 . VAL   A 1 35  ? 21.787 -2.122  10.169  1.00 15.38 ?  35  VAL   A HG23 1 
ATOM   911  N N    . VAL   A 1 36  ? 23.948 -3.626  8.130   1.00 10.28 ?  36  VAL   A N    1 
ATOM   912  C CA   . VAL   A 1 36  ? 24.324 -3.638  6.722   1.00 9.96  ?  36  VAL   A CA   1 
ATOM   913  C C    . VAL   A 1 36  ? 23.860 -2.351  6.056   1.00 10.21 ?  36  VAL   A C    1 
ATOM   914  O O    . VAL   A 1 36  ? 22.699 -1.945  6.193   1.00 10.98 ?  36  VAL   A O    1 
ATOM   915  C CB   . VAL   A 1 36  ? 23.725 -4.856  6.004   1.00 10.19 ?  36  VAL   A CB   1 
ATOM   916  C CG1  . VAL   A 1 36  ? 23.988 -4.779  4.519   1.00 10.96 ?  36  VAL   A CG1  1 
ATOM   917  C CG2  . VAL   A 1 36  ? 24.275 -6.145  6.588   1.00 11.30 ?  36  VAL   A CG2  1 
ATOM   918  H H    . VAL   A 1 36  ? 23.155 -3.943  8.277   1.00 12.36 ?  36  VAL   A H    1 
ATOM   919  H HA   . VAL   A 1 36  ? 25.291 -3.697  6.650   1.00 11.97 ?  36  VAL   A HA   1 
ATOM   920  H HB   . VAL   A 1 36  ? 22.763 -4.855  6.133   1.00 12.25 ?  36  VAL   A HB   1 
ATOM   921  H HG11 . VAL   A 1 36  ? 23.864 -5.657  4.128   1.00 13.17 ?  36  VAL   A HG11 1 
ATOM   922  H HG12 . VAL   A 1 36  ? 23.365 -4.151  4.114   1.00 13.17 ?  36  VAL   A HG12 1 
ATOM   923  H HG13 . VAL   A 1 36  ? 24.899 -4.479  4.374   1.00 13.17 ?  36  VAL   A HG13 1 
ATOM   924  H HG21 . VAL   A 1 36  ? 23.893 -6.899  6.109   1.00 13.58 ?  36  VAL   A HG21 1 
ATOM   925  H HG22 . VAL   A 1 36  ? 25.239 -6.148  6.493   1.00 13.58 ?  36  VAL   A HG22 1 
ATOM   926  H HG23 . VAL   A 1 36  ? 24.034 -6.197  7.526   1.00 13.58 ?  36  VAL   A HG23 1 
ATOM   927  N N    . ASN   A 1 37  ? 24.780 -1.717  5.319   1.00 9.64  ?  37  ASN   A N    1 
ATOM   928  C CA   . ASN   A 1 37  ? 24.453 -0.595  4.457   1.00 9.46  ?  37  ASN   A CA   1 
ATOM   929  C C    . ASN   A 1 37  ? 24.316 -1.061  3.018   1.00 9.35  ?  37  ASN   A C    1 
ATOM   930  O O    . ASN   A 1 37  ? 25.100 -1.893  2.542   1.00 10.19 ?  37  ASN   A O    1 
ATOM   931  C CB   . ASN   A 1 37  ? 25.533 0.481   4.539   1.00 9.68  ?  37  ASN   A CB   1 
ATOM   932  C CG   . ASN   A 1 37  ? 25.209 1.684   3.690   1.00 9.97  ?  37  ASN   A CG   1 
ATOM   933  O OD1  . ASN   A 1 37  ? 24.038 2.016   3.498   1.00 10.67 ?  37  ASN   A OD1  1 
ATOM   934  N ND2  . ASN   A 1 37  ? 26.242 2.338   3.172   1.00 10.50 ?  37  ASN   A ND2  1 
ATOM   935  H H    . ASN   A 1 37  ? 25.619 -1.921  5.314   1.00 11.59 ?  37  ASN   A H    1 
ATOM   936  H HA   . ASN   A 1 37  ? 23.616 -0.203  4.739   1.00 11.37 ?  37  ASN   A HA   1 
ATOM   937  H HB2  . ASN   A 1 37  ? 25.617 0.781   5.461   1.00 11.64 ?  37  ASN   A HB2  1 
ATOM   938  H HB3  . ASN   A 1 37  ? 26.380 0.112   4.236   1.00 11.64 ?  37  ASN   A HB3  1 
ATOM   939  H HD21 . ASN   A 1 37  ? 26.107 3.029   2.677   1.00 12.62 ?  37  ASN   A HD21 1 
ATOM   940  H HD22 . ASN   A 1 37  ? 27.041 2.081   3.329   1.00 12.62 ?  37  ASN   A HD22 1 
ATOM   941  N N    A ALA   A 1 38  ? 23.301 -0.516  2.339   0.72 10.00 ?  38  ALA   A N    1 
ATOM   942  N N    B ALA   A 1 38  ? 23.305 -0.531  2.326   0.28 9.79  ?  38  ALA   A N    1 
ATOM   943  C CA   A ALA   A 1 38  ? 23.111 -0.657  0.897   0.72 10.11 ?  38  ALA   A CA   1 
ATOM   944  C CA   B ALA   A 1 38  ? 23.138 -0.767  0.892   0.28 10.19 ?  38  ALA   A CA   1 
ATOM   945  C C    A ALA   A 1 38  ? 24.030 0.338   0.187   0.72 10.10 ?  38  ALA   A C    1 
ATOM   946  C C    B ALA   A 1 38  ? 23.987 0.255   0.138   0.28 10.18 ?  38  ALA   A C    1 
ATOM   947  O O    A ALA   A 1 38  ? 23.628 1.443   -0.191  0.72 9.92  ?  38  ALA   A O    1 
ATOM   948  O O    B ALA   A 1 38  ? 23.494 1.226   -0.445  0.28 9.76  ?  38  ALA   A O    1 
ATOM   949  C CB   A ALA   A 1 38  ? 21.649 -0.412  0.543   0.72 11.24 ?  38  ALA   A CB   1 
ATOM   950  C CB   B ALA   A 1 38  ? 21.668 -0.695  0.504   0.28 10.89 ?  38  ALA   A CB   1 
ATOM   951  H H    A ALA   A 1 38  ? 22.700 -0.027  2.711   0.72 12.02 ?  38  ALA   A H    1 
ATOM   952  H H    B ALA   A 1 38  ? 22.698 -0.028  2.673   0.28 11.77 ?  38  ALA   A H    1 
ATOM   953  H HA   A ALA   A 1 38  ? 23.353 -1.554  0.622   0.72 12.15 ?  38  ALA   A HA   1 
ATOM   954  H HA   B ALA   A 1 38  ? 23.469 -1.655  0.676   0.28 12.25 ?  38  ALA   A HA   1 
ATOM   955  H HB1  A ALA   A 1 38  ? 21.533 -0.512  -0.414  0.72 13.51 ?  38  ALA   A HB1  1 
ATOM   956  H HB1  B ALA   A 1 38  ? 21.590 -0.853  -0.449  0.28 13.09 ?  38  ALA   A HB1  1 
ATOM   957  H HB2  A ALA   A 1 38  ? 21.098 -1.060  1.013   0.72 13.51 ?  38  ALA   A HB2  1 
ATOM   958  H HB2  B ALA   A 1 38  ? 21.176 -1.371  0.995   0.28 13.09 ?  38  ALA   A HB2  1 
ATOM   959  H HB3  A ALA   A 1 38  ? 21.403 0.487   0.815   0.72 13.51 ?  38  ALA   A HB3  1 
ATOM   960  H HB3  B ALA   A 1 38  ? 21.330 0.187   0.721   0.28 13.09 ?  38  ALA   A HB3  1 
ATOM   961  N N    A ALA   A 1 39  ? 25.284 -0.069  -0.002  0.72 9.80  ?  39  ALA   A N    1 
ATOM   962  N N    B ALA   A 1 39  ? 25.296 0.018   0.153   0.28 10.41 ?  39  ALA   A N    1 
ATOM   963  C CA   A ALA   A 1 39  ? 26.340 0.812   -0.472  0.72 9.70  ?  39  ALA   A CA   1 
ATOM   964  C CA   B ALA   A 1 39  ? 26.260 0.963   -0.381  0.28 10.82 ?  39  ALA   A CA   1 
ATOM   965  C C    A ALA   A 1 39  ? 26.472 0.776   -1.990  0.72 9.96  ?  39  ALA   A C    1 
ATOM   966  C C    B ALA   A 1 39  ? 26.421 0.793   -1.886  0.28 9.99  ?  39  ALA   A C    1 
ATOM   967  O O    A ALA   A 1 39  ? 25.967 -0.120  -2.671  0.72 10.34 ?  39  ALA   A O    1 
ATOM   968  O O    B ALA   A 1 39  ? 26.024 -0.216  -2.475  0.28 9.81  ?  39  ALA   A O    1 
ATOM   969  C CB   A ALA   A 1 39  ? 27.666 0.406   0.180   0.72 10.25 ?  39  ALA   A CB   1 
ATOM   970  C CB   B ALA   A 1 39  ? 27.620 0.753   0.283   0.28 11.94 ?  39  ALA   A CB   1 
ATOM   971  H H    A ALA   A 1 39  ? 25.548 -0.879  0.147   0.72 11.77 ?  39  ALA   A H    1 
ATOM   972  H H    B ALA   A 1 39  ? 25.650 -0.698  0.468   0.28 12.51 ?  39  ALA   A H    1 
ATOM   973  H HA   A ALA   A 1 39  ? 26.129 1.721   -0.206  0.72 11.66 ?  39  ALA   A HA   1 
ATOM   974  H HA   B ALA   A 1 39  ? 25.964 1.867   -0.203  0.28 13.01 ?  39  ALA   A HA   1 
ATOM   975  H HB1  A ALA   A 1 39  ? 28.359 1.007   -0.136  0.72 12.32 ?  39  ALA   A HB1  1 
ATOM   976  H HB1  B ALA   A 1 39  ? 28.250 1.390   -0.086  0.28 14.34 ?  39  ALA   A HB1  1 
ATOM   977  H HB2  A ALA   A 1 39  ? 27.576 0.489   1.146   0.72 12.32 ?  39  ALA   A HB2  1 
ATOM   978  H HB2  B ALA   A 1 39  ? 27.526 0.890   1.237   0.28 14.34 ?  39  ALA   A HB2  1 
ATOM   979  H HB3  A ALA   A 1 39  ? 27.871 -0.503  -0.060  0.72 12.32 ?  39  ALA   A HB3  1 
ATOM   980  H HB3  B ALA   A 1 39  ? 27.920 -0.153  0.104   0.28 14.34 ?  39  ALA   A HB3  1 
ATOM   981  N N    A ASN   A 1 40  ? 27.178 1.776   -2.516  0.72 10.40 ?  40  ASN   A N    1 
ATOM   982  N N    B ASN   A 1 40  ? 27.025 1.807   -2.505  0.28 9.97  ?  40  ASN   A N    1 
ATOM   983  C CA   A ASN   A 1 40  ? 27.731 1.729   -3.863  0.72 10.56 ?  40  ASN   A CA   1 
ATOM   984  C CA   B ASN   A 1 40  ? 27.484 1.750   -3.885  0.28 10.19 ?  40  ASN   A CA   1 
ATOM   985  C C    A ASN   A 1 40  ? 29.254 1.625   -3.778  0.72 9.74  ?  40  ASN   A C    1 
ATOM   986  C C    B ASN   A 1 40  ? 29.005 1.612   -3.910  0.28 9.99  ?  40  ASN   A C    1 
ATOM   987  O O    A ASN   A 1 40  ? 29.844 1.726   -2.698  0.72 10.08 ?  40  ASN   A O    1 
ATOM   988  O O    B ASN   A 1 40  ? 29.672 1.678   -2.875  0.28 10.30 ?  40  ASN   A O    1 
ATOM   989  C CB   A ASN   A 1 40  ? 27.248 2.904   -4.732  0.72 11.14 ?  40  ASN   A CB   1 
ATOM   990  C CB   B ASN   A 1 40  ? 27.027 2.988   -4.667  0.28 10.93 ?  40  ASN   A CB   1 
ATOM   991  C CG   A ASN   A 1 40  ? 27.608 4.259   -4.164  0.72 12.07 ?  40  ASN   A CG   1 
ATOM   992  C CG   B ASN   A 1 40  ? 27.430 4.286   -3.997  0.28 12.06 ?  40  ASN   A CG   1 
ATOM   993  O OD1  A ASN   A 1 40  ? 28.770 4.518   -3.829  0.72 12.93 ?  40  ASN   A OD1  1 
ATOM   994  O OD1  B ASN   A 1 40  ? 28.618 4.567   -3.827  0.28 12.90 ?  40  ASN   A OD1  1 
ATOM   995  N ND2  A ASN   A 1 40  ? 26.604 5.144   -4.061  0.72 12.26 ?  40  ASN   A ND2  1 
ATOM   996  N ND2  B ASN   A 1 40  ? 26.439 5.094   -3.626  0.28 12.22 ?  40  ASN   A ND2  1 
ATOM   997  H H    A ASN   A 1 40  ? 27.360 2.498   -2.094  0.72 12.50 ?  40  ASN   A H    1 
ATOM   998  H H    B ASN   A 1 40  ? 27.184 2.564   -2.125  0.28 11.99 ?  40  ASN   A H    1 
ATOM   999  H HA   A ASN   A 1 40  ? 27.425 0.913   -4.285  0.72 12.70 ?  40  ASN   A HA   1 
ATOM   1000 H HA   B ASN   A 1 40  ? 27.102 0.967   -4.314  0.28 12.24 ?  40  ASN   A HA   1 
ATOM   1001 H HB2  A ASN   A 1 40  ? 27.654 2.826   -5.610  0.72 13.39 ?  40  ASN   A HB2  1 
ATOM   1002 H HB2  B ASN   A 1 40  ? 27.424 2.969   -5.551  0.28 13.14 ?  40  ASN   A HB2  1 
ATOM   1003 H HB3  A ASN   A 1 40  ? 26.283 2.852   -4.809  0.72 13.39 ?  40  ASN   A HB3  1 
ATOM   1004 H HB3  B ASN   A 1 40  ? 26.060 2.969   -4.740  0.28 13.14 ?  40  ASN   A HB3  1 
ATOM   1005 H HD21 A ASN   A 1 40  ? 26.749 5.932   -3.748  0.72 14.73 ?  40  ASN   A HD21 1 
ATOM   1006 H HD21 B ASN   A 1 40  ? 26.613 5.845   -3.245  0.28 14.68 ?  40  ASN   A HD21 1 
ATOM   1007 H HD22 A ASN   A 1 40  ? 25.806 4.923   -4.304  0.72 14.73 ?  40  ASN   A HD22 1 
ATOM   1008 H HD22 B ASN   A 1 40  ? 25.620 4.864   -3.766  0.28 14.68 ?  40  ASN   A HD22 1 
ATOM   1009 N N    A VAL   A 1 41  ? 29.885 1.371   -4.929  0.72 10.07 ?  41  VAL   A N    1 
ATOM   1010 N N    B VAL   A 1 41  ? 29.559 1.412   -5.112  0.28 10.01 ?  41  VAL   A N    1 
ATOM   1011 C CA   A VAL   A 1 41  ? 31.313 1.060   -4.944  0.72 10.44 ?  41  VAL   A CA   1 
ATOM   1012 C CA   B VAL   A 1 41  ? 30.986 1.097   -5.221  0.28 10.23 ?  41  VAL   A CA   1 
ATOM   1013 C C    A VAL   A 1 41  ? 32.165 2.215   -4.456  0.72 10.57 ?  41  VAL   A C    1 
ATOM   1014 C C    B VAL   A 1 41  ? 31.863 2.238   -4.725  0.28 10.27 ?  41  VAL   A C    1 
ATOM   1015 O O    A VAL   A 1 41  ? 33.301 1.995   -4.021  0.72 11.01 ?  41  VAL   A O    1 
ATOM   1016 O O    B VAL   A 1 41  ? 33.020 2.016   -4.343  0.28 9.93  ?  41  VAL   A O    1 
ATOM   1017 C CB   A VAL   A 1 41  ? 31.801 0.567   -6.329  0.72 10.51 ?  41  VAL   A CB   1 
ATOM   1018 C CB   B VAL   A 1 41  ? 31.381 0.683   -6.653  0.28 10.55 ?  41  VAL   A CB   1 
ATOM   1019 C CG1  A VAL   A 1 41  ? 31.115 -0.739  -6.721  0.72 11.58 ?  41  VAL   A CG1  1 
ATOM   1020 C CG1  B VAL   A 1 41  ? 30.728 -0.637  -7.030  0.28 11.09 ?  41  VAL   A CG1  1 
ATOM   1021 C CG2  A VAL   A 1 41  ? 31.641 1.634   -7.411  0.72 10.49 ?  41  VAL   A CG2  1 
ATOM   1022 C CG2  B VAL   A 1 41  ? 31.040 1.784   -7.653  0.28 10.87 ?  41  VAL   A CG2  1 
ATOM   1023 H H    A VAL   A 1 41  ? 29.514 1.364   -5.700  0.72 12.11 ?  41  VAL   A H    1 
ATOM   1024 H H    B VAL   A 1 41  ? 29.133 1.444   -5.860  0.28 12.03 ?  41  VAL   A H    1 
ATOM   1025 H HA   A VAL   A 1 41  ? 31.470 0.332   -4.326  0.72 12.55 ?  41  VAL   A HA   1 
ATOM   1026 H HA   B VAL   A 1 41  ? 31.158 0.332   -4.651  0.28 12.29 ?  41  VAL   A HA   1 
ATOM   1027 H HB   A VAL   A 1 41  ? 32.750 0.373   -6.264  0.72 12.63 ?  41  VAL   A HB   1 
ATOM   1028 H HB   B VAL   A 1 41  ? 32.342 0.552   -6.678  0.28 12.68 ?  41  VAL   A HB   1 
ATOM   1029 H HG11 A VAL   A 1 41  ? 31.453 -1.034  -7.582  0.72 13.91 ?  41  VAL   A HG11 1 
ATOM   1030 H HG11 B VAL   A 1 41  ? 30.943 -0.843  -7.952  0.28 13.32 ?  41  VAL   A HG11 1 
ATOM   1031 H HG12 A VAL   A 1 41  ? 31.300 -1.412  -6.046  0.72 13.91 ?  41  VAL   A HG12 1 
ATOM   1032 H HG12 B VAL   A 1 41  ? 31.072 -1.335  -6.447  0.28 13.32 ?  41  VAL   A HG12 1 
ATOM   1033 H HG13 A VAL   A 1 41  ? 30.156 -0.589  -6.780  0.72 13.91 ?  41  VAL   A HG13 1 
ATOM   1034 H HG13 B VAL   A 1 41  ? 29.770 -0.562  -6.921  0.28 13.32 ?  41  VAL   A HG13 1 
ATOM   1035 H HG21 A VAL   A 1 41  ? 31.891 1.250   -8.270  0.72 12.61 ?  41  VAL   A HG21 1 
ATOM   1036 H HG21 B VAL   A 1 41  ? 31.326 1.504   -8.537  0.28 13.06 ?  41  VAL   A HG21 1 
ATOM   1037 H HG22 A VAL   A 1 41  ? 30.722 1.927   -7.434  0.72 12.61 ?  41  VAL   A HG22 1 
ATOM   1038 H HG22 B VAL   A 1 41  ? 30.082 1.933   -7.650  0.28 13.06 ?  41  VAL   A HG22 1 
ATOM   1039 H HG23 A VAL   A 1 41  ? 32.227 2.380   -7.206  0.72 12.61 ?  41  VAL   A HG23 1 
ATOM   1040 H HG23 B VAL   A 1 41  ? 31.503 2.598   -7.400  0.28 13.06 ?  41  VAL   A HG23 1 
ATOM   1041 N N    A TYR   A 1 42  ? 31.656 3.447   -4.538  0.72 10.44 ?  42  TYR   A N    1 
ATOM   1042 N N    B TYR   A 1 42  ? 31.358 3.469   -4.754  0.28 10.40 ?  42  TYR   A N    1 
ATOM   1043 C CA   A TYR   A 1 42  ? 32.389 4.634   -4.115  0.72 10.64 ?  42  TYR   A CA   1 
ATOM   1044 C CA   B TYR   A 1 42  ? 32.134 4.630   -4.338  0.28 10.73 ?  42  TYR   A CA   1 
ATOM   1045 C C    A TYR   A 1 42  ? 32.117 5.004   -2.666  0.72 10.49 ?  42  TYR   A C    1 
ATOM   1046 C C    B TYR   A 1 42  ? 31.909 5.011   -2.884  0.28 10.50 ?  42  TYR   A C    1 
ATOM   1047 O O    A TYR   A 1 42  ? 32.680 5.992   -2.171  0.72 11.24 ?  42  TYR   A O    1 
ATOM   1048 O O    B TYR   A 1 42  ? 32.480 6.008   -2.428  0.28 10.76 ?  42  TYR   A O    1 
ATOM   1049 C CB   A TYR   A 1 42  ? 32.052 5.821   -5.038  0.72 11.34 ?  42  TYR   A CB   1 
ATOM   1050 C CB   B TYR   A 1 42  ? 31.803 5.833   -5.225  0.28 11.18 ?  42  TYR   A CB   1 
ATOM   1051 C CG   A TYR   A 1 42  ? 32.247 5.500   -6.507  0.72 12.19 ?  42  TYR   A CG   1 
ATOM   1052 C CG   B TYR   A 1 42  ? 31.965 5.558   -6.698  0.28 11.84 ?  42  TYR   A CG   1 
ATOM   1053 C CD1  A TYR   A 1 42  ? 33.515 5.301   -7.030  0.72 13.06 ?  42  TYR   A CD1  1 
ATOM   1054 C CD1  B TYR   A 1 42  ? 33.220 5.352   -7.250  0.28 11.85 ?  42  TYR   A CD1  1 
ATOM   1055 C CD2  A TYR   A 1 42  ? 31.162 5.360   -7.363  0.72 13.41 ?  42  TYR   A CD2  1 
ATOM   1056 C CD2  B TYR   A 1 42  ? 30.861 5.501   -7.535  0.28 12.70 ?  42  TYR   A CD2  1 
ATOM   1057 C CE1  A TYR   A 1 42  ? 33.701 4.986   -8.369  0.72 13.45 ?  42  TYR   A CE1  1 
ATOM   1058 C CE1  B TYR   A 1 42  ? 33.371 5.095   -8.597  0.28 12.19 ?  42  TYR   A CE1  1 
ATOM   1059 C CE2  A TYR   A 1 42  ? 31.339 5.048   -8.702  0.72 14.31 ?  42  TYR   A CE2  1 
ATOM   1060 C CE2  B TYR   A 1 42  ? 31.001 5.249   -8.881  0.28 13.17 ?  42  TYR   A CE2  1 
ATOM   1061 C CZ   A TYR   A 1 42  ? 32.613 4.863   -9.199  0.72 14.28 ?  42  TYR   A CZ   1 
ATOM   1062 C CZ   B TYR   A 1 42  ? 32.257 5.045   -9.410  0.28 12.86 ?  42  TYR   A CZ   1 
ATOM   1063 O OH   A TYR   A 1 42  ? 32.793 4.546   -10.525 0.72 15.60 ?  42  TYR   A OH   1 
ATOM   1064 O OH   B TYR   A 1 42  ? 32.398 4.794   -10.754 0.28 13.44 ?  42  TYR   A OH   1 
ATOM   1065 H H    A TYR   A 1 42  ? 30.872 3.622   -4.843  0.72 12.55 ?  42  TYR   A H    1 
ATOM   1066 H H    B TYR   A 1 42  ? 30.562 3.658   -5.022  0.28 12.50 ?  42  TYR   A H    1 
ATOM   1067 H HA   A TYR   A 1 42  ? 33.341 4.466   -4.203  0.72 12.79 ?  42  TYR   A HA   1 
ATOM   1068 H HA   B TYR   A 1 42  ? 33.074 4.432   -4.447  0.28 12.89 ?  42  TYR   A HA   1 
ATOM   1069 H HB2  A TYR   A 1 42  ? 31.124 6.074   -4.908  0.72 13.63 ?  42  TYR   A HB2  1 
ATOM   1070 H HB2  B TYR   A 1 42  ? 30.881 6.094   -5.067  0.28 13.43 ?  42  TYR   A HB2  1 
ATOM   1071 H HB3  A TYR   A 1 42  ? 32.630 6.573   -4.820  0.72 13.63 ?  42  TYR   A HB3  1 
ATOM   1072 H HB3  B TYR   A 1 42  ? 32.395 6.565   -4.990  0.28 13.43 ?  42  TYR   A HB3  1 
ATOM   1073 H HD1  A TYR   A 1 42  ? 34.259 5.383   -6.476  0.72 15.69 ?  42  TYR   A HD1  1 
ATOM   1074 H HD1  B TYR   A 1 42  ? 33.971 5.384   -6.698  0.28 14.24 ?  42  TYR   A HD1  1 
ATOM   1075 H HD2  A TYR   A 1 42  ? 30.300 5.489   -7.034  0.72 16.11 ?  42  TYR   A HD2  1 
ATOM   1076 H HD2  B TYR   A 1 42  ? 30.012 5.638   -7.179  0.28 15.27 ?  42  TYR   A HD2  1 
ATOM   1077 H HE1  A TYR   A 1 42  ? 34.560 4.862   -8.707  0.72 16.16 ?  42  TYR   A HE1  1 
ATOM   1078 H HE1  B TYR   A 1 42  ? 34.219 4.959   -8.952  0.28 14.65 ?  42  TYR   A HE1  1 
ATOM   1079 H HE2  A TYR   A 1 42  ? 30.599 4.967   -9.267  0.72 17.19 ?  42  TYR   A HE2  1 
ATOM   1080 H HE2  B TYR   A 1 42  ? 30.252 5.215   -9.429  0.28 15.83 ?  42  TYR   A HE2  1 
ATOM   1081 H HH   A TYR   A 1 42  ? 33.611 4.453   -10.693 0.72 18.74 ?  42  TYR   A HH   1 
ATOM   1082 H HH   B TYR   A 1 42  ? 31.647 4.795   -11.122 0.28 16.15 ?  42  TYR   A HH   1 
ATOM   1083 N N    A LEU   A 1 43  ? 31.254 4.244   -1.991  0.72 10.54 ?  43  LEU   A N    1 
ATOM   1084 N N    B LEU   A 1 43  ? 31.090 4.250   -2.155  0.28 10.08 ?  43  LEU   A N    1 
ATOM   1085 C CA   A LEU   A 1 43  ? 30.792 4.580   -0.647  0.72 10.38 ?  43  LEU   A CA   1 
ATOM   1086 C CA   B LEU   A 1 43  ? 30.698 4.587   -0.785  0.28 10.38 ?  43  LEU   A CA   1 
ATOM   1087 C C    A LEU   A 1 43  ? 30.318 6.030   -0.561  0.72 10.64 ?  43  LEU   A C    1 
ATOM   1088 C C    B LEU   A 1 43  ? 30.212 6.031   -0.675  0.28 10.91 ?  43  LEU   A C    1 
ATOM   1089 O O    A LEU   A 1 43  ? 30.592 6.740   0.410   0.72 11.72 ?  43  LEU   A O    1 
ATOM   1090 O O    B LEU   A 1 43  ? 30.456 6.719   0.318   0.28 11.06 ?  43  LEU   A O    1 
ATOM   1091 C CB   A LEU   A 1 43  ? 31.832 4.270   0.426   0.72 10.78 ?  43  LEU   A CB   1 
ATOM   1092 C CB   B LEU   A 1 43  ? 31.804 4.291   0.229   0.28 10.40 ?  43  LEU   A CB   1 
ATOM   1093 C CG   A LEU   A 1 43  ? 32.347 2.827   0.496   0.72 11.14 ?  43  LEU   A CG   1 
ATOM   1094 C CG   B LEU   A 1 43  ? 32.218 2.825   0.395   0.28 10.51 ?  43  LEU   A CG   1 
ATOM   1095 C CD1  A LEU   A 1 43  ? 33.395 2.714   1.591   0.72 12.07 ?  43  LEU   A CD1  1 
ATOM   1096 C CD1  B LEU   A 1 43  ? 33.241 2.693   1.514   0.28 10.88 ?  43  LEU   A CD1  1 
ATOM   1097 C CD2  A LEU   A 1 43  ? 31.225 1.831   0.720   0.72 11.54 ?  43  LEU   A CD2  1 
ATOM   1098 C CD2  B LEU   A 1 43  ? 31.014 1.931   0.659   0.28 10.61 ?  43  LEU   A CD2  1 
ATOM   1099 H H    A LEU   A 1 43  ? 30.919 3.511   -2.297  0.72 12.67 ?  43  LEU   A H    1 
ATOM   1100 H H    B LEU   A 1 43  ? 30.738 3.518   -2.434  0.28 12.11 ?  43  LEU   A H    1 
ATOM   1101 H HA   A LEU   A 1 43  ? 30.022 4.023   -0.457  0.72 12.47 ?  43  LEU   A HA   1 
ATOM   1102 H HA   B LEU   A 1 43  ? 29.943 4.026   -0.548  0.28 12.48 ?  43  LEU   A HA   1 
ATOM   1103 H HB2  A LEU   A 1 43  ? 32.598 4.848   0.281   0.72 12.96 ?  43  LEU   A HB2  1 
ATOM   1104 H HB2  B LEU   A 1 43  ? 32.595 4.787   -0.028  0.28 12.51 ?  43  LEU   A HB2  1 
ATOM   1105 H HB3  A LEU   A 1 43  ? 31.437 4.475   1.290   0.72 12.96 ?  43  LEU   A HB3  1 
ATOM   1106 H HB3  B LEU   A 1 43  ? 31.502 4.599   1.101   0.28 12.51 ?  43  LEU   A HB3  1 
ATOM   1107 H HG   A LEU   A 1 43  ? 32.780 2.610   -0.345  0.72 13.39 ?  43  LEU   A HG   1 
ATOM   1108 H HG   B LEU   A 1 43  ? 32.639 2.526   -0.425  0.28 12.63 ?  43  LEU   A HG   1 
ATOM   1109 H HD11 A LEU   A 1 43  ? 33.717 1.802   1.628   0.72 14.50 ?  43  LEU   A HD11 1 
ATOM   1110 H HD11 B LEU   A 1 43  ? 33.495 1.761   1.600   0.28 13.07 ?  43  LEU   A HD11 1 
ATOM   1111 H HD12 A LEU   A 1 43  ? 34.129 3.318   1.391   0.72 14.50 ?  43  LEU   A HD12 1 
ATOM   1112 H HD12 B LEU   A 1 43  ? 34.019 3.230   1.297   0.28 13.07 ?  43  LEU   A HD12 1 
ATOM   1113 H HD13 A LEU   A 1 43  ? 32.990 2.958   2.440   0.72 14.50 ?  43  LEU   A HD13 1 
ATOM   1114 H HD13 B LEU   A 1 43  ? 32.844 3.005   2.343   0.28 13.07 ?  43  LEU   A HD13 1 
ATOM   1115 H HD21 A LEU   A 1 43  ? 31.609 0.946   0.836   0.72 13.87 ?  43  LEU   A HD21 1 
ATOM   1116 H HD21 B LEU   A 1 43  ? 31.327 1.056   0.938   0.28 12.76 ?  43  LEU   A HD21 1 
ATOM   1117 H HD22 A LEU   A 1 43  ? 30.732 2.084   1.514   0.72 13.87 ?  43  LEU   A HD22 1 
ATOM   1118 H HD22 B LEU   A 1 43  ? 30.472 2.329   1.357   0.28 12.76 ?  43  LEU   A HD22 1 
ATOM   1119 H HD23 A LEU   A 1 43  ? 30.640 1.837   -0.053  0.72 13.87 ?  43  LEU   A HD23 1 
ATOM   1120 H HD23 B LEU   A 1 43  ? 30.498 1.852   -0.158  0.28 12.76 ?  43  LEU   A HD23 1 
ATOM   1121 N N    A LYS   A 1 44  ? 29.579 6.468   -1.586  0.72 10.52 ?  44  LYS   A N    1 
ATOM   1122 N N    B LYS   A 1 44  ? 29.500 6.489   -1.702  0.28 11.29 ?  44  LYS   A N    1 
ATOM   1123 C CA   A LYS   A 1 44  ? 28.938 7.782   -1.597  0.72 10.85 ?  44  LYS   A CA   1 
ATOM   1124 C CA   B LYS   A 1 44  ? 28.854 7.800   -1.684  0.28 11.82 ?  44  LYS   A CA   1 
ATOM   1125 C C    A LYS   A 1 44  ? 27.504 7.585   -1.117  0.72 10.38 ?  44  LYS   A C    1 
ATOM   1126 C C    B LYS   A 1 44  ? 27.447 7.615   -1.139  0.28 10.89 ?  44  LYS   A C    1 
ATOM   1127 O O    A LYS   A 1 44  ? 26.654 7.052   -1.837  0.72 11.44 ?  44  LYS   A O    1 
ATOM   1128 O O    B LYS   A 1 44  ? 26.549 7.145   -1.843  0.28 11.18 ?  44  LYS   A O    1 
ATOM   1129 C CB   A LYS   A 1 44  ? 28.996 8.415   -2.981  0.72 12.89 ?  44  LYS   A CB   1 
ATOM   1130 C CB   B LYS   A 1 44  ? 28.848 8.410   -3.082  0.28 14.00 ?  44  LYS   A CB   1 
ATOM   1131 C CG   A LYS   A 1 44  ? 30.389 8.868   -3.398  0.72 16.26 ?  44  LYS   A CG   1 
ATOM   1132 C CG   B LYS   A 1 44  ? 30.189 8.986   -3.505  0.28 16.53 ?  44  LYS   A CG   1 
ATOM   1133 C CD   A LYS   A 1 44  ? 31.036 9.813   -2.388  0.72 21.18 ?  44  LYS   A CD   1 
ATOM   1134 C CD   B LYS   A 1 44  ? 30.818 9.804   -2.384  0.28 19.31 ?  44  LYS   A CD   1 
ATOM   1135 C CE   A LYS   A 1 44  ? 32.363 10.345  -2.903  0.72 24.21 ?  44  LYS   A CE   1 
ATOM   1136 C CE   B LYS   A 1 44  ? 32.115 10.435  -2.821  0.28 21.09 ?  44  LYS   A CE   1 
ATOM   1137 N NZ   A LYS   A 1 44  ? 33.188 10.940  -1.817  0.72 25.83 ?  44  LYS   A NZ   1 
ATOM   1138 N NZ   B LYS   A 1 44  ? 32.849 11.027  -1.674  0.28 22.16 ?  44  LYS   A NZ   1 
ATOM   1139 H H    A LYS   A 1 44  ? 29.432 6.007   -2.301  0.72 12.65 ?  44  LYS   A H    1 
ATOM   1140 H H    B LYS   A 1 44  ? 29.376 6.054   -2.433  0.28 13.57 ?  44  LYS   A H    1 
ATOM   1141 H HA   A LYS   A 1 44  ? 29.383 8.360   -0.961  0.72 13.04 ?  44  LYS   A HA   1 
ATOM   1142 H HA   B LYS   A 1 44  ? 29.311 8.382   -1.059  0.28 14.20 ?  44  LYS   A HA   1 
ATOM   1143 H HB2  A LYS   A 1 44  ? 28.687 7.773   -3.634  0.72 15.49 ?  44  LYS   A HB2  1 
ATOM   1144 H HB2  B LYS   A 1 44  ? 28.609 7.720   -3.725  0.28 16.82 ?  44  LYS   A HB2  1 
ATOM   1145 H HB3  A LYS   A 1 44  ? 28.422 9.198   -2.988  0.72 15.49 ?  44  LYS   A HB3  1 
ATOM   1146 H HB3  B LYS   A 1 44  ? 28.196 9.126   -3.113  0.28 16.82 ?  44  LYS   A HB3  1 
ATOM   1147 H HG2  A LYS   A 1 44  ? 30.963 8.088   -3.488  0.72 19.54 ?  44  LYS   A HG2  1 
ATOM   1148 H HG2  B LYS   A 1 44  ? 30.793 8.261   -3.732  0.28 19.86 ?  44  LYS   A HG2  1 
ATOM   1149 H HG3  A LYS   A 1 44  ? 30.332 9.333   -4.248  0.72 19.54 ?  44  LYS   A HG3  1 
ATOM   1150 H HG3  B LYS   A 1 44  ? 30.061 9.569   -4.272  0.28 19.86 ?  44  LYS   A HG3  1 
ATOM   1151 H HD2  A LYS   A 1 44  ? 30.439 10.561  -2.226  0.72 25.44 ?  44  LYS   A HD2  1 
ATOM   1152 H HD2  B LYS   A 1 44  ? 30.194 10.497  -2.103  0.28 23.19 ?  44  LYS   A HD2  1 
ATOM   1153 H HD3  A LYS   A 1 44  ? 31.205 9.331   -1.562  0.72 25.44 ?  44  LYS   A HD3  1 
ATOM   1154 H HD3  B LYS   A 1 44  ? 31.032 9.221   -1.637  0.28 23.19 ?  44  LYS   A HD3  1 
ATOM   1155 H HE2  A LYS   A 1 44  ? 32.866 9.615   -3.298  0.72 29.08 ?  44  LYS   A HE2  1 
ATOM   1156 H HE2  B LYS   A 1 44  ? 32.676 9.751   -3.222  0.28 25.33 ?  44  LYS   A HE2  1 
ATOM   1157 H HE3  A LYS   A 1 44  ? 32.193 11.031  -3.567  0.72 29.08 ?  44  LYS   A HE3  1 
ATOM   1158 H HE3  B LYS   A 1 44  ? 31.926 11.135  -3.459  0.28 25.33 ?  44  LYS   A HE3  1 
ATOM   1159 H HZ1  A LYS   A 1 44  ? 33.955 11.243  -2.149  0.72 31.01 ?  44  LYS   A HZ1  1 
ATOM   1160 H HZ1  B LYS   A 1 44  ? 33.610 11.389  -1.958  0.28 26.62 ?  44  LYS   A HZ1  1 
ATOM   1161 H HZ2  A LYS   A 1 44  ? 32.748 11.620  -1.441  0.72 31.01 ?  44  LYS   A HZ2  1 
ATOM   1162 H HZ2  B LYS   A 1 44  ? 32.353 11.656  -1.288  0.28 26.62 ?  44  LYS   A HZ2  1 
ATOM   1163 H HZ3  A LYS   A 1 44  ? 33.360 10.330  -1.195  0.72 31.01 ?  44  LYS   A HZ3  1 
ATOM   1164 H HZ3  B LYS   A 1 44  ? 33.036 10.396  -1.073  0.28 26.62 ?  44  LYS   A HZ3  1 
ATOM   1165 N N    . HIS   A 1 45  ? 27.253 7.980   0.127   1.00 10.36 ?  45  HIS   A N    1 
ATOM   1166 C CA   . HIS   A 1 45  ? 26.016 7.640   0.825   1.00 10.47 ?  45  HIS   A CA   1 
ATOM   1167 C C    . HIS   A 1 45  ? 25.000 8.766   0.653   1.00 11.24 ?  45  HIS   A C    1 
ATOM   1168 O O    . HIS   A 1 45  ? 24.705 9.528   1.573   1.00 12.96 ?  45  HIS   A O    1 
ATOM   1169 C CB   . HIS   A 1 45  ? 26.313 7.393   2.291   1.00 10.40 ?  45  HIS   A CB   1 
ATOM   1170 C CG   . HIS   A 1 45  ? 27.423 6.425   2.524   1.00 10.09 ?  45  HIS   A CG   1 
ATOM   1171 N ND1  . HIS   A 1 45  ? 27.414 5.135   2.031   1.00 10.41 ?  45  HIS   A ND1  1 
ATOM   1172 C CD2  . HIS   A 1 45  ? 28.593 6.579   3.192   1.00 10.26 ?  45  HIS   A CD2  1 
ATOM   1173 C CE1  . HIS   A 1 45  ? 28.534 4.538   2.401   1.00 10.07 ?  45  HIS   A CE1  1 
ATOM   1174 N NE2  . HIS   A 1 45  ? 29.266 5.389   3.104   1.00 10.33 ?  45  HIS   A NE2  1 
ATOM   1175 H H    A HIS   A 1 45  ? 27.795 8.456   0.598   0.72 12.45 ?  45  HIS   A H    1 
ATOM   1176 H H    B HIS   A 1 45  ? 27.820 8.417   0.606   0.28 12.45 ?  45  HIS   A H    1 
ATOM   1177 H HA   . HIS   A 1 45  ? 25.639 6.828   0.444   1.00 12.59 ?  45  HIS   A HA   1 
ATOM   1178 H HB2  . HIS   A 1 45  ? 26.549 8.237   2.707   1.00 12.50 ?  45  HIS   A HB2  1 
ATOM   1179 H HB3  . HIS   A 1 45  ? 25.508 7.038   2.715   1.00 12.50 ?  45  HIS   A HB3  1 
ATOM   1180 H HD2  . HIS   A 1 45  ? 28.887 7.349   3.627   1.00 12.33 ?  45  HIS   A HD2  1 
ATOM   1181 H HE1  . HIS   A 1 45  ? 28.765 3.659   2.211   1.00 12.10 ?  45  HIS   A HE1  1 
ATOM   1182 H HE2  . HIS   A 1 45  ? 30.037 5.223   3.449   1.00 12.42 ?  45  HIS   A HE2  1 
ATOM   1183 N N    A GLY   A 1 46  ? 24.396 8.811   -0.529  0.72 12.13 ?  46  GLY   A N    1 
ATOM   1184 N N    B GLY   A 1 46  ? 24.509 8.902   -0.574  0.28 11.49 ?  46  GLY   A N    1 
ATOM   1185 C CA   A GLY   A 1 46  ? 23.539 9.932   -0.867  0.72 12.59 ?  46  GLY   A CA   1 
ATOM   1186 C CA   B GLY   A 1 46  ? 23.763 10.093  -0.939  0.28 11.62 ?  46  GLY   A CA   1 
ATOM   1187 C C    A GLY   A 1 46  ? 22.061 9.764   -0.573  0.72 12.57 ?  46  GLY   A C    1 
ATOM   1188 C C    B GLY   A 1 46  ? 22.281 10.022  -0.639  0.28 11.34 ?  46  GLY   A C    1 
ATOM   1189 O O    A GLY   A 1 46  ? 21.394 10.726  -0.169  0.72 13.34 ?  46  GLY   A O    1 
ATOM   1190 O O    B GLY   A 1 46  ? 21.640 11.047  -0.382  0.28 11.69 ?  46  GLY   A O    1 
ATOM   1191 H H    A GLY   A 1 46  ? 24.456 8.213   -1.142  0.72 14.57 ?  46  GLY   A H    1 
ATOM   1192 H H    B GLY   A 1 46  ? 24.587 8.324   -1.205  0.28 13.81 ?  46  GLY   A H    1 
ATOM   1193 H HA2  A GLY   A 1 46  ? 23.836 10.717  -0.376  0.72 15.13 ?  46  GLY   A HA2  1 
ATOM   1194 H HA2  B GLY   A 1 46  ? 24.135 10.857  -0.463  0.28 13.97 ?  46  GLY   A HA2  1 
ATOM   1195 H HA3  A GLY   A 1 46  ? 23.632 10.125  -1.812  0.72 15.13 ?  46  GLY   A HA3  1 
ATOM   1196 H HA3  B GLY   A 1 46  ? 23.863 10.254  -1.888  0.28 13.97 ?  46  GLY   A HA3  1 
ATOM   1197 N N    A GLY   A 1 47  ? 21.528 8.564   -0.793  0.72 12.63 ?  47  GLY   A N    1 
ATOM   1198 N N    B GLY   A 1 47  ? 21.720 8.823   -0.695  0.28 10.77 ?  47  GLY   A N    1 
ATOM   1199 C CA   A GLY   A 1 47  ? 20.097 8.351   -0.740  0.72 12.59 ?  47  GLY   A CA   1 
ATOM   1200 C CA   B GLY   A 1 47  ? 20.306 8.635   -0.473  0.28 11.15 ?  47  GLY   A CA   1 
ATOM   1201 C C    A GLY   A 1 47  ? 19.766 6.934   -0.326  0.72 12.03 ?  47  GLY   A C    1 
ATOM   1202 C C    B GLY   A 1 47  ? 20.001 7.177   -0.203  0.28 10.99 ?  47  GLY   A C    1 
ATOM   1203 O O    A GLY   A 1 47  ? 20.651 6.112   -0.086  0.72 11.86 ?  47  GLY   A O    1 
ATOM   1204 O O    B GLY   A 1 47  ? 20.903 6.354   -0.031  0.28 11.34 ?  47  GLY   A O    1 
ATOM   1205 H H    A GLY   A 1 47  ? 21.985 7.849   -0.960  0.72 15.17 ?  47  GLY   A H    1 
ATOM   1206 H H    B GLY   A 1 47  ? 22.148 8.101   -0.862  0.28 12.94 ?  47  GLY   A H    1 
ATOM   1207 H HA2  A GLY   A 1 47  ? 19.695 8.958   -0.103  0.72 15.13 ?  47  GLY   A HA2  1 
ATOM   1208 H HA2  B GLY   A 1 47  ? 20.014 9.166   0.286   0.28 13.40 ?  47  GLY   A HA2  1 
ATOM   1209 H HA3  A GLY   A 1 47  ? 19.710 8.509   -1.614  0.72 15.13 ?  47  GLY   A HA3  1 
ATOM   1210 H HA3  B GLY   A 1 47  ? 19.815 8.923   -1.260  0.28 13.40 ?  47  GLY   A HA3  1 
ATOM   1211 N N    A GLY   A 1 48  ? 18.470 6.643   -0.260  0.72 12.54 ?  48  GLY   A N    1 
ATOM   1212 N N    B GLY   A 1 48  ? 18.709 6.865   -0.164  0.28 11.34 ?  48  GLY   A N    1 
ATOM   1213 C CA   A GLY   A 1 48  ? 18.038 5.345   0.204   0.72 12.25 ?  48  GLY   A CA   1 
ATOM   1214 C CA   B GLY   A 1 48  ? 18.295 5.500   0.102   0.28 11.32 ?  48  GLY   A CA   1 
ATOM   1215 C C    A GLY   A 1 48  ? 18.556 5.069   1.601   0.72 11.82 ?  48  GLY   A C    1 
ATOM   1216 C C    B GLY   A 1 48  ? 18.661 5.068   1.513   0.28 10.84 ?  48  GLY   A C    1 
ATOM   1217 O O    A GLY   A 1 48  ? 18.750 5.984   2.417   0.72 12.68 ?  48  GLY   A O    1 
ATOM   1218 O O    B GLY   A 1 48  ? 18.700 5.872   2.452   0.28 11.44 ?  48  GLY   A O    1 
ATOM   1219 H H    A GLY   A 1 48  ? 17.830 7.179   -0.469  0.72 15.07 ?  48  GLY   A H    1 
ATOM   1220 H H    B GLY   A 1 48  ? 18.068 7.420   -0.285  0.28 13.63 ?  48  GLY   A H    1 
ATOM   1221 H HA2  A GLY   A 1 48  ? 17.069 5.299   0.217   0.72 14.72 ?  48  GLY   A HA2  1 
ATOM   1222 H HA2  B GLY   A 1 48  ? 17.338 5.426   -0.009  0.28 13.61 ?  48  GLY   A HA2  1 
ATOM   1223 H HA3  A GLY   A 1 48  ? 18.374 4.654   -0.388  0.72 14.72 ?  48  GLY   A HA3  1 
ATOM   1224 H HA3  B GLY   A 1 48  ? 18.732 4.900   -0.523  0.28 13.61 ?  48  GLY   A HA3  1 
ATOM   1225 N N    A VAL   A 1 49  ? 18.798 3.784   1.876   0.72 11.17 ?  49  VAL   A N    1 
ATOM   1226 N N    B VAL   A 1 49  ? 18.937 3.770   1.660   0.28 10.24 ?  49  VAL   A N    1 
ATOM   1227 C CA   A VAL   A 1 49  ? 19.316 3.375   3.179   0.72 11.30 ?  49  VAL   A CA   1 
ATOM   1228 C CA   B VAL   A 1 49  ? 19.433 3.256   2.935   0.28 9.80  ?  49  VAL   A CA   1 
ATOM   1229 C C    A VAL   A 1 49  ? 20.634 4.082   3.488   0.72 10.28 ?  49  VAL   A C    1 
ATOM   1230 C C    B VAL   A 1 49  ? 20.712 3.976   3.335   0.28 9.29  ?  49  VAL   A C    1 
ATOM   1231 O O    A VAL   A 1 49  ? 20.860 4.536   4.615   0.72 10.79 ?  49  VAL   A O    1 
ATOM   1232 O O    B VAL   A 1 49  ? 20.896 4.342   4.501   0.28 9.37  ?  49  VAL   A O    1 
ATOM   1233 C CB   A VAL   A 1 49  ? 19.462 1.841   3.230   0.72 12.29 ?  49  VAL   A CB   1 
ATOM   1234 C CB   B VAL   A 1 49  ? 19.650 1.731   2.856   0.28 9.42  ?  49  VAL   A CB   1 
ATOM   1235 C CG1  A VAL   A 1 49  ? 20.289 1.411   4.436   0.72 12.32 ?  49  VAL   A CG1  1 
ATOM   1236 C CG1  B VAL   A 1 49  ? 20.521 1.254   4.018   0.28 9.45  ?  49  VAL   A CG1  1 
ATOM   1237 C CG2  A VAL   A 1 49  ? 18.084 1.187   3.252   0.72 14.16 ?  49  VAL   A CG2  1 
ATOM   1238 C CG2  B VAL   A 1 49  ? 18.321 0.996   2.852   0.28 9.52  ?  49  VAL   A CG2  1 
ATOM   1239 H H    A VAL   A 1 49  ? 18.671 3.133   1.324   0.72 13.43 ?  49  VAL   A H    1 
ATOM   1240 H H    B VAL   A 1 49  ? 18.859 3.179   1.044   0.28 12.31 ?  49  VAL   A H    1 
ATOM   1241 H HA   A VAL   A 1 49  ? 18.682 3.631   3.859   0.72 13.58 ?  49  VAL   A HA   1 
ATOM   1242 H HA   B VAL   A 1 49  ? 18.770 3.425   3.621   0.28 11.78 ?  49  VAL   A HA   1 
ATOM   1243 H HB   A VAL   A 1 49  ? 19.925 1.540   2.429   0.72 14.77 ?  49  VAL   A HB   1 
ATOM   1244 H HB   B VAL   A 1 49  ? 20.111 1.519   2.031   0.28 11.32 ?  49  VAL   A HB   1 
ATOM   1245 H HG11 A VAL   A 1 49  ? 20.136 0.469   4.598   0.72 14.80 ?  49  VAL   A HG11 1 
ATOM   1246 H HG11 B VAL   A 1 49  ? 20.403 0.298   4.125   0.28 11.36 ?  49  VAL   A HG11 1 
ATOM   1247 H HG12 A VAL   A 1 49  ? 21.228 1.568   4.250   0.72 14.80 ?  49  VAL   A HG12 1 
ATOM   1248 H HG12 B VAL   A 1 49  ? 21.451 1.450   3.822   0.28 11.36 ?  49  VAL   A HG12 1 
ATOM   1249 H HG13 A VAL   A 1 49  ? 20.009 1.930   5.206   0.72 14.80 ?  49  VAL   A HG13 1 
ATOM   1250 H HG13 B VAL   A 1 49  ? 20.246 1.711   4.828   0.28 11.36 ?  49  VAL   A HG13 1 
ATOM   1251 H HG21 A VAL   A 1 49  ? 18.193 0.226   3.282   0.72 17.01 ?  49  VAL   A HG21 1 
ATOM   1252 H HG21 B VAL   A 1 49  ? 18.485 0.047   2.740   0.28 11.45 ?  49  VAL   A HG21 1 
ATOM   1253 H HG22 A VAL   A 1 49  ? 17.606 1.495   4.037   0.72 17.01 ?  49  VAL   A HG22 1 
ATOM   1254 H HG22 B VAL   A 1 49  ? 17.870 1.155   3.697   0.28 11.45 ?  49  VAL   A HG22 1 
ATOM   1255 H HG23 A VAL   A 1 49  ? 17.604 1.444   2.449   0.72 17.01 ?  49  VAL   A HG23 1 
ATOM   1256 H HG23 B VAL   A 1 49  ? 17.780 1.329   2.120   0.28 11.45 ?  49  VAL   A HG23 1 
ATOM   1257 N N    A ALA   A 1 50  ? 21.538 4.140   2.508   0.72 9.87  ?  50  ALA   A N    1 
ATOM   1258 N N    B ALA   A 1 50  ? 21.629 4.157   2.385   0.28 9.10  ?  50  ALA   A N    1 
ATOM   1259 C CA   A ALA   A 1 50  ? 22.862 4.703   2.762   0.72 9.94  ?  50  ALA   A CA   1 
ATOM   1260 C CA   B ALA   A 1 50  ? 22.927 4.741   2.708   0.28 9.40  ?  50  ALA   A CA   1 
ATOM   1261 C C    A ALA   A 1 50  ? 22.774 6.164   3.178   0.72 10.07 ?  50  ALA   A C    1 
ATOM   1262 C C    B ALA   A 1 50  ? 22.791 6.190   3.155   0.28 9.51  ?  50  ALA   A C    1 
ATOM   1263 O O    A ALA   A 1 50  ? 23.408 6.584   4.152   0.72 10.45 ?  50  ALA   A O    1 
ATOM   1264 O O    B ALA   A 1 50  ? 23.410 6.601   4.144   0.28 9.57  ?  50  ALA   A O    1 
ATOM   1265 C CB   A ALA   A 1 50  ? 23.742 4.557   1.523   0.72 9.83  ?  50  ALA   A CB   1 
ATOM   1266 C CB   B ALA   A 1 50  ? 23.856 4.638   1.500   0.28 9.53  ?  50  ALA   A CB   1 
ATOM   1267 H H    A ALA   A 1 50  ? 21.419 3.869   1.699   0.72 11.87 ?  50  ALA   A H    1 
ATOM   1268 H H    B ALA   A 1 50  ? 21.523 3.949   1.560   0.28 10.94 ?  50  ALA   A H    1 
ATOM   1269 H HA   A ALA   A 1 50  ? 23.282 4.218   3.489   0.72 11.95 ?  50  ALA   A HA   1 
ATOM   1270 H HA   B ALA   A 1 50  ? 23.327 4.244   3.436   0.28 11.30 ?  50  ALA   A HA   1 
ATOM   1271 H HB1  A ALA   A 1 50  ? 24.620 4.936   1.709   0.72 11.82 ?  50  ALA   A HB1  1 
ATOM   1272 H HB1  B ALA   A 1 50  ? 24.714 5.030   1.727   0.28 11.45 ?  50  ALA   A HB1  1 
ATOM   1273 H HB2  A ALA   A 1 50  ? 23.832 3.616   1.306   0.72 11.82 ?  50  ALA   A HB2  1 
ATOM   1274 H HB2  B ALA   A 1 50  ? 23.972 3.702   1.269   0.28 11.45 ?  50  ALA   A HB2  1 
ATOM   1275 H HB3  A ALA   A 1 50  ? 23.331 5.031   0.783   0.72 11.82 ?  50  ALA   A HB3  1 
ATOM   1276 H HB3  B ALA   A 1 50  ? 23.461 5.115   0.754   0.28 11.45 ?  50  ALA   A HB3  1 
ATOM   1277 N N    A GLY   A 1 51  ? 21.993 6.959   2.447   0.72 10.16 ?  51  GLY   A N    1 
ATOM   1278 N N    B GLY   A 1 51  ? 21.987 6.980   2.443   0.28 9.80  ?  51  GLY   A N    1 
ATOM   1279 C CA   A GLY   A 1 51  ? 21.829 8.347   2.831   0.72 10.91 ?  51  GLY   A CA   1 
ATOM   1280 C CA   B GLY   A 1 51  ? 21.814 8.369   2.828   0.28 10.38 ?  51  GLY   A CA   1 
ATOM   1281 C C    A GLY   A 1 51  ? 21.235 8.484   4.217   0.72 10.75 ?  51  GLY   A C    1 
ATOM   1282 C C    B GLY   A 1 51  ? 21.198 8.514   4.205   0.28 10.47 ?  51  GLY   A C    1 
ATOM   1283 O O    A GLY   A 1 51  ? 21.637 9.357   4.993   0.72 11.38 ?  51  GLY   A O    1 
ATOM   1284 O O    B GLY   A 1 51  ? 21.551 9.423   4.962   0.28 10.55 ?  51  GLY   A O    1 
ATOM   1285 H H    A GLY   A 1 51  ? 21.567 6.721   1.737   0.72 12.21 ?  51  GLY   A H    1 
ATOM   1286 H H    B GLY   A 1 51  ? 21.545 6.736   1.748   0.28 11.77 ?  51  GLY   A H    1 
ATOM   1287 H HA2  A GLY   A 1 51  ? 22.688 8.794   2.814   0.72 13.11 ?  51  GLY   A HA2  1 
ATOM   1288 H HA2  B GLY   A 1 51  ? 22.675 8.814   2.826   0.28 12.47 ?  51  GLY   A HA2  1 
ATOM   1289 H HA3  A GLY   A 1 51  ? 21.240 8.790   2.196   0.72 13.11 ?  51  GLY   A HA3  1 
ATOM   1290 H HA3  B GLY   A 1 51  ? 21.237 8.811   2.185   0.28 12.47 ?  51  GLY   A HA3  1 
ATOM   1291 N N    . ALA   A 1 52  ? 20.266 7.622   4.547   1.00 10.74 ?  52  ALA   A N    1 
ATOM   1292 C CA   . ALA   A 1 52  ? 19.623 7.680   5.856   1.00 11.26 ?  52  ALA   A CA   1 
ATOM   1293 C C    . ALA   A 1 52  ? 20.582 7.272   6.973   1.00 10.65 ?  52  ALA   A C    1 
ATOM   1294 O O    . ALA   A 1 52  ? 20.658 7.938   8.011   1.00 11.64 ?  52  ALA   A O    1 
ATOM   1295 C CB   . ALA   A 1 52  ? 18.368 6.803   5.854   1.00 12.94 ?  52  ALA   A CB   1 
ATOM   1296 H H    A ALA   A 1 52  ? 19.975 6.991   4.032   0.72 12.91 ?  52  ALA   A H    1 
ATOM   1297 H H    B ALA   A 1 52  ? 19.998 6.972   4.042   0.28 12.91 ?  52  ALA   A H    1 
ATOM   1298 H HA   . ALA   A 1 52  ? 19.345 8.589   6.021   1.00 13.54 ?  52  ALA   A HA   1 
ATOM   1299 H HB1  . ALA   A 1 52  ? 17.947 6.855   6.728   1.00 15.55 ?  52  ALA   A HB1  1 
ATOM   1300 H HB2  . ALA   A 1 52  ? 17.756 7.129   5.175   1.00 15.55 ?  52  ALA   A HB2  1 
ATOM   1301 H HB3  . ALA   A 1 52  ? 18.618 5.886   5.663   1.00 15.55 ?  52  ALA   A HB3  1 
ATOM   1302 N N    A LEU   A 1 53  ? 21.313 6.169   6.794   0.72 10.75 ?  53  LEU   A N    1 
ATOM   1303 N N    B LEU   A 1 53  ? 21.324 6.175   6.773   0.28 10.41 ?  53  LEU   A N    1 
ATOM   1304 C CA   A LEU   A 1 53  ? 22.289 5.775   7.809   0.72 11.20 ?  53  LEU   A CA   1 
ATOM   1305 C CA   B LEU   A 1 53  ? 22.294 5.738   7.777   0.28 10.36 ?  53  LEU   A CA   1 
ATOM   1306 C C    A LEU   A 1 53  ? 23.326 6.870   8.003   0.72 10.30 ?  53  LEU   A C    1 
ATOM   1307 C C    B LEU   A 1 53  ? 23.376 6.789   7.988   0.28 10.09 ?  53  LEU   A C    1 
ATOM   1308 O O    A LEU   A 1 53  ? 23.622 7.273   9.133   0.72 11.24 ?  53  LEU   A O    1 
ATOM   1309 O O    B LEU   A 1 53  ? 23.776 7.058   9.125   0.28 10.50 ?  53  LEU   A O    1 
ATOM   1310 C CB   A LEU   A 1 53  ? 22.968 4.451   7.436   0.72 11.66 ?  53  LEU   A CB   1 
ATOM   1311 C CB   B LEU   A 1 53  ? 22.933 4.407   7.361   0.28 10.16 ?  53  LEU   A CB   1 
ATOM   1312 C CG   A LEU   A 1 53  ? 22.088 3.198   7.443   0.72 12.71 ?  53  LEU   A CG   1 
ATOM   1313 C CG   B LEU   A 1 53  ? 22.144 3.104   7.531   0.28 9.94  ?  53  LEU   A CG   1 
ATOM   1314 C CD1  A LEU   A 1 53  ? 22.889 2.005   6.943   0.72 13.38 ?  53  LEU   A CD1  1 
ATOM   1315 C CD1  B LEU   A 1 53  ? 22.823 1.988   6.749   0.28 10.62 ?  53  LEU   A CD1  1 
ATOM   1316 C CD2  A LEU   A 1 53  ? 21.518 2.921   8.829   0.72 13.42 ?  53  LEU   A CD2  1 
ATOM   1317 C CD2  B LEU   A 1 53  ? 22.021 2.710   8.993   0.28 9.42  ?  53  LEU   A CD2  1 
ATOM   1318 H H    A LEU   A 1 53  ? 21.264 5.641   6.113   0.72 12.92 ?  53  LEU   A H    1 
ATOM   1319 H H    B LEU   A 1 53  ? 21.287 5.675   6.073   0.28 12.51 ?  53  LEU   A H    1 
ATOM   1320 H HA   A LEU   A 1 53  ? 21.832 5.644   8.652   0.72 13.46 ?  53  LEU   A HA   1 
ATOM   1321 H HA   B LEU   A 1 53  ? 21.839 5.601   8.621   0.28 12.45 ?  53  LEU   A HA   1 
ATOM   1322 H HB2  A LEU   A 1 53  ? 23.334 4.535   6.541   0.72 14.01 ?  53  LEU   A HB2  1 
ATOM   1323 H HB2  B LEU   A 1 53  ? 23.158 4.469   6.421   0.28 12.21 ?  53  LEU   A HB2  1 
ATOM   1324 H HB3  A LEU   A 1 53  ? 23.691 4.291   8.062   0.72 14.01 ?  53  LEU   A HB3  1 
ATOM   1325 H HB3  B LEU   A 1 53  ? 23.748 4.299   7.873   0.28 12.21 ?  53  LEU   A HB3  1 
ATOM   1326 H HG   A LEU   A 1 53  ? 21.343 3.332   6.833   0.72 15.27 ?  53  LEU   A HG   1 
ATOM   1327 H HG   B LEU   A 1 53  ? 21.251 3.218   7.170   0.28 11.95 ?  53  LEU   A HG   1 
ATOM   1328 H HD11 A LEU   A 1 53  ? 22.321 1.218   6.950   0.72 16.08 ?  53  LEU   A HD11 1 
ATOM   1329 H HD11 B LEU   A 1 53  ? 22.324 1.165   6.874   0.28 12.77 ?  53  LEU   A HD11 1 
ATOM   1330 H HD12 A LEU   A 1 53  ? 23.192 2.185   6.039   0.72 16.08 ?  53  LEU   A HD12 1 
ATOM   1331 H HD12 B LEU   A 1 53  ? 22.839 2.225   5.809   0.28 12.77 ?  53  LEU   A HD12 1 
ATOM   1332 H HD13 A LEU   A 1 53  ? 23.650 1.870   7.527   0.72 16.08 ?  53  LEU   A HD13 1 
ATOM   1333 H HD13 B LEU   A 1 53  ? 23.729 1.878   7.079   0.28 12.77 ?  53  LEU   A HD13 1 
ATOM   1334 H HD21 A LEU   A 1 53  ? 21.048 2.072   8.815   0.72 16.12 ?  53  LEU   A HD21 1 
ATOM   1335 H HD21 B LEU   A 1 53  ? 21.476 1.909   9.060   0.28 11.32 ?  53  LEU   A HD21 1 
ATOM   1336 H HD22 A LEU   A 1 53  ? 22.243 2.889   9.469   0.72 16.12 ?  53  LEU   A HD22 1 
ATOM   1337 H HD22 B LEU   A 1 53  ? 22.907 2.538   9.349   0.28 11.32 ?  53  LEU   A HD22 1 
ATOM   1338 H HD23 A LEU   A 1 53  ? 20.900 3.633   9.064   0.72 16.12 ?  53  LEU   A HD23 1 
ATOM   1339 H HD23 B LEU   A 1 53  ? 21.603 3.437   9.479   0.28 11.32 ?  53  LEU   A HD23 1 
ATOM   1340 N N    . ASN   A 1 54  ? 23.865 7.389   6.903   1.00 10.17 ?  54  ASN   A N    1 
ATOM   1341 C CA   . ASN   A 1 54  ? 24.913 8.391   7.032   1.00 10.22 ?  54  ASN   A CA   1 
ATOM   1342 C C    . ASN   A 1 54  ? 24.400 9.638   7.751   1.00 10.65 ?  54  ASN   A C    1 
ATOM   1343 O O    . ASN   A 1 54  ? 25.089 10.195  8.617   1.00 11.16 ?  54  ASN   A O    1 
ATOM   1344 C CB   . ASN   A 1 54  ? 25.475 8.750   5.667   1.00 10.48 ?  54  ASN   A CB   1 
ATOM   1345 C CG   . ASN   A 1 54  ? 26.491 9.851   5.768   1.00 10.42 ?  54  ASN   A CG   1 
ATOM   1346 O OD1  . ASN   A 1 54  ? 27.500 9.712   6.471   1.00 10.69 ?  54  ASN   A OD1  1 
ATOM   1347 N ND2  . ASN   A 1 54  ? 26.229 10.968  5.105   1.00 11.41 ?  54  ASN   A ND2  1 
ATOM   1348 H H    A ASN   A 1 54  ? 23.641 7.187   6.097   0.72 12.22 ?  54  ASN   A H    1 
ATOM   1349 H H    B ASN   A 1 54  ? 23.599 7.240   6.098   0.28 12.22 ?  54  ASN   A H    1 
ATOM   1350 H HA   . ASN   A 1 54  ? 25.630 8.022   7.562   1.00 12.28 ?  54  ASN   A HA   1 
ATOM   1351 H HB2  . ASN   A 1 54  ? 25.912 7.963   5.290   1.00 12.59 ?  54  ASN   A HB2  1 
ATOM   1352 H HB3  . ASN   A 1 54  ? 24.757 9.040   5.087   1.00 12.59 ?  54  ASN   A HB3  1 
ATOM   1353 H HD21 . ASN   A 1 54  ? 26.778 11.624  5.139   1.00 13.71 ?  54  ASN   A HD21 1 
ATOM   1354 H HD22 . ASN   A 1 54  ? 25.508 11.030  4.635   1.00 13.71 ?  54  ASN   A HD22 1 
ATOM   1355 N N    . LYS   A 1 55  ? 23.189 10.087  7.410   1.00 10.78 ?  55  LYS   A N    1 
ATOM   1356 C CA   . LYS   A 1 55  ? 22.605 11.241  8.078   1.00 11.52 ?  55  LYS   A CA   1 
ATOM   1357 C C    . LYS   A 1 55  ? 22.515 11.009  9.579   1.00 11.75 ?  55  LYS   A C    1 
ATOM   1358 O O    . LYS   A 1 55  ? 22.799 11.911  10.376  1.00 12.47 ?  55  LYS   A O    1 
ATOM   1359 C CB   . LYS   A 1 55  ? 21.232 11.527  7.464   1.00 12.19 ?  55  LYS   A CB   1 
ATOM   1360 C CG   . LYS   A 1 55  ? 20.480 12.693  8.081   1.00 13.88 ?  55  LYS   A CG   1 
ATOM   1361 C CD   . LYS   A 1 55  ? 19.156 12.929  7.357   1.00 14.83 ?  55  LYS   A CD   1 
ATOM   1362 C CE   . LYS   A 1 55  ? 18.292 13.955  8.067   1.00 16.65 ?  55  LYS   A CE   1 
ATOM   1363 N NZ   . LYS   A 1 55  ? 16.983 14.133  7.372   1.00 17.54 ?  55  LYS   A NZ   1 
ATOM   1364 H H    . LYS   A 1 55  ? 22.681 9.733   6.802   1.00 12.95 ?  55  LYS   A H    1 
ATOM   1365 H HA   . LYS   A 1 55  ? 23.166 12.014  7.924   1.00 13.84 ?  55  LYS   A HA   1 
ATOM   1366 H HB2  . LYS   A 1 55  ? 21.346 11.728  6.521   1.00 14.65 ?  55  LYS   A HB2  1 
ATOM   1367 H HB3  . LYS   A 1 55  ? 20.673 10.740  7.562   1.00 14.65 ?  55  LYS   A HB3  1 
ATOM   1368 H HG2  . LYS   A 1 55  ? 20.286 12.493  9.011   1.00 16.67 ?  55  LYS   A HG2  1 
ATOM   1369 H HG3  . LYS   A 1 55  ? 21.017 13.495  8.010   1.00 16.67 ?  55  LYS   A HG3  1 
ATOM   1370 H HD2  . LYS   A 1 55  ? 19.343 13.251  6.460   1.00 17.82 ?  55  LYS   A HD2  1 
ATOM   1371 H HD3  . LYS   A 1 55  ? 18.668 12.090  7.313   1.00 17.82 ?  55  LYS   A HD3  1 
ATOM   1372 H HE2  . LYS   A 1 55  ? 18.120 13.650  8.973   1.00 20.00 ?  55  LYS   A HE2  1 
ATOM   1373 H HE3  . LYS   A 1 55  ? 18.754 14.805  8.080   1.00 20.00 ?  55  LYS   A HE3  1 
ATOM   1374 H HZ1  . LYS   A 1 55  ? 16.408 14.543  7.911   1.00 21.07 ?  55  LYS   A HZ1  1 
ATOM   1375 H HZ2  . LYS   A 1 55  ? 17.094 14.625  6.639   1.00 21.07 ?  55  LYS   A HZ2  1 
ATOM   1376 H HZ3  . LYS   A 1 55  ? 16.649 13.340  7.142   1.00 21.07 ?  55  LYS   A HZ3  1 
ATOM   1377 N N    . ALA   A 1 56  ? 22.128 9.797   9.985   1.00 12.11 ?  56  ALA   A N    1 
ATOM   1378 C CA   . ALA   A 1 56  ? 22.001 9.476   11.400  1.00 12.83 ?  56  ALA   A CA   1 
ATOM   1379 C C    . ALA   A 1 56  ? 23.340 9.507   12.126  1.00 12.52 ?  56  ALA   A C    1 
ATOM   1380 O O    . ALA   A 1 56  ? 23.359 9.689   13.345  1.00 13.89 ?  56  ALA   A O    1 
ATOM   1381 C CB   . ALA   A 1 56  ? 21.322 8.114   11.571  1.00 13.83 ?  56  ALA   A CB   1 
ATOM   1382 H H    . ALA   A 1 56  ? 21.940 9.146   9.456   1.00 14.56 ?  56  ALA   A H    1 
ATOM   1383 H HA   . ALA   A 1 56  ? 21.435 10.133  11.818  1.00 15.41 ?  56  ALA   A HA   1 
ATOM   1384 H HB1  . ALA   A 1 56  ? 21.243 7.915   12.519  1.00 16.62 ?  56  ALA   A HB1  1 
ATOM   1385 H HB2  . ALA   A 1 56  ? 20.442 8.149   11.167  1.00 16.62 ?  56  ALA   A HB2  1 
ATOM   1386 H HB3  . ALA   A 1 56  ? 21.858 7.430   11.136  1.00 16.62 ?  56  ALA   A HB3  1 
ATOM   1387 N N    . THR   A 1 57  ? 24.455 9.319   11.413  1.00 11.68 ?  57  THR   A N    1 
ATOM   1388 C CA   . THR   A 1 57  ? 25.795 9.448   11.992  1.00 11.78 ?  57  THR   A CA   1 
ATOM   1389 C C    . THR   A 1 57  ? 26.349 10.865  11.910  1.00 12.33 ?  57  THR   A C    1 
ATOM   1390 O O    . THR   A 1 57  ? 27.535 11.073  12.199  1.00 12.72 ?  57  THR   A O    1 
ATOM   1391 C CB   . THR   A 1 57  ? 26.806 8.497   11.324  1.00 11.58 ?  57  THR   A CB   1 
ATOM   1392 O OG1  . THR   A 1 57  ? 27.192 8.997   10.031  1.00 11.42 ?  57  THR   A OG1  1 
ATOM   1393 C CG2  . THR   A 1 57  ? 26.270 7.080   11.214  1.00 11.45 ?  57  THR   A CG2  1 
ATOM   1394 H H    . THR   A 1 57  ? 24.463 9.091   10.584  1.00 14.04 ?  57  THR   A H    1 
ATOM   1395 H HA   . THR   A 1 57  ? 25.749 9.195   12.934  1.00 14.16 ?  57  THR   A HA   1 
ATOM   1396 H HB   . THR   A 1 57  ? 27.600 8.451   11.885  1.00 13.92 ?  57  THR   A HB   1 
ATOM   1397 H HG1  . THR   A 1 57  ? 26.514 9.069   9.543   1.00 13.73 ?  57  THR   A HG1  1 
ATOM   1398 H HG21 . THR   A 1 57  ? 26.884 6.525   10.703  1.00 13.76 ?  57  THR   A HG21 1 
ATOM   1399 H HG22 . THR   A 1 57  ? 26.162 6.688   12.097  1.00 13.76 ?  57  THR   A HG22 1 
ATOM   1400 H HG23 . THR   A 1 57  ? 25.409 7.075   10.768  1.00 13.76 ?  57  THR   A HG23 1 
ATOM   1401 N N    . ASN   A 1 58  ? 25.533 11.839  11.509  1.00 12.88 ?  58  ASN   A N    1 
ATOM   1402 C CA   . ASN   A 1 58  ? 25.996 13.218  11.406  1.00 13.66 ?  58  ASN   A CA   1 
ATOM   1403 C C    . ASN   A 1 58  ? 27.149 13.337  10.402  1.00 12.62 ?  58  ASN   A C    1 
ATOM   1404 O O    . ASN   A 1 58  ? 28.045 14.168  10.562  1.00 13.29 ?  58  ASN   A O    1 
ATOM   1405 C CB   . ASN   A 1 58  ? 26.368 13.763  12.798  1.00 16.37 ?  58  ASN   A CB   1 
ATOM   1406 C CG   . ASN   A 1 58  ? 26.782 15.221  12.786  1.00 20.18 ?  58  ASN   A CG   1 
ATOM   1407 O OD1  . ASN   A 1 58  ? 26.157 16.046  12.130  1.00 21.69 ?  58  ASN   A OD1  1 
ATOM   1408 N ND2  . ASN   A 1 58  ? 27.837 15.548  13.536  1.00 21.66 ?  58  ASN   A ND2  1 
ATOM   1409 H H    . ASN   A 1 58  ? 24.708 11.718  11.285  1.00 15.47 ?  58  ASN   A H    1 
ATOM   1410 H HA   . ASN   A 1 58  ? 25.266 13.752  11.070  1.00 16.41 ?  58  ASN   A HA   1 
ATOM   1411 H HB2  . ASN   A 1 58  ? 25.594 13.672  13.386  1.00 19.66 ?  58  ASN   A HB2  1 
ATOM   1412 H HB3  . ASN   A 1 58  ? 27.107 13.252  13.157  1.00 19.66 ?  58  ASN   A HB3  1 
ATOM   1413 H HD21 . ASN   A 1 58  ? 28.103 16.367  13.567  1.00 26.01 ?  58  ASN   A HD21 1 
ATOM   1414 H HD22 . ASN   A 1 58  ? 28.245 14.944  13.985  1.00 26.01 ?  58  ASN   A HD22 1 
ATOM   1415 N N    . ASN   A 1 59  ? 27.131 12.519  9.346   1.00 11.57 ?  59  ASN   A N    1 
ATOM   1416 C CA   . ASN   A 1 59  ? 28.113 12.500  8.251   1.00 11.19 ?  59  ASN   A CA   1 
ATOM   1417 C C    . ASN   A 1 59  ? 29.428 11.816  8.640   1.00 10.86 ?  59  ASN   A C    1 
ATOM   1418 O O    . ASN   A 1 59  ? 30.345 11.771  7.812   1.00 11.10 ?  59  ASN   A O    1 
ATOM   1419 C CB   . ASN   A 1 59  ? 28.403 13.887  7.644   1.00 11.51 ?  59  ASN   A CB   1 
ATOM   1420 C CG   . ASN   A 1 59  ? 28.762 13.817  6.176   1.00 11.74 ?  59  ASN   A CG   1 
ATOM   1421 O OD1  . ASN   A 1 59  ? 28.053 13.197  5.380   1.00 11.97 ?  59  ASN   A OD1  1 
ATOM   1422 N ND2  . ASN   A 1 59  ? 29.856 14.472  5.800   1.00 12.41 ?  59  ASN   A ND2  1 
ATOM   1423 H H    . ASN   A 1 59  ? 26.518 11.923  9.233   1.00 13.91 ?  59  ASN   A H    1 
ATOM   1424 H HA   . ASN   A 1 59  ? 27.734 11.970  7.537   1.00 13.44 ?  59  ASN   A HA   1 
ATOM   1425 H HB2  . ASN   A 1 59  ? 27.614 14.446  7.730   1.00 13.83 ?  59  ASN   A HB2  1 
ATOM   1426 H HB3  . ASN   A 1 59  ? 29.149 14.294  8.112   1.00 13.83 ?  59  ASN   A HB3  1 
ATOM   1427 H HD21 . ASN   A 1 59  ? 30.106 14.463  4.976   1.00 14.91 ?  59  ASN   A HD21 1 
ATOM   1428 H HD22 . ASN   A 1 59  ? 30.332 14.895  6.384   1.00 14.91 ?  59  ASN   A HD22 1 
ATOM   1429 N N    . ALA   A 1 60  ? 29.552 11.268  9.848   1.00 10.93 ?  60  ALA   A N    1 
ATOM   1430 C CA   . ALA   A 1 60  ? 30.788 10.582  10.207  1.00 11.21 ?  60  ALA   A CA   1 
ATOM   1431 C C    . ALA   A 1 60  ? 31.009 9.347   9.341   1.00 11.17 ?  60  ALA   A C    1 
ATOM   1432 O O    . ALA   A 1 60  ? 32.152 9.024   9.005   1.00 11.57 ?  60  ALA   A O    1 
ATOM   1433 C CB   . ALA   A 1 60  ? 30.776 10.214  11.688  1.00 12.17 ?  60  ALA   A CB   1 
ATOM   1434 H H    . ALA   A 1 60  ? 28.949 11.271  10.460  1.00 13.14 ?  60  ALA   A H    1 
ATOM   1435 H HA   . ALA   A 1 60  ? 31.534 11.185  10.055  1.00 13.47 ?  60  ALA   A HA   1 
ATOM   1436 H HB1  . ALA   A 1 60  ? 31.605 9.762   11.907  1.00 14.63 ?  60  ALA   A HB1  1 
ATOM   1437 H HB2  . ALA   A 1 60  ? 30.692 11.026  12.212  1.00 14.63 ?  60  ALA   A HB2  1 
ATOM   1438 H HB3  . ALA   A 1 60  ? 30.022 9.629   11.860  1.00 14.63 ?  60  ALA   A HB3  1 
ATOM   1439 N N    . MET   A 1 61  ? 29.935 8.658   8.956   1.00 10.81 ?  61  MET   A N    1 
ATOM   1440 C CA   . MET   A 1 61  ? 30.074 7.520   8.054   1.00 10.58 ?  61  MET   A CA   1 
ATOM   1441 C C    . MET   A 1 61  ? 30.709 7.942   6.732   1.00 10.43 ?  61  MET   A C    1 
ATOM   1442 O O    . MET   A 1 61  ? 31.601 7.257   6.219   1.00 10.79 ?  61  MET   A O    1 
ATOM   1443 C CB   . MET   A 1 61  ? 28.712 6.859   7.840   1.00 10.38 ?  61  MET   A CB   1 
ATOM   1444 C CG   . MET   A 1 61  ? 28.726 5.691   6.870   1.00 11.14 ?  61  MET   A CG   1 
ATOM   1445 S SD   . MET   A 1 61  ? 27.101 4.946   6.657   1.00 11.90 ?  61  MET   A SD   1 
ATOM   1446 C CE   . MET   A 1 61  ? 26.963 4.038   8.204   1.00 13.39 ?  61  MET   A CE   1 
ATOM   1447 H H    . MET   A 1 61  ? 29.128 8.830   9.191   1.00 13.00 ?  61  MET   A H    1 
ATOM   1448 H HA   . MET   A 1 61  ? 30.652 6.863   8.474   1.00 12.72 ?  61  MET   A HA   1 
ATOM   1449 H HB2  . MET   A 1 61  ? 28.391 6.529   8.692   1.00 12.48 ?  61  MET   A HB2  1 
ATOM   1450 H HB3  . MET   A 1 61  ? 28.097 7.519   7.490   1.00 12.48 ?  61  MET   A HB3  1 
ATOM   1451 H HG2  . MET   A 1 61  ? 29.021 5.990   6.000   1.00 13.38 ?  61  MET   A HG2  1 
ATOM   1452 H HG3  . MET   A 1 61  ? 29.322 5.000   7.206   1.00 13.38 ?  61  MET   A HG3  1 
ATOM   1453 H HE1  . MET   A 1 61  ? 26.119 3.558   8.218   1.00 16.08 ?  61  MET   A HE1  1 
ATOM   1454 H HE2  . MET   A 1 61  ? 27.700 3.412   8.271   1.00 16.08 ?  61  MET   A HE2  1 
ATOM   1455 H HE3  . MET   A 1 61  ? 26.995 4.665   8.947   1.00 16.08 ?  61  MET   A HE3  1 
ATOM   1456 N N    . GLN   A 1 62  ? 30.268 9.075   6.173   1.00 10.55 ?  62  GLN   A N    1 
ATOM   1457 C CA   . GLN   A 1 62  ? 30.832 9.545   4.911   1.00 10.59 ?  62  GLN   A CA   1 
ATOM   1458 C C    . GLN   A 1 62  ? 32.301 9.923   5.061   1.00 10.58 ?  62  GLN   A C    1 
ATOM   1459 O O    . GLN   A 1 62  ? 33.111 9.611   4.183   1.00 10.86 ?  62  GLN   A O    1 
ATOM   1460 C CB   . GLN   A 1 62  ? 30.029 10.730  4.379   1.00 10.86 ?  62  GLN   A CB   1 
ATOM   1461 C CG   . GLN   A 1 62  ? 30.399 11.095  2.947   1.00 10.78 ?  62  GLN   A CG   1 
ATOM   1462 C CD   . GLN   A 1 62  ? 30.076 9.961   2.003   1.00 11.09 ?  62  GLN   A CD   1 
ATOM   1463 O OE1  . GLN   A 1 62  ? 28.896 9.657   1.783   1.00 11.72 ?  62  GLN   A OE1  1 
ATOM   1464 N NE2  . GLN   A 1 62  ? 31.101 9.292   1.483   1.00 11.43 ?  62  GLN   A NE2  1 
ATOM   1465 H H    . GLN   A 1 62  ? 29.651 9.570   6.500   1.00 12.68 ?  62  GLN   A H    1 
ATOM   1466 H HA   . GLN   A 1 62  ? 30.779 8.825   4.262   1.00 12.72 ?  62  GLN   A HA   1 
ATOM   1467 H HB2  . GLN   A 1 62  ? 29.087 10.510  4.402   1.00 13.05 ?  62  GLN   A HB2  1 
ATOM   1468 H HB3  . GLN   A 1 62  ? 30.204 11.504  4.939   1.00 13.05 ?  62  GLN   A HB3  1 
ATOM   1469 H HG2  . GLN   A 1 62  ? 29.881 11.871  2.674   1.00 12.95 ?  62  GLN   A HG2  1 
ATOM   1470 H HG3  . GLN   A 1 62  ? 31.345 11.283  2.893   1.00 12.95 ?  62  GLN   A HG3  1 
ATOM   1471 H HE21 . GLN   A 1 62  ? 31.906 9.525   1.676   1.00 13.74 ?  62  GLN   A HE21 1 
ATOM   1472 H HE22 . GLN   A 1 62  ? 30.961 8.632   0.950   1.00 13.74 ?  62  GLN   A HE22 1 
ATOM   1473 N N    . VAL   A 1 63  ? 32.662 10.609  6.150   1.00 11.08 ?  63  VAL   A N    1 
ATOM   1474 C CA   . VAL   A 1 63  ? 34.056 11.000  6.365   1.00 11.95 ?  63  VAL   A CA   1 
ATOM   1475 C C    . VAL   A 1 63  ? 34.953 9.764   6.428   1.00 11.23 ?  63  VAL   A C    1 
ATOM   1476 O O    . VAL   A 1 63  ? 36.006 9.696   5.777   1.00 11.82 ?  63  VAL   A O    1 
ATOM   1477 C CB   . VAL   A 1 63  ? 34.167 11.873  7.628   1.00 13.48 ?  63  VAL   A CB   1 
ATOM   1478 C CG1  . VAL   A 1 63  ? 35.605 12.126  7.993   1.00 15.09 ?  63  VAL   A CG1  1 
ATOM   1479 C CG2  . VAL   A 1 63  ? 33.437 13.200  7.416   1.00 13.88 ?  63  VAL   A CG2  1 
ATOM   1480 H H    . VAL   A 1 63  ? 32.119 10.854  6.777   1.00 13.31 ?  63  VAL   A H    1 
ATOM   1481 H HA   . VAL   A 1 63  ? 34.342 11.535  5.613   1.00 14.36 ?  63  VAL   A HA   1 
ATOM   1482 H HB   . VAL   A 1 63  ? 33.747 11.416  8.375   1.00 16.20 ?  63  VAL   A HB   1 
ATOM   1483 H HG11 . VAL   A 1 63  ? 35.644 12.857  8.628   1.00 18.13 ?  63  VAL   A HG11 1 
ATOM   1484 H HG12 . VAL   A 1 63  ? 35.977 11.323  8.388   1.00 18.13 ?  63  VAL   A HG12 1 
ATOM   1485 H HG13 . VAL   A 1 63  ? 36.093 12.360  7.189   1.00 18.13 ?  63  VAL   A HG13 1 
ATOM   1486 H HG21 . VAL   A 1 63  ? 33.523 13.744  8.216   1.00 16.67 ?  63  VAL   A HG21 1 
ATOM   1487 H HG22 . VAL   A 1 63  ? 33.834 13.663  6.660   1.00 16.67 ?  63  VAL   A HG22 1 
ATOM   1488 H HG23 . VAL   A 1 63  ? 32.500 13.022  7.238   1.00 16.67 ?  63  VAL   A HG23 1 
ATOM   1489 N N    . GLU   A 1 64  ? 34.532 8.756   7.200   1.00 11.16 ?  64  GLU   A N    1 
ATOM   1490 C CA   . GLU   A 1 64  ? 35.288 7.512   7.293   1.00 11.29 ?  64  GLU   A CA   1 
ATOM   1491 C C    . GLU   A 1 64  ? 35.375 6.828   5.935   1.00 11.00 ?  64  GLU   A C    1 
ATOM   1492 O O    . GLU   A 1 64  ? 36.422 6.279   5.561   1.00 11.45 ?  64  GLU   A O    1 
ATOM   1493 C CB   . GLU   A 1 64  ? 34.592 6.601   8.303   1.00 11.68 ?  64  GLU   A CB   1 
ATOM   1494 C CG   . GLU   A 1 64  ? 35.247 5.257   8.465   1.00 12.45 ?  64  GLU   A CG   1 
ATOM   1495 C CD   . GLU   A 1 64  ? 34.362 4.263   9.188   1.00 13.05 ?  64  GLU   A CD   1 
ATOM   1496 O OE1  . GLU   A 1 64  ? 33.124 4.352   9.047   1.00 13.77 ?  64  GLU   A OE1  1 
ATOM   1497 O OE2  . GLU   A 1 64  ? 34.910 3.374   9.881   1.00 13.39 -1 64  GLU   A OE2  1 
ATOM   1498 H H    . GLU   A 1 64  ? 33.806 8.765   7.661   1.00 13.42 ?  64  GLU   A H    1 
ATOM   1499 H HA   . GLU   A 1 64  ? 36.186 7.706   7.611   1.00 13.57 ?  64  GLU   A HA   1 
ATOM   1500 H HB2  . GLU   A 1 64  ? 34.596 7.042   9.174   1.00 14.03 ?  64  GLU   A HB2  1 
ATOM   1501 H HB3  . GLU   A 1 64  ? 33.677 6.465   8.015   1.00 14.03 ?  64  GLU   A HB3  1 
ATOM   1502 H HG2  . GLU   A 1 64  ? 35.450 4.885   7.591   1.00 14.96 ?  64  GLU   A HG2  1 
ATOM   1503 H HG3  . GLU   A 1 64  ? 36.062 5.363   8.976   1.00 14.96 ?  64  GLU   A HG3  1 
ATOM   1504 N N    . SER   A 1 65  ? 34.260 6.823   5.200   1.00 10.69 ?  65  SER   A N    1 
ATOM   1505 C CA   . SER   A 1 65  ? 34.209 6.166   3.898   1.00 10.73 ?  65  SER   A CA   1 
ATOM   1506 C C    . SER   A 1 65  ? 35.133 6.833   2.888   1.00 10.77 ?  65  SER   A C    1 
ATOM   1507 O O    . SER   A 1 65  ? 35.773 6.152   2.079   1.00 11.57 ?  65  SER   A O    1 
ATOM   1508 C CB   . SER   A 1 65  ? 32.775 6.173   3.365   1.00 10.68 ?  65  SER   A CB   1 
ATOM   1509 O OG   . SER   A 1 65  ? 31.922 5.360   4.156   1.00 11.35 ?  65  SER   A OG   1 
ATOM   1510 H H    . SER   A 1 65  ? 33.525 7.203   5.432   1.00 12.85 ?  65  SER   A H    1 
ATOM   1511 H HA   . SER   A 1 65  ? 34.490 5.244   3.997   1.00 12.90 ?  65  SER   A HA   1 
ATOM   1512 H HB2  . SER   A 1 65  ? 32.435 7.080   3.377   1.00 12.84 ?  65  SER   A HB2  1 
ATOM   1513 H HB3  . SER   A 1 65  ? 32.778 5.834   2.455   1.00 12.84 ?  65  SER   A HB3  1 
ATOM   1514 H HG   . SER   A 1 65  ? 31.919 5.639   4.950   1.00 13.64 ?  65  SER   A HG   1 
ATOM   1515 N N    . ASP   A 1 66  ? 35.207 8.168   2.906   1.00 10.92 ?  66  ASP   A N    1 
ATOM   1516 C CA   . ASP   A 1 66  ? 36.069 8.866   1.959   1.00 12.04 ?  66  ASP   A CA   1 
ATOM   1517 C C    . ASP   A 1 66  ? 37.531 8.509   2.193   1.00 11.69 ?  66  ASP   A C    1 
ATOM   1518 O O    . ASP   A 1 66  ? 38.300 8.333   1.240   1.00 12.65 ?  66  ASP   A O    1 
ATOM   1519 C CB   . ASP   A 1 66  ? 35.848 10.372  2.070   1.00 13.23 ?  66  ASP   A CB   1 
ATOM   1520 C CG   . ASP   A 1 66  ? 34.517 10.831  1.470   1.00 15.02 ?  66  ASP   A CG   1 
ATOM   1521 O OD1  . ASP   A 1 66  ? 33.802 10.035  0.825   1.00 15.21 ?  66  ASP   A OD1  1 
ATOM   1522 O OD2  . ASP   A 1 66  ? 34.213 12.029  1.624   1.00 17.81 -1 66  ASP   A OD2  1 
ATOM   1523 H H    . ASP   A 1 66  ? 34.765 8.680   3.441   1.00 13.12 ?  66  ASP   A H    1 
ATOM   1524 H HA   . ASP   A 1 66  ? 35.832 8.595   1.058   1.00 14.46 ?  66  ASP   A HA   1 
ATOM   1525 H HB2  . ASP   A 1 66  ? 35.855 10.626  3.006   1.00 15.90 ?  66  ASP   A HB2  1 
ATOM   1526 H HB3  . ASP   A 1 66  ? 36.565 10.830  1.599   1.00 15.90 ?  66  ASP   A HB3  1 
ATOM   1527 N N    . ASP   A 1 67  ? 37.930 8.378   3.458   1.00 11.87 ?  67  ASP   A N    1 
ATOM   1528 C CA   . ASP   A 1 67  ? 39.285 7.930   3.756   1.00 12.58 ?  67  ASP   A CA   1 
ATOM   1529 C C    . ASP   A 1 67  ? 39.505 6.495   3.291   1.00 12.88 ?  67  ASP   A C    1 
ATOM   1530 O O    . ASP   A 1 67  ? 40.566 6.169   2.742   1.00 13.32 ?  67  ASP   A O    1 
ATOM   1531 C CB   . ASP   A 1 67  ? 39.555 8.068   5.251   1.00 14.17 ?  67  ASP   A CB   1 
ATOM   1532 C CG   . ASP   A 1 67  ? 40.848 7.404   5.674   1.00 15.25 ?  67  ASP   A CG   1 
ATOM   1533 O OD1  . ASP   A 1 67  ? 41.925 8.030   5.541   1.00 17.82 ?  67  ASP   A OD1  1 
ATOM   1534 O OD2  . ASP   A 1 67  ? 40.792 6.242   6.133   1.00 15.26 -1 67  ASP   A OD2  1 
ATOM   1535 H H    . ASP   A 1 67  ? 37.444 8.536   4.148   1.00 14.26 ?  67  ASP   A H    1 
ATOM   1536 H HA   . ASP   A 1 67  ? 39.913 8.493   3.279   1.00 15.12 ?  67  ASP   A HA   1 
ATOM   1537 H HB2  . ASP   A 1 67  ? 39.614 9.005   5.470   1.00 17.03 ?  67  ASP   A HB2  1 
ATOM   1538 H HB3  . ASP   A 1 67  ? 38.832 7.648   5.739   1.00 17.03 ?  67  ASP   A HB3  1 
ATOM   1539 N N    . TYR   A 1 68  ? 38.511 5.617   3.491   1.00 12.39 ?  68  TYR   A N    1 
ATOM   1540 C CA   . TYR   A 1 68  ? 38.628 4.239   3.015   1.00 12.51 ?  68  TYR   A CA   1 
ATOM   1541 C C    . TYR   A 1 68  ? 38.872 4.192   1.507   1.00 12.11 ?  68  TYR   A C    1 
ATOM   1542 O O    . TYR   A 1 68  ? 39.747 3.459   1.032   1.00 12.64 ?  68  TYR   A O    1 
ATOM   1543 C CB   . TYR   A 1 68  ? 37.374 3.420   3.387   1.00 12.91 ?  68  TYR   A CB   1 
ATOM   1544 C CG   . TYR   A 1 68  ? 37.401 2.032   2.756   1.00 14.52 ?  68  TYR   A CG   1 
ATOM   1545 C CD1  . TYR   A 1 68  ? 36.940 1.839   1.458   1.00 16.00 ?  68  TYR   A CD1  1 
ATOM   1546 C CD2  . TYR   A 1 68  ? 37.939 0.943   3.426   1.00 16.16 ?  68  TYR   A CD2  1 
ATOM   1547 C CE1  . TYR   A 1 68  ? 37.005 0.620   0.845   1.00 17.26 ?  68  TYR   A CE1  1 
ATOM   1548 C CE2  . TYR   A 1 68  ? 37.997 -0.315  2.815   1.00 16.79 ?  68  TYR   A CE2  1 
ATOM   1549 C CZ   . TYR   A 1 68  ? 37.539 -0.452  1.525   1.00 17.33 ?  68  TYR   A CZ   1 
ATOM   1550 O OH   . TYR   A 1 68  ? 37.619 -1.672  0.909   1.00 18.42 ?  68  TYR   A OH   1 
ATOM   1551 H H    . TYR   A 1 68  ? 37.769 5.793   3.890   1.00 14.88 ?  68  TYR   A H    1 
ATOM   1552 H HA   . TYR   A 1 68  ? 39.387 3.822   3.447   1.00 15.03 ?  68  TYR   A HA   1 
ATOM   1553 H HB2  . TYR   A 1 68  ? 37.336 3.313   4.348   1.00 15.51 ?  68  TYR   A HB2  1 
ATOM   1554 H HB3  . TYR   A 1 68  ? 36.582 3.884   3.068   1.00 15.51 ?  68  TYR   A HB3  1 
ATOM   1555 H HD1  . TYR   A 1 68  ? 36.588 2.565   0.989   1.00 19.23 ?  68  TYR   A HD1  1 
ATOM   1556 H HD2  . TYR   A 1 68  ? 38.267 1.052   4.285   1.00 19.41 ?  68  TYR   A HD2  1 
ATOM   1557 H HE1  . TYR   A 1 68  ? 36.678 0.515   -0.022  1.00 20.73 ?  68  TYR   A HE1  1 
ATOM   1558 H HE2  . TYR   A 1 68  ? 38.360 -1.045  3.256   1.00 20.17 ?  68  TYR   A HE2  1 
ATOM   1559 H HH   . TYR   A 1 68  ? 37.946 -2.238  1.440   1.00 22.13 ?  68  TYR   A HH   1 
ATOM   1560 N N    . ILE   A 1 69  ? 38.084 4.952   0.734   1.00 11.57 ?  69  ILE   A N    1 
ATOM   1561 C CA   . ILE   A 1 69  ? 38.220 4.937   -0.722  1.00 11.69 ?  69  ILE   A CA   1 
ATOM   1562 C C    . ILE   A 1 69  ? 39.553 5.543   -1.151  1.00 11.75 ?  69  ILE   A C    1 
ATOM   1563 O O    . ILE   A 1 69  ? 40.199 5.057   -2.086  1.00 12.23 ?  69  ILE   A O    1 
ATOM   1564 C CB   . ILE   A 1 69  ? 37.025 5.650   -1.385  1.00 12.83 ?  69  ILE   A CB   1 
ATOM   1565 C CG1  . ILE   A 1 69  ? 35.709 4.919   -1.106  1.00 13.16 ?  69  ILE   A CG1  1 
ATOM   1566 C CG2  . ILE   A 1 69  ? 37.266 5.845   -2.890  1.00 14.44 ?  69  ILE   A CG2  1 
ATOM   1567 C CD1  . ILE   A 1 69  ? 35.555 3.613   -1.852  1.00 14.18 ?  69  ILE   A CD1  1 
ATOM   1568 H H    . ILE   A 1 69  ? 37.479 5.487   1.029   1.00 13.91 ?  69  ILE   A H    1 
ATOM   1569 H HA   . ILE   A 1 69  ? 38.214 4.016   -1.019  1.00 14.04 ?  69  ILE   A HA   1 
ATOM   1570 H HB   . ILE   A 1 69  ? 36.955 6.530   -0.989  1.00 15.41 ?  69  ILE   A HB   1 
ATOM   1571 H HG12 . ILE   A 1 69  ? 35.660 4.725   -0.156  1.00 15.81 ?  69  ILE   A HG12 1 
ATOM   1572 H HG13 . ILE   A 1 69  ? 34.975 5.495   -1.361  1.00 15.81 ?  69  ILE   A HG13 1 
ATOM   1573 H HG21 . ILE   A 1 69  ? 36.422 6.059   -3.320  1.00 17.35 ?  69  ILE   A HG21 1 
ATOM   1574 H HG22 . ILE   A 1 69  ? 37.890 6.584   -3.019  1.00 17.35 ?  69  ILE   A HG22 1 
ATOM   1575 H HG23 . ILE   A 1 69  ? 37.633 5.034   -3.265  1.00 17.35 ?  69  ILE   A HG23 1 
ATOM   1576 H HD11 . ILE   A 1 69  ? 34.737 3.184   -1.561  1.00 17.04 ?  69  ILE   A HD11 1 
ATOM   1577 H HD12 . ILE   A 1 69  ? 35.513 3.796   -2.803  1.00 17.04 ?  69  ILE   A HD12 1 
ATOM   1578 H HD13 . ILE   A 1 69  ? 36.315 3.044   -1.656  1.00 17.04 ?  69  ILE   A HD13 1 
ATOM   1579 N N    . ALA   A 1 70  ? 39.973 6.625   -0.497  1.00 12.18 ?  70  ALA   A N    1 
ATOM   1580 C CA   . ALA   A 1 70  ? 41.251 7.235   -0.849  1.00 13.08 ?  70  ALA   A CA   1 
ATOM   1581 C C    . ALA   A 1 70  ? 42.400 6.251   -0.678  1.00 13.24 ?  70  ALA   A C    1 
ATOM   1582 O O    . ALA   A 1 70  ? 43.367 6.284   -1.444  1.00 15.28 ?  70  ALA   A O    1 
ATOM   1583 C CB   . ALA   A 1 70  ? 41.486 8.495   -0.012  1.00 13.63 ?  70  ALA   A CB   1 
ATOM   1584 H H    . ALA   A 1 70  ? 39.546 7.015   0.137   1.00 14.64 ?  70  ALA   A H    1 
ATOM   1585 H HA   . ALA   A 1 70  ? 41.223 7.505   -1.780  1.00 15.71 ?  70  ALA   A HA   1 
ATOM   1586 H HB1  . ALA   A 1 70  ? 42.344 8.884   -0.263  1.00 16.37 ?  70  ALA   A HB1  1 
ATOM   1587 H HB2  . ALA   A 1 70  ? 40.777 9.131   -0.183  1.00 16.37 ?  70  ALA   A HB2  1 
ATOM   1588 H HB3  . ALA   A 1 70  ? 41.501 8.254   0.927   1.00 16.37 ?  70  ALA   A HB3  1 
ATOM   1589 N N    . THR   A 1 71  ? 42.300 5.356   0.302   1.00 12.93 ?  71  THR   A N    1 
ATOM   1590 C CA   . THR   A 1 71  ? 43.351 4.376   0.552   1.00 14.31 ?  71  THR   A CA   1 
ATOM   1591 C C    . THR   A 1 71  ? 43.229 3.151   -0.345  1.00 14.27 ?  71  THR   A C    1 
ATOM   1592 O O    . THR   A 1 71  ? 44.240 2.638   -0.842  1.00 16.35 ?  71  THR   A O    1 
ATOM   1593 C CB   . THR   A 1 71  ? 43.280 3.927   2.007   1.00 16.26 ?  71  THR   A CB   1 
ATOM   1594 O OG1  . THR   A 1 71  ? 43.527 5.049   2.858   1.00 17.55 ?  71  THR   A OG1  1 
ATOM   1595 C CG2  . THR   A 1 71  ? 44.289 2.812   2.294   1.00 17.59 ?  71  THR   A CG2  1 
ATOM   1596 H H    . THR   A 1 71  ? 41.628 5.289   0.830   1.00 15.54 ?  71  THR   A H    1 
ATOM   1597 H HA   . THR   A 1 71  ? 44.215 4.779   0.391   1.00 17.20 ?  71  THR   A HA   1 
ATOM   1598 H HB   . THR   A 1 71  ? 42.393 3.573   2.185   1.00 19.53 ?  71  THR   A HB   1 
ATOM   1599 H HG1  . THR   A 1 71  ? 43.489 4.803   3.660   1.00 21.08 ?  71  THR   A HG1  1 
ATOM   1600 H HG21 . THR   A 1 71  ? 44.422 2.726   3.252   1.00 21.13 ?  71  THR   A HG21 1 
ATOM   1601 H HG22 . THR   A 1 71  ? 43.970 1.964   1.946   1.00 21.13 ?  71  THR   A HG22 1 
ATOM   1602 H HG23 . THR   A 1 71  ? 45.143 3.020   1.879   1.00 21.13 ?  71  THR   A HG23 1 
ATOM   1603 N N    . ASN   A 1 72  ? 42.005 2.647   -0.537  1.00 13.62 ?  72  ASN   A N    1 
ATOM   1604 C CA   . ASN   A 1 72  ? 41.786 1.321   -1.096  1.00 13.68 ?  72  ASN   A CA   1 
ATOM   1605 C C    . ASN   A 1 72  ? 41.171 1.307   -2.484  1.00 13.98 ?  72  ASN   A C    1 
ATOM   1606 O O    . ASN   A 1 72  ? 41.181 0.249   -3.129  1.00 15.30 ?  72  ASN   A O    1 
ATOM   1607 C CB   . ASN   A 1 72  ? 40.896 0.503   -0.154  1.00 14.33 ?  72  ASN   A CB   1 
ATOM   1608 C CG   . ASN   A 1 72  ? 41.511 0.352   1.213   1.00 15.42 ?  72  ASN   A CG   1 
ATOM   1609 O OD1  . ASN   A 1 72  ? 41.059 0.950   2.184   1.00 17.28 ?  72  ASN   A OD1  1 
ATOM   1610 N ND2  . ASN   A 1 72  ? 42.565 -0.430  1.291   1.00 15.93 ?  72  ASN   A ND2  1 
ATOM   1611 H H    . ASN   A 1 72  ? 41.275 3.068   -0.350  1.00 16.37 ?  72  ASN   A H    1 
ATOM   1612 H HA   . ASN   A 1 72  ? 42.637 0.872   -1.159  1.00 16.44 ?  72  ASN   A HA   1 
ATOM   1613 H HB2  . ASN   A 1 72  ? 40.041 0.947   -0.054  1.00 17.22 ?  72  ASN   A HB2  1 
ATOM   1614 H HB3  . ASN   A 1 72  ? 40.772 -0.384  -0.527  1.00 17.22 ?  72  ASN   A HB3  1 
ATOM   1615 H HD21 . ASN   A 1 72  ? 42.960 -0.544  2.048   1.00 19.14 ?  72  ASN   A HD21 1 
ATOM   1616 H HD22 . ASN   A 1 72  ? 42.865 -0.822  0.587   1.00 19.14 ?  72  ASN   A HD22 1 
ATOM   1617 N N    . GLY   A 1 73  ? 40.618 2.420   -2.947  1.00 13.49 ?  73  GLY   A N    1 
ATOM   1618 C CA   . GLY   A 1 73  ? 39.891 2.425   -4.190  1.00 13.23 ?  73  GLY   A CA   1 
ATOM   1619 C C    . GLY   A 1 73  ? 38.495 1.857   -4.020  1.00 12.64 ?  73  GLY   A C    1 
ATOM   1620 O O    . GLY   A 1 73  ? 38.107 1.408   -2.936  1.00 13.26 ?  73  GLY   A O    1 
ATOM   1621 H H    . GLY   A 1 73  ? 40.652 3.194   -2.559  1.00 16.21 ?  73  GLY   A H    1 
ATOM   1622 H HA2  . GLY   A 1 73  ? 39.817 3.337   -4.521  1.00 15.90 ?  73  GLY   A HA2  1 
ATOM   1623 H HA3  . GLY   A 1 73  ? 40.365 1.896   -4.850  1.00 15.90 ?  73  GLY   A HA3  1 
ATOM   1624 N N    . PRO   A 1 74  ? 37.717 1.875   -5.099  1.00 13.09 ?  74  PRO   A N    1 
ATOM   1625 C CA   . PRO   A 1 74  ? 36.319 1.445   -5.013  1.00 13.26 ?  74  PRO   A CA   1 
ATOM   1626 C C    . PRO   A 1 74  ? 36.173 -0.036  -4.701  1.00 12.67 ?  74  PRO   A C    1 
ATOM   1627 O O    . PRO   A 1 74  ? 37.040 -0.863  -4.992  1.00 13.52 ?  74  PRO   A O    1 
ATOM   1628 C CB   . PRO   A 1 74  ? 35.765 1.755   -6.411  1.00 15.02 ?  74  PRO   A CB   1 
ATOM   1629 C CG   . PRO   A 1 74  ? 36.710 2.746   -7.004  1.00 17.40 ?  74  PRO   A CG   1 
ATOM   1630 C CD   . PRO   A 1 74  ? 38.050 2.403   -6.432  1.00 14.97 ?  74  PRO   A CD   1 
ATOM   1631 H HA   . PRO   A 1 74  ? 35.838 1.969   -4.350  1.00 15.94 ?  74  PRO   A HA   1 
ATOM   1632 H HB2  . PRO   A 1 74  ? 35.741 0.943   -6.939  1.00 18.05 ?  74  PRO   A HB2  1 
ATOM   1633 H HB3  . PRO   A 1 74  ? 34.874 2.138   -6.332  1.00 18.05 ?  74  PRO   A HB3  1 
ATOM   1634 H HG2  . PRO   A 1 74  ? 36.716 2.655   -7.969  1.00 20.91 ?  74  PRO   A HG2  1 
ATOM   1635 H HG3  . PRO   A 1 74  ? 36.448 3.643   -6.745  1.00 20.91 ?  74  PRO   A HG3  1 
ATOM   1636 H HD2  . PRO   A 1 74  ? 38.488 1.721   -6.969  1.00 17.98 ?  74  PRO   A HD2  1 
ATOM   1637 H HD3  . PRO   A 1 74  ? 38.598 3.203   -6.362  1.00 17.98 ?  74  PRO   A HD3  1 
ATOM   1638 N N    . LEU   A 1 75  ? 35.028 -0.361  -4.110  1.00 11.77 ?  75  LEU   A N    1 
ATOM   1639 C CA   . LEU   A 1 75  ? 34.617 -1.747  -3.967  1.00 11.44 ?  75  LEU   A CA   1 
ATOM   1640 C C    . LEU   A 1 75  ? 34.235 -2.326  -5.328  1.00 12.09 ?  75  LEU   A C    1 
ATOM   1641 O O    . LEU   A 1 75  ? 34.111 -1.613  -6.329  1.00 13.32 ?  75  LEU   A O    1 
ATOM   1642 C CB   . LEU   A 1 75  ? 33.429 -1.861  -3.015  1.00 11.74 ?  75  LEU   A CB   1 
ATOM   1643 C CG   . LEU   A 1 75  ? 33.646 -1.466  -1.557  1.00 13.40 ?  75  LEU   A CG   1 
ATOM   1644 C CD1  . LEU   A 1 75  ? 32.366 -1.661  -0.755  1.00 15.42 ?  75  LEU   A CD1  1 
ATOM   1645 C CD2  . LEU   A 1 75  ? 34.788 -2.206  -0.916  1.00 16.73 ?  75  LEU   A CD2  1 
ATOM   1646 H H    . LEU   A 1 75  ? 34.472 0.208   -3.783  1.00 14.15 ?  75  LEU   A H    1 
ATOM   1647 H HA   . LEU   A 1 75  ? 35.351 -2.265  -3.610  1.00 13.75 ?  75  LEU   A HA   1 
ATOM   1648 H HB2  . LEU   A 1 75  ? 32.713 -1.304  -3.356  1.00 14.11 ?  75  LEU   A HB2  1 
ATOM   1649 H HB3  . LEU   A 1 75  ? 33.135 -2.789  -3.015  1.00 14.11 ?  75  LEU   A HB3  1 
ATOM   1650 H HG   . LEU   A 1 75  ? 33.870 -0.521  -1.530  1.00 16.10 ?  75  LEU   A HG   1 
ATOM   1651 H HD11 . LEU   A 1 75  ? 32.530 -1.397  0.165   1.00 18.52 ?  75  LEU   A HD11 1 
ATOM   1652 H HD12 . LEU   A 1 75  ? 31.671 -1.104  -1.139  1.00 18.52 ?  75  LEU   A HD12 1 
ATOM   1653 H HD13 . LEU   A 1 75  ? 32.110 -2.592  -0.794  1.00 18.52 ?  75  LEU   A HD13 1 
ATOM   1654 H HD21 . LEU   A 1 75  ? 34.833 -1.969  0.023   1.00 20.10 ?  75  LEU   A HD21 1 
ATOM   1655 H HD22 . LEU   A 1 75  ? 34.641 -3.159  -1.012  1.00 20.10 ?  75  LEU   A HD22 1 
ATOM   1656 H HD23 . LEU   A 1 75  ? 35.619 -1.956  -1.358  1.00 20.10 ?  75  LEU   A HD23 1 
ATOM   1657 N N    . LYS   A 1 76  ? 34.058 -3.647  -5.348  1.00 12.58 ?  76  LYS   A N    1 
ATOM   1658 C CA   . LYS   A 1 76  ? 33.454 -4.361  -6.468  1.00 13.08 ?  76  LYS   A CA   1 
ATOM   1659 C C    . LYS   A 1 76  ? 31.941 -4.444  -6.269  1.00 11.70 ?  76  LYS   A C    1 
ATOM   1660 O O    . LYS   A 1 76  ? 31.463 -4.566  -5.143  1.00 11.81 ?  76  LYS   A O    1 
ATOM   1661 C CB   . LYS   A 1 76  ? 33.994 -5.800  -6.525  1.00 14.84 ?  76  LYS   A CB   1 
ATOM   1662 C CG   . LYS   A 1 76  ? 35.502 -5.915  -6.737  1.00 16.07 ?  76  LYS   A CG   1 
ATOM   1663 C CD   . LYS   A 1 76  ? 36.027 -7.312  -6.488  1.00 17.44 ?  76  LYS   A CD   1 
ATOM   1664 C CE   . LYS   A 1 76  ? 37.519 -7.376  -6.732  1.00 19.85 ?  76  LYS   A CE   1 
ATOM   1665 N NZ   . LYS   A 1 76  ? 38.050 -8.736  -6.509  1.00 20.52 ?  76  LYS   A NZ   1 
ATOM   1666 H H    . LYS   A 1 76  ? 34.287 -4.167  -4.702  1.00 15.11 ?  76  LYS   A H    1 
ATOM   1667 H HA   . LYS   A 1 76  ? 33.649 -3.909  -7.306  1.00 15.71 ?  76  LYS   A HA   1 
ATOM   1668 H HB2  . LYS   A 1 76  ? 33.780 -6.238  -5.688  1.00 17.83 ?  76  LYS   A HB2  1 
ATOM   1669 H HB3  . LYS   A 1 76  ? 33.558 -6.261  -7.257  1.00 17.83 ?  76  LYS   A HB3  1 
ATOM   1670 H HG2  . LYS   A 1 76  ? 35.711 -5.674  -7.654  1.00 19.30 ?  76  LYS   A HG2  1 
ATOM   1671 H HG3  . LYS   A 1 76  ? 35.954 -5.311  -6.126  1.00 19.30 ?  76  LYS   A HG3  1 
ATOM   1672 H HD2  . LYS   A 1 76  ? 35.856 -7.563  -5.565  1.00 20.94 ?  76  LYS   A HD2  1 
ATOM   1673 H HD3  . LYS   A 1 76  ? 35.592 -7.935  -7.092  1.00 20.94 ?  76  LYS   A HD3  1 
ATOM   1674 H HE2  . LYS   A 1 76  ? 37.704 -7.122  -7.649  1.00 23.84 ?  76  LYS   A HE2  1 
ATOM   1675 H HE3  . LYS   A 1 76  ? 37.968 -6.771  -6.119  1.00 23.84 ?  76  LYS   A HE3  1 
ATOM   1676 H HZ1  . LYS   A 1 76  ? 38.927 -8.754  -6.659  1.00 24.64 ?  76  LYS   A HZ1  1 
ATOM   1677 H HZ2  . LYS   A 1 76  ? 37.895 -8.995  -5.671  1.00 24.64 ?  76  LYS   A HZ2  1 
ATOM   1678 H HZ3  . LYS   A 1 76  ? 37.654 -9.314  -7.064  1.00 24.64 ?  76  LYS   A HZ3  1 
ATOM   1679 N N    . VAL   A 1 77  ? 31.187 -4.411  -7.374  1.00 12.02 ?  77  VAL   A N    1 
ATOM   1680 C CA   . VAL   A 1 77  ? 29.780 -4.798  -7.289  1.00 12.13 ?  77  VAL   A CA   1 
ATOM   1681 C C    . VAL   A 1 77  ? 29.719 -6.251  -6.850  1.00 11.87 ?  77  VAL   A C    1 
ATOM   1682 O O    . VAL   A 1 77  ? 30.376 -7.121  -7.433  1.00 12.24 ?  77  VAL   A O    1 
ATOM   1683 C CB   . VAL   A 1 77  ? 29.051 -4.580  -8.624  1.00 13.18 ?  77  VAL   A CB   1 
ATOM   1684 C CG1  . VAL   A 1 77  ? 27.594 -5.021  -8.505  1.00 13.86 ?  77  VAL   A CG1  1 
ATOM   1685 C CG2  . VAL   A 1 77  ? 29.133 -3.127  -9.050  1.00 14.80 ?  77  VAL   A CG2  1 
ATOM   1686 H H    . VAL   A 1 77  ? 31.461 -4.168  -8.154  1.00 14.44 ?  77  VAL   A H    1 
ATOM   1687 H HA   . VAL   A 1 77  ? 29.345 -4.259  -6.614  1.00 14.58 ?  77  VAL   A HA   1 
ATOM   1688 H HB   . VAL   A 1 77  ? 29.477 -5.117  -9.310  1.00 15.84 ?  77  VAL   A HB   1 
ATOM   1689 H HG11 . VAL   A 1 77  ? 27.119 -4.746  -9.302  1.00 16.65 ?  77  VAL   A HG11 1 
ATOM   1690 H HG12 . VAL   A 1 77  ? 27.562 -5.986  -8.415  1.00 16.65 ?  77  VAL   A HG12 1 
ATOM   1691 H HG13 . VAL   A 1 77  ? 27.203 -4.601  -7.724  1.00 16.65 ?  77  VAL   A HG13 1 
ATOM   1692 H HG21 . VAL   A 1 77  ? 28.621 -3.011  -9.865  1.00 17.79 ?  77  VAL   A HG21 1 
ATOM   1693 H HG22 . VAL   A 1 77  ? 28.762 -2.572  -8.345  1.00 17.79 ?  77  VAL   A HG22 1 
ATOM   1694 H HG23 . VAL   A 1 77  ? 30.060 -2.893  -9.203  1.00 17.79 ?  77  VAL   A HG23 1 
ATOM   1695 N N    . GLY   A 1 78  ? 28.939 -6.521  -5.805  1.00 11.55 ?  78  GLY   A N    1 
ATOM   1696 C CA   . GLY   A 1 78  ? 28.923 -7.810  -5.151  1.00 11.61 ?  78  GLY   A CA   1 
ATOM   1697 C C    . GLY   A 1 78  ? 29.834 -7.902  -3.947  1.00 11.17 ?  78  GLY   A C    1 
ATOM   1698 O O    . GLY   A 1 78  ? 29.775 -8.906  -3.222  1.00 12.14 ?  78  GLY   A O    1 
ATOM   1699 H H    . GLY   A 1 78  ? 28.396 -5.948  -5.457  1.00 13.88 ?  78  GLY   A H    1 
ATOM   1700 H HA2  . GLY   A 1 78  ? 28.021 -8.005  -4.865  1.00 13.95 ?  78  GLY   A HA2  1 
ATOM   1701 H HA3  . GLY   A 1 78  ? 29.195 -8.488  -5.789  1.00 13.95 ?  78  GLY   A HA3  1 
ATOM   1702 N N    . GLY   A 1 79  ? 30.684 -6.895  -3.720  1.00 11.24 ?  79  GLY   A N    1 
ATOM   1703 C CA   . GLY   A 1 79  ? 31.647 -6.915  -2.642  1.00 11.66 ?  79  GLY   A CA   1 
ATOM   1704 C C    . GLY   A 1 79  ? 31.197 -6.120  -1.431  1.00 11.06 ?  79  GLY   A C    1 
ATOM   1705 O O    . GLY   A 1 79  ? 30.077 -5.609  -1.359  1.00 11.51 ?  79  GLY   A O    1 
ATOM   1706 H H    . GLY   A 1 79  ? 30.722 -6.178  -4.195  1.00 13.51 ?  79  GLY   A H    1 
ATOM   1707 H HA2  . GLY   A 1 79  ? 31.803 -7.839  -2.371  1.00 14.02 ?  79  GLY   A HA2  1 
ATOM   1708 H HA3  . GLY   A 1 79  ? 32.488 -6.548  -2.953  1.00 14.02 ?  79  GLY   A HA3  1 
ATOM   1709 N N    . SER   A 1 80  ? 32.101 -6.023  -0.456  1.00 11.69 ?  80  SER   A N    1 
ATOM   1710 C CA   . SER   A 1 80  ? 31.779 -5.397  0.817   1.00 11.19 ?  80  SER   A CA   1 
ATOM   1711 C C    . SER   A 1 80  ? 33.052 -4.948  1.516   1.00 10.95 ?  80  SER   A C    1 
ATOM   1712 O O    . SER   A 1 80  ? 34.164 -5.377  1.186   1.00 12.39 ?  80  SER   A O    1 
ATOM   1713 C CB   . SER   A 1 80  ? 31.020 -6.361  1.736   1.00 12.29 ?  80  SER   A CB   1 
ATOM   1714 O OG   . SER   A 1 80  ? 31.853 -7.410  2.208   1.00 13.95 ?  80  SER   A OG   1 
ATOM   1715 H H    . SER   A 1 80  ? 32.913 -6.303  -0.515  1.00 14.05 ?  80  SER   A H    1 
ATOM   1716 H HA   . SER   A 1 80  ? 31.226 -4.615  0.641   1.00 13.45 ?  80  SER   A HA   1 
ATOM   1717 H HB2  . SER   A 1 80  ? 30.681 -5.858  2.492   1.00 14.77 ?  80  SER   A HB2  1 
ATOM   1718 H HB3  . SER   A 1 80  ? 30.282 -6.742  1.236   1.00 14.77 ?  80  SER   A HB3  1 
ATOM   1719 H HG   . SER   A 1 80  ? 32.156 -7.842  1.554   1.00 16.76 ?  80  SER   A HG   1 
ATOM   1720 N N    . CYS   A 1 81  ? 32.862 -4.101  2.525   1.00 10.75 ?  81  CYS   A N    1 
ATOM   1721 C CA   . CYS   A 1 81  ? 33.912 -3.814  3.490   1.00 11.02 ?  81  CYS   A CA   1 
ATOM   1722 C C    . CYS   A 1 81  ? 33.266 -3.580  4.848   1.00 11.05 ?  81  CYS   A C    1 
ATOM   1723 O O    . CYS   A 1 81  ? 32.102 -3.180  4.936   1.00 12.33 ?  81  CYS   A O    1 
ATOM   1724 C CB   . CYS   A 1 81  ? 34.785 -2.621  3.075   1.00 11.93 ?  81  CYS   A CB   1 
ATOM   1725 S SG   . CYS   A 1 81  ? 33.888 -1.050  3.083   1.00 11.84 ?  81  CYS   A SG   1 
ATOM   1726 H H    . CYS   A 1 81  ? 32.122 -3.685  2.681   1.00 12.93 ?  81  CYS   A H    1 
ATOM   1727 H HA   . CYS   A 1 81  ? 34.489 -4.589  3.564   1.00 13.24 ?  81  CYS   A HA   1 
ATOM   1728 H HB2  . CYS   A 1 81  ? 35.532 -2.548  3.696   1.00 14.33 ?  81  CYS   A HB2  1 
ATOM   1729 H HB3  . CYS   A 1 81  ? 35.124 -2.777  2.177   1.00 14.33 ?  81  CYS   A HB3  1 
ATOM   1730 H HG   . CYS   A 1 81  ? 34.634 -0.169  2.747   1.00 14.23 ?  81  CYS   A HG   1 
ATOM   1731 N N    . VAL   A 1 82  ? 34.035 -3.838  5.904   1.00 11.27 ?  82  VAL   A N    1 
ATOM   1732 C CA   . VAL   A 1 82  ? 33.606 -3.594  7.274   1.00 11.81 ?  82  VAL   A CA   1 
ATOM   1733 C C    . VAL   A 1 82  ? 34.204 -2.280  7.745   1.00 11.89 ?  82  VAL   A C    1 
ATOM   1734 O O    . VAL   A 1 82  ? 35.429 -2.107  7.731   1.00 12.71 ?  82  VAL   A O    1 
ATOM   1735 C CB   . VAL   A 1 82  ? 34.034 -4.733  8.210   1.00 13.19 ?  82  VAL   A CB   1 
ATOM   1736 C CG1  . VAL   A 1 82  ? 33.579 -4.445  9.632   1.00 14.63 ?  82  VAL   A CG1  1 
ATOM   1737 C CG2  . VAL   A 1 82  ? 33.479 -6.057  7.726   1.00 14.43 ?  82  VAL   A CG2  1 
ATOM   1738 H H    . VAL   A 1 82  ? 34.834 -4.173  5.848   1.00 13.55 ?  82  VAL   A H    1 
ATOM   1739 H HA   . VAL   A 1 82  ? 32.640 -3.518  7.297   1.00 14.19 ?  82  VAL   A HA   1 
ATOM   1740 H HB   . VAL   A 1 82  ? 35.000 -4.790  8.213   1.00 15.85 ?  82  VAL   A HB   1 
ATOM   1741 H HG11 . VAL   A 1 82  ? 33.675 -5.252  10.162  1.00 17.57 ?  82  VAL   A HG11 1 
ATOM   1742 H HG12 . VAL   A 1 82  ? 34.127 -3.738  10.009  1.00 17.57 ?  82  VAL   A HG12 1 
ATOM   1743 H HG13 . VAL   A 1 82  ? 32.648 -4.170  9.619   1.00 17.57 ?  82  VAL   A HG13 1 
ATOM   1744 H HG21 . VAL   A 1 82  ? 33.714 -6.748  8.364   1.00 17.33 ?  82  VAL   A HG21 1 
ATOM   1745 H HG22 . VAL   A 1 82  ? 32.513 -5.987  7.654   1.00 17.33 ?  82  VAL   A HG22 1 
ATOM   1746 H HG23 . VAL   A 1 82  ? 33.861 -6.261  6.859   1.00 17.33 ?  82  VAL   A HG23 1 
ATOM   1747 N N    . LEU   A 1 83  ? 33.348 -1.358  8.166   1.00 11.35 ?  83  LEU   A N    1 
ATOM   1748 C CA   . LEU   A 1 83  ? 33.771 -0.094  8.746   1.00 11.51 ?  83  LEU   A CA   1 
ATOM   1749 C C    . LEU   A 1 83  ? 33.053 0.084   10.080  1.00 11.41 ?  83  LEU   A C    1 
ATOM   1750 O O    . LEU   A 1 83  ? 32.328 -0.805  10.544  1.00 12.09 ?  83  LEU   A O    1 
ATOM   1751 C CB   . LEU   A 1 83  ? 33.520 1.064   7.767   1.00 11.90 ?  83  LEU   A CB   1 
ATOM   1752 C CG   . LEU   A 1 83  ? 34.426 1.067   6.530   1.00 12.37 ?  83  LEU   A CG   1 
ATOM   1753 C CD1  . LEU   A 1 83  ? 33.986 2.114   5.529   1.00 13.09 ?  83  LEU   A CD1  1 
ATOM   1754 C CD2  . LEU   A 1 83  ? 35.902 1.289   6.908   1.00 13.05 ?  83  LEU   A CD2  1 
ATOM   1755 H H    . LEU   A 1 83  ? 32.492 -1.444  8.124   1.00 13.65 ?  83  LEU   A H    1 
ATOM   1756 H HA   . LEU   A 1 83  ? 34.720 -0.127  8.923   1.00 13.83 ?  83  LEU   A HA   1 
ATOM   1757 H HB2  . LEU   A 1 83  ? 32.607 1.018   7.447   1.00 14.31 ?  83  LEU   A HB2  1 
ATOM   1758 H HB3  . LEU   A 1 83  ? 33.662 1.904   8.227   1.00 14.31 ?  83  LEU   A HB3  1 
ATOM   1759 H HG   . LEU   A 1 83  ? 34.369 0.206   6.093   1.00 14.86 ?  83  LEU   A HG   1 
ATOM   1760 H HD11 . LEU   A 1 83  ? 34.581 2.088   4.759   1.00 15.72 ?  83  LEU   A HD11 1 
ATOM   1761 H HD12 . LEU   A 1 83  ? 33.079 1.921   5.251   1.00 15.72 ?  83  LEU   A HD12 1 
ATOM   1762 H HD13 . LEU   A 1 83  ? 34.029 2.989   5.945   1.00 15.72 ?  83  LEU   A HD13 1 
ATOM   1763 H HD21 . LEU   A 1 83  ? 36.425 1.428   6.098   1.00 15.68 ?  83  LEU   A HD21 1 
ATOM   1764 H HD22 . LEU   A 1 83  ? 35.972 2.073   7.478   1.00 15.68 ?  83  LEU   A HD22 1 
ATOM   1765 H HD23 . LEU   A 1 83  ? 36.232 0.509   7.379   1.00 15.68 ?  83  LEU   A HD23 1 
ATOM   1766 N N    . SER   A 1 84  ? 33.266 1.237   10.709  1.00 12.06 ?  84  SER   A N    1 
ATOM   1767 C CA   . SER   A 1 84  ? 32.621 1.499   11.987  1.00 12.27 ?  84  SER   A CA   1 
ATOM   1768 C C    . SER   A 1 84  ? 31.101 1.577   11.840  1.00 12.16 ?  84  SER   A C    1 
ATOM   1769 O O    . SER   A 1 84  ? 30.571 2.033   10.829  1.00 12.10 ?  84  SER   A O    1 
ATOM   1770 C CB   . SER   A 1 84  ? 33.113 2.822   12.558  1.00 13.11 ?  84  SER   A CB   1 
ATOM   1771 O OG   . SER   A 1 84  ? 32.486 3.090   13.796  1.00 14.23 ?  84  SER   A OG   1 
ATOM   1772 H H    . SER   A 1 84  ? 33.763 1.880   10.410  1.00 14.49 ?  84  SER   A H    1 
ATOM   1773 H HA   . SER   A 1 84  ? 32.842 0.788   12.603  1.00 14.74 ?  84  SER   A HA   1 
ATOM   1774 H HB2  . SER   A 1 84  ? 34.073 2.776   12.682  1.00 15.75 ?  84  SER   A HB2  1 
ATOM   1775 H HB3  . SER   A 1 84  ? 32.894 3.536   11.936  1.00 15.75 ?  84  SER   A HB3  1 
ATOM   1776 H HG   . SER   A 1 84  ? 32.770 3.817   14.111  1.00 17.09 ?  84  SER   A HG   1 
ATOM   1777 N N    . GLY   A 1 85  ? 30.396 1.166   12.890  1.00 13.02 ?  85  GLY   A N    1 
ATOM   1778 C CA   . GLY   A 1 85  ? 28.971 1.390   12.992  1.00 13.35 ?  85  GLY   A CA   1 
ATOM   1779 C C    . GLY   A 1 85  ? 28.602 2.707   13.635  1.00 13.10 ?  85  GLY   A C    1 
ATOM   1780 O O    . GLY   A 1 85  ? 27.410 3.020   13.741  1.00 13.97 ?  85  GLY   A O    1 
ATOM   1781 H H    . GLY   A 1 85  ? 30.731 0.745   13.560  1.00 15.64 ?  85  GLY   A H    1 
ATOM   1782 H HA2  . GLY   A 1 85  ? 28.582 1.365   12.103  1.00 16.04 ?  85  GLY   A HA2  1 
ATOM   1783 H HA3  . GLY   A 1 85  ? 28.574 0.678   13.514  1.00 16.04 ?  85  GLY   A HA3  1 
ATOM   1784 N N    . HIS   A 1 86  ? 29.589 3.484   14.073  1.00 12.70 ?  86  HIS   A N    1 
ATOM   1785 C CA   . HIS   A 1 86  ? 29.367 4.824   14.633  1.00 13.53 ?  86  HIS   A CA   1 
ATOM   1786 C C    . HIS   A 1 86  ? 28.379 4.704   15.787  1.00 14.48 ?  86  HIS   A C    1 
ATOM   1787 O O    . HIS   A 1 86  ? 28.556 3.822   16.643  1.00 15.37 ?  86  HIS   A O    1 
ATOM   1788 C CB   . HIS   A 1 86  ? 28.999 5.810   13.529  1.00 13.49 ?  86  HIS   A CB   1 
ATOM   1789 C CG   . HIS   A 1 86  ? 30.055 5.905   12.485  1.00 13.51 ?  86  HIS   A CG   1 
ATOM   1790 N ND1  . HIS   A 1 86  ? 31.151 6.731   12.613  1.00 14.68 ?  86  HIS   A ND1  1 
ATOM   1791 C CD2  . HIS   A 1 86  ? 30.229 5.215   11.336  1.00 13.10 ?  86  HIS   A CD2  1 
ATOM   1792 C CE1  . HIS   A 1 86  ? 31.939 6.564   11.566  1.00 14.32 ?  86  HIS   A CE1  1 
ATOM   1793 N NE2  . HIS   A 1 86  ? 31.408 5.644   10.782  1.00 13.27 ?  86  HIS   A NE2  1 
ATOM   1794 H H    . HIS   A 1 86  ? 30.413 3.257   14.065  1.00 15.26 ?  86  HIS   A H    1 
ATOM   1795 H HA   . HIS   A 1 86  ? 30.200 5.132   15.014  1.00 16.25 ?  86  HIS   A HA   1 
ATOM   1796 H HB2  . HIS   A 1 86  ? 28.174 5.528   13.104  1.00 16.21 ?  86  HIS   A HB2  1 
ATOM   1797 H HB3  . HIS   A 1 86  ? 28.881 6.698   13.916  1.00 16.21 ?  86  HIS   A HB3  1 
ATOM   1798 H HD2  . HIS   A 1 86  ? 29.658 4.557   10.993  1.00 15.74 ?  86  HIS   A HD2  1 
ATOM   1799 H HE1  . HIS   A 1 86  ? 32.731 7.017   11.398  1.00 17.20 ?  86  HIS   A HE1  1 
ATOM   1800 H HE2  . HIS   A 1 86  ? 31.737 5.362   10.034  1.00 15.95 ?  86  HIS   A HE2  1 
ATOM   1801 N N    . ASN   A 1 87  ? 27.366 5.554   15.855  1.00 15.44 ?  87  ASN   A N    1 
ATOM   1802 C CA   . ASN   A 1 87  ? 26.385 5.543   16.924  1.00 16.54 ?  87  ASN   A CA   1 
ATOM   1803 C C    . ASN   A 1 87  ? 25.260 4.550   16.685  1.00 17.70 ?  87  ASN   A C    1 
ATOM   1804 O O    . ASN   A 1 87  ? 24.332 4.493   17.496  1.00 19.66 ?  87  ASN   A O    1 
ATOM   1805 C CB   . ASN   A 1 87  ? 25.788 6.947   17.084  1.00 17.40 ?  87  ASN   A CB   1 
ATOM   1806 C CG   . ASN   A 1 87  ? 25.279 7.523   15.768  1.00 18.13 ?  87  ASN   A CG   1 
ATOM   1807 O OD1  . ASN   A 1 87  ? 25.929 7.413   14.730  1.00 18.62 ?  87  ASN   A OD1  1 
ATOM   1808 N ND2  . ASN   A 1 87  ? 24.116 8.146   15.812  1.00 18.99 ?  87  ASN   A ND2  1 
ATOM   1809 H H    . ASN   A 1 87  ? 27.222 6.169   15.275  1.00 18.54 ?  87  ASN   A H    1 
ATOM   1810 H HA   . ASN   A 1 87  ? 26.814 5.304   17.761  1.00 19.87 ?  87  ASN   A HA   1 
ATOM   1811 H HB2  . ASN   A 1 87  ? 25.043 6.906   17.709  1.00 20.91 ?  87  ASN   A HB2  1 
ATOM   1812 H HB3  . ASN   A 1 87  ? 26.473 7.540   17.432  1.00 20.91 ?  87  ASN   A HB3  1 
ATOM   1813 H HD21 . ASN   A 1 87  ? 23.788 8.486   15.096  1.00 22.81 ?  87  ASN   A HD21 1 
ATOM   1814 H HD22 . ASN   A 1 87  ? 23.688 8.210   16.557  1.00 22.81 ?  87  ASN   A HD22 1 
ATOM   1815 N N    . LEU   A 1 88  ? 25.314 3.772   15.609  1.00 16.48 ?  88  LEU   A N    1 
ATOM   1816 C CA   . LEU   A 1 88  ? 24.203 2.910   15.220  1.00 16.08 ?  88  LEU   A CA   1 
ATOM   1817 C C    . LEU   A 1 88  ? 24.422 1.433   15.520  1.00 15.76 ?  88  LEU   A C    1 
ATOM   1818 O O    . LEU   A 1 88  ? 23.441 0.701   15.692  1.00 16.78 ?  88  LEU   A O    1 
ATOM   1819 C CB   . LEU   A 1 88  ? 23.937 3.060   13.722  1.00 16.42 ?  88  LEU   A CB   1 
ATOM   1820 C CG   . LEU   A 1 88  ? 23.658 4.480   13.230  1.00 18.21 ?  88  LEU   A CG   1 
ATOM   1821 C CD1  . LEU   A 1 88  ? 23.527 4.493   11.716  1.00 18.47 ?  88  LEU   A CD1  1 
ATOM   1822 C CD2  . LEU   A 1 88  ? 22.409 5.054   13.882  1.00 19.78 ?  88  LEU   A CD2  1 
ATOM   1823 H H    . LEU   A 1 88  ? 25.988 3.731   15.081  1.00 19.80 ?  88  LEU   A H    1 
ATOM   1824 H HA   . LEU   A 1 88  ? 23.406 3.194   15.694  1.00 19.31 ?  88  LEU   A HA   1 
ATOM   1825 H HB2  . LEU   A 1 88  ? 24.707 2.736   13.237  1.00 19.72 ?  88  LEU   A HB2  1 
ATOM   1826 H HB3  . LEU   A 1 88  ? 23.160 2.524   13.496  1.00 19.72 ?  88  LEU   A HB3  1 
ATOM   1827 H HG   . LEU   A 1 88  ? 24.405 5.050   13.465  1.00 21.87 ?  88  LEU   A HG   1 
ATOM   1828 H HD11 . LEU   A 1 88  ? 23.370 5.404   11.419  1.00 22.19 ?  88  LEU   A HD11 1 
ATOM   1829 H HD12 . LEU   A 1 88  ? 24.350 4.157   11.326  1.00 22.19 ?  88  LEU   A HD12 1 
ATOM   1830 H HD13 . LEU   A 1 88  ? 22.783 3.928   11.458  1.00 22.19 ?  88  LEU   A HD13 1 
ATOM   1831 H HD21 . LEU   A 1 88  ? 22.212 5.916   13.481  1.00 23.75 ?  88  LEU   A HD21 1 
ATOM   1832 H HD22 . LEU   A 1 88  ? 21.670 4.444   13.735  1.00 23.75 ?  88  LEU   A HD22 1 
ATOM   1833 H HD23 . LEU   A 1 88  ? 22.571 5.159   14.831  1.00 23.75 ?  88  LEU   A HD23 1 
ATOM   1834 N N    . ALA   A 1 89  ? 25.672 0.983   15.561  1.00 14.96 ?  89  ALA   A N    1 
ATOM   1835 C CA   . ALA   A 1 89  ? 26.011 -0.429  15.657  1.00 14.78 ?  89  ALA   A CA   1 
ATOM   1836 C C    . ALA   A 1 89  ? 27.496 -0.501  15.971  1.00 15.04 ?  89  ALA   A C    1 
ATOM   1837 O O    . ALA   A 1 89  ? 28.212 0.493   15.860  1.00 15.70 ?  89  ALA   A O    1 
ATOM   1838 C CB   . ALA   A 1 89  ? 25.725 -1.135  14.333  1.00 14.29 ?  89  ALA   A CB   1 
ATOM   1839 H H    . ALA   A 1 89  ? 26.359 1.499   15.528  1.00 17.97 ?  89  ALA   A H    1 
ATOM   1840 H HA   . ALA   A 1 89  ? 25.503 -0.847  16.370  1.00 17.75 ?  89  ALA   A HA   1 
ATOM   1841 H HB1  . ALA   A 1 89  ? 25.966 -2.072  14.420  1.00 17.17 ?  89  ALA   A HB1  1 
ATOM   1842 H HB2  . ALA   A 1 89  ? 24.778 -1.058  14.128  1.00 17.17 ?  89  ALA   A HB2  1 
ATOM   1843 H HB3  . ALA   A 1 89  ? 26.250 -0.722  13.633  1.00 17.17 ?  89  ALA   A HB3  1 
ATOM   1844 N N    . LYS   A 1 90  ? 27.970 -1.683  16.356  1.00 15.93 ?  90  LYS   A N    1 
ATOM   1845 C CA   . LYS   A 1 90  ? 29.413 -1.836  16.510  1.00 16.54 ?  90  LYS   A CA   1 
ATOM   1846 C C    . LYS   A 1 90  ? 30.119 -1.646  15.170  1.00 15.25 ?  90  LYS   A C    1 
ATOM   1847 O O    . LYS   A 1 90  ? 31.065 -0.849  15.050  1.00 16.78 ?  90  LYS   A O    1 
ATOM   1848 C CB   . LYS   A 1 90  ? 29.746 -3.199  17.118  1.00 19.31 ?  90  LYS   A CB   1 
ATOM   1849 C CG   . LYS   A 1 90  ? 31.225 -3.353  17.450  1.00 23.79 ?  90  LYS   A CG   1 
ATOM   1850 C CD   . LYS   A 1 90  ? 31.471 -4.564  18.336  1.00 28.35 ?  90  LYS   A CD   1 
ATOM   1851 C CE   . LYS   A 1 90  ? 32.880 -4.563  18.915  1.00 31.88 ?  90  LYS   A CE   1 
ATOM   1852 N NZ   . LYS   A 1 90  ? 33.917 -4.922  17.909  1.00 34.01 ?  90  LYS   A NZ   1 
ATOM   1853 H H    . LYS   A 1 90  ? 27.492 -2.372  16.535  1.00 19.13 ?  90  LYS   A H    1 
ATOM   1854 H HA   . LYS   A 1 90  ? 29.736 -1.153  17.114  1.00 19.87 ?  90  LYS   A HA   1 
ATOM   1855 H HB2  . LYS   A 1 90  ? 29.238 -3.310  17.939  1.00 23.19 ?  90  LYS   A HB2  1 
ATOM   1856 H HB3  . LYS   A 1 90  ? 29.504 -3.895  16.486  1.00 23.19 ?  90  LYS   A HB3  1 
ATOM   1857 H HG2  . LYS   A 1 90  ? 31.728 -3.468  16.629  1.00 28.57 ?  90  LYS   A HG2  1 
ATOM   1858 H HG3  . LYS   A 1 90  ? 31.530 -2.562  17.923  1.00 28.57 ?  90  LYS   A HG3  1 
ATOM   1859 H HD2  . LYS   A 1 90  ? 30.840 -4.555  19.073  1.00 34.05 ?  90  LYS   A HD2  1 
ATOM   1860 H HD3  . LYS   A 1 90  ? 31.359 -5.373  17.810  1.00 34.05 ?  90  LYS   A HD3  1 
ATOM   1861 H HE2  . LYS   A 1 90  ? 33.084 -3.676  19.251  1.00 38.27 ?  90  LYS   A HE2  1 
ATOM   1862 H HE3  . LYS   A 1 90  ? 32.927 -5.209  19.637  1.00 38.27 ?  90  LYS   A HE3  1 
ATOM   1863 H HZ1  . LYS   A 1 90  ? 33.759 -5.737  17.587  1.00 40.83 ?  90  LYS   A HZ1  1 
ATOM   1864 H HZ2  . LYS   A 1 90  ? 33.906 -4.339  17.238  1.00 40.83 ?  90  LYS   A HZ2  1 
ATOM   1865 H HZ3  . LYS   A 1 90  ? 34.724 -4.913  18.286  1.00 40.83 ?  90  LYS   A HZ3  1 
ATOM   1866 N N    . HIS   A 1 91  ? 29.647 -2.355  14.145  1.00 13.39 ?  91  HIS   A N    1 
ATOM   1867 C CA   . HIS   A 1 91  ? 30.226 -2.337  12.816  1.00 12.98 ?  91  HIS   A CA   1 
ATOM   1868 C C    . HIS   A 1 91  ? 29.141 -2.061  11.791  1.00 11.89 ?  91  HIS   A C    1 
ATOM   1869 O O    . HIS   A 1 91  ? 27.974 -2.418  11.984  1.00 12.66 ?  91  HIS   A O    1 
ATOM   1870 C CB   . HIS   A 1 91  ? 30.821 -3.705  12.455  1.00 15.57 ?  91  HIS   A CB   1 
ATOM   1871 C CG   . HIS   A 1 91  ? 31.815 -4.218  13.446  1.00 19.86 ?  91  HIS   A CG   1 
ATOM   1872 N ND1  . HIS   A 1 91  ? 33.088 -3.705  13.557  1.00 22.01 ?  91  HIS   A ND1  1 
ATOM   1873 C CD2  . HIS   A 1 91  ? 31.727 -5.207  14.367  1.00 21.55 ?  91  HIS   A CD2  1 
ATOM   1874 C CE1  . HIS   A 1 91  ? 33.742 -4.353  14.505  1.00 22.91 ?  91  HIS   A CE1  1 
ATOM   1875 N NE2  . HIS   A 1 91  ? 32.938 -5.271  15.011  1.00 22.82 ?  91  HIS   A NE2  1 
ATOM   1876 H H    . HIS   A 1 91  ? 28.964 -2.889  14.209  1.00 16.09 ?  91  HIS   A H    1 
ATOM   1877 H HA   . HIS   A 1 91  ? 30.913 -1.662  12.754  1.00 15.59 ?  91  HIS   A HA   1 
ATOM   1878 H HB2  . HIS   A 1 91  ? 30.102 -4.356  12.397  1.00 18.71 ?  91  HIS   A HB2  1 
ATOM   1879 H HB3  . HIS   A 1 91  ? 31.267 -3.636  11.597  1.00 18.71 ?  91  HIS   A HB3  1 
ATOM   1880 H HD1  . HIS   A 1 91  ? 33.409 -3.063  13.080  1.00 26.43 ?  91  HIS   A HD1  1 
ATOM   1881 H HD2  . HIS   A 1 91  ? 30.991 -5.744  14.535  1.00 25.88 ?  91  HIS   A HD2  1 
ATOM   1882 H HE1  . HIS   A 1 91  ? 34.622 -4.186  14.769  1.00 27.51 ?  91  HIS   A HE1  1 
ATOM   1883 N N    . CYS   A 1 92  ? 29.549 -1.462  10.677  1.00 11.53 ?  92  CYS   A N    1 
ATOM   1884 C CA   . CYS   A 1 92  ? 28.717 -1.384  9.485   1.00 11.31 ?  92  CYS   A CA   1 
ATOM   1885 C C    . CYS   A 1 92  ? 29.369 -2.206  8.379   1.00 10.94 ?  92  CYS   A C    1 
ATOM   1886 O O    . CYS   A 1 92  ? 30.526 -1.957  8.014   1.00 11.62 ?  92  CYS   A O    1 
ATOM   1887 C CB   . CYS   A 1 92  ? 28.509 0.059   9.021   1.00 11.55 ?  92  CYS   A CB   1 
ATOM   1888 S SG   . CYS   A 1 92  ? 27.490 0.167   7.511   1.00 11.22 ?  92  CYS   A SG   1 
ATOM   1889 H H    . CYS   A 1 92  ? 30.320 -1.085  10.590  1.00 13.86 ?  92  CYS   A H    1 
ATOM   1890 H HA   . CYS   A 1 92  ? 27.850 -1.764  9.677   1.00 13.60 ?  92  CYS   A HA   1 
ATOM   1891 H HB2  . CYS   A 1 92  ? 28.060 0.560   9.720   1.00 13.88 ?  92  CYS   A HB2  1 
ATOM   1892 H HB3  . CYS   A 1 92  ? 29.370 0.461   8.825   1.00 13.88 ?  92  CYS   A HB3  1 
ATOM   1893 H HG   . CYS   A 1 92  ? 27.355 1.323   7.218   1.00 13.49 ?  92  CYS   A HG   1 
ATOM   1894 N N    . LEU   A 1 93  ? 28.632 -3.192  7.870   1.00 10.87 ?  93  LEU   A N    1 
ATOM   1895 C CA   . LEU   A 1 93  ? 29.032 -3.950  6.689   1.00 10.49 ?  93  LEU   A CA   1 
ATOM   1896 C C    . LEU   A 1 93  ? 28.438 -3.257  5.467   1.00 10.00 ?  93  LEU   A C    1 
ATOM   1897 O O    . LEU   A 1 93  ? 27.223 -3.309  5.241   1.00 10.19 ?  93  LEU   A O    1 
ATOM   1898 C CB   . LEU   A 1 93  ? 28.548 -5.395  6.797   1.00 11.03 ?  93  LEU   A CB   1 
ATOM   1899 C CG   . LEU   A 1 93  ? 28.946 -6.296  5.627   1.00 11.34 ?  93  LEU   A CG   1 
ATOM   1900 C CD1  . LEU   A 1 93  ? 30.451 -6.551  5.614   1.00 12.16 ?  93  LEU   A CD1  1 
ATOM   1901 C CD2  . LEU   A 1 93  ? 28.174 -7.616  5.676   1.00 12.04 ?  93  LEU   A CD2  1 
ATOM   1902 H H    . LEU   A 1 93  ? 27.878 -3.438  8.208   1.00 13.07 ?  93  LEU   A H    1 
ATOM   1903 H HA   . LEU   A 1 93  ? 29.994 -3.946  6.617   1.00 12.61 ?  93  LEU   A HA   1 
ATOM   1904 H HB2  . LEU   A 1 93  ? 28.914 -5.784  7.609   1.00 13.26 ?  93  LEU   A HB2  1 
ATOM   1905 H HB3  . LEU   A 1 93  ? 27.579 -5.397  6.847   1.00 13.26 ?  93  LEU   A HB3  1 
ATOM   1906 H HG   . LEU   A 1 93  ? 28.726 -5.857  4.799   1.00 13.63 ?  93  LEU   A HG   1 
ATOM   1907 H HD11 . LEU   A 1 93  ? 30.665 -7.168  4.897   1.00 14.61 ?  93  LEU   A HD11 1 
ATOM   1908 H HD12 . LEU   A 1 93  ? 30.917 -5.712  5.481   1.00 14.61 ?  93  LEU   A HD12 1 
ATOM   1909 H HD13 . LEU   A 1 93  ? 30.716 -6.941  6.468   1.00 14.61 ?  93  LEU   A HD13 1 
ATOM   1910 H HD21 . LEU   A 1 93  ? 28.451 -8.172  4.928   1.00 14.47 ?  93  LEU   A HD21 1 
ATOM   1911 H HD22 . LEU   A 1 93  ? 28.369 -8.070  6.511   1.00 14.47 ?  93  LEU   A HD22 1 
ATOM   1912 H HD23 . LEU   A 1 93  ? 27.227 -7.427  5.613   1.00 14.47 ?  93  LEU   A HD23 1 
ATOM   1913 N N    . HIS   A 1 94  ? 29.289 -2.567  4.708   1.00 9.86  ?  94  HIS   A N    1 
ATOM   1914 C CA   . HIS   A 1 94  ? 28.869 -1.891  3.483   1.00 9.97  ?  94  HIS   A CA   1 
ATOM   1915 C C    . HIS   A 1 94  ? 28.882 -2.922  2.369   1.00 9.99  ?  94  HIS   A C    1 
ATOM   1916 O O    . HIS   A 1 94  ? 29.947 -3.434  2.024   1.00 11.46 ?  94  HIS   A O    1 
ATOM   1917 C CB   . HIS   A 1 94  ? 29.828 -0.749  3.155   1.00 9.95  ?  94  HIS   A CB   1 
ATOM   1918 C CG   . HIS   A 1 94  ? 29.814 0.346   4.168   1.00 9.87  ?  94  HIS   A CG   1 
ATOM   1919 N ND1  . HIS   A 1 94  ? 28.933 1.408   4.115   1.00 10.17 ?  94  HIS   A ND1  1 
ATOM   1920 C CD2  . HIS   A 1 94  ? 30.550 0.514   5.288   1.00 10.53 ?  94  HIS   A CD2  1 
ATOM   1921 C CE1  . HIS   A 1 94  ? 29.148 2.189   5.157   1.00 10.34 ?  94  HIS   A CE1  1 
ATOM   1922 N NE2  . HIS   A 1 94  ? 30.122 1.670   5.884   1.00 10.80 ?  94  HIS   A NE2  1 
ATOM   1923 H H    . HIS   A 1 94  ? 30.121 -2.467  4.889   1.00 11.85 ?  94  HIS   A H    1 
ATOM   1924 H HA   . HIS   A 1 94  ? 27.964 -1.539  3.582   1.00 11.99 ?  94  HIS   A HA   1 
ATOM   1925 H HB2  . HIS   A 1 94  ? 30.722 -1.100  3.107   1.00 11.95 ?  94  HIS   A HB2  1 
ATOM   1926 H HB3  . HIS   A 1 94  ? 29.568 -0.364  2.301   1.00 11.95 ?  94  HIS   A HB3  1 
ATOM   1927 H HD2  . HIS   A 1 94  ? 31.227 -0.041  5.592   1.00 12.66 ?  94  HIS   A HD2  1 
ATOM   1928 H HE1  . HIS   A 1 94  ? 28.679 2.973   5.345   1.00 12.42 ?  94  HIS   A HE1  1 
ATOM   1929 H HE2  . HIS   A 1 94  ? 30.435 2.014   6.604   1.00 12.98 ?  94  HIS   A HE2  1 
ATOM   1930 N N    . VAL   A 1 95  ? 27.711 -3.247  1.818   1.00 9.32  ?  95  VAL   A N    1 
ATOM   1931 C CA   . VAL   A 1 95  ? 27.568 -4.285  0.799   1.00 9.82  ?  95  VAL   A CA   1 
ATOM   1932 C C    . VAL   A 1 95  ? 27.024 -3.647  -0.467  1.00 9.47  ?  95  VAL   A C    1 
ATOM   1933 O O    . VAL   A 1 95  ? 26.016 -2.929  -0.416  1.00 10.21 ?  95  VAL   A O    1 
ATOM   1934 C CB   . VAL   A 1 95  ? 26.641 -5.432  1.251   1.00 10.34 ?  95  VAL   A CB   1 
ATOM   1935 C CG1  . VAL   A 1 95  ? 26.551 -6.478  0.155   1.00 11.01 ?  95  VAL   A CG1  1 
ATOM   1936 C CG2  . VAL   A 1 95  ? 27.142 -6.042  2.543   1.00 10.54 ?  95  VAL   A CG2  1 
ATOM   1937 H H    . VAL   A 1 95  ? 26.965 -2.876  2.028   1.00 11.20 ?  95  VAL   A H    1 
ATOM   1938 H HA   . VAL   A 1 95  ? 28.436 -4.661  0.595   1.00 11.80 ?  95  VAL   A HA   1 
ATOM   1939 H HB   . VAL   A 1 95  ? 25.753 -5.085  1.405   1.00 12.42 ?  95  VAL   A HB   1 
ATOM   1940 H HG11 . VAL   A 1 95  ? 26.155 -7.291  0.524   1.00 13.23 ?  95  VAL   A HG11 1 
ATOM   1941 H HG12 . VAL   A 1 95  ? 25.995 -6.147  -0.566  1.00 13.23 ?  95  VAL   A HG12 1 
ATOM   1942 H HG13 . VAL   A 1 95  ? 27.442 -6.678  -0.176  1.00 13.23 ?  95  VAL   A HG13 1 
ATOM   1943 H HG21 . VAL   A 1 95  ? 26.582 -6.800  2.771   1.00 12.67 ?  95  VAL   A HG21 1 
ATOM   1944 H HG22 . VAL   A 1 95  ? 28.059 -6.327  2.426   1.00 12.67 ?  95  VAL   A HG22 1 
ATOM   1945 H HG23 . VAL   A 1 95  ? 27.089 -5.371  3.244   1.00 12.67 ?  95  VAL   A HG23 1 
ATOM   1946 N N    . VAL   A 1 96  ? 27.658 -3.935  -1.600  1.00 9.52  ?  96  VAL   A N    1 
ATOM   1947 C CA   . VAL   A 1 96  ? 27.250 -3.381  -2.883  1.00 10.22 ?  96  VAL   A CA   1 
ATOM   1948 C C    . VAL   A 1 96  ? 26.449 -4.429  -3.650  1.00 10.47 ?  96  VAL   A C    1 
ATOM   1949 O O    . VAL   A 1 96  ? 27.012 -5.378  -4.207  1.00 11.44 ?  96  VAL   A O    1 
ATOM   1950 C CB   . VAL   A 1 96  ? 28.444 -2.900  -3.710  1.00 10.46 ?  96  VAL   A CB   1 
ATOM   1951 C CG1  . VAL   A 1 96  ? 27.939 -2.267  -4.989  1.00 10.99 ?  96  VAL   A CG1  1 
ATOM   1952 C CG2  . VAL   A 1 96  ? 29.302 -1.930  -2.918  1.00 11.09 ?  96  VAL   A CG2  1 
ATOM   1953 H H    . VAL   A 1 96  ? 28.346 -4.453  -1.649  1.00 11.45 ?  96  VAL   A H    1 
ATOM   1954 H HA   . VAL   A 1 96  ? 26.674 -2.618  -2.727  1.00 12.28 ?  96  VAL   A HA   1 
ATOM   1955 H HB   . VAL   A 1 96  ? 28.995 -3.658  -3.947  1.00 12.58 ?  96  VAL   A HB   1 
ATOM   1956 H HG11 . VAL   A 1 96  ? 28.672 -1.777  -5.400  1.00 13.21 ?  96  VAL   A HG11 1 
ATOM   1957 H HG12 . VAL   A 1 96  ? 27.634 -2.963  -5.588  1.00 13.21 ?  96  VAL   A HG12 1 
ATOM   1958 H HG13 . VAL   A 1 96  ? 27.217 -1.659  -4.778  1.00 13.21 ?  96  VAL   A HG13 1 
ATOM   1959 H HG21 . VAL   A 1 96  ? 30.010 -1.586  -3.485  1.00 13.33 ?  96  VAL   A HG21 1 
ATOM   1960 H HG22 . VAL   A 1 96  ? 28.747 -1.191  -2.606  1.00 13.33 ?  96  VAL   A HG22 1 
ATOM   1961 H HG23 . VAL   A 1 96  ? 29.686 -2.390  -2.153  1.00 13.33 ?  96  VAL   A HG23 1 
ATOM   1962 N N    A GLY   A 1 97  ? 25.129 -4.278  -3.673  0.72 10.52 ?  97  GLY   A N    1 
ATOM   1963 N N    B GLY   A 1 97  ? 25.132 -4.245  -3.709  0.28 10.62 ?  97  GLY   A N    1 
ATOM   1964 C CA   A GLY   A 1 97  ? 24.321 -5.037  -4.592  0.72 11.21 ?  97  GLY   A CA   1 
ATOM   1965 C CA   B GLY   A 1 97  ? 24.310 -5.015  -4.607  0.28 10.94 ?  97  GLY   A CA   1 
ATOM   1966 C C    A GLY   A 1 97  ? 24.317 -4.365  -5.950  0.72 11.36 ?  97  GLY   A C    1 
ATOM   1967 C C    B GLY   A 1 97  ? 24.304 -4.395  -5.991  0.28 11.17 ?  97  GLY   A C    1 
ATOM   1968 O O    A GLY   A 1 97  ? 24.611 -3.173  -6.072  0.72 12.13 ?  97  GLY   A O    1 
ATOM   1969 O O    B GLY   A 1 97  ? 24.567 -3.201  -6.158  0.28 11.45 ?  97  GLY   A O    1 
ATOM   1970 H H    A GLY   A 1 97  ? 24.685 -3.738  -3.165  0.72 12.65 ?  97  GLY   A H    1 
ATOM   1971 H H    B GLY   A 1 97  ? 24.695 -3.674  -3.231  0.28 12.76 ?  97  GLY   A H    1 
ATOM   1972 H HA2  A GLY   A 1 97  ? 24.685 -5.931  -4.677  0.72 13.47 ?  97  GLY   A HA2  1 
ATOM   1973 H HA2  B GLY   A 1 97  ? 24.659 -5.918  -4.665  0.28 13.15 ?  97  GLY   A HA2  1 
ATOM   1974 H HA3  A GLY   A 1 97  ? 23.412 -5.096  -4.259  0.72 13.47 ?  97  GLY   A HA3  1 
ATOM   1975 H HA3  B GLY   A 1 97  ? 23.400 -5.051  -4.275  0.28 13.15 ?  97  GLY   A HA3  1 
ATOM   1976 N N    A PRO   A 1 98  ? 23.985 -5.110  -7.001  0.72 11.27 ?  98  PRO   A N    1 
ATOM   1977 N N    B PRO   A 1 98  ? 24.001 -5.192  -7.014  0.28 11.39 ?  98  PRO   A N    1 
ATOM   1978 C CA   A PRO   A 1 98  ? 23.856 -4.485  -8.322  0.72 12.39 ?  98  PRO   A CA   1 
ATOM   1979 C CA   B PRO   A 1 98  ? 23.967 -4.650  -8.378  0.28 12.09 ?  98  PRO   A CA   1 
ATOM   1980 C C    A PRO   A 1 98  ? 22.737 -3.451  -8.341  0.72 12.45 ?  98  PRO   A C    1 
ATOM   1981 C C    B PRO   A 1 98  ? 22.861 -3.620  -8.545  0.28 12.53 ?  98  PRO   A C    1 
ATOM   1982 O O    A PRO   A 1 98  ? 21.666 -3.648  -7.762  0.72 12.41 ?  98  PRO   A O    1 
ATOM   1983 O O    B PRO   A 1 98  ? 21.775 -3.741  -7.972  0.28 12.66 ?  98  PRO   A O    1 
ATOM   1984 C CB   A PRO   A 1 98  ? 23.546 -5.670  -9.244  0.72 12.74 ?  98  PRO   A CB   1 
ATOM   1985 C CB   B PRO   A 1 98  ? 23.707 -5.889  -9.243  0.28 12.01 ?  98  PRO   A CB   1 
ATOM   1986 C CG   A PRO   A 1 98  ? 22.951 -6.712  -8.339  0.72 12.97 ?  98  PRO   A CG   1 
ATOM   1987 C CG   B PRO   A 1 98  ? 23.015 -6.844  -8.325  0.28 12.05 ?  98  PRO   A CG   1 
ATOM   1988 C CD   A PRO   A 1 98  ? 23.690 -6.554  -7.036  0.72 11.89 ?  98  PRO   A CD   1 
ATOM   1989 C CD   B PRO   A 1 98  ? 23.661 -6.625  -6.984  0.28 11.51 ?  98  PRO   A CD   1 
ATOM   1990 H HA   A PRO   A 1 98  ? 24.693 -4.071  -8.585  0.72 14.89 ?  98  PRO   A HA   1 
ATOM   1991 H HA   B PRO   A 1 98  ? 24.823 -4.255  -8.614  0.28 14.52 ?  98  PRO   A HA   1 
ATOM   1992 H HB2  A PRO   A 1 98  ? 22.908 -5.398  -9.921  0.72 15.30 ?  98  PRO   A HB2  1 
ATOM   1993 H HB2  B PRO   A 1 98  ? 23.136 -5.651  -9.991  0.28 14.43 ?  98  PRO   A HB2  1 
ATOM   1994 H HB3  A PRO   A 1 98  ? 24.366 -5.992  -9.649  0.72 15.30 ?  98  PRO   A HB3  1 
ATOM   1995 H HB3  B PRO   A 1 98  ? 24.549 -6.254  -9.553  0.28 14.43 ?  98  PRO   A HB3  1 
ATOM   1996 H HG2  A PRO   A 1 98  ? 22.006 -6.540  -8.219  0.72 15.58 ?  98  PRO   A HG2  1 
ATOM   1997 H HG2  B PRO   A 1 98  ? 22.069 -6.632  -8.289  0.28 14.48 ?  98  PRO   A HG2  1 
ATOM   1998 H HG3  A PRO   A 1 98  ? 23.101 -7.592  -8.712  0.72 15.58 ?  98  PRO   A HG3  1 
ATOM   1999 H HG3  B PRO   A 1 98  ? 23.157 -7.749  -8.633  0.28 14.48 ?  98  PRO   A HG3  1 
ATOM   2000 H HD2  A PRO   A 1 98  ? 23.121 -6.808  -6.288  0.72 14.29 ?  98  PRO   A HD2  1 
ATOM   2001 H HD2  B PRO   A 1 98  ? 23.033 -6.812  -6.269  0.28 13.83 ?  98  PRO   A HD2  1 
ATOM   2002 H HD3  A PRO   A 1 98  ? 24.515 -7.067  -7.042  0.72 14.29 ?  98  PRO   A HD3  1 
ATOM   2003 H HD3  B PRO   A 1 98  ? 24.466 -7.161  -6.902  0.28 13.83 ?  98  PRO   A HD3  1 
ATOM   2004 N N    A ASN   A 1 99  ? 23.002 -2.332  -9.007  0.72 12.95 ?  99  ASN   A N    1 
ATOM   2005 N N    B ASN   A 1 99  ? 23.147 -2.600  -9.346  0.28 12.88 ?  99  ASN   A N    1 
ATOM   2006 C CA   A ASN   A 1 99  ? 22.016 -1.278  -9.223  0.72 13.96 ?  99  ASN   A CA   1 
ATOM   2007 C CA   B ASN   A 1 99  ? 22.204 -1.528  -9.628  0.28 13.86 ?  99  ASN   A CA   1 
ATOM   2008 C C    A ASN   A 1 99  ? 21.481 -1.432  -10.643 0.72 15.31 ?  99  ASN   A C    1 
ATOM   2009 C C    B ASN   A 1 99  ? 21.515 -1.817  -10.955 0.28 14.84 ?  99  ASN   A C    1 
ATOM   2010 O O    A ASN   A 1 99  ? 22.175 -1.116  -11.618 0.72 16.17 ?  99  ASN   A O    1 
ATOM   2011 O O    B ASN   A 1 99  ? 22.171 -1.867  -12.002 0.28 14.31 ?  99  ASN   A O    1 
ATOM   2012 C CB   A ASN   A 1 99  ? 22.648 0.098   -9.016  0.72 13.93 ?  99  ASN   A CB   1 
ATOM   2013 C CB   B ASN   A 1 99  ? 22.936 -0.191  -9.707  0.28 14.36 ?  99  ASN   A CB   1 
ATOM   2014 C CG   A ASN   A 1 99  ? 21.623 1.229   -9.010  0.72 14.10 ?  99  ASN   A CG   1 
ATOM   2015 C CG   B ASN   A 1 99  ? 21.994 0.984   -9.862  0.28 14.98 ?  99  ASN   A CG   1 
ATOM   2016 O OD1  A ASN   A 1 99  ? 20.610 1.172   -9.707  0.72 14.56 ?  99  ASN   A OD1  1 
ATOM   2017 O OD1  B ASN   A 1 99  ? 20.931 0.866   -10.470 0.28 14.87 ?  99  ASN   A OD1  1 
ATOM   2018 N ND2  A ASN   A 1 99  ? 21.889 2.265   -8.220  0.72 14.55 ?  99  ASN   A ND2  1 
ATOM   2019 N ND2  B ASN   A 1 99  ? 22.384 2.130   -9.310  0.28 15.79 ?  99  ASN   A ND2  1 
ATOM   2020 H H    A ASN   A 1 99  ? 23.773 -2.148  -9.340  0.72 15.56 ?  99  ASN   A H    1 
ATOM   2021 H H    B ASN   A 1 99  ? 23.905 -2.500  -9.740  0.28 15.47 ?  99  ASN   A H    1 
ATOM   2022 H HA   A ASN   A 1 99  ? 21.280 -1.380  -8.588  0.72 16.78 ?  99  ASN   A HA   1 
ATOM   2023 H HA   B ASN   A 1 99  ? 21.531 -1.483  -8.925  0.28 16.66 ?  99  ASN   A HA   1 
ATOM   2024 H HB2  A ASN   A 1 99  ? 23.113 0.112   -8.166  0.72 16.73 ?  99  ASN   A HB2  1 
ATOM   2025 H HB2  B ASN   A 1 99  ? 23.444 -0.063  -8.896  0.28 17.25 ?  99  ASN   A HB2  1 
ATOM   2026 H HB3  A ASN   A 1 99  ? 23.274 0.263   -9.739  0.72 16.73 ?  99  ASN   A HB3  1 
ATOM   2027 H HB3  B ASN   A 1 99  ? 23.526 -0.206  -10.476 0.28 17.25 ?  99  ASN   A HB3  1 
ATOM   2028 H HD21 A ASN   A 1 99  ? 21.344 2.930   -8.182  0.72 17.48 ?  99  ASN   A HD21 1 
ATOM   2029 H HD21 B ASN   A 1 99  ? 21.891 2.834   -9.369  0.28 18.97 ?  99  ASN   A HD21 1 
ATOM   2030 H HD22 A ASN   A 1 99  ? 22.605 2.270   -7.744  0.72 17.48 ?  99  ASN   A HD22 1 
ATOM   2031 H HD22 B ASN   A 1 99  ? 23.137 2.171   -8.894  0.28 18.97 ?  99  ASN   A HD22 1 
ATOM   2032 N N    A VAL   A 1 100 ? 20.247 -1.935  -10.751 0.72 16.82 ?  100 VAL   A N    1 
ATOM   2033 N N    B VAL   A 1 100 ? 20.191 -1.981  -10.907 0.28 16.77 ?  100 VAL   A N    1 
ATOM   2034 C CA   A VAL   A 1 100 ? 19.634 -2.159  -12.057 0.72 18.56 ?  100 VAL   A CA   1 
ATOM   2035 C CA   B VAL   A 1 100 ? 19.432 -2.298  -12.114 0.28 18.88 ?  100 VAL   A CA   1 
ATOM   2036 C C    A VAL   A 1 100 ? 19.491 -0.849  -12.821 0.72 19.13 ?  100 VAL   A C    1 
ATOM   2037 C C    B VAL   A 1 100 ? 19.531 -1.169  -13.127 0.28 20.66 ?  100 VAL   A C    1 
ATOM   2038 O O    A VAL   A 1 100 ? 19.552 -0.833  -14.056 0.72 20.48 ?  100 VAL   A O    1 
ATOM   2039 O O    B VAL   A 1 100 ? 19.643 -1.409  -14.336 0.28 21.21 ?  100 VAL   A O    1 
ATOM   2040 C CB   A VAL   A 1 100 ? 18.292 -2.907  -11.896 0.72 19.77 ?  100 VAL   A CB   1 
ATOM   2041 C CB   B VAL   A 1 100 ? 17.972 -2.624  -11.756 0.28 19.15 ?  100 VAL   A CB   1 
ATOM   2042 C CG1  A VAL   A 1 100 ? 17.631 -3.151  -13.248 0.72 20.35 ?  100 VAL   A CG1  1 
ATOM   2043 C CG1  B VAL   A 1 100 ? 17.076 -2.543  -12.984 0.28 19.27 ?  100 VAL   A CG1  1 
ATOM   2044 C CG2  A VAL   A 1 100 ? 18.516 -4.226  -11.170 0.72 20.21 ?  100 VAL   A CG2  1 
ATOM   2045 C CG2  B VAL   A 1 100 ? 17.890 -3.987  -11.113 0.28 19.26 ?  100 VAL   A CG2  1 
ATOM   2046 H H    A VAL   A 1 100 ? 19.743 -2.154  -10.082 0.72 20.21 ?  100 VAL   A H    1 
ATOM   2047 H H    B VAL   A 1 100 ? 19.714 -1.911  -10.191 0.28 20.14 ?  100 VAL   A H    1 
ATOM   2048 H HA   A VAL   A 1 100 ? 20.219 -2.728  -12.574 0.72 22.29 ?  100 VAL   A HA   1 
ATOM   2049 H HA   B VAL   A 1 100 ? 19.810 -3.083  -12.522 0.28 22.67 ?  100 VAL   A HA   1 
ATOM   2050 H HB   A VAL   A 1 100 ? 17.687 -2.369  -11.363 0.72 23.74 ?  100 VAL   A HB   1 
ATOM   2051 H HB   B VAL   A 1 100 ? 17.669 -1.970  -11.121 0.28 23.00 ?  100 VAL   A HB   1 
ATOM   2052 H HG11 A VAL   A 1 100 ? 16.869 -3.740  -13.127 0.72 24.44 ?  100 VAL   A HG11 1 
ATOM   2053 H HG11 B VAL   A 1 100 ? 16.243 -3.003  -12.793 0.28 23.14 ?  100 VAL   A HG11 1 
ATOM   2054 H HG12 A VAL   A 1 100 ? 17.335 -2.303  -13.617 0.72 24.44 ?  100 VAL   A HG12 1 
ATOM   2055 H HG12 B VAL   A 1 100 ? 16.894 -1.611  -13.189 0.28 23.14 ?  100 VAL   A HG12 1 
ATOM   2056 H HG13 A VAL   A 1 100 ? 18.274 -3.565  -13.846 0.72 24.44 ?  100 VAL   A HG13 1 
ATOM   2057 H HG13 B VAL   A 1 100 ? 17.526 -2.968  -13.727 0.28 23.14 ?  100 VAL   A HG13 1 
ATOM   2058 H HG21 A VAL   A 1 100 ? 17.690 -4.735  -11.177 0.72 24.28 ?  100 VAL   A HG21 1 
ATOM   2059 H HG21 B VAL   A 1 100 ? 16.970 -4.172  -10.878 0.28 23.14 ?  100 VAL   A HG21 1 
ATOM   2060 H HG22 A VAL   A 1 100 ? 19.214 -4.722  -11.627 0.72 24.28 ?  100 VAL   A HG22 1 
ATOM   2061 H HG22 B VAL   A 1 100 ? 18.215 -4.646  -11.745 0.28 23.14 ?  100 VAL   A HG22 1 
ATOM   2062 H HG23 A VAL   A 1 100 ? 18.784 -4.042  -10.257 0.72 24.28 ?  100 VAL   A HG23 1 
ATOM   2063 H HG23 B VAL   A 1 100 ? 18.444 -3.990  -10.316 0.28 23.14 ?  100 VAL   A HG23 1 
ATOM   2064 N N    A ASN   A 1 101 ? 19.306 0.266   -12.116 0.72 19.89 ?  101 ASN   A N    1 
ATOM   2065 N N    B ASN   A 1 101 ? 19.493 0.077   -12.657 0.28 21.79 ?  101 ASN   A N    1 
ATOM   2066 C CA   A ASN   A 1 101 ? 19.233 1.551   -12.804 0.72 21.27 ?  101 ASN   A CA   1 
ATOM   2067 C CA   B ASN   A 1 101 ? 19.551 1.228   -13.548 0.28 22.65 ?  101 ASN   A CA   1 
ATOM   2068 C C    A ASN   A 1 101 ? 20.582 2.003   -13.363 0.72 23.43 ?  101 ASN   A C    1 
ATOM   2069 C C    B ASN   A 1 101 ? 20.967 1.539   -14.017 0.28 23.33 ?  101 ASN   A C    1 
ATOM   2070 O O    A ASN   A 1 101 ? 20.633 3.053   -14.015 0.72 25.11 ?  101 ASN   A O    1 
ATOM   2071 O O    B ASN   A 1 101 ? 21.222 2.647   -14.506 0.28 23.74 ?  101 ASN   A O    1 
ATOM   2072 C CB   A ASN   A 1 101 ? 18.615 2.601   -11.879 0.72 21.02 ?  101 ASN   A CB   1 
ATOM   2073 C CB   B ASN   A 1 101 ? 18.902 2.453   -12.896 0.28 22.83 ?  101 ASN   A CB   1 
ATOM   2074 C CG   A ASN   A 1 101 ? 17.232 2.187   -11.380 0.72 20.79 ?  101 ASN   A CG   1 
ATOM   2075 C CG   B ASN   A 1 101 ? 17.830 2.081   -11.888 0.28 22.94 ?  101 ASN   A CG   1 
ATOM   2076 O OD1  A ASN   A 1 101 ? 16.404 1.675   -12.144 0.72 21.50 ?  101 ASN   A OD1  1 
ATOM   2077 O OD1  B ASN   A 1 101 ? 16.783 1.540   -12.245 0.28 23.11 ?  101 ASN   A OD1  1 
ATOM   2078 N ND2  A ASN   A 1 101 ? 16.985 2.385   -10.093 0.72 20.58 ?  101 ASN   A ND2  1 
ATOM   2079 N ND2  B ASN   A 1 101 ? 18.088 2.374   -10.618 0.28 23.01 ?  101 ASN   A ND2  1 
ATOM   2080 H H    A ASN   A 1 101 ? 19.211 0.307   -11.264 0.72 23.89 ?  101 ASN   A H    1 
ATOM   2081 H H    B ASN   A 1 101 ? 19.444 0.275   -11.818 0.28 26.17 ?  101 ASN   A H    1 
ATOM   2082 H HA   A ASN   A 1 101 ? 18.636 1.455   -13.558 0.72 25.54 ?  101 ASN   A HA   1 
ATOM   2083 H HA   B ASN   A 1 101 ? 19.046 1.027   -14.342 0.28 27.19 ?  101 ASN   A HA   1 
ATOM   2084 H HB2  A ASN   A 1 101 ? 19.192 2.730   -11.110 0.72 25.25 ?  101 ASN   A HB2  1 
ATOM   2085 H HB2  B ASN   A 1 101 ? 19.580 2.961   -12.439 0.28 27.41 ?  101 ASN   A HB2  1 
ATOM   2086 H HB3  A ASN   A 1 101 ? 18.527 3.441   -12.368 0.72 25.25 ?  101 ASN   A HB3  1 
ATOM   2087 H HB3  B ASN   A 1 101 ? 18.488 3.002   -13.582 0.28 27.41 ?  101 ASN   A HB3  1 
ATOM   2088 H HD21 A ASN   A 1 101 ? 16.219 2.171   -9.769  0.72 24.72 ?  101 ASN   A HD21 1 
ATOM   2089 H HD21 B ASN   A 1 101 ? 17.516 2.183   -10.007 0.28 27.63 ?  101 ASN   A HD21 1 
ATOM   2090 H HD22 A ASN   A 1 101 ? 17.584 2.738   -9.588  0.72 24.72 ?  101 ASN   A HD22 1 
ATOM   2091 H HD22 B ASN   A 1 101 ? 18.831 2.757   -10.407 0.28 27.63 ?  101 ASN   A HD22 1 
ATOM   2092 N N    A LYS   A 1 102 ? 21.653 1.231   -13.141 0.72 24.98 ?  102 LYS   A N    1 
ATOM   2093 N N    B LYS   A 1 102 ? 21.886 0.579   -13.883 0.28 23.41 ?  102 LYS   A N    1 
ATOM   2094 C CA   A LYS   A 1 102 ? 22.941 1.425   -13.797 0.72 26.06 ?  102 LYS   A CA   1 
ATOM   2095 C CA   B LYS   A 1 102 ? 23.238 0.710   -14.409 0.28 23.37 ?  102 LYS   A CA   1 
ATOM   2096 C C    A LYS   A 1 102 ? 23.256 0.327   -14.805 0.72 26.38 ?  102 LYS   A C    1 
ATOM   2097 C C    B LYS   A 1 102 ? 23.621 -0.457  -15.313 0.28 22.49 ?  102 LYS   A C    1 
ATOM   2098 O O    A LYS   A 1 102 ? 24.333 0.355   -15.407 0.72 26.63 ?  102 LYS   A O    1 
ATOM   2099 O O    B LYS   A 1 102 ? 24.779 -0.539  -15.736 0.28 22.48 ?  102 LYS   A O    1 
ATOM   2100 C CB   A LYS   A 1 102 ? 24.071 1.476   -12.759 0.72 27.10 ?  102 LYS   A CB   1 
ATOM   2101 C CB   B LYS   A 1 102 ? 24.271 0.820   -13.279 0.28 24.26 ?  102 LYS   A CB   1 
ATOM   2102 C CG   A LYS   A 1 102 ? 23.964 2.604   -11.753 0.72 27.89 ?  102 LYS   A CG   1 
ATOM   2103 C CG   B LYS   A 1 102 ? 24.208 2.103   -12.468 0.28 25.15 ?  102 LYS   A CG   1 
ATOM   2104 C CD   A LYS   A 1 102 ? 25.116 2.548   -10.758 0.72 28.72 ?  102 LYS   A CD   1 
ATOM   2105 C CD   B LYS   A 1 102 ? 25.459 2.250   -11.606 0.28 26.26 ?  102 LYS   A CD   1 
ATOM   2106 C CE   A LYS   A 1 102 ? 25.048 3.684   -9.753  0.72 29.57 ?  102 LYS   A CE   1 
ATOM   2107 C CE   B LYS   A 1 102 ? 25.488 3.577   -10.866 0.28 27.07 ?  102 LYS   A CE   1 
ATOM   2108 N NZ   A LYS   A 1 102 ? 26.162 3.614   -8.763  0.72 29.96 ?  102 LYS   A NZ   1 
ATOM   2109 N NZ   B LYS   A 1 102 ? 26.832 3.872   -10.289 0.28 27.52 ?  102 LYS   A NZ   1 
ATOM   2110 H H    A LYS   A 1 102 ? 21.655 0.561   -12.601 0.72 30.00 ?  102 LYS   A H    1 
ATOM   2111 H H    B LYS   A 1 102 ? 21.740 -0.170  -13.486 0.28 28.11 ?  102 LYS   A H    1 
ATOM   2112 H HA   A LYS   A 1 102 ? 22.934 2.267   -14.273 0.72 31.29 ?  102 LYS   A HA   1 
ATOM   2113 H HA   B LYS   A 1 102 ? 23.283 1.522   -14.933 0.28 28.07 ?  102 LYS   A HA   1 
ATOM   2114 H HB2  A LYS   A 1 102 ? 24.076 0.642   -12.265 0.72 32.54 ?  102 LYS   A HB2  1 
ATOM   2115 H HB2  B LYS   A 1 102 ? 24.137 0.081   -12.667 0.28 29.13 ?  102 LYS   A HB2  1 
ATOM   2116 H HB3  A LYS   A 1 102 ? 24.917 1.580   -13.226 0.72 32.54 ?  102 LYS   A HB3  1 
ATOM   2117 H HB3  B LYS   A 1 102 ? 25.158 0.762   -13.670 0.28 29.13 ?  102 LYS   A HB3  1 
ATOM   2118 H HG2  A LYS   A 1 102 ? 24.000 3.454   -12.218 0.72 33.49 ?  102 LYS   A HG2  1 
ATOM   2119 H HG2  B LYS   A 1 102 ? 24.158 2.863   -13.068 0.28 30.20 ?  102 LYS   A HG2  1 
ATOM   2120 H HG3  A LYS   A 1 102 ? 23.131 2.520   -11.264 0.72 33.49 ?  102 LYS   A HG3  1 
ATOM   2121 H HG3  B LYS   A 1 102 ? 23.432 2.080   -11.886 0.28 30.20 ?  102 LYS   A HG3  1 
ATOM   2122 H HD2  A LYS   A 1 102 ? 25.077 1.709   -10.272 0.72 34.48 ?  102 LYS   A HD2  1 
ATOM   2123 H HD2  B LYS   A 1 102 ? 25.479 1.535   -10.949 0.28 31.53 ?  102 LYS   A HD2  1 
ATOM   2124 H HD3  A LYS   A 1 102 ? 25.956 2.617   -11.239 0.72 34.48 ?  102 LYS   A HD3  1 
ATOM   2125 H HD3  B LYS   A 1 102 ? 26.244 2.203   -12.174 0.28 31.53 ?  102 LYS   A HD3  1 
ATOM   2126 H HE2  A LYS   A 1 102 ? 25.112 4.530   -10.224 0.72 35.51 ?  102 LYS   A HE2  1 
ATOM   2127 H HE2  B LYS   A 1 102 ? 25.260 4.289   -11.482 0.28 32.50 ?  102 LYS   A HE2  1 
ATOM   2128 H HE3  A LYS   A 1 102 ? 24.208 3.633   -9.271  0.72 35.51 ?  102 LYS   A HE3  1 
ATOM   2129 H HE3  B LYS   A 1 102 ? 24.848 3.547   -10.137 0.28 32.50 ?  102 LYS   A HE3  1 
ATOM   2130 H HZ1  A LYS   A 1 102 ? 26.099 4.288   -8.187  0.72 35.97 ?  102 LYS   A HZ1  1 
ATOM   2131 H HZ1  B LYS   A 1 102 ? 26.816 4.654   -9.863  0.28 33.04 ?  102 LYS   A HZ1  1 
ATOM   2132 H HZ2  A LYS   A 1 102 ? 26.121 2.845   -8.316  0.72 35.97 ?  102 LYS   A HZ2  1 
ATOM   2133 H HZ2  B LYS   A 1 102 ? 27.065 3.235   -9.713  0.28 33.04 ?  102 LYS   A HZ2  1 
ATOM   2134 H HZ3  A LYS   A 1 102 ? 26.944 3.662   -9.184  0.72 35.97 ?  102 LYS   A HZ3  1 
ATOM   2135 H HZ3  B LYS   A 1 102 ? 27.440 3.911   -10.939 0.28 33.04 ?  102 LYS   A HZ3  1 
ATOM   2136 N N    A GLY   A 1 103 ? 22.362 -0.642  -14.992 0.72 26.91 ?  103 GLY   A N    1 
ATOM   2137 N N    B GLY   A 1 103 ? 22.694 -1.366  -15.606 0.28 21.75 ?  103 GLY   A N    1 
ATOM   2138 C CA   A GLY   A 1 103 ? 22.596 -1.736  -15.917 0.72 27.05 ?  103 GLY   A CA   1 
ATOM   2139 C CA   B GLY   A 1 103 ? 23.015 -2.533  -16.398 0.28 21.13 ?  103 GLY   A CA   1 
ATOM   2140 C C    A GLY   A 1 103 ? 23.442 -2.866  -15.374 0.72 27.18 ?  103 GLY   A C    1 
ATOM   2141 C C    B GLY   A 1 103 ? 23.742 -3.626  -15.649 0.28 20.22 ?  103 GLY   A C    1 
ATOM   2142 O O    A GLY   A 1 103 ? 24.003 -3.634  -16.161 0.72 28.21 ?  103 GLY   A O    1 
ATOM   2143 O O    B GLY   A 1 103 ? 24.129 -4.626  -16.268 0.28 20.28 ?  103 GLY   A O    1 
ATOM   2144 H H    A GLY   A 1 103 ? 21.609 -0.688  -14.591 0.72 32.31 ?  103 GLY   A H    1 
ATOM   2145 H H    B GLY   A 1 103 ? 21.872 -1.327  -15.350 0.28 26.12 ?  103 GLY   A H    1 
ATOM   2146 H HA2  A GLY   A 1 103 ? 21.738 -2.101  -16.199 0.72 32.48 ?  103 GLY   A HA2  1 
ATOM   2147 H HA2  B GLY   A 1 103 ? 22.200 -2.907  -16.763 0.28 25.37 ?  103 GLY   A HA2  1 
ATOM   2148 H HA3  A GLY   A 1 103 ? 23.045 -1.397  -16.707 0.72 32.48 ?  103 GLY   A HA3  1 
ATOM   2149 H HA3  B GLY   A 1 103 ? 23.579 -2.253  -17.137 0.28 25.37 ?  103 GLY   A HA3  1 
ATOM   2150 N N    A GLU   A 1 104 ? 23.551 -2.998  -14.055 0.72 25.65 ?  104 GLU   A N    1 
ATOM   2151 N N    B GLU   A 1 104 ? 23.934 -3.475  -14.342 0.28 19.07 ?  104 GLU   A N    1 
ATOM   2152 C CA   A GLU   A 1 104 ? 24.426 -3.997  -13.459 0.72 24.27 ?  104 GLU   A CA   1 
ATOM   2153 C CA   B GLU   A 1 104 ? 24.748 -4.417  -13.588 0.28 18.04 ?  104 GLU   A CA   1 
ATOM   2154 C C    A GLU   A 1 104 ? 23.738 -5.358  -13.369 0.72 24.56 ?  104 GLU   A C    1 
ATOM   2155 C C    B GLU   A 1 104 ? 24.016 -5.747  -13.423 0.28 18.39 ?  104 GLU   A C    1 
ATOM   2156 O O    A GLU   A 1 104 ? 22.511 -5.459  -13.270 0.72 24.75 ?  104 GLU   A O    1 
ATOM   2157 O O    B GLU   A 1 104 ? 22.832 -5.786  -13.071 0.28 18.21 ?  104 GLU   A O    1 
ATOM   2158 C CB   A GLU   A 1 104 ? 24.921 -3.507  -12.093 0.72 22.56 ?  104 GLU   A CB   1 
ATOM   2159 C CB   B GLU   A 1 104 ? 25.124 -3.805  -12.238 0.28 17.24 ?  104 GLU   A CB   1 
ATOM   2160 C CG   A GLU   A 1 104 ? 25.893 -2.328  -12.249 0.72 21.69 ?  104 GLU   A CG   1 
ATOM   2161 C CG   B GLU   A 1 104 ? 25.848 -2.466  -12.394 0.28 17.21 ?  104 GLU   A CG   1 
ATOM   2162 C CD   A GLU   A 1 104 ? 26.178 -1.525  -10.986 0.72 20.49 ?  104 GLU   A CD   1 
ATOM   2163 C CD   B GLU   A 1 104 ? 26.298 -1.843  -11.082 0.28 17.01 ?  104 GLU   A CD   1 
ATOM   2164 O OE1  A GLU   A 1 104 ? 25.599 -1.810  -9.921  0.72 18.99 ?  104 GLU   A OE1  1 
ATOM   2165 O OE1  B GLU   A 1 104 ? 25.764 -2.207  -10.015 0.28 16.64 ?  104 GLU   A OE1  1 
ATOM   2166 O OE2  A GLU   A 1 104 ? 26.994 -0.577  -11.085 0.72 21.11 -1 104 GLU   A OE2  1 
ATOM   2167 O OE2  B GLU   A 1 104 ? 27.194 -0.971  -11.127 0.28 17.56 -1 104 GLU   A OE2  1 
ATOM   2168 H H    A GLU   A 1 104 ? 23.133 -2.512  -13.486 0.72 30.80 ?  104 GLU   A H    1 
ATOM   2169 H H    B GLU   A 1 104 ? 23.604 -2.831  -13.874 0.28 22.90 ?  104 GLU   A H    1 
ATOM   2170 H HA   A GLU   A 1 104 ? 25.201 -4.103  -14.029 0.72 29.14 ?  104 GLU   A HA   1 
ATOM   2171 H HA   B GLU   A 1 104 ? 25.571 -4.581  -14.077 0.28 21.66 ?  104 GLU   A HA   1 
ATOM   2172 H HB2  A GLU   A 1 104 ? 24.160 -3.218  -11.566 0.72 27.09 ?  104 GLU   A HB2  1 
ATOM   2173 H HB2  B GLU   A 1 104 ? 24.319 -3.651  -11.721 0.28 20.71 ?  104 GLU   A HB2  1 
ATOM   2174 H HB3  A GLU   A 1 104 ? 25.383 -4.234  -11.646 0.72 27.09 ?  104 GLU   A HB3  1 
ATOM   2175 H HB3  B GLU   A 1 104 ? 25.716 -4.410  -11.767 0.28 20.71 ?  104 GLU   A HB3  1 
ATOM   2176 H HG2  A GLU   A 1 104 ? 26.734 -2.674  -12.573 0.72 26.05 ?  104 GLU   A HG2  1 
ATOM   2177 H HG2  B GLU   A 1 104 ? 26.635 -2.598  -12.944 0.28 20.68 ?  104 GLU   A HG2  1 
ATOM   2178 H HG3  A GLU   A 1 104 ? 25.516 -1.712  -12.892 0.72 26.05 ?  104 GLU   A HG3  1 
ATOM   2179 H HG3  B GLU   A 1 104 ? 25.250 -1.835  -12.826 0.28 20.68 ?  104 GLU   A HG3  1 
ATOM   2180 N N    A ASP   A 1 105 ? 24.555 -6.412  -13.410 0.72 25.12 ?  105 ASP   A N    1 
ATOM   2181 N N    B ASP   A 1 105 ? 24.736 -6.836  -13.690 0.28 19.60 ?  105 ASP   A N    1 
ATOM   2182 C CA   A ASP   A 1 105 ? 24.066 -7.779  -13.568 0.72 26.23 ?  105 ASP   A CA   1 
ATOM   2183 C CA   B ASP   A 1 105 ? 24.154 -8.174  -13.716 0.28 21.00 ?  105 ASP   A CA   1 
ATOM   2184 C C    A ASP   A 1 105 ? 23.375 -8.252  -12.292 0.72 24.11 ?  105 ASP   A C    1 
ATOM   2185 C C    B ASP   A 1 105 ? 23.454 -8.497  -12.402 0.28 21.03 ?  105 ASP   A C    1 
ATOM   2186 O O    A ASP   A 1 105 ? 24.014 -8.383  -11.244 0.72 22.14 ?  105 ASP   A O    1 
ATOM   2187 O O    B ASP   A 1 105 ? 24.037 -8.370  -11.322 0.28 20.66 ?  105 ASP   A O    1 
ATOM   2188 C CB   A ASP   A 1 105 ? 25.247 -8.688  -13.902 0.72 29.26 ?  105 ASP   A CB   1 
ATOM   2189 C CB   B ASP   A 1 105 ? 25.273 -9.184  -13.974 0.28 22.42 ?  105 ASP   A CB   1 
ATOM   2190 C CG   A ASP   A 1 105 ? 24.827 -10.103 -14.228 0.72 31.69 ?  105 ASP   A CG   1 
ATOM   2191 C CG   B ASP   A 1 105 ? 24.833 -10.624 -13.779 0.28 23.56 ?  105 ASP   A CG   1 
ATOM   2192 O OD1  A ASP   A 1 105 ? 23.609 -10.352 -14.333 0.72 32.41 ?  105 ASP   A OD1  1 
ATOM   2193 O OD1  B ASP   A 1 105 ? 23.622 -10.911 -13.883 0.28 23.66 ?  105 ASP   A OD1  1 
ATOM   2194 O OD2  A ASP   A 1 105 ? 25.721 -10.963 -14.387 0.72 32.82 -1 105 ASP   A OD2  1 
ATOM   2195 O OD2  B ASP   A 1 105 ? 25.713 -11.473 -13.517 0.28 24.46 -1 105 ASP   A OD2  1 
ATOM   2196 H H    A ASP   A 1 105 ? 25.414 -6.359  -13.353 0.72 30.16 ?  105 ASP   A H    1 
ATOM   2197 H H    B ASP   A 1 105 ? 25.574 -6.818  -13.869 0.28 23.54 ?  105 ASP   A H    1 
ATOM   2198 H HA   A ASP   A 1 105 ? 23.431 -7.819  -14.298 0.72 31.49 ?  105 ASP   A HA   1 
ATOM   2199 H HA   B ASP   A 1 105 ? 23.503 -8.231  -14.434 0.28 25.22 ?  105 ASP   A HA   1 
ATOM   2200 H HB2  A ASP   A 1 105 ? 25.708 -8.340  -14.682 0.72 35.14 ?  105 ASP   A HB2  1 
ATOM   2201 H HB2  B ASP   A 1 105 ? 25.578 -9.081  -14.889 0.28 26.92 ?  105 ASP   A HB2  1 
ATOM   2202 H HB3  A ASP   A 1 105 ? 25.853 -8.716  -13.145 0.72 35.14 ?  105 ASP   A HB3  1 
ATOM   2203 H HB3  B ASP   A 1 105 ? 26.002 -9.003  -13.360 0.28 26.92 ?  105 ASP   A HB3  1 
ATOM   2204 N N    A ILE   A 1 106 ? 22.073 -8.533  -12.386 0.72 23.96 ?  106 ILE   A N    1 
ATOM   2205 N N    B ILE   A 1 106 ? 22.196 -8.936  -12.502 0.28 21.35 ?  106 ILE   A N    1 
ATOM   2206 C CA   A ILE   A 1 106 ? 21.313 -8.965  -11.218 0.72 23.23 ?  106 ILE   A CA   1 
ATOM   2207 C CA   B ILE   A 1 106 ? 21.422 -9.255  -11.308 0.28 21.79 ?  106 ILE   A CA   1 
ATOM   2208 C C    A ILE   A 1 106 ? 21.856 -10.261 -10.642 0.72 22.28 ?  106 ILE   A C    1 
ATOM   2209 C C    B ILE   A 1 106 ? 21.947 -10.502 -10.608 0.28 21.52 ?  106 ILE   A C    1 
ATOM   2210 O O    A ILE   A 1 106 ? 21.662 -10.532 -9.453  0.72 21.44 ?  106 ILE   A O    1 
ATOM   2211 O O    B ILE   A 1 106 ? 21.701 -10.681 -9.410  0.28 21.45 ?  106 ILE   A O    1 
ATOM   2212 C CB   A ILE   A 1 106 ? 19.806 -9.060  -11.548 0.72 24.50 ?  106 ILE   A CB   1 
ATOM   2213 C CB   B ILE   A 1 106 ? 19.920 -9.364  -11.644 0.28 22.76 ?  106 ILE   A CB   1 
ATOM   2214 C CG1  A ILE   A 1 106 ? 18.975 -9.164  -10.266 0.72 25.08 ?  106 ILE   A CG1  1 
ATOM   2215 C CG1  B ILE   A 1 106 ? 19.074 -9.283  -10.371 0.28 23.34 ?  106 ILE   A CG1  1 
ATOM   2216 C CG2  A ILE   A 1 106 ? 19.527 -10.249 -12.450 0.72 25.06 ?  106 ILE   A CG2  1 
ATOM   2217 C CG2  B ILE   A 1 106 ? 19.627 -10.660 -12.378 0.28 22.96 ?  106 ILE   A CG2  1 
ATOM   2218 C CD1  A ILE   A 1 106 ? 19.112 -7.968  -9.349  0.72 25.36 ?  106 ILE   A CD1  1 
ATOM   2219 C CD1  B ILE   A 1 106 ? 19.285 -8.014  -9.575  0.28 23.63 ?  106 ILE   A CD1  1 
ATOM   2220 H H    A ILE   A 1 106 ? 21.615 -8.477  -13.107 0.72 28.77 ?  106 ILE   A H    1 
ATOM   2221 H H    B ILE   A 1 106 ? 21.775 -9.046  -13.242 0.28 25.64 ?  106 ILE   A H    1 
ATOM   2222 H HA   A ILE   A 1 106 ? 21.421 -8.298  -10.532 0.72 27.89 ?  106 ILE   A HA   1 
ATOM   2223 H HA   B ILE   A 1 106 ? 21.531 -8.520  -10.691 0.28 26.17 ?  106 ILE   A HA   1 
ATOM   2224 H HB   A ILE   A 1 106 ? 19.547 -8.255  -12.018 0.72 29.42 ?  106 ILE   A HB   1 
ATOM   2225 H HB   B ILE   A 1 106 ? 19.676 -8.622  -12.221 0.28 27.34 ?  106 ILE   A HB   1 
ATOM   2226 H HG12 A ILE   A 1 106 ? 18.039 -9.242  -10.508 0.72 30.12 ?  106 ILE   A HG12 1 
ATOM   2227 H HG12 B ILE   A 1 106 ? 18.134 -9.323  -10.614 0.28 28.02 ?  106 ILE   A HG12 1 
ATOM   2228 H HG13 A ILE   A 1 106 ? 19.253 -9.950  -9.772  0.72 30.12 ?  106 ILE   A HG13 1 
ATOM   2229 H HG13 B ILE   A 1 106 ? 19.296 -10.032 -9.797  0.28 28.02 ?  106 ILE   A HG13 1 
ATOM   2230 H HG21 A ILE   A 1 106 ? 18.629 -10.167 -12.806 0.72 30.10 ?  106 ILE   A HG21 1 
ATOM   2231 H HG21 B ILE   A 1 106 ? 18.744 -10.603 -12.777 0.28 27.57 ?  106 ILE   A HG21 1 
ATOM   2232 H HG22 A ILE   A 1 106 ? 20.172 -10.251 -13.174 0.72 30.10 ?  106 ILE   A HG22 1 
ATOM   2233 H HG22 B ILE   A 1 106 ? 20.295 -10.787 -13.068 0.28 27.57 ?  106 ILE   A HG22 1 
ATOM   2234 H HG23 A ILE   A 1 106 ? 19.606 -11.065 -11.933 0.72 30.10 ?  106 ILE   A HG23 1 
ATOM   2235 H HG23 B ILE   A 1 106 ? 19.657 -11.395 -11.746 0.28 27.57 ?  106 ILE   A HG23 1 
ATOM   2236 H HD11 A ILE   A 1 106 ? 18.378 -7.970  -8.718  0.72 30.45 ?  106 ILE   A HD11 1 
ATOM   2237 H HD11 B ILE   A 1 106 ? 18.524 -7.876  -8.994  0.28 28.38 ?  106 ILE   A HD11 1 
ATOM   2238 H HD12 A ILE   A 1 106 ? 19.957 -8.028  -8.874  0.72 30.45 ?  106 ILE   A HD12 1 
ATOM   2239 H HD12 B ILE   A 1 106 ? 20.094 -8.104  -9.045  0.28 28.38 ?  106 ILE   A HD12 1 
ATOM   2240 H HD13 A ILE   A 1 106 ? 19.088 -7.158  -9.882  0.72 30.45 ?  106 ILE   A HD13 1 
ATOM   2241 H HD13 B ILE   A 1 106 ? 19.373 -7.268  -10.190 0.28 28.38 ?  106 ILE   A HD13 1 
ATOM   2242 N N    A GLN   A 1 107 ? 22.555 -11.065 -11.453 0.72 23.00 ?  107 GLN   A N    1 
ATOM   2243 N N    B GLN   A 1 107 ? 22.672 -11.370 -11.321 0.28 21.35 ?  107 GLN   A N    1 
ATOM   2244 C CA   A GLN   A 1 107 ? 23.181 -12.282 -10.948 0.72 24.90 ?  107 GLN   A CA   1 
ATOM   2245 C CA   B GLN   A 1 107 ? 23.266 -12.534 -10.671 0.28 21.89 ?  107 GLN   A CA   1 
ATOM   2246 C C    A GLN   A 1 107 ? 24.158 -11.988 -9.819  0.72 22.33 ?  107 GLN   A C    1 
ATOM   2247 C C    B GLN   A 1 107 ? 24.243 -12.118 -9.581  0.28 19.80 ?  107 GLN   A C    1 
ATOM   2248 O O    A GLN   A 1 107 ? 24.399 -12.861 -8.978  0.72 23.90 ?  107 GLN   A O    1 
ATOM   2249 O O    B GLN   A 1 107 ? 24.473 -12.870 -8.625  0.28 19.78 ?  107 GLN   A O    1 
ATOM   2250 C CB   A GLN   A 1 107 ? 23.883 -13.026 -12.094 0.72 29.02 ?  107 GLN   A CB   1 
ATOM   2251 C CB   B GLN   A 1 107 ? 23.948 -13.422 -11.712 0.28 24.44 ?  107 GLN   A CB   1 
ATOM   2252 C CG   A GLN   A 1 107 ? 22.995 -13.280 -13.309 0.72 33.41 ?  107 GLN   A CG   1 
ATOM   2253 C CG   B GLN   A 1 107 ? 22.999 -13.944 -12.780 0.28 26.87 ?  107 GLN   A CG   1 
ATOM   2254 C CD   A GLN   A 1 107 ? 21.755 -14.081 -12.969 0.72 36.93 ?  107 GLN   A CD   1 
ATOM   2255 C CD   B GLN   A 1 107 ? 21.769 -14.605 -12.187 0.28 29.05 ?  107 GLN   A CD   1 
ATOM   2256 O OE1  A GLN   A 1 107 ? 21.837 -15.142 -12.350 0.72 38.36 ?  107 GLN   A OE1  1 
ATOM   2257 O OE1  B GLN   A 1 107 ? 21.867 -15.407 -11.258 0.28 29.75 ?  107 GLN   A OE1  1 
ATOM   2258 N NE2  A GLN   A 1 107 ? 20.595 -13.573 -13.370 0.72 38.18 ?  107 GLN   A NE2  1 
ATOM   2259 N NE2  B GLN   A 1 107 ? 20.600 -14.258 -12.713 0.28 29.73 ?  107 GLN   A NE2  1 
ATOM   2260 H H    A GLN   A 1 107 ? 22.687 -10.924 -12.290 0.72 27.62 ?  107 GLN   A H    1 
ATOM   2261 H H    B GLN   A 1 107 ? 22.829 -11.304 -12.166 0.28 25.65 ?  107 GLN   A H    1 
ATOM   2262 H HA   A GLN   A 1 107 ? 22.503 -12.874 -10.595 0.72 29.90 ?  107 GLN   A HA   1 
ATOM   2263 H HA   B GLN   A 1 107 ? 22.561 -13.048 -10.256 0.28 26.29 ?  107 GLN   A HA   1 
ATOM   2264 H HB2  A GLN   A 1 107 ? 24.643 -12.505 -12.397 0.72 34.85 ?  107 GLN   A HB2  1 
ATOM   2265 H HB2  B GLN   A 1 107 ? 24.644 -12.914 -12.158 0.28 29.34 ?  107 GLN   A HB2  1 
ATOM   2266 H HB3  A GLN   A 1 107 ? 24.188 -13.893 -11.777 0.72 34.85 ?  107 GLN   A HB3  1 
ATOM   2267 H HB3  B GLN   A 1 107 ? 24.338 -14.188 -11.265 0.28 29.34 ?  107 GLN   A HB3  1 
ATOM   2268 H HG2  A GLN   A 1 107 ? 22.708 -12.432 -13.679 0.72 40.11 ?  107 GLN   A HG2  1 
ATOM   2269 H HG2  B GLN   A 1 107 ? 22.706 -13.203 -13.333 0.28 32.26 ?  107 GLN   A HG2  1 
ATOM   2270 H HG3  A GLN   A 1 107 ? 23.499 -13.776 -13.974 0.72 40.11 ?  107 GLN   A HG3  1 
ATOM   2271 H HG3  B GLN   A 1 107 ? 23.460 -14.603 -13.321 0.28 32.26 ?  107 GLN   A HG3  1 
ATOM   2272 H HE21 A GLN   A 1 107 ? 20.577 -12.829 -13.800 0.72 45.83 ?  107 GLN   A HE21 1 
ATOM   2273 H HE21 B GLN   A 1 107 ? 20.571 -13.691 -13.360 0.28 35.70 ?  107 GLN   A HE21 1 
ATOM   2274 H HE22 A GLN   A 1 107 ? 19.863 -13.990 -13.200 0.72 45.83 ?  107 GLN   A HE22 1 
ATOM   2275 H HE22 B GLN   A 1 107 ? 19.872 -14.599 -12.407 0.28 35.70 ?  107 GLN   A HE22 1 
ATOM   2276 N N    A LEU   A 1 108 ? 24.699 -10.768 -9.759  0.72 18.23 ?  108 LEU   A N    1 
ATOM   2277 N N    B LEU   A 1 108 ? 24.810 -10.917 -9.695  0.28 17.79 ?  108 LEU   A N    1 
ATOM   2278 C CA   A LEU   A 1 108 ? 25.635 -10.401 -8.703  0.72 15.84 ?  108 LEU   A CA   1 
ATOM   2279 C CA   B LEU   A 1 108 ? 25.681 -10.390 -8.655  0.28 16.00 ?  108 LEU   A CA   1 
ATOM   2280 C C    A LEU   A 1 108 ? 24.955 -10.240 -7.350  0.72 13.83 ?  108 LEU   A C    1 
ATOM   2281 C C    B LEU   A 1 108 ? 24.959 -10.209 -7.326  0.28 14.41 ?  108 LEU   A C    1 
ATOM   2282 O O    A LEU   A 1 108 ? 25.649 -10.099 -6.340  0.72 14.17 ?  108 LEU   A O    1 
ATOM   2283 O O    B LEU   A 1 108 ? 25.627 -10.011 -6.306  0.28 14.54 ?  108 LEU   A O    1 
ATOM   2284 C CB   A LEU   A 1 108 ? 26.396 -9.124  -9.087  0.72 16.00 ?  108 LEU   A CB   1 
ATOM   2285 C CB   B LEU   A 1 108 ? 26.301 -9.066  -9.117  0.28 16.00 ?  108 LEU   A CB   1 
ATOM   2286 C CG   A LEU   A 1 108 ? 27.399 -9.331  -10.227 0.72 17.62 ?  108 LEU   A CG   1 
ATOM   2287 C CG   B LEU   A 1 108 ? 27.314 -9.192  -10.257 0.28 16.55 ?  108 LEU   A CG   1 
ATOM   2288 C CD1  A LEU   A 1 108 ? 27.945 -8.005  -10.736 0.72 18.18 ?  108 LEU   A CD1  1 
ATOM   2289 C CD1  B LEU   A 1 108 ? 27.653 -7.829  -10.842 0.28 16.68 ?  108 LEU   A CD1  1 
ATOM   2290 C CD2  A LEU   A 1 108 ? 28.544 -10.239 -9.790  0.72 19.04 ?  108 LEU   A CD2  1 
ATOM   2291 C CD2  B LEU   A 1 108 ? 28.576 -9.888  -9.770  0.28 17.03 ?  108 LEU   A CD2  1 
ATOM   2292 H H    A LEU   A 1 108 ? 24.531 -10.142 -10.317 0.72 21.89 ?  108 LEU   A H    1 
ATOM   2293 H H    B LEU   A 1 108 ? 24.705 -10.394 -10.365 0.28 21.37 ?  108 LEU   A H    1 
ATOM   2294 H HA   A LEU   A 1 108 ? 26.285 -11.109 -8.608  0.72 19.03 ?  108 LEU   A HA   1 
ATOM   2295 H HA   B LEU   A 1 108 ? 26.402 -11.018 -8.505  0.28 19.22 ?  108 LEU   A HA   1 
ATOM   2296 H HB2  A LEU   A 1 108 ? 25.758 -8.449  -9.374  0.72 19.22 ?  108 LEU   A HB2  1 
ATOM   2297 H HB2  B LEU   A 1 108 ? 25.591 -8.480  -9.422  0.28 19.22 ?  108 LEU   A HB2  1 
ATOM   2298 H HB3  A LEU   A 1 108 ? 26.886 -8.805  -8.314  0.72 19.22 ?  108 LEU   A HB3  1 
ATOM   2299 H HB3  B LEU   A 1 108 ? 26.758 -8.659  -8.366  0.28 19.22 ?  108 LEU   A HB3  1 
ATOM   2300 H HG   A LEU   A 1 108 ? 26.945 -9.763  -10.966 0.72 21.16 ?  108 LEU   A HG   1 
ATOM   2301 H HG   B LEU   A 1 108 ? 26.930 -9.733  -10.966 0.28 19.87 ?  108 LEU   A HG   1 
ATOM   2302 H HD11 A LEU   A 1 108 ? 28.566 -8.177  -11.464 0.72 21.84 ?  108 LEU   A HD11 1 
ATOM   2303 H HD11 B LEU   A 1 108 ? 28.219 -7.951  -11.622 0.28 20.04 ?  108 LEU   A HD11 1 
ATOM   2304 H HD12 A LEU   A 1 108 ? 27.209 -7.460  -11.055 0.72 21.84 ?  108 LEU   A HD12 1 
ATOM   2305 H HD12 B LEU   A 1 108 ? 26.832 -7.382  -11.097 0.28 20.04 ?  108 LEU   A HD12 1 
ATOM   2306 H HD13 A LEU   A 1 108 ? 28.405 -7.551  -10.013 0.72 21.84 ?  108 LEU   A HD13 1 
ATOM   2307 H HD13 B LEU   A 1 108 ? 28.122 -7.306  -10.174 0.28 20.04 ?  108 LEU   A HD13 1 
ATOM   2308 H HD21 A LEU   A 1 108 ? 29.254 -10.188 -10.448 0.72 22.87 ?  108 LEU   A HD21 1 
ATOM   2309 H HD21 B LEU   A 1 108 ? 29.252 -9.839  -10.462 0.28 20.46 ?  108 LEU   A HD21 1 
ATOM   2310 H HD22 A LEU   A 1 108 ? 28.869 -9.941  -8.926  0.72 22.87 ?  108 LEU   A HD22 1 
ATOM   2311 H HD22 B LEU   A 1 108 ? 28.890 -9.444  -8.967  0.28 20.46 ?  108 LEU   A HD22 1 
ATOM   2312 H HD23 A LEU   A 1 108 ? 28.217 -11.149 -9.724  0.72 22.87 ?  108 LEU   A HD23 1 
ATOM   2313 H HD23 B LEU   A 1 108 ? 28.369 -10.816 -9.574  0.28 20.46 ?  108 LEU   A HD23 1 
ATOM   2314 N N    . LEU   A 1 109 ? 23.624 -10.283 -7.299  1.00 13.49 ?  109 LEU   A N    1 
ATOM   2315 C CA   . LEU   A 1 109 ? 22.930 -10.157 -6.025  1.00 12.75 ?  109 LEU   A CA   1 
ATOM   2316 C C    . LEU   A 1 109 ? 23.276 -11.313 -5.090  1.00 12.08 ?  109 LEU   A C    1 
ATOM   2317 O O    . LEU   A 1 109 ? 23.421 -11.117 -3.877  1.00 12.43 ?  109 LEU   A O    1 
ATOM   2318 C CB   . LEU   A 1 109 ? 21.426 -10.070 -6.270  1.00 13.34 ?  109 LEU   A CB   1 
ATOM   2319 C CG   . LEU   A 1 109 ? 20.537 -9.788  -5.064  1.00 13.55 ?  109 LEU   A CG   1 
ATOM   2320 C CD1  . LEU   A 1 109 ? 20.981 -8.520  -4.361  1.00 13.89 ?  109 LEU   A CD1  1 
ATOM   2321 C CD2  . LEU   A 1 109 ? 19.079 -9.666  -5.500  1.00 14.84 ?  109 LEU   A CD2  1 
ATOM   2322 H H    A LEU   A 1 109 ? 23.105 -10.377 -7.978  0.72 16.21 ?  109 LEU   A H    1 
ATOM   2323 H H    B LEU   A 1 109 ? 23.114 -10.397 -7.982  0.28 16.21 ?  109 LEU   A H    1 
ATOM   2324 H HA   . LEU   A 1 109 ? 23.216 -9.334  -5.594  1.00 15.32 ?  109 LEU   A HA   1 
ATOM   2325 H HB2  . LEU   A 1 109 ? 21.269 -9.355  -6.908  1.00 16.03 ?  109 LEU   A HB2  1 
ATOM   2326 H HB3  . LEU   A 1 109 ? 21.133 -10.908 -6.647  1.00 16.03 ?  109 LEU   A HB3  1 
ATOM   2327 H HG   . LEU   A 1 109 ? 20.601 -10.518 -4.433  1.00 16.28 ?  109 LEU   A HG   1 
ATOM   2328 H HD11 . LEU   A 1 109 ? 20.305 -8.259  -3.712  1.00 16.69 ?  109 LEU   A HD11 1 
ATOM   2329 H HD12 . LEU   A 1 109 ? 21.824 -8.676  -3.917  1.00 16.69 ?  109 LEU   A HD12 1 
ATOM   2330 H HD13 . LEU   A 1 109 ? 21.080 -7.808  -5.023  1.00 16.69 ?  109 LEU   A HD13 1 
ATOM   2331 H HD21 . LEU   A 1 109 ? 18.543 -9.371  -4.747  1.00 17.83 ?  109 LEU   A HD21 1 
ATOM   2332 H HD22 . LEU   A 1 109 ? 19.015 -9.023  -6.223  1.00 17.83 ?  109 LEU   A HD22 1 
ATOM   2333 H HD23 . LEU   A 1 109 ? 18.768 -10.536 -5.806  1.00 17.83 ?  109 LEU   A HD23 1 
ATOM   2334 N N    . LYS   A 1 110 ? 23.420 -12.527 -5.627  1.00 11.96 ?  110 LYS   A N    1 
ATOM   2335 C CA   . LYS   A 1 110 ? 23.795 -13.649 -4.772  1.00 12.07 ?  110 LYS   A CA   1 
ATOM   2336 C C    . LYS   A 1 110 ? 25.179 -13.430 -4.166  1.00 11.81 ?  110 LYS   A C    1 
ATOM   2337 O O    . LYS   A 1 110 ? 25.379 -13.630 -2.966  1.00 11.92 ?  110 LYS   A O    1 
ATOM   2338 C CB   . LYS   A 1 110 ? 23.717 -14.973 -5.538  1.00 12.66 ?  110 LYS   A CB   1 
ATOM   2339 C CG   . LYS   A 1 110 ? 23.928 -16.191 -4.633  1.00 13.13 ?  110 LYS   A CG   1 
ATOM   2340 C CD   . LYS   A 1 110 ? 23.701 -17.509 -5.348  1.00 13.71 ?  110 LYS   A CD   1 
ATOM   2341 C CE   . LYS   A 1 110 ? 23.800 -18.691 -4.392  1.00 14.59 ?  110 LYS   A CE   1 
ATOM   2342 N NZ   . LYS   A 1 110 ? 22.617 -18.806 -3.496  1.00 14.94 ?  110 LYS   A NZ   1 
ATOM   2343 H H    . LYS   A 1 110 ? 23.310 -12.721 -6.455  1.00 14.37 ?  110 LYS   A H    1 
ATOM   2344 H HA   . LYS   A 1 110 ? 23.157 -13.699 -4.037  1.00 14.51 ?  110 LYS   A HA   1 
ATOM   2345 H HB2  . LYS   A 1 110 ? 22.840 -15.051 -5.943  1.00 15.21 ?  110 LYS   A HB2  1 
ATOM   2346 H HB3  . LYS   A 1 110 ? 24.404 -14.982 -6.218  1.00 15.21 ?  110 LYS   A HB3  1 
ATOM   2347 H HG2  . LYS   A 1 110 ? 24.841 -16.182 -4.299  1.00 15.78 ?  110 LYS   A HG2  1 
ATOM   2348 H HG3  . LYS   A 1 110 ? 23.307 -16.143 -3.888  1.00 15.78 ?  110 LYS   A HG3  1 
ATOM   2349 H HD2  . LYS   A 1 110 ? 22.820 -17.509 -5.742  1.00 16.47 ?  110 LYS   A HD2  1 
ATOM   2350 H HD3  . LYS   A 1 110 ? 24.380 -17.616 -6.034  1.00 16.47 ?  110 LYS   A HD3  1 
ATOM   2351 H HE2  . LYS   A 1 110 ? 23.867 -19.512 -4.906  1.00 17.53 ?  110 LYS   A HE2  1 
ATOM   2352 H HE3  . LYS   A 1 110 ? 24.589 -18.587 -3.833  1.00 17.53 ?  110 LYS   A HE3  1 
ATOM   2353 H HZ1  . LYS   A 1 110 ? 22.706 -19.503 -2.955  1.00 17.94 ?  110 LYS   A HZ1  1 
ATOM   2354 H HZ2  . LYS   A 1 110 ? 22.535 -18.065 -3.005  1.00 17.94 ?  110 LYS   A HZ2  1 
ATOM   2355 H HZ3  . LYS   A 1 110 ? 21.877 -18.908 -3.984  1.00 17.94 ?  110 LYS   A HZ3  1 
ATOM   2356 N N    . SER   A 1 111 ? 26.142 -12.996 -4.986  1.00 11.86 ?  111 SER   A N    1 
ATOM   2357 C CA   . SER   A 1 111 ? 27.474 -12.679 -4.475  1.00 11.95 ?  111 SER   A CA   1 
ATOM   2358 C C    . SER   A 1 111 ? 27.407 -11.635 -3.365  1.00 11.57 ?  111 SER   A C    1 
ATOM   2359 O O    . SER   A 1 111 ? 28.105 -11.742 -2.350  1.00 11.98 ?  111 SER   A O    1 
ATOM   2360 C CB   . SER   A 1 111 ? 28.359 -12.182 -5.622  1.00 13.08 ?  111 SER   A CB   1 
ATOM   2361 O OG   . SER   A 1 111 ? 28.472 -13.181 -6.625  1.00 15.22 ?  111 SER   A OG   1 
ATOM   2362 H H    . SER   A 1 111 ? 26.043 -12.877 -5.827  1.00 14.25 ?  111 SER   A H    1 
ATOM   2363 H HA   . SER   A 1 111 ? 27.876 -13.483 -4.113  1.00 14.36 ?  111 SER   A HA   1 
ATOM   2364 H HB2  . SER   A 1 111 ? 27.952 -11.391 -6.015  1.00 15.71 ?  111 SER   A HB2  1 
ATOM   2365 H HB3  . SER   A 1 111 ? 29.237 -11.969 -5.278  1.00 15.71 ?  111 SER   A HB3  1 
ATOM   2366 H HG   . SER   A 1 111 ? 28.966 -12.901 -7.252  1.00 18.29 ?  111 SER   A HG   1 
ATOM   2367 N N    . ALA   A 1 112 ? 26.559 -10.618 -3.541  1.00 11.75 ?  112 ALA   A N    1 
ATOM   2368 C CA   . ALA   A 1 112 ? 26.415 -9.580  -2.522  1.00 11.61 ?  112 ALA   A CA   1 
ATOM   2369 C C    . ALA   A 1 112 ? 25.937 -10.179 -1.200  1.00 11.55 ?  112 ALA   A C    1 
ATOM   2370 O O    . ALA   A 1 112 ? 26.484 -9.882  -0.131  1.00 11.83 ?  112 ALA   A O    1 
ATOM   2371 C CB   . ALA   A 1 112 ? 25.456 -8.493  -3.017  1.00 12.02 ?  112 ALA   A CB   1 
ATOM   2372 H H    . ALA   A 1 112 ? 26.061 -10.506 -4.232  1.00 14.12 ?  112 ALA   A H    1 
ATOM   2373 H HA   . ALA   A 1 112 ? 27.278 -9.163  -2.367  1.00 13.96 ?  112 ALA   A HA   1 
ATOM   2374 H HB1  . ALA   A 1 112 ? 25.381 -7.799  -2.337  1.00 14.45 ?  112 ALA   A HB1  1 
ATOM   2375 H HB2  . ALA   A 1 112 ? 25.804 -8.107  -3.837  1.00 14.45 ?  112 ALA   A HB2  1 
ATOM   2376 H HB3  . ALA   A 1 112 ? 24.585 -8.884  -3.180  1.00 14.45 ?  112 ALA   A HB3  1 
ATOM   2377 N N    . TYR   A 1 113 ? 24.899 -11.022 -1.250  1.00 11.42 ?  113 TYR   A N    1 
ATOM   2378 C CA   . TYR   A 1 113 ? 24.387 -11.626 -0.023  1.00 11.01 ?  113 TYR   A CA   1 
ATOM   2379 C C    . TYR   A 1 113 ? 25.390 -12.579 0.625   1.00 10.91 ?  113 TYR   A C    1 
ATOM   2380 O O    . TYR   A 1 113 ? 25.349 -12.767 1.845   1.00 11.53 ?  113 TYR   A O    1 
ATOM   2381 C CB   . TYR   A 1 113 ? 23.070 -12.355 -0.297  1.00 11.37 ?  113 TYR   A CB   1 
ATOM   2382 C CG   . TYR   A 1 113 ? 21.852 -11.459 -0.211  1.00 11.23 ?  113 TYR   A CG   1 
ATOM   2383 C CD1  . TYR   A 1 113 ? 21.489 -10.868 0.995   1.00 11.27 ?  113 TYR   A CD1  1 
ATOM   2384 C CD2  . TYR   A 1 113 ? 21.044 -11.230 -1.321  1.00 11.52 ?  113 TYR   A CD2  1 
ATOM   2385 C CE1  . TYR   A 1 113 ? 20.362 -10.074 1.093   1.00 11.64 ?  113 TYR   A CE1  1 
ATOM   2386 C CE2  . TYR   A 1 113 ? 19.901 -10.429 -1.228  1.00 11.80 ?  113 TYR   A CE2  1 
ATOM   2387 C CZ   . TYR   A 1 113 ? 19.571 -9.862  -0.016  1.00 11.54 ?  113 TYR   A CZ   1 
ATOM   2388 O OH   . TYR   A 1 113 ? 18.449 -9.072  0.116   1.00 12.35 ?  113 TYR   A OH   1 
ATOM   2389 H H    . TYR   A 1 113 ? 24.481 -11.244 -1.973  1.00 13.72 ?  113 TYR   A H    1 
ATOM   2390 H HA   . TYR   A 1 113 ? 24.206 -10.919 0.613   1.00 13.23 ?  113 TYR   A HA   1 
ATOM   2391 H HB2  . TYR   A 1 113 ? 23.096 -12.728 -1.188  1.00 13.67 ?  113 TYR   A HB2  1 
ATOM   2392 H HB3  . TYR   A 1 113 ? 22.965 -13.061 0.358   1.00 13.67 ?  113 TYR   A HB3  1 
ATOM   2393 H HD1  . TYR   A 1 113 ? 22.016 -11.019 1.749   1.00 13.54 ?  113 TYR   A HD1  1 
ATOM   2394 H HD2  . TYR   A 1 113 ? 21.261 -11.626 -2.133  1.00 13.85 ?  113 TYR   A HD2  1 
ATOM   2395 H HE1  . TYR   A 1 113 ? 20.139 -9.691  1.909   1.00 13.99 ?  113 TYR   A HE1  1 
ATOM   2396 H HE2  . TYR   A 1 113 ? 19.362 -10.282 -1.973  1.00 14.18 ?  113 TYR   A HE2  1 
ATOM   2397 H HH   . TYR   A 1 113 ? 18.058 -9.016  -0.629  1.00 14.84 ?  113 TYR   A HH   1 
ATOM   2398 N N    . GLU   A 1 114 ? 26.293 -13.190 -0.156  1.00 11.21 ?  114 GLU   A N    1 
ATOM   2399 C CA   . GLU   A 1 114 ? 27.284 -14.087 0.441   1.00 11.40 ?  114 GLU   A CA   1 
ATOM   2400 C C    . GLU   A 1 114 ? 28.130 -13.376 1.493   1.00 11.33 ?  114 GLU   A C    1 
ATOM   2401 O O    . GLU   A 1 114 ? 28.603 -14.007 2.447   1.00 11.63 ?  114 GLU   A O    1 
ATOM   2402 C CB   . GLU   A 1 114 ? 28.151 -14.729 -0.651  1.00 11.36 ?  114 GLU   A CB   1 
ATOM   2403 C CG   . GLU   A 1 114 ? 27.385 -15.778 -1.447  1.00 11.86 ?  114 GLU   A CG   1 
ATOM   2404 C CD   . GLU   A 1 114 ? 28.102 -16.319 -2.674  1.00 12.44 ?  114 GLU   A CD   1 
ATOM   2405 O OE1  . GLU   A 1 114 ? 29.059 -15.688 -3.169  1.00 12.56 ?  114 GLU   A OE1  1 
ATOM   2406 O OE2  . GLU   A 1 114 ? 27.660 -17.383 -3.163  1.00 13.44 -1 114 GLU   A OE2  1 
ATOM   2407 H H    . GLU   A 1 114 ? 26.350 -13.094 -1.015  1.00 13.48 ?  114 GLU   A H    1 
ATOM   2408 H HA   . GLU   A 1 114 ? 26.808 -14.800 0.885   1.00 13.70 ?  114 GLU   A HA   1 
ATOM   2409 H HB2  . GLU   A 1 114 ? 28.449 -14.046 -1.273  1.00 13.66 ?  114 GLU   A HB2  1 
ATOM   2410 H HB3  . GLU   A 1 114 ? 28.909 -15.166 -0.242  1.00 13.66 ?  114 GLU   A HB3  1 
ATOM   2411 H HG2  . GLU   A 1 114 ? 27.201 -16.531 -0.870  1.00 14.25 ?  114 GLU   A HG2  1 
ATOM   2412 H HG3  . GLU   A 1 114 ? 26.546 -15.387 -1.747  1.00 14.25 ?  114 GLU   A HG3  1 
ATOM   2413 N N    . ASN   A 1 115 ? 28.314 -12.059 1.360   1.00 11.13 ?  115 ASN   A N    1 
ATOM   2414 C CA   . ASN   A 1 115 ? 29.079 -11.331 2.368   1.00 11.68 ?  115 ASN   A CA   1 
ATOM   2415 C C    . ASN   A 1 115 ? 28.461 -11.464 3.756   1.00 11.33 ?  115 ASN   A C    1 
ATOM   2416 O O    . ASN   A 1 115 ? 29.172 -11.392 4.764   1.00 11.69 ?  115 ASN   A O    1 
ATOM   2417 C CB   . ASN   A 1 115 ? 29.176 -9.855  1.992   1.00 11.73 ?  115 ASN   A CB   1 
ATOM   2418 C CG   . ASN   A 1 115 ? 29.985 -9.628  0.738   1.00 12.36 ?  115 ASN   A CG   1 
ATOM   2419 O OD1  . ASN   A 1 115 ? 31.205 -9.719  0.765   1.00 15.70 ?  115 ASN   A OD1  1 
ATOM   2420 N ND2  . ASN   A 1 115 ? 29.317 -9.330  -0.364  1.00 11.75 ?  115 ASN   A ND2  1 
ATOM   2421 H H    . ASN   A 1 115 ? 28.006 -11.572 0.715   1.00 13.37 ?  115 ASN   A H    1 
ATOM   2422 H HA   . ASN   A 1 115 ? 29.974 -11.695 2.404   1.00 14.03 ?  115 ASN   A HA   1 
ATOM   2423 H HB2  . ASN   A 1 115 ? 28.283 -9.507  1.850   1.00 14.10 ?  115 ASN   A HB2  1 
ATOM   2424 H HB3  . ASN   A 1 115 ? 29.608 -9.378  2.719   1.00 14.10 ?  115 ASN   A HB3  1 
ATOM   2425 H HD21 . ASN   A 1 115 ? 29.737 -9.194  -1.102  1.00 14.12 ?  115 ASN   A HD21 1 
ATOM   2426 H HD22 . ASN   A 1 115 ? 28.456 -9.289  -0.347  1.00 14.12 ?  115 ASN   A HD22 1 
ATOM   2427 N N    . PHE   A 1 116 ? 27.134 -11.636 3.833   1.00 11.33 ?  116 PHE   A N    1 
ATOM   2428 C CA   . PHE   A 1 116 ? 26.479 -11.737 5.135   1.00 11.30 ?  116 PHE   A CA   1 
ATOM   2429 C C    . PHE   A 1 116 ? 26.955 -12.968 5.906   1.00 11.31 ?  116 PHE   A C    1 
ATOM   2430 O O    . PHE   A 1 116 ? 26.881 -12.990 7.136   1.00 12.01 ?  116 PHE   A O    1 
ATOM   2431 C CB   . PHE   A 1 116 ? 24.950 -11.863 4.991   1.00 11.34 ?  116 PHE   A CB   1 
ATOM   2432 C CG   . PHE   A 1 116 ? 24.198 -10.613 4.532   1.00 11.23 ?  116 PHE   A CG   1 
ATOM   2433 C CD1  . PHE   A 1 116 ? 24.776 -9.585  3.797   1.00 11.25 ?  116 PHE   A CD1  1 
ATOM   2434 C CD2  . PHE   A 1 116 ? 22.840 -10.511 4.843   1.00 11.84 ?  116 PHE   A CD2  1 
ATOM   2435 C CE1  . PHE   A 1 116 ? 24.010 -8.504  3.385   1.00 11.72 ?  116 PHE   A CE1  1 
ATOM   2436 C CE2  . PHE   A 1 116 ? 22.084 -9.434  4.440   1.00 11.81 ?  116 PHE   A CE2  1 
ATOM   2437 C CZ   . PHE   A 1 116 ? 22.662 -8.432  3.709   1.00 11.27 ?  116 PHE   A CZ   1 
ATOM   2438 H H    . PHE   A 1 116 ? 26.600 -11.687 3.155   1.00 13.61 ?  116 PHE   A H    1 
ATOM   2439 H HA   . PHE   A 1 116 ? 26.671 -10.945 5.660   1.00 13.59 ?  116 PHE   A HA   1 
ATOM   2440 H HB2  . PHE   A 1 116 ? 24.765 -12.566 4.345   1.00 13.63 ?  116 PHE   A HB2  1 
ATOM   2441 H HB3  . PHE   A 1 116 ? 24.588 -12.124 5.853   1.00 13.63 ?  116 PHE   A HB3  1 
ATOM   2442 H HD1  . PHE   A 1 116 ? 25.671 -9.640  3.569   1.00 13.52 ?  116 PHE   A HD1  1 
ATOM   2443 H HD2  . PHE   A 1 116 ? 22.430 -11.202 5.331   1.00 14.23 ?  116 PHE   A HD2  1 
ATOM   2444 H HE1  . PHE   A 1 116 ? 24.406 -7.821  2.899   1.00 14.09 ?  116 PHE   A HE1  1 
ATOM   2445 H HE2  . PHE   A 1 116 ? 21.180 -9.393  4.663   1.00 14.20 ?  116 PHE   A HE2  1 
ATOM   2446 H HZ   . PHE   A 1 116 ? 22.156 -7.698  3.449   1.00 13.55 ?  116 PHE   A HZ   1 
ATOM   2447 N N    . ASN   A 1 117 ? 27.402 -14.014 5.202   1.00 11.68 ?  117 ASN   A N    1 
ATOM   2448 C CA   . ASN   A 1 117 ? 27.769 -15.257 5.871   1.00 11.88 ?  117 ASN   A CA   1 
ATOM   2449 C C    . ASN   A 1 117 ? 29.029 -15.138 6.709   1.00 12.54 ?  117 ASN   A C    1 
ATOM   2450 O O    . ASN   A 1 117 ? 29.326 -16.061 7.477   1.00 13.51 ?  117 ASN   A O    1 
ATOM   2451 C CB   . ASN   A 1 117 ? 27.887 -16.383 4.850   1.00 12.15 ?  117 ASN   A CB   1 
ATOM   2452 C CG   . ASN   A 1 117 ? 26.536 -16.767 4.308   1.00 11.94 ?  117 ASN   A CG   1 
ATOM   2453 O OD1  . ASN   A 1 117 ? 25.552 -16.790 5.051   1.00 12.83 ?  117 ASN   A OD1  1 
ATOM   2454 N ND2  . ASN   A 1 117 ? 26.459 -17.022 3.019   1.00 11.98 ?  117 ASN   A ND2  1 
ATOM   2455 H H    . ASN   A 1 117 ? 27.490 -14.024 4.341   1.00 14.03 ?  117 ASN   A H    1 
ATOM   2456 H HA   . ASN   A 1 117 ? 27.042 -15.490 6.470   1.00 14.28 ?  117 ASN   A HA   1 
ATOM   2457 H HB2  . ASN   A 1 117 ? 28.437 -16.087 4.109   1.00 14.60 ?  117 ASN   A HB2  1 
ATOM   2458 H HB3  . ASN   A 1 117 ? 28.276 -17.157 5.278   1.00 14.60 ?  117 ASN   A HB3  1 
ATOM   2459 H HD21 . ASN   A 1 117 ? 25.705 -17.238 2.673   1.00 14.40 ?  117 ASN   A HD21 1 
ATOM   2460 H HD22 . ASN   A 1 117 ? 27.166 -16.982 2.534   1.00 14.40 ?  117 ASN   A HD22 1 
ATOM   2461 N N    . GLN   A 1 118 ? 29.755 -14.024 6.598   1.00 12.43 ?  118 GLN   A N    1 
ATOM   2462 C CA   . GLN   A 1 118 ? 30.934 -13.788 7.418   1.00 12.90 ?  118 GLN   A CA   1 
ATOM   2463 C C    . GLN   A 1 118 ? 30.589 -13.212 8.787   1.00 13.03 ?  118 GLN   A C    1 
ATOM   2464 O O    . GLN   A 1 118 ? 31.500 -12.923 9.572   1.00 14.47 ?  118 GLN   A O    1 
ATOM   2465 C CB   . GLN   A 1 118 ? 31.925 -12.885 6.675   1.00 13.24 ?  118 GLN   A CB   1 
ATOM   2466 C CG   . GLN   A 1 118 ? 32.390 -13.470 5.354   1.00 13.13 ?  118 GLN   A CG   1 
ATOM   2467 C CD   . GLN   A 1 118 ? 33.228 -14.726 5.534   1.00 13.66 ?  118 GLN   A CD   1 
ATOM   2468 O OE1  . GLN   A 1 118 ? 34.091 -14.788 6.420   1.00 14.59 ?  118 GLN   A OE1  1 
ATOM   2469 N NE2  . GLN   A 1 118 ? 32.978 -15.735 4.697   1.00 13.91 ?  118 GLN   A NE2  1 
ATOM   2470 H H    . GLN   A 1 118 ? 29.573 -13.378 6.048   1.00 14.94 ?  118 GLN   A H    1 
ATOM   2471 H HA   . GLN   A 1 118 ? 31.364 -14.643 7.564   1.00 15.50 ?  118 GLN   A HA   1 
ATOM   2472 H HB2  . GLN   A 1 118 ? 31.497 -12.033 6.497   1.00 15.90 ?  118 GLN   A HB2  1 
ATOM   2473 H HB3  . GLN   A 1 118 ? 32.702 -12.755 7.237   1.00 15.90 ?  118 GLN   A HB3  1 
ATOM   2474 H HG2  . GLN   A 1 118 ? 31.612 -13.693 4.812   1.00 15.78 ?  118 GLN   A HG2  1 
ATOM   2475 H HG3  . GLN   A 1 118 ? 32.932 -12.812 4.891   1.00 15.78 ?  118 GLN   A HG3  1 
ATOM   2476 H HE21 . GLN   A 1 118 ? 32.358 -15.659 4.095   1.00 16.71 ?  118 GLN   A HE21 1 
ATOM   2477 H HE22 . GLN   A 1 118 ? 33.415 -16.471 4.759   1.00 16.71 ?  118 GLN   A HE22 1 
ATOM   2478 N N    . HIS   A 1 119 ? 29.299 -13.061 9.096   1.00 12.63 ?  119 HIS   A N    1 
ATOM   2479 C CA   . HIS   A 1 119 ? 28.844 -12.454 10.340  1.00 12.87 ?  119 HIS   A CA   1 
ATOM   2480 C C    . HIS   A 1 119 ? 27.703 -13.276 10.911  1.00 13.28 ?  119 HIS   A C    1 
ATOM   2481 O O    . HIS   A 1 119 ? 26.759 -13.612 10.191  1.00 13.69 ?  119 HIS   A O    1 
ATOM   2482 C CB   . HIS   A 1 119 ? 28.389 -11.024 10.066  1.00 13.53 ?  119 HIS   A CB   1 
ATOM   2483 C CG   . HIS   A 1 119 ? 29.470 -10.214 9.449   1.00 14.84 ?  119 HIS   A CG   1 
ATOM   2484 N ND1  . HIS   A 1 119 ? 30.440 -9.593  10.200  1.00 17.17 ?  119 HIS   A ND1  1 
ATOM   2485 C CD2  . HIS   A 1 119 ? 29.807 -10.020 8.153   1.00 15.79 ?  119 HIS   A CD2  1 
ATOM   2486 C CE1  . HIS   A 1 119 ? 31.303 -9.007  9.391   1.00 17.04 ?  119 HIS   A CE1  1 
ATOM   2487 N NE2  . HIS   A 1 119 ? 30.950 -9.259  8.144   1.00 17.20 ?  119 HIS   A NE2  1 
ATOM   2488 H H    . HIS   A 1 119 ? 28.648 -13.318 8.588   1.00 15.18 ?  119 HIS   A H    1 
ATOM   2489 H HA   . HIS   A 1 119 ? 29.572 -12.442 10.983  1.00 15.47 ?  119 HIS   A HA   1 
ATOM   2490 H HB2  . HIS   A 1 119 ? 27.633 -11.048 9.460   1.00 16.26 ?  119 HIS   A HB2  1 
ATOM   2491 H HB3  . HIS   A 1 119 ? 28.135 -10.613 10.906  1.00 16.26 ?  119 HIS   A HB3  1 
ATOM   2492 H HD1  . HIS   A 1 119 ? 30.469 -9.578  11.059  1.00 20.62 ?  119 HIS   A HD1  1 
ATOM   2493 H HD2  . HIS   A 1 119 ? 29.342 -10.338 7.410   1.00 18.97 ?  119 HIS   A HD2  1 
ATOM   2494 H HE1  . HIS   A 1 119 ? 32.034 -8.500  9.652   1.00 20.47 ?  119 HIS   A HE1  1 
ATOM   2495 N N    . GLU   A 1 120 ? 27.785 -13.582 12.208  1.00 14.32 ?  120 GLU   A N    1 
ATOM   2496 C CA   . GLU   A 1 120 ? 26.829 -14.515 12.802  1.00 16.48 ?  120 GLU   A CA   1 
ATOM   2497 C C    . GLU   A 1 120 ? 25.413 -13.952 12.866  1.00 14.79 ?  120 GLU   A C    1 
ATOM   2498 O O    . GLU   A 1 120 ? 24.441 -14.715 12.757  1.00 14.92 ?  120 GLU   A O    1 
ATOM   2499 C CB   . GLU   A 1 120 ? 27.295 -14.926 14.199  1.00 22.10 ?  120 GLU   A CB   1 
ATOM   2500 C CG   . GLU   A 1 120 ? 28.506 -15.846 14.203  1.00 29.45 ?  120 GLU   A CG   1 
ATOM   2501 C CD   . GLU   A 1 120 ? 28.710 -16.538 15.536  1.00 36.51 ?  120 GLU   A CD   1 
ATOM   2502 O OE1  . GLU   A 1 120 ? 28.272 -15.987 16.569  1.00 38.42 ?  120 GLU   A OE1  1 
ATOM   2503 O OE2  . GLU   A 1 120 ? 29.304 -17.637 15.550  1.00 40.74 -1 120 GLU   A OE2  1 
ATOM   2504 H H    . GLU   A 1 120 ? 28.377 -13.270 12.757  1.00 17.21 ?  120 GLU   A H    1 
ATOM   2505 H HA   . GLU   A 1 120 ? 26.808 -15.319 12.265  1.00 19.80 ?  120 GLU   A HA   1 
ATOM   2506 H HB2  . GLU   A 1 120 ? 27.535 -14.136 14.707  1.00 26.54 ?  120 GLU   A HB2  1 
ATOM   2507 H HB3  . GLU   A 1 120 ? 26.575 -15.398 14.652  1.00 26.54 ?  120 GLU   A HB3  1 
ATOM   2508 H HG2  . GLU   A 1 120 ? 28.394 -16.527 13.521  1.00 35.36 ?  120 GLU   A HG2  1 
ATOM   2509 H HG3  . GLU   A 1 120 ? 29.306 -15.328 14.030  1.00 35.36 ?  120 GLU   A HG3  1 
ATOM   2510 N N    . VAL   A 1 121 ? 25.277 -12.643 13.082  1.00 14.21 ?  121 VAL   A N    1 
ATOM   2511 C CA   . VAL   A 1 121 ? 23.982 -11.975 13.200  1.00 14.26 ?  121 VAL   A CA   1 
ATOM   2512 C C    . VAL   A 1 121 ? 24.092 -10.594 12.560  1.00 13.03 ?  121 VAL   A C    1 
ATOM   2513 O O    . VAL   A 1 121 ? 25.063 -9.868  12.800  1.00 13.67 ?  121 VAL   A O    1 
ATOM   2514 C CB   . VAL   A 1 121 ? 23.542 -11.826 14.675  1.00 16.96 ?  121 VAL   A CB   1 
ATOM   2515 C CG1  . VAL   A 1 121 ? 22.147 -11.207 14.765  1.00 17.58 ?  121 VAL   A CG1  1 
ATOM   2516 C CG2  . VAL   A 1 121 ? 23.575 -13.153 15.415  1.00 18.94 ?  121 VAL   A CG2  1 
ATOM   2517 H H    . VAL   A 1 121 ? 25.943 -12.104 13.166  1.00 17.07 ?  121 VAL   A H    1 
ATOM   2518 H HA   . VAL   A 1 121 ? 23.309 -12.492 12.726  1.00 17.14 ?  121 VAL   A HA   1 
ATOM   2519 H HB   . VAL   A 1 121 ? 24.156 -11.229 15.122  1.00 20.37 ?  121 VAL   A HB   1 
ATOM   2520 H HG11 . VAL   A 1 121 ? 21.839 -11.252 15.687  1.00 21.12 ?  121 VAL   A HG11 1 
ATOM   2521 H HG12 . VAL   A 1 121 ? 22.189 -10.282 14.479  1.00 21.12 ?  121 VAL   A HG12 1 
ATOM   2522 H HG13 . VAL   A 1 121 ? 21.539 -11.704 14.194  1.00 21.12 ?  121 VAL   A HG13 1 
ATOM   2523 H HG21 . VAL   A 1 121 ? 23.227 -13.023 16.317  1.00 22.75 ?  121 VAL   A HG21 1 
ATOM   2524 H HG22 . VAL   A 1 121 ? 23.019 -13.797 14.945  1.00 22.75 ?  121 VAL   A HG22 1 
ATOM   2525 H HG23 . VAL   A 1 121 ? 24.487 -13.473 15.461  1.00 22.75 ?  121 VAL   A HG23 1 
ATOM   2526 N N    . LEU   A 1 122 ? 23.082 -10.209 11.773  1.00 12.47 ?  122 LEU   A N    1 
ATOM   2527 C CA   . LEU   A 1 122 ? 23.083 -8.913  11.099  1.00 12.24 ?  122 LEU   A CA   1 
ATOM   2528 C C    . LEU   A 1 122 ? 21.684 -8.321  11.071  1.00 12.25 ?  122 LEU   A C    1 
ATOM   2529 O O    . LEU   A 1 122 ? 20.694 -9.042  10.935  1.00 13.15 ?  122 LEU   A O    1 
ATOM   2530 C CB   . LEU   A 1 122 ? 23.509 -9.015  9.631   1.00 13.26 ?  122 LEU   A CB   1 
ATOM   2531 C CG   . LEU   A 1 122 ? 24.719 -9.870  9.282   1.00 13.39 ?  122 LEU   A CG   1 
ATOM   2532 C CD1  . LEU   A 1 122 ? 24.322 -11.315 9.055   1.00 14.46 ?  122 LEU   A CD1  1 
ATOM   2533 C CD2  . LEU   A 1 122 ? 25.417 -9.306  8.058   1.00 13.22 ?  122 LEU   A CD2  1 
ATOM   2534 H H    . LEU   A 1 122 ? 22.377 -10.685 11.610  1.00 14.98 ?  122 LEU   A H    1 
ATOM   2535 H HA   . LEU   A 1 122 ? 23.680 -8.300  11.558  1.00 14.70 ?  122 LEU   A HA   1 
ATOM   2536 H HB2  . LEU   A 1 122 ? 22.767 -9.373  9.128   1.00 15.93 ?  122 LEU   A HB2  1 
ATOM   2537 H HB3  . LEU   A 1 122 ? 23.709 -8.122  9.315   1.00 15.93 ?  122 LEU   A HB3  1 
ATOM   2538 H HG   . LEU   A 1 122 ? 25.355 -9.854  10.016  1.00 16.09 ?  122 LEU   A HG   1 
ATOM   2539 H HD11 . LEU   A 1 122 ? 25.101 -11.828 8.787   1.00 17.37 ?  122 LEU   A HD11 1 
ATOM   2540 H HD12 . LEU   A 1 122 ? 23.961 -11.679 9.881   1.00 17.37 ?  122 LEU   A HD12 1 
ATOM   2541 H HD13 . LEU   A 1 122 ? 23.647 -11.354 8.358   1.00 17.37 ?  122 LEU   A HD13 1 
ATOM   2542 H HD21 . LEU   A 1 122 ? 26.165 -9.885  7.817   1.00 15.88 ?  122 LEU   A HD21 1 
ATOM   2543 H HD22 . LEU   A 1 122 ? 24.789 -9.263  7.323   1.00 15.88 ?  122 LEU   A HD22 1 
ATOM   2544 H HD23 . LEU   A 1 122 ? 25.750 -8.418  8.264   1.00 15.88 ?  122 LEU   A HD23 1 
ATOM   2545 N N    . LEU   A 1 123 ? 21.621 -6.991  11.170  1.00 11.85 ?  123 LEU   A N    1 
ATOM   2546 C CA   . LEU   A 1 123 ? 20.450 -6.198  10.800  1.00 11.71 ?  123 LEU   A CA   1 
ATOM   2547 C C    . LEU   A 1 123 ? 20.704 -5.675  9.393   1.00 11.17 ?  123 LEU   A C    1 
ATOM   2548 O O    . LEU   A 1 123 ? 21.752 -5.069  9.151   1.00 11.99 ?  123 LEU   A O    1 
ATOM   2549 C CB   . LEU   A 1 123 ? 20.317 -5.022  11.768  1.00 12.21 ?  123 LEU   A CB   1 
ATOM   2550 C CG   . LEU   A 1 123 ? 19.271 -3.960  11.431  1.00 13.01 ?  123 LEU   A CG   1 
ATOM   2551 C CD1  . LEU   A 1 123 ? 17.875 -4.564  11.426  1.00 13.67 ?  123 LEU   A CD1  1 
ATOM   2552 C CD2  . LEU   A 1 123 ? 19.359 -2.788  12.408  1.00 13.93 ?  123 LEU   A CD2  1 
ATOM   2553 H H    . LEU   A 1 123 ? 22.276 -6.507  11.453  1.00 14.24 ?  123 LEU   A H    1 
ATOM   2554 H HA   . LEU   A 1 123 ? 19.647 -6.738  10.812  1.00 14.07 ?  123 LEU   A HA   1 
ATOM   2555 H HB2  . LEU   A 1 123 ? 20.086 -5.378  12.642  1.00 14.67 ?  123 LEU   A HB2  1 
ATOM   2556 H HB3  . LEU   A 1 123 ? 21.170 -4.571  11.821  1.00 14.67 ?  123 LEU   A HB3  1 
ATOM   2557 H HG   . LEU   A 1 123 ? 19.439 -3.611  10.540  1.00 15.63 ?  123 LEU   A HG   1 
ATOM   2558 H HD11 . LEU   A 1 123 ? 17.223 -3.869  11.257  1.00 16.42 ?  123 LEU   A HD11 1 
ATOM   2559 H HD12 . LEU   A 1 123 ? 17.824 -5.242  10.731  1.00 16.42 ?  123 LEU   A HD12 1 
ATOM   2560 H HD13 . LEU   A 1 123 ? 17.705 -4.973  12.292  1.00 16.42 ?  123 LEU   A HD13 1 
ATOM   2561 H HD21 . LEU   A 1 123 ? 18.686 -2.130  12.177  1.00 16.74 ?  123 LEU   A HD21 1 
ATOM   2562 H HD22 . LEU   A 1 123 ? 19.200 -3.121  13.308  1.00 16.74 ?  123 LEU   A HD22 1 
ATOM   2563 H HD23 . LEU   A 1 123 ? 20.242 -2.399  12.350  1.00 16.74 ?  123 LEU   A HD23 1 
ATOM   2564 N N    A ALA   A 1 124 ? 19.735 -5.838  8.488   0.72 10.73 ?  124 ALA   A N    1 
ATOM   2565 N N    B ALA   A 1 124 ? 19.796 -5.939  8.464   0.28 11.06 ?  124 ALA   A N    1 
ATOM   2566 C CA   A ALA   A 1 124 ? 20.008 -5.540  7.090   0.72 10.58 ?  124 ALA   A CA   1 
ATOM   2567 C CA   B ALA   A 1 124 ? 20.106 -5.703  7.064   0.28 11.29 ?  124 ALA   A CA   1 
ATOM   2568 C C    A ALA   A 1 124 ? 18.770 -5.098  6.324   0.72 10.37 ?  124 ALA   A C    1 
ATOM   2569 C C    B ALA   A 1 124 ? 18.876 -5.219  6.316   0.28 10.95 ?  124 ALA   A C    1 
ATOM   2570 O O    A ALA   A 1 124 ? 17.643 -5.484  6.668   0.72 11.46 ?  124 ALA   A O    1 
ATOM   2571 O O    B ALA   A 1 124 ? 17.741 -5.470  6.737   0.28 11.25 ?  124 ALA   A O    1 
ATOM   2572 C CB   A ALA   A 1 124 ? 20.609 -6.762  6.385   0.72 10.79 ?  124 ALA   A CB   1 
ATOM   2573 C CB   B ALA   A 1 124 ? 20.643 -6.973  6.391   0.28 11.78 ?  124 ALA   A CB   1 
ATOM   2574 H H    A ALA   A 1 124 ? 18.934 -6.106  8.656   0.72 12.89 ?  124 ALA   A H    1 
ATOM   2575 H H    B ALA   A 1 124 ? 19.002 -6.247  8.612   0.28 13.30 ?  124 ALA   A H    1 
ATOM   2576 H HA   A ALA   A 1 124 ? 20.665 -4.829  7.056   0.72 12.71 ?  124 ALA   A HA   1 
ATOM   2577 H HA   B ALA   A 1 124 ? 20.793 -5.023  7.010   0.28 13.57 ?  124 ALA   A HA   1 
ATOM   2578 H HB1  A ALA   A 1 124 ? 20.788 -6.538  5.457   0.72 12.96 ?  124 ALA   A HB1  1 
ATOM   2579 H HB1  B ALA   A 1 124 ? 20.846 -6.780  5.461   0.28 14.15 ?  124 ALA   A HB1  1 
ATOM   2580 H HB2  A ALA   A 1 124 ? 21.442 -7.006  6.827   0.72 12.96 ?  124 ALA   A HB2  1 
ATOM   2581 H HB2  B ALA   A 1 124 ? 21.451 -7.259  6.850   0.28 14.15 ?  124 ALA   A HB2  1 
ATOM   2582 H HB3  A ALA   A 1 124 ? 19.984 -7.499  6.434   0.72 12.96 ?  124 ALA   A HB3  1 
ATOM   2583 H HB3  B ALA   A 1 124 ? 19.971 -7.670  6.445   0.28 14.15 ?  124 ALA   A HB3  1 
ATOM   2584 N N    A PRO   A 1 125 ? 18.962 -4.332  5.253   0.72 10.58 ?  125 PRO   A N    1 
ATOM   2585 N N    B PRO   A 1 125 ? 19.074 -4.521  5.192   0.28 10.34 ?  125 PRO   A N    1 
ATOM   2586 C CA   A PRO   A 1 125 ? 17.917 -4.113  4.254   0.72 11.09 ?  125 PRO   A CA   1 
ATOM   2587 C CA   B PRO   A 1 125 ? 17.951 -4.163  4.322   0.28 10.82 ?  125 PRO   A CA   1 
ATOM   2588 C C    A PRO   A 1 125 ? 17.982 -5.202  3.186   0.72 10.81 ?  125 PRO   A C    1 
ATOM   2589 C C    B PRO   A 1 125 ? 17.892 -5.103  3.130   0.28 11.16 ?  125 PRO   A C    1 
ATOM   2590 O O    A PRO   A 1 125 ? 18.961 -5.944  3.079   0.72 11.04 ?  125 PRO   A O    1 
ATOM   2591 O O    B PRO   A 1 125 ? 18.771 -5.958  2.978   0.28 11.58 ?  125 PRO   A O    1 
ATOM   2592 C CB   A PRO   A 1 125 ? 18.355 -2.778  3.639   0.72 11.24 ?  125 PRO   A CB   1 
ATOM   2593 C CB   B PRO   A 1 125 ? 18.328 -2.750  3.875   0.28 10.75 ?  125 PRO   A CB   1 
ATOM   2594 C CG   A PRO   A 1 125 ? 19.862 -2.926  3.592   0.72 11.47 ?  125 PRO   A CG   1 
ATOM   2595 C CG   B PRO   A 1 125 ? 19.842 -2.831  3.741   0.28 10.70 ?  125 PRO   A CG   1 
ATOM   2596 C CD   A PRO   A 1 125 ? 20.210 -3.623  4.899   0.72 11.22 ?  125 PRO   A CD   1 
ATOM   2597 C CD   B PRO   A 1 125 ? 20.326 -3.895  4.724   0.28 9.95  ?  125 PRO   A CD   1 
ATOM   2598 H HA   A PRO   A 1 125 ? 17.029 -4.053  4.647   0.72 13.32 ?  125 PRO   A HA   1 
ATOM   2599 H HA   B PRO   A 1 125 ? 17.108 -4.158  4.807   0.28 13.00 ?  125 PRO   A HA   1 
ATOM   2600 H HB2  A PRO   A 1 125 ? 17.975 -2.679  2.750   0.72 13.51 ?  125 PRO   A HB2  1 
ATOM   2601 H HB2  B PRO   A 1 125 ? 17.910 -2.549  3.021   0.28 12.92 ?  125 PRO   A HB2  1 
ATOM   2602 H HB3  A PRO   A 1 125 ? 18.085 -2.042  4.216   0.72 13.51 ?  125 PRO   A HB3  1 
ATOM   2603 H HB3  B PRO   A 1 125 ? 18.066 -2.104  4.551   0.28 12.92 ?  125 PRO   A HB3  1 
ATOM   2604 H HG2  A PRO   A 1 125 ? 20.115 -3.473  2.832   0.72 13.79 ?  125 PRO   A HG2  1 
ATOM   2605 H HG2  B PRO   A 1 125 ? 20.070 -3.081  2.833   0.28 12.86 ?  125 PRO   A HG2  1 
ATOM   2606 H HG3  A PRO   A 1 125 ? 20.275 -2.050  3.542   0.72 13.79 ?  125 PRO   A HG3  1 
ATOM   2607 H HG3  B PRO   A 1 125 ? 20.229 -1.970  3.961   0.28 12.86 ?  125 PRO   A HG3  1 
ATOM   2608 H HD2  A PRO   A 1 125 ? 20.933 -4.247  4.771   0.72 13.49 ?  125 PRO   A HD2  1 
ATOM   2609 H HD2  B PRO   A 1 125 ? 20.887 -4.545  4.269   0.28 11.96 ?  125 PRO   A HD2  1 
ATOM   2610 H HD3  A PRO   A 1 125 ? 20.423 -2.962  5.585   0.72 13.49 ?  125 PRO   A HD3  1 
ATOM   2611 H HD3  B PRO   A 1 125 ? 20.794 -3.477  5.463   0.28 11.96 ?  125 PRO   A HD3  1 
ATOM   2612 N N    A LEU   A 1 126 ? 16.930 -5.257  2.369   0.72 10.88 ?  126 LEU   A N    1 
ATOM   2613 N N    B LEU   A 1 126 ? 16.892 -4.946  2.268   0.28 11.44 ?  126 LEU   A N    1 
ATOM   2614 C CA   A LEU   A 1 126 ? 16.954 -6.081  1.168   0.72 10.88 ?  126 LEU   A CA   1 
ATOM   2615 C CA   B LEU   A 1 126 ? 16.792 -5.767  1.062   0.28 11.22 ?  126 LEU   A CA   1 
ATOM   2616 C C    A LEU   A 1 126 ? 17.886 -5.459  0.132   0.72 10.78 ?  126 LEU   A C    1 
ATOM   2617 C C    B LEU   A 1 126 ? 17.740 -5.204  0.010   0.28 10.83 ?  126 LEU   A C    1 
ATOM   2618 O O    A LEU   A 1 126 ? 17.682 -4.322  -0.306  0.72 11.65 ?  126 LEU   A O    1 
ATOM   2619 O O    B LEU   A 1 126 ? 17.429 -4.221  -0.667  0.28 10.99 ?  126 LEU   A O    1 
ATOM   2620 C CB   A LEU   A 1 126 ? 15.545 -6.232  0.605   0.72 11.44 ?  126 LEU   A CB   1 
ATOM   2621 C CB   B LEU   A 1 126 ? 15.361 -5.787  0.543   0.28 12.20 ?  126 LEU   A CB   1 
ATOM   2622 C CG   A LEU   A 1 126 ? 14.628 -7.171  1.389   0.72 11.90 ?  126 LEU   A CG   1 
ATOM   2623 C CG   B LEU   A 1 126 ? 14.351 -6.636  1.313   0.28 12.60 ?  126 LEU   A CG   1 
ATOM   2624 C CD1  A LEU   A 1 126 ? 13.205 -7.037  0.895   0.72 13.28 ?  126 LEU   A CD1  1 
ATOM   2625 C CD1  B LEU   A 1 126 ? 12.975 -6.474  0.693   0.28 12.82 ?  126 LEU   A CD1  1 
ATOM   2626 C CD2  A LEU   A 1 126 ? 15.103 -8.616  1.267   0.72 12.02 ?  126 LEU   A CD2  1 
ATOM   2627 C CD2  B LEU   A 1 126 ? 14.756 -8.099  1.326   0.28 12.76 ?  126 LEU   A CD2  1 
ATOM   2628 H H    A LEU   A 1 126 ? 16.197 -4.821  2.484   0.72 13.08 ?  126 LEU   A H    1 
ATOM   2629 H H    B LEU   A 1 126 ? 16.256 -4.369  2.362   0.28 13.75 ?  126 LEU   A H    1 
ATOM   2630 H HA   A LEU   A 1 126 ? 17.291 -6.960  1.388   0.72 13.08 ?  126 LEU   A HA   1 
ATOM   2631 H HA   B LEU   A 1 126 ? 17.063 -6.676  1.272   0.28 13.48 ?  126 LEU   A HA   1 
ATOM   2632 H HB2  A LEU   A 1 126 ? 15.120 -5.359  0.594   0.72 13.74 ?  126 LEU   A HB2  1 
ATOM   2633 H HB2  B LEU   A 1 126 ? 15.028 -4.877  0.545   0.28 14.66 ?  126 LEU   A HB2  1 
ATOM   2634 H HB3  A LEU   A 1 126 ? 15.605 -6.573  -0.300  0.72 13.74 ?  126 LEU   A HB3  1 
ATOM   2635 H HB3  B LEU   A 1 126 ? 15.379 -6.121  -0.365  0.28 14.66 ?  126 LEU   A HB3  1 
ATOM   2636 H HG   A LEU   A 1 126 ? 14.644 -6.928  2.327   0.72 14.30 ?  126 LEU   A HG   1 
ATOM   2637 H HG   B LEU   A 1 126 ? 14.303 -6.324  2.230   0.28 15.14 ?  126 LEU   A HG   1 
ATOM   2638 H HD11 A LEU   A 1 126 ? 12.635 -7.642  1.397   0.72 15.96 ?  126 LEU   A HD11 1 
ATOM   2639 H HD11 B LEU   A 1 126 ? 12.342 -7.024  1.182   0.28 15.41 ?  126 LEU   A HD11 1 
ATOM   2640 H HD12 A LEU   A 1 126 ? 12.910 -6.123  1.024   0.72 15.96 ?  126 LEU   A HD12 1 
ATOM   2641 H HD12 B LEU   A 1 126 ? 12.712 -5.542  0.741   0.28 15.41 ?  126 LEU   A HD12 1 
ATOM   2642 H HD13 A LEU   A 1 126 ? 13.174 -7.264  -0.049  0.72 15.96 ?  126 LEU   A HD13 1 
ATOM   2643 H HD13 B LEU   A 1 126 ? 13.011 -6.760  -0.234  0.28 15.41 ?  126 LEU   A HD13 1 
ATOM   2644 H HD21 A LEU   A 1 126 ? 14.433 -9.206  1.647   0.72 14.44 ?  126 LEU   A HD21 1 
ATOM   2645 H HD21 B LEU   A 1 126 ? 14.018 -8.626  1.671   0.28 15.33 ?  126 LEU   A HD21 1 
ATOM   2646 H HD22 A LEU   A 1 126 ? 15.237 -8.828  0.330   0.72 14.44 ?  126 LEU   A HD22 1 
ATOM   2647 H HD22 B LEU   A 1 126 ? 14.966 -8.374  0.421   0.28 15.33 ?  126 LEU   A HD22 1 
ATOM   2648 H HD23 A LEU   A 1 126 ? 15.940 -8.717  1.750   0.72 14.44 ?  126 LEU   A HD23 1 
ATOM   2649 H HD23 B LEU   A 1 126 ? 15.533 -8.204  1.894   0.28 15.33 ?  126 LEU   A HD23 1 
ATOM   2650 N N    A LEU   A 1 127 ? 18.915 -6.207  -0.258  0.72 10.88 ?  127 LEU   A N    1 
ATOM   2651 N N    B LEU   A 1 127 ? 18.903 -5.833  -0.139  0.28 10.49 ?  127 LEU   A N    1 
ATOM   2652 C CA   A LEU   A 1 127 ? 19.903 -5.693  -1.194  0.72 10.72 ?  127 LEU   A CA   1 
ATOM   2653 C CA   B LEU   A 1 127 ? 19.887 -5.340  -1.091  0.28 10.45 ?  127 LEU   A CA   1 
ATOM   2654 C C    A LEU   A 1 127 ? 19.291 -5.498  -2.572  0.72 10.50 ?  127 LEU   A C    1 
ATOM   2655 C C    B LEU   A 1 127 ? 19.315 -5.304  -2.502  0.28 10.80 ?  127 LEU   A C    1 
ATOM   2656 O O    A LEU   A 1 127 ? 18.460 -6.289  -3.032  0.72 10.90 ?  127 LEU   A O    1 
ATOM   2657 O O    B LEU   A 1 127 ? 18.517 -6.159  -2.897  0.28 11.17 ?  127 LEU   A O    1 
ATOM   2658 C CB   A LEU   A 1 127 ? 21.091 -6.650  -1.281  0.72 11.24 ?  127 LEU   A CB   1 
ATOM   2659 C CB   B LEU   A 1 127 ? 21.130 -6.224  -1.062  0.28 10.69 ?  127 LEU   A CB   1 
ATOM   2660 C CG   A LEU   A 1 127 ? 21.889 -6.859  0.008   0.72 11.90 ?  127 LEU   A CG   1 
ATOM   2661 C CG   B LEU   A 1 127 ? 21.929 -6.168  0.241   0.28 10.94 ?  127 LEU   A CG   1 
ATOM   2662 C CD1  A LEU   A 1 127 ? 22.994 -7.867  -0.231  0.72 12.15 ?  127 LEU   A CD1  1 
ATOM   2663 C CD1  B LEU   A 1 127 ? 23.067 -7.166  0.194   0.28 11.47 ?  127 LEU   A CD1  1 
ATOM   2664 C CD2  A LEU   A 1 127 ? 22.482 -5.556  0.514   0.72 12.50 ?  127 LEU   A CD2  1 
ATOM   2665 C CD2  B LEU   A 1 127 ? 22.451 -4.755  0.505   0.28 11.11 ?  127 LEU   A CD2  1 
ATOM   2666 H H    A LEU   A 1 127 ? 19.066 -7.012  0.014   0.72 13.08 ?  127 LEU   A H    1 
ATOM   2667 H H    B LEU   A 1 127 ? 19.146 -6.530  0.307   0.28 12.60 ?  127 LEU   A H    1 
ATOM   2668 H HA   A LEU   A 1 127 ? 20.228 -4.838  -0.878  0.72 12.88 ?  127 LEU   A HA   1 
ATOM   2669 H HA   B LEU   A 1 127 ? 20.144 -4.436  -0.840  0.28 12.56 ?  127 LEU   A HA   1 
ATOM   2670 H HB2  A LEU   A 1 127 ? 20.765 -7.520  -1.558  0.72 13.51 ?  127 LEU   A HB2  1 
ATOM   2671 H HB2  B LEU   A 1 127 ? 20.855 -7.143  -1.204  0.28 12.85 ?  127 LEU   A HB2  1 
ATOM   2672 H HB3  A LEU   A 1 127 ? 21.709 -6.311  -1.948  0.72 13.51 ?  127 LEU   A HB3  1 
ATOM   2673 H HB3  B LEU   A 1 127 ? 21.717 -5.945  -1.783  0.28 12.85 ?  127 LEU   A HB3  1 
ATOM   2674 H HG   A LEU   A 1 127 ? 21.300 -7.208  0.698   0.72 14.30 ?  127 LEU   A HG   1 
ATOM   2675 H HG   B LEU   A 1 127 ? 21.346 -6.413  0.975   0.28 13.15 ?  127 LEU   A HG   1 
ATOM   2676 H HD11 A LEU   A 1 127 ? 23.475 -8.011  0.600   0.72 14.60 ?  127 LEU   A HD11 1 
ATOM   2677 H HD11 B LEU   A 1 127 ? 23.599 -7.071  0.997   0.28 13.78 ?  127 LEU   A HD11 1 
ATOM   2678 H HD12 A LEU   A 1 127 ? 22.600 -8.698  -0.535  0.72 14.60 ?  127 LEU   A HD12 1 
ATOM   2679 H HD12 B LEU   A 1 127 ? 22.695 -8.062  0.145   0.28 13.78 ?  127 LEU   A HD12 1 
ATOM   2680 H HD13 A LEU   A 1 127 ? 23.596 -7.517  -0.906  0.72 14.60 ?  127 LEU   A HD13 1 
ATOM   2681 H HD13 B LEU   A 1 127 ? 23.609 -6.988  -0.589  0.28 13.78 ?  127 LEU   A HD13 1 
ATOM   2682 H HD21 A LEU   A 1 127 ? 23.073 -5.744  1.259   0.72 15.02 ?  127 LEU   A HD21 1 
ATOM   2683 H HD21 B LEU   A 1 127 ? 23.098 -4.789  1.227   0.28 13.36 ?  127 LEU   A HD21 1 
ATOM   2684 H HD22 A LEU   A 1 127 ? 22.983 -5.138  -0.207  0.72 15.02 ?  127 LEU   A HD22 1 
ATOM   2685 H HD22 B LEU   A 1 127 ? 22.872 -4.418  -0.301  0.28 13.36 ?  127 LEU   A HD22 1 
ATOM   2686 H HD23 A LEU   A 1 127 ? 21.765 -4.968  0.799   0.72 15.02 ?  127 LEU   A HD23 1 
ATOM   2687 H HD23 B LEU   A 1 127 ? 21.708 -4.183  0.753   0.28 13.36 ?  127 LEU   A HD23 1 
ATOM   2688 N N    A SER   A 1 128 ? 19.721 -4.431  -3.235  0.72 10.53 ?  128 SER   A N    1 
ATOM   2689 N N    B SER   A 1 128 ? 19.737 -4.294  -3.258  0.28 10.85 ?  128 SER   A N    1 
ATOM   2690 C CA   A SER   A 1 128 ? 19.313 -4.039  -4.575  0.72 11.12 ?  128 SER   A CA   1 
ATOM   2691 C CA   B SER   A 1 128 ? 19.384 -4.030  -4.650  0.28 10.74 ?  128 SER   A CA   1 
ATOM   2692 C C    A SER   A 1 128 ? 17.855 -3.597  -4.661  0.72 11.46 ?  128 SER   A C    1 
ATOM   2693 C C    B SER   A 1 128 ? 17.945 -3.567  -4.847  0.28 10.42 ?  128 SER   A C    1 
ATOM   2694 O O    A SER   A 1 128 ? 17.392 -3.288  -5.758  0.72 12.72 ?  128 SER   A O    1 
ATOM   2695 O O    B SER   A 1 128 ? 17.582 -3.206  -5.971  0.28 10.66 ?  128 SER   A O    1 
ATOM   2696 C CB   A SER   A 1 128 ? 19.640 -5.094  -5.643  0.72 11.35 ?  128 SER   A CB   1 
ATOM   2697 C CB   B SER   A 1 128 ? 19.714 -5.187  -5.602  0.28 10.74 ?  128 SER   A CB   1 
ATOM   2698 O OG   A SER   A 1 128 ? 21.047 -5.301  -5.721  0.72 12.06 ?  128 SER   A OG   1 
ATOM   2699 O OG   B SER   A 1 128 ? 21.119 -5.341  -5.736  0.28 11.04 ?  128 SER   A OG   1 
ATOM   2700 H H    A SER   A 1 128 ? 20.306 -3.886  -2.906  0.72 12.65 ?  128 SER   A H    1 
ATOM   2701 H H    B SER   A 1 128 ? 20.283 -3.703  -2.952  0.28 13.03 ?  128 SER   A H    1 
ATOM   2702 H HA   A SER   A 1 128 ? 19.839 -3.263  -4.809  0.72 13.36 ?  128 SER   A HA   1 
ATOM   2703 H HA   B SER   A 1 128 ? 19.934 -3.290  -4.931  0.28 12.91 ?  128 SER   A HA   1 
ATOM   2704 H HB2  A SER   A 1 128 ? 19.204 -5.928  -5.412  0.72 13.64 ?  128 SER   A HB2  1 
ATOM   2705 H HB2  B SER   A 1 128 ? 19.334 -6.004  -5.252  0.28 12.91 ?  128 SER   A HB2  1 
ATOM   2706 H HB3  A SER   A 1 128 ? 19.311 -4.780  -6.506  0.72 13.64 ?  128 SER   A HB3  1 
ATOM   2707 H HB3  B SER   A 1 128 ? 19.334 -4.988  -6.475  0.28 12.91 ?  128 SER   A HB3  1 
ATOM   2708 H HG   A SER   A 1 128 ? 21.427 -4.580  -5.927  0.72 14.49 ?  128 SER   A HG   1 
ATOM   2709 H HG   B SER   A 1 128 ? 21.453 -4.626  -6.028  0.28 13.26 ?  128 SER   A HG   1 
ATOM   2710 N N    A ALA   A 1 129 ? 17.130 -3.534  -3.544  0.72 11.99 ?  129 ALA   A N    1 
ATOM   2711 N N    B ALA   A 1 129 ? 17.124 -3.545  -3.800  0.28 10.67 ?  129 ALA   A N    1 
ATOM   2712 C CA   A ALA   A 1 129 ? 15.753 -3.059  -3.542  0.72 12.03 ?  129 ALA   A CA   1 
ATOM   2713 C CA   B ALA   A 1 129 ? 15.774 -3.007  -3.890  0.28 10.91 ?  129 ALA   A CA   1 
ATOM   2714 C C    A ALA   A 1 129 ? 15.723 -1.531  -3.510  0.72 11.96 ?  129 ALA   A C    1 
ATOM   2715 C C    B ALA   A 1 129 ? 15.834 -1.489  -3.717  0.28 11.43 ?  129 ALA   A C    1 
ATOM   2716 O O    A ALA   A 1 129 ? 16.754 -0.854  -3.585  0.72 11.94 ?  129 ALA   A O    1 
ATOM   2717 O O    B ALA   A 1 129 ? 16.909 -0.884  -3.680  0.28 11.49 ?  129 ALA   A O    1 
ATOM   2718 C CB   A ALA   A 1 129 ? 14.981 -3.660  -2.366  0.72 13.08 ?  129 ALA   A CB   1 
ATOM   2719 C CB   B ALA   A 1 129 ? 14.862 -3.695  -2.877  0.28 11.11 ?  129 ALA   A CB   1 
ATOM   2720 H H    A ALA   A 1 129 ? 17.417 -3.765  -2.766  0.72 14.41 ?  129 ALA   A H    1 
ATOM   2721 H H    B ALA   A 1 129 ? 17.328 -3.833  -3.017  0.28 12.82 ?  129 ALA   A H    1 
ATOM   2722 H HA   A ALA   A 1 129 ? 15.322 -3.347  -4.359  0.72 14.45 ?  129 ALA   A HA   1 
ATOM   2723 H HA   B ALA   A 1 129 ? 15.424 -3.183  -4.774  0.28 13.11 ?  129 ALA   A HA   1 
ATOM   2724 H HB1  A ALA   A 1 129 ? 14.063 -3.341  -2.395  0.72 15.71 ?  129 ALA   A HB1  1 
ATOM   2725 H HB1  B ALA   A 1 129 ? 13.974 -3.309  -2.940  0.28 13.35 ?  129 ALA   A HB1  1 
ATOM   2726 H HB2  A ALA   A 1 129 ? 14.996 -4.625  -2.437  0.72 15.71 ?  129 ALA   A HB2  1 
ATOM   2727 H HB2  B ALA   A 1 129 ? 14.828 -4.642  -3.076  0.28 13.35 ?  129 ALA   A HB2  1 
ATOM   2728 H HB3  A ALA   A 1 129 ? 15.399 -3.381  -1.536  0.72 15.71 ?  129 ALA   A HB3  1 
ATOM   2729 H HB3  B ALA   A 1 129 ? 15.218 -3.556  -1.985  0.28 13.35 ?  129 ALA   A HB3  1 
ATOM   2730 N N    A GLY   A 1 130 ? 14.518 -0.979  -3.421  0.72 12.58 ?  130 GLY   A N    1 
ATOM   2731 N N    B GLY   A 1 130 ? 14.674 -0.851  -3.621  0.28 11.87 ?  130 GLY   A N    1 
ATOM   2732 C CA   A GLY   A 1 130 ? 14.381 0.467   -3.380  0.72 12.77 ?  130 GLY   A CA   1 
ATOM   2733 C CA   B GLY   A 1 130 ? 14.666 0.595   -3.483  0.28 12.18 ?  130 GLY   A CA   1 
ATOM   2734 C C    A GLY   A 1 130 ? 14.995 1.113   -4.603  0.72 12.02 ?  130 GLY   A C    1 
ATOM   2735 C C    B GLY   A 1 130 ? 15.282 1.239   -4.709  0.28 12.41 ?  130 GLY   A C    1 
ATOM   2736 O O    A GLY   A 1 130 ? 14.781 0.668   -5.735  0.72 12.47 ?  130 GLY   A O    1 
ATOM   2737 O O    B GLY   A 1 130 ? 15.003 0.852   -5.849  0.28 12.94 ?  130 GLY   A O    1 
ATOM   2738 H H    A GLY   A 1 130 ? 13.776 -1.412  -3.386  0.72 15.11 ?  130 GLY   A H    1 
ATOM   2739 H H    B GLY   A 1 130 ? 13.899 -1.220  -3.645  0.28 14.26 ?  130 GLY   A H    1 
ATOM   2740 H HA2  A GLY   A 1 130 ? 13.439 0.706   -3.345  0.72 15.35 ?  130 GLY   A HA2  1 
ATOM   2741 H HA2  B GLY   A 1 130 ? 13.754 0.911   -3.369  0.28 14.64 ?  130 GLY   A HA2  1 
ATOM   2742 H HA3  A GLY   A 1 130 ? 14.821 0.819   -2.597  0.72 15.35 ?  130 GLY   A HA3  1 
ATOM   2743 H HA3  B GLY   A 1 130 ? 15.185 0.861   -2.707  0.28 14.64 ?  130 GLY   A HA3  1 
ATOM   2744 N N    A ILE   A 1 131 ? 15.765 2.186   -4.377  0.72 11.93 ?  131 ILE   A N    1 
ATOM   2745 N N    B ILE   A 1 131 ? 16.160 2.219   -4.477  0.28 12.18 ?  131 ILE   A N    1 
ATOM   2746 C CA   A ILE   A 1 131 ? 16.328 2.965   -5.478  0.72 11.75 ?  131 ILE   A CA   1 
ATOM   2747 C CA   B ILE   A 1 131 ? 16.737 2.994   -5.571  0.28 12.06 ?  131 ILE   A CA   1 
ATOM   2748 C C    A ILE   A 1 131 ? 17.370 2.206   -6.292  0.72 11.71 ?  131 ILE   A C    1 
ATOM   2749 C C    B ILE   A 1 131 ? 17.707 2.198   -6.430  0.28 11.82 ?  131 ILE   A C    1 
ATOM   2750 O O    A ILE   A 1 131 ? 17.776 2.700   -7.350  0.72 12.76 ?  131 ILE   A O    1 
ATOM   2751 O O    B ILE   A 1 131 ? 18.145 2.704   -7.472  0.28 12.27 ?  131 ILE   A O    1 
ATOM   2752 C CB   A ILE   A 1 131 ? 16.856 4.346   -5.023  0.72 12.72 ?  131 ILE   A CB   1 
ATOM   2753 C CB   B ILE   A 1 131 ? 17.395 4.294   -5.059  0.28 12.23 ?  131 ILE   A CB   1 
ATOM   2754 C CG1  A ILE   A 1 131 ? 18.085 4.214   -4.114  0.72 13.97 ?  131 ILE   A CG1  1 
ATOM   2755 C CG1  B ILE   A 1 131 ? 18.603 3.987   -4.168  0.28 12.62 ?  131 ILE   A CG1  1 
ATOM   2756 C CG2  A ILE   A 1 131 ? 15.745 5.143   -4.340  0.72 13.54 ?  131 ILE   A CG2  1 
ATOM   2757 C CG2  B ILE   A 1 131 ? 16.375 5.143   -4.310  0.28 12.11 ?  131 ILE   A CG2  1 
ATOM   2758 C CD1  A ILE   A 1 131 ? 18.696 5.555   -3.715  0.72 15.38 ?  131 ILE   A CD1  1 
ATOM   2759 C CD1  B ILE   A 1 131 ? 19.314 5.233   -3.636  0.28 12.82 ?  131 ILE   A CD1  1 
ATOM   2760 H H    A ILE   A 1 131 ? 15.957 2.489   -3.592  0.72 14.33 ?  131 ILE   A H    1 
ATOM   2761 H H    B ILE   A 1 131 ? 16.437 2.446   -3.697  0.28 14.64 ?  131 ILE   A H    1 
ATOM   2762 H HA   A ILE   A 1 131 ? 15.605 3.154   -6.087  0.72 14.12 ?  131 ILE   A HA   1 
ATOM   2763 H HA   B ILE   A 1 131 ? 16.019 3.259   -6.155  0.28 14.49 ?  131 ILE   A HA   1 
ATOM   2764 H HB   A ILE   A 1 131 ? 17.125 4.836   -5.812  0.72 15.29 ?  131 ILE   A HB   1 
ATOM   2765 H HB   B ILE   A 1 131 ? 17.704 4.799   -5.827  0.28 14.70 ?  131 ILE   A HB   1 
ATOM   2766 H HG12 A ILE   A 1 131 ? 17.830 3.752   -3.300  0.72 16.78 ?  131 ILE   A HG12 1 
ATOM   2767 H HG12 B ILE   A 1 131 ? 18.308 3.470   -3.405  0.28 15.16 ?  131 ILE   A HG12 1 
ATOM   2768 H HG13 A ILE   A 1 131 ? 18.770 3.709   -4.579  0.72 16.78 ?  131 ILE   A HG13 1 
ATOM   2769 H HG13 B ILE   A 1 131 ? 19.253 3.481   -4.679  0.28 15.16 ?  131 ILE   A HG13 1 
ATOM   2770 H HG21 A ILE   A 1 131 ? 16.042 6.058   -4.207  0.72 16.26 ?  131 ILE   A HG21 1 
ATOM   2771 H HG21 B ILE   A 1 131 ? 16.749 6.025   -4.156  0.28 14.55 ?  131 ILE   A HG21 1 
ATOM   2772 H HG22 A ILE   A 1 131 ? 14.957 5.132   -4.905  0.72 16.26 ?  131 ILE   A HG22 1 
ATOM   2773 H HG22 B ILE   A 1 131 ? 15.571 5.214   -4.847  0.28 14.55 ?  131 ILE   A HG22 1 
ATOM   2774 H HG23 A ILE   A 1 131 ? 15.541 4.734   -3.483  0.72 16.26 ?  131 ILE   A HG23 1 
ATOM   2775 H HG23 B ILE   A 1 131 ? 16.171 4.716   -3.463  0.28 14.55 ?  131 ILE   A HG23 1 
ATOM   2776 H HD11 A ILE   A 1 131 ? 19.533 5.396   -3.249  0.72 18.48 ?  131 ILE   A HD11 1 
ATOM   2777 H HD11 B ILE   A 1 131 ? 20.137 4.966   -3.195  0.28 15.40 ?  131 ILE   A HD11 1 
ATOM   2778 H HD12 A ILE   A 1 131 ? 18.859 6.079   -4.515  0.72 18.48 ?  131 ILE   A HD12 1 
ATOM   2779 H HD12 B ILE   A 1 131 ? 19.517 5.826   -4.378  0.28 15.40 ?  131 ILE   A HD12 1 
ATOM   2780 H HD13 A ILE   A 1 131 ? 18.079 6.025   -3.132  0.72 18.48 ?  131 ILE   A HD13 1 
ATOM   2781 H HD13 B ILE   A 1 131 ? 18.735 5.687   -3.002  0.28 15.40 ?  131 ILE   A HD13 1 
ATOM   2782 N N    A PHE   A 1 132 ? 17.803 1.014   -5.850  0.72 11.71 ?  132 PHE   A N    1 
ATOM   2783 N N    B PHE   A 1 132 ? 18.054 0.968   -6.036  0.28 11.70 ?  132 PHE   A N    1 
ATOM   2784 C CA   A PHE   A 1 132 ? 18.675 0.178   -6.673  0.72 11.48 ?  132 PHE   A CA   1 
ATOM   2785 C CA   B PHE   A 1 132 ? 18.976 0.168   -6.836  0.28 11.90 ?  132 PHE   A CA   1 
ATOM   2786 C C    A PHE   A 1 132 ? 17.912 -0.587  -7.757  0.72 11.99 ?  132 PHE   A C    1 
ATOM   2787 C C    B PHE   A 1 132 ? 18.289 -0.571  -7.982  0.28 12.72 ?  132 PHE   A C    1 
ATOM   2788 O O    A PHE   A 1 132 ? 18.540 -1.237  -8.601  0.72 12.72 ?  132 PHE   A O    1 
ATOM   2789 O O    B PHE   A 1 132 ? 18.981 -1.113  -8.851  0.28 13.42 ?  132 PHE   A O    1 
ATOM   2790 C CB   A PHE   A 1 132 ? 19.481 -0.798  -5.805  0.72 11.34 ?  132 PHE   A CB   1 
ATOM   2791 C CB   B PHE   A 1 132 ? 19.768 -0.801  -5.953  0.28 11.16 ?  132 PHE   A CB   1 
ATOM   2792 C CG   A PHE   A 1 132 ? 20.714 -0.199  -5.151  0.72 11.69 ?  132 PHE   A CG   1 
ATOM   2793 C CG   B PHE   A 1 132 ? 20.966 -0.172  -5.279  0.28 11.15 ?  132 PHE   A CG   1 
ATOM   2794 C CD1  A PHE   A 1 132 ? 20.609 0.827   -4.225  0.72 12.75 ?  132 PHE   A CD1  1 
ATOM   2795 C CD1  B PHE   A 1 132 ? 20.811 0.870   -4.378  0.28 11.72 ?  132 PHE   A CD1  1 
ATOM   2796 C CD2  A PHE   A 1 132 ? 21.973 -0.718  -5.419  0.72 12.26 ?  132 PHE   A CD2  1 
ATOM   2797 C CD2  B PHE   A 1 132 ? 22.245 -0.636  -5.540  0.28 11.57 ?  132 PHE   A CD2  1 
ATOM   2798 C CE1  A PHE   A 1 132 ? 21.741 1.348   -3.611  0.72 13.16 ?  132 PHE   A CE1  1 
ATOM   2799 C CE1  B PHE   A 1 132 ? 21.914 1.441   -3.758  0.28 12.00 ?  132 PHE   A CE1  1 
ATOM   2800 C CE2  A PHE   A 1 132 ? 23.108 -0.204  -4.809  0.72 12.46 ?  132 PHE   A CE2  1 
ATOM   2801 C CE2  B PHE   A 1 132 ? 23.348 -0.071  -4.924  0.28 11.80 ?  132 PHE   A CE2  1 
ATOM   2802 C CZ   A PHE   A 1 132 ? 22.988 0.834   -3.901  0.72 12.77 ?  132 PHE   A CZ   1 
ATOM   2803 C CZ   B PHE   A 1 132 ? 23.181 0.968   -4.031  0.28 12.05 ?  132 PHE   A CZ   1 
ATOM   2804 H H    A PHE   A 1 132 ? 17.604 0.671   -5.081  0.72 14.07 ?  132 PHE   A H    1 
ATOM   2805 H H    B PHE   A 1 132 ? 17.771 0.578   -5.317  0.28 14.06 ?  132 PHE   A H    1 
ATOM   2806 H HA   A PHE   A 1 132 ? 19.315 0.759   -7.113  0.72 13.80 ?  132 PHE   A HA   1 
ATOM   2807 H HA   B PHE   A 1 132 ? 19.621 0.775   -7.221  0.28 14.30 ?  132 PHE   A HA   1 
ATOM   2808 H HB2  A PHE   A 1 132 ? 18.909 -1.129  -5.094  0.72 13.62 ?  132 PHE   A HB2  1 
ATOM   2809 H HB2  B PHE   A 1 132 ? 19.186 -1.143  -5.258  0.28 13.41 ?  132 PHE   A HB2  1 
ATOM   2810 H HB3  A PHE   A 1 132 ? 19.775 -1.538  -6.359  0.72 13.62 ?  132 PHE   A HB3  1 
ATOM   2811 H HB3  B PHE   A 1 132 ? 20.090 -1.534  -6.503  0.28 13.41 ?  132 PHE   A HB3  1 
ATOM   2812 H HD1  A PHE   A 1 132 ? 19.777 1.180   -4.019  0.72 15.32 ?  132 PHE   A HD1  1 
ATOM   2813 H HD1  B PHE   A 1 132 ? 19.961 1.194   -4.188  0.28 14.09 ?  132 PHE   A HD1  1 
ATOM   2814 H HD2  A PHE   A 1 132 ? 22.064 -1.416  -6.030  0.72 14.73 ?  132 PHE   A HD2  1 
ATOM   2815 H HD2  B PHE   A 1 132 ? 22.365 -1.336  -6.140  0.28 13.91 ?  132 PHE   A HD2  1 
ATOM   2816 H HE1  A PHE   A 1 132 ? 21.660 2.045   -3.000  0.72 15.81 ?  132 PHE   A HE1  1 
ATOM   2817 H HE1  B PHE   A 1 132 ? 21.800 2.142   -3.156  0.28 14.42 ?  132 PHE   A HE1  1 
ATOM   2818 H HE2  A PHE   A 1 132 ? 23.949 -0.554  -5.013  0.72 14.97 ?  132 PHE   A HE2  1 
ATOM   2819 H HE2  B PHE   A 1 132 ? 24.202 -0.392  -5.112  0.28 14.18 ?  132 PHE   A HE2  1 
ATOM   2820 H HZ   A PHE   A 1 132 ? 23.747 1.186   -3.493  0.72 15.34 ?  132 PHE   A HZ   1 
ATOM   2821 H HZ   B PHE   A 1 132 ? 23.923 1.351   -3.617  0.28 14.48 ?  132 PHE   A HZ   1 
ATOM   2822 N N    A GLY   A 1 133 ? 16.580 -0.544  -7.746  0.72 12.05 ?  133 GLY   A N    1 
ATOM   2823 N N    B GLY   A 1 133 ? 16.957 -0.621  -7.997  0.28 12.66 ?  133 GLY   A N    1 
ATOM   2824 C CA   A GLY   A 1 133 ? 15.780 -0.915  -8.899  0.72 13.08 ?  133 GLY   A CA   1 
ATOM   2825 C CA   B GLY   A 1 133 ? 16.193 -0.972  -9.173  0.28 12.81 ?  133 GLY   A CA   1 
ATOM   2826 C C    A GLY   A 1 133 ? 15.521 -2.390  -9.132  0.72 13.92 ?  133 GLY   A C    1 
ATOM   2827 C C    B GLY   A 1 133 ? 15.536 -2.337  -9.152  0.28 13.05 ?  133 GLY   A C    1 
ATOM   2828 O O    A GLY   A 1 133 ? 14.951 -2.727  -10.176 0.72 15.29 ?  133 GLY   A O    1 
ATOM   2829 O O    B GLY   A 1 133 ? 14.606 -2.563  -9.937  0.28 13.11 ?  133 GLY   A O    1 
ATOM   2830 H H    A GLY   A 1 133 ? 16.116 -0.291  -7.072  0.72 14.49 ?  133 GLY   A H    1 
ATOM   2831 H H    B GLY   A 1 133 ? 16.469 -0.454  -7.315  0.28 15.22 ?  133 GLY   A H    1 
ATOM   2832 H HA2  A GLY   A 1 133 ? 14.914 -0.481  -8.821  0.72 15.72 ?  133 GLY   A HA2  1 
ATOM   2833 H HA2  B GLY   A 1 133 ? 15.484 -0.340  -9.279  0.28 15.40 ?  133 GLY   A HA2  1 
ATOM   2834 H HA3  A GLY   A 1 133 ? 16.207 -0.573  -9.698  0.72 15.72 ?  133 GLY   A HA3  1 
ATOM   2835 H HA3  B GLY   A 1 133 ? 16.749 -0.885  -9.957  0.28 15.40 ?  133 GLY   A HA3  1 
ATOM   2836 N N    A ALA   A 1 134 ? 15.912 -3.283  -8.224  0.72 13.56 ?  134 ALA   A N    1 
ATOM   2837 N N    B ALA   A 1 134 ? 15.964 -3.246  -8.281  0.28 13.20 ?  134 ALA   A N    1 
ATOM   2838 C CA   A ALA   A 1 134 ? 15.601 -4.693  -8.407  0.72 14.03 ?  134 ALA   A CA   1 
ATOM   2839 C CA   B ALA   A 1 134 ? 15.480 -4.616  -8.365  0.28 13.46 ?  134 ALA   A CA   1 
ATOM   2840 C C    A ALA   A 1 134 ? 14.229 -5.016  -7.815  0.72 13.87 ?  134 ALA   A C    1 
ATOM   2841 C C    B ALA   A 1 134 ? 14.196 -4.818  -7.562  0.28 13.40 ?  134 ALA   A C    1 
ATOM   2842 O O    A ALA   A 1 134 ? 13.637 -4.230  -7.072  0.72 14.74 ?  134 ALA   A O    1 
ATOM   2843 O O    B ALA   A 1 134 ? 13.855 -4.040  -6.667  0.28 13.68 ?  134 ALA   A O    1 
ATOM   2844 C CB   A ALA   A 1 134 ? 16.681 -5.584  -7.794  0.72 14.97 ?  134 ALA   A CB   1 
ATOM   2845 C CB   B ALA   A 1 134 ? 16.542 -5.599  -7.883  0.28 13.76 ?  134 ALA   A CB   1 
ATOM   2846 H H    A ALA   A 1 134 ? 16.353 -3.096  -7.505  0.72 16.29 ?  134 ALA   A H    1 
ATOM   2847 H H    B ALA   A 1 134 ? 16.525 -3.094  -7.640  0.28 15.87 ?  134 ALA   A H    1 
ATOM   2848 H HA   A ALA   A 1 134 ? 15.562 -4.883  -9.356  0.72 16.86 ?  134 ALA   A HA   1 
ATOM   2849 H HA   B ALA   A 1 134 ? 15.291 -4.808  -9.298  0.28 16.18 ?  134 ALA   A HA   1 
ATOM   2850 H HB1  A ALA   A 1 134 ? 16.449 -6.511  -7.953  0.72 17.98 ?  134 ALA   A HB1  1 
ATOM   2851 H HB1  B ALA   A 1 134 ? 16.188 -6.496  -7.963  0.28 16.53 ?  134 ALA   A HB1  1 
ATOM   2852 H HB2  A ALA   A 1 134 ? 17.531 -5.378  -8.217  0.72 17.98 ?  134 ALA   A HB2  1 
ATOM   2853 H HB2  B ALA   A 1 134 ? 17.330 -5.498  -8.435  0.28 16.53 ?  134 ALA   A HB2  1 
ATOM   2854 H HB3  A ALA   A 1 134 ? 16.733 -5.410  -6.844  0.72 17.98 ?  134 ALA   A HB3  1 
ATOM   2855 H HB3  B ALA   A 1 134 ? 16.751 -5.402  -6.959  0.28 16.53 ?  134 ALA   A HB3  1 
ATOM   2856 N N    A ASP   A 1 135 ? 13.720 -6.191  -8.166  0.72 13.89 ?  135 ASP   A N    1 
ATOM   2857 N N    B ASP   A 1 135 ? 13.493 -5.900  -7.892  0.28 13.58 ?  135 ASP   A N    1 
ATOM   2858 C CA   A ASP   A 1 135 ? 12.457 -6.670  -7.617  0.72 14.58 ?  135 ASP   A CA   1 
ATOM   2859 C CA   B ASP   A 1 135 ? 12.244 -6.254  -7.226  0.28 13.69 ?  135 ASP   A CA   1 
ATOM   2860 C C    A ASP   A 1 135 ? 12.684 -7.112  -6.178  0.72 14.01 ?  135 ASP   A C    1 
ATOM   2861 C C    B ASP   A 1 135 ? 12.542 -6.751  -5.816  0.28 12.93 ?  135 ASP   A C    1 
ATOM   2862 O O    A ASP   A 1 135 ? 13.476 -8.032  -5.946  0.72 13.84 ?  135 ASP   A O    1 
ATOM   2863 O O    B ASP   A 1 135 ? 13.275 -7.738  -5.660  0.28 12.70 ?  135 ASP   A O    1 
ATOM   2864 C CB   A ASP   A 1 135 ? 11.983 -7.853  -8.456  0.72 17.07 ?  135 ASP   A CB   1 
ATOM   2865 C CB   B ASP   A 1 135 ? 11.559 -7.357  -8.030  0.28 14.38 ?  135 ASP   A CB   1 
ATOM   2866 C CG   A ASP   A 1 135 ? 10.679 -8.463  -7.954  0.72 19.26 ?  135 ASP   A CG   1 
ATOM   2867 C CG   B ASP   A 1 135 ? 10.146 -7.645  -7.555  0.28 15.55 ?  135 ASP   A CG   1 
ATOM   2868 O OD1  A ASP   A 1 135 ? 10.145 -8.019  -6.918  0.72 19.19 ?  135 ASP   A OD1  1 
ATOM   2869 O OD1  B ASP   A 1 135 ? 9.838  -7.366  -6.376  0.28 15.86 ?  135 ASP   A OD1  1 
ATOM   2870 O OD2  A ASP   A 1 135 ? 10.182 -9.397  -8.616  0.72 21.65 -1 135 ASP   A OD2  1 
ATOM   2871 O OD2  B ASP   A 1 135 ? 9.352  -8.175  -8.361  0.28 16.43 -1 135 ASP   A OD2  1 
ATOM   2872 H H    A ASP   A 1 135 ? 14.086 -6.737  -8.718  0.72 16.68 ?  135 ASP   A H    1 
ATOM   2873 H H    B ASP   A 1 135 ? 13.722 -6.451  -8.509  0.28 16.32 ?  135 ASP   A H    1 
ATOM   2874 H HA   A ASP   A 1 135 ? 11.789 -5.969  -7.652  0.72 17.52 ?  135 ASP   A HA   1 
ATOM   2875 H HA   B ASP   A 1 135 ? 11.655 -5.479  -7.200  0.28 16.45 ?  135 ASP   A HA   1 
ATOM   2876 H HB2  A ASP   A 1 135 ? 11.831 -7.557  -9.364  0.72 20.50 ?  135 ASP   A HB2  1 
ATOM   2877 H HB2  B ASP   A 1 135 ? 11.549 -7.103  -8.969  0.28 17.27 ?  135 ASP   A HB2  1 
ATOM   2878 H HB3  A ASP   A 1 135 ? 12.661 -8.546  -8.440  0.72 20.50 ?  135 ASP   A HB3  1 
ATOM   2879 H HB3  B ASP   A 1 135 ? 12.048 -8.181  -7.914  0.28 17.27 ?  135 ASP   A HB3  1 
ATOM   2880 N N    A PRO   A 1 136 ? 12.034 -6.495  -5.189  0.72 13.85 ?  136 PRO   A N    1 
ATOM   2881 N N    B PRO   A 1 136 ? 12.007 -6.114  -4.771  0.28 12.43 ?  136 PRO   A N    1 
ATOM   2882 C CA   A PRO   A 1 136 ? 12.278 -6.900  -3.793  0.72 14.18 ?  136 PRO   A CA   1 
ATOM   2883 C CA   B PRO   A 1 136 ? 12.281 -6.591  -3.404  0.28 12.59 ?  136 PRO   A CA   1 
ATOM   2884 C C    A PRO   A 1 136 ? 11.860 -8.327  -3.476  0.72 13.55 ?  136 PRO   A C    1 
ATOM   2885 C C    B PRO   A 1 136 ? 11.829 -8.019  -3.151  0.28 12.44 ?  136 PRO   A C    1 
ATOM   2886 O O    A PRO   A 1 136 ? 12.469 -8.955  -2.601  0.72 13.52 ?  136 PRO   A O    1 
ATOM   2887 O O    B PRO   A 1 136 ? 12.390 -8.689  -2.274  0.28 11.71 ?  136 PRO   A O    1 
ATOM   2888 C CB   A PRO   A 1 136 ? 11.479 -5.869  -2.984  0.72 15.07 ?  136 PRO   A CB   1 
ATOM   2889 C CB   B PRO   A 1 136 ? 11.534 -5.576  -2.523  0.28 12.96 ?  136 PRO   A CB   1 
ATOM   2890 C CG   A PRO   A 1 136 ? 10.419 -5.384  -3.930  0.72 15.53 ?  136 PRO   A CG   1 
ATOM   2891 C CG   B PRO   A 1 136 ? 10.498 -4.980  -3.422  0.28 13.07 ?  136 PRO   A CG   1 
ATOM   2892 C CD   A PRO   A 1 136 ? 11.053 -5.400  -5.286  0.72 14.72 ?  136 PRO   A CD   1 
ATOM   2893 C CD   B PRO   A 1 136 ? 11.143 -4.923  -4.771  0.28 12.55 ?  136 PRO   A CD   1 
ATOM   2894 H HA   A PRO   A 1 136 ? 13.222 -6.803  -3.578  0.72 17.03 ?  136 PRO   A HA   1 
ATOM   2895 H HA   B PRO   A 1 136 ? 13.230 -6.524  -3.216  0.28 15.12 ?  136 PRO   A HA   1 
ATOM   2896 H HB2  A PRO   A 1 136 ? 11.083 -6.297  -2.207  0.72 18.11 ?  136 PRO   A HB2  1 
ATOM   2897 H HB2  B PRO   A 1 136 ? 11.118 -6.029  -1.776  0.28 15.57 ?  136 PRO   A HB2  1 
ATOM   2898 H HB3  A PRO   A 1 136 ? 12.066 -5.143  -2.713  0.72 18.11 ?  136 PRO   A HB3  1 
ATOM   2899 H HB3  B PRO   A 1 136 ? 12.149 -4.890  -2.213  0.28 15.57 ?  136 PRO   A HB3  1 
ATOM   2900 H HG2  A PRO   A 1 136 ? 9.660  -5.982  -3.899  0.72 18.66 ?  136 PRO   A HG2  1 
ATOM   2901 H HG2  B PRO   A 1 136 ? 9.713  -5.551  -3.442  0.28 15.71 ?  136 PRO   A HG2  1 
ATOM   2902 H HG3  A PRO   A 1 136 ? 10.160 -4.482  -3.687  0.72 18.66 ?  136 PRO   A HG3  1 
ATOM   2903 H HG3  B PRO   A 1 136 ? 10.268 -4.090  -3.117  0.28 15.71 ?  136 PRO   A HG3  1 
ATOM   2904 H HD2  A PRO   A 1 136 ? 10.387 -5.604  -5.964  0.72 17.68 ?  136 PRO   A HD2  1 
ATOM   2905 H HD2  B PRO   A 1 136 ? 10.471 -4.988  -5.470  0.28 15.08 ?  136 PRO   A HD2  1 
ATOM   2906 H HD3  A PRO   A 1 136 ? 11.500 -4.560  -5.466  0.72 17.68 ?  136 PRO   A HD3  1 
ATOM   2907 H HD3  B PRO   A 1 136 ? 11.676 -4.115  -4.866  0.28 15.08 ?  136 PRO   A HD3  1 
ATOM   2908 N N    A ILE   A 1 137 ? 10.826 -8.856  -4.134  0.72 13.66 ?  137 ILE   A N    1 
ATOM   2909 N N    B ILE   A 1 137 ? 10.826 -8.506  -3.885  0.28 13.03 ?  137 ILE   A N    1 
ATOM   2910 C CA   A ILE   A 1 137 ? 10.465 -10.258 -3.932  0.72 13.85 ?  137 ILE   A CA   1 
ATOM   2911 C CA   B ILE   A 1 137 ? 10.398 -9.896  -3.735  0.28 13.43 ?  137 ILE   A CA   1 
ATOM   2912 C C    A ILE   A 1 137 ? 11.627 -11.155 -4.333  0.72 13.56 ?  137 ILE   A C    1 
ATOM   2913 C C    B ILE   A 1 137 ? 11.529 -10.841 -4.131  0.28 13.23 ?  137 ILE   A C    1 
ATOM   2914 O O    A ILE   A 1 137 ? 11.949 -12.133 -3.647  0.72 13.89 ?  137 ILE   A O    1 
ATOM   2915 O O    B ILE   A 1 137 ? 11.821 -11.820 -3.435  0.28 13.15 ?  137 ILE   A O    1 
ATOM   2916 C CB   A ILE   A 1 137 ? 9.174  -10.597 -4.700  0.72 15.06 ?  137 ILE   A CB   1 
ATOM   2917 C CB   B ILE   A 1 137 ? 9.124  -10.157 -4.561  0.28 13.95 ?  137 ILE   A CB   1 
ATOM   2918 C CG1  A ILE   A 1 137 ? 7.992  -9.775  -4.167  0.72 16.83 ?  137 ILE   A CG1  1 
ATOM   2919 C CG1  B ILE   A 1 137 ? 8.032  -9.136  -4.213  0.28 14.92 ?  137 ILE   A CG1  1 
ATOM   2920 C CG2  A ILE   A 1 137 ? 8.881  -12.091 -4.607  0.72 15.42 ?  137 ILE   A CG2  1 
ATOM   2921 C CG2  B ILE   A 1 137 ? 8.628  -11.583 -4.338  0.28 13.86 ?  137 ILE   A CG2  1 
ATOM   2922 C CD1  A ILE   A 1 137 ? 6.717  -9.936  -4.965  0.72 18.22 ?  137 ILE   A CD1  1 
ATOM   2923 C CD1  B ILE   A 1 137 ? 6.799  -9.233  -5.086  0.28 15.59 ?  137 ILE   A CD1  1 
ATOM   2924 H H    A ILE   A 1 137 ? 10.330 -8.433  -4.690  0.72 16.41 ?  137 ILE   A H    1 
ATOM   2925 H H    B ILE   A 1 137 ? 10.383 -8.050  -4.467  0.28 15.65 ?  137 ILE   A H    1 
ATOM   2926 H HA   A ILE   A 1 137 ? 10.297 -10.409 -2.991  0.72 16.64 ?  137 ILE   A HA   1 
ATOM   2927 H HA   B ILE   A 1 137 ? 10.183 -10.056 -2.803  0.28 16.13 ?  137 ILE   A HA   1 
ATOM   2928 H HB   A ILE   A 1 137 ? 9.303  -10.376 -5.633  0.72 18.09 ?  137 ILE   A HB   1 
ATOM   2929 H HB   B ILE   A 1 137 ? 9.344  -10.054 -5.498  0.28 16.76 ?  137 ILE   A HB   1 
ATOM   2930 H HG12 A ILE   A 1 137 ? 7.813  -10.045 -3.254  0.72 20.22 ?  137 ILE   A HG12 1 
ATOM   2931 H HG12 B ILE   A 1 137 ? 7.756  -9.273  -3.295  0.28 17.93 ?  137 ILE   A HG12 1 
ATOM   2932 H HG13 A ILE   A 1 137 ? 8.239  -8.835  -4.188  0.72 20.22 ?  137 ILE   A HG13 1 
ATOM   2933 H HG13 B ILE   A 1 137 ? 8.386  -8.238  -4.318  0.28 17.93 ?  137 ILE   A HG13 1 
ATOM   2934 H HG21 A ILE   A 1 137 ? 7.975  -12.273 -4.906  0.72 18.53 ?  137 ILE   A HG21 1 
ATOM   2935 H HG21 B ILE   A 1 137 ? 7.793  -11.706 -4.815  0.28 16.65 ?  137 ILE   A HG21 1 
ATOM   2936 H HG22 A ILE   A 1 137 ? 9.507  -12.572 -5.169  0.72 18.53 ?  137 ILE   A HG22 1 
ATOM   2937 H HG22 B ILE   A 1 137 ? 9.292  -12.204 -4.672  0.28 16.65 ?  137 ILE   A HG22 1 
ATOM   2938 H HG23 A ILE   A 1 137 ? 8.979  -12.374 -3.685  0.72 18.53 ?  137 ILE   A HG23 1 
ATOM   2939 H HG23 B ILE   A 1 137 ? 8.490  -11.722 -3.388  0.28 16.65 ?  137 ILE   A HG23 1 
ATOM   2940 H HD11 A ILE   A 1 137 ? 5.988  -10.117 -4.354  0.72 21.89 ?  137 ILE   A HD11 1 
ATOM   2941 H HD11 B ILE   A 1 137 ? 6.493  -8.338  -5.302  0.28 18.73 ?  137 ILE   A HD11 1 
ATOM   2942 H HD12 A ILE   A 1 137 ? 6.557  -9.113  -5.446  0.72 21.89 ?  137 ILE   A HD12 1 
ATOM   2943 H HD12 B ILE   A 1 137 ? 7.027  -9.708  -5.901  0.28 18.73 ?  137 ILE   A HD12 1 
ATOM   2944 H HD13 A ILE   A 1 137 ? 6.816  -10.666 -5.594  0.72 21.89 ?  137 ILE   A HD13 1 
ATOM   2945 H HD13 B ILE   A 1 137 ? 6.109  -9.716  -4.606  0.28 18.73 ?  137 ILE   A HD13 1 
ATOM   2946 N N    A HIS   A 1 138 ? 12.284 -10.822 -5.445  0.72 13.61 ?  138 HIS   A N    1 
ATOM   2947 N N    B HIS   A 1 138 ? 12.183 -10.553 -5.260  0.28 13.38 ?  138 HIS   A N    1 
ATOM   2948 C CA   A HIS   A 1 138 ? 13.483 -11.548 -5.841  0.72 13.83 ?  138 HIS   A CA   1 
ATOM   2949 C CA   B HIS   A 1 138 ? 13.279 -11.396 -5.732  0.28 13.34 ?  138 HIS   A CA   1 
ATOM   2950 C C    A HIS   A 1 138 ? 14.607 -11.364 -4.825  0.72 13.36 ?  138 HIS   A C    1 
ATOM   2951 C C    B HIS   A 1 138 ? 14.466 -11.341 -4.778  0.28 13.14 ?  138 HIS   A C    1 
ATOM   2952 O O    A HIS   A 1 138 ? 15.296 -12.333 -4.478  0.72 13.73 ?  138 HIS   A O    1 
ATOM   2953 O O    B HIS   A 1 138 ? 15.066 -12.373 -4.454  0.28 13.34 ?  138 HIS   A O    1 
ATOM   2954 C CB   A HIS   A 1 138 ? 13.921 -11.120 -7.240  0.72 14.78 ?  138 HIS   A CB   1 
ATOM   2955 C CB   B HIS   A 1 138 ? 13.692 -10.942 -7.134  0.28 13.45 ?  138 HIS   A CB   1 
ATOM   2956 C CG   A HIS   A 1 138 ? 15.170 -11.800 -7.705  0.72 15.72 ?  138 HIS   A CG   1 
ATOM   2957 C CG   B HIS   A 1 138 ? 14.994 -11.518 -7.598  0.28 13.69 ?  138 HIS   A CG   1 
ATOM   2958 N ND1  A HIS   A 1 138 ? 15.253 -13.166 -7.881  0.72 16.94 ?  138 HIS   A ND1  1 
ATOM   2959 N ND1  B HIS   A 1 138 ? 15.118 -12.817 -8.039  0.28 14.40 ?  138 HIS   A ND1  1 
ATOM   2960 C CD2  A HIS   A 1 138 ? 16.393 -11.306 -8.009  0.72 15.97 ?  138 HIS   A CD2  1 
ATOM   2961 C CD2  B HIS   A 1 138 ? 16.229 -10.970 -7.690  0.28 13.59 ?  138 HIS   A CD2  1 
ATOM   2962 C CE1  A HIS   A 1 138 ? 16.470 -13.481 -8.285  0.72 17.34 ?  138 HIS   A CE1  1 
ATOM   2963 C CE1  B HIS   A 1 138 ? 16.373 -13.045 -8.382  0.28 14.39 ?  138 HIS   A CE1  1 
ATOM   2964 N NE2  A HIS   A 1 138 ? 17.182 -12.371 -8.371  0.72 16.66 ?  138 HIS   A NE2  1 
ATOM   2965 N NE2  B HIS   A 1 138 ? 17.069 -11.940 -8.181  0.28 14.08 ?  138 HIS   A NE2  1 
ATOM   2966 H H    A HIS   A 1 138 ? 12.052 -10.190 -5.984  0.72 16.35 ?  138 HIS   A H    1 
ATOM   2967 H H    B HIS   A 1 138 ? 12.014 -9.875  -5.762  0.28 16.08 ?  138 HIS   A H    1 
ATOM   2968 H HA   A HIS   A 1 138 ? 13.271 -12.491 -5.879  0.72 16.61 ?  138 HIS   A HA   1 
ATOM   2969 H HA   B HIS   A 1 138 ? 12.973 -12.312 -5.787  0.28 16.03 ?  138 HIS   A HA   1 
ATOM   2970 H HB2  A HIS   A 1 138 ? 13.209 -11.335 -7.871  0.72 17.75 ?  138 HIS   A HB2  1 
ATOM   2971 H HB2  B HIS   A 1 138 ? 13.003 -11.213 -7.765  0.28 16.17 ?  138 HIS   A HB2  1 
ATOM   2972 H HB3  A HIS   A 1 138 ? 14.079 -10.164 -7.245  0.72 17.75 ?  138 HIS   A HB3  1 
ATOM   2973 H HB3  B HIS   A 1 138 ? 13.774 -9.975  -7.139  0.28 16.17 ?  138 HIS   A HB3  1 
ATOM   2974 H HD1  A HIS   A 1 138 ? 14.606 -13.723 -7.754  0.72 20.35 ?  138 HIS   A HD1  1 
ATOM   2975 H HD1  B HIS   A 1 138 ? 14.475 -13.389 -8.083  0.28 17.29 ?  138 HIS   A HD1  1 
ATOM   2976 H HD2  A HIS   A 1 138 ? 16.643 -10.411 -7.982  0.72 19.18 ?  138 HIS   A HD2  1 
ATOM   2977 H HD2  B HIS   A 1 138 ? 16.462 -10.099 -7.463  0.28 16.33 ?  138 HIS   A HD2  1 
ATOM   2978 H HE1  A HIS   A 1 138 ? 16.771 -14.338 -8.474  0.72 20.83 ?  138 HIS   A HE1  1 
ATOM   2979 H HE1  B HIS   A 1 138 ? 16.707 -13.849 -8.709  0.28 17.29 ?  138 HIS   A HE1  1 
ATOM   2980 N N    . SER   A 1 139 ? 14.814 -10.138 -4.326  1.00 13.09 ?  139 SER   A N    1 
ATOM   2981 C CA   . SER   A 1 139 ? 15.882 -9.957  -3.352  1.00 12.97 ?  139 SER   A CA   1 
ATOM   2982 C C    . SER   A 1 139 ? 15.662 -10.805 -2.105  1.00 12.62 ?  139 SER   A C    1 
ATOM   2983 O O    . SER   A 1 139 ? 16.610 -11.398 -1.575  1.00 12.59 ?  139 SER   A O    1 
ATOM   2984 C CB   . SER   A 1 139 ? 16.012 -8.481  -2.982  1.00 12.67 ?  139 SER   A CB   1 
ATOM   2985 O OG   . SER   A 1 139 ? 17.104 -8.308  -2.098  1.00 12.84 ?  139 SER   A OG   1 
ATOM   2986 H H    A SER   A 1 139 ? 14.370 -9.428  -4.527  0.72 15.73 ?  139 SER   A H    1 
ATOM   2987 H H    B SER   A 1 139 ? 14.435 -9.404  -4.568  0.28 15.73 ?  139 SER   A H    1 
ATOM   2988 H HA   . SER   A 1 139 ? 16.722 -10.229 -3.752  1.00 15.59 ?  139 SER   A HA   1 
ATOM   2989 H HB2  . SER   A 1 139 ? 16.163 -7.954  -3.783  1.00 15.22 ?  139 SER   A HB2  1 
ATOM   2990 H HB3  . SER   A 1 139 ? 15.195 -8.185  -2.540  1.00 15.22 ?  139 SER   A HB3  1 
ATOM   2991 H HG   . SER   A 1 139 ? 17.180 -7.494  -1.885  1.00 15.43 ?  139 SER   A HG   1 
ATOM   2992 N N    . LEU   A 1 140 ? 14.423 -10.868 -1.615  1.00 12.31 ?  140 LEU   A N    1 
ATOM   2993 C CA   . LEU   A 1 140 ? 14.147 -11.688 -0.438  1.00 12.11 ?  140 LEU   A CA   1 
ATOM   2994 C C    . LEU   A 1 140 ? 14.419 -13.162 -0.718  1.00 12.28 ?  140 LEU   A C    1 
ATOM   2995 O O    . LEU   A 1 140 ? 14.972 -13.876 0.132   1.00 13.23 ?  140 LEU   A O    1 
ATOM   2996 C CB   . LEU   A 1 140 ? 12.706 -11.478 0.015   1.00 12.94 ?  140 LEU   A CB   1 
ATOM   2997 C CG   . LEU   A 1 140 ? 12.242 -12.329 1.194   1.00 13.41 ?  140 LEU   A CG   1 
ATOM   2998 C CD1  . LEU   A 1 140 ? 13.142 -12.143 2.407   1.00 13.85 ?  140 LEU   A CD1  1 
ATOM   2999 C CD2  . LEU   A 1 140 ? 10.781 -12.023 1.539   1.00 14.43 ?  140 LEU   A CD2  1 
ATOM   3000 H H    . LEU   A 1 140 ? 13.741 -10.453 -1.934  1.00 14.79 ?  140 LEU   A H    1 
ATOM   3001 H HA   . LEU   A 1 140 ? 14.731 -11.410 0.285   1.00 14.56 ?  140 LEU   A HA   1 
ATOM   3002 H HB2  . LEU   A 1 140 ? 12.595 -10.555 0.271   1.00 15.55 ?  140 LEU   A HB2  1 
ATOM   3003 H HB3  . LEU   A 1 140 ? 12.120 -11.685 -0.731  1.00 15.55 ?  140 LEU   A HB3  1 
ATOM   3004 H HG   . LEU   A 1 140 ? 12.282 -13.269 0.941   1.00 16.11 ?  140 LEU   A HG   1 
ATOM   3005 H HD11 . LEU   A 1 140 ? 12.757 -12.620 3.161   1.00 16.63 ?  140 LEU   A HD11 1 
ATOM   3006 H HD12 . LEU   A 1 140 ? 14.019 -12.510 2.203   1.00 16.63 ?  140 LEU   A HD12 1 
ATOM   3007 H HD13 . LEU   A 1 140 ? 13.211 -11.202 2.606   1.00 16.63 ?  140 LEU   A HD13 1 
ATOM   3008 H HD21 . LEU   A 1 140 ? 10.508 -12.581 2.291   1.00 17.34 ?  140 LEU   A HD21 1 
ATOM   3009 H HD22 . LEU   A 1 140 ? 10.698 -11.090 1.775   1.00 17.34 ?  140 LEU   A HD22 1 
ATOM   3010 H HD23 . LEU   A 1 140 ? 10.223 -12.224 0.769   1.00 17.34 ?  140 LEU   A HD23 1 
ATOM   3011 N N    . ARG   A 1 141 ? 14.030 -13.637 -1.904  1.00 12.67 ?  141 ARG   A N    1 
ATOM   3012 C CA   . ARG   A 1 141 ? 14.270 -15.029 -2.272  1.00 13.91 ?  141 ARG   A CA   1 
ATOM   3013 C C    . ARG   A 1 141 ? 15.766 -15.332 -2.288  1.00 13.42 ?  141 ARG   A C    1 
ATOM   3014 O O    . ARG   A 1 141 ? 16.220 -16.339 -1.728  1.00 13.69 ?  141 ARG   A O    1 
ATOM   3015 C CB   . ARG   A 1 141 ? 13.643 -15.293 -3.644  1.00 15.63 ?  141 ARG   A CB   1 
ATOM   3016 C CG   . ARG   A 1 141 ? 13.644 -16.741 -4.085  1.00 18.46 ?  141 ARG   A CG   1 
ATOM   3017 C CD   . ARG   A 1 141 ? 12.614 -17.512 -3.319  1.00 20.62 ?  141 ARG   A CD   1 
ATOM   3018 N NE   . ARG   A 1 141 ? 13.227 -18.287 -2.254  1.00 21.37 ?  141 ARG   A NE   1 
ATOM   3019 C CZ   . ARG   A 1 141 ? 12.547 -18.859 -1.269  1.00 22.23 ?  141 ARG   A CZ   1 
ATOM   3020 N NH1  . ARG   A 1 141 ? 11.253 -18.637 -1.101  1.00 21.71 ?  141 ARG   A NH1  1 
ATOM   3021 N NH2  . ARG   A 1 141 ? 13.183 -19.667 -0.425  1.00 23.27 ?  141 ARG   A NH2  1 
ATOM   3022 H H    . ARG   A 1 141 ? 13.627 -13.175 -2.509  1.00 15.22 ?  141 ARG   A H    1 
ATOM   3023 H HA   . ARG   A 1 141 ? 13.850 -15.610 -1.624  1.00 16.72 ?  141 ARG   A HA   1 
ATOM   3024 H HB2  . ARG   A 1 141 ? 12.722 -14.987 -3.627  1.00 18.78 ?  141 ARG   A HB2  1 
ATOM   3025 H HB3  . ARG   A 1 141 ? 14.136 -14.788 -4.309  1.00 18.78 ?  141 ARG   A HB3  1 
ATOM   3026 H HG2  . ARG   A 1 141 ? 13.430 -16.795 -5.032  1.00 22.17 ?  141 ARG   A HG2  1 
ATOM   3027 H HG3  . ARG   A 1 141 ? 14.516 -17.137 -3.917  1.00 22.17 ?  141 ARG   A HG3  1 
ATOM   3028 H HD2  . ARG   A 1 141 ? 11.982 -16.897 -2.913  1.00 24.76 ?  141 ARG   A HD2  1 
ATOM   3029 H HD3  . ARG   A 1 141 ? 12.148 -18.116 -3.921  1.00 24.76 ?  141 ARG   A HD3  1 
ATOM   3030 H HE   . ARG   A 1 141 ? 14.058 -18.488 -2.332  1.00 25.66 ?  141 ARG   A HE   1 
ATOM   3031 H HH11 . ARG   A 1 141 ? 10.826 -18.128 -1.647  1.00 26.08 ?  141 ARG   A HH11 1 
ATOM   3032 H HH12 . ARG   A 1 141 ? 10.831 -19.015 -0.452  1.00 26.08 ?  141 ARG   A HH12 1 
ATOM   3033 H HH21 . ARG   A 1 141 ? 14.024 -19.816 -0.523  1.00 27.95 ?  141 ARG   A HH21 1 
ATOM   3034 H HH22 . ARG   A 1 141 ? 12.755 -20.033 0.227   1.00 27.95 ?  141 ARG   A HH22 1 
ATOM   3035 N N    . VAL   A 1 142 ? 16.555 -14.465 -2.925  1.00 12.80 ?  142 VAL   A N    1 
ATOM   3036 C CA   . VAL   A 1 142 ? 18.001 -14.672 -2.951  1.00 12.58 ?  142 VAL   A CA   1 
ATOM   3037 C C    . VAL   A 1 142 ? 18.568 -14.651 -1.538  1.00 12.04 ?  142 VAL   A C    1 
ATOM   3038 O O    . VAL   A 1 142 ? 19.434 -15.461 -1.193  1.00 12.73 ?  142 VAL   A O    1 
ATOM   3039 C CB   . VAL   A 1 142 ? 18.696 -13.648 -3.867  1.00 13.03 ?  142 VAL   A CB   1 
ATOM   3040 C CG1  . VAL   A 1 142 ? 20.208 -13.854 -3.825  1.00 12.92 ?  142 VAL   A CG1  1 
ATOM   3041 C CG2  . VAL   A 1 142 ? 18.205 -13.782 -5.292  1.00 14.35 ?  142 VAL   A CG2  1 
ATOM   3042 H H    . VAL   A 1 142 ? 16.288 -13.752 -3.338  1.00 15.39 ?  142 VAL   A H    1 
ATOM   3043 H HA   . VAL   A 1 142 ? 18.178 -15.545 -3.321  1.00 15.11 ?  142 VAL   A HA   1 
ATOM   3044 H HB   . VAL   A 1 142 ? 18.509 -12.743 -3.561  1.00 15.66 ?  142 VAL   A HB   1 
ATOM   3045 H HG11 . VAL   A 1 142 ? 20.618 -13.366 -4.558  1.00 15.53 ?  142 VAL   A HG11 1 
ATOM   3046 H HG12 . VAL   A 1 142 ? 20.555 -13.526 -2.980  1.00 15.53 ?  142 VAL   A HG12 1 
ATOM   3047 H HG13 . VAL   A 1 142 ? 20.399 -14.801 -3.916  1.00 15.53 ?  142 VAL   A HG13 1 
ATOM   3048 H HG21 . VAL   A 1 142 ? 18.677 -13.142 -5.850  1.00 17.24 ?  142 VAL   A HG21 1 
ATOM   3049 H HG22 . VAL   A 1 142 ? 18.391 -14.684 -5.598  1.00 17.24 ?  142 VAL   A HG22 1 
ATOM   3050 H HG23 . VAL   A 1 142 ? 17.257 -13.608 -5.313  1.00 17.24 ?  142 VAL   A HG23 1 
ATOM   3051 N N    . CYS   A 1 143 ? 18.097 -13.727 -0.700  1.00 11.83 ?  143 CYS   A N    1 
ATOM   3052 C CA   . CYS   A 1 143 ? 18.558 -13.682 0.684   1.00 12.22 ?  143 CYS   A CA   1 
ATOM   3053 C C    . CYS   A 1 143 ? 18.333 -15.024 1.373   1.00 12.44 ?  143 CYS   A C    1 
ATOM   3054 O O    . CYS   A 1 143 ? 19.253 -15.607 1.950   1.00 12.38 ?  143 CYS   A O    1 
ATOM   3055 C CB   . CYS   A 1 143 ? 17.825 -12.571 1.433   1.00 12.63 ?  143 CYS   A CB   1 
ATOM   3056 S SG   . CYS   A 1 143 ? 18.328 -12.394 3.158   1.00 12.88 ?  143 CYS   A SG   1 
ATOM   3057 H H    . CYS   A 1 143 ? 17.512 -13.132 -0.903  1.00 14.22 ?  143 CYS   A H    1 
ATOM   3058 H HA   . CYS   A 1 143 ? 19.505 -13.493 0.699   1.00 14.69 ?  143 CYS   A HA   1 
ATOM   3059 H HB2  . CYS   A 1 143 ? 17.991 -11.728 0.984   1.00 15.18 ?  143 CYS   A HB2  1 
ATOM   3060 H HB3  . CYS   A 1 143 ? 16.875 -12.762 1.423   1.00 15.18 ?  143 CYS   A HB3  1 
ATOM   3061 H HG   . CYS   A 1 143 ? 17.770 -11.446 3.627   1.00 15.48 ?  143 CYS   A HG   1 
ATOM   3062 N N    . VAL   A 1 144 ? 17.104 -15.530 1.317   1.00 13.20 ?  144 VAL   A N    1 
ATOM   3063 C CA   . VAL   A 1 144 ? 16.766 -16.765 2.017   1.00 14.30 ?  144 VAL   A CA   1 
ATOM   3064 C C    . VAL   A 1 144 ? 17.583 -17.935 1.487   1.00 13.97 ?  144 VAL   A C    1 
ATOM   3065 O O    . VAL   A 1 144 ? 17.948 -18.847 2.242   1.00 14.51 ?  144 VAL   A O    1 
ATOM   3066 C CB   . VAL   A 1 144 ? 15.249 -17.013 1.903   1.00 17.08 ?  144 VAL   A CB   1 
ATOM   3067 C CG1  . VAL   A 1 144 ? 14.893 -18.446 2.257   1.00 19.06 ?  144 VAL   A CG1  1 
ATOM   3068 C CG2  . VAL   A 1 144 ? 14.495 -16.019 2.783   1.00 16.76 ?  144 VAL   A CG2  1 
ATOM   3069 H H    . VAL   A 1 144 ? 16.446 -15.176 0.882   1.00 15.86 ?  144 VAL   A H    1 
ATOM   3070 H HA   . VAL   A 1 144 ? 16.970 -16.660 2.954   1.00 17.19 ?  144 VAL   A HA   1 
ATOM   3071 H HB   . VAL   A 1 144 ? 14.968 -16.857 0.983   1.00 20.52 ?  144 VAL   A HB   1 
ATOM   3072 H HG11 . VAL   A 1 144 ? 13.940 -18.498 2.451   1.00 22.90 ?  144 VAL   A HG11 1 
ATOM   3073 H HG12 . VAL   A 1 144 ? 15.104 -19.024 1.508   1.00 22.90 ?  144 VAL   A HG12 1 
ATOM   3074 H HG13 . VAL   A 1 144 ? 15.399 -18.712 3.039   1.00 22.90 ?  144 VAL   A HG13 1 
ATOM   3075 H HG21 . VAL   A 1 144 ? 13.540 -16.186 2.714   1.00 20.14 ?  144 VAL   A HG21 1 
ATOM   3076 H HG22 . VAL   A 1 144 ? 14.782 -16.128 3.703   1.00 20.14 ?  144 VAL   A HG22 1 
ATOM   3077 H HG23 . VAL   A 1 144 ? 14.690 -15.114 2.483   1.00 20.14 ?  144 VAL   A HG23 1 
ATOM   3078 N N    . ASP   A 1 145 ? 17.849 -17.951 0.182   1.00 14.01 ?  145 ASP   A N    1 
ATOM   3079 C CA   . ASP   A 1 145 ? 18.558 -19.055 -0.453  1.00 14.52 ?  145 ASP   A CA   1 
ATOM   3080 C C    . ASP   A 1 145 ? 20.078 -18.908 -0.411  1.00 14.30 ?  145 ASP   A C    1 
ATOM   3081 O O    . ASP   A 1 145 ? 20.783 -19.798 -0.898  1.00 16.17 ?  145 ASP   A O    1 
ATOM   3082 C CB   . ASP   A 1 145 ? 18.109 -19.193 -1.911  1.00 16.10 ?  145 ASP   A CB   1 
ATOM   3083 C CG   . ASP   A 1 145 ? 16.658 -19.625 -2.042  1.00 18.18 ?  145 ASP   A CG   1 
ATOM   3084 O OD1  . ASP   A 1 145 ? 16.104 -20.175 -1.067  1.00 18.59 ?  145 ASP   A OD1  1 
ATOM   3085 O OD2  . ASP   A 1 145 ? 16.076 -19.411 -3.123  1.00 19.41 -1 145 ASP   A OD2  1 
ATOM   3086 H H    . ASP   A 1 145 ? 17.610 -17.329 -0.368  1.00 16.83 ?  145 ASP   A H    1 
ATOM   3087 H HA   . ASP   A 1 145 ? 18.324 -19.877 0.007   1.00 17.45 ?  145 ASP   A HA   1 
ATOM   3088 H HB2  . ASP   A 1 145 ? 18.213 -18.338 -2.354  1.00 19.34 ?  145 ASP   A HB2  1 
ATOM   3089 H HB3  . ASP   A 1 145 ? 18.655 -19.865 -2.344  1.00 19.34 ?  145 ASP   A HB3  1 
ATOM   3090 N N    . THR   A 1 146 ? 20.603 -17.820 0.144   1.00 12.93 ?  146 THR   A N    1 
ATOM   3091 C CA   . THR   A 1 146 ? 22.047 -17.568 0.164   1.00 12.48 ?  146 THR   A CA   1 
ATOM   3092 C C    . THR   A 1 146 ? 22.604 -17.381 1.563   1.00 12.29 ?  146 THR   A C    1 
ATOM   3093 O O    . THR   A 1 146 ? 23.681 -17.911 1.875   1.00 13.46 ?  146 THR   A O    1 
ATOM   3094 C CB   . THR   A 1 146 ? 22.368 -16.316 -0.677  1.00 12.32 ?  146 THR   A CB   1 
ATOM   3095 O OG1  . THR   A 1 146 ? 21.840 -16.480 -1.994  1.00 12.99 ?  146 THR   A OG1  1 
ATOM   3096 C CG2  . THR   A 1 146 ? 23.872 -16.085 -0.778  1.00 13.10 ?  146 THR   A CG2  1 
ATOM   3097 H H    . THR   A 1 146 ? 20.140 -17.197 0.518   1.00 15.54 ?  146 THR   A H    1 
ATOM   3098 H HA   . THR   A 1 146 ? 22.506 -18.317 -0.236  1.00 14.99 ?  146 THR   A HA   1 
ATOM   3099 H HB   . THR   A 1 146 ? 21.969 -15.534 -0.259  1.00 14.80 ?  146 THR   A HB   1 
ATOM   3100 H HG1  . THR   A 1 146 ? 21.001 -16.551 -1.957  1.00 15.61 ?  146 THR   A HG1  1 
ATOM   3101 H HG21 . THR   A 1 146 ? 24.055 -15.408 -1.447  1.00 15.74 ?  146 THR   A HG21 1 
ATOM   3102 H HG22 . THR   A 1 146 ? 24.221 -15.787 0.075   1.00 15.74 ?  146 THR   A HG22 1 
ATOM   3103 H HG23 . THR   A 1 146 ? 24.313 -16.909 -1.034  1.00 15.74 ?  146 THR   A HG23 1 
ATOM   3104 N N    . VAL   A 1 147 ? 21.918 -16.606 2.400   1.00 12.39 ?  147 VAL   A N    1 
ATOM   3105 C CA   . VAL   A 1 147 ? 22.403 -16.305 3.739   1.00 12.51 ?  147 VAL   A CA   1 
ATOM   3106 C C    . VAL   A 1 147 ? 22.083 -17.472 4.660   1.00 12.65 ?  147 VAL   A C    1 
ATOM   3107 O O    . VAL   A 1 147 ? 20.940 -17.948 4.713   1.00 13.31 ?  147 VAL   A O    1 
ATOM   3108 C CB   . VAL   A 1 147 ? 21.786 -14.998 4.257   1.00 12.51 ?  147 VAL   A CB   1 
ATOM   3109 C CG1  . VAL   A 1 147 ? 22.316 -14.691 5.644   1.00 13.46 ?  147 VAL   A CG1  1 
ATOM   3110 C CG2  . VAL   A 1 147 ? 22.057 -13.856 3.290   1.00 12.86 ?  147 VAL   A CG2  1 
ATOM   3111 H H    . VAL   A 1 147 ? 21.157 -16.247 2.219   1.00 14.89 ?  147 VAL   A H    1 
ATOM   3112 H HA   . VAL   A 1 147 ? 23.364 -16.197 3.712   1.00 15.03 ?  147 VAL   A HA   1 
ATOM   3113 H HB   . VAL   A 1 147 ? 20.827 -15.108 4.327   1.00 15.03 ?  147 VAL   A HB   1 
ATOM   3114 H HG11 . VAL   A 1 147 ? 22.080 -13.783 5.877   1.00 16.17 ?  147 VAL   A HG11 1 
ATOM   3115 H HG12 . VAL   A 1 147 ? 21.913 -15.309 6.279   1.00 16.17 ?  147 VAL   A HG12 1 
ATOM   3116 H HG13 . VAL   A 1 147 ? 23.278 -14.799 5.646   1.00 16.17 ?  147 VAL   A HG13 1 
ATOM   3117 H HG21 . VAL   A 1 147 ? 21.735 -13.030 3.683   1.00 15.45 ?  147 VAL   A HG21 1 
ATOM   3118 H HG22 . VAL   A 1 147 ? 23.011 -13.799 3.131   1.00 15.45 ?  147 VAL   A HG22 1 
ATOM   3119 H HG23 . VAL   A 1 147 ? 21.590 -14.033 2.459   1.00 15.45 ?  147 VAL   A HG23 1 
ATOM   3120 N N    . ARG   A 1 148 ? 23.104 -17.937 5.378   1.00 13.03 ?  148 ARG   A N    1 
ATOM   3121 C CA   . ARG   A 1 148 ? 22.975 -19.017 6.343   1.00 13.17 ?  148 ARG   A CA   1 
ATOM   3122 C C    . ARG   A 1 148 ? 23.096 -18.546 7.779   1.00 13.36 ?  148 ARG   A C    1 
ATOM   3123 O O    . ARG   A 1 148 ? 22.691 -19.274 8.693   1.00 15.18 ?  148 ARG   A O    1 
ATOM   3124 C CB   . ARG   A 1 148 ? 24.014 -20.117 6.068   1.00 13.57 ?  148 ARG   A CB   1 
ATOM   3125 C CG   . ARG   A 1 148 ? 23.865 -20.752 4.696   1.00 15.03 ?  148 ARG   A CG   1 
ATOM   3126 C CD   . ARG   A 1 148 ? 24.944 -21.787 4.415   1.00 16.03 ?  148 ARG   A CD   1 
ATOM   3127 N NE   . ARG   A 1 148 ? 26.281 -21.205 4.442   1.00 15.94 ?  148 ARG   A NE   1 
ATOM   3128 C CZ   . ARG   A 1 148 ? 26.794 -20.465 3.467   1.00 15.10 ?  148 ARG   A CZ   1 
ATOM   3129 N NH1  . ARG   A 1 148 ? 26.123 -20.233 2.349   1.00 15.73 ?  148 ARG   A NH1  1 
ATOM   3130 N NH2  . ARG   A 1 148 ? 28.013 -19.943 3.616   1.00 15.31 ?  148 ARG   A NH2  1 
ATOM   3131 H H    . ARG   A 1 148 ? 23.909 -17.635 5.310   1.00 15.66 ?  148 ARG   A H    1 
ATOM   3132 H HA   . ARG   A 1 148 ? 22.100 -19.416 6.242   1.00 15.83 ?  148 ARG   A HA   1 
ATOM   3133 H HB2  . ARG   A 1 148 ? 24.903 -19.741 6.125   1.00 16.31 ?  148 ARG   A HB2  1 
ATOM   3134 H HB3  . ARG   A 1 148 ? 23.908 -20.824 6.726   1.00 16.31 ?  148 ARG   A HB3  1 
ATOM   3135 H HG2  . ARG   A 1 148 ? 22.999 -21.184 4.641   1.00 18.06 ?  148 ARG   A HG2  1 
ATOM   3136 H HG3  . ARG   A 1 148 ? 23.928 -20.051 4.022   1.00 18.06 ?  148 ARG   A HG3  1 
ATOM   3137 H HD2  . ARG   A 1 148 ? 24.901 -22.476 5.092   1.00 19.26 ?  148 ARG   A HD2  1 
ATOM   3138 H HD3  . ARG   A 1 148 ? 24.795 -22.166 3.536   1.00 19.26 ?  148 ARG   A HD3  1 
ATOM   3139 H HE   . ARG   A 1 148 ? 26.765 -21.341 5.137   1.00 19.14 ?  148 ARG   A HE   1 
ATOM   3140 H HH11 . ARG   A 1 148 ? 25.336 -20.553 2.240   1.00 18.90 ?  148 ARG   A HH11 1 
ATOM   3141 H HH12 . ARG   A 1 148 ? 26.476 -19.743 1.731   1.00 18.90 ?  148 ARG   A HH12 1 
ATOM   3142 H HH21 . ARG   A 1 148 ? 28.452 -20.078 4.339   1.00 18.39 ?  148 ARG   A HH21 1 
ATOM   3143 H HH22 . ARG   A 1 148 ? 28.352 -19.455 2.990   1.00 18.39 ?  148 ARG   A HH22 1 
ATOM   3144 N N    . THR   A 1 149 ? 23.641 -17.353 7.993   1.00 13.35 ?  149 THR   A N    1 
ATOM   3145 C CA   . THR   A 1 149 ? 23.720 -16.753 9.310   1.00 13.72 ?  149 THR   A CA   1 
ATOM   3146 C C    . THR   A 1 149 ? 22.395 -16.054 9.619   1.00 13.22 ?  149 THR   A C    1 
ATOM   3147 O O    . THR   A 1 149 ? 21.457 -16.049 8.813   1.00 13.78 ?  149 THR   A O    1 
ATOM   3148 C CB   . THR   A 1 149 ? 24.921 -15.817 9.370   1.00 14.16 ?  149 THR   A CB   1 
ATOM   3149 O OG1  . THR   A 1 149 ? 24.804 -14.888 8.292   1.00 14.36 ?  149 THR   A OG1  1 
ATOM   3150 C CG2  . THR   A 1 149 ? 26.231 -16.615 9.247   1.00 14.79 ?  149 THR   A CG2  1 
ATOM   3151 H H    . THR   A 1 149 ? 23.989 -16.862 7.371   1.00 16.04 ?  149 THR   A H    1 
ATOM   3152 H HA   . THR   A 1 149 ? 23.847 -17.457 9.965   1.00 16.49 ?  149 THR   A HA   1 
ATOM   3153 H HB   . THR   A 1 149 ? 24.913 -15.344 10.216  1.00 17.01 ?  149 THR   A HB   1 
ATOM   3154 H HG1  . THR   A 1 149 ? 25.456 -14.358 8.301   1.00 17.25 ?  149 THR   A HG1  1 
ATOM   3155 H HG21 . THR   A 1 149 ? 26.990 -16.019 9.307   1.00 17.77 ?  149 THR   A HG21 1 
ATOM   3156 H HG22 . THR   A 1 149 ? 26.290 -17.274 9.961   1.00 17.77 ?  149 THR   A HG22 1 
ATOM   3157 H HG23 . THR   A 1 149 ? 26.261 -17.081 8.394   1.00 17.77 ?  149 THR   A HG23 1 
ATOM   3158 N N    . ASN   A 1 150 ? 22.277 -15.513 10.823  1.00 13.52 ?  150 ASN   A N    1 
ATOM   3159 C CA   . ASN   A 1 150 ? 20.993 -15.007 11.306  1.00 13.93 ?  150 ASN   A CA   1 
ATOM   3160 C C    . ASN   A 1 150 ? 20.809 -13.568 10.842  1.00 13.18 ?  150 ASN   A C    1 
ATOM   3161 O O    . ASN   A 1 150 ? 21.557 -12.674 11.255  1.00 14.69 ?  150 ASN   A O    1 
ATOM   3162 C CB   . ASN   A 1 150 ? 20.932 -15.121 12.824  1.00 16.19 ?  150 ASN   A CB   1 
ATOM   3163 C CG   . ASN   A 1 150 ? 20.828 -16.556 13.285  1.00 20.24 ?  150 ASN   A CG   1 
ATOM   3164 O OD1  . ASN   A 1 150 ? 20.234 -17.388 12.603  1.00 21.74 ?  150 ASN   A OD1  1 
ATOM   3165 N ND2  . ASN   A 1 150 ? 21.420 -16.860 14.436  1.00 22.57 ?  150 ASN   A ND2  1 
ATOM   3166 H H    . ASN   A 1 150 ? 22.922 -15.436 11.384  1.00 16.25 ?  150 ASN   A H    1 
ATOM   3167 H HA   . ASN   A 1 150 ? 20.275 -15.548 10.934  1.00 16.74 ?  150 ASN   A HA   1 
ATOM   3168 H HB2  . ASN   A 1 150 ? 21.738 -14.742 13.205  1.00 19.45 ?  150 ASN   A HB2  1 
ATOM   3169 H HB3  . ASN   A 1 150 ? 20.151 -14.649 13.148  1.00 19.45 ?  150 ASN   A HB3  1 
ATOM   3170 H HD21 . ASN   A 1 150 ? 21.392 -17.668 14.742  1.00 27.11 ?  150 ASN   A HD21 1 
ATOM   3171 H HD22 . ASN   A 1 150 ? 21.828 -16.250 14.887  1.00 27.11 ?  150 ASN   A HD22 1 
ATOM   3172 N N    . VAL   A 1 151 ? 19.821 -13.338 9.982   1.00 13.02 ?  151 VAL   A N    1 
ATOM   3173 C CA   . VAL   A 1 151 ? 19.607 -12.030 9.380   1.00 13.00 ?  151 VAL   A CA   1 
ATOM   3174 C C    . VAL   A 1 151 ? 18.216 -11.515 9.738   1.00 12.88 ?  151 VAL   A C    1 
ATOM   3175 O O    . VAL   A 1 151 ? 17.209 -12.227 9.600   1.00 14.15 ?  151 VAL   A O    1 
ATOM   3176 C CB   . VAL   A 1 151 ? 19.909 -12.024 7.865   1.00 14.12 ?  151 VAL   A CB   1 
ATOM   3177 C CG1  . VAL   A 1 151 ? 19.091 -13.053 7.112   1.00 15.24 ?  151 VAL   A CG1  1 
ATOM   3178 C CG2  . VAL   A 1 151 ? 19.722 -10.625 7.281   1.00 14.23 ?  151 VAL   A CG2  1 
ATOM   3179 H H    . VAL   A 1 151 ? 19.251 -13.937 9.730   1.00 15.65 ?  151 VAL   A H    1 
ATOM   3180 H HA   . VAL   A 1 151 ? 20.244 -11.419 9.778   1.00 15.62 ?  151 VAL   A HA   1 
ATOM   3181 H HB   . VAL   A 1 151 ? 20.844 -12.260 7.739   1.00 16.96 ?  151 VAL   A HB   1 
ATOM   3182 H HG11 . VAL   A 1 151 ? 19.301 -13.002 6.164   1.00 18.31 ?  151 VAL   A HG11 1 
ATOM   3183 H HG12 . VAL   A 1 151 ? 19.311 -13.943 7.444   1.00 18.31 ?  151 VAL   A HG12 1 
ATOM   3184 H HG13 . VAL   A 1 151 ? 18.148 -12.878 7.250   1.00 18.31 ?  151 VAL   A HG13 1 
ATOM   3185 H HG21 . VAL   A 1 151 ? 20.043 -10.622 6.363   1.00 17.09 ?  151 VAL   A HG21 1 
ATOM   3186 H HG22 . VAL   A 1 151 ? 18.780 -10.398 7.299   1.00 17.09 ?  151 VAL   A HG22 1 
ATOM   3187 H HG23 . VAL   A 1 151 ? 20.229 -9.992  7.808   1.00 17.09 ?  151 VAL   A HG23 1 
ATOM   3188 N N    . TYR   A 1 152 ? 18.196 -10.268 10.218  1.00 12.79 ?  152 TYR   A N    1 
ATOM   3189 C CA   . TYR   A 1 152 ? 16.999 -9.537  10.604  1.00 12.52 ?  152 TYR   A CA   1 
ATOM   3190 C C    . TYR   A 1 152 ? 16.809 -8.432  9.577   1.00 11.95 ?  152 TYR   A C    1 
ATOM   3191 O O    . TYR   A 1 152 ? 17.589 -7.473  9.534   1.00 12.40 ?  152 TYR   A O    1 
ATOM   3192 C CB   . TYR   A 1 152 ? 17.171 -8.993  12.020  1.00 13.40 ?  152 TYR   A CB   1 
ATOM   3193 C CG   . TYR   A 1 152 ? 17.125 -10.118 13.018  1.00 14.06 ?  152 TYR   A CG   1 
ATOM   3194 C CD1  . TYR   A 1 152 ? 18.256 -10.871 13.301  1.00 15.54 ?  152 TYR   A CD1  1 
ATOM   3195 C CD2  . TYR   A 1 152 ? 15.939 -10.470 13.640  1.00 14.33 ?  152 TYR   A CD2  1 
ATOM   3196 C CE1  . TYR   A 1 152 ? 18.213 -11.930 14.187  1.00 16.66 ?  152 TYR   A CE1  1 
ATOM   3197 C CE2  . TYR   A 1 152 ? 15.880 -11.537 14.532  1.00 15.61 ?  152 TYR   A CE2  1 
ATOM   3198 C CZ   . TYR   A 1 152 ? 17.024 -12.263 14.802  1.00 16.43 ?  152 TYR   A CZ   1 
ATOM   3199 O OH   . TYR   A 1 152 ? 16.984 -13.326 15.682  1.00 18.46 ?  152 TYR   A OH   1 
ATOM   3200 H H    . TYR   A 1 152 ? 18.916 -9.797  10.318  1.00 15.37 ?  152 TYR   A H    1 
ATOM   3201 H HA   . TYR   A 1 152 ? 16.234 -10.129 10.579  1.00 15.05 ?  152 TYR   A HA   1 
ATOM   3202 H HB2  . TYR   A 1 152 ? 18.032 -8.555  12.092  1.00 16.10 ?  152 TYR   A HB2  1 
ATOM   3203 H HB3  . TYR   A 1 152 ? 16.455 -8.375  12.215  1.00 16.10 ?  152 TYR   A HB3  1 
ATOM   3204 H HD1  . TYR   A 1 152 ? 19.060 -10.655 12.880  1.00 18.67 ?  152 TYR   A HD1  1 
ATOM   3205 H HD2  . TYR   A 1 152 ? 15.162 -9.984  13.452  1.00 17.21 ?  152 TYR   A HD2  1 
ATOM   3206 H HE1  . TYR   A 1 152 ? 18.984 -12.411 14.367  1.00 20.01 ?  152 TYR   A HE1  1 
ATOM   3207 H HE2  . TYR   A 1 152 ? 15.078 -11.747 14.947  1.00 18.76 ?  152 TYR   A HE2  1 
ATOM   3208 H HH   . TYR   A 1 152 ? 16.209 -13.398 15.993  1.00 22.17 ?  152 TYR   A HH   1 
ATOM   3209 N N    A LEU   A 1 153 ? 15.813 -8.618  8.713   0.72 12.09 ?  153 LEU   A N    1 
ATOM   3210 N N    B LEU   A 1 153 ? 15.754 -8.530  8.782   0.28 11.83 ?  153 LEU   A N    1 
ATOM   3211 C CA   A LEU   A 1 153 ? 15.555 -7.746  7.575   0.72 12.10 ?  153 LEU   A CA   1 
ATOM   3212 C CA   B LEU   A 1 153 ? 15.504 -7.571  7.716   0.28 11.54 ?  153 LEU   A CA   1 
ATOM   3213 C C    A LEU   A 1 153 ? 14.556 -6.660  7.943   0.72 12.50 ?  153 LEU   A C    1 
ATOM   3214 C C    B LEU   A 1 153 ? 14.527 -6.504  8.191   0.28 11.64 ?  153 LEU   A C    1 
ATOM   3215 O O    A LEU   A 1 153 ? 13.448 -6.952  8.405   0.72 13.42 ?  153 LEU   A O    1 
ATOM   3216 O O    B LEU   A 1 153 ? 13.438 -6.825  8.680   0.28 12.06 ?  153 LEU   A O    1 
ATOM   3217 C CB   A LEU   A 1 153 ? 14.987 -8.562  6.413   0.72 12.13 ?  153 LEU   A CB   1 
ATOM   3218 C CB   B LEU   A 1 153 ? 14.951 -8.279  6.480   0.28 11.59 ?  153 LEU   A CB   1 
ATOM   3219 C CG   A LEU   A 1 153 ? 15.947 -9.537  5.736   0.72 12.16 ?  153 LEU   A CG   1 
ATOM   3220 C CG   B LEU   A 1 153 ? 15.868 -9.341  5.869   0.28 11.92 ?  153 LEU   A CG   1 
ATOM   3221 C CD1  A LEU   A 1 153 ? 15.162 -10.461 4.820   0.72 12.37 ?  153 LEU   A CD1  1 
ATOM   3222 C CD1  B LEU   A 1 153 ? 15.138 -10.084 4.757   0.28 12.53 ?  153 LEU   A CD1  1 
ATOM   3223 C CD2  A LEU   A 1 153 ? 17.003 -8.777  4.954   0.72 12.09 ?  153 LEU   A CD2  1 
ATOM   3224 C CD2  B LEU   A 1 153 ? 17.166 -8.726  5.356   0.28 12.06 ?  153 LEU   A CD2  1 
ATOM   3225 H H    A LEU   A 1 153 ? 15.249 -9.274  8.774   0.72 14.53 ?  153 LEU   A H    1 
ATOM   3226 H H    B LEU   A 1 153 ? 15.149 -9.140  8.851   0.28 14.22 ?  153 LEU   A H    1 
ATOM   3227 H HA   A LEU   A 1 153 ? 16.379 -7.338  7.291   0.72 14.54 ?  153 LEU   A HA   1 
ATOM   3228 H HA   B LEU   A 1 153 ? 16.331 -7.138  7.477   0.28 13.87 ?  153 LEU   A HA   1 
ATOM   3229 H HB2  A LEU   A 1 153 ? 14.232 -9.085  6.744   0.72 14.57 ?  153 LEU   A HB2  1 
ATOM   3230 H HB2  B LEU   A 1 153 ? 14.121 -8.716  6.724   0.28 13.93 ?  153 LEU   A HB2  1 
ATOM   3231 H HB3  A LEU   A 1 153 ? 14.673 -7.950  5.732   0.72 14.57 ?  153 LEU   A HB3  1 
ATOM   3232 H HB3  B LEU   A 1 153 ? 14.780 -7.613  5.798   0.28 13.93 ?  153 LEU   A HB3  1 
ATOM   3233 H HG   A LEU   A 1 153 ? 16.391 -10.079 6.414   0.72 14.61 ?  153 LEU   A HG   1 
ATOM   3234 H HG   B LEU   A 1 153 ? 16.099 -9.985  6.557   0.28 14.32 ?  153 LEU   A HG   1 
ATOM   3235 H HD11 A LEU   A 1 153 ? 15.755 -11.149 4.483   0.72 14.86 ?  153 LEU   A HD11 1 
ATOM   3236 H HD11 B LEU   A 1 153 ? 15.720 -10.774 4.404   0.28 15.06 ?  153 LEU   A HD11 1 
ATOM   3237 H HD12 A LEU   A 1 153 ? 14.438 -10.863 5.321   0.72 14.86 ?  153 LEU   A HD12 1 
ATOM   3238 H HD12 B LEU   A 1 153 ? 14.333 -10.483 5.121   0.28 15.06 ?  153 LEU   A HD12 1 
ATOM   3239 H HD13 A LEU   A 1 153 ? 14.808 -9.938  4.083   0.72 14.86 ?  153 LEU   A HD13 1 
ATOM   3240 H HD13 B LEU   A 1 153 ? 14.907 -9.454  4.056   0.28 15.06 ?  153 LEU   A HD13 1 
ATOM   3241 H HD21 A LEU   A 1 153 ? 17.576 -9.412  4.507   0.72 14.53 ?  153 LEU   A HD21 1 
ATOM   3242 H HD21 B LEU   A 1 153 ? 17.677 -9.410  4.896   0.28 14.49 ?  153 LEU   A HD21 1 
ATOM   3243 H HD22 A LEU   A 1 153 ? 16.555 -8.212  4.306   0.72 14.53 ?  153 LEU   A HD22 1 
ATOM   3244 H HD22 B LEU   A 1 153 ? 16.953 -8.004  4.746   0.28 14.49 ?  153 LEU   A HD22 1 
ATOM   3245 H HD23 A LEU   A 1 153 ? 17.517 -8.236  5.571   0.72 14.53 ?  153 LEU   A HD23 1 
ATOM   3246 H HD23 B LEU   A 1 153 ? 17.674 -8.384  6.109   0.28 14.49 ?  153 LEU   A HD23 1 
ATOM   3247 N N    A ALA   A 1 154 ? 14.938 -5.414  7.698   0.72 12.06 ?  154 ALA   A N    1 
ATOM   3248 N N    B ALA   A 1 154 ? 14.925 -5.239  8.056   0.28 11.10 ?  154 ALA   A N    1 
ATOM   3249 C CA   A ALA   A 1 154 ? 14.082 -4.258  7.918   0.72 12.51 ?  154 ALA   A CA   1 
ATOM   3250 C CA   B ALA   A 1 154 ? 14.048 -4.099  8.293   0.28 11.68 ?  154 ALA   A CA   1 
ATOM   3251 C C    A ALA   A 1 154 ? 13.573 -3.767  6.569   0.72 11.72 ?  154 ALA   A C    1 
ATOM   3252 C C    B ALA   A 1 154 ? 13.625 -3.546  6.937   0.28 11.72 ?  154 ALA   A C    1 
ATOM   3253 O O    A ALA   A 1 154 ? 14.368 -3.389  5.701   0.72 12.42 ?  154 ALA   A O    1 
ATOM   3254 O O    B ALA   A 1 154 ? 14.477 -3.142  6.139   0.28 11.52 ?  154 ALA   A O    1 
ATOM   3255 C CB   A ALA   A 1 154 ? 14.863 -3.148  8.616   0.72 12.88 ?  154 ALA   A CB   1 
ATOM   3256 C CB   B ALA   A 1 154 ? 14.768 -3.021  9.107   0.28 11.84 ?  154 ALA   A CB   1 
ATOM   3257 H H    A ALA   A 1 154 ? 15.713 -5.213  7.386   0.72 14.50 ?  154 ALA   A H    1 
ATOM   3258 H H    B ALA   A 1 154 ? 15.724 -5.003  7.820   0.28 13.34 ?  154 ALA   A H    1 
ATOM   3259 H HA   A ALA   A 1 154 ? 13.323 -4.515  8.472   0.72 15.04 ?  154 ALA   A HA   1 
ATOM   3260 H HA   B ALA   A 1 154 ? 13.258 -4.376  8.778   0.28 14.03 ?  154 ALA   A HA   1 
ATOM   3261 H HB1  A ALA   A 1 154 ? 14.274 -2.394  8.753   0.72 15.47 ?  154 ALA   A HB1  1 
ATOM   3262 H HB1  B ALA   A 1 154 ? 14.165 -2.273  9.254   0.28 14.23 ?  154 ALA   A HB1  1 
ATOM   3263 H HB2  A ALA   A 1 154 ? 15.187 -3.480  9.467   0.72 15.47 ?  154 ALA   A HB2  1 
ATOM   3264 H HB2  B ALA   A 1 154 ? 15.038 -3.397  9.960   0.28 14.23 ?  154 ALA   A HB2  1 
ATOM   3265 H HB3  A ALA   A 1 154 ? 15.609 -2.893  8.052   0.72 15.47 ?  154 ALA   A HB3  1 
ATOM   3266 H HB3  B ALA   A 1 154 ? 15.550 -2.720  8.617   0.28 14.23 ?  154 ALA   A HB3  1 
ATOM   3267 N N    A VAL   A 1 155 ? 12.253 -3.778  6.401   0.32 9.26  ?  155 VAL   A N    1 
ATOM   3268 N N    B VAL   A 1 155 ? 12.319 -3.540  6.672   0.28 11.53 ?  155 VAL   A N    1 
ATOM   3269 C CA   A VAL   A 1 155 ? 11.580 -3.276  5.209   0.32 11.59 ?  155 VAL   A CA   1 
ATOM   3270 C CA   B VAL   A 1 155 ? 11.768 -3.060  5.405   0.28 14.09 ?  155 VAL   A CA   1 
ATOM   3271 C CA   T VAL   A 1 155 ? 11.628 -3.317  5.260   0.40 14.35 ?  155 VAL   A CA   1 
ATOM   3272 C C    A VAL   A 1 155 ? 10.899 -1.969  5.595   0.32 12.96 ?  155 VAL   A C    1 
ATOM   3273 C C    B VAL   A 1 155 ? 10.907 -1.837  5.698   0.28 16.05 ?  155 VAL   A C    1 
ATOM   3274 C C    T VAL   A 1 155 ? 11.020 -1.940  5.556   0.40 14.06 ?  155 VAL   A C    1 
ATOM   3275 O O    A VAL   A 1 155 ? 9.979  -1.960  6.421   0.32 13.90 ?  155 VAL   A O    1 
ATOM   3276 O O    B VAL   A 1 155 ? 9.825  -1.955  6.288   0.28 16.72 ?  155 VAL   A O    1 
ATOM   3277 O O    T VAL   A 1 155 ? 10.203 -1.787  6.463   0.40 14.08 ?  155 VAL   A O    1 
ATOM   3278 C CB   A VAL   A 1 155 ? 10.567 -4.292  4.663   0.32 11.78 ?  155 VAL   A CB   1 
ATOM   3279 C CB   B VAL   A 1 155 ? 10.965 -4.143  4.671   0.28 14.10 ?  155 VAL   A CB   1 
ATOM   3280 C CB   T VAL   A 1 155 ? 10.595 -4.343  4.742   0.40 14.09 ?  155 VAL   A CB   1 
ATOM   3281 C CG1  A VAL   A 1 155 ? 9.889  -3.750  3.411   0.32 12.06 ?  155 VAL   A CG1  1 
ATOM   3282 C CG1  B VAL   A 1 155 ? 10.438 -3.601  3.352   0.28 14.33 ?  155 VAL   A CG1  1 
ATOM   3283 C CG1  T VAL   A 1 155 ? 9.885  -3.816  3.503   0.40 14.33 ?  155 VAL   A CG1  1 
ATOM   3284 C CG2  A VAL   A 1 155 ? 11.252 -5.621  4.372   0.32 12.24 ?  155 VAL   A CG2  1 
ATOM   3285 C CG2  B VAL   A 1 155 ? 11.828 -5.371  4.433   0.28 14.06 ?  155 VAL   A CG2  1 
ATOM   3286 C CG2  T VAL   A 1 155 ? 11.277 -5.677  4.441   0.40 14.47 ?  155 VAL   A CG2  1 
ATOM   3287 H H    A VAL   A 1 155 ? 11.704 -4.115  6.981   0.32 11.13 ?  155 VAL   A H    1 
ATOM   3288 H H    B VAL   A 1 155 ? 11.715 -3.810  7.226   0.28 13.86 ?  155 VAL   A H    1 
ATOM   3289 H HA   A VAL   A 1 155 ? 12.235 -3.093  4.521   0.32 13.93 ?  155 VAL   A HA   1 
ATOM   3290 H HA   B VAL   A 1 155 ? 12.494 -2.786  4.826   0.28 16.93 ?  155 VAL   A HA   1 
ATOM   3291 H HB   A VAL   A 1 155 ? 9.878  -4.447  5.330   0.32 14.15 ?  155 VAL   A HB   1 
ATOM   3292 H HB   B VAL   A 1 155 ? 10.209 -4.407  5.216   0.28 16.94 ?  155 VAL   A HB   1 
ATOM   3293 H HB   T VAL   A 1 155 ? 9.927  -4.496  5.429   0.40 16.92 ?  155 VAL   A HB   1 
ATOM   3294 H HG11 A VAL   A 1 155 ? 9.357  -4.455  3.009   0.32 14.49 ?  155 VAL   A HG11 1 
ATOM   3295 H HG11 B VAL   A 1 155 ? 10.196 -4.345  2.778   0.28 17.22 ?  155 VAL   A HG11 1 
ATOM   3296 H HG11 T VAL   A 1 155 ? 9.348  -4.526  3.119   0.40 17.21 ?  155 VAL   A HG11 1 
ATOM   3297 H HG12 A VAL   A 1 155 ? 9.316  -3.005  3.655   0.32 14.49 ?  155 VAL   A HG12 1 
ATOM   3298 H HG12 B VAL   A 1 155 ? 9.662  -3.048  3.524   0.28 17.22 ?  155 VAL   A HG12 1 
ATOM   3299 H HG12 T VAL   A 1 155 ? 9.316  -3.072  3.755   0.40 17.21 ?  155 VAL   A HG12 1 
ATOM   3300 H HG13 A VAL   A 1 155 ? 10.570 -3.454  2.788   0.32 14.49 ?  155 VAL   A HG13 1 
ATOM   3301 H HG13 B VAL   A 1 155 ? 11.135 -3.074  2.931   0.28 17.22 ?  155 VAL   A HG13 1 
ATOM   3302 H HG13 T VAL   A 1 155 ? 10.550 -3.521  2.860   0.40 17.21 ?  155 VAL   A HG13 1 
ATOM   3303 H HG21 A VAL   A 1 155 ? 10.615 -6.218  3.950   0.32 14.71 ?  155 VAL   A HG21 1 
ATOM   3304 H HG21 B VAL   A 1 155 ? 11.318 -6.021  3.924   0.28 16.89 ?  155 VAL   A HG21 1 
ATOM   3305 H HG21 T VAL   A 1 155 ? 10.614 -6.308  4.119   0.40 17.39 ?  155 VAL   A HG21 1 
ATOM   3306 H HG22 A VAL   A 1 155 ? 12.002 -5.462  3.778   0.32 14.71 ?  155 VAL   A HG22 1 
ATOM   3307 H HG22 B VAL   A 1 155 ? 12.619 -5.109  3.937   0.28 16.89 ?  155 VAL   A HG22 1 
ATOM   3308 H HG22 T VAL   A 1 155 ? 11.955 -5.536  3.759   0.40 17.39 ?  155 VAL   A HG22 1 
ATOM   3309 H HG23 A VAL   A 1 155 ? 11.564 -6.003  5.206   0.32 14.71 ?  155 VAL   A HG23 1 
ATOM   3310 H HG23 B VAL   A 1 155 ? 12.084 -5.748  5.289   0.28 16.89 ?  155 VAL   A HG23 1 
ATOM   3311 H HG23 T VAL   A 1 155 ? 11.689 -6.012  5.252   0.40 17.39 ?  155 VAL   A HG23 1 
ATOM   3312 N N    A PHE   A 1 156 ? 11.345 -0.860  4.998   0.32 13.92 ?  156 PHE   A N    1 
ATOM   3313 N N    B PHE   A 1 156 ? 11.380 -0.664  5.272   0.28 17.53 ?  156 PHE   A N    1 
ATOM   3314 N N    T PHE   A 1 156 ? 11.441 -0.935  4.785   0.40 14.27 ?  156 PHE   A N    1 
ATOM   3315 C CA   A PHE   A 1 156 ? 10.814 0.445   5.389   0.32 15.23 ?  156 PHE   A CA   1 
ATOM   3316 C CA   B PHE   A 1 156 ? 10.735 0.612   5.589   0.28 19.49 ?  156 PHE   A CA   1 
ATOM   3317 C CA   T PHE   A 1 156 ? 11.040 0.442   5.070   0.40 14.58 ?  156 PHE   A CA   1 
ATOM   3318 C C    A PHE   A 1 156 ? 9.351  0.596   4.994   0.32 15.22 ?  156 PHE   A C    1 
ATOM   3319 C C    B PHE   A 1 156 ? 9.562  0.905   4.645   0.28 20.64 ?  156 PHE   A C    1 
ATOM   3320 C C    T PHE   A 1 156 ? 9.573  0.674   4.735   0.40 15.26 ?  156 PHE   A C    1 
ATOM   3321 O O    A PHE   A 1 156 ? 8.532  1.079   5.787   0.32 15.58 ?  156 PHE   A O    1 
ATOM   3322 O O    B PHE   A 1 156 ? 9.558  1.878   3.890   0.28 21.11 ?  156 PHE   A O    1 
ATOM   3323 O O    T PHE   A 1 156 ? 8.846  1.317   5.503   0.40 15.55 ?  156 PHE   A O    1 
ATOM   3324 C CB   A PHE   A 1 156 ? 11.655 1.564   4.770   0.32 15.99 ?  156 PHE   A CB   1 
ATOM   3325 C CB   B PHE   A 1 156 ? 11.776 1.727   5.545   0.28 20.37 ?  156 PHE   A CB   1 
ATOM   3326 C CB   T PHE   A 1 156 ? 11.917 1.406   4.271   0.40 13.76 ?  156 PHE   A CB   1 
ATOM   3327 C CG   A PHE   A 1 156 ? 11.151 2.948   5.092   0.32 16.74 ?  156 PHE   A CG   1 
ATOM   3328 C CG   B PHE   A 1 156 ? 11.322 3.030   6.159   0.28 21.19 ?  156 PHE   A CG   1 
ATOM   3329 C CG   T PHE   A 1 156 ? 11.578 2.862   4.480   0.40 13.78 ?  156 PHE   A CG   1 
ATOM   3330 C CD1  A PHE   A 1 156 ? 11.077 3.381   6.405   0.32 17.03 ?  156 PHE   A CD1  1 
ATOM   3331 C CD1  B PHE   A 1 156 ? 10.187 3.099   6.952   0.28 21.68 ?  156 PHE   A CD1  1 
ATOM   3332 C CD1  T PHE   A 1 156 ? 11.945 3.508   5.652   0.40 14.99 ?  156 PHE   A CD1  1 
ATOM   3333 C CD2  A PHE   A 1 156 ? 10.764 3.818   4.083   0.32 17.26 ?  156 PHE   A CD2  1 
ATOM   3334 C CD2  B PHE   A 1 156 ? 12.047 4.191   5.937   0.28 21.46 ?  156 PHE   A CD2  1 
ATOM   3335 C CD2  T PHE   A 1 156 ? 10.909 3.585   3.503   0.40 14.15 ?  156 PHE   A CD2  1 
ATOM   3336 C CE1  A PHE   A 1 156 ? 10.619 4.649   6.709   0.32 17.35 ?  156 PHE   A CE1  1 
ATOM   3337 C CE1  B PHE   A 1 156 ? 9.784  4.300   7.510   0.28 21.76 ?  156 PHE   A CE1  1 
ATOM   3338 C CE1  T PHE   A 1 156 ? 11.641 4.843   5.852   0.40 15.67 ?  156 PHE   A CE1  1 
ATOM   3339 C CE2  A PHE   A 1 156 ? 10.300 5.089   4.381   0.32 17.65 ?  156 PHE   A CE2  1 
ATOM   3340 C CE2  B PHE   A 1 156 ? 11.648 5.394   6.491   0.28 21.73 ?  156 PHE   A CE2  1 
ATOM   3341 C CE2  T PHE   A 1 156 ? 10.605 4.921   3.696   0.40 15.12 ?  156 PHE   A CE2  1 
ATOM   3342 C CZ   A PHE   A 1 156 ? 10.232 5.506   5.696   0.32 17.63 ?  156 PHE   A CZ   1 
ATOM   3343 C CZ   B PHE   A 1 156 ? 10.516 5.448   7.279   0.28 21.76 ?  156 PHE   A CZ   1 
ATOM   3344 C CZ   T PHE   A 1 156 ? 10.973 5.551   4.873   0.40 15.55 ?  156 PHE   A CZ   1 
ATOM   3345 H H    A PHE   A 1 156 ? 11.940 -0.842  4.374   0.32 16.73 ?  156 PHE   A H    1 
ATOM   3346 H H    B PHE   A 1 156 ? 12.096 -0.580  4.804   0.28 21.06 ?  156 PHE   A H    1 
ATOM   3347 H H    T PHE   A 1 156 ? 11.948 -1.029  4.100   0.40 17.14 ?  156 PHE   A H    1 
ATOM   3348 H HA   A PHE   A 1 156 ? 10.876 0.529   6.351   0.32 18.29 ?  156 PHE   A HA   1 
ATOM   3349 H HA   B PHE   A 1 156 ? 10.392 0.547   6.491   0.28 23.40 ?  156 PHE   A HA   1 
ATOM   3350 H HA   T PHE   A 1 156 ? 11.169 0.616   6.015   0.40 17.52 ?  156 PHE   A HA   1 
ATOM   3351 H HB2  A PHE   A 1 156 ? 12.567 1.495   5.102   0.32 19.21 ?  156 PHE   A HB2  1 
ATOM   3352 H HB2  B PHE   A 1 156 ? 12.566 1.437   6.027   0.28 24.46 ?  156 PHE   A HB2  1 
ATOM   3353 H HB2  T PHE   A 1 156 ? 12.840 1.272   4.536   0.40 16.53 ?  156 PHE   A HB2  1 
ATOM   3354 H HB3  A PHE   A 1 156 ? 11.652 1.464   3.804   0.32 19.21 ?  156 PHE   A HB3  1 
ATOM   3355 H HB3  B PHE   A 1 156 ? 12.007 1.904   4.619   0.28 24.46 ?  156 PHE   A HB3  1 
ATOM   3356 H HB3  T PHE   A 1 156 ? 11.813 1.206   3.328   0.40 16.53 ?  156 PHE   A HB3  1 
ATOM   3357 H HD1  A PHE   A 1 156 ? 11.337 2.809   7.093   0.32 20.46 ?  156 PHE   A HD1  1 
ATOM   3358 H HD1  B PHE   A 1 156 ? 9.691  2.330   7.114   0.28 26.04 ?  156 PHE   A HD1  1 
ATOM   3359 H HD1  T PHE   A 1 156 ? 12.390 3.029   6.319   0.40 18.01 ?  156 PHE   A HD1  1 
ATOM   3360 H HD2  A PHE   A 1 156 ? 10.810 3.542   3.196   0.32 20.73 ?  156 PHE   A HD2  1 
ATOM   3361 H HD2  B PHE   A 1 156 ? 12.811 4.161   5.407   0.28 25.77 ?  156 PHE   A HD2  1 
ATOM   3362 H HD2  T PHE   A 1 156 ? 10.658 3.162   2.715   0.40 17.00 ?  156 PHE   A HD2  1 
ATOM   3363 H HE1  A PHE   A 1 156 ? 10.573 4.927   7.597   0.32 20.84 ?  156 PHE   A HE1  1 
ATOM   3364 H HE1  B PHE   A 1 156 ? 9.021  4.333   8.041   0.28 26.13 ?  156 PHE   A HE1  1 
ATOM   3365 H HE1  T PHE   A 1 156 ? 11.887 5.258   6.647   0.40 18.82 ?  156 PHE   A HE1  1 
ATOM   3366 H HE2  A PHE   A 1 156 ? 10.044 5.663   3.696   0.32 21.20 ?  156 PHE   A HE2  1 
ATOM   3367 H HE2  B PHE   A 1 156 ? 12.144 6.165   6.333   0.28 26.09 ?  156 PHE   A HE2  1 
ATOM   3368 H HE2  T PHE   A 1 156 ? 10.153 5.392   3.039   0.40 18.16 ?  156 PHE   A HE2  1 
ATOM   3369 H HZ   A PHE   A 1 156 ? 9.924  6.360   5.901   0.32 21.18 ?  156 PHE   A HZ   1 
ATOM   3370 H HZ   B PHE   A 1 156 ? 10.246 6.257   7.653   0.28 26.13 ?  156 PHE   A HZ   1 
ATOM   3371 H HZ   T PHE   A 1 156 ? 10.766 6.446   5.008   0.40 18.67 ?  156 PHE   A HZ   1 
ATOM   3372 N N    A ASP   A 1 157 ? 9.007  0.191   3.776   0.32 15.10 ?  157 ASP   A N    1 
ATOM   3373 N N    B ASP   A 1 157 ? 8.548  0.044   4.705   0.28 21.20 ?  157 ASP   A N    1 
ATOM   3374 N N    T ASP   A 1 157 ? 9.129  0.160   3.598   0.40 15.87 ?  157 ASP   A N    1 
ATOM   3375 C CA   A ASP   A 1 157 ? 7.683  0.440   3.221   0.32 16.13 ?  157 ASP   A CA   1 
ATOM   3376 C CA   B ASP   A 1 157 ? 7.289  0.291   4.007   0.28 21.76 ?  157 ASP   A CA   1 
ATOM   3377 C CA   T ASP   A 1 157 ? 7.823  0.471   3.041   0.40 16.72 ?  157 ASP   A CA   1 
ATOM   3378 C C    A ASP   A 1 157 ? 6.702  -0.608  3.741   0.32 16.63 ?  157 ASP   A C    1 
ATOM   3379 C C    B ASP   A 1 157 ? 6.259  -0.729  4.464   0.28 22.35 ?  157 ASP   A C    1 
ATOM   3380 C C    T ASP   A 1 157 ? 6.791  -0.500  3.604   0.40 17.06 ?  157 ASP   A C    1 
ATOM   3381 O O    A ASP   A 1 157 ? 6.872  -1.808  3.492   0.32 15.99 ?  157 ASP   A O    1 
ATOM   3382 O O    B ASP   A 1 157 ? 6.600  -1.875  4.771   0.28 23.00 ?  157 ASP   A O    1 
ATOM   3383 O O    T ASP   A 1 157 ? 6.891  -1.714  3.387   0.40 16.86 ?  157 ASP   A O    1 
ATOM   3384 C CB   A ASP   A 1 157 ? 7.770  0.399   1.697   0.32 16.88 ?  157 ASP   A CB   1 
ATOM   3385 C CB   B ASP   A 1 157 ? 7.448  0.211   2.484   0.28 21.59 ?  157 ASP   A CB   1 
ATOM   3386 C CB   T ASP   A 1 157 ? 7.920  0.329   1.525   0.40 17.20 ?  157 ASP   A CB   1 
ATOM   3387 C CG   A ASP   A 1 157 ? 6.512  0.910   1.023   0.32 17.71 ?  157 ASP   A CG   1 
ATOM   3388 C CG   B ASP   A 1 157 ? 6.224  0.721   1.744   0.28 21.45 ?  157 ASP   A CG   1 
ATOM   3389 C CG   T ASP   A 1 157 ? 6.776  0.980   0.809   0.40 17.41 ?  157 ASP   A CG   1 
ATOM   3390 O OD1  A ASP   A 1 157 ? 6.236  2.125   1.104   0.32 18.47 ?  157 ASP   A OD1  1 
ATOM   3391 O OD1  B ASP   A 1 157 ? 5.910  1.925   1.857   0.28 21.35 ?  157 ASP   A OD1  1 
ATOM   3392 O OD1  T ASP   A 1 157 ? 5.685  0.378   0.798   0.40 17.75 ?  157 ASP   A OD1  1 
ATOM   3393 O OD2  A ASP   A 1 157 ? 5.801  0.090   0.405   0.32 17.73 -1 157 ASP   A OD2  1 
ATOM   3394 O OD2  B ASP   A 1 157 ? 5.574  -0.084  1.046   0.28 21.44 -1 157 ASP   A OD2  1 
ATOM   3395 O OD2  T ASP   A 1 157 ? 6.958  2.092   0.272   0.40 17.01 -1 157 ASP   A OD2  1 
ATOM   3396 H H    A ASP   A 1 157 ? 9.535  -0.238  3.246   0.32 18.14 ?  157 ASP   A H    1 
ATOM   3397 H H    B ASP   A 1 157 ? 8.565  -0.696  5.143   0.28 25.46 ?  157 ASP   A H    1 
ATOM   3398 H H    T ASP   A 1 157 ? 9.584  -0.385  3.112   0.40 19.06 ?  157 ASP   A H    1 
ATOM   3399 H HA   A ASP   A 1 157 ? 7.380  1.320   3.491   0.32 19.38 ?  157 ASP   A HA   1 
ATOM   3400 H HA   B ASP   A 1 157 ? 6.964  1.175   4.235   0.28 26.13 ?  157 ASP   A HA   1 
ATOM   3401 H HA   T ASP   A 1 157 ? 7.569  1.384   3.262   0.40 20.09 ?  157 ASP   A HA   1 
ATOM   3402 H HB2  A ASP   A 1 157 ? 8.534  0.931   1.410   0.32 20.28 ?  157 ASP   A HB2  1 
ATOM   3403 H HB2  B ASP   A 1 157 ? 8.219  0.730   2.216   0.28 25.93 ?  157 ASP   A HB2  1 
ATOM   3404 H HB2  T ASP   A 1 157 ? 8.751  0.724   1.223   0.40 20.66 ?  157 ASP   A HB2  1 
ATOM   3405 H HB3  A ASP   A 1 157 ? 7.893  -0.517  1.413   0.32 20.28 ?  157 ASP   A HB3  1 
ATOM   3406 H HB3  B ASP   A 1 157 ? 7.564  -0.717  2.229   0.28 25.93 ?  157 ASP   A HB3  1 
ATOM   3407 H HB3  T ASP   A 1 157 ? 7.912  -0.618  1.304   0.40 20.66 ?  157 ASP   A HB3  1 
ATOM   3408 N N    A LYS   A 1 158 ? 5.678  -0.157  4.473   0.32 18.19 ?  158 LYS   A N    1 
ATOM   3409 N N    B LYS   A 1 158 ? 4.994  -0.304  4.489   0.28 22.25 ?  158 LYS   A N    1 
ATOM   3410 N N    T LYS   A 1 158 ? 5.800  0.030   4.331   0.40 18.32 ?  158 LYS   A N    1 
ATOM   3411 C CA   A LYS   A 1 158 ? 4.703  -1.093  5.026   0.32 19.30 ?  158 LYS   A CA   1 
ATOM   3412 C CA   B LYS   A 1 158 ? 3.919  -1.186  4.929   0.28 22.25 ?  158 LYS   A CA   1 
ATOM   3413 C CA   T LYS   A 1 158 ? 4.805  -0.848  4.941   0.40 19.67 ?  158 LYS   A CA   1 
ATOM   3414 C C    A LYS   A 1 158 ? 3.966  -1.829  3.917   0.32 19.15 ?  158 LYS   A C    1 
ATOM   3415 C C    B LYS   A 1 158 ? 3.473  -2.124  3.808   0.28 20.90 ?  158 LYS   A C    1 
ATOM   3416 C C    T LYS   A 1 158 ? 4.041  -1.627  3.881   0.40 19.02 ?  158 LYS   A C    1 
ATOM   3417 O O    A LYS   A 1 158 ? 3.773  -3.048  3.992   0.32 19.54 ?  158 LYS   A O    1 
ATOM   3418 O O    B LYS   A 1 158 ? 3.515  -3.351  3.955   0.28 20.92 ?  158 LYS   A O    1 
ATOM   3419 O O    T LYS   A 1 158 ? 3.794  -2.827  4.040   0.40 19.24 ?  158 LYS   A O    1 
ATOM   3420 C CB   A LYS   A 1 158 ? 3.717  -0.358  5.938   0.32 20.56 ?  158 LYS   A CB   1 
ATOM   3421 C CB   B LYS   A 1 158 ? 2.736  -0.358  5.456   0.28 23.37 ?  158 LYS   A CB   1 
ATOM   3422 C CB   T LYS   A 1 158 ? 3.836  -0.058  5.823   0.40 21.83 ?  158 LYS   A CB   1 
ATOM   3423 C CG   A LYS   A 1 158 ? 2.486  -1.177  6.347   0.32 21.90 ?  158 LYS   A CG   1 
ATOM   3424 C CG   B LYS   A 1 158 ? 2.285  -0.720  6.873   0.28 24.39 ?  158 LYS   A CG   1 
ATOM   3425 C CG   T LYS   A 1 158 ? 2.612  -0.863  6.280   0.40 23.84 ?  158 LYS   A CG   1 
ATOM   3426 C CD   A LYS   A 1 158 ? 2.844  -2.441  7.131   0.32 22.90 ?  158 LYS   A CD   1 
ATOM   3427 C CD   B LYS   A 1 158 ? 2.402  -2.217  7.135   0.28 25.24 ?  158 LYS   A CD   1 
ATOM   3428 C CD   T LYS   A 1 158 ? 2.994  -2.098  7.099   0.40 25.61 ?  158 LYS   A CD   1 
ATOM   3429 C CE   A LYS   A 1 158 ? 1.590  -3.127  7.673   0.32 23.45 ?  158 LYS   A CE   1 
ATOM   3430 C CE   B LYS   A 1 158 ? 1.288  -2.729  8.018   0.28 25.76 ?  158 LYS   A CE   1 
ATOM   3431 C CE   T LYS   A 1 158 ? 1.758  -2.911  7.491   0.40 26.90 ?  158 LYS   A CE   1 
ATOM   3432 N NZ   A LYS   A 1 158 ? 1.880  -4.442  8.315   0.32 23.78 ?  158 LYS   A NZ   1 
ATOM   3433 N NZ   B LYS   A 1 158 ? 1.503  -4.154  8.393   0.28 26.08 ?  158 LYS   A NZ   1 
ATOM   3434 N NZ   T LYS   A 1 158 ? 2.090  -4.126  8.294   0.40 27.60 ?  158 LYS   A NZ   1 
ATOM   3435 H H    A LYS   A 1 158 ? 5.534  0.670   4.655   0.32 21.85 ?  158 LYS   A H    1 
ATOM   3436 H H    B LYS   A 1 158 ? 4.730  0.483   4.269   0.28 26.73 ?  158 LYS   A H    1 
ATOM   3437 H H    T LYS   A 1 158 ? 5.685  0.871   4.479   0.40 22.01 ?  158 LYS   A H    1 
ATOM   3438 H HA   A LYS   A 1 158 ? 5.170  -1.751  5.561   0.32 23.18 ?  158 LYS   A HA   1 
ATOM   3439 H HA   B LYS   A 1 158 ? 4.270  -1.727  5.651   0.28 26.72 ?  158 LYS   A HA   1 
ATOM   3440 H HA   T LYS   A 1 158 ? 5.263  -1.488  5.511   0.40 23.62 ?  158 LYS   A HA   1 
ATOM   3441 H HB2  A LYS   A 1 158 ? 4.182  -0.096  6.749   0.32 24.69 ?  158 LYS   A HB2  1 
ATOM   3442 H HB2  B LYS   A 1 158 ? 2.986  0.582   5.465   0.28 28.06 ?  158 LYS   A HB2  1 
ATOM   3443 H HB2  T LYS   A 1 158 ? 4.307  0.237   6.621   0.40 26.22 ?  158 LYS   A HB2  1 
ATOM   3444 H HB3  A LYS   A 1 158 ? 3.404  0.435   5.476   0.32 24.69 ?  158 LYS   A HB3  1 
ATOM   3445 H HB3  B LYS   A 1 158 ? 1.971  -0.483  4.872   0.28 28.06 ?  158 LYS   A HB3  1 
ATOM   3446 H HB3  T LYS   A 1 158 ? 3.516  0.711   5.329   0.40 26.22 ?  158 LYS   A HB3  1 
ATOM   3447 H HG2  A LYS   A 1 158 ? 1.925  -0.626  6.912   0.32 26.30 ?  158 LYS   A HG2  1 
ATOM   3448 H HG2  B LYS   A 1 158 ? 2.842  -0.249  7.516   0.28 29.29 ?  158 LYS   A HG2  1 
ATOM   3449 H HG2  T LYS   A 1 158 ? 2.058  -0.300  6.839   0.40 28.62 ?  158 LYS   A HG2  1 
ATOM   3450 H HG3  A LYS   A 1 158 ? 1.991  -1.439  5.554   0.32 26.30 ?  158 LYS   A HG3  1 
ATOM   3451 H HG3  B LYS   A 1 158 ? 1.354  -0.465  6.991   0.28 29.29 ?  158 LYS   A HG3  1 
ATOM   3452 H HG3  T LYS   A 1 158 ? 2.103  -1.157  5.506   0.40 28.62 ?  158 LYS   A HG3  1 
ATOM   3453 H HD2  A LYS   A 1 158 ? 3.306  -3.063  6.548   0.32 27.50 ?  158 LYS   A HD2  1 
ATOM   3454 H HD2  B LYS   A 1 158 ? 2.355  -2.695  6.291   0.28 30.31 ?  158 LYS   A HD2  1 
ATOM   3455 H HD2  T LYS   A 1 158 ? 3.576  -2.670  6.575   0.40 30.75 ?  158 LYS   A HD2  1 
ATOM   3456 H HD3  A LYS   A 1 158 ? 3.406  -2.202  7.884   0.32 27.50 ?  158 LYS   A HD3  1 
ATOM   3457 H HD3  B LYS   A 1 158 ? 3.256  -2.393  7.570   0.28 30.31 ?  158 LYS   A HD3  1 
ATOM   3458 H HD3  T LYS   A 1 158 ? 3.441  -1.818  7.913   0.40 30.75 ?  158 LYS   A HD3  1 
ATOM   3459 H HE2  A LYS   A 1 158 ? 1.178  -2.552  8.338   0.32 28.16 ?  158 LYS   A HE2  1 
ATOM   3460 H HE2  B LYS   A 1 158 ? 1.254  -2.199  8.827   0.28 30.93 ?  158 LYS   A HE2  1 
ATOM   3461 H HE2  T LYS   A 1 158 ? 1.167  -2.355  8.022   0.40 32.31 ?  158 LYS   A HE2  1 
ATOM   3462 H HE3  A LYS   A 1 158 ? 0.973  -3.280  6.941   0.32 28.16 ?  158 LYS   A HE3  1 
ATOM   3463 H HE3  B LYS   A 1 158 ? 0.448  -2.663  7.535   0.28 30.93 ?  158 LYS   A HE3  1 
ATOM   3464 H HE3  T LYS   A 1 158 ? 1.302  -3.203  6.685   0.40 32.31 ?  158 LYS   A HE3  1 
ATOM   3465 H HZ1  A LYS   A 1 158 ? 1.126  -4.806  8.616   0.32 28.55 ?  158 LYS   A HZ1  1 
ATOM   3466 H HZ1  B LYS   A 1 158 ? 0.770  -4.482  8.775   0.28 31.32 ?  158 LYS   A HZ1  1 
ATOM   3467 H HZ1  T LYS   A 1 158 ? 1.345  -4.569  8.499   0.40 33.14 ?  158 LYS   A HZ1  1 
ATOM   3468 H HZ2  A LYS   A 1 158 ? 2.252  -4.993  7.723   0.32 28.55 ?  158 LYS   A HZ2  1 
ATOM   3469 H HZ2  B LYS   A 1 158 ? 1.693  -4.635  7.669   0.28 31.32 ?  158 LYS   A HZ2  1 
ATOM   3470 H HZ2  T LYS   A 1 158 ? 2.625  -4.663  7.827   0.40 33.14 ?  158 LYS   A HZ2  1 
ATOM   3471 H HZ3  A LYS   A 1 158 ? 2.440  -4.330  8.998   0.32 28.55 ?  158 LYS   A HZ3  1 
ATOM   3472 H HZ3  B LYS   A 1 158 ? 2.183  -4.217  8.964   0.28 31.32 ?  158 LYS   A HZ3  1 
ATOM   3473 H HZ3  T LYS   A 1 158 ? 2.503  -3.890  9.046   0.40 33.14 ?  158 LYS   A HZ3  1 
ATOM   3474 N N    A ASN   A 1 159 ? 3.548  -1.109  2.876   0.32 19.09 ?  159 ASN   A N    1 
ATOM   3475 N N    B ASN   A 1 159 ? 3.037  -1.558  2.678   0.28 19.83 ?  159 ASN   A N    1 
ATOM   3476 N N    T ASN   A 1 159 ? 3.649  -0.966  2.800   0.40 19.12 ?  159 ASN   A N    1 
ATOM   3477 C CA   A ASN   A 1 159 ? 2.861  -1.768  1.773   0.32 18.67 ?  159 ASN   A CA   1 
ATOM   3478 C CA   B ASN   A 1 159 ? 2.562  -2.376  1.564   0.28 18.90 ?  159 ASN   A CA   1 
ATOM   3479 C CA   T ASN   A 1 159 ? 2.920  -1.652  1.744   0.40 19.12 ?  159 ASN   A CA   1 
ATOM   3480 C C    A ASN   A 1 159 ? 3.749  -2.826  1.129   0.32 17.71 ?  159 ASN   A C    1 
ATOM   3481 C C    B ASN   A 1 159 ? 3.591  -3.427  1.174   0.28 18.04 ?  159 ASN   A C    1 
ATOM   3482 C C    T ASN   A 1 159 ? 3.752  -2.757  1.101   0.40 19.05 ?  159 ASN   A C    1 
ATOM   3483 O O    A ASN   A 1 159 ? 3.292  -3.938  0.839   0.32 17.42 ?  159 ASN   A O    1 
ATOM   3484 O O    B ASN   A 1 159 ? 3.250  -4.592  0.939   0.28 17.43 ?  159 ASN   A O    1 
ATOM   3485 O O    T ASN   A 1 159 ? 3.222  -3.808  0.749   0.40 18.91 ?  159 ASN   A O    1 
ATOM   3486 C CB   A ASN   A 1 159 ? 2.380  -0.731  0.756   0.32 19.69 ?  159 ASN   A CB   1 
ATOM   3487 C CB   B ASN   A 1 159 ? 2.249  -1.484  0.361   0.28 19.13 ?  159 ASN   A CB   1 
ATOM   3488 C CB   T ASN   A 1 159 ? 2.408  -0.660  0.697   0.40 20.05 ?  159 ASN   A CB   1 
ATOM   3489 C CG   A ASN   A 1 159 ? 1.170  0.045   1.246   0.32 20.89 ?  159 ASN   A CG   1 
ATOM   3490 C CG   B ASN   A 1 159 ? 0.805  -1.036  0.321   0.28 19.52 ?  159 ASN   A CG   1 
ATOM   3491 C CG   T ASN   A 1 159 ? 1.196  0.121   1.180   0.40 21.18 ?  159 ASN   A CG   1 
ATOM   3492 O OD1  A ASN   A 1 159 ? 0.342  -0.485  1.987   0.32 21.77 ?  159 ASN   A OD1  1 
ATOM   3493 O OD1  B ASN   A 1 159 ? 0.162  -0.878  1.357   0.28 20.00 ?  159 ASN   A OD1  1 
ATOM   3494 O OD1  T ASN   A 1 159 ? 0.416  -0.372  1.993   0.40 22.11 ?  159 ASN   A OD1  1 
ATOM   3495 N ND2  A ASN   A 1 159 ? 1.061  1.304   0.838   0.32 21.23 ?  159 ASN   A ND2  1 
ATOM   3496 N ND2  B ASN   A 1 159 ? 0.284  -0.835  -0.885  0.28 19.56 ?  159 ASN   A ND2  1 
ATOM   3497 N ND2  T ASN   A 1 159 ? 1.034  1.339   0.684   0.40 21.53 ?  159 ASN   A ND2  1 
ATOM   3498 H H    A ASN   A 1 159 ? 3.652  -0.260  2.788   0.32 22.93 ?  159 ASN   A H    1 
ATOM   3499 H H    B ASN   A 1 159 ? 3.017  -0.713  2.537   0.28 23.82 ?  159 ASN   A H    1 
ATOM   3500 H H    T ASN   A 1 159 ? 3.782  -0.130  2.664   0.40 22.96 ?  159 ASN   A H    1 
ATOM   3501 H HA   A ASN   A 1 159 ? 2.076  -2.217  2.122   0.32 22.42 ?  159 ASN   A HA   1 
ATOM   3502 H HA   B ASN   A 1 159 ? 1.742  -2.825  1.824   0.28 22.70 ?  159 ASN   A HA   1 
ATOM   3503 H HA   T ASN   A 1 159 ? 2.147  -2.079  2.139   0.40 22.97 ?  159 ASN   A HA   1 
ATOM   3504 H HB2  A ASN   A 1 159 ? 3.089  -0.094  0.587   0.32 23.65 ?  159 ASN   A HB2  1 
ATOM   3505 H HB2  B ASN   A 1 159 ? 2.808  -0.688  0.400   0.28 22.98 ?  159 ASN   A HB2  1 
ATOM   3506 H HB2  T ASN   A 1 159 ? 3.107  -0.025  0.490   0.40 24.08 ?  159 ASN   A HB2  1 
ATOM   3507 H HB3  A ASN   A 1 159 ? 2.134  -1.184  -0.067  0.32 23.65 ?  159 ASN   A HB3  1 
ATOM   3508 H HB3  B ASN   A 1 159 ? 2.430  -1.973  -0.454  0.28 22.98 ?  159 ASN   A HB3  1 
ATOM   3509 H HB3  T ASN   A 1 159 ? 2.155  -1.152  -0.104  0.40 24.08 ?  159 ASN   A HB3  1 
ATOM   3510 H HD21 A ASN   A 1 159 ? 0.389  1.780   1.087   0.32 25.49 ?  159 ASN   A HD21 1 
ATOM   3511 H HD21 B ASN   A 1 159 ? -0.533 -0.577  -0.965  0.28 23.50 ?  159 ASN   A HD21 1 
ATOM   3512 H HD21 T ASN   A 1 159 ? 0.359  1.812   0.926   0.40 25.86 ?  159 ASN   A HD21 1 
ATOM   3513 H HD22 A ASN   A 1 159 ? 1.661  1.641   0.325   0.32 25.49 ?  159 ASN   A HD22 1 
ATOM   3514 H HD22 B ASN   A 1 159 ? 0.764  -0.962  -1.588  0.28 23.50 ?  159 ASN   A HD22 1 
ATOM   3515 H HD22 T ASN   A 1 159 ? 1.603  1.650   0.124   0.40 25.86 ?  159 ASN   A HD22 1 
ATOM   3516 N N    A LEU   A 1 160 ? 5.029  -2.517  0.924   0.32 16.67 ?  160 LEU   A N    1 
ATOM   3517 N N    B LEU   A 1 160 ? 4.860  -3.027  1.093   0.28 17.87 ?  160 LEU   A N    1 
ATOM   3518 N N    T LEU   A 1 160 ? 5.054  -2.543  0.963   0.40 18.82 ?  160 LEU   A N    1 
ATOM   3519 C CA   A LEU   A 1 160 ? 5.932  -3.526  0.382   0.32 15.46 ?  160 LEU   A CA   1 
ATOM   3520 C CA   B LEU   A 1 160 ? 5.913  -3.957  0.705   0.28 17.55 ?  160 LEU   A CA   1 
ATOM   3521 C CA   T LEU   A 1 160 ? 5.908  -3.593  0.423   0.40 18.18 ?  160 LEU   A CA   1 
ATOM   3522 C C    A LEU   A 1 160 ? 6.099  -4.694  1.348   0.32 13.59 ?  160 LEU   A C    1 
ATOM   3523 C C    B LEU   A 1 160 ? 6.109  -5.041  1.755   0.28 16.11 ?  160 LEU   A C    1 
ATOM   3524 O O    A LEU   A 1 160 ? 6.105  -5.858  0.933   0.32 12.49 ?  160 LEU   A O    1 
ATOM   3525 O O    B LEU   A 1 160 ? 6.175  -6.228  1.421   0.28 15.54 ?  160 LEU   A O    1 
ATOM   3526 C CB   A LEU   A 1 160 ? 7.285  -2.904  0.054   0.32 15.49 ?  160 LEU   A CB   1 
ATOM   3527 C CB   B LEU   A 1 160 ? 7.218  -3.205  0.462   0.28 18.82 ?  160 LEU   A CB   1 
ATOM   3528 C CB   T LEU   A 1 160 ? 7.277  -3.047  0.038   0.40 17.43 ?  160 LEU   A CB   1 
ATOM   3529 C CG   A LEU   A 1 160 ? 8.343  -3.935  -0.336  0.32 16.33 ?  160 LEU   A CG   1 
ATOM   3530 C CG   B LEU   A 1 160 ? 7.579  -3.012  -1.009  0.28 20.07 ?  160 LEU   A CG   1 
ATOM   3531 C CG   T LEU   A 1 160 ? 8.271  -4.126  -0.381  0.40 17.56 ?  160 LEU   A CG   1 
ATOM   3532 C CD1  A LEU   A 1 160 ? 7.895  -4.733  -1.546  0.32 16.89 ?  160 LEU   A CD1  1 
ATOM   3533 C CD1  B LEU   A 1 160 ? 6.640  -2.010  -1.662  0.28 20.48 ?  160 LEU   A CD1  1 
ATOM   3534 C CD1  T LEU   A 1 160 ? 7.787  -4.861  -1.614  0.40 18.00 ?  160 LEU   A CD1  1 
ATOM   3535 C CD2  A LEU   A 1 160 ? 9.667  -3.257  -0.600  0.32 16.49 ?  160 LEU   A CD2  1 
ATOM   3536 C CD2  B LEU   A 1 160 ? 9.026  -2.578  -1.155  0.28 20.36 ?  160 LEU   A CD2  1 
ATOM   3537 C CD2  T LEU   A 1 160 ? 9.625  -3.500  -0.631  0.40 17.49 ?  160 LEU   A CD2  1 
ATOM   3538 H H    A LEU   A 1 160 ? 5.387  -1.750  1.092   0.32 20.02 ?  160 LEU   A H    1 
ATOM   3539 H H    B LEU   A 1 160 ? 5.126  -2.229  1.253   0.28 21.47 ?  160 LEU   A H    1 
ATOM   3540 H H    T LEU   A 1 160 ? 5.464  -1.811  1.175   0.40 22.60 ?  160 LEU   A H    1 
ATOM   3541 H HA   A LEU   A 1 160 ? 5.553  -3.865  -0.441  0.32 18.57 ?  160 LEU   A HA   1 
ATOM   3542 H HA   B LEU   A 1 160 ? 5.660  -4.393  -0.121  0.28 21.08 ?  160 LEU   A HA   1 
ATOM   3543 H HB2  A LEU   A 1 160 ? 7.184  -2.271  -0.682  0.32 18.61 ?  160 LEU   A HB2  1 
ATOM   3544 H HB2  B LEU   A 1 160 ? 7.146  -2.326  0.863   0.28 22.61 ?  160 LEU   A HB2  1 
ATOM   3545 H HB2  T LEU   A 1 160 ? 7.181  -2.417  -0.699  0.40 20.93 ?  160 LEU   A HB2  1 
ATOM   3546 H HB3  A LEU   A 1 160 ? 7.610  -2.444  0.841   0.32 18.61 ?  160 LEU   A HB3  1 
ATOM   3547 H HB3  B LEU   A 1 160 ? 7.942  -3.696  0.882   0.28 22.61 ?  160 LEU   A HB3  1 
ATOM   3548 H HB3  T LEU   A 1 160 ? 7.653  -2.597  0.808   0.40 20.93 ?  160 LEU   A HB3  1 
ATOM   3549 H HG   A LEU   A 1 160 ? 8.478  -4.551  0.400   0.32 19.61 ?  160 LEU   A HG   1 
ATOM   3550 H HG   B LEU   A 1 160 ? 7.475  -3.858  -1.468  0.28 24.10 ?  160 LEU   A HG   1 
ATOM   3551 H HG   T LEU   A 1 160 ? 8.366  -4.768  0.339   0.40 21.09 ?  160 LEU   A HG   1 
ATOM   3552 H HD11 A LEU   A 1 160 ? 8.630  -5.290  -1.842  0.32 20.29 ?  160 LEU   A HD11 1 
ATOM   3553 H HD11 B LEU   A 1 160 ? 6.896  -1.897  -2.590  0.28 24.60 ?  160 LEU   A HD11 1 
ATOM   3554 H HD11 T LEU   A 1 160 ? 8.480  -5.473  -1.907  0.40 21.62 ?  160 LEU   A HD11 1 
ATOM   3555 H HD12 A LEU   A 1 160 ? 7.139  -5.288  -1.298  0.32 20.29 ?  160 LEU   A HD12 1 
ATOM   3556 H HD12 B LEU   A 1 160 ? 5.731  -2.347  -1.607  0.28 24.60 ?  160 LEU   A HD12 1 
ATOM   3557 H HD12 T LEU   A 1 160 ? 6.982  -5.351  -1.393  0.40 21.62 ?  160 LEU   A HD12 1 
ATOM   3558 H HD13 A LEU   A 1 160 ? 7.639  -4.118  -2.251  0.32 20.29 ?  160 LEU   A HD13 1 
ATOM   3559 H HD13 B LEU   A 1 160 ? 6.706  -1.163  -1.194  0.28 24.60 ?  160 LEU   A HD13 1 
ATOM   3560 H HD13 T LEU   A 1 160 ? 7.602  -4.213  -2.313  0.40 21.62 ?  160 LEU   A HD13 1 
ATOM   3561 H HD21 A LEU   A 1 160 ? 10.323 -3.932  -0.840  0.32 19.81 ?  160 LEU   A HD21 1 
ATOM   3562 H HD21 B LEU   A 1 160 ? 9.218  -2.435  -2.094  0.28 24.45 ?  160 LEU   A HD21 1 
ATOM   3563 H HD21 T LEU   A 1 160 ? 10.251 -4.193  -0.895  0.40 21.01 ?  160 LEU   A HD21 1 
ATOM   3564 H HD22 A LEU   A 1 160 ? 9.560  -2.626  -1.327  0.32 19.81 ?  160 LEU   A HD22 1 
ATOM   3565 H HD22 B LEU   A 1 160 ? 9.155  -1.753  -0.662  0.28 24.45 ?  160 LEU   A HD22 1 
ATOM   3566 H HD22 T LEU   A 1 160 ? 9.544  -2.841  -1.339  0.40 21.01 ?  160 LEU   A HD22 1 
ATOM   3567 H HD23 A LEU   A 1 160 ? 9.951  -2.793  0.204   0.32 19.81 ?  160 LEU   A HD23 1 
ATOM   3568 H HD23 B LEU   A 1 160 ? 9.604  -3.273  -0.798  0.28 24.45 ?  160 LEU   A HD23 1 
ATOM   3569 H HD23 T LEU   A 1 160 ? 9.932  -3.071  0.184   0.40 21.01 ?  160 LEU   A HD23 1 
ATOM   3570 N N    A TYR   A 1 161 ? 6.252  -4.400  2.639   0.72 15.29 ?  161 TYR   A N    1 
ATOM   3571 N N    B TYR   A 1 161 ? 6.217  -4.651  3.030   0.28 16.29 ?  161 TYR   A N    1 
ATOM   3572 C CA   A TYR   A 1 161 ? 6.377  -5.462  3.633   0.72 15.10 ?  161 TYR   A CA   1 
ATOM   3573 C CA   B TYR   A 1 161 ? 6.380  -5.636  4.096   0.28 16.20 ?  161 TYR   A CA   1 
ATOM   3574 C C    A TYR   A 1 161 ? 5.213  -6.441  3.552   0.72 16.17 ?  161 TYR   A C    1 
ATOM   3575 C C    B TYR   A 1 161 ? 5.242  -6.651  4.081   0.28 16.40 ?  161 TYR   A C    1 
ATOM   3576 O O    A TYR   A 1 161 ? 5.410  -7.661  3.548   0.72 15.66 ?  161 TYR   A O    1 
ATOM   3577 O O    B TYR   A 1 161 ? 5.477  -7.864  4.077   0.28 16.08 ?  161 TYR   A O    1 
ATOM   3578 C CB   A TYR   A 1 161 ? 6.464  -4.860  5.033   0.72 15.02 ?  161 TYR   A CB   1 
ATOM   3579 C CB   B TYR   A 1 161 ? 6.470  -4.941  5.458   0.28 16.41 ?  161 TYR   A CB   1 
ATOM   3580 C CG   A TYR   A 1 161 ? 6.367  -5.902  6.113   0.72 14.40 ?  161 TYR   A CG   1 
ATOM   3581 C CG   B TYR   A 1 161 ? 6.378  -5.896  6.628   0.28 16.22 ?  161 TYR   A CG   1 
ATOM   3582 C CD1  A TYR   A 1 161 ? 7.476  -6.645  6.482   0.72 13.66 ?  161 TYR   A CD1  1 
ATOM   3583 C CD1  B TYR   A 1 161 ? 5.149  -6.220  7.186   0.28 16.44 ?  161 TYR   A CD1  1 
ATOM   3584 C CD2  A TYR   A 1 161 ? 5.162  -6.154  6.758   0.72 14.61 ?  161 TYR   A CD2  1 
ATOM   3585 C CD2  B TYR   A 1 161 ? 7.517  -6.476  7.171   0.28 15.90 ?  161 TYR   A CD2  1 
ATOM   3586 C CE1  A TYR   A 1 161 ? 7.394  -7.609  7.460   0.72 13.36 ?  161 TYR   A CE1  1 
ATOM   3587 C CE1  B TYR   A 1 161 ? 5.055  -7.093  8.245   0.28 16.47 ?  161 TYR   A CE1  1 
ATOM   3588 C CE2  A TYR   A 1 161 ? 5.069  -7.120  7.739   0.72 14.27 ?  161 TYR   A CE2  1 
ATOM   3589 C CE2  B TYR   A 1 161 ? 7.431  -7.353  8.235   0.28 16.06 ?  161 TYR   A CE2  1 
ATOM   3590 C CZ   A TYR   A 1 161 ? 6.190  -7.845  8.086   0.72 13.64 ?  161 TYR   A CZ   1 
ATOM   3591 C CZ   B TYR   A 1 161 ? 6.196  -7.656  8.769   0.28 16.42 ?  161 TYR   A CZ   1 
ATOM   3592 O OH   A TYR   A 1 161 ? 6.130  -8.813  9.060   0.72 14.23 ?  161 TYR   A OH   1 
ATOM   3593 O OH   B TYR   A 1 161 ? 6.093  -8.526  9.829   0.28 16.94 ?  161 TYR   A OH   1 
ATOM   3594 H H    A TYR   A 1 161 ? 6.279  -3.603  2.964   0.72 18.37 ?  161 TYR   A H    1 
ATOM   3595 H H    B TYR   A 1 161 ? 6.203  -3.833  3.299   0.28 19.57 ?  161 TYR   A H    1 
ATOM   3596 H HA   A TYR   A 1 161 ? 7.190  -5.955  3.466   0.72 18.14 ?  161 TYR   A HA   1 
ATOM   3597 H HA   B TYR   A 1 161 ? 7.210  -6.116  3.957   0.28 19.46 ?  161 TYR   A HA   1 
ATOM   3598 H HB2  A TYR   A 1 161 ? 7.320  -4.411  5.133   0.72 18.05 ?  161 TYR   A HB2  1 
ATOM   3599 H HB2  B TYR   A 1 161 ? 7.321  -4.478  5.521   0.28 19.71 ?  161 TYR   A HB2  1 
ATOM   3600 H HB3  A TYR   A 1 161 ? 5.740  -4.230  5.161   0.72 18.05 ?  161 TYR   A HB3  1 
ATOM   3601 H HB3  B TYR   A 1 161 ? 5.743  -4.305  5.538   0.28 19.71 ?  161 TYR   A HB3  1 
ATOM   3602 H HD1  A TYR   A 1 161 ? 8.289  -6.496  6.059   0.72 16.41 ?  161 TYR   A HD1  1 
ATOM   3603 H HD1  B TYR   A 1 161 ? 4.374  -5.844  6.837   0.28 19.74 ?  161 TYR   A HD1  1 
ATOM   3604 H HD2  A TYR   A 1 161 ? 4.401  -5.675  6.530   0.72 17.55 ?  161 TYR   A HD2  1 
ATOM   3605 H HD2  B TYR   A 1 161 ? 8.350  -6.271  6.814   0.28 19.10 ?  161 TYR   A HD2  1 
ATOM   3606 H HE1  A TYR   A 1 161 ? 8.149  -8.108  7.693   0.72 16.06 ?  161 TYR   A HE1  1 
ATOM   3607 H HE1  B TYR   A 1 161 ? 4.223  -7.299  8.606   0.28 19.78 ?  161 TYR   A HE1  1 
ATOM   3608 H HE2  A TYR   A 1 161 ? 4.254  -7.289  8.167   0.72 17.15 ?  161 TYR   A HE2  1 
ATOM   3609 H HE2  B TYR   A 1 161 ? 8.202  -7.732  8.592   0.28 19.29 ?  161 TYR   A HE2  1 
ATOM   3610 H HH   A TYR   A 1 161 ? 6.878  -9.182  9.166   0.72 17.10 ?  161 TYR   A HH   1 
ATOM   3611 H HH   B TYR   A 1 161 ? 6.854  -8.791  10.057  0.28 20.35 ?  161 TYR   A HH   1 
ATOM   3612 N N    A ASP   A 1 162 ? 3.984  -5.921  3.504   0.72 17.14 ?  162 ASP   A N    1 
ATOM   3613 N N    B ASP   A 1 162 ? 3.996  -6.172  4.086   0.28 17.02 ?  162 ASP   A N    1 
ATOM   3614 C CA   A ASP   A 1 162 ? 2.824  -6.806  3.448   0.72 18.14 ?  162 ASP   A CA   1 
ATOM   3615 C CA   B ASP   A 1 162 ? 2.859  -7.086  4.035   0.28 17.61 ?  162 ASP   A CA   1 
ATOM   3616 C C    A ASP   A 1 162 ? 2.862  -7.668  2.194   0.72 18.24 ?  162 ASP   A C    1 
ATOM   3617 C C    B ASP   A 1 162 ? 2.904  -7.941  2.778   0.28 17.91 ?  162 ASP   A C    1 
ATOM   3618 O O    A ASP   A 1 162 ? 2.520  -8.857  2.235   0.72 18.46 ?  162 ASP   A O    1 
ATOM   3619 O O    B ASP   A 1 162 ? 2.566  -9.130  2.812   0.28 17.79 ?  162 ASP   A O    1 
ATOM   3620 C CB   A ASP   A 1 162 ? 1.523  -5.998  3.502   0.72 19.79 ?  162 ASP   A CB   1 
ATOM   3621 C CB   B ASP   A 1 162 ? 1.546  -6.303  4.096   0.28 18.00 ?  162 ASP   A CB   1 
ATOM   3622 C CG   A ASP   A 1 162 ? 1.253  -5.385  4.865   0.72 21.33 ?  162 ASP   A CG   1 
ATOM   3623 C CG   B ASP   A 1 162 ? 1.251  -5.765  5.479   0.28 18.49 ?  162 ASP   A CG   1 
ATOM   3624 O OD1  A ASP   A 1 162 ? 1.863  -5.817  5.862   0.72 22.29 ?  162 ASP   A OD1  1 
ATOM   3625 O OD1  B ASP   A 1 162 ? 1.918  -6.198  6.442   0.28 18.91 ?  162 ASP   A OD1  1 
ATOM   3626 O OD2  A ASP   A 1 162 ? 0.389  -4.481  4.936   0.72 22.39 -1 162 ASP   A OD2  1 
ATOM   3627 O OD2  B ASP   A 1 162 ? 0.349  -4.908  5.601   0.28 18.69 -1 162 ASP   A OD2  1 
ATOM   3628 H H    A ASP   A 1 162 ? 3.797  -5.078  3.495   0.72 20.59 ?  162 ASP   A H    1 
ATOM   3629 H H    B ASP   A 1 162 ? 3.789  -5.340  4.114   0.28 20.44 ?  162 ASP   A H    1 
ATOM   3630 H HA   A ASP   A 1 162 ? 2.841  -7.395  4.213   0.72 21.78 ?  162 ASP   A HA   1 
ATOM   3631 H HA   B ASP   A 1 162 ? 2.894  -7.680  4.799   0.28 21.15 ?  162 ASP   A HA   1 
ATOM   3632 H HB2  A ASP   A 1 162 ? 1.567  -5.272  2.869   0.72 23.77 ?  162 ASP   A HB2  1 
ATOM   3633 H HB2  B ASP   A 1 162 ? 1.594  -5.552  3.488   0.28 21.62 ?  162 ASP   A HB2  1 
ATOM   3634 H HB3  A ASP   A 1 162 ? 0.778  -6.582  3.302   0.72 23.77 ?  162 ASP   A HB3  1 
ATOM   3635 H HB3  B ASP   A 1 162 ? 0.816  -6.892  3.843   0.28 21.62 ?  162 ASP   A HB3  1 
ATOM   3636 N N    A LYS   A 1 163 ? 3.286  -7.089  1.069   0.72 18.88 ?  163 LYS   A N    1 
ATOM   3637 N N    B LYS   A 1 163 ? 3.320  -7.352  1.657   0.28 18.62 ?  163 LYS   A N    1 
ATOM   3638 C CA   A LYS   A 1 163 ? 3.386  -7.868  -0.160  0.72 19.64 ?  163 LYS   A CA   1 
ATOM   3639 C CA   B LYS   A 1 163 ? 3.387  -8.104  0.410   0.28 19.40 ?  163 LYS   A CA   1 
ATOM   3640 C C    A LYS   A 1 163 ? 4.462  -8.941  -0.050  0.72 19.09 ?  163 LYS   A C    1 
ATOM   3641 C C    B LYS   A 1 163 ? 4.517  -9.129  0.445   0.28 18.95 ?  163 LYS   A C    1 
ATOM   3642 O O    A LYS   A 1 163 ? 4.298  -10.047 -0.574  0.72 19.26 ?  163 LYS   A O    1 
ATOM   3643 O O    B LYS   A 1 163 ? 4.370  -10.240 -0.077  0.28 19.03 ?  163 LYS   A O    1 
ATOM   3644 C CB   A LYS   A 1 163 ? 3.664  -6.947  -1.349  0.72 21.96 ?  163 LYS   A CB   1 
ATOM   3645 C CB   B LYS   A 1 163 ? 3.560  -7.135  -0.757  0.28 21.01 ?  163 LYS   A CB   1 
ATOM   3646 C CG   A LYS   A 1 163 ? 3.775  -7.682  -2.675  0.72 24.79 ?  163 LYS   A CG   1 
ATOM   3647 C CG   B LYS   A 1 163 ? 3.190  -7.695  -2.109  0.28 22.54 ?  163 LYS   A CG   1 
ATOM   3648 C CD   A LYS   A 1 163 ? 4.178  -6.748  -3.799  0.72 27.73 ?  163 LYS   A CD   1 
ATOM   3649 C CD   B LYS   A 1 163 ? 3.328  -6.621  -3.171  0.28 23.79 ?  163 LYS   A CD   1 
ATOM   3650 C CE   A LYS   A 1 163 ? 4.140  -7.457  -5.143  0.72 29.97 ?  163 LYS   A CE   1 
ATOM   3651 C CE   B LYS   A 1 163 ? 3.781  -7.207  -4.492  0.28 24.81 ?  163 LYS   A CE   1 
ATOM   3652 N NZ   A LYS   A 1 163 ? 4.773  -6.651  -6.222  0.72 31.20 ?  163 LYS   A NZ   1 
ATOM   3653 N NZ   B LYS   A 1 163 ? 4.114  -6.148  -5.483  0.28 25.26 ?  163 LYS   A NZ   1 
ATOM   3654 H H    A LYS   A 1 163 ? 3.513  -6.256  0.993   0.72 22.67 ?  163 LYS   A H    1 
ATOM   3655 H H    B LYS   A 1 163 ? 3.563  -6.529  1.594   0.28 22.36 ?  163 LYS   A H    1 
ATOM   3656 H HA   A LYS   A 1 163 ? 2.535  -8.305  -0.320  0.72 23.59 ?  163 LYS   A HA   1 
ATOM   3657 H HA   B LYS   A 1 163 ? 2.554  -8.580  0.282   0.28 23.30 ?  163 LYS   A HA   1 
ATOM   3658 H HB2  A LYS   A 1 163 ? 2.934  -6.305  -1.429  0.72 26.37 ?  163 LYS   A HB2  1 
ATOM   3659 H HB2  B LYS   A 1 163 ? 2.997  -6.361  -0.604  0.28 25.24 ?  163 LYS   A HB2  1 
ATOM   3660 H HB3  A LYS   A 1 163 ? 4.495  -6.476  -1.197  0.72 26.37 ?  163 LYS   A HB3  1 
ATOM   3661 H HB3  B LYS   A 1 163 ? 4.489  -6.860  -0.800  0.28 25.24 ?  163 LYS   A HB3  1 
ATOM   3662 H HG2  A LYS   A 1 163 ? 4.450  -8.375  -2.606  0.72 29.77 ?  163 LYS   A HG2  1 
ATOM   3663 H HG2  B LYS   A 1 163 ? 3.782  -8.429  -2.332  0.28 27.07 ?  163 LYS   A HG2  1 
ATOM   3664 H HG3  A LYS   A 1 163 ? 2.915  -8.074  -2.898  0.72 29.77 ?  163 LYS   A HG3  1 
ATOM   3665 H HG3  B LYS   A 1 163 ? 2.266  -7.996  -2.094  0.28 27.07 ?  163 LYS   A HG3  1 
ATOM   3666 H HD2  A LYS   A 1 163 ? 3.562  -6.001  -3.832  0.72 33.29 ?  163 LYS   A HD2  1 
ATOM   3667 H HD2  B LYS   A 1 163 ? 2.468  -6.190  -3.306  0.28 28.57 ?  163 LYS   A HD2  1 
ATOM   3668 H HD3  A LYS   A 1 163 ? 5.082  -6.434  -3.645  0.72 33.29 ?  163 LYS   A HD3  1 
ATOM   3669 H HD3  B LYS   A 1 163 ? 3.986  -5.968  -2.882  0.28 28.57 ?  163 LYS   A HD3  1 
ATOM   3670 H HE2  A LYS   A 1 163 ? 4.609  -8.302  -5.072  0.72 35.98 ?  163 LYS   A HE2  1 
ATOM   3671 H HE2  B LYS   A 1 163 ? 4.575  -7.744  -4.343  0.28 29.79 ?  163 LYS   A HE2  1 
ATOM   3672 H HE3  A LYS   A 1 163 ? 3.216  -7.615  -5.390  0.72 35.98 ?  163 LYS   A HE3  1 
ATOM   3673 H HE3  B LYS   A 1 163 ? 3.070  -7.754  -4.858  0.28 29.79 ?  163 LYS   A HE3  1 
ATOM   3674 H HZ1  A LYS   A 1 163 ? 4.736  -7.091  -6.994  0.72 37.46 ?  163 LYS   A HZ1  1 
ATOM   3675 H HZ1  B LYS   A 1 163 ? 4.378  -6.520  -6.247  0.28 30.33 ?  163 LYS   A HZ1  1 
ATOM   3676 H HZ2  A LYS   A 1 163 ? 4.345  -5.875  -6.311  0.72 37.46 ?  163 LYS   A HZ2  1 
ATOM   3677 H HZ2  B LYS   A 1 163 ? 3.400  -5.642  -5.639  0.28 30.33 ?  163 LYS   A HZ2  1 
ATOM   3678 H HZ3  A LYS   A 1 163 ? 5.625  -6.489  -6.022  0.72 37.46 ?  163 LYS   A HZ3  1 
ATOM   3679 H HZ3  B LYS   A 1 163 ? 4.771  -5.634  -5.171  0.28 30.33 ?  163 LYS   A HZ3  1 
ATOM   3680 N N    A LEU   A 1 164 ? 5.578  -8.628  0.611   0.72 17.26 ?  164 LEU   A N    1 
ATOM   3681 N N    B LEU   A 1 164 ? 5.648  -8.776  1.062   0.28 18.30 ?  164 LEU   A N    1 
ATOM   3682 C CA   A LEU   A 1 164 ? 6.646  -9.614  0.758   0.72 16.62 ?  164 LEU   A CA   1 
ATOM   3683 C CA   B LEU   A 1 164 ? 6.766  -9.711  1.156   0.28 17.57 ?  164 LEU   A CA   1 
ATOM   3684 C C    A LEU   A 1 164 ? 6.205  -10.783 1.627   0.72 16.79 ?  164 LEU   A C    1 
ATOM   3685 C C    B LEU   A 1 164 ? 6.385  -10.942 1.968   0.28 17.89 ?  164 LEU   A C    1 
ATOM   3686 O O    A LEU   A 1 164 ? 6.496  -11.942 1.309   0.72 17.21 ?  164 LEU   A O    1 
ATOM   3687 O O    B LEU   A 1 164 ? 6.729  -12.071 1.597   0.28 17.90 ?  164 LEU   A O    1 
ATOM   3688 C CB   A LEU   A 1 164 ? 7.882  -8.952  1.353   0.72 15.87 ?  164 LEU   A CB   1 
ATOM   3689 C CB   B LEU   A 1 164 ? 7.976  -9.016  1.784   0.28 16.72 ?  164 LEU   A CB   1 
ATOM   3690 C CG   A LEU   A 1 164 ? 8.644  -8.028  0.406   0.72 15.69 ?  164 LEU   A CG   1 
ATOM   3691 C CG   B LEU   A 1 164 ? 8.711  -7.965  0.946   0.28 16.34 ?  164 LEU   A CG   1 
ATOM   3692 C CD1  A LEU   A 1 164 ? 9.586  -7.149  1.204   0.72 14.82 ?  164 LEU   A CD1  1 
ATOM   3693 C CD1  B LEU   A 1 164 ? 9.596  -7.100  1.837   0.28 16.07 ?  164 LEU   A CD1  1 
ATOM   3694 C CD2  A LEU   A 1 164 ? 9.416  -8.821  -0.642  0.72 16.23 ?  164 LEU   A CD2  1 
ATOM   3695 C CD2  B LEU   A 1 164 ? 9.540  -8.617  -0.153  0.28 16.31 ?  164 LEU   A CD2  1 
ATOM   3696 H H    A LEU   A 1 164 ? 5.737  -7.858  0.977   0.72 20.73 ?  164 LEU   A H    1 
ATOM   3697 H H    B LEU   A 1 164 ? 5.789  -8.012  1.431   0.28 21.98 ?  164 LEU   A H    1 
ATOM   3698 H HA   A LEU   A 1 164 ? 6.875  -9.954  -0.117  0.72 19.96 ?  164 LEU   A HA   1 
ATOM   3699 H HA   B LEU   A 1 164 ? 7.014  -10.003 0.268   0.28 21.11 ?  164 LEU   A HA   1 
ATOM   3700 H HB2  A LEU   A 1 164 ? 7.614  -8.422  2.119   0.72 19.07 ?  164 LEU   A HB2  1 
ATOM   3701 H HB2  B LEU   A 1 164 ? 7.682  -8.572  2.593   0.28 20.08 ?  164 LEU   A HB2  1 
ATOM   3702 H HB3  A LEU   A 1 164 ? 8.495  -9.646  1.633   0.72 19.07 ?  164 LEU   A HB3  1 
ATOM   3703 H HB3  B LEU   A 1 164 ? 8.628  -9.696  2.013   0.28 20.08 ?  164 LEU   A HB3  1 
ATOM   3704 H HG   A LEU   A 1 164 ? 8.014  -7.452  -0.054  0.72 18.84 ?  164 LEU   A HG   1 
ATOM   3705 H HG   B LEU   A 1 164 ? 8.063  -7.385  0.522   0.28 19.63 ?  164 LEU   A HG   1 
ATOM   3706 H HD11 A LEU   A 1 164 ? 10.077 -6.578  0.594   0.72 17.80 ?  164 LEU   A HD11 1 
ATOM   3707 H HD11 B LEU   A 1 164 ? 10.052 -6.442  1.289   0.28 19.31 ?  164 LEU   A HD11 1 
ATOM   3708 H HD12 A LEU   A 1 164 ? 9.066  -6.607  1.818   0.72 17.80 ?  164 LEU   A HD12 1 
ATOM   3709 H HD12 B LEU   A 1 164 ? 9.039  -6.652  2.494   0.28 19.31 ?  164 LEU   A HD12 1 
ATOM   3710 H HD13 A LEU   A 1 164 ? 10.200 -7.713  1.699   0.72 17.80 ?  164 LEU   A HD13 1 
ATOM   3711 H HD13 B LEU   A 1 164 ? 10.245 -7.665  2.284   0.28 19.31 ?  164 LEU   A HD13 1 
ATOM   3712 H HD21 A LEU   A 1 164 ? 9.925  -8.204  -1.192  0.72 19.49 ?  164 LEU   A HD21 1 
ATOM   3713 H HD21 B LEU   A 1 164 ? 9.999  -7.924  -0.657  0.28 19.59 ?  164 LEU   A HD21 1 
ATOM   3714 H HD22 A LEU   A 1 164 ? 10.014 -9.438  -0.195  0.72 19.49 ?  164 LEU   A HD22 1 
ATOM   3715 H HD22 B LEU   A 1 164 ? 10.188 -9.215  0.250   0.28 19.59 ?  164 LEU   A HD22 1 
ATOM   3716 H HD23 A LEU   A 1 164 ? 8.785  -9.310  -1.194  0.72 19.49 ?  164 LEU   A HD23 1 
ATOM   3717 H HD23 B LEU   A 1 164 ? 8.949  -9.114  -0.739  0.28 19.59 ?  164 LEU   A HD23 1 
ATOM   3718 N N    A VAL   A 1 165 ? 5.521  -10.497 2.737   0.72 15.92 ?  165 VAL   A N    1 
ATOM   3719 N N    B VAL   A 1 165 ? 5.684  -10.744 3.085   0.28 17.88 ?  165 VAL   A N    1 
ATOM   3720 C CA   A VAL   A 1 165 ? 5.040  -11.568 3.606   0.72 16.00 ?  165 VAL   A CA   1 
ATOM   3721 C CA   B VAL   A 1 165 ? 5.260  -11.876 3.901   0.28 18.08 ?  165 VAL   A CA   1 
ATOM   3722 C C    A VAL   A 1 165 ? 4.032  -12.435 2.864   0.72 16.30 ?  165 VAL   A C    1 
ATOM   3723 C C    B VAL   A 1 165 ? 4.098  -12.608 3.246   0.28 18.03 ?  165 VAL   A C    1 
ATOM   3724 O O    A VAL   A 1 165 ? 4.146  -13.666 2.832   0.72 16.50 ?  165 VAL   A O    1 
ATOM   3725 O O    B VAL   A 1 165 ? 4.065  -13.844 3.216   0.28 17.67 ?  165 VAL   A O    1 
ATOM   3726 C CB   A VAL   A 1 165 ? 4.458  -10.984 4.908   0.72 16.05 ?  165 VAL   A CB   1 
ATOM   3727 C CB   B VAL   A 1 165 ? 4.919  -11.413 5.329   0.28 18.51 ?  165 VAL   A CB   1 
ATOM   3728 C CG1  A VAL   A 1 165 ? 3.719  -12.056 5.707   0.72 16.32 ?  165 VAL   A CG1  1 
ATOM   3729 C CG1  B VAL   A 1 165 ? 4.209  -12.520 6.094   0.28 18.49 ?  165 VAL   A CG1  1 
ATOM   3730 C CG2  A VAL   A 1 165 ? 5.562  -10.345 5.750   0.72 16.27 ?  165 VAL   A CG2  1 
ATOM   3731 C CG2  B VAL   A 1 165 ? 6.183  -10.994 6.058   0.28 18.83 ?  165 VAL   A CG2  1 
ATOM   3732 H H    A VAL   A 1 165 ? 5.317  -9.701  3.004   0.72 19.13 ?  165 VAL   A H    1 
ATOM   3733 H H    B VAL   A 1 165 ? 5.454  -9.974  3.392   0.28 21.48 ?  165 VAL   A H    1 
ATOM   3734 H HA   A VAL   A 1 165 ? 5.786  -12.129 3.849   0.72 19.22 ?  165 VAL   A HA   1 
ATOM   3735 H HA   B VAL   A 1 165 ? 5.997  -12.501 3.968   0.28 21.71 ?  165 VAL   A HA   1 
ATOM   3736 H HB   A VAL   A 1 165 ? 3.819  -10.287 4.689   0.72 19.28 ?  165 VAL   A HB   1 
ATOM   3737 H HB   B VAL   A 1 165 ? 4.326  -10.648 5.286   0.28 22.23 ?  165 VAL   A HB   1 
ATOM   3738 H HG11 A VAL   A 1 165 ? 3.597  -11.742 6.620   0.72 19.61 ?  165 VAL   A HG11 1 
ATOM   3739 H HG11 B VAL   A 1 165 ? 4.233  -12.311 7.040   0.28 22.21 ?  165 VAL   A HG11 1 
ATOM   3740 H HG12 A VAL   A 1 165 ? 2.853  -12.215 5.299   0.72 19.61 ?  165 VAL   A HG12 1 
ATOM   3741 H HG12 B VAL   A 1 165 ? 3.290  -12.577 5.793   0.28 22.21 ?  165 VAL   A HG12 1 
ATOM   3742 H HG13 A VAL   A 1 165 ? 4.244  -12.869 5.707   0.72 19.61 ?  165 VAL   A HG13 1 
ATOM   3743 H HG13 B VAL   A 1 165 ? 4.667  -13.360 5.931   0.28 22.21 ?  165 VAL   A HG13 1 
ATOM   3744 H HG21 A VAL   A 1 165 ? 5.180  -10.012 6.579   0.72 19.54 ?  165 VAL   A HG21 1 
ATOM   3745 H HG21 B VAL   A 1 165 ? 5.951  -10.710 6.955   0.28 22.61 ?  165 VAL   A HG21 1 
ATOM   3746 H HG22 A VAL   A 1 165 ? 6.240  -11.010 5.943   0.72 19.54 ?  165 VAL   A HG22 1 
ATOM   3747 H HG22 B VAL   A 1 165 ? 6.790  -11.751 6.096   0.28 22.61 ?  165 VAL   A HG22 1 
ATOM   3748 H HG23 A VAL   A 1 165 ? 5.954  -9.609  5.251   0.72 19.54 ?  165 VAL   A HG23 1 
ATOM   3749 H HG23 B VAL   A 1 165 ? 6.597  -10.263 5.574   0.28 22.61 ?  165 VAL   A HG23 1 
ATOM   3750 N N    A SER   A 1 166 ? 3.035  -11.798 2.243   0.72 16.66 ?  166 SER   A N    1 
ATOM   3751 N N    B SER   A 1 166 ? 3.127  -11.864 2.708   0.28 18.20 ?  166 SER   A N    1 
ATOM   3752 C CA   A SER   A 1 166 ? 1.930  -12.546 1.652   0.72 17.66 ?  166 SER   A CA   1 
ATOM   3753 C CA   B SER   A 1 166 ? 1.929  -12.503 2.175   0.28 18.31 ?  166 SER   A CA   1 
ATOM   3754 C C    A SER   A 1 166 ? 2.377  -13.378 0.460   0.72 18.42 ?  166 SER   A C    1 
ATOM   3755 C C    B SER   A 1 166 ? 2.259  -13.459 1.038   0.28 18.79 ?  166 SER   A C    1 
ATOM   3756 O O    A SER   A 1 166 ? 1.740  -14.391 0.145   0.72 20.07 ?  166 SER   A O    1 
ATOM   3757 O O    B SER   A 1 166 ? 1.542  -14.443 0.833   0.28 19.15 ?  166 SER   A O    1 
ATOM   3758 C CB   A SER   A 1 166 ? 0.806  -11.595 1.226   0.72 18.46 ?  166 SER   A CB   1 
ATOM   3759 C CB   B SER   A 1 166 ? 0.899  -11.456 1.730   0.28 18.01 ?  166 SER   A CB   1 
ATOM   3760 O OG   A SER   A 1 166 ? 0.177  -10.983 2.345   0.72 19.83 ?  166 SER   A OG   1 
ATOM   3761 O OG   B SER   A 1 166 ? 1.211  -10.911 0.458   0.28 17.96 ?  166 SER   A OG   1 
ATOM   3762 H H    A SER   A 1 166 ? 2.965  -10.946 2.162   0.72 20.01 ?  166 SER   A H    1 
ATOM   3763 H H    B SER   A 1 166 ? 3.141  -11.008 2.640   0.28 21.86 ?  166 SER   A H    1 
ATOM   3764 H HA   A SER   A 1 166 ? 1.562  -13.155 2.314   0.72 21.21 ?  166 SER   A HA   1 
ATOM   3765 H HA   B SER   A 1 166 ? 1.518  -13.025 2.877   0.28 21.99 ?  166 SER   A HA   1 
ATOM   3766 H HB2  A SER   A 1 166 ? 1.176  -10.910 0.647   0.72 22.17 ?  166 SER   A HB2  1 
ATOM   3767 H HB2  B SER   A 1 166 ? 0.025  -11.876 1.676   0.28 21.64 ?  166 SER   A HB2  1 
ATOM   3768 H HB3  A SER   A 1 166 ? 0.129  -12.100 0.743   0.72 22.17 ?  166 SER   A HB3  1 
ATOM   3769 H HB3  B SER   A 1 166 ? 0.867  -10.738 2.384   0.28 21.64 ?  166 SER   A HB3  1 
ATOM   3770 H HG   A SER   A 1 166 ? -0.417 -10.452 2.086   0.72 23.81 ?  166 SER   A HG   1 
ATOM   3771 H HG   B SER   A 1 166 ? 0.640  -10.329 0.248   0.28 21.57 ?  166 SER   A HG   1 
ATOM   3772 N N    A SER   A 1 167 ? 3.444  -12.965 -0.223  0.72 17.69 ?  167 SER   A N    1 
ATOM   3773 N N    B SER   A 1 167 ? 3.349  -13.217 0.310   0.28 19.52 ?  167 SER   A N    1 
ATOM   3774 C CA   A SER   A 1 167 ? 3.934  -13.680 -1.392  0.72 18.78 ?  167 SER   A CA   1 
ATOM   3775 C CA   B SER   A 1 167 ? 3.676  -14.017 -0.864  0.28 20.29 ?  167 SER   A CA   1 
ATOM   3776 C C    A SER   A 1 167 ? 5.067  -14.643 -1.064  0.72 19.09 ?  167 SER   A C    1 
ATOM   3777 C C    B SER   A 1 167 ? 4.967  -14.813 -0.684  0.28 20.66 ?  167 SER   A C    1 
ATOM   3778 O O    A SER   A 1 167 ? 5.545  -15.345 -1.961  0.72 19.82 ?  167 SER   A O    1 
ATOM   3779 O O    B SER   A 1 167 ? 5.636  -15.141 -1.666  0.28 20.83 ?  167 SER   A O    1 
ATOM   3780 C CB   A SER   A 1 167 ? 4.382  -12.688 -2.475  0.72 18.92 ?  167 SER   A CB   1 
ATOM   3781 C CB   B SER   A 1 167 ? 3.747  -13.152 -2.123  0.28 21.17 ?  167 SER   A CB   1 
ATOM   3782 O OG   A SER   A 1 167 ? 5.425  -11.853 -1.990  0.72 19.03 ?  167 SER   A OG   1 
ATOM   3783 O OG   B SER   A 1 167 ? 4.700  -12.115 -1.975  0.28 21.92 ?  167 SER   A OG   1 
ATOM   3784 H H    A SER   A 1 167 ? 3.892  -12.252 -0.033  0.72 21.25 ?  167 SER   A H    1 
ATOM   3785 H H    B SER   A 1 167 ? 3.921  -12.598 0.489   0.28 23.44 ?  167 SER   A H    1 
ATOM   3786 H HA   A SER   A 1 167 ? 3.208  -14.196 -1.765  0.72 22.56 ?  167 SER   A HA   1 
ATOM   3787 H HA   B SER   A 1 167 ? 2.954  -14.651 -1.002  0.28 24.37 ?  167 SER   A HA   1 
ATOM   3788 H HB2  A SER   A 1 167 ? 4.714  -13.180 -3.243  0.72 22.72 ?  167 SER   A HB2  1 
ATOM   3789 H HB2  B SER   A 1 167 ? 4.005  -13.714 -2.872  0.28 25.42 ?  167 SER   A HB2  1 
ATOM   3790 H HB3  A SER   A 1 167 ? 3.619  -12.142 -2.747  0.72 22.72 ?  167 SER   A HB3  1 
ATOM   3791 H HB3  B SER   A 1 167 ? 2.873  -12.765 -2.288  0.28 25.42 ?  167 SER   A HB3  1 
ATOM   3792 H HG   A SER   A 1 167 ? 5.130  -11.381 -1.350  0.72 22.86 ?  167 SER   A HG   1 
ATOM   3793 H HG   B SER   A 1 167 ? 4.480  -11.613 -1.338  0.28 26.32 ?  167 SER   A HG   1 
ATOM   3794 N N    A PHE   A 1 168 ? 5.504  -14.701 0.192   0.72 18.50 ?  168 PHE   A N    1 
ATOM   3795 N N    B PHE   A 1 168 ? 5.334  -15.138 0.555   0.28 20.83 ?  168 PHE   A N    1 
ATOM   3796 C CA   A PHE   A 1 168 ? 6.669  -15.513 0.525   0.72 18.80 ?  168 PHE   A CA   1 
ATOM   3797 C CA   B PHE   A 1 168 ? 6.524  -15.943 0.812   0.28 21.34 ?  168 PHE   A CA   1 
ATOM   3798 C C    A PHE   A 1 168 ? 6.353  -16.997 0.407   0.72 20.18 ?  168 PHE   A C    1 
ATOM   3799 C C    B PHE   A 1 168 ? 6.135  -17.414 0.790   0.28 23.60 ?  168 PHE   A C    1 
ATOM   3800 O O    A PHE   A 1 168 ? 5.337  -17.475 0.926   0.72 21.98 ?  168 PHE   A O    1 
ATOM   3801 O O    B PHE   A 1 168 ? 5.420  -17.889 1.677   0.28 23.28 ?  168 PHE   A O    1 
ATOM   3802 C CB   A PHE   A 1 168 ? 7.160  -15.228 1.940   0.72 18.23 ?  168 PHE   A CB   1 
ATOM   3803 C CB   B PHE   A 1 168 ? 7.164  -15.587 2.149   0.28 19.89 ?  168 PHE   A CB   1 
ATOM   3804 C CG   A PHE   A 1 168 ? 8.429  -15.966 2.278   0.72 17.48 ?  168 PHE   A CG   1 
ATOM   3805 C CG   B PHE   A 1 168 ? 8.379  -16.412 2.466   0.28 18.64 ?  168 PHE   A CG   1 
ATOM   3806 C CD1  A PHE   A 1 168 ? 9.625  -15.577 1.710   0.72 17.27 ?  168 PHE   A CD1  1 
ATOM   3807 C CD1  B PHE   A 1 168 ? 9.593  -16.132 1.863   0.28 18.32 ?  168 PHE   A CD1  1 
ATOM   3808 C CD2  A PHE   A 1 168 ? 8.428  -17.061 3.126   0.72 17.27 ?  168 PHE   A CD2  1 
ATOM   3809 C CD2  B PHE   A 1 168 ? 8.306  -17.476 3.351   0.28 18.14 ?  168 PHE   A CD2  1 
ATOM   3810 C CE1  A PHE   A 1 168 ? 10.798 -16.253 1.995   0.72 16.47 ?  168 PHE   A CE1  1 
ATOM   3811 C CE1  B PHE   A 1 168 ? 10.714 -16.890 2.143   0.28 18.03 ?  168 PHE   A CE1  1 
ATOM   3812 C CE2  A PHE   A 1 168 ? 9.605  -17.739 3.415   0.72 17.12 ?  168 PHE   A CE2  1 
ATOM   3813 C CE2  B PHE   A 1 168 ? 9.426  -18.237 3.636   0.28 18.07 ?  168 PHE   A CE2  1 
ATOM   3814 C CZ   A PHE   A 1 168 ? 10.788 -17.332 2.849   0.72 16.62 ?  168 PHE   A CZ   1 
ATOM   3815 C CZ   B PHE   A 1 168 ? 10.630 -17.943 3.031   0.28 18.13 ?  168 PHE   A CZ   1 
ATOM   3816 H H    A PHE   A 1 168 ? 5.165  -14.265 0.852   0.72 22.22 ?  168 PHE   A H    1 
ATOM   3817 H H    B PHE   A 1 168 ? 4.913  -14.903 1.271   0.28 25.01 ?  168 PHE   A H    1 
ATOM   3818 H HA   A PHE   A 1 168 ? 7.390  -15.299 -0.095  0.72 22.58 ?  168 PHE   A HA   1 
ATOM   3819 H HA   B PHE   A 1 168 ? 7.173  -15.792 0.109   0.28 25.63 ?  168 PHE   A HA   1 
ATOM   3820 H HB2  A PHE   A 1 168 ? 7.333  -14.277 2.030   0.72 21.89 ?  168 PHE   A HB2  1 
ATOM   3821 H HB2  B PHE   A 1 168 ? 7.433  -14.657 2.127   0.28 23.88 ?  168 PHE   A HB2  1 
ATOM   3822 H HB3  A PHE   A 1 168 ? 6.478  -15.503 2.569   0.72 21.89 ?  168 PHE   A HB3  1 
ATOM   3823 H HB3  B PHE   A 1 168 ? 6.515  -15.729 2.856   0.28 23.88 ?  168 PHE   A HB3  1 
ATOM   3824 H HD1  A PHE   A 1 168 ? 9.650  -14.847 1.133   0.72 20.75 ?  168 PHE   A HD1  1 
ATOM   3825 H HD1  B PHE   A 1 168 ? 9.656  -15.424 1.265   0.28 22.00 ?  168 PHE   A HD1  1 
ATOM   3826 H HD2  A PHE   A 1 168 ? 7.631  -17.340 3.510   0.72 20.75 ?  168 PHE   A HD2  1 
ATOM   3827 H HD2  B PHE   A 1 168 ? 7.497  -17.680 3.761   0.28 21.79 ?  168 PHE   A HD2  1 
ATOM   3828 H HE1  A PHE   A 1 168 ? 11.605 -15.975 1.613   0.72 19.79 ?  168 PHE   A HE1  1 
ATOM   3829 H HE1  B PHE   A 1 168 ? 11.525 -16.690 1.733   0.28 21.66 ?  168 PHE   A HE1  1 
ATOM   3830 H HE2  A PHE   A 1 168 ? 9.588  -18.469 3.991   0.72 20.56 ?  168 PHE   A HE2  1 
ATOM   3831 H HE2  B PHE   A 1 168 ? 9.366  -18.949 4.233   0.28 21.70 ?  168 PHE   A HE2  1 
ATOM   3832 H HZ   A PHE   A 1 168 ? 11.579 -17.787 3.043   0.72 19.96 ?  168 PHE   A HZ   1 
ATOM   3833 H HZ   B PHE   A 1 168 ? 11.384 -18.456 3.220   0.28 21.78 ?  168 PHE   A HZ   1 
ATOM   3834 N N    A LEU   A 1 169 ? 7.255  -17.733 -0.236  0.72 21.77 ?  169 LEU   A N    1 
ATOM   3835 N N    B LEU   A 1 169 ? 6.619  -18.136 -0.212  0.28 26.22 ?  169 LEU   A N    1 
ATOM   3836 C CA   A LEU   A 1 169 ? 7.072  -19.163 -0.405  0.72 25.61 ?  169 LEU   A CA   1 
ATOM   3837 C CA   B LEU   A 1 169 ? 6.286  -19.541 -0.358  0.28 28.44 ?  169 LEU   A CA   1 
ATOM   3838 C C    A LEU   A 1 169 ? 7.919  -19.915 0.607   0.72 26.49 ?  169 LEU   A C    1 
ATOM   3839 C C    B LEU   A 1 169 ? 7.080  -20.408 0.616   0.28 29.74 ?  169 LEU   A C    1 
ATOM   3840 O O    A LEU   A 1 169 ? 7.396  -20.362 1.632   0.72 27.05 ?  169 LEU   A O    1 
ATOM   3841 O O    B LEU   A 1 169 ? 6.515  -20.991 1.543   0.28 30.11 ?  169 LEU   A O    1 
ATOM   3842 C CB   A LEU   A 1 169 ? 7.398  -19.590 -1.842  0.72 27.59 ?  169 LEU   A CB   1 
ATOM   3843 C CB   B LEU   A 1 169 ? 6.550  -19.992 -1.798  0.28 29.13 ?  169 LEU   A CB   1 
ATOM   3844 C CG   A LEU   A 1 169 ? 7.124  -21.059 -2.184  0.72 29.33 ?  169 LEU   A CG   1 
ATOM   3845 C CG   B LEU   A 1 169 ? 5.939  -21.323 -2.233  0.28 29.66 ?  169 LEU   A CG   1 
ATOM   3846 C CD1  A LEU   A 1 169 ? 5.715  -21.457 -1.772  0.72 30.04 ?  169 LEU   A CD1  1 
ATOM   3847 C CD1  B LEU   A 1 169 ? 4.549  -21.493 -1.647  0.28 29.78 ?  169 LEU   A CD1  1 
ATOM   3848 C CD2  A LEU   A 1 169 ? 7.333  -21.318 -3.669  0.72 29.74 ?  169 LEU   A CD2  1 
ATOM   3849 C CD2  B LEU   A 1 169 ? 5.888  -21.394 -3.751  0.28 29.82 ?  169 LEU   A CD2  1 
ATOM   3850 O OXT  A LEU   A 1 169 ? 9.127  -20.078 0.434   0.72 25.95 -1 169 LEU   A OXT  1 
ATOM   3851 O OXT  B LEU   A 1 169 ? 8.299  -20.544 0.504   0.28 30.39 -1 169 LEU   A OXT  1 
ATOM   3852 H H    A LEU   A 1 169 ? 7.985  -17.424 -0.577  0.72 26.15 ?  169 LEU   A H    1 
ATOM   3853 H H    B LEU   A 1 169 ? 7.133  -17.834 -0.829  0.28 31.49 ?  169 LEU   A H    1 
ATOM   3854 H HA   A LEU   A 1 169 ? 6.156  -19.390 -0.219  0.72 30.76 ?  169 LEU   A HA   1 
ATOM   3855 H HA   B LEU   A 1 169 ? 5.344  -19.637 -0.152  0.28 34.15 ?  169 LEU   A HA   1 
ATOM   3856 H HB2  A LEU   A 1 169 ? 6.862  -19.052 -2.449  0.72 33.13 ?  169 LEU   A HB2  1 
ATOM   3857 H HB2  B LEU   A 1 169 ? 6.210  -19.313 -2.400  0.28 34.97 ?  169 LEU   A HB2  1 
ATOM   3858 H HB3  A LEU   A 1 169 ? 8.337  -19.426 -2.012  0.72 33.13 ?  169 LEU   A HB3  1 
ATOM   3859 H HB3  B LEU   A 1 169 ? 7.512  -20.070 -1.918  0.28 34.97 ?  169 LEU   A HB3  1 
ATOM   3860 H HG   A LEU   A 1 169 ? 7.747  -21.619 -1.696  0.72 35.21 ?  169 LEU   A HG   1 
ATOM   3861 H HG   B LEU   A 1 169 ? 6.494  -22.054 -1.915  0.28 35.61 ?  169 LEU   A HG   1 
ATOM   3862 H HD11 A LEU   A 1 169 ? 5.496  -22.310 -2.178  0.72 36.07 ?  169 LEU   A HD11 1 
ATOM   3863 H HD11 B LEU   A 1 169 ? 3.990  -21.945 -2.292  0.28 35.76 ?  169 LEU   A HD11 1 
ATOM   3864 H HD12 A LEU   A 1 169 ? 5.677  -21.531 -0.806  0.72 36.07 ?  169 LEU   A HD12 1 
ATOM   3865 H HD12 B LEU   A 1 169 ? 4.614  -22.012 -0.835  0.28 35.76 ?  169 LEU   A HD12 1 
ATOM   3866 H HD13 A LEU   A 1 169 ? 5.094  -20.777 -2.078  0.72 36.07 ?  169 LEU   A HD13 1 
ATOM   3867 H HD13 B LEU   A 1 169 ? 4.172  -20.624 -1.445  0.28 35.76 ?  169 LEU   A HD13 1 
ATOM   3868 H HD21 A LEU   A 1 169 ? 7.161  -22.255 -3.855  0.72 35.71 ?  169 LEU   A HD21 1 
ATOM   3869 H HD21 B LEU   A 1 169 ? 5.535  -22.257 -4.017  0.28 35.81 ?  169 LEU   A HD21 1 
ATOM   3870 H HD22 A LEU   A 1 169 ? 6.718  -20.763 -4.175  0.72 35.71 ?  169 LEU   A HD22 1 
ATOM   3871 H HD22 B LEU   A 1 169 ? 5.312  -20.685 -4.080  0.28 35.81 ?  169 LEU   A HD22 1 
ATOM   3872 H HD23 A LEU   A 1 169 ? 8.247  -21.096 -3.903  0.72 35.71 ?  169 LEU   A HD23 1 
ATOM   3873 H HD23 B LEU   A 1 169 ? 6.785  -21.280 -4.103  0.28 35.81 ?  169 LEU   A HD23 1 
ATOM   3874 N N    A SER   B 1 1   ? 50.778 -9.237  -23.730 0.72 27.93 ?  1   SER   B N    1 
ATOM   3875 N N    B SER   B 1 1   ? 50.707 -9.238  -23.725 0.28 26.15 ?  1   SER   B N    1 
ATOM   3876 C CA   A SER   B 1 1   ? 51.278 -10.297 -22.833 0.72 27.87 ?  1   SER   B CA   1 
ATOM   3877 C CA   B SER   B 1 1   ? 51.217 -10.257 -22.784 0.28 26.04 ?  1   SER   B CA   1 
ATOM   3878 C C    A SER   B 1 1   ? 50.204 -11.346 -22.580 0.72 26.66 ?  1   SER   B C    1 
ATOM   3879 C C    B SER   B 1 1   ? 50.160 -11.325 -22.539 0.28 25.39 ?  1   SER   B C    1 
ATOM   3880 O O    A SER   B 1 1   ? 49.011 -11.142 -22.851 0.72 26.38 ?  1   SER   B O    1 
ATOM   3881 O O    B SER   B 1 1   ? 48.990 -11.162 -22.899 0.28 25.10 ?  1   SER   B O    1 
ATOM   3882 C CB   A SER   B 1 1   ? 51.751 -9.707  -21.508 0.72 28.71 ?  1   SER   B CB   1 
ATOM   3883 C CB   B SER   B 1 1   ? 51.620 -9.614  -21.461 0.28 26.39 ?  1   SER   B CB   1 
ATOM   3884 O OG   A SER   B 1 1   ? 50.653 -9.389  -20.675 0.72 30.43 ?  1   SER   B OG   1 
ATOM   3885 O OG   B SER   B 1 1   ? 50.490 -9.438  -20.627 0.28 27.13 ?  1   SER   B OG   1 
ATOM   3886 H H1   A SER   B 1 1   ? 50.670 -9.576  -24.543 0.72 33.53 ?  1   SER   B H1   1 
ATOM   3887 H H1   B SER   B 1 1   ? 50.591 -9.613  -24.522 0.28 31.40 ?  1   SER   B H1   1 
ATOM   3888 H H2   A SER   B 1 1   ? 50.005 -8.937  -23.419 0.72 33.53 ?  1   SER   B H2   1 
ATOM   3889 H H2   B SER   B 1 1   ? 49.936 -8.924  -23.423 0.28 31.40 ?  1   SER   B H2   1 
ATOM   3890 H H3   A SER   B 1 1   ? 51.373 -8.579  -23.754 0.72 33.53 ?  1   SER   B H3   1 
ATOM   3891 H H3   B SER   B 1 1   ? 51.301 -8.580  -23.785 0.28 31.40 ?  1   SER   B H3   1 
ATOM   3892 H HA   A SER   B 1 1   ? 52.032 -10.725 -23.261 0.72 33.47 ?  1   SER   B HA   1 
ATOM   3893 H HA   B SER   B 1 1   ? 51.995 -10.673 -23.176 0.28 31.27 ?  1   SER   B HA   1 
ATOM   3894 H HB2  A SER   B 1 1   ? 52.310 -10.361 -21.061 0.72 34.48 ?  1   SER   B HB2  1 
ATOM   3895 H HB2  B SER   B 1 1   ? 52.263 -10.191 -21.021 0.28 31.69 ?  1   SER   B HB2  1 
ATOM   3896 H HB3  A SER   B 1 1   ? 52.260 -8.900  -21.683 0.72 34.48 ?  1   SER   B HB3  1 
ATOM   3897 H HB3  B SER   B 1 1   ? 52.017 -8.746  -21.637 0.28 31.69 ?  1   SER   B HB3  1 
ATOM   3898 H HG   A SER   B 1 1   ? 50.913 -8.900  -20.042 0.72 36.53 ?  1   SER   B HG   1 
ATOM   3899 H HG   B SER   B 1 1   ? 50.662 -8.869  -20.035 0.28 32.58 ?  1   SER   B HG   1 
ATOM   3900 N N    A MET   B 1 2   ? 50.651 -12.473 -22.047 0.72 25.98 ?  2   MET   B N    1 
ATOM   3901 N N    B MET   B 1 2   ? 50.583 -12.415 -21.912 0.28 25.04 ?  2   MET   B N    1 
ATOM   3902 C CA   A MET   B 1 2   ? 49.829 -13.662 -21.879 0.72 25.97 ?  2   MET   B CA   1 
ATOM   3903 C CA   B MET   B 1 2   ? 49.762 -13.606 -21.738 0.28 24.75 ?  2   MET   B CA   1 
ATOM   3904 C C    A MET   B 1 2   ? 49.583 -13.857 -20.391 0.72 23.66 ?  2   MET   B C    1 
ATOM   3905 C C    B MET   B 1 2   ? 49.493 -13.796 -20.252 0.28 23.18 ?  2   MET   B C    1 
ATOM   3906 O O    A MET   B 1 2   ? 50.518 -14.123 -19.631 0.72 23.86 ?  2   MET   B O    1 
ATOM   3907 O O    B MET   B 1 2   ? 50.392 -14.180 -19.496 0.28 23.48 ?  2   MET   B O    1 
ATOM   3908 C CB   A MET   B 1 2   ? 50.559 -14.857 -22.480 0.72 29.76 ?  2   MET   B CB   1 
ATOM   3909 C CB   B MET   B 1 2   ? 50.506 -14.805 -22.308 0.28 26.42 ?  2   MET   B CB   1 
ATOM   3910 C CG   A MET   B 1 2   ? 49.720 -16.113 -22.633 0.72 33.17 ?  2   MET   B CG   1 
ATOM   3911 C CG   B MET   B 1 2   ? 49.620 -15.950 -22.770 0.28 27.80 ?  2   MET   B CG   1 
ATOM   3912 S SD   A MET   B 1 2   ? 50.552 -17.330 -23.670 0.72 36.43 ?  2   MET   B SD   1 
ATOM   3913 S SD   B MET   B 1 2   ? 50.512 -17.046 -23.880 0.28 29.05 ?  2   MET   B SD   1 
ATOM   3914 C CE   A MET   B 1 2   ? 51.063 -16.277 -25.022 0.72 36.76 ?  2   MET   B CE   1 
ATOM   3915 C CE   B MET   B 1 2   ? 51.388 -15.846 -24.865 0.28 29.28 ?  2   MET   B CE   1 
ATOM   3916 H H    A MET   B 1 2   ? 51.458 -12.582 -21.764 0.72 31.19 ?  2   MET   B H    1 
ATOM   3917 H H    B MET   B 1 2   ? 51.373 -12.495 -21.577 0.28 30.07 ?  2   MET   B H    1 
ATOM   3918 H HA   A MET   B 1 2   ? 48.987 -13.555 -22.344 0.72 31.18 ?  2   MET   B HA   1 
ATOM   3919 H HA   B MET   B 1 2   ? 48.930 -13.511 -22.229 0.28 29.72 ?  2   MET   B HA   1 
ATOM   3920 H HB2  A MET   B 1 2   ? 50.874 -14.576 -23.349 0.72 35.73 ?  2   MET   B HB2  1 
ATOM   3921 H HB2  B MET   B 1 2   ? 51.032 -14.464 -23.042 0.28 31.73 ?  2   MET   B HB2  1 
ATOM   3922 H HB3  A MET   B 1 2   ? 51.314 -15.091 -21.923 0.72 35.73 ?  2   MET   B HB3  1 
ATOM   3923 H HB3  B MET   B 1 2   ? 51.096 -15.173 -21.641 0.28 31.73 ?  2   MET   B HB3  1 
ATOM   3924 H HG2  A MET   B 1 2   ? 49.569 -16.505 -21.756 0.72 39.82 ?  2   MET   B HG2  1 
ATOM   3925 H HG2  B MET   B 1 2   ? 49.332 -16.466 -21.996 0.28 33.38 ?  2   MET   B HG2  1 
ATOM   3926 H HG3  A MET   B 1 2   ? 48.875 -15.893 -23.054 0.72 39.82 ?  2   MET   B HG3  1 
ATOM   3927 H HG3  B MET   B 1 2   ? 48.851 -15.608 -23.245 0.28 33.38 ?  2   MET   B HG3  1 
ATOM   3928 H HE1  A MET   B 1 2   ? 51.205 -16.822 -25.798 0.72 44.13 ?  2   MET   B HE1  1 
ATOM   3929 H HE1  B MET   B 1 2   ? 51.598 -16.259 -25.694 0.28 35.16 ?  2   MET   B HE1  1 
ATOM   3930 H HE2  A MET   B 1 2   ? 50.357 -15.628 -25.189 0.72 44.13 ?  2   MET   B HE2  1 
ATOM   3931 H HE2  B MET   B 1 2   ? 50.814 -15.073 -25.014 0.28 35.16 ?  2   MET   B HE2  1 
ATOM   3932 H HE3  A MET   B 1 2   ? 51.884 -15.811 -24.782 0.72 44.13 ?  2   MET   B HE3  1 
ATOM   3933 H HE3  B MET   B 1 2   ? 52.203 -15.574 -24.400 0.28 35.16 ?  2   MET   B HE3  1 
ATOM   3934 N N    A VAL   B 1 3   ? 48.330 -13.695 -19.975 0.72 21.32 ?  3   VAL   B N    1 
ATOM   3935 N N    B VAL   B 1 3   ? 48.264 -13.516 -19.835 0.28 21.36 ?  3   VAL   B N    1 
ATOM   3936 C CA   A VAL   B 1 3   ? 47.917 -13.942 -18.601 0.72 20.16 ?  3   VAL   B CA   1 
ATOM   3937 C CA   B VAL   B 1 3   ? 47.826 -13.782 -18.471 0.28 19.88 ?  3   VAL   B CA   1 
ATOM   3938 C C    A VAL   B 1 3   ? 46.682 -14.833 -18.622 0.72 18.60 ?  3   VAL   B C    1 
ATOM   3939 C C    B VAL   B 1 3   ? 46.577 -14.650 -18.512 0.28 18.29 ?  3   VAL   B C    1 
ATOM   3940 O O    A VAL   B 1 3   ? 45.970 -14.933 -19.624 0.72 18.72 ?  3   VAL   B O    1 
ATOM   3941 O O    B VAL   B 1 3   ? 45.753 -14.553 -19.426 0.28 18.11 ?  3   VAL   B O    1 
ATOM   3942 C CB   A VAL   B 1 3   ? 47.638 -12.633 -17.828 0.72 21.63 ?  3   VAL   B CB   1 
ATOM   3943 C CB   B VAL   B 1 3   ? 47.560 -12.490 -17.668 0.28 20.21 ?  3   VAL   B CB   1 
ATOM   3944 C CG1  A VAL   B 1 3   ? 48.905 -11.780 -17.736 0.72 22.28 ?  3   VAL   B CG1  1 
ATOM   3945 C CG1  B VAL   B 1 3   ? 48.830 -11.658 -17.553 0.28 20.40 ?  3   VAL   B CG1  1 
ATOM   3946 C CG2  A VAL   B 1 3   ? 46.509 -11.858 -18.486 0.72 22.09 ?  3   VAL   B CG2  1 
ATOM   3947 C CG2  B VAL   B 1 3   ? 46.435 -11.690 -18.305 0.28 20.28 ?  3   VAL   B CG2  1 
ATOM   3948 H H    A VAL   B 1 3   ? 47.691 -13.438 -20.486 0.72 25.60 ?  3   VAL   B H    1 
ATOM   3949 H H    B VAL   B 1 3   ? 47.666 -13.158 -20.337 0.28 25.65 ?  3   VAL   B H    1 
ATOM   3950 H HA   A VAL   B 1 3   ? 48.623 -14.421 -18.137 0.72 24.21 ?  3   VAL   B HA   1 
ATOM   3951 H HA   B VAL   B 1 3   ? 48.522 -14.279 -18.016 0.28 23.88 ?  3   VAL   B HA   1 
ATOM   3952 H HB   A VAL   B 1 3   ? 47.365 -12.856 -16.924 0.72 25.98 ?  3   VAL   B HB   1 
ATOM   3953 H HB   B VAL   B 1 3   ? 47.281 -12.739 -16.774 0.28 24.27 ?  3   VAL   B HB   1 
ATOM   3954 H HG11 A VAL   B 1 3   ? 48.705 -10.975 -17.235 0.72 26.76 ?  3   VAL   B HG11 1 
ATOM   3955 H HG11 B VAL   B 1 3   ? 48.637 -10.865 -17.030 0.28 24.49 ?  3   VAL   B HG11 1 
ATOM   3956 H HG12 A VAL   B 1 3   ? 49.595 -12.290 -17.284 0.72 26.76 ?  3   VAL   B HG12 1 
ATOM   3957 H HG12 B VAL   B 1 3   ? 49.514 -12.187 -17.114 0.28 24.49 ?  3   VAL   B HG12 1 
ATOM   3958 H HG13 A VAL   B 1 3   ? 49.195 -11.552 -18.632 0.72 26.76 ?  3   VAL   B HG13 1 
ATOM   3959 H HG13 B VAL   B 1 3   ? 49.124 -11.407 -18.442 0.28 24.49 ?  3   VAL   B HG13 1 
ATOM   3960 H HG21 A VAL   B 1 3   ? 46.450 -10.982 -18.079 0.72 26.53 ?  3   VAL   B HG21 1 
ATOM   3961 H HG21 B VAL   B 1 3   ? 46.383 -10.826 -17.871 0.28 24.36 ?  3   VAL   B HG21 1 
ATOM   3962 H HG22 A VAL   B 1 3   ? 46.693 -11.774 -19.434 0.72 26.53 ?  3   VAL   B HG22 1 
ATOM   3963 H HG22 B VAL   B 1 3   ? 46.623 -11.577 -19.250 0.28 24.36 ?  3   VAL   B HG22 1 
ATOM   3964 H HG23 A VAL   B 1 3   ? 45.676 -12.341 -18.354 0.72 26.53 ?  3   VAL   B HG23 1 
ATOM   3965 H HG23 B VAL   B 1 3   ? 45.599 -12.170 -18.190 0.28 24.36 ?  3   VAL   B HG23 1 
ATOM   3966 N N    . ASN   B 1 4   ? 46.438 -15.497 -17.493 1.00 17.13 ?  4   ASN   B N    1 
ATOM   3967 C CA   . ASN   B 1 4   ? 45.302 -16.412 -17.375 1.00 16.13 ?  4   ASN   B CA   1 
ATOM   3968 C C    . ASN   B 1 4   ? 45.243 -17.377 -18.558 1.00 16.44 ?  4   ASN   B C    1 
ATOM   3969 O O    . ASN   B 1 4   ? 44.181 -17.631 -19.122 1.00 17.05 ?  4   ASN   B O    1 
ATOM   3970 C CB   . ASN   B 1 4   ? 43.981 -15.654 -17.206 1.00 15.58 ?  4   ASN   B CB   1 
ATOM   3971 C CG   . ASN   B 1 4   ? 43.943 -14.834 -15.929 1.00 14.80 ?  4   ASN   B CG   1 
ATOM   3972 O OD1  . ASN   B 1 4   ? 44.227 -15.339 -14.842 1.00 14.69 ?  4   ASN   B OD1  1 
ATOM   3973 N ND2  . ASN   B 1 4   ? 43.602 -13.559 -16.057 1.00 15.76 ?  4   ASN   B ND2  1 
ATOM   3974 H H    A ASN   B 1 4   ? 46.922 -15.443 -16.786 0.72 20.58 ?  4   ASN   B H    1 
ATOM   3975 H H    B ASN   B 1 4   ? 46.998 -15.557 -16.844 0.28 20.58 ?  4   ASN   B H    1 
ATOM   3976 H HA   . ASN   B 1 4   ? 45.433 -16.946 -16.576 1.00 19.38 ?  4   ASN   B HA   1 
ATOM   3977 H HB2  . ASN   B 1 4   ? 43.864 -15.050 -17.956 1.00 18.71 ?  4   ASN   B HB2  1 
ATOM   3978 H HB3  . ASN   B 1 4   ? 43.253 -16.294 -17.178 1.00 18.71 ?  4   ASN   B HB3  1 
ATOM   3979 H HD21 . ASN   B 1 4   ? 43.572 -13.050 -15.363 1.00 18.93 ?  4   ASN   B HD21 1 
ATOM   3980 H HD22 . ASN   B 1 4   ? 43.420 -13.234 -16.833 1.00 18.93 ?  4   ASN   B HD22 1 
ATOM   3981 N N    . SER   B 1 5   ? 46.401 -17.918 -18.943 1.00 17.60 ?  5   SER   B N    1 
ATOM   3982 C CA   . SER   B 1 5   ? 46.494 -18.838 -20.076 1.00 20.08 ?  5   SER   B CA   1 
ATOM   3983 C C    . SER   B 1 5   ? 46.491 -20.258 -19.523 1.00 21.34 ?  5   SER   B C    1 
ATOM   3984 O O    . SER   B 1 5   ? 47.517 -20.927 -19.436 1.00 23.31 ?  5   SER   B O    1 
ATOM   3985 C CB   . SER   B 1 5   ? 47.745 -18.552 -20.905 1.00 21.60 ?  5   SER   B CB   1 
ATOM   3986 O OG   . SER   B 1 5   ? 48.923 -18.767 -20.146 1.00 24.36 ?  5   SER   B OG   1 
ATOM   3987 H H    . SER   B 1 5   ? 47.156 -17.767 -18.559 1.00 21.14 ?  5   SER   B H    1 
ATOM   3988 H HA   . SER   B 1 5   ? 45.720 -18.731 -20.647 1.00 24.12 ?  5   SER   B HA   1 
ATOM   3989 H HB2  . SER   B 1 5   ? 47.752 -19.139 -21.680 1.00 25.94 ?  5   SER   B HB2  1 
ATOM   3990 H HB3  . SER   B 1 5   ? 47.714 -17.628 -21.193 1.00 25.94 ?  5   SER   B HB3  1 
ATOM   3991 H HG   . SER   B 1 5   ? 48.977 -19.575 -19.925 1.00 29.25 ?  5   SER   B HG   1 
ATOM   3992 N N    . PHE   B 1 6   ? 45.304 -20.707 -19.128 1.00 21.78 ?  6   PHE   B N    1 
ATOM   3993 C CA   . PHE   B 1 6   ? 45.132 -22.049 -18.593 1.00 21.15 ?  6   PHE   B CA   1 
ATOM   3994 C C    . PHE   B 1 6   ? 45.072 -23.043 -19.742 1.00 24.52 ?  6   PHE   B C    1 
ATOM   3995 O O    . PHE   B 1 6   ? 44.403 -22.795 -20.749 1.00 26.48 ?  6   PHE   B O    1 
ATOM   3996 C CB   . PHE   B 1 6   ? 43.846 -22.118 -17.771 1.00 19.13 ?  6   PHE   B CB   1 
ATOM   3997 C CG   . PHE   B 1 6   ? 43.859 -21.243 -16.549 1.00 17.23 ?  6   PHE   B CG   1 
ATOM   3998 C CD1  . PHE   B 1 6   ? 44.363 -21.716 -15.352 1.00 16.28 ?  6   PHE   B CD1  1 
ATOM   3999 C CD2  . PHE   B 1 6   ? 43.365 -19.949 -16.600 1.00 16.74 ?  6   PHE   B CD2  1 
ATOM   4000 C CE1  . PHE   B 1 6   ? 44.367 -20.914 -14.220 1.00 15.88 ?  6   PHE   B CE1  1 
ATOM   4001 C CE2  . PHE   B 1 6   ? 43.375 -19.139 -15.479 1.00 17.15 ?  6   PHE   B CE2  1 
ATOM   4002 C CZ   . PHE   B 1 6   ? 43.880 -19.616 -14.288 1.00 16.44 ?  6   PHE   B CZ   1 
ATOM   4003 H H    . PHE   B 1 6   ? 44.577 -20.253 -19.165 1.00 26.15 ?  6   PHE   B H    1 
ATOM   4004 H HA   . PHE   B 1 6   ? 45.880 -22.282 -18.023 1.00 25.40 ?  6   PHE   B HA   1 
ATOM   4005 H HB2  . PHE   B 1 6   ? 43.102 -21.839 -18.328 1.00 22.97 ?  6   PHE   B HB2  1 
ATOM   4006 H HB3  . PHE   B 1 6   ? 43.707 -23.035 -17.478 1.00 22.97 ?  6   PHE   B HB3  1 
ATOM   4007 H HD1  . PHE   B 1 6   ? 44.700 -22.583 -15.303 1.00 19.55 ?  6   PHE   B HD1  1 
ATOM   4008 H HD2  . PHE   B 1 6   ? 43.022 -19.626 -17.401 1.00 20.10 ?  6   PHE   B HD2  1 
ATOM   4009 H HE1  . PHE   B 1 6   ? 44.720 -21.236 -13.421 1.00 19.08 ?  6   PHE   B HE1  1 
ATOM   4010 H HE2  . PHE   B 1 6   ? 43.037 -18.275 -15.530 1.00 20.60 ?  6   PHE   B HE2  1 
ATOM   4011 H HZ   . PHE   B 1 6   ? 43.886 -19.076 -13.533 1.00 19.75 ?  6   PHE   B HZ   1 
ATOM   4012 N N    . SER   B 1 7   ? 45.785 -24.159 -19.598 1.00 25.80 ?  7   SER   B N    1 
ATOM   4013 C CA   . SER   B 1 7   ? 45.882 -25.156 -20.653 1.00 28.16 ?  7   SER   B CA   1 
ATOM   4014 C C    . SER   B 1 7   ? 45.806 -26.552 -20.055 1.00 26.92 ?  7   SER   B C    1 
ATOM   4015 O O    . SER   B 1 7   ? 46.375 -26.817 -18.992 1.00 27.66 ?  7   SER   B O    1 
ATOM   4016 C CB   . SER   B 1 7   ? 47.193 -25.000 -21.435 1.00 31.19 ?  7   SER   B CB   1 
ATOM   4017 O OG   . SER   B 1 7   ? 47.216 -25.849 -22.568 1.00 33.21 ?  7   SER   B OG   1 
ATOM   4018 H H    . SER   B 1 7   ? 46.236 -24.356 -18.889 1.00 30.98 ?  7   SER   B H    1 
ATOM   4019 H HA   . SER   B 1 7   ? 45.145 -25.048 -21.269 1.00 33.81 ?  7   SER   B HA   1 
ATOM   4020 H HB2  . SER   B 1 7   ? 47.276 -24.078 -21.730 1.00 37.44 ?  7   SER   B HB2  1 
ATOM   4021 H HB3  . SER   B 1 7   ? 47.937 -25.227 -20.855 1.00 37.44 ?  7   SER   B HB3  1 
ATOM   4022 H HG   . SER   B 1 7   ? 47.938 -25.750 -22.985 1.00 39.87 ?  7   SER   B HG   1 
ATOM   4023 N N    . GLY   B 1 8   ? 45.097 -27.442 -20.748 1.00 26.42 ?  8   GLY   B N    1 
ATOM   4024 C CA   . GLY   B 1 8   ? 45.047 -28.832 -20.357 1.00 25.69 ?  8   GLY   B CA   1 
ATOM   4025 C C    . GLY   B 1 8   ? 44.093 -29.152 -19.236 1.00 24.19 ?  8   GLY   B C    1 
ATOM   4026 O O    . GLY   B 1 8   ? 44.222 -30.216 -18.617 1.00 25.62 ?  8   GLY   B O    1 
ATOM   4027 H H    . GLY   B 1 8   ? 44.641 -27.253 -21.450 1.00 31.73 ?  8   GLY   B H    1 
ATOM   4028 H HA2  . GLY   B 1 8   ? 44.787 -29.363 -21.123 1.00 30.85 ?  8   GLY   B HA2  1 
ATOM   4029 H HA3  . GLY   B 1 8   ? 45.930 -29.114 -20.078 1.00 30.85 ?  8   GLY   B HA3  1 
ATOM   4030 N N    . TYR   B 1 9   ? 43.119 -28.286 -18.963 1.00 22.46 ?  9   TYR   B N    1 
ATOM   4031 C CA   . TYR   B 1 9   ? 42.157 -28.556 -17.908 1.00 20.65 ?  9   TYR   B CA   1 
ATOM   4032 C C    . TYR   B 1 9   ? 40.974 -29.348 -18.432 1.00 20.21 ?  9   TYR   B C    1 
ATOM   4033 O O    . TYR   B 1 9   ? 40.564 -29.214 -19.588 1.00 22.07 ?  9   TYR   B O    1 
ATOM   4034 C CB   . TYR   B 1 9   ? 41.651 -27.266 -17.269 1.00 20.03 ?  9   TYR   B CB   1 
ATOM   4035 C CG   . TYR   B 1 9   ? 42.673 -26.644 -16.352 1.00 19.34 ?  9   TYR   B CG   1 
ATOM   4036 C CD1  . TYR   B 1 9   ? 43.780 -25.984 -16.867 1.00 19.70 ?  9   TYR   B CD1  1 
ATOM   4037 C CD2  . TYR   B 1 9   ? 42.545 -26.731 -14.975 1.00 18.87 ?  9   TYR   B CD2  1 
ATOM   4038 C CE1  . TYR   B 1 9   ? 44.728 -25.424 -16.037 1.00 20.07 ?  9   TYR   B CE1  1 
ATOM   4039 C CE2  . TYR   B 1 9   ? 43.491 -26.173 -14.134 1.00 18.97 ?  9   TYR   B CE2  1 
ATOM   4040 C CZ   . TYR   B 1 9   ? 44.581 -25.517 -14.673 1.00 19.89 ?  9   TYR   B CZ   1 
ATOM   4041 O OH   . TYR   B 1 9   ? 45.528 -24.965 -13.848 1.00 20.59 ?  9   TYR   B OH   1 
ATOM   4042 H H    . TYR   B 1 9   ? 42.980 -27.548 -19.385 1.00 26.97 ?  9   TYR   B H    1 
ATOM   4043 H HA   . TYR   B 1 9   ? 42.580 -29.082 -17.217 1.00 24.79 ?  9   TYR   B HA   1 
ATOM   4044 H HB2  . TYR   B 1 9   ? 41.428 -26.622 -17.961 1.00 24.05 ?  9   TYR   B HB2  1 
ATOM   4045 H HB3  . TYR   B 1 9   ? 40.867 -27.474 -16.741 1.00 24.05 ?  9   TYR   B HB3  1 
ATOM   4046 H HD1  . TYR   B 1 9   ? 43.882 -25.922 -17.790 1.00 23.66 ?  9   TYR   B HD1  1 
ATOM   4047 H HD2  . TYR   B 1 9   ? 41.805 -27.175 -14.612 1.00 22.67 ?  9   TYR   B HD2  1 
ATOM   4048 H HE1  . TYR   B 1 9   ? 45.460 -24.990 -16.398 1.00 24.10 ?  9   TYR   B HE1  1 
ATOM   4049 H HE2  . TYR   B 1 9   ? 43.383 -26.243 -13.212 1.00 22.79 ?  9   TYR   B HE2  1 
ATOM   4050 H HH   . TYR   B 1 9   ? 46.123 -24.605 -14.308 1.00 24.72 ?  9   TYR   B HH   1 
ATOM   4051 N N    . LEU   B 1 10  ? 40.435 -30.189 -17.559 1.00 18.35 ?  10  LEU   B N    1 
ATOM   4052 C CA   . LEU   B 1 10  ? 39.229 -30.946 -17.835 1.00 18.17 ?  10  LEU   B CA   1 
ATOM   4053 C C    . LEU   B 1 10  ? 38.042 -30.176 -17.272 1.00 17.75 ?  10  LEU   B C    1 
ATOM   4054 O O    . LEU   B 1 10  ? 38.057 -29.760 -16.110 1.00 17.51 ?  10  LEU   B O    1 
ATOM   4055 C CB   . LEU   B 1 10  ? 39.335 -32.316 -17.168 1.00 18.96 ?  10  LEU   B CB   1 
ATOM   4056 C CG   . LEU   B 1 10  ? 38.193 -33.272 -17.490 1.00 20.77 ?  10  LEU   B CG   1 
ATOM   4057 C CD1  . LEU   B 1 10  ? 38.298 -33.763 -18.928 1.00 22.07 ?  10  LEU   B CD1  1 
ATOM   4058 C CD2  . LEU   B 1 10  ? 38.162 -34.433 -16.513 1.00 21.91 ?  10  LEU   B CD2  1 
ATOM   4059 H H    . LEU   B 1 10  ? 40.757 -30.341 -16.773 1.00 22.04 ?  10  LEU   B H    1 
ATOM   4060 H HA   . LEU   B 1 10  ? 39.110 -31.065 -18.787 1.00 21.82 ?  10  LEU   B HA   1 
ATOM   4061 H HB2  . LEU   B 1 10  ? 40.161 -32.739 -17.456 1.00 22.77 ?  10  LEU   B HB2  1 
ATOM   4062 H HB3  . LEU   B 1 10  ? 39.353 -32.197 -16.204 1.00 22.77 ?  10  LEU   B HB3  1 
ATOM   4063 H HG   . LEU   B 1 10  ? 37.354 -32.798 -17.403 1.00 24.94 ?  10  LEU   B HG   1 
ATOM   4064 H HD11 . LEU   B 1 10  ? 37.604 -34.421 -19.086 1.00 26.50 ?  10  LEU   B HD11 1 
ATOM   4065 H HD12 . LEU   B 1 10  ? 38.179 -33.007 -19.526 1.00 26.50 ?  10  LEU   B HD12 1 
ATOM   4066 H HD13 . LEU   B 1 10  ? 39.171 -34.160 -19.063 1.00 26.50 ?  10  LEU   B HD13 1 
ATOM   4067 H HD21 . LEU   B 1 10  ? 37.428 -35.021 -16.749 1.00 26.31 ?  10  LEU   B HD21 1 
ATOM   4068 H HD22 . LEU   B 1 10  ? 39.003 -34.910 -16.565 1.00 26.31 ?  10  LEU   B HD22 1 
ATOM   4069 H HD23 . LEU   B 1 10  ? 38.031 -34.082 -15.618 1.00 26.31 ?  10  LEU   B HD23 1 
ATOM   4070 N N    . LYS   B 1 11  ? 37.018 -29.992 -18.097 1.00 19.04 ?  11  LYS   B N    1 
ATOM   4071 C CA   . LYS   B 1 11  ? 35.823 -29.272 -17.683 1.00 21.02 ?  11  LYS   B CA   1 
ATOM   4072 C C    . LYS   B 1 11  ? 34.939 -30.197 -16.851 1.00 20.13 ?  11  LYS   B C    1 
ATOM   4073 O O    . LYS   B 1 11  ? 34.564 -31.284 -17.308 1.00 21.94 ?  11  LYS   B O    1 
ATOM   4074 C CB   . LYS   B 1 11  ? 35.082 -28.790 -18.929 1.00 24.79 ?  11  LYS   B CB   1 
ATOM   4075 C CG   . LYS   B 1 11  ? 33.919 -27.851 -18.673 1.00 28.23 ?  11  LYS   B CG   1 
ATOM   4076 C CD   . LYS   B 1 11  ? 33.168 -27.569 -19.969 1.00 31.01 ?  11  LYS   B CD   1 
ATOM   4077 C CE   . LYS   B 1 11  ? 32.149 -26.455 -19.803 1.00 32.96 ?  11  LYS   B CE   1 
ATOM   4078 N NZ   . LYS   B 1 11  ? 32.805 -25.135 -19.598 1.00 34.05 ?  11  LYS   B NZ   1 
ATOM   4079 H H    . LYS   B 1 11  ? 36.986 -30.284 -18.906 1.00 22.87 ?  11  LYS   B H    1 
ATOM   4080 H HA   . LYS   B 1 11  ? 36.071 -28.503 -17.147 1.00 25.24 ?  11  LYS   B HA   1 
ATOM   4081 H HB2  . LYS   B 1 11  ? 35.713 -28.319 -19.498 1.00 29.77 ?  11  LYS   B HB2  1 
ATOM   4082 H HB3  . LYS   B 1 11  ? 34.735 -29.561 -19.401 1.00 29.77 ?  11  LYS   B HB3  1 
ATOM   4083 H HG2  . LYS   B 1 11  ? 33.304 -28.261 -18.047 1.00 33.90 ?  11  LYS   B HG2  1 
ATOM   4084 H HG3  . LYS   B 1 11  ? 34.252 -27.011 -18.323 1.00 33.90 ?  11  LYS   B HG3  1 
ATOM   4085 H HD2  . LYS   B 1 11  ? 33.802 -27.301 -20.653 1.00 37.23 ?  11  LYS   B HD2  1 
ATOM   4086 H HD3  . LYS   B 1 11  ? 32.699 -28.372 -20.247 1.00 37.23 ?  11  LYS   B HD3  1 
ATOM   4087 H HE2  . LYS   B 1 11  ? 31.601 -26.402 -20.602 1.00 39.58 ?  11  LYS   B HE2  1 
ATOM   4088 H HE3  . LYS   B 1 11  ? 31.596 -26.647 -19.030 1.00 39.58 ?  11  LYS   B HE3  1 
ATOM   4089 H HZ1  . LYS   B 1 11  ? 32.188 -24.498 -19.524 1.00 40.87 ?  11  LYS   B HZ1  1 
ATOM   4090 H HZ2  . LYS   B 1 11  ? 33.296 -25.150 -18.857 1.00 40.87 ?  11  LYS   B HZ2  1 
ATOM   4091 H HZ3  . LYS   B 1 11  ? 33.332 -24.947 -20.291 1.00 40.87 ?  11  LYS   B HZ3  1 
ATOM   4092 N N    . LEU   B 1 12  ? 34.605 -29.771 -15.632 1.00 18.66 ?  12  LEU   B N    1 
ATOM   4093 C CA   . LEU   B 1 12  ? 33.645 -30.483 -14.793 1.00 17.95 ?  12  LEU   B CA   1 
ATOM   4094 C C    . LEU   B 1 12  ? 32.253 -29.877 -14.880 1.00 17.62 ?  12  LEU   B C    1 
ATOM   4095 O O    . LEU   B 1 12  ? 31.268 -30.594 -15.059 1.00 18.09 ?  12  LEU   B O    1 
ATOM   4096 C CB   . LEU   B 1 12  ? 34.104 -30.509 -13.329 1.00 17.33 ?  12  LEU   B CB   1 
ATOM   4097 C CG   . LEU   B 1 12  ? 35.450 -31.180 -13.058 1.00 17.16 ?  12  LEU   B CG   1 
ATOM   4098 C CD1  . LEU   B 1 12  ? 35.808 -31.135 -11.579 1.00 17.35 ?  12  LEU   B CD1  1 
ATOM   4099 C CD2  . LEU   B 1 12  ? 35.454 -32.611 -13.572 1.00 17.65 ?  12  LEU   B CD2  1 
ATOM   4100 H H    . LEU   B 1 12  ? 34.920 -29.058 -15.266 1.00 22.41 ?  12  LEU   B H    1 
ATOM   4101 H HA   . LEU   B 1 12  ? 33.577 -31.398 -15.105 1.00 21.56 ?  12  LEU   B HA   1 
ATOM   4102 H HB2  . LEU   B 1 12  ? 34.162 -29.597 -13.013 1.00 20.81 ?  12  LEU   B HB2  1 
ATOM   4103 H HB3  . LEU   B 1 12  ? 33.432 -30.986 -12.812 1.00 20.81 ?  12  LEU   B HB3  1 
ATOM   4104 H HG   . LEU   B 1 12  ? 36.134 -30.693 -13.539 1.00 20.61 ?  12  LEU   B HG   1 
ATOM   4105 H HD11 . LEU   B 1 12  ? 36.671 -31.567 -11.451 1.00 20.84 ?  12  LEU   B HD11 1 
ATOM   4106 H HD12 . LEU   B 1 12  ? 35.858 -30.212 -11.290 1.00 20.84 ?  12  LEU   B HD12 1 
ATOM   4107 H HD13 . LEU   B 1 12  ? 35.129 -31.606 -11.071 1.00 20.84 ?  12  LEU   B HD13 1 
ATOM   4108 H HD21 . LEU   B 1 12  ? 36.256 -33.055 -13.261 1.00 21.20 ?  12  LEU   B HD21 1 
ATOM   4109 H HD22 . LEU   B 1 12  ? 34.667 -33.069 -13.236 1.00 21.20 ?  12  LEU   B HD22 1 
ATOM   4110 H HD23 . LEU   B 1 12  ? 35.437 -32.597 -14.543 1.00 21.20 ?  12  LEU   B HD23 1 
ATOM   4111 N N    . THR   B 1 13  ? 32.162 -28.559 -14.752 1.00 17.53 ?  13  THR   B N    1 
ATOM   4112 C CA   . THR   B 1 13  ? 30.939 -27.805 -14.960 1.00 17.73 ?  13  THR   B CA   1 
ATOM   4113 C C    . THR   B 1 13  ? 31.277 -26.614 -15.849 1.00 19.69 ?  13  THR   B C    1 
ATOM   4114 O O    . THR   B 1 13  ? 32.421 -26.432 -16.281 1.00 20.42 ?  13  THR   B O    1 
ATOM   4115 C CB   . THR   B 1 13  ? 30.339 -27.329 -13.631 1.00 17.56 ?  13  THR   B CB   1 
ATOM   4116 O OG1  . THR   B 1 13  ? 31.184 -26.313 -13.075 1.00 17.56 ?  13  THR   B OG1  1 
ATOM   4117 C CG2  . THR   B 1 13  ? 30.208 -28.482 -12.639 1.00 18.19 ?  13  THR   B CG2  1 
ATOM   4118 H H    . THR   B 1 13  ? 32.826 -28.059 -14.534 1.00 21.06 ?  13  THR   B H    1 
ATOM   4119 H HA   . THR   B 1 13  ? 30.282 -28.360 -15.410 1.00 21.29 ?  13  THR   B HA   1 
ATOM   4120 H HB   . THR   B 1 13  ? 29.455 -26.953 -13.788 1.00 21.09 ?  13  THR   B HB   1 
ATOM   4121 H HG1  . THR   B 1 13  ? 30.893 -25.546 -13.278 1.00 21.09 ?  13  THR   B HG1  1 
ATOM   4122 H HG21 . THR   B 1 13  ? 29.694 -28.198 -11.866 1.00 21.84 ?  13  THR   B HG21 1 
ATOM   4123 H HG22 . THR   B 1 13  ? 29.759 -29.229 -13.060 1.00 21.84 ?  13  THR   B HG22 1 
ATOM   4124 H HG23 . THR   B 1 13  ? 31.088 -28.766 -12.345 1.00 21.84 ?  13  THR   B HG23 1 
ATOM   4125 N N    A ASP   B 1 14  ? 30.266 -25.789 -16.118 0.72 20.56 ?  14  ASP   B N    1 
ATOM   4126 N N    B ASP   B 1 14  ? 30.271 -25.777 -16.112 0.28 20.36 ?  14  ASP   B N    1 
ATOM   4127 C CA   A ASP   B 1 14  ? 30.480 -24.628 -16.972 0.72 22.04 ?  14  ASP   B CA   1 
ATOM   4128 C CA   B ASP   B 1 14  ? 30.478 -24.621 -16.978 0.28 21.19 ?  14  ASP   B CA   1 
ATOM   4129 C C    A ASP   B 1 14  ? 31.580 -23.720 -16.436 0.72 20.48 ?  14  ASP   B C    1 
ATOM   4130 C C    B ASP   B 1 14  ? 31.494 -23.637 -16.416 0.28 19.72 ?  14  ASP   B C    1 
ATOM   4131 O O    A ASP   B 1 14  ? 32.247 -23.034 -17.220 0.72 21.78 ?  14  ASP   B O    1 
ATOM   4132 O O    B ASP   B 1 14  ? 31.993 -22.791 -17.166 0.28 20.05 ?  14  ASP   B O    1 
ATOM   4133 C CB   A ASP   B 1 14  ? 29.175 -23.847 -17.136 0.72 25.32 ?  14  ASP   B CB   1 
ATOM   4134 C CB   B ASP   B 1 14  ? 29.157 -23.892 -17.225 0.28 23.51 ?  14  ASP   B CB   1 
ATOM   4135 C CG   A ASP   B 1 14  ? 28.202 -24.519 -18.081 0.72 28.81 ?  14  ASP   B CG   1 
ATOM   4136 C CG   B ASP   B 1 14  ? 28.281 -24.603 -18.239 0.28 25.68 ?  14  ASP   B CG   1 
ATOM   4137 O OD1  A ASP   B 1 14  ? 28.575 -25.516 -18.739 0.72 30.07 ?  14  ASP   B OD1  1 
ATOM   4138 O OD1  B ASP   B 1 14  ? 28.835 -25.249 -19.154 0.28 26.43 ?  14  ASP   B OD1  1 
ATOM   4139 O OD2  A ASP   B 1 14  ? 27.049 -24.047 -18.158 0.72 30.27 -1 14  ASP   B OD2  1 
ATOM   4140 O OD2  B ASP   B 1 14  ? 27.040 -24.521 -18.123 0.28 26.44 -1 14  ASP   B OD2  1 
ATOM   4141 H H    A ASP   B 1 14  ? 29.467 -25.868 -15.812 0.72 24.70 ?  14  ASP   B H    1 
ATOM   4142 H H    B ASP   B 1 14  ? 29.473 -25.855 -15.804 0.28 24.46 ?  14  ASP   B H    1 
ATOM   4143 H HA   A ASP   B 1 14  ? 30.760 -24.926 -17.846 0.72 26.46 ?  14  ASP   B HA   1 
ATOM   4144 H HA   B ASP   B 1 14  ? 30.810 -24.931 -17.834 0.28 25.45 ?  14  ASP   B HA   1 
ATOM   4145 H HB2  A ASP   B 1 14  ? 28.730 -23.779 -16.279 0.72 30.40 ?  14  ASP   B HB2  1 
ATOM   4146 H HB2  B ASP   B 1 14  ? 28.667 -23.834 -16.389 0.28 28.23 ?  14  ASP   B HB2  1 
ATOM   4147 H HB3  A ASP   B 1 14  ? 29.371 -22.962 -17.482 0.72 30.40 ?  14  ASP   B HB3  1 
ATOM   4148 H HB3  B ASP   B 1 14  ? 29.350 -22.995 -17.553 0.28 28.23 ?  14  ASP   B HB3  1 
ATOM   4149 N N    . ASN   B 1 15  ? 31.795 -23.705 -15.117 1.00 18.15 ?  15  ASN   B N    1 
ATOM   4150 C CA   . ASN   B 1 15  ? 32.756 -22.789 -14.509 1.00 15.67 ?  15  ASN   B CA   1 
ATOM   4151 C C    . ASN   B 1 15  ? 33.846 -23.442 -13.669 1.00 14.63 ?  15  ASN   B C    1 
ATOM   4152 O O    . ASN   B 1 15  ? 34.695 -22.715 -13.140 1.00 14.82 ?  15  ASN   B O    1 
ATOM   4153 C CB   . ASN   B 1 15  ? 32.037 -21.737 -13.650 1.00 15.80 ?  15  ASN   B CB   1 
ATOM   4154 C CG   . ASN   B 1 15  ? 31.413 -22.336 -12.410 1.00 15.61 ?  15  ASN   B CG   1 
ATOM   4155 O OD1  . ASN   B 1 15  ? 30.469 -23.130 -12.498 1.00 17.12 ?  15  ASN   B OD1  1 
ATOM   4156 N ND2  . ASN   B 1 15  ? 31.940 -21.987 -11.250 1.00 15.01 ?  15  ASN   B ND2  1 
ATOM   4157 H H    A ASN   B 1 15  ? 31.391 -24.216 -14.554 0.72 21.79 ?  15  ASN   B H    1 
ATOM   4158 H H    B ASN   B 1 15  ? 31.430 -24.252 -14.562 0.28 21.79 ?  15  ASN   B H    1 
ATOM   4159 H HA   . ASN   B 1 15  ? 33.206 -22.306 -15.211 1.00 18.82 ?  15  ASN   B HA   1 
ATOM   4160 H HB2  . ASN   B 1 15  ? 32.682 -21.060 -13.371 1.00 18.98 ?  15  ASN   B HB2  1 
ATOM   4161 H HB3  . ASN   B 1 15  ? 31.333 -21.318 -14.172 1.00 18.98 ?  15  ASN   B HB3  1 
ATOM   4162 H HD21 . ASN   B 1 15  ? 31.620 -22.301 -10.516 1.00 18.03 ?  15  ASN   B HD21 1 
ATOM   4163 H HD22 . ASN   B 1 15  ? 32.606 -21.434 -11.221 1.00 18.03 ?  15  ASN   B HD22 1 
ATOM   4164 N N    . VAL   B 1 16  ? 33.861 -24.766 -13.525 1.00 14.36 ?  16  VAL   B N    1 
ATOM   4165 C CA   . VAL   B 1 16  ? 34.863 -25.455 -12.720 1.00 14.09 ?  16  VAL   B CA   1 
ATOM   4166 C C    . VAL   B 1 16  ? 35.652 -26.393 -13.618 1.00 14.27 ?  16  VAL   B C    1 
ATOM   4167 O O    . VAL   B 1 16  ? 35.071 -27.270 -14.276 1.00 15.33 ?  16  VAL   B O    1 
ATOM   4168 C CB   . VAL   B 1 16  ? 34.239 -26.221 -11.541 1.00 14.61 ?  16  VAL   B CB   1 
ATOM   4169 C CG1  . VAL   B 1 16  ? 35.331 -26.942 -10.743 1.00 14.54 ?  16  VAL   B CG1  1 
ATOM   4170 C CG2  . VAL   B 1 16  ? 33.430 -25.276 -10.655 1.00 15.26 ?  16  VAL   B CG2  1 
ATOM   4171 H H    . VAL   B 1 16  ? 33.283 -25.295 -13.888 1.00 17.26 ?  16  VAL   B H    1 
ATOM   4172 H HA   . VAL   B 1 16  ? 35.476 -24.799 -12.353 1.00 16.93 ?  16  VAL   B HA   1 
ATOM   4173 H HB   . VAL   B 1 16  ? 33.635 -26.896 -11.889 1.00 17.56 ?  16  VAL   B HB   1 
ATOM   4174 H HG11 . VAL   B 1 16  ? 34.956 -27.251 -9.903  1.00 17.47 ?  16  VAL   B HG11 1 
ATOM   4175 H HG12 . VAL   B 1 16  ? 35.659 -27.696 -11.255 1.00 17.47 ?  16  VAL   B HG12 1 
ATOM   4176 H HG13 . VAL   B 1 16  ? 36.057 -26.319 -10.567 1.00 17.47 ?  16  VAL   B HG13 1 
ATOM   4177 H HG21 . VAL   B 1 16  ? 33.102 -25.770 -9.886  1.00 18.34 ?  16  VAL   B HG21 1 
ATOM   4178 H HG22 . VAL   B 1 16  ? 33.998 -24.549 -10.366 1.00 18.34 ?  16  VAL   B HG22 1 
ATOM   4179 H HG23 . VAL   B 1 16  ? 32.681 -24.930 -11.168 1.00 18.34 ?  16  VAL   B HG23 1 
ATOM   4180 N N    . TYR   B 1 17  ? 36.976 -26.227 -13.598 1.00 14.76 ?  17  TYR   B N    1 
ATOM   4181 C CA   . TYR   B 1 17  ? 37.925 -26.979 -14.405 1.00 15.15 ?  17  TYR   B CA   1 
ATOM   4182 C C    . TYR   B 1 17  ? 38.973 -27.587 -13.482 1.00 14.29 ?  17  TYR   B C    1 
ATOM   4183 O O    . TYR   B 1 17  ? 39.250 -27.049 -12.407 1.00 14.42 ?  17  TYR   B O    1 
ATOM   4184 C CB   . TYR   B 1 17  ? 38.635 -26.052 -15.399 1.00 17.55 ?  17  TYR   B CB   1 
ATOM   4185 C CG   . TYR   B 1 17  ? 37.710 -25.284 -16.311 1.00 20.44 ?  17  TYR   B CG   1 
ATOM   4186 C CD1  . TYR   B 1 17  ? 37.129 -24.090 -15.904 1.00 21.67 ?  17  TYR   B CD1  1 
ATOM   4187 C CD2  . TYR   B 1 17  ? 37.423 -25.753 -17.584 1.00 22.32 ?  17  TYR   B CD2  1 
ATOM   4188 C CE1  . TYR   B 1 17  ? 36.281 -23.385 -16.740 1.00 23.16 ?  17  TYR   B CE1  1 
ATOM   4189 C CE2  . TYR   B 1 17  ? 36.580 -25.055 -18.428 1.00 23.74 ?  17  TYR   B CE2  1 
ATOM   4190 C CZ   . TYR   B 1 17  ? 36.012 -23.874 -18.001 1.00 24.26 ?  17  TYR   B CZ   1 
ATOM   4191 O OH   . TYR   B 1 17  ? 35.176 -23.177 -18.840 1.00 25.67 ?  17  TYR   B OH   1 
ATOM   4192 H H    . TYR   B 1 17  ? 37.367 -25.646 -13.094 1.00 17.73 ?  17  TYR   B H    1 
ATOM   4193 H HA   . TYR   B 1 17  ? 37.464 -27.687 -14.891 1.00 18.20 ?  17  TYR   B HA   1 
ATOM   4194 H HB2  . TYR   B 1 17  ? 39.167 -25.411 -14.904 1.00 21.07 ?  17  TYR   B HB2  1 
ATOM   4195 H HB3  . TYR   B 1 17  ? 39.207 -26.591 -15.962 1.00 21.07 ?  17  TYR   B HB3  1 
ATOM   4196 H HD1  . TYR   B 1 17  ? 37.309 -23.758 -15.055 1.00 26.02 ?  17  TYR   B HD1  1 
ATOM   4197 H HD2  . TYR   B 1 17  ? 37.800 -26.549 -17.876 1.00 26.81 ?  17  TYR   B HD2  1 
ATOM   4198 H HE1  . TYR   B 1 17  ? 35.897 -22.584 -16.457 1.00 27.82 ?  17  TYR   B HE1  1 
ATOM   4199 H HE2  . TYR   B 1 17  ? 36.391 -25.381 -19.281 1.00 28.51 ?  17  TYR   B HE2  1 
ATOM   4200 H HH   . TYR   B 1 17  ? 35.092 -23.580 -19.573 1.00 30.82 ?  17  TYR   B HH   1 
ATOM   4201 N N    . ILE   B 1 18  ? 39.583 -28.695 -13.905 1.00 14.37 ?  18  ILE   B N    1 
ATOM   4202 C CA   . ILE   B 1 18  ? 40.513 -29.414 -13.041 1.00 14.30 ?  18  ILE   B CA   1 
ATOM   4203 C C    . ILE   B 1 18  ? 41.674 -29.968 -13.858 1.00 14.71 ?  18  ILE   B C    1 
ATOM   4204 O O    . ILE   B 1 18  ? 41.514 -30.357 -15.020 1.00 15.99 ?  18  ILE   B O    1 
ATOM   4205 C CB   . ILE   B 1 18  ? 39.764 -30.512 -12.242 1.00 14.70 ?  18  ILE   B CB   1 
ATOM   4206 C CG1  . ILE   B 1 18  ? 40.623 -31.050 -11.095 1.00 14.83 ?  18  ILE   B CG1  1 
ATOM   4207 C CG2  . ILE   B 1 18  ? 39.286 -31.641 -13.161 1.00 15.07 ?  18  ILE   B CG2  1 
ATOM   4208 C CD1  . ILE   B 1 18  ? 39.820 -31.879 -10.102 1.00 16.31 ?  18  ILE   B CD1  1 
ATOM   4209 H H    . ILE   B 1 18  ? 39.474 -29.048 -14.679 1.00 17.26 ?  18  ILE   B H    1 
ATOM   4210 H HA   . ILE   B 1 18  ? 40.875 -28.797 -12.390 1.00 17.18 ?  18  ILE   B HA   1 
ATOM   4211 H HB   . ILE   B 1 18  ? 38.974 -30.114 -11.844 1.00 17.66 ?  18  ILE   B HB   1 
ATOM   4212 H HG12 . ILE   B 1 18  ? 41.326 -31.610 -11.456 1.00 17.82 ?  18  ILE   B HG12 1 
ATOM   4213 H HG13 . ILE   B 1 18  ? 41.009 -30.299 -10.612 1.00 17.82 ?  18  ILE   B HG13 1 
ATOM   4214 H HG21 . ILE   B 1 18  ? 38.680 -32.217 -12.667 1.00 18.11 ?  18  ILE   B HG21 1 
ATOM   4215 H HG22 . ILE   B 1 18  ? 38.827 -31.250 -13.918 1.00 18.11 ?  18  ILE   B HG22 1 
ATOM   4216 H HG23 . ILE   B 1 18  ? 40.054 -32.150 -13.461 1.00 18.11 ?  18  ILE   B HG23 1 
ATOM   4217 H HD11 . ILE   B 1 18  ? 40.396 -32.138 -9.364  1.00 19.59 ?  18  ILE   B HD11 1 
ATOM   4218 H HD12 . ILE   B 1 18  ? 39.078 -31.349 -9.771  1.00 19.59 ?  18  ILE   B HD12 1 
ATOM   4219 H HD13 . ILE   B 1 18  ? 39.484 -32.672 -10.551 1.00 19.59 ?  18  ILE   B HD13 1 
ATOM   4220 N N    . LYS   B 1 19  ? 42.853 -30.006 -13.235 1.00 15.01 ?  19  LYS   B N    1 
ATOM   4221 C CA   . LYS   B 1 19  ? 44.065 -30.481 -13.888 1.00 15.46 ?  19  LYS   B CA   1 
ATOM   4222 C C    . LYS   B 1 19  ? 44.966 -31.155 -12.864 1.00 15.51 ?  19  LYS   B C    1 
ATOM   4223 O O    . LYS   B 1 19  ? 45.046 -30.718 -11.714 1.00 15.03 ?  19  LYS   B O    1 
ATOM   4224 C CB   . LYS   B 1 19  ? 44.829 -29.313 -14.523 1.00 16.93 ?  19  LYS   B CB   1 
ATOM   4225 C CG   . LYS   B 1 19  ? 46.024 -29.713 -15.370 1.00 18.87 ?  19  LYS   B CG   1 
ATOM   4226 C CD   . LYS   B 1 19  ? 46.747 -28.476 -15.893 1.00 20.60 ?  19  LYS   B CD   1 
ATOM   4227 C CE   . LYS   B 1 19  ? 47.905 -28.843 -16.799 1.00 22.42 ?  19  LYS   B CE   1 
ATOM   4228 N NZ   . LYS   B 1 19  ? 48.653 -27.644 -17.266 1.00 23.52 ?  19  LYS   B NZ   1 
ATOM   4229 H H    . LYS   B 1 19  ? 42.967 -29.752 -12.416 1.00 18.03 ?  19  LYS   B H    1 
ATOM   4230 H HA   . LYS   B 1 19  ? 43.827 -31.123 -14.575 1.00 18.58 ?  19  LYS   B HA   1 
ATOM   4231 H HB2  . LYS   B 1 19  ? 44.216 -28.825 -15.091 1.00 20.33 ?  19  LYS   B HB2  1 
ATOM   4232 H HB3  . LYS   B 1 19  ? 45.146 -28.733 -13.810 1.00 20.33 ?  19  LYS   B HB3  1 
ATOM   4233 H HG2  . LYS   B 1 19  ? 46.639 -30.231 -14.830 1.00 22.66 ?  19  LYS   B HG2  1 
ATOM   4234 H HG3  . LYS   B 1 19  ? 45.712 -30.237 -16.126 1.00 22.66 ?  19  LYS   B HG3  1 
ATOM   4235 H HD2  . LYS   B 1 19  ? 46.121 -27.933 -16.398 1.00 24.74 ?  19  LYS   B HD2  1 
ATOM   4236 H HD3  . LYS   B 1 19  ? 47.094 -27.972 -15.140 1.00 24.74 ?  19  LYS   B HD3  1 
ATOM   4237 H HE2  . LYS   B 1 19  ? 48.519 -29.415 -16.312 1.00 26.93 ?  19  LYS   B HE2  1 
ATOM   4238 H HE3  . LYS   B 1 19  ? 47.562 -29.310 -17.577 1.00 26.93 ?  19  LYS   B HE3  1 
ATOM   4239 H HZ1  . LYS   B 1 19  ? 49.290 -27.887 -17.838 1.00 28.24 ?  19  LYS   B HZ1  1 
ATOM   4240 H HZ2  . LYS   B 1 19  ? 48.099 -27.079 -17.674 1.00 28.24 ?  19  LYS   B HZ2  1 
ATOM   4241 H HZ3  . LYS   B 1 19  ? 49.028 -27.231 -16.573 1.00 28.24 ?  19  LYS   B HZ3  1 
ATOM   4242 N N    . ASN   B 1 20  ? 45.649 -32.214 -13.290 1.00 16.52 ?  20  ASN   B N    1 
ATOM   4243 C CA   . ASN   B 1 20  ? 46.685 -32.843 -12.474 1.00 17.66 ?  20  ASN   B CA   1 
ATOM   4244 C C    . ASN   B 1 20  ? 47.955 -32.020 -12.663 1.00 17.97 ?  20  ASN   B C    1 
ATOM   4245 O O    . ASN   B 1 20  ? 48.605 -32.099 -13.709 1.00 19.93 ?  20  ASN   B O    1 
ATOM   4246 C CB   . ASN   B 1 20  ? 46.866 -34.295 -12.908 1.00 19.24 ?  20  ASN   B CB   1 
ATOM   4247 C CG   . ASN   B 1 20  ? 48.027 -34.994 -12.217 1.00 20.70 ?  20  ASN   B CG   1 
ATOM   4248 O OD1  . ASN   B 1 20  ? 48.705 -35.832 -12.824 1.00 22.87 ?  20  ASN   B OD1  1 
ATOM   4249 N ND2  . ASN   B 1 20  ? 48.251 -34.680 -10.949 1.00 20.23 ?  20  ASN   B ND2  1 
ATOM   4250 H H    . ASN   B 1 20  ? 45.529 -32.588 -14.054 1.00 19.84 ?  20  ASN   B H    1 
ATOM   4251 H HA   . ASN   B 1 20  ? 46.416 -32.826 -11.540 1.00 21.21 ?  20  ASN   B HA   1 
ATOM   4252 H HB2  . ASN   B 1 20  ? 46.055 -34.791 -12.702 1.00 23.11 ?  20  ASN   B HB2  1 
ATOM   4253 H HB3  . ASN   B 1 20  ? 47.029 -34.316 -13.863 1.00 23.11 ?  20  ASN   B HB3  1 
ATOM   4254 H HD21 . ASN   B 1 20  ? 48.900 -35.045 -10.522 1.00 24.29 ?  20  ASN   B HD21 1 
ATOM   4255 H HD22 . ASN   B 1 20  ? 47.754 -34.096 -10.551 1.00 24.29 ?  20  ASN   B HD22 1 
ATOM   4256 N N    . ALA   B 1 21  ? 48.305 -31.211 -11.661 1.00 17.63 ?  21  ALA   B N    1 
ATOM   4257 C CA   . ALA   B 1 21  ? 49.424 -30.295 -11.815 1.00 18.25 ?  21  ALA   B CA   1 
ATOM   4258 C C    . ALA   B 1 21  ? 49.884 -29.795 -10.456 1.00 17.34 ?  21  ALA   B C    1 
ATOM   4259 O O    . ALA   B 1 21  ? 49.142 -29.823 -9.470  1.00 17.15 ?  21  ALA   B O    1 
ATOM   4260 C CB   . ALA   B 1 21  ? 49.048 -29.113 -12.707 1.00 19.49 ?  21  ALA   B CB   1 
ATOM   4261 H H    . ALA   B 1 21  ? 47.908 -31.178 -10.892 1.00 21.17 ?  21  ALA   B H    1 
ATOM   4262 H HA   . ALA   B 1 21  ? 50.161 -30.775 -12.226 1.00 21.92 ?  21  ALA   B HA   1 
ATOM   4263 H HB1  . ALA   B 1 21  ? 49.838 -28.574 -12.843 1.00 23.41 ?  21  ALA   B HB1  1 
ATOM   4264 H HB2  . ALA   B 1 21  ? 48.725 -29.456 -13.552 1.00 23.41 ?  21  ALA   B HB2  1 
ATOM   4265 H HB3  . ALA   B 1 21  ? 48.355 -28.599 -12.266 1.00 23.41 ?  21  ALA   B HB3  1 
ATOM   4266 N N    . ASP   B 1 22  ? 51.141 -29.348 -10.438 1.00 16.58 ?  22  ASP   B N    1 
ATOM   4267 C CA   . ASP   B 1 22  ? 51.748 -28.647 -9.313  1.00 15.98 ?  22  ASP   B CA   1 
ATOM   4268 C C    . ASP   B 1 22  ? 51.338 -27.177 -9.400  1.00 14.60 ?  22  ASP   B C    1 
ATOM   4269 O O    . ASP   B 1 22  ? 51.644 -26.508 -10.390 1.00 14.79 ?  22  ASP   B O    1 
ATOM   4270 C CB   . ASP   B 1 22  ? 53.266 -28.815 -9.464  1.00 17.32 ?  22  ASP   B CB   1 
ATOM   4271 C CG   . ASP   B 1 22  ? 54.083 -28.064 -8.419  1.00 18.75 ?  22  ASP   B CG   1 
ATOM   4272 O OD1  . ASP   B 1 22  ? 53.712 -26.952 -8.013  1.00 18.71 ?  22  ASP   B OD1  1 
ATOM   4273 O OD2  . ASP   B 1 22  ? 55.147 -28.587 -8.026  1.00 21.12 -1 22  ASP   B OD2  1 
ATOM   4274 H H    . ASP   B 1 22  ? 51.684 -29.445 -11.101 1.00 19.91 ?  22  ASP   B H    1 
ATOM   4275 H HA   . ASP   B 1 22  ? 51.462 -29.027 -8.468  1.00 19.20 ?  22  ASP   B HA   1 
ATOM   4276 H HB2  . ASP   B 1 22  ? 53.493 -29.752 -9.395  1.00 20.80 ?  22  ASP   B HB2  1 
ATOM   4277 H HB3  . ASP   B 1 22  ? 53.537 -28.470 -10.330 1.00 20.80 ?  22  ASP   B HB3  1 
ATOM   4278 N N    . ILE   B 1 23  ? 50.628 -26.681 -8.379  1.00 13.93 ?  23  ILE   B N    1 
ATOM   4279 C CA   . ILE   B 1 23  ? 50.033 -25.342 -8.449  1.00 13.12 ?  23  ILE   B CA   1 
ATOM   4280 C C    . ILE   B 1 23  ? 51.089 -24.254 -8.588  1.00 12.88 ?  23  ILE   B C    1 
ATOM   4281 O O    . ILE   B 1 23  ? 50.824 -23.210 -9.193  1.00 12.55 ?  23  ILE   B O    1 
ATOM   4282 C CB   . ILE   B 1 23  ? 49.097 -25.100 -7.249  1.00 13.61 ?  23  ILE   B CB   1 
ATOM   4283 C CG1  . ILE   B 1 23  ? 48.260 -23.836 -7.461  1.00 14.48 ?  23  ILE   B CG1  1 
ATOM   4284 C CG2  . ILE   B 1 23  ? 49.873 -25.049 -5.949  1.00 14.71 ?  23  ILE   B CG2  1 
ATOM   4285 C CD1  . ILE   B 1 23  ? 47.132 -23.675 -6.455  1.00 15.15 ?  23  ILE   B CD1  1 
ATOM   4286 H H    . ILE   B 1 23  ? 50.474 -27.102 -7.645  1.00 16.74 ?  23  ILE   B H    1 
ATOM   4287 H HA   . ILE   B 1 23  ? 49.484 -25.304 -9.247  1.00 15.76 ?  23  ILE   B HA   1 
ATOM   4288 H HB   . ILE   B 1 23  ? 48.483 -25.849 -7.199  1.00 16.35 ?  23  ILE   B HB   1 
ATOM   4289 H HG12 . ILE   B 1 23  ? 48.838 -23.058 -7.384  1.00 17.40 ?  23  ILE   B HG12 1 
ATOM   4290 H HG13 . ILE   B 1 23  ? 47.867 -23.861 -8.350  1.00 17.40 ?  23  ILE   B HG13 1 
ATOM   4291 H HG21 . ILE   B 1 23  ? 49.249 -25.044 -5.208  1.00 17.67 ?  23  ILE   B HG21 1 
ATOM   4292 H HG22 . ILE   B 1 23  ? 50.447 -25.828 -5.895  1.00 17.67 ?  23  ILE   B HG22 1 
ATOM   4293 H HG23 . ILE   B 1 23  ? 50.412 -24.241 -5.933  1.00 17.67 ?  23  ILE   B HG23 1 
ATOM   4294 H HD11 . ILE   B 1 23  ? 46.607 -22.895 -6.689  1.00 18.20 ?  23  ILE   B HD11 1 
ATOM   4295 H HD12 . ILE   B 1 23  ? 46.573 -24.471 -6.485  1.00 18.20 ?  23  ILE   B HD12 1 
ATOM   4296 H HD13 . ILE   B 1 23  ? 47.510 -23.571 -5.571  1.00 18.20 ?  23  ILE   B HD13 1 
ATOM   4297 N N    . VAL   B 1 24  ? 52.285 -24.461 -8.029  1.00 13.31 ?  24  VAL   B N    1 
ATOM   4298 C CA   . VAL   B 1 24  ? 53.363 -23.484 -8.196  1.00 13.90 ?  24  VAL   B CA   1 
ATOM   4299 C C    . VAL   B 1 24  ? 53.816 -23.438 -9.647  1.00 14.18 ?  24  VAL   B C    1 
ATOM   4300 O O    . VAL   B 1 24  ? 53.961 -22.360 -10.240 1.00 14.52 ?  24  VAL   B O    1 
ATOM   4301 C CB   . VAL   B 1 24  ? 54.539 -23.802 -7.252  1.00 14.76 ?  24  VAL   B CB   1 
ATOM   4302 C CG1  . VAL   B 1 24  ? 55.748 -22.920 -7.573  1.00 15.55 ?  24  VAL   B CG1  1 
ATOM   4303 C CG2  . VAL   B 1 24  ? 54.127 -23.625 -5.812  1.00 15.71 ?  24  VAL   B CG2  1 
ATOM   4304 H H    . VAL   B 1 24  ? 52.496 -25.148 -7.558  1.00 16.00 ?  24  VAL   B H    1 
ATOM   4305 H HA   . VAL   B 1 24  ? 53.030 -22.607 -7.961  1.00 16.70 ?  24  VAL   B HA   1 
ATOM   4306 H HB   . VAL   B 1 24  ? 54.806 -24.729 -7.371  1.00 17.74 ?  24  VAL   B HB   1 
ATOM   4307 H HG11 . VAL   B 1 24  ? 56.346 -22.920 -6.809  1.00 18.68 ?  24  VAL   B HG11 1 
ATOM   4308 H HG12 . VAL   B 1 24  ? 56.202 -23.283 -8.347  1.00 18.68 ?  24  VAL   B HG12 1 
ATOM   4309 H HG13 . VAL   B 1 24  ? 55.438 -22.021 -7.752  1.00 18.68 ?  24  VAL   B HG13 1 
ATOM   4310 H HG21 . VAL   B 1 24  ? 54.864 -23.876 -5.236  1.00 18.87 ?  24  VAL   B HG21 1 
ATOM   4311 H HG22 . VAL   B 1 24  ? 53.893 -22.695 -5.666  1.00 18.87 ?  24  VAL   B HG22 1 
ATOM   4312 H HG23 . VAL   B 1 24  ? 53.358 -24.191 -5.632  1.00 18.87 ?  24  VAL   B HG23 1 
ATOM   4313 N N    . GLU   B 1 25  ? 54.069 -24.610 -10.237 1.00 15.00 ?  25  GLU   B N    1 
ATOM   4314 C CA   . GLU   B 1 25  ? 54.464 -24.645 -11.639 1.00 16.49 ?  25  GLU   B CA   1 
ATOM   4315 C C    . GLU   B 1 25  ? 53.356 -24.101 -12.525 1.00 15.46 ?  25  GLU   B C    1 
ATOM   4316 O O    . GLU   B 1 25  ? 53.620 -23.379 -13.495 1.00 16.16 ?  25  GLU   B O    1 
ATOM   4317 C CB   . GLU   B 1 25  ? 54.854 -26.067 -12.041 1.00 20.13 ?  25  GLU   B CB   1 
ATOM   4318 C CG   . GLU   B 1 25  ? 56.146 -26.528 -11.388 1.00 25.48 ?  25  GLU   B CG   1 
ATOM   4319 C CD   . GLU   B 1 25  ? 57.264 -25.499 -11.479 1.00 30.58 ?  25  GLU   B CD   1 
ATOM   4320 O OE1  . GLU   B 1 25  ? 57.645 -25.126 -12.609 1.00 32.34 ?  25  GLU   B OE1  1 
ATOM   4321 O OE2  . GLU   B 1 25  ? 57.750 -25.043 -10.417 1.00 32.04 -1 25  GLU   B OE2  1 
ATOM   4322 H H    . GLU   B 1 25  ? 54.018 -25.380 -9.854  1.00 18.02 ?  25  GLU   B H    1 
ATOM   4323 H HA   . GLU   B 1 25  ? 55.224 -24.062 -11.764 1.00 19.80 ?  25  GLU   B HA   1 
ATOM   4324 H HB2  . GLU   B 1 25  ? 54.147 -26.677 -11.771 1.00 24.18 ?  25  GLU   B HB2  1 
ATOM   4325 H HB3  . GLU   B 1 25  ? 54.969 -26.102 -13.004 1.00 24.18 ?  25  GLU   B HB3  1 
ATOM   4326 H HG2  . GLU   B 1 25  ? 55.986 -26.688 -10.450 1.00 30.60 ?  25  GLU   B HG2  1 
ATOM   4327 H HG3  . GLU   B 1 25  ? 56.448 -27.337 -11.827 1.00 30.60 ?  25  GLU   B HG3  1 
ATOM   4328 N N    . GLU   B 1 26  ? 52.106 -24.416 -12.190 1.00 14.44 ?  26  GLU   B N    1 
ATOM   4329 C CA   . GLU   B 1 26  ? 50.979 -23.891 -12.951 1.00 14.95 ?  26  GLU   B CA   1 
ATOM   4330 C C    . GLU   B 1 26  ? 50.937 -22.374 -12.878 1.00 14.19 ?  26  GLU   B C    1 
ATOM   4331 O O    . GLU   B 1 26  ? 50.745 -21.701 -13.894 1.00 15.43 ?  26  GLU   B O    1 
ATOM   4332 C CB   . GLU   B 1 26  ? 49.667 -24.471 -12.422 1.00 16.67 ?  26  GLU   B CB   1 
ATOM   4333 C CG   . GLU   B 1 26  ? 49.239 -25.759 -13.092 1.00 20.08 ?  26  GLU   B CG   1 
ATOM   4334 C CD   . GLU   B 1 26  ? 49.006 -25.621 -14.596 1.00 21.90 ?  26  GLU   B CD   1 
ATOM   4335 O OE1  . GLU   B 1 26  ? 48.043 -24.949 -15.023 1.00 22.20 ?  26  GLU   B OE1  1 
ATOM   4336 O OE2  . GLU   B 1 26  ? 49.786 -26.216 -15.353 1.00 24.01 -1 26  GLU   B OE2  1 
ATOM   4337 H H    . GLU   B 1 26  ? 51.882 -24.933 -11.533 1.00 17.35 ?  26  GLU   B H    1 
ATOM   4338 H HA   . GLU   B 1 26  ? 51.072 -24.145 -13.879 1.00 17.96 ?  26  GLU   B HA   1 
ATOM   4339 H HB2  . GLU   B 1 26  ? 49.762 -24.654 -11.471 1.00 20.02 ?  26  GLU   B HB2  1 
ATOM   4340 H HB3  . GLU   B 1 26  ? 48.957 -23.820 -12.553 1.00 20.02 ?  26  GLU   B HB3  1 
ATOM   4341 H HG2  . GLU   B 1 26  ? 49.938 -26.410 -12.973 1.00 24.12 ?  26  GLU   B HG2  1 
ATOM   4342 H HG3  . GLU   B 1 26  ? 48.414 -26.066 -12.681 1.00 24.12 ?  26  GLU   B HG3  1 
ATOM   4343 N N    . ALA   B 1 27  ? 51.084 -21.820 -11.672 1.00 13.49 ?  27  ALA   B N    1 
ATOM   4344 C CA   . ALA   B 1 27  ? 51.044 -20.369 -11.524 1.00 13.84 ?  27  ALA   B CA   1 
ATOM   4345 C C    . ALA   B 1 27  ? 52.113 -19.703 -12.383 1.00 14.92 ?  27  ALA   B C    1 
ATOM   4346 O O    . ALA   B 1 27  ? 51.852 -18.697 -13.059 1.00 15.66 ?  27  ALA   B O    1 
ATOM   4347 C CB   . ALA   B 1 27  ? 51.206 -19.987 -10.052 1.00 13.92 ?  27  ALA   B CB   1 
ATOM   4348 H H    . ALA   B 1 27  ? 51.200 -22.256 -10.935 1.00 16.21 ?  27  ALA   B H    1 
ATOM   4349 H HA   . ALA   B 1 27  ? 50.181 -20.044 -11.818 1.00 16.63 ?  27  ALA   B HA   1 
ATOM   4350 H HB1  . ALA   B 1 27  ? 51.173 -19.020 -9.968  1.00 16.73 ?  27  ALA   B HB1  1 
ATOM   4351 H HB2  . ALA   B 1 27  ? 50.482 -20.385 -9.538  1.00 16.73 ?  27  ALA   B HB2  1 
ATOM   4352 H HB3  . ALA   B 1 27  ? 52.058 -20.317 -9.727  1.00 16.73 ?  27  ALA   B HB3  1 
ATOM   4353 N N    . LYS   B 1 28  ? 53.328 -20.257 -12.378 1.00 16.18 ?  28  LYS   B N    1 
ATOM   4354 C CA   . LYS   B 1 28  ? 54.405 -19.644 -13.146 1.00 18.16 ?  28  LYS   B CA   1 
ATOM   4355 C C    . LYS   B 1 28  ? 54.146 -19.718 -14.649 1.00 19.02 ?  28  LYS   B C    1 
ATOM   4356 O O    . LYS   B 1 28  ? 54.554 -18.815 -15.389 1.00 20.12 ?  28  LYS   B O    1 
ATOM   4357 C CB   . LYS   B 1 28  ? 55.752 -20.261 -12.755 1.00 20.70 ?  28  LYS   B CB   1 
ATOM   4358 C CG   . LYS   B 1 28  ? 56.181 -19.885 -11.338 1.00 23.81 ?  28  LYS   B CG   1 
ATOM   4359 C CD   . LYS   B 1 28  ? 57.611 -20.291 -11.021 1.00 28.04 ?  28  LYS   B CD   1 
ATOM   4360 C CE   . LYS   B 1 28  ? 57.705 -21.748 -10.642 1.00 31.39 ?  28  LYS   B CE   1 
ATOM   4361 N NZ   . LYS   B 1 28  ? 59.060 -22.080 -10.123 1.00 32.80 ?  28  LYS   B NZ   1 
ATOM   4362 H H    . LYS   B 1 28  ? 53.550 -20.974 -11.947 1.00 19.44 ?  28  LYS   B H    1 
ATOM   4363 H HA   . LYS   B 1 28  ? 54.451 -18.708 -12.906 1.00 21.81 ?  28  LYS   B HA   1 
ATOM   4364 H HB2  . LYS   B 1 28  ? 55.691 -21.228 -12.797 1.00 24.86 ?  28  LYS   B HB2  1 
ATOM   4365 H HB3  . LYS   B 1 28  ? 56.440 -19.945 -13.364 1.00 24.86 ?  28  LYS   B HB3  1 
ATOM   4366 H HG2  . LYS   B 1 28  ? 56.113 -18.922 -11.235 1.00 28.60 ?  28  LYS   B HG2  1 
ATOM   4367 H HG3  . LYS   B 1 28  ? 55.596 -20.328 -10.704 1.00 28.60 ?  28  LYS   B HG3  1 
ATOM   4368 H HD2  . LYS   B 1 28  ? 58.166 -20.142 -11.803 1.00 33.66 ?  28  LYS   B HD2  1 
ATOM   4369 H HD3  . LYS   B 1 28  ? 57.935 -19.760 -10.275 1.00 33.66 ?  28  LYS   B HD3  1 
ATOM   4370 H HE2  . LYS   B 1 28  ? 57.056 -21.941 -9.948  1.00 37.69 ?  28  LYS   B HE2  1 
ATOM   4371 H HE3  . LYS   B 1 28  ? 57.534 -22.295 -11.425 1.00 37.69 ?  28  LYS   B HE3  1 
ATOM   4372 H HZ1  . LYS   B 1 28  ? 59.100 -22.941 -9.904  1.00 39.38 ?  28  LYS   B HZ1  1 
ATOM   4373 H HZ2  . LYS   B 1 28  ? 59.673 -21.910 -10.745 1.00 39.38 ?  28  LYS   B HZ2  1 
ATOM   4374 H HZ3  . LYS   B 1 28  ? 59.237 -21.589 -9.402  1.00 39.38 ?  28  LYS   B HZ3  1 
ATOM   4375 N N    . LYS   B 1 29  ? 53.452 -20.761 -15.111 1.00 20.04 ?  29  LYS   B N    1 
ATOM   4376 C CA   . LYS   B 1 29  ? 53.147 -20.916 -16.532 1.00 22.83 ?  29  LYS   B CA   1 
ATOM   4377 C C    . LYS   B 1 29  ? 51.908 -20.134 -16.957 1.00 21.71 ?  29  LYS   B C    1 
ATOM   4378 O O    . LYS   B 1 29  ? 51.914 -19.494 -18.014 1.00 22.97 ?  29  LYS   B O    1 
ATOM   4379 C CB   . LYS   B 1 29  ? 52.968 -22.399 -16.867 1.00 27.43 ?  29  LYS   B CB   1 
ATOM   4380 C CG   . LYS   B 1 29  ? 52.875 -22.685 -18.362 1.00 31.90 ?  29  LYS   B CG   1 
ATOM   4381 C CD   . LYS   B 1 29  ? 53.127 -24.152 -18.685 1.00 35.56 ?  29  LYS   B CD   1 
ATOM   4382 C CE   . LYS   B 1 29  ? 52.021 -25.044 -18.150 1.00 38.08 ?  29  LYS   B CE   1 
ATOM   4383 N NZ   . LYS   B 1 29  ? 52.277 -26.481 -18.453 1.00 39.42 ?  29  LYS   B NZ   1 
ATOM   4384 H H    . LYS   B 1 29  ? 53.174 -21.401 -14.619 1.00 24.06 ?  29  LYS   B H    1 
ATOM   4385 H HA   . LYS   B 1 29  ? 53.884 -20.581 -17.052 1.00 27.42 ?  29  LYS   B HA   1 
ATOM   4386 H HB2  . LYS   B 1 29  ? 53.729 -22.886 -16.515 1.00 32.93 ?  29  LYS   B HB2  1 
ATOM   4387 H HB3  . LYS   B 1 29  ? 52.152 -22.719 -16.450 1.00 32.93 ?  29  LYS   B HB3  1 
ATOM   4388 H HG2  . LYS   B 1 29  ? 51.986 -22.459 -18.675 1.00 38.30 ?  29  LYS   B HG2  1 
ATOM   4389 H HG3  . LYS   B 1 29  ? 53.539 -22.156 -18.830 1.00 38.30 ?  29  LYS   B HG3  1 
ATOM   4390 H HD2  . LYS   B 1 29  ? 53.168 -24.264 -19.649 1.00 42.69 ?  29  LYS   B HD2  1 
ATOM   4391 H HD3  . LYS   B 1 29  ? 53.964 -24.430 -18.281 1.00 42.69 ?  29  LYS   B HD3  1 
ATOM   4392 H HE2  . LYS   B 1 29  ? 51.966 -24.942 -17.187 1.00 45.72 ?  29  LYS   B HE2  1 
ATOM   4393 H HE3  . LYS   B 1 29  ? 51.180 -24.791 -18.562 1.00 45.72 ?  29  LYS   B HE3  1 
ATOM   4394 H HZ1  . LYS   B 1 29  ? 51.616 -26.982 -18.130 1.00 47.33 ?  29  LYS   B HZ1  1 
ATOM   4395 H HZ2  . LYS   B 1 29  ? 52.328 -26.602 -19.333 1.00 47.33 ?  29  LYS   B HZ2  1 
ATOM   4396 H HZ3  . LYS   B 1 29  ? 53.044 -26.738 -18.081 1.00 47.33 ?  29  LYS   B HZ3  1 
ATOM   4397 N N    . VAL   B 1 30  ? 50.838 -20.190 -16.159 1.00 19.89 ?  30  VAL   B N    1 
ATOM   4398 C CA   . VAL   B 1 30  ? 49.549 -19.605 -16.536 1.00 19.77 ?  30  VAL   B CA   1 
ATOM   4399 C C    . VAL   B 1 30  ? 49.549 -18.093 -16.370 1.00 18.65 ?  30  VAL   B C    1 
ATOM   4400 O O    . VAL   B 1 30  ? 48.820 -17.379 -17.076 1.00 19.63 ?  30  VAL   B O    1 
ATOM   4401 C CB   . VAL   B 1 30  ? 48.447 -20.235 -15.659 1.00 20.89 ?  30  VAL   B CB   1 
ATOM   4402 C CG1  . VAL   B 1 30  ? 47.157 -19.419 -15.713 1.00 21.33 ?  30  VAL   B CG1  1 
ATOM   4403 C CG2  . VAL   B 1 30  ? 48.196 -21.684 -16.057 1.00 21.66 ?  30  VAL   B CG2  1 
ATOM   4404 H H    . VAL   B 1 30  ? 50.826 -20.571 -15.381 1.00 23.89 ?  30  VAL   B H    1 
ATOM   4405 H HA   . VAL   B 1 30  ? 49.354 -19.825 -17.461 1.00 23.75 ?  30  VAL   B HA   1 
ATOM   4406 H HB   . VAL   B 1 30  ? 48.748 -20.248 -14.737 1.00 25.08 ?  30  VAL   B HB   1 
ATOM   4407 H HG11 . VAL   B 1 30  ? 46.411 -20.005 -15.501 1.00 25.61 ?  30  VAL   B HG11 1 
ATOM   4408 H HG12 . VAL   B 1 30  ? 47.202 -18.704 -15.061 1.00 25.61 ?  30  VAL   B HG12 1 
ATOM   4409 H HG13 . VAL   B 1 30  ? 47.038 -19.063 -16.602 1.00 25.61 ?  30  VAL   B HG13 1 
ATOM   4410 H HG21 . VAL   B 1 30  ? 47.501 -22.057 -15.484 1.00 26.01 ?  30  VAL   B HG21 1 
ATOM   4411 H HG22 . VAL   B 1 30  ? 47.902 -21.712 -16.982 1.00 26.01 ?  30  VAL   B HG22 1 
ATOM   4412 H HG23 . VAL   B 1 30  ? 49.013 -22.191 -15.953 1.00 26.01 ?  30  VAL   B HG23 1 
ATOM   4413 N N    A LYS   B 1 31  ? 50.326 -17.585 -15.421 0.72 18.18 ?  31  LYS   B N    1 
ATOM   4414 N N    B LYS   B 1 31  ? 50.356 -17.593 -15.443 0.28 18.43 ?  31  LYS   B N    1 
ATOM   4415 C CA   A LYS   B 1 31  ? 50.367 -16.173 -15.065 0.72 18.61 ?  31  LYS   B CA   1 
ATOM   4416 C CA   B LYS   B 1 31  ? 50.361 -16.187 -15.064 0.28 18.66 ?  31  LYS   B CA   1 
ATOM   4417 C C    A LYS   B 1 31  ? 48.970 -15.686 -14.676 0.72 16.61 ?  31  LYS   B C    1 
ATOM   4418 C C    B LYS   B 1 31  ? 48.954 -15.711 -14.693 0.28 16.64 ?  31  LYS   B C    1 
ATOM   4419 O O    A LYS   B 1 31  ? 48.440 -14.748 -15.286 0.72 17.36 ?  31  LYS   B O    1 
ATOM   4420 O O    B LYS   B 1 31  ? 48.399 -14.820 -15.344 0.28 16.77 ?  31  LYS   B O    1 
ATOM   4421 C CB   A LYS   B 1 31  ? 50.998 -15.362 -16.203 0.72 21.55 ?  31  LYS   B CB   1 
ATOM   4422 C CB   B LYS   B 1 31  ? 50.971 -15.324 -16.160 0.28 20.92 ?  31  LYS   B CB   1 
ATOM   4423 C CG   A LYS   B 1 31  ? 52.437 -15.766 -16.517 0.72 24.34 ?  31  LYS   B CG   1 
ATOM   4424 C CG   B LYS   B 1 31  ? 52.357 -15.811 -16.563 0.28 22.92 ?  31  LYS   B CG   1 
ATOM   4425 C CD   A LYS   B 1 31  ? 53.001 -14.950 -17.669 0.72 26.96 ?  31  LYS   B CD   1 
ATOM   4426 C CD   B LYS   B 1 31  ? 52.932 -15.023 -17.719 0.28 24.68 ?  31  LYS   B CD   1 
ATOM   4427 C CE   A LYS   B 1 31  ? 54.474 -15.218 -17.872 0.72 28.86 ?  31  LYS   B CE   1 
ATOM   4428 C CE   B LYS   B 1 31  ? 54.404 -15.338 -17.913 0.28 25.98 ?  31  LYS   B CE   1 
ATOM   4429 N NZ   A LYS   B 1 31  ? 55.239 -14.877 -16.644 0.72 30.12 ?  31  LYS   B NZ   1 
ATOM   4430 N NZ   B LYS   B 1 31  ? 55.191 -15.028 -16.687 0.28 26.70 ?  31  LYS   B NZ   1 
ATOM   4431 H H    A LYS   B 1 31  ? 50.852 -18.071 -14.950 0.72 21.83 ?  31  LYS   B H    1 
ATOM   4432 H H    B LYS   B 1 31  ? 50.930 -18.064 -15.014 0.28 22.14 ?  31  LYS   B H    1 
ATOM   4433 H HA   A LYS   B 1 31  ? 50.929 -16.085 -14.289 0.72 22.35 ?  31  LYS   B HA   1 
ATOM   4434 H HA   B LYS   B 1 31  ? 50.910 -16.100 -14.281 0.28 22.41 ?  31  LYS   B HA   1 
ATOM   4435 H HB2  A LYS   B 1 31  ? 50.473 -15.491 -17.007 0.72 25.88 ?  31  LYS   B HB2  1 
ATOM   4436 H HB2  B LYS   B 1 31  ? 50.404 -15.346 -16.944 0.28 25.13 ?  31  LYS   B HB2  1 
ATOM   4437 H HB3  A LYS   B 1 31  ? 50.999 -14.434 -15.946 0.72 25.88 ?  31  LYS   B HB3  1 
ATOM   4438 H HB3  B LYS   B 1 31  ? 51.056 -14.416 -15.830 0.28 25.13 ?  31  LYS   B HB3  1 
ATOM   4439 H HG2  A LYS   B 1 31  ? 52.986 -15.617 -15.730 0.72 29.23 ?  31  LYS   B HG2  1 
ATOM   4440 H HG2  B LYS   B 1 31  ? 52.953 -15.722 -15.803 0.28 27.52 ?  31  LYS   B HG2  1 
ATOM   4441 H HG3  A LYS   B 1 31  ? 52.462 -16.705 -16.766 0.72 29.23 ?  31  LYS   B HG3  1 
ATOM   4442 H HG3  B LYS   B 1 31  ? 52.304 -16.741 -16.834 0.28 27.52 ?  31  LYS   B HG3  1 
ATOM   4443 H HD2  A LYS   B 1 31  ? 52.530 -15.185 -18.483 0.72 32.37 ?  31  LYS   B HD2  1 
ATOM   4444 H HD2  B LYS   B 1 31  ? 52.459 -15.260 -18.531 0.28 29.64 ?  31  LYS   B HD2  1 
ATOM   4445 H HD3  A LYS   B 1 31  ? 52.886 -14.007 -17.473 0.72 32.37 ?  31  LYS   B HD3  1 
ATOM   4446 H HD3  B LYS   B 1 31  ? 52.842 -14.077 -17.536 0.28 29.64 ?  31  LYS   B HD3  1 
ATOM   4447 H HE2  A LYS   B 1 31  ? 54.609 -16.159 -18.069 0.72 34.66 ?  31  LYS   B HE2  1 
ATOM   4448 H HE2  B LYS   B 1 31  ? 54.508 -16.283 -18.111 0.28 31.19 ?  31  LYS   B HE2  1 
ATOM   4449 H HE3  A LYS   B 1 31  ? 54.803 -14.669 -18.603 0.72 34.66 ?  31  LYS   B HE3  1 
ATOM   4450 H HE3  B LYS   B 1 31  ? 54.752 -14.802 -18.642 0.28 31.19 ?  31  LYS   B HE3  1 
ATOM   4451 H HZ1  A LYS   B 1 31  ? 56.111 -14.907 -16.811 0.72 36.16 ?  31  LYS   B HZ1  1 
ATOM   4452 H HZ1  B LYS   B 1 31  ? 56.061 -15.059 -16.867 0.28 32.06 ?  31  LYS   B HZ1  1 
ATOM   4453 H HZ2  A LYS   B 1 31  ? 55.022 -14.058 -16.371 0.72 36.16 ?  31  LYS   B HZ2  1 
ATOM   4454 H HZ2  B LYS   B 1 31  ? 54.985 -14.213 -16.392 0.28 32.06 ?  31  LYS   B HZ2  1 
ATOM   4455 H HZ3  A LYS   B 1 31  ? 55.047 -15.457 -15.996 0.72 36.16 ?  31  LYS   B HZ3  1 
ATOM   4456 H HZ3  B LYS   B 1 31  ? 55.007 -15.620 -16.048 0.28 32.06 ?  31  LYS   B HZ3  1 
ATOM   4457 N N    . PRO   B 1 32  ? 48.354 -16.287 -13.652 1.00 14.75 ?  32  PRO   B N    1 
ATOM   4458 C CA   . PRO   B 1 32  ? 46.978 -15.924 -13.296 1.00 13.67 ?  32  PRO   B CA   1 
ATOM   4459 C C    . PRO   B 1 32  ? 46.897 -14.578 -12.594 1.00 13.86 ?  32  PRO   B C    1 
ATOM   4460 O O    . PRO   B 1 32  ? 47.820 -14.154 -11.894 1.00 15.09 ?  32  PRO   B O    1 
ATOM   4461 C CB   . PRO   B 1 32  ? 46.576 -17.041 -12.326 1.00 13.99 ?  32  PRO   B CB   1 
ATOM   4462 C CG   . PRO   B 1 32  ? 47.874 -17.397 -11.647 1.00 14.21 ?  32  PRO   B CG   1 
ATOM   4463 C CD   . PRO   B 1 32  ? 48.925 -17.273 -12.710 1.00 14.41 ?  32  PRO   B CD   1 
ATOM   4464 H HA   . PRO   B 1 32  ? 46.399 -15.935 -14.077 1.00 16.42 ?  32  PRO   B HA   1 
ATOM   4465 H HB2  . PRO   B 1 32  ? 45.926 -16.713 -11.685 1.00 16.81 ?  32  PRO   B HB2  1 
ATOM   4466 H HB3  . PRO   B 1 32  ? 46.224 -17.803 -12.818 1.00 16.81 ?  32  PRO   B HB3  1 
ATOM   4467 H HG2  . PRO   B 1 32  ? 48.042 -16.776 -10.920 1.00 17.07 ?  32  PRO   B HG2  1 
ATOM   4468 H HG3  . PRO   B 1 32  ? 47.831 -18.309 -11.312 1.00 17.07 ?  32  PRO   B HG3  1 
ATOM   4469 H HD2  . PRO   B 1 32  ? 49.743 -16.934 -12.326 1.00 17.31 ?  32  PRO   B HD2  1 
ATOM   4470 H HD3  . PRO   B 1 32  ? 49.050 -18.121 -13.149 1.00 17.31 ?  32  PRO   B HD3  1 
ATOM   4471 N N    . THR   B 1 33  ? 45.746 -13.924 -12.764 1.00 13.42 ?  33  THR   B N    1 
ATOM   4472 C CA   . THR   B 1 33  ? 45.452 -12.749 -11.954 1.00 13.59 ?  33  THR   B CA   1 
ATOM   4473 C C    . THR   B 1 33  ? 45.404 -13.102 -10.471 1.00 13.23 ?  33  THR   B C    1 
ATOM   4474 O O    . THR   B 1 33  ? 45.868 -12.321 -9.626  1.00 14.09 ?  33  THR   B O    1 
ATOM   4475 C CB   . THR   B 1 33  ? 44.134 -12.112 -12.406 1.00 14.25 ?  33  THR   B CB   1 
ATOM   4476 O OG1  . THR   B 1 33  ? 44.173 -11.863 -13.815 1.00 14.28 ?  33  THR   B OG1  1 
ATOM   4477 C CG2  . THR   B 1 33  ? 43.877 -10.812 -11.660 1.00 15.43 ?  33  THR   B CG2  1 
ATOM   4478 H H    . THR   B 1 33  ? 45.132 -14.139 -13.330 1.00 16.12 ?  33  THR   B H    1 
ATOM   4479 H HA   . THR   B 1 33  ? 46.154 -12.096 -12.081 1.00 16.33 ?  33  THR   B HA   1 
ATOM   4480 H HB   . THR   B 1 33  ? 43.400 -12.723 -12.215 1.00 17.12 ?  33  THR   B HB   1 
ATOM   4481 H HG1  . THR   B 1 33  ? 43.456 -11.496 -14.063 1.00 17.15 ?  33  THR   B HG1  1 
ATOM   4482 H HG21 . THR   B 1 33  ? 43.119 -10.351 -12.046 1.00 18.54 ?  33  THR   B HG21 1 
ATOM   4483 H HG22 . THR   B 1 33  ? 43.693 -10.993 -10.724 1.00 18.54 ?  33  THR   B HG22 1 
ATOM   4484 H HG23 . THR   B 1 33  ? 44.659 -10.238 -11.720 1.00 18.54 ?  33  THR   B HG23 1 
ATOM   4485 N N    . VAL   B 1 34  ? 44.855 -14.272 -10.133 1.00 12.71 ?  34  VAL   B N    1 
ATOM   4486 C CA   . VAL   B 1 34  ? 44.663 -14.670 -8.742  1.00 12.21 ?  34  VAL   B CA   1 
ATOM   4487 C C    . VAL   B 1 34  ? 45.088 -16.120 -8.572  1.00 11.19 ?  34  VAL   B C    1 
ATOM   4488 O O    . VAL   B 1 34  ? 44.563 -17.011 -9.251  1.00 11.85 ?  34  VAL   B O    1 
ATOM   4489 C CB   . VAL   B 1 34  ? 43.192 -14.527 -8.299  1.00 13.16 ?  34  VAL   B CB   1 
ATOM   4490 C CG1  . VAL   B 1 34  ? 43.026 -14.964 -6.851  1.00 13.57 ?  34  VAL   B CG1  1 
ATOM   4491 C CG2  . VAL   B 1 34  ? 42.692 -13.106 -8.495  1.00 14.30 ?  34  VAL   B CG2  1 
ATOM   4492 H H    . VAL   B 1 34  ? 44.590 -14.865 -10.698 1.00 15.27 ?  34  VAL   B H    1 
ATOM   4493 H HA   . VAL   B 1 34  ? 45.215 -14.118 -8.163  1.00 14.67 ?  34  VAL   B HA   1 
ATOM   4494 H HB   . VAL   B 1 34  ? 42.645 -15.110 -8.846  1.00 15.81 ?  34  VAL   B HB   1 
ATOM   4495 H HG11 . VAL   B 1 34  ? 42.166 -14.651 -6.523  1.00 16.31 ?  34  VAL   B HG11 1 
ATOM   4496 H HG12 . VAL   B 1 34  ? 43.062 -15.932 -6.801  1.00 16.31 ?  34  VAL   B HG12 1 
ATOM   4497 H HG13 . VAL   B 1 34  ? 43.739 -14.577 -6.317  1.00 16.31 ?  34  VAL   B HG13 1 
ATOM   4498 H HG21 . VAL   B 1 34  ? 41.774 -13.046 -8.181  1.00 17.18 ?  34  VAL   B HG21 1 
ATOM   4499 H HG22 . VAL   B 1 34  ? 43.253 -12.498 -7.988  1.00 17.18 ?  34  VAL   B HG22 1 
ATOM   4500 H HG23 . VAL   B 1 34  ? 42.731 -12.883 -9.439  1.00 17.18 ?  34  VAL   B HG23 1 
ATOM   4501 N N    . VAL   B 1 35  ? 45.994 -16.368 -7.630  1.00 10.64 ?  35  VAL   B N    1 
ATOM   4502 C CA   . VAL   B 1 35  ? 46.228 -17.709 -7.108  1.00 10.56 ?  35  VAL   B CA   1 
ATOM   4503 C C    . VAL   B 1 35  ? 45.688 -17.763 -5.688  1.00 10.26 ?  35  VAL   B C    1 
ATOM   4504 O O    . VAL   B 1 35  ? 45.906 -16.836 -4.898  1.00 10.89 ?  35  VAL   B O    1 
ATOM   4505 C CB   . VAL   B 1 35  ? 47.710 -18.132 -7.192  1.00 11.32 ?  35  VAL   B CB   1 
ATOM   4506 C CG1  . VAL   B 1 35  ? 48.612 -17.295 -6.280  1.00 11.76 ?  35  VAL   B CG1  1 
ATOM   4507 C CG2  . VAL   B 1 35  ? 47.853 -19.628 -6.860  1.00 12.06 ?  35  VAL   B CG2  1 
ATOM   4508 H H    . VAL   B 1 35  ? 46.497 -15.765 -7.271  1.00 12.79 ?  35  VAL   B H    1 
ATOM   4509 H HA   . VAL   B 1 35  ? 45.712 -18.339 -7.632  1.00 12.70 ?  35  VAL   B HA   1 
ATOM   4510 H HB   . VAL   B 1 35  ? 48.013 -18.012 -8.106  1.00 13.61 ?  35  VAL   B HB   1 
ATOM   4511 H HG11 . VAL   B 1 35  ? 49.532 -17.528 -6.461  1.00 14.13 ?  35  VAL   B HG11 1 
ATOM   4512 H HG12 . VAL   B 1 35  ? 48.453 -16.363 -6.465  1.00 14.13 ?  35  VAL   B HG12 1 
ATOM   4513 H HG13 . VAL   B 1 35  ? 48.390 -17.499 -5.357  1.00 14.13 ?  35  VAL   B HG13 1 
ATOM   4514 H HG21 . VAL   B 1 35  ? 48.775 -19.898 -6.969  1.00 14.49 ?  35  VAL   B HG21 1 
ATOM   4515 H HG22 . VAL   B 1 35  ? 47.571 -19.782 -5.940  1.00 14.49 ?  35  VAL   B HG22 1 
ATOM   4516 H HG23 . VAL   B 1 35  ? 47.285 -20.148 -7.460  1.00 14.49 ?  35  VAL   B HG23 1 
ATOM   4517 N N    . VAL   B 1 36  ? 44.966 -18.838 -5.373  1.00 10.32 ?  36  VAL   B N    1 
ATOM   4518 C CA   . VAL   B 1 36  ? 44.422 -19.043 -4.041  1.00 10.25 ?  36  VAL   B CA   1 
ATOM   4519 C C    . VAL   B 1 36  ? 45.430 -19.809 -3.190  1.00 9.93  ?  36  VAL   B C    1 
ATOM   4520 O O    . VAL   B 1 36  ? 45.974 -20.840 -3.612  1.00 10.98 ?  36  VAL   B O    1 
ATOM   4521 C CB   . VAL   B 1 36  ? 43.082 -19.798 -4.113  1.00 10.63 ?  36  VAL   B CB   1 
ATOM   4522 C CG1  . VAL   B 1 36  ? 42.581 -20.159 -2.719  1.00 11.33 ?  36  VAL   B CG1  1 
ATOM   4523 C CG2  . VAL   B 1 36  ? 42.047 -18.967 -4.843  1.00 11.08 ?  36  VAL   B CG2  1 
ATOM   4524 H H    . VAL   B 1 36  ? 44.786 -19.473 -5.923  1.00 12.41 ?  36  VAL   B H    1 
ATOM   4525 H HA   . VAL   B 1 36  ? 44.259 -18.183 -3.624  1.00 12.32 ?  36  VAL   B HA   1 
ATOM   4526 H HB   . VAL   B 1 36  ? 43.209 -20.624 -4.607  1.00 12.78 ?  36  VAL   B HB   1 
ATOM   4527 H HG11 . VAL   B 1 36  ? 41.642 -20.396 -2.776  1.00 13.61 ?  36  VAL   B HG11 1 
ATOM   4528 H HG12 . VAL   B 1 36  ? 43.092 -20.904 -2.377  1.00 13.61 ?  36  VAL   B HG12 1 
ATOM   4529 H HG13 . VAL   B 1 36  ? 42.687 -19.385 -2.139  1.00 13.61 ?  36  VAL   B HG13 1 
ATOM   4530 H HG21 . VAL   B 1 36  ? 41.210 -19.454 -4.866  1.00 13.32 ?  36  VAL   B HG21 1 
ATOM   4531 H HG22 . VAL   B 1 36  ? 41.930 -18.127 -4.371  1.00 13.32 ?  36  VAL   B HG22 1 
ATOM   4532 H HG23 . VAL   B 1 36  ? 42.359 -18.797 -5.745  1.00 13.32 ?  36  VAL   B HG23 1 
ATOM   4533 N N    . ASN   B 1 37  ? 45.647 -19.318 -1.973  1.00 10.30 ?  37  ASN   B N    1 
ATOM   4534 C CA   . ASN   B 1 37  ? 46.400 -20.037 -0.960  1.00 10.55 ?  37  ASN   B CA   1 
ATOM   4535 C C    . ASN   B 1 37  ? 45.451 -20.708 0.025   1.00 10.42 ?  37  ASN   B C    1 
ATOM   4536 O O    . ASN   B 1 37  ? 44.445 -20.127 0.436   1.00 11.01 ?  37  ASN   B O    1 
ATOM   4537 C CB   . ASN   B 1 37  ? 47.330 -19.089 -0.204  1.00 10.39 ?  37  ASN   B CB   1 
ATOM   4538 C CG   . ASN   B 1 37  ? 48.186 -19.803 0.811   1.00 10.83 ?  37  ASN   B CG   1 
ATOM   4539 O OD1  . ASN   B 1 37  ? 48.521 -20.981 0.637   1.00 11.65 ?  37  ASN   B OD1  1 
ATOM   4540 N ND2  . ASN   B 1 37  ? 48.537 -19.107 1.884   1.00 10.87 ?  37  ASN   B ND2  1 
ATOM   4541 H H    . ASN   B 1 37  ? 45.354 -18.552 -1.702  1.00 12.37 ?  37  ASN   B H    1 
ATOM   4542 H HA   . ASN   B 1 37  ? 46.934 -20.727 -1.380  1.00 12.68 ?  37  ASN   B HA   1 
ATOM   4543 H HB2  . ASN   B 1 37  ? 47.922 -18.661 -0.840  1.00 12.49 ?  37  ASN   B HB2  1 
ATOM   4544 H HB3  . ASN   B 1 37  ? 46.803 -18.430 0.264   1.00 12.49 ?  37  ASN   B HB3  1 
ATOM   4545 H HD21 . ASN   B 1 37  ? 49.035 -19.467 2.488   1.00 13.06 ?  37  ASN   B HD21 1 
ATOM   4546 H HD22 . ASN   B 1 37  ? 48.293 -18.292 1.968   1.00 13.06 ?  37  ASN   B HD22 1 
ATOM   4547 N N    . ALA   B 1 38  ? 45.800 -21.940 0.403   1.00 10.73 ?  38  ALA   B N    1 
ATOM   4548 C CA   . ALA   B 1 38  ? 45.143 -22.686 1.479   1.00 11.31 ?  38  ALA   B CA   1 
ATOM   4549 C C    . ALA   B 1 38  ? 45.732 -22.200 2.803   1.00 10.90 ?  38  ALA   B C    1 
ATOM   4550 O O    . ALA   B 1 38  ? 46.633 -22.808 3.390   1.00 11.81 ?  38  ALA   B O    1 
ATOM   4551 C CB   . ALA   B 1 38  ? 45.367 -24.178 1.288   1.00 12.26 ?  38  ALA   B CB   1 
ATOM   4552 H H    . ALA   B 1 38  ? 46.447 -22.379 0.046   1.00 12.90 ?  38  ALA   B H    1 
ATOM   4553 H HA   . ALA   B 1 38  ? 44.187 -22.507 1.475   1.00 13.60 ?  38  ALA   B HA   1 
ATOM   4554 H HB1  . ALA   B 1 38  ? 44.919 -24.661 2.009   1.00 14.73 ?  38  ALA   B HB1  1 
ATOM   4555 H HB2  . ALA   B 1 38  ? 44.988 -24.449 0.436   1.00 14.73 ?  38  ALA   B HB2  1 
ATOM   4556 H HB3  . ALA   B 1 38  ? 46.314 -24.364 1.308   1.00 14.73 ?  38  ALA   B HB3  1 
ATOM   4557 N N    . ALA   B 1 39  ? 45.213 -21.063 3.265   1.00 10.90 ?  39  ALA   B N    1 
ATOM   4558 C CA   . ALA   B 1 39  ? 45.767 -20.327 4.391   1.00 11.20 ?  39  ALA   B CA   1 
ATOM   4559 C C    . ALA   B 1 39  ? 45.149 -20.768 5.717   1.00 11.21 ?  39  ALA   B C    1 
ATOM   4560 O O    . ALA   B 1 39  ? 44.120 -21.443 5.765   1.00 12.31 ?  39  ALA   B O    1 
ATOM   4561 C CB   . ALA   B 1 39  ? 45.524 -18.827 4.197   1.00 11.86 ?  39  ALA   B CB   1 
ATOM   4562 H H    . ALA   B 1 39  ? 44.515 -20.692 2.925   1.00 13.10 ?  39  ALA   B H    1 
ATOM   4563 H HA   . ALA   B 1 39  ? 46.719 -20.477 4.434   1.00 13.46 ?  39  ALA   B HA   1 
ATOM   4564 H HB1  . ALA   B 1 39  ? 45.898 -18.345 4.954   1.00 14.25 ?  39  ALA   B HB1  1 
ATOM   4565 H HB2  . ALA   B 1 39  ? 45.960 -18.538 3.378   1.00 14.25 ?  39  ALA   B HB2  1 
ATOM   4566 H HB3  . ALA   B 1 39  ? 44.571 -18.659 4.139   1.00 14.25 ?  39  ALA   B HB3  1 
ATOM   4567 N N    . ASN   B 1 40  ? 45.786 -20.341 6.806   1.00 11.67 ?  40  ASN   B N    1 
ATOM   4568 C CA   . ASN   B 1 40  ? 45.225 -20.397 8.146   1.00 12.57 ?  40  ASN   B CA   1 
ATOM   4569 C C    . ASN   B 1 40  ? 45.042 -18.971 8.671   1.00 12.35 ?  40  ASN   B C    1 
ATOM   4570 O O    . ASN   B 1 40  ? 45.455 -17.989 8.044   1.00 12.12 ?  40  ASN   B O    1 
ATOM   4571 C CB   . ASN   B 1 40  ? 46.075 -21.272 9.085   1.00 13.51 ?  40  ASN   B CB   1 
ATOM   4572 C CG   . ASN   B 1 40  ? 47.529 -20.866 9.114   1.00 14.51 ?  40  ASN   B CG   1 
ATOM   4573 O OD1  . ASN   B 1 40  ? 47.849 -19.687 9.182   1.00 16.51 ?  40  ASN   B OD1  1 
ATOM   4574 N ND2  . ASN   B 1 40  ? 48.419 -21.842 9.067   1.00 14.70 ?  40  ASN   B ND2  1 
ATOM   4575 H H    . ASN   B 1 40  ? 46.576 -20.005 6.784   1.00 14.03 ?  40  ASN   B H    1 
ATOM   4576 H HA   . ASN   B 1 40  ? 44.347 -20.798 8.099   1.00 15.11 ?  40  ASN   B HA   1 
ATOM   4577 H HB2  . ASN   B 1 40  ? 45.728 -21.199 9.987   1.00 16.23 ?  40  ASN   B HB2  1 
ATOM   4578 H HB3  . ASN   B 1 40  ? 46.030 -22.193 8.785   1.00 16.23 ?  40  ASN   B HB3  1 
ATOM   4579 H HD21 . ASN   B 1 40  ? 49.261 -21.663 9.080   1.00 17.66 ?  40  ASN   B HD21 1 
ATOM   4580 H HD22 . ASN   B 1 40  ? 48.157 -22.661 9.019   1.00 17.66 ?  40  ASN   B HD22 1 
ATOM   4581 N N    . VAL   B 1 41  ? 44.395 -18.848 9.831   1.00 12.85 ?  41  VAL   B N    1 
ATOM   4582 C CA   . VAL   B 1 41  ? 43.937 -17.530 10.273  1.00 13.39 ?  41  VAL   B CA   1 
ATOM   4583 C C    . VAL   B 1 41  ? 45.089 -16.579 10.572  1.00 13.23 ?  41  VAL   B C    1 
ATOM   4584 O O    . VAL   B 1 41  ? 44.915 -15.357 10.482  1.00 13.44 ?  41  VAL   B O    1 
ATOM   4585 C CB   . VAL   B 1 41  ? 42.955 -17.607 11.459  1.00 15.14 ?  41  VAL   B CB   1 
ATOM   4586 C CG1  . VAL   B 1 41  ? 41.652 -18.279 11.043  1.00 15.19 ?  41  VAL   B CG1  1 
ATOM   4587 C CG2  . VAL   B 1 41  ? 43.588 -18.305 12.655  1.00 16.42 ?  41  VAL   B CG2  1 
ATOM   4588 H H    . VAL   B 1 41  ? 44.216 -19.493 10.364  1.00 15.44 ?  41  VAL   B H    1 
ATOM   4589 H HA   . VAL   B 1 41  ? 43.444 -17.134 9.541   1.00 16.09 ?  41  VAL   B HA   1 
ATOM   4590 H HB   . VAL   B 1 41  ? 42.735 -16.705 11.737  1.00 18.19 ?  41  VAL   B HB   1 
ATOM   4591 H HG11 . VAL   B 1 41  ? 41.040 -18.278 11.797  1.00 18.24 ?  41  VAL   B HG11 1 
ATOM   4592 H HG12 . VAL   B 1 41  ? 41.265 -17.785 10.304  1.00 18.24 ?  41  VAL   B HG12 1 
ATOM   4593 H HG13 . VAL   B 1 41  ? 41.839 -19.191 10.772  1.00 18.24 ?  41  VAL   B HG13 1 
ATOM   4594 H HG21 . VAL   B 1 41  ? 42.948 -18.325 13.385  1.00 19.73 ?  41  VAL   B HG21 1 
ATOM   4595 H HG22 . VAL   B 1 41  ? 43.830 -19.210 12.404  1.00 19.73 ?  41  VAL   B HG22 1 
ATOM   4596 H HG23 . VAL   B 1 41  ? 44.379 -17.813 12.925  1.00 19.73 ?  41  VAL   B HG23 1 
ATOM   4597 N N    . TYR   B 1 42  ? 46.256 -17.095 10.953  1.00 13.45 ?  42  TYR   B N    1 
ATOM   4598 C CA   . TYR   B 1 42  ? 47.406 -16.245 11.226  1.00 13.96 ?  42  TYR   B CA   1 
ATOM   4599 C C    . TYR   B 1 42  ? 48.375 -16.176 10.048  1.00 13.30 ?  42  TYR   B C    1 
ATOM   4600 O O    . TYR   B 1 42  ? 49.466 -15.610 10.185  1.00 14.49 ?  42  TYR   B O    1 
ATOM   4601 C CB   . TYR   B 1 42  ? 48.097 -16.656 12.532  1.00 15.96 ?  42  TYR   B CB   1 
ATOM   4602 C CG   . TYR   B 1 42  ? 47.497 -15.974 13.756  1.00 16.26 ?  42  TYR   B CG   1 
ATOM   4603 C CD1  . TYR   B 1 42  ? 47.718 -14.622 13.993  1.00 15.64 ?  42  TYR   B CD1  1 
ATOM   4604 C CD2  . TYR   B 1 42  ? 46.708 -16.670 14.658  1.00 17.94 ?  42  TYR   B CD2  1 
ATOM   4605 C CE1  . TYR   B 1 42  ? 47.176 -13.984 15.092  1.00 16.75 ?  42  TYR   B CE1  1 
ATOM   4606 C CE2  . TYR   B 1 42  ? 46.166 -16.043 15.766  1.00 18.19 ?  42  TYR   B CE2  1 
ATOM   4607 C CZ   . TYR   B 1 42  ? 46.398 -14.695 15.978  1.00 18.50 ?  42  TYR   B CZ   1 
ATOM   4608 O OH   . TYR   B 1 42  ? 45.862 -14.058 17.079  1.00 21.37 ?  42  TYR   B OH   1 
ATOM   4609 H H    . TYR   B 1 42  ? 46.406 -17.941 11.043  1.00 16.16 ?  42  TYR   B H    1 
ATOM   4610 H HA   . TYR   B 1 42  ? 47.076 -15.347 11.361  1.00 16.78 ?  42  TYR   B HA   1 
ATOM   4611 H HB2  . TYR   B 1 42  ? 48.006 -17.614 12.647  1.00 19.18 ?  42  TYR   B HB2  1 
ATOM   4612 H HB3  . TYR   B 1 42  ? 49.033 -16.414 12.478  1.00 19.18 ?  42  TYR   B HB3  1 
ATOM   4613 H HD1  . TYR   B 1 42  ? 48.246 -14.136 13.390  1.00 18.79 ?  42  TYR   B HD1  1 
ATOM   4614 H HD2  . TYR   B 1 42  ? 46.545 -17.577 14.514  1.00 21.54 ?  42  TYR   B HD2  1 
ATOM   4615 H HE1  . TYR   B 1 42  ? 47.345 -13.080 15.231  1.00 20.12 ?  42  TYR   B HE1  1 
ATOM   4616 H HE2  . TYR   B 1 42  ? 45.641 -16.526 16.359  1.00 21.85 ?  42  TYR   B HE2  1 
ATOM   4617 H HH   . TYR   B 1 42  ? 46.096 -13.257 17.077  1.00 25.66 ?  42  TYR   B HH   1 
ATOM   4618 N N    . LEU   B 1 43  ? 47.975 -16.685 8.884   1.00 12.37 ?  43  LEU   B N    1 
ATOM   4619 C CA   . LEU   B 1 43  ? 48.787 -16.614 7.673   1.00 12.09 ?  43  LEU   B CA   1 
ATOM   4620 C C    . LEU   B 1 43  ? 50.197 -17.126 7.930   1.00 12.38 ?  43  LEU   B C    1 
ATOM   4621 O O    . LEU   B 1 43  ? 51.182 -16.533 7.488   1.00 13.10 ?  43  LEU   B O    1 
ATOM   4622 C CB   . LEU   B 1 43  ? 48.809 -15.209 7.067   1.00 12.28 ?  43  LEU   B CB   1 
ATOM   4623 C CG   . LEU   B 1 43  ? 47.457 -14.590 6.695   1.00 12.55 ?  43  LEU   B CG   1 
ATOM   4624 C CD1  . LEU   B 1 43  ? 47.669 -13.198 6.103   1.00 13.63 ?  43  LEU   B CD1  1 
ATOM   4625 C CD2  . LEU   B 1 43  ? 46.688 -15.488 5.733   1.00 13.02 ?  43  LEU   B CD2  1 
ATOM   4626 H H    . LEU   B 1 43  ? 47.224 -17.088 8.768   1.00 14.87 ?  43  LEU   B H    1 
ATOM   4627 H HA   . LEU   B 1 43  ? 48.389 -17.204 7.010   1.00 14.53 ?  43  LEU   B HA   1 
ATOM   4628 H HB2  . LEU   B 1 43  ? 49.233 -14.614 7.701   1.00 14.75 ?  43  LEU   B HB2  1 
ATOM   4629 H HB3  . LEU   B 1 43  ? 49.336 -15.242 6.253   1.00 14.75 ?  43  LEU   B HB3  1 
ATOM   4630 H HG   . LEU   B 1 43  ? 46.926 -14.488 7.500   1.00 15.08 ?  43  LEU   B HG   1 
ATOM   4631 H HD11 . LEU   B 1 43  ? 46.805 -12.817 5.874   1.00 16.38 ?  43  LEU   B HD11 1 
ATOM   4632 H HD12 . LEU   B 1 43  ? 48.112 -12.639 6.760   1.00 16.38 ?  43  LEU   B HD12 1 
ATOM   4633 H HD13 . LEU   B 1 43  ? 48.218 -13.273 5.308   1.00 16.38 ?  43  LEU   B HD13 1 
ATOM   4634 H HD21 . LEU   B 1 43  ? 45.893 -15.021 5.431   1.00 15.64 ?  43  LEU   B HD21 1 
ATOM   4635 H HD22 . LEU   B 1 43  ? 47.255 -15.700 4.977   1.00 15.64 ?  43  LEU   B HD22 1 
ATOM   4636 H HD23 . LEU   B 1 43  ? 46.435 -16.302 6.197   1.00 15.64 ?  43  LEU   B HD23 1 
ATOM   4637 N N    . LYS   B 1 44  ? 50.292 -18.248 8.646   1.00 12.56 ?  44  LYS   B N    1 
ATOM   4638 C CA   . LYS   B 1 44  ? 51.559 -18.922 8.889   1.00 13.38 ?  44  LYS   B CA   1 
ATOM   4639 C C    . LYS   B 1 44  ? 51.680 -20.042 7.865   1.00 12.75 ?  44  LYS   B C    1 
ATOM   4640 O O    . LYS   B 1 44  ? 50.984 -21.057 7.952   1.00 14.01 ?  44  LYS   B O    1 
ATOM   4641 C CB   . LYS   B 1 44  ? 51.620 -19.434 10.327  1.00 15.05 ?  44  LYS   B CB   1 
ATOM   4642 C CG   . LYS   B 1 44  ? 51.817 -18.325 11.354  1.00 17.50 ?  44  LYS   B CG   1 
ATOM   4643 C CD   . LYS   B 1 44  ? 53.011 -17.456 10.956  1.00 20.54 ?  44  LYS   B CD   1 
ATOM   4644 C CE   . LYS   B 1 44  ? 53.518 -16.593 12.080  1.00 23.15 ?  44  LYS   B CE   1 
ATOM   4645 N NZ   . LYS   B 1 44  ? 54.695 -15.792 11.669  1.00 24.39 ?  44  LYS   B NZ   1 
ATOM   4646 H H    . LYS   B 1 44  ? 49.615 -18.637 9.011   1.00 15.09 ?  44  LYS   B H    1 
ATOM   4647 H HA   . LYS   B 1 44  ? 52.287 -18.304 8.729   1.00 16.08 ?  44  LYS   B HA   1 
ATOM   4648 H HB2  . LYS   B 1 44  ? 50.783 -19.884 10.538  1.00 18.08 ?  44  LYS   B HB2  1 
ATOM   4649 H HB3  . LYS   B 1 44  ? 52.357 -20.053 10.413  1.00 18.08 ?  44  LYS   B HB3  1 
ATOM   4650 H HG2  . LYS   B 1 44  ? 51.024 -17.770 11.392  1.00 21.02 ?  44  LYS   B HG2  1 
ATOM   4651 H HG3  . LYS   B 1 44  ? 51.999 -18.720 12.225  1.00 21.02 ?  44  LYS   B HG3  1 
ATOM   4652 H HD2  . LYS   B 1 44  ? 53.732 -18.037 10.654  1.00 24.66 ?  44  LYS   B HD2  1 
ATOM   4653 H HD3  . LYS   B 1 44  ? 52.738 -16.868 10.233  1.00 24.66 ?  44  LYS   B HD3  1 
ATOM   4654 H HE2  . LYS   B 1 44  ? 52.823 -15.970 12.317  1.00 27.79 ?  44  LYS   B HE2  1 
ATOM   4655 H HE3  . LYS   B 1 44  ? 53.762 -17.152 12.837  1.00 27.79 ?  44  LYS   B HE3  1 
ATOM   4656 H HZ1  . LYS   B 1 44  ? 54.970 -15.288 12.348  1.00 29.29 ?  44  LYS   B HZ1  1 
ATOM   4657 H HZ2  . LYS   B 1 44  ? 55.357 -16.326 11.414  1.00 29.29 ?  44  LYS   B HZ2  1 
ATOM   4658 H HZ3  . LYS   B 1 44  ? 54.474 -15.260 10.987  1.00 29.29 ?  44  LYS   B HZ3  1 
ATOM   4659 N N    . HIS   B 1 45  ? 52.532 -19.826 6.866   1.00 12.46 ?  45  HIS   B N    1 
ATOM   4660 C CA   . HIS   B 1 45  ? 52.554 -20.655 5.662   1.00 12.46 ?  45  HIS   B CA   1 
ATOM   4661 C C    . HIS   B 1 45  ? 53.566 -21.784 5.829   1.00 14.62 ?  45  HIS   B C    1 
ATOM   4662 O O    . HIS   B 1 45  ? 54.624 -21.812 5.209   1.00 16.87 ?  45  HIS   B O    1 
ATOM   4663 C CB   . HIS   B 1 45  ? 52.880 -19.797 4.451   1.00 12.36 ?  45  HIS   B CB   1 
ATOM   4664 C CG   . HIS   B 1 45  ? 52.007 -18.596 4.332   1.00 12.14 ?  45  HIS   B CG   1 
ATOM   4665 N ND1  . HIS   B 1 45  ? 50.629 -18.672 4.299   1.00 12.37 ?  45  HIS   B ND1  1 
ATOM   4666 C CD2  . HIS   B 1 45  ? 52.325 -17.284 4.253   1.00 13.19 ?  45  HIS   B CD2  1 
ATOM   4667 C CE1  . HIS   B 1 45  ? 50.143 -17.448 4.194   1.00 12.16 ?  45  HIS   B CE1  1 
ATOM   4668 N NE2  . HIS   B 1 45  ? 51.148 -16.589 4.159   1.00 12.62 ?  45  HIS   B NE2  1 
ATOM   4669 H H    . HIS   B 1 45  ? 53.103 -19.184 6.858   1.00 14.97 ?  45  HIS   B H    1 
ATOM   4670 H HA   . HIS   B 1 45  ? 51.675 -21.047 5.528   1.00 14.97 ?  45  HIS   B HA   1 
ATOM   4671 H HB2  . HIS   B 1 45  ? 53.799 -19.494 4.520   1.00 14.85 ?  45  HIS   B HB2  1 
ATOM   4672 H HB3  . HIS   B 1 45  ? 52.768 -20.332 3.650   1.00 14.85 ?  45  HIS   B HB3  1 
ATOM   4673 H HD2  . HIS   B 1 45  ? 53.183 -16.921 4.254   1.00 15.85 ?  45  HIS   B HD2  1 
ATOM   4674 H HE1  . HIS   B 1 45  ? 49.242 -17.229 4.142   1.00 14.61 ?  45  HIS   B HE1  1 
ATOM   4675 H HE2  . HIS   B 1 45  ? 51.074 -15.734 4.098   1.00 15.16 ?  45  HIS   B HE2  1 
ATOM   4676 N N    A GLY   B 1 46  ? 53.193 -22.750 6.663   0.72 15.55 ?  46  GLY   B N    1 
ATOM   4677 N N    B GLY   B 1 46  ? 53.207 -22.732 6.687   0.28 15.38 ?  46  GLY   B N    1 
ATOM   4678 C CA   A GLY   B 1 46  ? 54.114 -23.802 7.051   0.72 17.39 ?  46  GLY   B CA   1 
ATOM   4679 C CA   B GLY   B 1 46  ? 54.118 -23.804 7.030   0.28 16.48 ?  46  GLY   B CA   1 
ATOM   4680 C C    A GLY   B 1 46  ? 54.177 -25.019 6.148   0.72 18.89 ?  46  GLY   B C    1 
ATOM   4681 C C    B GLY   B 1 46  ? 54.157 -24.935 6.022   0.28 17.58 ?  46  GLY   B C    1 
ATOM   4682 O O    A GLY   B 1 46  ? 55.265 -25.445 5.748   0.72 21.49 ?  46  GLY   B O    1 
ATOM   4683 O O    B GLY   B 1 46  ? 55.191 -25.188 5.395   0.28 18.11 ?  46  GLY   B O    1 
ATOM   4684 H H    A GLY   B 1 46  ? 52.412 -22.805 7.030   0.72 18.68 ?  46  GLY   B H    1 
ATOM   4685 H H    B GLY   B 1 46  ? 52.440 -22.770 7.084   0.28 18.47 ?  46  GLY   B H    1 
ATOM   4686 H HA2  A GLY   B 1 46  ? 55.006 -23.427 7.106   0.72 20.89 ?  46  GLY   B HA2  1 
ATOM   4687 H HA2  B GLY   B 1 46  ? 55.013 -23.440 7.112   0.28 19.80 ?  46  GLY   B HA2  1 
ATOM   4688 H HA3  A GLY   B 1 46  ? 53.869 -24.119 7.934   0.72 20.89 ?  46  GLY   B HA3  1 
ATOM   4689 H HA3  B GLY   B 1 46  ? 53.863 -24.167 7.895   0.28 19.80 ?  46  GLY   B HA3  1 
ATOM   4690 N N    . GLY   B 1 47  ? 53.025 -25.613 5.840   1.00 18.35 ?  47  GLY   B N    1 
ATOM   4691 C CA   . GLY   B 1 47  ? 52.979 -26.873 5.126   1.00 16.48 ?  47  GLY   B CA   1 
ATOM   4692 C C    . GLY   B 1 47  ? 52.060 -26.850 3.919   1.00 14.32 ?  47  GLY   B C    1 
ATOM   4693 O O    . GLY   B 1 47  ? 51.410 -25.846 3.620   1.00 14.40 ?  47  GLY   B O    1 
ATOM   4694 H H    A GLY   B 1 47  ? 52.249 -25.313 6.063   0.72 22.04 ?  47  GLY   B H    1 
ATOM   4695 H H    B GLY   B 1 47  ? 52.256 -25.354 6.130   0.28 22.04 ?  47  GLY   B H    1 
ATOM   4696 H HA2  . GLY   B 1 47  ? 53.870 -27.110 4.822   1.00 19.80 ?  47  GLY   B HA2  1 
ATOM   4697 H HA3  . GLY   B 1 47  ? 52.674 -27.571 5.730   1.00 19.80 ?  47  GLY   B HA3  1 
ATOM   4698 N N    . GLY   B 1 48  ? 52.015 -27.993 3.232   1.00 13.51 ?  48  GLY   B N    1 
ATOM   4699 C CA   . GLY   B 1 48  ? 51.094 -28.143 2.121   1.00 13.26 ?  48  GLY   B CA   1 
ATOM   4700 C C    . GLY   B 1 48  ? 51.231 -27.031 1.108   1.00 12.56 ?  48  GLY   B C    1 
ATOM   4701 O O    . GLY   B 1 48  ? 52.334 -26.567 0.798   1.00 13.26 ?  48  GLY   B O    1 
ATOM   4702 H H    . GLY   B 1 48  ? 52.510 -28.675 3.381   1.00 16.23 ?  48  GLY   B H    1 
ATOM   4703 H HA2  . GLY   B 1 48  ? 51.260 -28.990 1.674   1.00 15.93 ?  48  GLY   B HA2  1 
ATOM   4704 H HA3  . GLY   B 1 48  ? 50.183 -28.142 2.449   1.00 15.93 ?  48  GLY   B HA3  1 
ATOM   4705 N N    . VAL   B 1 49  ? 50.086 -26.595 0.579   1.00 12.39 ?  49  VAL   B N    1 
ATOM   4706 C CA   . VAL   B 1 49  ? 50.072 -25.575 -0.466  1.00 12.56 ?  49  VAL   B CA   1 
ATOM   4707 C C    . VAL   B 1 49  ? 50.728 -24.288 0.022   1.00 11.65 ?  49  VAL   B C    1 
ATOM   4708 O O    . VAL   B 1 49  ? 51.516 -23.664 -0.699  1.00 12.51 ?  49  VAL   B O    1 
ATOM   4709 C CB   . VAL   B 1 49  ? 48.630 -25.324 -0.952  1.00 13.68 ?  49  VAL   B CB   1 
ATOM   4710 C CG1  . VAL   B 1 49  ? 48.570 -24.086 -1.839  1.00 13.83 ?  49  VAL   B CG1  1 
ATOM   4711 C CG2  . VAL   B 1 49  ? 48.082 -26.541 -1.693  1.00 14.97 ?  49  VAL   B CG2  1 
ATOM   4712 H H    . VAL   B 1 49  ? 49.300 -26.876 0.805   1.00 14.89 ?  49  VAL   B H    1 
ATOM   4713 H HA   . VAL   B 1 49  ? 50.579 -25.894 -1.224  1.00 15.09 ?  49  VAL   B HA   1 
ATOM   4714 H HB   . VAL   B 1 49  ? 48.058 -25.167 -0.188  1.00 16.43 ?  49  VAL   B HB   1 
ATOM   4715 H HG11 . VAL   B 1 49  ? 47.746 -24.103 -2.353  1.00 16.61 ?  49  VAL   B HG11 1 
ATOM   4716 H HG12 . VAL   B 1 49  ? 48.589 -23.294 -1.278  1.00 16.61 ?  49  VAL   B HG12 1 
ATOM   4717 H HG13 . VAL   B 1 49  ? 49.332 -24.088 -2.439  1.00 16.61 ?  49  VAL   B HG13 1 
ATOM   4718 H HG21 . VAL   B 1 49  ? 47.174 -26.356 -1.986  1.00 17.99 ?  49  VAL   B HG21 1 
ATOM   4719 H HG22 . VAL   B 1 49  ? 48.644 -26.724 -2.465  1.00 17.99 ?  49  VAL   B HG22 1 
ATOM   4720 H HG23 . VAL   B 1 49  ? 48.086 -27.304 -1.095  1.00 17.99 ?  49  VAL   B HG23 1 
ATOM   4721 N N    . ALA   B 1 50  ? 50.383 -23.846 1.232   1.00 11.42 ?  50  ALA   B N    1 
ATOM   4722 C CA   . ALA   B 1 50  ? 50.899 -22.569 1.712   1.00 11.37 ?  50  ALA   B CA   1 
ATOM   4723 C C    . ALA   B 1 50  ? 52.418 -22.595 1.819   1.00 11.83 ?  50  ALA   B C    1 
ATOM   4724 O O    . ALA   B 1 50  ? 53.097 -21.628 1.446   1.00 11.70 ?  50  ALA   B O    1 
ATOM   4725 C CB   . ALA   B 1 50  ? 50.274 -22.215 3.058   1.00 11.70 ?  50  ALA   B CB   1 
ATOM   4726 H H    . ALA   B 1 50  ? 49.861 -24.256 1.783   1.00 13.73 ?  50  ALA   B H    1 
ATOM   4727 H HA   . ALA   B 1 50  ? 50.661 -21.875 1.083   1.00 13.67 ?  50  ALA   B HA   1 
ATOM   4728 H HB1  . ALA   B 1 50  ? 50.632 -21.364 3.360   1.00 14.06 ?  50  ALA   B HB1  1 
ATOM   4729 H HB2  . ALA   B 1 50  ? 49.312 -22.149 2.954   1.00 14.06 ?  50  ALA   B HB2  1 
ATOM   4730 H HB3  . ALA   B 1 50  ? 50.490 -22.909 3.702   1.00 14.06 ?  50  ALA   B HB3  1 
ATOM   4731 N N    . GLY   B 1 51  ? 52.969 -23.688 2.335   1.00 12.30 ?  51  GLY   B N    1 
ATOM   4732 C CA   . GLY   B 1 51  ? 54.413 -23.792 2.409   1.00 12.96 ?  51  GLY   B CA   1 
ATOM   4733 C C    . GLY   B 1 51  ? 55.065 -23.744 1.042   1.00 12.83 ?  51  GLY   B C    1 
ATOM   4734 O O    . GLY   B 1 51  ? 56.105 -23.106 0.860   1.00 13.58 ?  51  GLY   B O    1 
ATOM   4735 H H    . GLY   B 1 51  ? 52.540 -24.370 2.637   1.00 14.78 ?  51  GLY   B H    1 
ATOM   4736 H HA2  . GLY   B 1 51  ? 54.763 -23.060 2.942   1.00 15.57 ?  51  GLY   B HA2  1 
ATOM   4737 H HA3  . GLY   B 1 51  ? 54.658 -24.628 2.837   1.00 15.57 ?  51  GLY   B HA3  1 
ATOM   4738 N N    . ALA   B 1 52  ? 54.457 -24.405 0.057   1.00 12.56 ?  52  ALA   B N    1 
ATOM   4739 C CA   . ALA   B 1 52  ? 55.020 -24.409 -1.287  1.00 12.83 ?  52  ALA   B CA   1 
ATOM   4740 C C    . ALA   B 1 52  ? 54.937 -23.035 -1.942  1.00 12.38 ?  52  ALA   B C    1 
ATOM   4741 O O    . ALA   B 1 52  ? 55.909 -22.585 -2.572  1.00 13.11 ?  52  ALA   B O    1 
ATOM   4742 C CB   . ALA   B 1 52  ? 54.327 -25.459 -2.147  1.00 13.56 ?  52  ALA   B CB   1 
ATOM   4743 H H    . ALA   B 1 52  ? 53.717 -24.838 0.140   1.00 15.09 ?  52  ALA   B H    1 
ATOM   4744 H HA   . ALA   B 1 52  ? 55.954 -24.646 -1.223  1.00 15.41 ?  52  ALA   B HA   1 
ATOM   4745 H HB1  . ALA   B 1 52  ? 54.724 -25.447 -3.034  1.00 16.29 ?  52  ALA   B HB1  1 
ATOM   4746 H HB2  . ALA   B 1 52  ? 54.460 -26.332 -1.741  1.00 16.29 ?  52  ALA   B HB2  1 
ATOM   4747 H HB3  . ALA   B 1 52  ? 53.384 -25.258 -2.201  1.00 16.29 ?  52  ALA   B HB3  1 
ATOM   4748 N N    . LEU   B 1 53  ? 53.792 -22.355 -1.825  1.00 11.85 ?  53  LEU   B N    1 
ATOM   4749 C CA   . LEU   B 1 53  ? 53.682 -21.017 -2.398  1.00 12.03 ?  53  LEU   B CA   1 
ATOM   4750 C C    . LEU   B 1 53  ? 54.689 -20.074 -1.751  1.00 11.79 ?  53  LEU   B C    1 
ATOM   4751 O O    . LEU   B 1 53  ? 55.394 -19.330 -2.440  1.00 12.63 ?  53  LEU   B O    1 
ATOM   4752 C CB   . LEU   B 1 53  ? 52.262 -20.473 -2.228  1.00 12.57 ?  53  LEU   B CB   1 
ATOM   4753 C CG   . LEU   B 1 53  ? 51.125 -21.203 -2.949  1.00 12.67 ?  53  LEU   B CG   1 
ATOM   4754 C CD1  . LEU   B 1 53  ? 49.785 -20.598 -2.582  1.00 14.17 ?  53  LEU   B CD1  1 
ATOM   4755 C CD2  . LEU   B 1 53  ? 51.313 -21.189 -4.455  1.00 14.43 ?  53  LEU   B CD2  1 
ATOM   4756 H H    . LEU   B 1 53  ? 53.087 -22.635 -1.427  1.00 14.24 ?  53  LEU   B H    1 
ATOM   4757 H HA   . LEU   B 1 53  ? 53.882 -21.063 -3.352  1.00 14.45 ?  53  LEU   B HA   1 
ATOM   4758 H HB2  . LEU   B 1 53  ? 52.054 -20.487 -1.285  1.00 15.10 ?  53  LEU   B HB2  1 
ATOM   4759 H HB3  . LEU   B 1 53  ? 52.256 -19.558 -2.547  1.00 15.10 ?  53  LEU   B HB3  1 
ATOM   4760 H HG   . LEU   B 1 53  ? 51.113 -22.128 -2.662  1.00 15.22 ?  53  LEU   B HG   1 
ATOM   4761 H HD11 . LEU   B 1 53  ? 49.079 -21.081 -3.046  1.00 17.02 ?  53  LEU   B HD11 1 
ATOM   4762 H HD12 . LEU   B 1 53  ? 49.654 -20.677 -1.621  1.00 17.02 ?  53  LEU   B HD12 1 
ATOM   4763 H HD13 . LEU   B 1 53  ? 49.773 -19.666 -2.842  1.00 17.02 ?  53  LEU   B HD13 1 
ATOM   4764 H HD21 . LEU   B 1 53  ? 50.597 -21.704 -4.867  1.00 17.34 ?  53  LEU   B HD21 1 
ATOM   4765 H HD22 . LEU   B 1 53  ? 51.277 -20.274 -4.771  1.00 17.34 ?  53  LEU   B HD22 1 
ATOM   4766 H HD23 . LEU   B 1 53  ? 52.168 -21.586 -4.673  1.00 17.34 ?  53  LEU   B HD23 1 
ATOM   4767 N N    . ASN   B 1 54  ? 54.781 -20.102 -0.425  1.00 11.44 ?  54  ASN   B N    1 
ATOM   4768 C CA   . ASN   B 1 54  ? 55.695 -19.190 0.249   1.00 12.31 ?  54  ASN   B CA   1 
ATOM   4769 C C    . ASN   B 1 54  ? 57.140 -19.470 -0.145  1.00 12.88 ?  54  ASN   B C    1 
ATOM   4770 O O    . ASN   B 1 54  ? 57.919 -18.536 -0.376  1.00 13.30 ?  54  ASN   B O    1 
ATOM   4771 C CB   . ASN   B 1 54  ? 55.534 -19.277 1.761   1.00 13.08 ?  54  ASN   B CB   1 
ATOM   4772 C CG   . ASN   B 1 54  ? 56.509 -18.364 2.482   1.00 13.21 ?  54  ASN   B CG   1 
ATOM   4773 O OD1  . ASN   B 1 54  ? 56.534 -17.154 2.236   1.00 13.23 ?  54  ASN   B OD1  1 
ATOM   4774 N ND2  . ASN   B 1 54  ? 57.344 -18.939 3.346   1.00 14.70 ?  54  ASN   B ND2  1 
ATOM   4775 H H    . ASN   B 1 54  ? 54.337 -20.624 0.090   1.00 13.74 ?  54  ASN   B H    1 
ATOM   4776 H HA   . ASN   B 1 54  ? 55.486 -18.282 -0.020  1.00 14.80 ?  54  ASN   B HA   1 
ATOM   4777 H HB2  . ASN   B 1 54  ? 54.631 -19.007 2.002   1.00 15.72 ?  54  ASN   B HB2  1 
ATOM   4778 H HB3  . ASN   B 1 54  ? 55.696 -20.188 2.050   1.00 15.72 ?  54  ASN   B HB3  1 
ATOM   4779 H HD21 . ASN   B 1 54  ? 57.915 -18.462 3.777   1.00 17.67 ?  54  ASN   B HD21 1 
ATOM   4780 H HD22 . ASN   B 1 54  ? 57.303 -19.789 3.486   1.00 17.67 ?  54  ASN   B HD22 1 
ATOM   4781 N N    . LYS   B 1 55  ? 57.523 -20.747 -0.204  1.00 13.35 ?  55  LYS   B N    1 
ATOM   4782 C CA   . LYS   B 1 55  ? 58.877 -21.094 -0.620  1.00 14.22 ?  55  LYS   B CA   1 
ATOM   4783 C C    . LYS   B 1 55  ? 59.177 -20.556 -2.014  1.00 13.91 ?  55  LYS   B C    1 
ATOM   4784 O O    . LYS   B 1 55  ? 60.277 -20.052 -2.270  1.00 14.74 ?  55  LYS   B O    1 
ATOM   4785 C CB   . LYS   B 1 55  ? 59.066 -22.611 -0.566  1.00 16.03 ?  55  LYS   B CB   1 
ATOM   4786 C CG   . LYS   B 1 55  ? 60.442 -23.077 -1.003  1.00 19.80 ?  55  LYS   B CG   1 
ATOM   4787 C CD   . LYS   B 1 55  ? 60.619 -24.575 -0.820  1.00 23.10 ?  55  LYS   B CD   1 
ATOM   4788 C CE   . LYS   B 1 55  ? 60.652 -24.969 0.653   1.00 25.99 ?  55  LYS   B CE   1 
ATOM   4789 N NZ   . LYS   B 1 55  ? 61.059 -26.383 0.847   1.00 27.32 ?  55  LYS   B NZ   1 
ATOM   4790 H H    . LYS   B 1 55  ? 57.018 -21.421 -0.011  1.00 16.04 ?  55  LYS   B H    1 
ATOM   4791 H HA   . LYS   B 1 55  ? 59.506 -20.695 -0.003  1.00 17.09 ?  55  LYS   B HA   1 
ATOM   4792 H HB2  . LYS   B 1 55  ? 58.926 -22.905 0.351   1.00 19.25 ?  55  LYS   B HB2  1 
ATOM   4793 H HB3  . LYS   B 1 55  ? 58.411 -23.031 -1.145  1.00 19.25 ?  55  LYS   B HB3  1 
ATOM   4794 H HG2  . LYS   B 1 55  ? 60.563 -22.873 -1.942  1.00 23.78 ?  55  LYS   B HG2  1 
ATOM   4795 H HG3  . LYS   B 1 55  ? 61.114 -22.625 -0.471  1.00 23.78 ?  55  LYS   B HG3  1 
ATOM   4796 H HD2  . LYS   B 1 55  ? 59.879 -25.042 -1.240  1.00 27.74 ?  55  LYS   B HD2  1 
ATOM   4797 H HD3  . LYS   B 1 55  ? 61.459 -24.851 -1.222  1.00 27.74 ?  55  LYS   B HD3  1 
ATOM   4798 H HE2  . LYS   B 1 55  ? 61.287 -24.397 1.117   1.00 31.21 ?  55  LYS   B HE2  1 
ATOM   4799 H HE3  . LYS   B 1 55  ? 59.764 -24.850 1.031   1.00 31.21 ?  55  LYS   B HE3  1 
ATOM   4800 H HZ1  . LYS   B 1 55  ? 61.036 -26.587 1.713   1.00 32.81 ?  55  LYS   B HZ1  1 
ATOM   4801 H HZ2  . LYS   B 1 55  ? 60.501 -26.919 0.408   1.00 32.81 ?  55  LYS   B HZ2  1 
ATOM   4802 H HZ3  . LYS   B 1 55  ? 61.883 -26.505 0.539   1.00 32.81 ?  55  LYS   B HZ3  1 
ATOM   4803 N N    . ALA   B 1 56  ? 58.205 -20.640 -2.928  1.00 13.63 ?  56  ALA   B N    1 
ATOM   4804 C CA   . ALA   B 1 56  ? 58.427 -20.138 -4.278  1.00 14.39 ?  56  ALA   B CA   1 
ATOM   4805 C C    . ALA   B 1 56  ? 58.704 -18.642 -4.277  1.00 13.96 ?  56  ALA   B C    1 
ATOM   4806 O O    . ALA   B 1 56  ? 59.436 -18.145 -5.146  1.00 15.20 ?  56  ALA   B O    1 
ATOM   4807 C CB   . ALA   B 1 56  ? 57.229 -20.470 -5.168  1.00 15.34 ?  56  ALA   B CB   1 
ATOM   4808 H H    . ALA   B 1 56  ? 57.418 -20.971 -2.790  1.00 16.38 ?  56  ALA   B H    1 
ATOM   4809 H HA   . ALA   B 1 56  ? 59.203 -20.577 -4.648  1.00 17.29 ?  56  ALA   B HA   1 
ATOM   4810 H HB1  . ALA   B 1 56  ? 57.399 -20.132 -6.063  1.00 18.43 ?  56  ALA   B HB1  1 
ATOM   4811 H HB2  . ALA   B 1 56  ? 57.118 -21.434 -5.196  1.00 18.43 ?  56  ALA   B HB2  1 
ATOM   4812 H HB3  . ALA   B 1 56  ? 56.434 -20.055 -4.803  1.00 18.43 ?  56  ALA   B HB3  1 
ATOM   4813 N N    . THR   B 1 57  ? 58.140 -17.907 -3.314  1.00 13.70 ?  57  THR   B N    1 
ATOM   4814 C CA   . THR   B 1 57  ? 58.379 -16.473 -3.193  1.00 13.97 ?  57  THR   B CA   1 
ATOM   4815 C C    . THR   B 1 57  ? 59.625 -16.147 -2.378  1.00 14.46 ?  57  THR   B C    1 
ATOM   4816 O O    . THR   B 1 57  ? 59.862 -14.972 -2.072  1.00 14.86 ?  57  THR   B O    1 
ATOM   4817 C CB   . THR   B 1 57  ? 57.177 -15.743 -2.568  1.00 13.16 ?  57  THR   B CB   1 
ATOM   4818 O OG1  . THR   B 1 57  ? 57.152 -15.953 -1.149  1.00 13.66 ?  57  THR   B OG1  1 
ATOM   4819 C CG2  . THR   B 1 57  ? 55.867 -16.175 -3.205  1.00 13.03 ?  57  THR   B CG2  1 
ATOM   4820 H H    . THR   B 1 57  ? 57.600 -18.219 -2.716  1.00 16.47 ?  57  THR   B H    1 
ATOM   4821 H HA   . THR   B 1 57  ? 58.505 -16.110 -4.083  1.00 16.78 ?  57  THR   B HA   1 
ATOM   4822 H HB   . THR   B 1 57  ? 57.279 -14.792 -2.738  1.00 15.81 ?  57  THR   B HB   1 
ATOM   4823 H HG1  . THR   B 1 57  ? 57.076 -16.773 -0.984  1.00 16.41 ?  57  THR   B HG1  1 
ATOM   4824 H HG21 . THR   B 1 57  ? 55.149 -15.596 -2.917  1.00 15.66 ?  57  THR   B HG21 1 
ATOM   4825 H HG22 . THR   B 1 57  ? 55.939 -16.135 -4.173  1.00 15.66 ?  57  THR   B HG22 1 
ATOM   4826 H HG23 . THR   B 1 57  ? 55.660 -17.088 -2.948  1.00 15.66 ?  57  THR   B HG23 1 
ATOM   4827 N N    . ASN   B 1 58  ? 60.419 -17.150 -2.016  1.00 15.44 ?  58  ASN   B N    1 
ATOM   4828 C CA   . ASN   B 1 58  ? 61.618 -16.933 -1.214  1.00 18.58 ?  58  ASN   B CA   1 
ATOM   4829 C C    . ASN   B 1 58  ? 61.283 -16.218 0.095   1.00 16.10 ?  58  ASN   B C    1 
ATOM   4830 O O    . ASN   B 1 58  ? 62.023 -15.343 0.556   1.00 16.59 ?  58  ASN   B O    1 
ATOM   4831 C CB   . ASN   B 1 58  ? 62.700 -16.187 -2.002  1.00 26.42 ?  58  ASN   B CB   1 
ATOM   4832 C CG   . ASN   B 1 58  ? 64.072 -16.314 -1.370  1.00 34.65 ?  58  ASN   B CG   1 
ATOM   4833 O OD1  . ASN   B 1 58  ? 64.381 -17.315 -0.724  1.00 37.35 ?  58  ASN   B OD1  1 
ATOM   4834 N ND2  . ASN   B 1 58  ? 64.904 -15.295 -1.551  1.00 39.34 ?  58  ASN   B ND2  1 
ATOM   4835 H H    . ASN   B 1 58  ? 60.280 -17.977 -2.221  1.00 18.55 ?  58  ASN   B H    1 
ATOM   4836 H HA   . ASN   B 1 58  ? 61.984 -17.804 -0.988  1.00 22.32 ?  58  ASN   B HA   1 
ATOM   4837 H HB2  . ASN   B 1 58  ? 62.746 -16.552 -2.902  1.00 31.72 ?  58  ASN   B HB2  1 
ATOM   4838 H HB3  . ASN   B 1 58  ? 62.473 -15.246 -2.038  1.00 31.72 ?  58  ASN   B HB3  1 
ATOM   4839 H HD21 . ASN   B 1 58  ? 65.694 -15.321 -1.213  1.00 47.23 ?  58  ASN   B HD21 1 
ATOM   4840 H HD22 . ASN   B 1 58  ? 64.652 -14.611 -2.006  1.00 47.23 ?  58  ASN   B HD22 1 
ATOM   4841 N N    . ASN   B 1 59  ? 60.159 -16.604 0.704   1.00 15.29 ?  59  ASN   B N    1 
ATOM   4842 C CA   . ASN   B 1 59  ? 59.680 -16.131 2.004   1.00 14.98 ?  59  ASN   B CA   1 
ATOM   4843 C C    . ASN   B 1 59  ? 59.083 -14.726 1.950   1.00 14.34 ?  59  ASN   B C    1 
ATOM   4844 O O    . ASN   B 1 59  ? 58.649 -14.223 2.995   1.00 14.38 ?  59  ASN   B O    1 
ATOM   4845 C CB   . ASN   B 1 59  ? 60.753 -16.184 3.106   1.00 15.90 ?  59  ASN   B CB   1 
ATOM   4846 C CG   . ASN   B 1 59  ? 60.168 -16.365 4.488   1.00 17.12 ?  59  ASN   B CG   1 
ATOM   4847 O OD1  . ASN   B 1 59  ? 59.343 -17.255 4.712   1.00 17.32 ?  59  ASN   B OD1  1 
ATOM   4848 N ND2  . ASN   B 1 59  ? 60.590 -15.525 5.426   1.00 17.89 ?  59  ASN   B ND2  1 
ATOM   4849 H H    . ASN   B 1 59  ? 59.623 -17.186 0.361   1.00 18.36 ?  59  ASN   B H    1 
ATOM   4850 H HA   . ASN   B 1 59  ? 58.972 -16.727 2.288   1.00 18.00 ?  59  ASN   B HA   1 
ATOM   4851 H HB2  . ASN   B 1 59  ? 61.347 -16.933 2.943   1.00 19.10 ?  59  ASN   B HB2  1 
ATOM   4852 H HB3  . ASN   B 1 59  ? 61.255 -15.356 3.108   1.00 19.10 ?  59  ASN   B HB3  1 
ATOM   4853 H HD21 . ASN   B 1 59  ? 60.285 -15.586 6.231   1.00 21.49 ?  59  ASN   B HD21 1 
ATOM   4854 H HD22 . ASN   B 1 59  ? 61.166 -14.918 5.233   1.00 21.49 ?  59  ASN   B HD22 1 
ATOM   4855 N N    . ALA   B 1 60  ? 59.027 -14.081 0.781   1.00 14.23 ?  60  ALA   B N    1 
ATOM   4856 C CA   . ALA   B 1 60  ? 58.430 -12.750 0.706   1.00 14.14 ?  60  ALA   B CA   1 
ATOM   4857 C C    . ALA   B 1 60  ? 56.960 -12.777 1.100   1.00 13.12 ?  60  ALA   B C    1 
ATOM   4858 O O    . ALA   B 1 60  ? 56.452 -11.826 1.709   1.00 13.48 ?  60  ALA   B O    1 
ATOM   4859 C CB   . ALA   B 1 60  ? 58.591 -12.170 -0.699  1.00 15.21 ?  60  ALA   B CB   1 
ATOM   4860 H H    . ALA   B 1 60  ? 59.323 -14.390 0.035   1.00 17.09 ?  60  ALA   B H    1 
ATOM   4861 H HA   . ALA   B 1 60  ? 58.890 -12.166 1.327   1.00 16.99 ?  60  ALA   B HA   1 
ATOM   4862 H HB1  . ALA   B 1 60  ? 58.191 -11.290 -0.723  1.00 18.27 ?  60  ALA   B HB1  1 
ATOM   4863 H HB2  . ALA   B 1 60  ? 59.539 -12.110 -0.906  1.00 18.27 ?  60  ALA   B HB2  1 
ATOM   4864 H HB3  . ALA   B 1 60  ? 58.153 -12.756 -1.334  1.00 18.27 ?  60  ALA   B HB3  1 
ATOM   4865 N N    . MET   B 1 61  ? 56.254 -13.855 0.751   1.00 12.63 ?  61  MET   B N    1 
ATOM   4866 C CA   . MET   B 1 61  ? 54.857 -13.976 1.144   1.00 12.38 ?  61  MET   B CA   1 
ATOM   4867 C C    . MET   B 1 61  ? 54.717 -13.981 2.666   1.00 12.52 ?  61  MET   B C    1 
ATOM   4868 O O    . MET   B 1 61  ? 53.812 -13.338 3.216   1.00 12.20 ?  61  MET   B O    1 
ATOM   4869 C CB   . MET   B 1 61  ? 54.273 -15.244 0.515   1.00 12.46 ?  61  MET   B CB   1 
ATOM   4870 C CG   . MET   B 1 61  ? 52.843 -15.552 0.948   1.00 12.24 ?  61  MET   B CG   1 
ATOM   4871 S SD   . MET   B 1 61  ? 52.191 -17.040 0.168   1.00 12.59 ?  61  MET   B SD   1 
ATOM   4872 C CE   . MET   B 1 61  ? 51.931 -16.439 -1.496  1.00 14.16 ?  61  MET   B CE   1 
ATOM   4873 H H    . MET   B 1 61  ? 56.560 -14.525 0.294   1.00 15.17 ?  61  MET   B H    1 
ATOM   4874 H HA   . MET   B 1 61  ? 54.367 -13.224 0.783   1.00 14.88 ?  61  MET   B HA   1 
ATOM   4875 H HB2  . MET   B 1 61  ? 54.267 -15.140 -0.454  1.00 14.98 ?  61  MET   B HB2  1 
ATOM   4876 H HB3  . MET   B 1 61  ? 54.826 -16.002 0.756   1.00 14.98 ?  61  MET   B HB3  1 
ATOM   4877 H HG2  . MET   B 1 61  ? 52.826 -15.692 1.910   1.00 14.70 ?  61  MET   B HG2  1 
ATOM   4878 H HG3  . MET   B 1 61  ? 52.270 -14.807 0.712   1.00 14.70 ?  61  MET   B HG3  1 
ATOM   4879 H HE1  . MET   B 1 61  ? 51.527 -17.141 -2.025  1.00 17.02 ?  61  MET   B HE1  1 
ATOM   4880 H HE2  . MET   B 1 61  ? 51.338 -15.667 -1.463  1.00 17.02 ?  61  MET   B HE2  1 
ATOM   4881 H HE3  . MET   B 1 61  ? 52.783 -16.180 -1.877  1.00 17.02 ?  61  MET   B HE3  1 
ATOM   4882 N N    . GLN   B 1 62  ? 55.599 -14.698 3.367   1.00 12.47 ?  62  GLN   B N    1 
ATOM   4883 C CA   . GLN   B 1 62  ? 55.491 -14.762 4.822   1.00 12.84 ?  62  GLN   B CA   1 
ATOM   4884 C C    . GLN   B 1 62  ? 55.776 -13.411 5.464   1.00 13.15 ?  62  GLN   B C    1 
ATOM   4885 O O    . GLN   B 1 62  ? 55.084 -13.009 6.408   1.00 13.65 ?  62  GLN   B O    1 
ATOM   4886 C CB   . GLN   B 1 62  ? 56.431 -15.827 5.387   1.00 12.95 ?  62  GLN   B CB   1 
ATOM   4887 C CG   . GLN   B 1 62  ? 56.211 -16.079 6.869   1.00 13.23 ?  62  GLN   B CG   1 
ATOM   4888 C CD   . GLN   B 1 62  ? 54.838 -16.677 7.117   1.00 13.01 ?  62  GLN   B CD   1 
ATOM   4889 O OE1  . GLN   B 1 62  ? 54.590 -17.836 6.771   1.00 13.35 ?  62  GLN   B OE1  1 
ATOM   4890 N NE2  . GLN   B 1 62  ? 53.922 -15.887 7.674   1.00 13.40 ?  62  GLN   B NE2  1 
ATOM   4891 H H    . GLN   B 1 62  ? 56.250 -15.151 3.026   1.00 14.99 ?  62  GLN   B H    1 
ATOM   4892 H HA   . GLN   B 1 62  ? 54.583 -15.016 5.050   1.00 15.43 ?  62  GLN   B HA   1 
ATOM   4893 H HB2  . GLN   B 1 62  ? 56.286 -16.665 4.918   1.00 15.56 ?  62  GLN   B HB2  1 
ATOM   4894 H HB3  . GLN   B 1 62  ? 57.349 -15.536 5.267   1.00 15.56 ?  62  GLN   B HB3  1 
ATOM   4895 H HG2  . GLN   B 1 62  ? 56.878 -16.704 7.191   1.00 15.89 ?  62  GLN   B HG2  1 
ATOM   4896 H HG3  . GLN   B 1 62  ? 56.273 -15.241 7.355   1.00 15.89 ?  62  GLN   B HG3  1 
ATOM   4897 H HE21 . GLN   B 1 62  ? 54.123 -15.079 7.889   1.00 16.09 ?  62  GLN   B HE21 1 
ATOM   4898 H HE22 . GLN   B 1 62  ? 53.129 -16.187 7.825   1.00 16.09 ?  62  GLN   B HE22 1 
ATOM   4899 N N    . VAL   B 1 63  ? 56.795 -12.698 4.978   1.00 13.62 ?  63  VAL   B N    1 
ATOM   4900 C CA   . VAL   B 1 63  ? 57.100 -11.381 5.532   1.00 14.55 ?  63  VAL   B CA   1 
ATOM   4901 C C    . VAL   B 1 63  ? 55.908 -10.446 5.351   1.00 13.84 ?  63  VAL   B C    1 
ATOM   4902 O O    . VAL   B 1 63  ? 55.494 -9.743  6.284   1.00 14.56 ?  63  VAL   B O    1 
ATOM   4903 C CB   . VAL   B 1 63  ? 58.391 -10.823 4.907   1.00 15.77 ?  63  VAL   B CB   1 
ATOM   4904 C CG1  . VAL   B 1 63  ? 58.624 -9.390  5.355   1.00 16.52 ?  63  VAL   B CG1  1 
ATOM   4905 C CG2  . VAL   B 1 63  ? 59.573 -11.699 5.296   1.00 16.36 ?  63  VAL   B CG2  1 
ATOM   4906 H H    . VAL   B 1 63  ? 57.311 -12.952 4.332   1.00 16.37 ?  63  VAL   B H    1 
ATOM   4907 H HA   . VAL   B 1 63  ? 57.258 -11.480 6.480   1.00 17.48 ?  63  VAL   B HA   1 
ATOM   4908 H HB   . VAL   B 1 63  ? 58.317 -10.834 3.939   1.00 18.95 ?  63  VAL   B HB   1 
ATOM   4909 H HG11 . VAL   B 1 63  ? 59.542 -9.148  5.161   1.00 19.84 ?  63  VAL   B HG11 1 
ATOM   4910 H HG12 . VAL   B 1 63  ? 58.017 -8.809  4.876   1.00 19.84 ?  63  VAL   B HG12 1 
ATOM   4911 H HG13 . VAL   B 1 63  ? 58.462 -9.334  6.309   1.00 19.84 ?  63  VAL   B HG13 1 
ATOM   4912 H HG21 . VAL   B 1 63  ? 60.386 -11.327 4.917   1.00 19.65 ?  63  VAL   B HG21 1 
ATOM   4913 H HG22 . VAL   B 1 63  ? 59.645 -11.720 6.266   1.00 19.65 ?  63  VAL   B HG22 1 
ATOM   4914 H HG23 . VAL   B 1 63  ? 59.433 -12.597 4.958   1.00 19.65 ?  63  VAL   B HG23 1 
ATOM   4915 N N    . GLU   B 1 64  ? 55.337 -10.433 4.145   1.00 13.19 ?  64  GLU   B N    1 
ATOM   4916 C CA   . GLU   B 1 64  ? 54.171 -9.595  3.873   1.00 13.04 ?  64  GLU   B CA   1 
ATOM   4917 C C    . GLU   B 1 64  ? 52.988 -9.999  4.747   1.00 12.60 ?  64  GLU   B C    1 
ATOM   4918 O O    . GLU   B 1 64  ? 52.241 -9.140  5.244   1.00 13.14 ?  64  GLU   B O    1 
ATOM   4919 C CB   . GLU   B 1 64  ? 53.807 -9.731  2.393   1.00 13.11 ?  64  GLU   B CB   1 
ATOM   4920 C CG   . GLU   B 1 64  ? 52.536 -9.003  1.962   1.00 13.53 ?  64  GLU   B CG   1 
ATOM   4921 C CD   . GLU   B 1 64  ? 52.002 -9.503  0.622   1.00 14.24 ?  64  GLU   B CD   1 
ATOM   4922 O OE1  . GLU   B 1 64  ? 52.184 -10.710 0.304   1.00 14.95 ?  64  GLU   B OE1  1 
ATOM   4923 O OE2  . GLU   B 1 64  ? 51.379 -8.692  -0.105  1.00 14.98 -1 64  GLU   B OE2  1 
ATOM   4924 H H    . GLU   B 1 64  ? 55.604 -10.899 3.470   1.00 15.84 ?  64  GLU   B H    1 
ATOM   4925 H HA   . GLU   B 1 64  ? 54.386 -8.668  4.058   1.00 15.67 ?  64  GLU   B HA   1 
ATOM   4926 H HB2  . GLU   B 1 64  ? 54.537 -9.365  1.863   1.00 15.75 ?  64  GLU   B HB2  1 
ATOM   4927 H HB3  . GLU   B 1 64  ? 53.693 -10.665 2.189   1.00 15.75 ?  64  GLU   B HB3  1 
ATOM   4928 H HG2  . GLU   B 1 64  ? 51.836 -9.137  2.625   1.00 16.26 ?  64  GLU   B HG2  1 
ATOM   4929 H HG3  . GLU   B 1 64  ? 52.723 -8.053  1.876   1.00 16.26 ?  64  GLU   B HG3  1 
ATOM   4930 N N    . SER   B 1 65  ? 52.804 -11.306 4.935   1.00 12.29 ?  65  SER   B N    1 
ATOM   4931 C CA   . SER   B 1 65  ? 51.694 -11.812 5.734   1.00 12.54 ?  65  SER   B CA   1 
ATOM   4932 C C    . SER   B 1 65  ? 51.823 -11.410 7.196   1.00 12.53 ?  65  SER   B C    1 
ATOM   4933 O O    . SER   B 1 65  ? 50.822 -11.042 7.830   1.00 12.96 ?  65  SER   B O    1 
ATOM   4934 C CB   . SER   B 1 65  ? 51.613 -13.332 5.607   1.00 12.62 ?  65  SER   B CB   1 
ATOM   4935 O OG   . SER   B 1 65  ? 51.263 -13.730 4.291   1.00 12.74 ?  65  SER   B OG   1 
ATOM   4936 H H    . SER   B 1 65  ? 53.311 -11.925 4.610   1.00 14.77 ?  65  SER   B H    1 
ATOM   4937 H HA   . SER   B 1 65  ? 50.863 -11.441 5.394   1.00 15.07 ?  65  SER   B HA   1 
ATOM   4938 H HB2  . SER   B 1 65  ? 52.472 -13.714 5.827   1.00 15.16 ?  65  SER   B HB2  1 
ATOM   4939 H HB3  . SER   B 1 65  ? 50.936 -13.662 6.222   1.00 15.16 ?  65  SER   B HB3  1 
ATOM   4940 H HG   . SER   B 1 65  ? 51.832 -13.447 3.737   1.00 15.31 ?  65  SER   B HG   1 
ATOM   4941 N N    . ASP   B 1 66  ? 53.030 -11.515 7.765   1.00 13.05 ?  66  ASP   B N    1 
ATOM   4942 C CA   . ASP   B 1 66  ? 53.220 -11.125 9.160   1.00 13.42 ?  66  ASP   B CA   1 
ATOM   4943 C C    . ASP   B 1 66  ? 52.908 -9.647  9.359   1.00 13.63 ?  66  ASP   B C    1 
ATOM   4944 O O    . ASP   B 1 66  ? 52.330 -9.256  10.380  1.00 13.84 ?  66  ASP   B O    1 
ATOM   4945 C CB   . ASP   B 1 66  ? 54.650 -11.435 9.614   1.00 14.50 ?  66  ASP   B CB   1 
ATOM   4946 C CG   . ASP   B 1 66  ? 54.917 -12.929 9.767   1.00 16.59 ?  66  ASP   B CG   1 
ATOM   4947 O OD1  . ASP   B 1 66  ? 53.966 -13.740 9.686   1.00 17.40 ?  66  ASP   B OD1  1 
ATOM   4948 O OD2  . ASP   B 1 66  ? 56.095 -13.297 9.978   1.00 19.01 -1 66  ASP   B OD2  1 
ATOM   4949 H H    . ASP   B 1 66  ? 53.734 -11.815 7.377   1.00 15.68 ?  66  ASP   B H    1 
ATOM   4950 H HA   . ASP   B 1 66  ? 52.614 -11.631 9.722   1.00 16.13 ?  66  ASP   B HA   1 
ATOM   4951 H HB2  . ASP   B 1 66  ? 55.272 -11.087 8.957   1.00 17.41 ?  66  ASP   B HB2  1 
ATOM   4952 H HB3  . ASP   B 1 66  ? 54.808 -11.007 10.475  1.00 17.41 ?  66  ASP   B HB3  1 
ATOM   4953 N N    . ASP   B 1 67  ? 53.286 -8.805  8.396   1.00 13.17 ?  67  ASP   B N    1 
ATOM   4954 C CA   . ASP   B 1 67  ? 52.941 -7.392  8.481   1.00 13.66 ?  67  ASP   B CA   1 
ATOM   4955 C C    . ASP   B 1 67  ? 51.431 -7.187  8.403   1.00 13.76 ?  67  ASP   B C    1 
ATOM   4956 O O    . ASP   B 1 67  ? 50.870 -6.384  9.157   1.00 14.46 ?  67  ASP   B O    1 
ATOM   4957 C CB   . ASP   B 1 67  ? 53.655 -6.616  7.380   1.00 15.12 ?  67  ASP   B CB   1 
ATOM   4958 C CG   . ASP   B 1 67  ? 53.225 -5.176  7.335   1.00 16.41 ?  67  ASP   B CG   1 
ATOM   4959 O OD1  . ASP   B 1 67  ? 53.721 -4.368  8.154   1.00 17.50 ?  67  ASP   B OD1  1 
ATOM   4960 O OD2  . ASP   B 1 67  ? 52.361 -4.868  6.495   1.00 17.53 -1 67  ASP   B OD2  1 
ATOM   4961 H H    . ASP   B 1 67  ? 53.742 -9.024  7.701   1.00 15.82 ?  67  ASP   B H    1 
ATOM   4962 H HA   . ASP   B 1 67  ? 53.243 -7.043  9.332   1.00 16.41 ?  67  ASP   B HA   1 
ATOM   4963 H HB2  . ASP   B 1 67  ? 54.612 -6.641  7.539   1.00 18.17 ?  67  ASP   B HB2  1 
ATOM   4964 H HB3  . ASP   B 1 67  ? 53.454 -7.024  6.518   1.00 18.17 ?  67  ASP   B HB3  1 
ATOM   4965 N N    . TYR   B 1 68  ? 50.752 -7.915  7.511   1.00 13.44 ?  68  TYR   B N    1 
ATOM   4966 C CA   . TYR   B 1 68  ? 49.295 -7.832  7.435   1.00 14.22 ?  68  TYR   B CA   1 
ATOM   4967 C C    . TYR   B 1 68  ? 48.658 -8.169  8.780   1.00 13.84 ?  68  TYR   B C    1 
ATOM   4968 O O    . TYR   B 1 68  ? 47.726 -7.490  9.229   1.00 14.57 ?  68  TYR   B O    1 
ATOM   4969 C CB   . TYR   B 1 68  ? 48.762 -8.762  6.338   1.00 15.01 ?  68  TYR   B CB   1 
ATOM   4970 C CG   . TYR   B 1 68  ? 47.256 -8.918  6.400   1.00 16.15 ?  68  TYR   B CG   1 
ATOM   4971 C CD1  . TYR   B 1 68  ? 46.671 -9.877  7.220   1.00 16.84 ?  68  TYR   B CD1  1 
ATOM   4972 C CD2  . TYR   B 1 68  ? 46.422 -8.081  5.678   1.00 17.18 ?  68  TYR   B CD2  1 
ATOM   4973 C CE1  . TYR   B 1 68  ? 45.300 -10.002 7.310   1.00 18.07 ?  68  TYR   B CE1  1 
ATOM   4974 C CE2  . TYR   B 1 68  ? 45.038 -8.211  5.754   1.00 17.79 ?  68  TYR   B CE2  1 
ATOM   4975 C CZ   . TYR   B 1 68  ? 44.496 -9.166  6.575   1.00 18.16 ?  68  TYR   B CZ   1 
ATOM   4976 O OH   . TYR   B 1 68  ? 43.129 -9.285  6.664   1.00 19.19 ?  68  TYR   B OH   1 
ATOM   4977 H H    . TYR   B 1 68  ? 51.109 -8.465  6.945   1.00 16.14 ?  68  TYR   B H    1 
ATOM   4978 H HA   . TYR   B 1 68  ? 49.048 -6.925  7.205   1.00 17.08 ?  68  TYR   B HA   1 
ATOM   4979 H HB2  . TYR   B 1 68  ? 48.986 -8.393  5.471   1.00 18.03 ?  68  TYR   B HB2  1 
ATOM   4980 H HB3  . TYR   B 1 68  ? 49.159 -9.640  6.442   1.00 18.03 ?  68  TYR   B HB3  1 
ATOM   4981 H HD1  . TYR   B 1 68  ? 47.212 -10.449 7.720   1.00 20.23 ?  68  TYR   B HD1  1 
ATOM   4982 H HD2  . TYR   B 1 68  ? 46.790 -7.427  5.134   1.00 20.64 ?  68  TYR   B HD2  1 
ATOM   4983 H HE1  . TYR   B 1 68  ? 44.920 -10.661 7.853   1.00 21.70 ?  68  TYR   B HE1  1 
ATOM   4984 H HE2  . TYR   B 1 68  ? 44.484 -7.643  5.269   1.00 21.37 ?  68  TYR   B HE2  1 
ATOM   4985 H HH   . TYR   B 1 68  ? 42.746 -8.723  6.162   1.00 23.05 ?  68  TYR   B HH   1 
ATOM   4986 N N    . ILE   B 1 69  ? 49.132 -9.242  9.423   1.00 13.68 ?  69  ILE   B N    1 
ATOM   4987 C CA   . ILE   B 1 69  ? 48.577 -9.672  10.704  1.00 14.37 ?  69  ILE   B CA   1 
ATOM   4988 C C    . ILE   B 1 69  ? 48.837 -8.633  11.787  1.00 14.10 ?  69  ILE   B C    1 
ATOM   4989 O O    . ILE   B 1 69  ? 47.968 -8.357  12.622  1.00 14.26 ?  69  ILE   B O    1 
ATOM   4990 C CB   . ILE   B 1 69  ? 49.151 -11.049 11.088  1.00 15.05 ?  69  ILE   B CB   1 
ATOM   4991 C CG1  . ILE   B 1 69  ? 48.620 -12.145 10.154  1.00 15.24 ?  69  ILE   B CG1  1 
ATOM   4992 C CG2  . ILE   B 1 69  ? 48.868 -11.363 12.552  1.00 16.05 ?  69  ILE   B CG2  1 
ATOM   4993 C CD1  . ILE   B 1 69  ? 47.156 -12.482 10.342  1.00 15.31 ?  69  ILE   B CD1  1 
ATOM   4994 H H    . ILE   B 1 69  ? 49.776 -9.732  9.142   1.00 16.44 ?  69  ILE   B H    1 
ATOM   4995 H HA   . ILE   B 1 69  ? 47.616 -9.764  10.610  1.00 17.26 ?  69  ILE   B HA   1 
ATOM   4996 H HB   . ILE   B 1 69  ? 50.114 -11.004 10.978  1.00 18.09 ?  69  ILE   B HB   1 
ATOM   4997 H HG12 . ILE   B 1 69  ? 48.741 -11.850 9.236   1.00 18.31 ?  69  ILE   B HG12 1 
ATOM   4998 H HG13 . ILE   B 1 69  ? 49.135 -12.952 10.307  1.00 18.31 ?  69  ILE   B HG13 1 
ATOM   4999 H HG21 . ILE   B 1 69  ? 48.996 -12.312 12.697  1.00 19.28 ?  69  ILE   B HG21 1 
ATOM   5000 H HG22 . ILE   B 1 69  ? 49.483 -10.861 13.112  1.00 19.28 ?  69  ILE   B HG22 1 
ATOM   5001 H HG23 . ILE   B 1 69  ? 47.953 -11.117 12.759  1.00 19.28 ?  69  ILE   B HG23 1 
ATOM   5002 H HD11 . ILE   B 1 69  ? 46.914 -13.162 9.696   1.00 18.39 ?  69  ILE   B HD11 1 
ATOM   5003 H HD12 . ILE   B 1 69  ? 47.026 -12.818 11.241  1.00 18.39 ?  69  ILE   B HD12 1 
ATOM   5004 H HD13 . ILE   B 1 69  ? 46.628 -11.685 10.201  1.00 18.39 ?  69  ILE   B HD13 1 
ATOM   5005 N N    . ALA   B 1 70  ? 50.034 -8.050  11.807  1.00 14.09 ?  70  ALA   B N    1 
ATOM   5006 C CA   . ALA   B 1 70  ? 50.316 -7.014  12.793  1.00 13.78 ?  70  ALA   B CA   1 
ATOM   5007 C C    . ALA   B 1 70  ? 49.318 -5.868  12.684  1.00 13.99 ?  70  ALA   B C    1 
ATOM   5008 O O    . ALA   B 1 70  ? 48.871 -5.326  13.700  1.00 14.32 ?  70  ALA   B O    1 
ATOM   5009 C CB   . ALA   B 1 70  ? 51.747 -6.510  12.617  1.00 14.43 ?  70  ALA   B CB   1 
ATOM   5010 H H    . ALA   B 1 70  ? 50.676 -8.234  11.275  1.00 16.93 ?  70  ALA   B H    1 
ATOM   5011 H HA   . ALA   B 1 70  ? 50.242 -7.393  13.681  1.00 16.56 ?  70  ALA   B HA   1 
ATOM   5012 H HB1  . ALA   B 1 70  ? 51.939 -5.851  13.302  1.00 17.33 ?  70  ALA   B HB1  1 
ATOM   5013 H HB2  . ALA   B 1 70  ? 52.360 -7.261  12.704  1.00 17.33 ?  70  ALA   B HB2  1 
ATOM   5014 H HB3  . ALA   B 1 70  ? 51.841 -6.112  11.737  1.00 17.33 ?  70  ALA   B HB3  1 
ATOM   5015 N N    . THR   B 1 71  ? 48.939 -5.502  11.460  1.00 14.46 ?  71  THR   B N    1 
ATOM   5016 C CA   . THR   B 1 71  ? 48.048 -4.365  11.253  1.00 15.49 ?  71  THR   B CA   1 
ATOM   5017 C C    . THR   B 1 71  ? 46.582 -4.733  11.454  1.00 15.98 ?  71  THR   B C    1 
ATOM   5018 O O    . THR   B 1 71  ? 45.802 -3.918  11.963  1.00 17.38 ?  71  THR   B O    1 
ATOM   5019 C CB   . THR   B 1 71  ? 48.268 -3.790  9.851   1.00 17.36 ?  71  THR   B CB   1 
ATOM   5020 O OG1  . THR   B 1 71  ? 49.591 -3.251  9.758   1.00 19.36 ?  71  THR   B OG1  1 
ATOM   5021 C CG2  . THR   B 1 71  ? 47.250 -2.697  9.534   1.00 18.36 ?  71  THR   B CG2  1 
ATOM   5022 H H    . THR   B 1 71  ? 49.185 -5.895  10.737  1.00 17.38 ?  71  THR   B H    1 
ATOM   5023 H HA   . THR   B 1 71  ? 48.269 -3.671  11.893  1.00 18.60 ?  71  THR   B HA   1 
ATOM   5024 H HB   . THR   B 1 71  ? 48.170 -4.497  9.193   1.00 20.85 ?  71  THR   B HB   1 
ATOM   5025 H HG1  . THR   B 1 71  ? 49.721 -2.926  8.991   1.00 23.25 ?  71  THR   B HG1  1 
ATOM   5026 H HG21 . THR   B 1 71  ? 47.554 -2.172  8.776   1.00 22.05 ?  71  THR   B HG21 1 
ATOM   5027 H HG22 . THR   B 1 71  ? 46.392 -3.091  9.319   1.00 22.05 ?  71  THR   B HG22 1 
ATOM   5028 H HG23 . THR   B 1 71  ? 47.148 -2.109  10.299  1.00 22.05 ?  71  THR   B HG23 1 
ATOM   5029 N N    . ASN   B 1 72  ? 46.188 -5.945  11.059  1.00 15.69 ?  72  ASN   B N    1 
ATOM   5030 C CA   . ASN   B 1 72  ? 44.782 -6.305  10.934  1.00 15.94 ?  72  ASN   B CA   1 
ATOM   5031 C C    . ASN   B 1 72  ? 44.313 -7.401  11.881  1.00 16.53 ?  72  ASN   B C    1 
ATOM   5032 O O    . ASN   B 1 72  ? 43.099 -7.558  12.055  1.00 17.62 ?  72  ASN   B O    1 
ATOM   5033 C CB   . ASN   B 1 72  ? 44.474 -6.731  9.488   1.00 16.82 ?  72  ASN   B CB   1 
ATOM   5034 C CG   . ASN   B 1 72  ? 44.752 -5.628  8.490   1.00 17.94 ?  72  ASN   B CG   1 
ATOM   5035 O OD1  . ASN   B 1 72  ? 45.770 -5.642  7.791   1.00 18.86 ?  72  ASN   B OD1  1 
ATOM   5036 N ND2  . ASN   B 1 72  ? 43.870 -4.648  8.440   1.00 19.36 ?  72  ASN   B ND2  1 
ATOM   5037 H H    . ASN   B 1 72  ? 46.726 -6.587  10.848  1.00 18.85 ?  72  ASN   B H    1 
ATOM   5038 H HA   . ASN   B 1 72  ? 44.251 -5.517  11.115  1.00 19.15 ?  72  ASN   B HA   1 
ATOM   5039 H HB2  . ASN   B 1 72  ? 45.032 -7.492  9.252   1.00 20.20 ?  72  ASN   B HB2  1 
ATOM   5040 H HB3  . ASN   B 1 72  ? 43.539 -6.970  9.416   1.00 20.20 ?  72  ASN   B HB3  1 
ATOM   5041 H HD21 . ASN   B 1 72  ? 43.979 -3.994  7.890   1.00 23.25 ?  72  ASN   B HD21 1 
ATOM   5042 H HD22 . ASN   B 1 72  ? 43.171 -4.671  8.943   1.00 23.25 ?  72  ASN   B HD22 1 
ATOM   5043 N N    . GLY   B 1 73  ? 45.217 -8.151  12.503  1.00 15.97 ?  73  GLY   B N    1 
ATOM   5044 C CA   . GLY   B 1 73  ? 44.820 -9.287  13.298  1.00 15.38 ?  73  GLY   B CA   1 
ATOM   5045 C C    . GLY   B 1 73  ? 44.453 -10.468 12.427  1.00 14.40 ?  73  GLY   B C    1 
ATOM   5046 O O    . GLY   B 1 73  ? 44.439 -10.380 11.197  1.00 14.22 ?  73  GLY   B O    1 
ATOM   5047 H H    . GLY   B 1 73  ? 46.068 -8.020  12.473  1.00 19.19 ?  73  GLY   B H    1 
ATOM   5048 H HA2  . GLY   B 1 73  ? 45.547 -9.544  13.884  1.00 18.48 ?  73  GLY   B HA2  1 
ATOM   5049 H HA3  . GLY   B 1 73  ? 44.051 -9.050  13.842  1.00 18.48 ?  73  GLY   B HA3  1 
ATOM   5050 N N    . PRO   B 1 74  ? 44.143 -11.596 13.062  1.00 14.63 ?  74  PRO   B N    1 
ATOM   5051 C CA   . PRO   B 1 74  ? 43.894 -12.828 12.313  1.00 14.12 ?  74  PRO   B CA   1 
ATOM   5052 C C    . PRO   B 1 74  ? 42.595 -12.772 11.521  1.00 13.53 ?  74  PRO   B C    1 
ATOM   5053 O O    . PRO   B 1 74  ? 41.653 -12.038 11.840  1.00 14.63 ?  74  PRO   B O    1 
ATOM   5054 C CB   . PRO   B 1 74  ? 43.815 -13.893 13.412  1.00 15.04 ?  74  PRO   B CB   1 
ATOM   5055 C CG   . PRO   B 1 74  ? 43.375 -13.141 14.629  1.00 16.55 ?  74  PRO   B CG   1 
ATOM   5056 C CD   . PRO   B 1 74  ? 44.030 -11.796 14.517  1.00 16.27 ?  74  PRO   B CD   1 
ATOM   5057 H HA   . PRO   B 1 74  ? 44.638 -13.023 11.718  1.00 16.97 ?  74  PRO   B HA   1 
ATOM   5058 H HB2  . PRO   B 1 74  ? 43.162 -14.567 13.167  1.00 18.06 ?  74  PRO   B HB2  1 
ATOM   5059 H HB3  . PRO   B 1 74  ? 44.689 -14.290 13.547  1.00 18.06 ?  74  PRO   B HB3  1 
ATOM   5060 H HG2  . PRO   B 1 74  ? 42.409 -13.054 14.626  1.00 19.88 ?  74  PRO   B HG2  1 
ATOM   5061 H HG3  . PRO   B 1 74  ? 43.677 -13.605 15.424  1.00 19.88 ?  74  PRO   B HG3  1 
ATOM   5062 H HD2  . PRO   B 1 74  ? 43.464 -11.113 14.915  1.00 19.55 ?  74  PRO   B HD2  1 
ATOM   5063 H HD3  . PRO   B 1 74  ? 44.908 -11.811 14.925  1.00 19.55 ?  74  PRO   B HD3  1 
ATOM   5064 N N    . LEU   B 1 75  ? 42.566 -13.582 10.465  1.00 12.69 ?  75  LEU   B N    1 
ATOM   5065 C CA   . LEU   B 1 75  ? 41.353 -13.799 9.697   1.00 13.09 ?  75  LEU   B CA   1 
ATOM   5066 C C    . LEU   B 1 75  ? 40.376 -14.659 10.497  1.00 13.72 ?  75  LEU   B C    1 
ATOM   5067 O O    . LEU   B 1 75  ? 40.716 -15.223 11.538  1.00 14.70 ?  75  LEU   B O    1 
ATOM   5068 C CB   . LEU   B 1 75  ? 41.680 -14.514 8.385   1.00 12.99 ?  75  LEU   B CB   1 
ATOM   5069 C CG   . LEU   B 1 75  ? 42.508 -13.756 7.341   1.00 14.89 ?  75  LEU   B CG   1 
ATOM   5070 C CD1  . LEU   B 1 75  ? 42.685 -14.577 6.064   1.00 16.36 ?  75  LEU   B CD1  1 
ATOM   5071 C CD2  . LEU   B 1 75  ? 41.899 -12.415 7.025   1.00 18.10 ?  75  LEU   B CD2  1 
ATOM   5072 H H    . LEU   B 1 75  ? 43.243 -14.029 10.171  1.00 15.25 ?  75  LEU   B H    1 
ATOM   5073 H HA   . LEU   B 1 75  ? 40.931 -12.950 9.497   1.00 15.73 ?  75  LEU   B HA   1 
ATOM   5074 H HB2  . LEU   B 1 75  ? 42.169 -15.326 8.599   1.00 15.61 ?  75  LEU   B HB2  1 
ATOM   5075 H HB3  . LEU   B 1 75  ? 40.841 -14.758 7.958   1.00 15.61 ?  75  LEU   B HB3  1 
ATOM   5076 H HG   . LEU   B 1 75  ? 43.390 -13.599 7.707   1.00 17.89 ?  75  LEU   B HG   1 
ATOM   5077 H HD11 . LEU   B 1 75  ? 43.220 -14.067 5.431   1.00 19.65 ?  75  LEU   B HD11 1 
ATOM   5078 H HD12 . LEU   B 1 75  ? 43.138 -15.408 6.278   1.00 19.65 ?  75  LEU   B HD12 1 
ATOM   5079 H HD13 . LEU   B 1 75  ? 41.814 -14.765 5.680   1.00 19.65 ?  75  LEU   B HD13 1 
ATOM   5080 H HD21 . LEU   B 1 75  ? 42.370 -12.025 6.274   1.00 21.75 ?  75  LEU   B HD21 1 
ATOM   5081 H HD22 . LEU   B 1 75  ? 40.964 -12.539 6.806   1.00 21.75 ?  75  LEU   B HD22 1 
ATOM   5082 H HD23 . LEU   B 1 75  ? 41.984 -11.842 7.804   1.00 21.75 ?  75  LEU   B HD23 1 
ATOM   5083 N N    . LYS   B 1 76  ? 39.145 -14.754 9.993   1.00 14.95 ?  76  LYS   B N    1 
ATOM   5084 C CA   . LYS   B 1 76  ? 38.163 -15.717 10.472  1.00 16.20 ?  76  LYS   B CA   1 
ATOM   5085 C C    . LYS   B 1 76  ? 38.254 -16.986 9.627   1.00 14.52 ?  76  LYS   B C    1 
ATOM   5086 O O    . LYS   B 1 76  ? 38.523 -16.923 8.429   1.00 14.28 ?  76  LYS   B O    1 
ATOM   5087 C CB   . LYS   B 1 76  ? 36.743 -15.153 10.304  1.00 18.26 ?  76  LYS   B CB   1 
ATOM   5088 C CG   . LYS   B 1 76  ? 36.473 -13.761 10.905  1.00 20.19 ?  76  LYS   B CG   1 
ATOM   5089 C CD   . LYS   B 1 76  ? 35.064 -13.238 10.558  1.00 21.50 ?  76  LYS   B CD   1 
ATOM   5090 C CE   . LYS   B 1 76  ? 34.802 -11.855 11.142  1.00 23.23 ?  76  LYS   B CE   1 
ATOM   5091 N NZ   . LYS   B 1 76  ? 33.483 -11.289 10.734  1.00 23.90 ?  76  LYS   B NZ   1 
ATOM   5092 H H    . LYS   B 1 76  ? 38.853 -14.264 9.350   1.00 17.97 ?  76  LYS   B H    1 
ATOM   5093 H HA   . LYS   B 1 76  ? 38.321 -15.939 11.404  1.00 19.45 ?  76  LYS   B HA   1 
ATOM   5094 H HB2  . LYS   B 1 76  ? 36.552 -15.098 9.354   1.00 21.94 ?  76  LYS   B HB2  1 
ATOM   5095 H HB3  . LYS   B 1 76  ? 36.121 -15.770 10.719  1.00 21.94 ?  76  LYS   B HB3  1 
ATOM   5096 H HG2  . LYS   B 1 76  ? 36.551 -13.812 11.870  1.00 24.25 ?  76  LYS   B HG2  1 
ATOM   5097 H HG3  . LYS   B 1 76  ? 37.127 -13.133 10.552  1.00 24.25 ?  76  LYS   B HG3  1 
ATOM   5098 H HD2  . LYS   B 1 76  ? 34.976 -13.179 9.593   1.00 25.82 ?  76  LYS   B HD2  1 
ATOM   5099 H HD3  . LYS   B 1 76  ? 34.402 -13.847 10.917  1.00 25.82 ?  76  LYS   B HD3  1 
ATOM   5100 H HE2  . LYS   B 1 76  ? 34.818 -11.914 12.109  1.00 27.90 ?  76  LYS   B HE2  1 
ATOM   5101 H HE3  . LYS   B 1 76  ? 35.495 -11.248 10.836  1.00 27.90 ?  76  LYS   B HE3  1 
ATOM   5102 H HZ1  . LYS   B 1 76  ? 33.441 -11.213 9.848   1.00 28.70 ?  76  LYS   B HZ1  1 
ATOM   5103 H HZ2  . LYS   B 1 76  ? 32.823 -11.820 11.009  1.00 28.70 ?  76  LYS   B HZ2  1 
ATOM   5104 H HZ3  . LYS   B 1 76  ? 33.370 -10.482 11.097  1.00 28.70 ?  76  LYS   B HZ3  1 
ATOM   5105 N N    . VAL   B 1 77  ? 38.007 -18.145 10.250  1.00 14.90 ?  77  VAL   B N    1 
ATOM   5106 C CA   . VAL   B 1 77  ? 37.798 -19.354 9.460   1.00 15.07 ?  77  VAL   B CA   1 
ATOM   5107 C C    . VAL   B 1 77  ? 36.607 -19.119 8.545   1.00 14.04 ?  77  VAL   B C    1 
ATOM   5108 O O    . VAL   B 1 77  ? 35.540 -18.677 8.991   1.00 14.09 ?  77  VAL   B O    1 
ATOM   5109 C CB   . VAL   B 1 77  ? 37.598 -20.578 10.366  1.00 16.51 ?  77  VAL   B CB   1 
ATOM   5110 C CG1  . VAL   B 1 77  ? 37.310 -21.811 9.518   1.00 17.13 ?  77  VAL   B CG1  1 
ATOM   5111 C CG2  . VAL   B 1 77  ? 38.828 -20.800 11.238  1.00 18.03 ?  77  VAL   B CG2  1 
ATOM   5112 H H    . VAL   B 1 77  ? 37.951 -18.252 11.097  1.00 17.91 ?  77  VAL   B H    1 
ATOM   5113 H HA   . VAL   B 1 77  ? 38.572 -19.512 8.902   1.00 18.11 ?  77  VAL   B HA   1 
ATOM   5114 H HB   . VAL   B 1 77  ? 36.832 -20.425 10.945  1.00 19.83 ?  77  VAL   B HB   1 
ATOM   5115 H HG11 . VAL   B 1 77  ? 37.364 -22.598 10.082  1.00 20.58 ?  77  VAL   B HG11 1 
ATOM   5116 H HG12 . VAL   B 1 77  ? 36.416 -21.740 9.141   1.00 20.58 ?  77  VAL   B HG12 1 
ATOM   5117 H HG13 . VAL   B 1 77  ? 37.965 -21.866 8.808   1.00 20.58 ?  77  VAL   B HG13 1 
ATOM   5118 H HG21 . VAL   B 1 77  ? 38.697 -21.603 11.762  1.00 21.65 ?  77  VAL   B HG21 1 
ATOM   5119 H HG22 . VAL   B 1 77  ? 39.601 -20.897 10.663  1.00 21.65 ?  77  VAL   B HG22 1 
ATOM   5120 H HG23 . VAL   B 1 77  ? 38.938 -20.034 11.821  1.00 21.65 ?  77  VAL   B HG23 1 
ATOM   5121 N N    . GLY   B 1 78  ? 36.789 -19.398 7.255   1.00 13.40 ?  78  GLY   B N    1 
ATOM   5122 C CA   . GLY   B 1 78  ? 35.810 -19.074 6.245   1.00 13.05 ?  78  GLY   B CA   1 
ATOM   5123 C C    . GLY   B 1 78  ? 36.052 -17.755 5.544   1.00 12.67 ?  78  GLY   B C    1 
ATOM   5124 O O    . GLY   B 1 78  ? 35.368 -17.470 4.555   1.00 12.98 ?  78  GLY   B O    1 
ATOM   5125 H H    . GLY   B 1 78  ? 37.487 -19.790 6.939   1.00 16.10 ?  78  GLY   B H    1 
ATOM   5126 H HA2  . GLY   B 1 78  ? 35.800 -19.766 5.571   1.00 15.67 ?  78  GLY   B HA2  1 
ATOM   5127 H HA3  . GLY   B 1 78  ? 34.930 -19.034 6.653   1.00 15.67 ?  78  GLY   B HA3  1 
ATOM   5128 N N    . GLY   B 1 79  ? 37.002 -16.949 6.030   1.00 12.86 ?  79  GLY   B N    1 
ATOM   5129 C CA   . GLY   B 1 79  ? 37.298 -15.655 5.452   1.00 12.62 ?  79  GLY   B CA   1 
ATOM   5130 C C    . GLY   B 1 79  ? 38.536 -15.675 4.563   1.00 12.04 ?  79  GLY   B C    1 
ATOM   5131 O O    . GLY   B 1 79  ? 39.154 -16.711 4.317   1.00 12.36 ?  79  GLY   B O    1 
ATOM   5132 H H    . GLY   B 1 79  ? 37.495 -17.141 6.706   1.00 15.45 ?  79  GLY   B H    1 
ATOM   5133 H HA2  . GLY   B 1 79  ? 36.546 -15.356 4.919   1.00 15.16 ?  79  GLY   B HA2  1 
ATOM   5134 H HA3  . GLY   B 1 79  ? 37.447 -15.012 6.161   1.00 15.16 ?  79  GLY   B HA3  1 
ATOM   5135 N N    . SER   B 1 80  ? 38.899 -14.482 4.086   1.00 12.28 ?  80  SER   B N    1 
ATOM   5136 C CA   . SER   B 1 80  ? 40.010 -14.349 3.154   1.00 11.64 ?  80  SER   B CA   1 
ATOM   5137 C C    . SER   B 1 80  ? 40.593 -12.943 3.216   1.00 11.78 ?  80  SER   B C    1 
ATOM   5138 O O    . SER   B 1 80  ? 39.979 -12.006 3.733   1.00 13.07 ?  80  SER   B O    1 
ATOM   5139 C CB   . SER   B 1 80  ? 39.569 -14.636 1.714   1.00 12.22 ?  80  SER   B CB   1 
ATOM   5140 O OG   . SER   B 1 80  ? 38.727 -13.610 1.211   1.00 13.16 ?  80  SER   B OG   1 
ATOM   5141 H H    . SER   B 1 80  ? 38.520 -13.739 4.290   1.00 14.75 ?  80  SER   B H    1 
ATOM   5142 H HA   . SER   B 1 80  ? 40.702 -14.979 3.399   1.00 13.98 ?  80  SER   B HA   1 
ATOM   5143 H HB2  . SER   B 1 80  ? 40.354 -14.696 1.149   1.00 14.68 ?  80  SER   B HB2  1 
ATOM   5144 H HB3  . SER   B 1 80  ? 39.084 -15.475 1.697   1.00 14.68 ?  80  SER   B HB3  1 
ATOM   5145 H HG   . SER   B 1 80  ? 38.037 -13.545 1.695   1.00 15.81 ?  80  SER   B HG   1 
ATOM   5146 N N    . CYS   B 1 81  ? 41.782 -12.802 2.633   1.00 11.47 ?  81  CYS   B N    1 
ATOM   5147 C CA   . CYS   B 1 81  ? 42.325 -11.488 2.315   1.00 11.52 ?  81  CYS   B CA   1 
ATOM   5148 C C    . CYS   B 1 81  ? 43.094 -11.572 1.005   1.00 10.93 ?  81  CYS   B C    1 
ATOM   5149 O O    . CYS   B 1 81  ? 43.610 -12.631 0.631   1.00 11.91 ?  81  CYS   B O    1 
ATOM   5150 C CB   . CYS   B 1 81  ? 43.222 -10.925 3.429   1.00 12.55 ?  81  CYS   B CB   1 
ATOM   5151 S SG   . CYS   B 1 81  ? 44.736 -11.868 3.699   1.00 12.70 ?  81  CYS   B SG   1 
ATOM   5152 H H    . CYS   B 1 81  ? 42.295 -13.459 2.404   1.00 13.78 ?  81  CYS   B H    1 
ATOM   5153 H HA   . CYS   B 1 81  ? 41.589 -10.870 2.186   1.00 13.85 ?  81  CYS   B HA   1 
ATOM   5154 H HB2  . CYS   B 1 81  ? 43.482 -10.020 3.196   1.00 15.08 ?  81  CYS   B HB2  1 
ATOM   5155 H HB3  . CYS   B 1 81  ? 42.720 -10.915 4.261   1.00 15.08 ?  81  CYS   B HB3  1 
ATOM   5156 H HG   . CYS   B 1 81  ? 45.358 -11.356 4.598   1.00 15.26 ?  81  CYS   B HG   1 
ATOM   5157 N N    . VAL   B 1 82  ? 43.199 -10.425 0.333   1.00 11.22 ?  82  VAL   B N    1 
ATOM   5158 C CA   . VAL   B 1 82  ? 43.967 -10.300 -0.904  1.00 11.62 ?  82  VAL   B CA   1 
ATOM   5159 C C    . VAL   B 1 82  ? 45.309 -9.659  -0.583  1.00 11.93 ?  82  VAL   B C    1 
ATOM   5160 O O    . VAL   B 1 82  ? 45.362 -8.543  -0.049  1.00 12.82 ?  82  VAL   B O    1 
ATOM   5161 C CB   . VAL   B 1 82  ? 43.222 -9.461  -1.954  1.00 12.85 ?  82  VAL   B CB   1 
ATOM   5162 C CG1  . VAL   B 1 82  ? 44.080 -9.310  -3.206  1.00 14.04 ?  82  VAL   B CG1  1 
ATOM   5163 C CG2  . VAL   B 1 82  ? 41.868 -10.064 -2.278  1.00 13.63 ?  82  VAL   B CG2  1 
ATOM   5164 H H    . VAL   B 1 82  ? 42.823 -9.684  0.577   1.00 13.48 ?  82  VAL   B H    1 
ATOM   5165 H HA   . VAL   B 1 82  ? 44.128 -11.180 -1.272  1.00 13.96 ?  82  VAL   B HA   1 
ATOM   5166 H HB   . VAL   B 1 82  ? 43.072 -8.576  -1.597  1.00 15.44 ?  82  VAL   B HB   1 
ATOM   5167 H HG11 . VAL   B 1 82  ? 43.522 -9.004  -3.938  1.00 16.86 ?  82  VAL   B HG11 1 
ATOM   5168 H HG12 . VAL   B 1 82  ? 44.782 -8.658  -3.035  1.00 16.86 ?  82  VAL   B HG12 1 
ATOM   5169 H HG13 . VAL   B 1 82  ? 44.475 -10.167 -3.428  1.00 16.86 ?  82  VAL   B HG13 1 
ATOM   5170 H HG21 . VAL   B 1 82  ? 41.440 -9.532  -2.969  1.00 16.37 ?  82  VAL   B HG21 1 
ATOM   5171 H HG22 . VAL   B 1 82  ? 41.991 -10.974 -2.593  1.00 16.37 ?  82  VAL   B HG22 1 
ATOM   5172 H HG23 . VAL   B 1 82  ? 41.322 -10.064 -1.476  1.00 16.37 ?  82  VAL   B HG23 1 
ATOM   5173 N N    . LEU   B 1 83  ? 46.389 -10.349 -0.942  1.00 11.57 ?  83  LEU   B N    1 
ATOM   5174 C CA   . LEU   B 1 83  ? 47.745 -9.831  -0.827  1.00 11.40 ?  83  LEU   B CA   1 
ATOM   5175 C C    . LEU   B 1 83  ? 48.447 -9.978  -2.178  1.00 11.39 ?  83  LEU   B C    1 
ATOM   5176 O O    . LEU   B 1 83  ? 47.844 -10.393 -3.172  1.00 11.39 ?  83  LEU   B O    1 
ATOM   5177 C CB   . LEU   B 1 83  ? 48.494 -10.504 0.329   1.00 12.04 ?  83  LEU   B CB   1 
ATOM   5178 C CG   . LEU   B 1 83  ? 47.984 -10.147 1.730   1.00 13.28 ?  83  LEU   B CG   1 
ATOM   5179 C CD1  . LEU   B 1 83  ? 48.592 -11.027 2.797   1.00 13.86 ?  83  LEU   B CD1  1 
ATOM   5180 C CD2  . LEU   B 1 83  ? 48.202 -8.668  2.061   1.00 14.06 ?  83  LEU   B CD2  1 
ATOM   5181 H H    . LEU   B 1 83  ? 46.349 -11.151 -1.262  1.00 13.90 ?  83  LEU   B H    1 
ATOM   5182 H HA   . LEU   B 1 83  ? 47.689 -8.886  -0.633  1.00 13.70 ?  83  LEU   B HA   1 
ATOM   5183 H HB2  . LEU   B 1 83  ? 48.425 -11.461 0.226   1.00 14.47 ?  83  LEU   B HB2  1 
ATOM   5184 H HB3  . LEU   B 1 83  ? 49.426 -10.235 0.278   1.00 14.47 ?  83  LEU   B HB3  1 
ATOM   5185 H HG   . LEU   B 1 83  ? 47.030 -10.299 1.745   1.00 15.96 ?  83  LEU   B HG   1 
ATOM   5186 H HD11 . LEU   B 1 83  ? 48.232 -10.769 3.661   1.00 16.65 ?  83  LEU   B HD11 1 
ATOM   5187 H HD12 . LEU   B 1 83  ? 48.361 -11.952 2.609   1.00 16.65 ?  83  LEU   B HD12 1 
ATOM   5188 H HD13 . LEU   B 1 83  ? 49.554 -10.919 2.792   1.00 16.65 ?  83  LEU   B HD13 1 
ATOM   5189 H HD21 . LEU   B 1 83  ? 47.978 -8.517  2.993   1.00 16.89 ?  83  LEU   B HD21 1 
ATOM   5190 H HD22 . LEU   B 1 83  ? 49.131 -8.439  1.903   1.00 16.89 ?  83  LEU   B HD22 1 
ATOM   5191 H HD23 . LEU   B 1 83  ? 47.628 -8.128  1.493   1.00 16.89 ?  83  LEU   B HD23 1 
ATOM   5192 N N    . SER   B 1 84  ? 49.722 -9.600  -2.231  1.00 12.45 ?  84  SER   B N    1 
ATOM   5193 C CA   . SER   B 1 84  ? 50.460 -9.717  -3.479  1.00 12.62 ?  84  SER   B CA   1 
ATOM   5194 C C    . SER   B 1 84  ? 50.617 -11.176 -3.892  1.00 11.62 ?  84  SER   B C    1 
ATOM   5195 O O    . SER   B 1 84  ? 50.726 -12.075 -3.059  1.00 11.82 ?  84  SER   B O    1 
ATOM   5196 C CB   . SER   B 1 84  ? 51.852 -9.112  -3.327  1.00 14.65 ?  84  SER   B CB   1 
ATOM   5197 O OG   . SER   B 1 84  ? 52.601 -9.321  -4.509  1.00 16.04 ?  84  SER   B OG   1 
ATOM   5198 H H    . SER   B 1 84  ? 50.168 -9.268  -1.575  1.00 14.96 ?  84  SER   B H    1 
ATOM   5199 H HA   . SER   B 1 84  ? 49.990 -9.244  -4.184  1.00 15.17 ?  84  SER   B HA   1 
ATOM   5200 H HB2  . SER   B 1 84  ? 51.766 -8.156  -3.158  1.00 17.60 ?  84  SER   B HB2  1 
ATOM   5201 H HB3  . SER   B 1 84  ? 52.308 -9.538  -2.588  1.00 17.60 ?  84  SER   B HB3  1 
ATOM   5202 H HG   . SER   B 1 84  ? 53.366 -8.968  -4.429  1.00 19.27 ?  84  SER   B HG   1 
ATOM   5203 N N    . GLY   B 1 85  ? 50.678 -11.397 -5.199  1.00 12.76 ?  85  GLY   B N    1 
ATOM   5204 C CA   . GLY   B 1 85  ? 51.027 -12.691 -5.732  1.00 13.53 ?  85  GLY   B CA   1 
ATOM   5205 C C    . GLY   B 1 85  ? 52.499 -12.883 -6.037  1.00 12.90 ?  85  GLY   B C    1 
ATOM   5206 O O    . GLY   B 1 85  ? 52.877 -13.958 -6.507  1.00 13.27 ?  85  GLY   B O    1 
ATOM   5207 H H    . GLY   B 1 85  ? 50.530 -10.804 -5.799  1.00 15.33 ?  85  GLY   B H    1 
ATOM   5208 H HA2  . GLY   B 1 85  ? 50.762 -13.378 -5.098  1.00 16.26 ?  85  GLY   B HA2  1 
ATOM   5209 H HA3  . GLY   B 1 85  ? 50.539 -12.838 -6.552  1.00 16.26 ?  85  GLY   B HA3  1 
ATOM   5210 N N    . HIS   B 1 86  ? 53.349 -11.883 -5.811  1.00 12.76 ?  86  HIS   B N    1 
ATOM   5211 C CA   . HIS   B 1 86  ? 54.811 -12.045 -5.891  1.00 12.62 ?  86  HIS   B CA   1 
ATOM   5212 C C    . HIS   B 1 86  ? 55.185 -12.554 -7.282  1.00 12.87 ?  86  HIS   B C    1 
ATOM   5213 O O    . HIS   B 1 86  ? 54.794 -11.942 -8.288  1.00 13.90 ?  86  HIS   B O    1 
ATOM   5214 C CB   . HIS   B 1 86  ? 55.284 -12.896 -4.713  1.00 13.11 ?  86  HIS   B CB   1 
ATOM   5215 C CG   . HIS   B 1 86  ? 54.974 -12.287 -3.387  1.00 13.21 ?  86  HIS   B CG   1 
ATOM   5216 N ND1  . HIS   B 1 86  ? 55.806 -11.375 -2.777  1.00 14.72 ?  86  HIS   B ND1  1 
ATOM   5217 C CD2  . HIS   B 1 86  ? 53.901 -12.428 -2.572  1.00 13.54 ?  86  HIS   B CD2  1 
ATOM   5218 C CE1  . HIS   B 1 86  ? 55.258 -10.981 -1.641  1.00 14.44 ?  86  HIS   B CE1  1 
ATOM   5219 N NE2  . HIS   B 1 86  ? 54.103 -11.605 -1.493  1.00 13.75 ?  86  HIS   B NE2  1 
ATOM   5220 H H    . HIS   B 1 86  ? 53.103 -11.085 -5.611  1.00 15.33 ?  86  HIS   B H    1 
ATOM   5221 H HA   . HIS   B 1 86  ? 55.215 -11.172 -5.785  1.00 15.17 ?  86  HIS   B HA   1 
ATOM   5222 H HB2  . HIS   B 1 86  ? 54.852 -13.763 -4.753  1.00 15.75 ?  86  HIS   B HB2  1 
ATOM   5223 H HB3  . HIS   B 1 86  ? 56.247 -13.005 -4.770  1.00 15.75 ?  86  HIS   B HB3  1 
ATOM   5224 H HD2  . HIS   B 1 86  ? 53.158 -12.969 -2.720  1.00 16.26 ?  86  HIS   B HD2  1 
ATOM   5225 H HE1  . HIS   B 1 86  ? 55.633 -10.380 -1.038  1.00 17.34 ?  86  HIS   B HE1  1 
ATOM   5226 H HE2  . HIS   B 1 86  ? 53.569 -11.516 -0.823  1.00 16.52 ?  86  HIS   B HE2  1 
ATOM   5227 N N    . ASN   B 1 87  ? 55.947 -13.639 -7.392  1.00 13.08 ?  87  ASN   B N    1 
ATOM   5228 C CA   . ASN   B 1 87  ? 56.342 -14.208 -8.671  1.00 13.96 ?  87  ASN   B CA   1 
ATOM   5229 C C    . ASN   B 1 87  ? 55.364 -15.256 -9.173  1.00 13.83 ?  87  ASN   B C    1 
ATOM   5230 O O    . ASN   B 1 87  ? 55.682 -15.973 -10.127 1.00 15.68 ?  87  ASN   B O    1 
ATOM   5231 C CB   . ASN   B 1 87  ? 57.738 -14.831 -8.558  1.00 15.88 ?  87  ASN   B CB   1 
ATOM   5232 C CG   . ASN   B 1 87  ? 57.799 -15.947 -7.521  1.00 16.66 ?  87  ASN   B CG   1 
ATOM   5233 O OD1  . ASN   B 1 87  ? 57.161 -15.869 -6.467  1.00 15.99 ?  87  ASN   B OD1  1 
ATOM   5234 N ND2  . ASN   B 1 87  ? 58.550 -17.007 -7.830  1.00 18.74 ?  87  ASN   B ND2  1 
ATOM   5235 H H    . ASN   B 1 87  ? 56.250 -14.077 -6.717  1.00 15.72 ?  87  ASN   B H    1 
ATOM   5236 H HA   . ASN   B 1 87  ? 56.379 -13.500 -9.329  1.00 16.77 ?  87  ASN   B HA   1 
ATOM   5237 H HB2  . ASN   B 1 87  ? 57.986 -15.203 -9.418  1.00 19.08 ?  87  ASN   B HB2  1 
ATOM   5238 H HB3  . ASN   B 1 87  ? 58.368 -14.143 -8.298  1.00 19.08 ?  87  ASN   B HB3  1 
ATOM   5239 H HD21 . ASN   B 1 87  ? 58.618 -17.661 -7.278  1.00 22.51 ?  87  ASN   B HD21 1 
ATOM   5240 H HD22 . ASN   B 1 87  ? 58.975 -17.029 -8.579  1.00 22.51 ?  87  ASN   B HD22 1 
ATOM   5241 N N    . LEU   B 1 88  ? 54.181 -15.354 -8.564  1.00 12.81 ?  88  LEU   B N    1 
ATOM   5242 C CA   . LEU   B 1 88  ? 53.205 -16.386 -8.891  1.00 13.19 ?  88  LEU   B CA   1 
ATOM   5243 C C    . LEU   B 1 88  ? 51.971 -15.871 -9.613  1.00 12.87 ?  88  LEU   B C    1 
ATOM   5244 O O    . LEU   B 1 88  ? 51.371 -16.620 -10.396 1.00 14.62 ?  88  LEU   B O    1 
ATOM   5245 C CB   . LEU   B 1 88  ? 52.736 -17.073 -7.605  1.00 14.13 ?  88  LEU   B CB   1 
ATOM   5246 C CG   . LEU   B 1 88  ? 53.852 -17.729 -6.802  1.00 16.40 ?  88  LEU   B CG   1 
ATOM   5247 C CD1  . LEU   B 1 88  ? 53.348 -18.108 -5.417  1.00 17.89 ?  88  LEU   B CD1  1 
ATOM   5248 C CD2  . LEU   B 1 88  ? 54.372 -18.944 -7.544  1.00 19.32 ?  88  LEU   B CD2  1 
ATOM   5249 H H    . LEU   B 1 88  ? 53.914 -14.821 -7.934  1.00 15.39 ?  88  LEU   B H    1 
ATOM   5250 H HA   . LEU   B 1 88  ? 53.618 -17.050 -9.451  1.00 15.84 ?  88  LEU   B HA   1 
ATOM   5251 H HB2  . LEU   B 1 88  ? 52.305 -16.419 -7.031  1.00 16.97 ?  88  LEU   B HB2  1 
ATOM   5252 H HB3  . LEU   B 1 88  ? 52.095 -17.769 -7.838  1.00 16.97 ?  88  LEU   B HB3  1 
ATOM   5253 H HG   . LEU   B 1 88  ? 54.580 -17.100 -6.697  1.00 19.70 ?  88  LEU   B HG   1 
ATOM   5254 H HD11 . LEU   B 1 88  ? 54.025 -18.638 -4.970  1.00 21.48 ?  88  LEU   B HD11 1 
ATOM   5255 H HD12 . LEU   B 1 88  ? 53.171 -17.298 -4.913  1.00 21.48 ?  88  LEU   B HD12 1 
ATOM   5256 H HD13 . LEU   B 1 88  ? 52.532 -18.623 -5.512  1.00 21.48 ?  88  LEU   B HD13 1 
ATOM   5257 H HD21 . LEU   B 1 88  ? 55.015 -19.403 -6.982  1.00 23.20 ?  88  LEU   B HD21 1 
ATOM   5258 H HD22 . LEU   B 1 88  ? 53.629 -19.532 -7.747  1.00 23.20 ?  88  LEU   B HD22 1 
ATOM   5259 H HD23 . LEU   B 1 88  ? 54.798 -18.653 -8.365  1.00 23.20 ?  88  LEU   B HD23 1 
ATOM   5260 N N    . ALA   B 1 89  ? 51.565 -14.635 -9.343  1.00 12.15 ?  89  ALA   B N    1 
ATOM   5261 C CA   . ALA   B 1 89  ? 50.272 -14.144 -9.791  1.00 11.69 ?  89  ALA   B CA   1 
ATOM   5262 C C    . ALA   B 1 89  ? 50.241 -12.652 -9.514  1.00 12.25 ?  89  ALA   B C    1 
ATOM   5263 O O    . ALA   B 1 89  ? 51.083 -12.128 -8.783  1.00 12.80 ?  89  ALA   B O    1 
ATOM   5264 C CB   . ALA   B 1 89  ? 49.134 -14.825 -9.032  1.00 12.18 ?  89  ALA   B CB   1 
ATOM   5265 H H    . ALA   B 1 89  ? 52.014 -14.054 -8.888  1.00 14.60 ?  89  ALA   B H    1 
ATOM   5266 H HA   . ALA   B 1 89  ? 50.160 -14.294 -10.743 1.00 14.05 ?  89  ALA   B HA   1 
ATOM   5267 H HB1  . ALA   B 1 89  ? 48.285 -14.489 -9.366  1.00 14.63 ?  89  ALA   B HB1  1 
ATOM   5268 H HB2  . ALA   B 1 89  ? 49.190 -15.782 -9.182  1.00 14.63 ?  89  ALA   B HB2  1 
ATOM   5269 H HB3  . ALA   B 1 89  ? 49.222 -14.629 -8.090  1.00 14.63 ?  89  ALA   B HB3  1 
ATOM   5270 N N    . LYS   B 1 90  ? 49.246 -11.965 -10.076 1.00 13.11 ?  90  LYS   B N    1 
ATOM   5271 C CA   . LYS   B 1 90  ? 49.057 -10.577 -9.674  1.00 13.24 ?  90  LYS   B CA   1 
ATOM   5272 C C    . LYS   B 1 90  ? 48.744 -10.501 -8.185  1.00 13.07 ?  90  LYS   B C    1 
ATOM   5273 O O    . LYS   B 1 90  ? 49.388 -9.746  -7.440  1.00 14.25 ?  90  LYS   B O    1 
ATOM   5274 C CB   . LYS   B 1 90  ? 47.977 -9.913  -10.528 1.00 14.55 ?  90  LYS   B CB   1 
ATOM   5275 C CG   . LYS   B 1 90  ? 47.689 -8.472  -10.151 1.00 14.86 ?  90  LYS   B CG   1 
ATOM   5276 C CD   . LYS   B 1 90  ? 48.901 -7.588  -10.237 1.00 17.60 ?  90  LYS   B CD   1 
ATOM   5277 C CE   . LYS   B 1 90  ? 48.463 -6.166  -9.996  1.00 19.58 ?  90  LYS   B CE   1 
ATOM   5278 N NZ   . LYS   B 1 90  ? 49.614 -5.243  -9.879  1.00 19.63 ?  90  LYS   B NZ   1 
ATOM   5279 H H    . LYS   B 1 90  ? 48.692 -12.269 -10.661 1.00 15.75 ?  90  LYS   B H    1 
ATOM   5280 H HA   . LYS   B 1 90  ? 49.882 -10.100 -9.824  1.00 15.91 ?  90  LYS   B HA   1 
ATOM   5281 H HB2  . LYS   B 1 90  ? 48.264 -9.920  -11.457 1.00 17.48 ?  90  LYS   B HB2  1 
ATOM   5282 H HB3  . LYS   B 1 90  ? 47.151 -10.413 -10.441 1.00 17.48 ?  90  LYS   B HB3  1 
ATOM   5283 H HG2  . LYS   B 1 90  ? 47.017 -8.117  -10.755 1.00 17.85 ?  90  LYS   B HG2  1 
ATOM   5284 H HG3  . LYS   B 1 90  ? 47.357 -8.443  -9.239  1.00 17.85 ?  90  LYS   B HG3  1 
ATOM   5285 H HD2  . LYS   B 1 90  ? 49.543 -7.837  -9.552  1.00 21.14 ?  90  LYS   B HD2  1 
ATOM   5286 H HD3  . LYS   B 1 90  ? 49.296 -7.652  -11.120 1.00 21.14 ?  90  LYS   B HD3  1 
ATOM   5287 H HE2  . LYS   B 1 90  ? 47.915 -5.865  -10.740 1.00 23.51 ?  90  LYS   B HE2  1 
ATOM   5288 H HE3  . LYS   B 1 90  ? 47.957 -6.116  -9.170  1.00 23.51 ?  90  LYS   B HE3  1 
ATOM   5289 H HZ1  . LYS   B 1 90  ? 49.331 -4.410  -9.740  1.00 23.58 ?  90  LYS   B HZ1  1 
ATOM   5290 H HZ2  . LYS   B 1 90  ? 50.135 -5.488  -9.199  1.00 23.58 ?  90  LYS   B HZ2  1 
ATOM   5291 H HZ3  . LYS   B 1 90  ? 50.096 -5.259  -10.630 1.00 23.58 ?  90  LYS   B HZ3  1 
ATOM   5292 N N    . HIS   B 1 91  ? 47.784 -11.316 -7.734  1.00 11.65 ?  91  HIS   B N    1 
ATOM   5293 C CA   . HIS   B 1 91  ? 47.322 -11.341 -6.359  1.00 11.59 ?  91  HIS   B CA   1 
ATOM   5294 C C    . HIS   B 1 91  ? 47.323 -12.769 -5.845  1.00 11.01 ?  91  HIS   B C    1 
ATOM   5295 O O    . HIS   B 1 91  ? 47.090 -13.721 -6.598  1.00 11.54 ?  91  HIS   B O    1 
ATOM   5296 C CB   . HIS   B 1 91  ? 45.868 -10.861 -6.242  1.00 13.24 ?  91  HIS   B CB   1 
ATOM   5297 C CG   . HIS   B 1 91  ? 45.655 -9.454  -6.684  1.00 16.56 ?  91  HIS   B CG   1 
ATOM   5298 N ND1  . HIS   B 1 91  ? 46.263 -8.379  -6.072  1.00 18.85 ?  91  HIS   B ND1  1 
ATOM   5299 C CD2  . HIS   B 1 91  ? 44.876 -8.941  -7.662  1.00 18.94 ?  91  HIS   B CD2  1 
ATOM   5300 C CE1  . HIS   B 1 91  ? 45.882 -7.261  -6.667  1.00 19.79 ?  91  HIS   B CE1  1 
ATOM   5301 N NE2  . HIS   B 1 91  ? 45.034 -7.576  -7.631  1.00 19.96 ?  91  HIS   B NE2  1 
ATOM   5302 H H    . HIS   B 1 91  ? 47.368 -11.884 -8.232  1.00 14.00 ?  91  HIS   B H    1 
ATOM   5303 H HA   . HIS   B 1 91  ? 47.894 -10.786 -5.796  1.00 13.93 ?  91  HIS   B HA   1 
ATOM   5304 H HB2  . HIS   B 1 91  ? 45.305 -11.427 -6.789  1.00 15.90 ?  91  HIS   B HB2  1 
ATOM   5305 H HB3  . HIS   B 1 91  ? 45.589 -10.922 -5.311  1.00 15.90 ?  91  HIS   B HB3  1 
ATOM   5306 H HD1  . HIS   B 1 91  ? 46.812 -8.426  -5.408  1.00 22.64 ?  91  HIS   B HD1  1 
ATOM   5307 H HD2  . HIS   B 1 91  ? 44.338 -9.413  -8.249  1.00 22.75 ?  91  HIS   B HD2  1 
ATOM   5308 H HE1  . HIS   B 1 91  ? 46.158 -6.400  -6.438  1.00 23.77 ?  91  HIS   B HE1  1 
ATOM   5309 N N    . CYS   B 1 92  ? 47.518 -12.903 -4.541  1.00 10.97 ?  92  CYS   B N    1 
ATOM   5310 C CA   . CYS   B 1 92  ? 47.213 -14.136 -3.829  1.00 10.56 ?  92  CYS   B CA   1 
ATOM   5311 C C    . CYS   B 1 92  ? 45.992 -13.899 -2.949  1.00 10.12 ?  92  CYS   B C    1 
ATOM   5312 O O    . CYS   B 1 92  ? 45.994 -12.998 -2.101  1.00 11.27 ?  92  CYS   B O    1 
ATOM   5313 C CB   . CYS   B 1 92  ? 48.389 -14.591 -2.973  1.00 11.10 ?  92  CYS   B CB   1 
ATOM   5314 S SG   . CYS   B 1 92  ? 48.034 -16.131 -2.074  1.00 11.25 ?  92  CYS   B SG   1 
ATOM   5315 H H    . CYS   B 1 92  ? 47.849 -12.284 -4.036  1.00 13.18 ?  92  CYS   B H    1 
ATOM   5316 H HA   . CYS   B 1 92  ? 47.011 -14.834 -4.472  1.00 12.69 ?  92  CYS   B HA   1 
ATOM   5317 H HB2  . CYS   B 1 92  ? 49.156 -14.741 -3.539  1.00 13.34 ?  92  CYS   B HB2  1 
ATOM   5318 H HB3  . CYS   B 1 92  ? 48.582 -13.899 -2.318  1.00 13.34 ?  92  CYS   B HB3  1 
ATOM   5319 H HG   . CYS   B 1 92  ? 49.007 -16.441 -1.446  1.00 13.51 ?  92  CYS   B HG   1 
ATOM   5320 N N    . LEU   B 1 93  ? 44.956 -14.707 -3.157  1.00 10.20 ?  93  LEU   B N    1 
ATOM   5321 C CA   . LEU   B 1 93  ? 43.779 -14.716 -2.298  1.00 10.38 ?  93  LEU   B CA   1 
ATOM   5322 C C    . LEU   B 1 93  ? 44.001 -15.781 -1.233  1.00 10.06 ?  93  LEU   B C    1 
ATOM   5323 O O    . LEU   B 1 93  ? 43.951 -16.982 -1.524  1.00 10.76 ?  93  LEU   B O    1 
ATOM   5324 C CB   . LEU   B 1 93  ? 42.522 -15.010 -3.111  1.00 10.84 ?  93  LEU   B CB   1 
ATOM   5325 C CG   . LEU   B 1 93  ? 41.221 -15.027 -2.306  1.00 11.41 ?  93  LEU   B CG   1 
ATOM   5326 C CD1  . LEU   B 1 93  ? 40.868 -13.642 -1.822  1.00 11.92 ?  93  LEU   B CD1  1 
ATOM   5327 C CD2  . LEU   B 1 93  ? 40.088 -15.619 -3.130  1.00 11.72 ?  93  LEU   B CD2  1 
ATOM   5328 H H    . LEU   B 1 93  ? 44.916 -15.284 -3.804  1.00 12.25 ?  93  LEU   B H    1 
ATOM   5329 H HA   . LEU   B 1 93  ? 43.684 -13.856 -1.870  1.00 12.48 ?  93  LEU   B HA   1 
ATOM   5330 H HB2  . LEU   B 1 93  ? 42.431 -14.323 -3.794  1.00 13.02 ?  93  LEU   B HB2  1 
ATOM   5331 H HB3  . LEU   B 1 93  ? 42.616 -15.875 -3.532  1.00 13.02 ?  93  LEU   B HB3  1 
ATOM   5332 H HG   . LEU   B 1 93  ? 41.341 -15.588 -1.529  1.00 13.71 ?  93  LEU   B HG   1 
ATOM   5333 H HD11 . LEU   B 1 93  ? 40.009 -13.673 -1.376  1.00 14.33 ?  93  LEU   B HD11 1 
ATOM   5334 H HD12 . LEU   B 1 93  ? 41.553 -13.340 -1.206  1.00 14.33 ?  93  LEU   B HD12 1 
ATOM   5335 H HD13 . LEU   B 1 93  ? 40.822 -13.042 -2.586  1.00 14.33 ?  93  LEU   B HD13 1 
ATOM   5336 H HD21 . LEU   B 1 93  ? 39.274 -15.616 -2.600  1.00 14.09 ?  93  LEU   B HD21 1 
ATOM   5337 H HD22 . LEU   B 1 93  ? 39.961 -15.088 -3.932  1.00 14.09 ?  93  LEU   B HD22 1 
ATOM   5338 H HD23 . LEU   B 1 93  ? 40.316 -16.533 -3.374  1.00 14.09 ?  93  LEU   B HD23 1 
ATOM   5339 N N    . HIS   B 1 94  ? 44.284 -15.347 -0.010  1.00 10.10 ?  94  HIS   B N    1 
ATOM   5340 C CA   . HIS   B 1 94  ? 44.501 -16.257 1.109   1.00 10.16 ?  94  HIS   B CA   1 
ATOM   5341 C C    . HIS   B 1 94  ? 43.140 -16.614 1.688   1.00 10.53 ?  94  HIS   B C    1 
ATOM   5342 O O    . HIS   B 1 94  ? 42.468 -15.744 2.242   1.00 11.96 ?  94  HIS   B O    1 
ATOM   5343 C CB   . HIS   B 1 94  ? 45.368 -15.578 2.167   1.00 10.59 ?  94  HIS   B CB   1 
ATOM   5344 C CG   . HIS   B 1 94  ? 46.750 -15.275 1.702   1.00 10.83 ?  94  HIS   B CG   1 
ATOM   5345 N ND1  . HIS   B 1 94  ? 47.776 -16.193 1.780   1.00 11.13 ?  94  HIS   B ND1  1 
ATOM   5346 C CD2  . HIS   B 1 94  ? 47.257 -14.170 1.105   1.00 11.04 ?  94  HIS   B CD2  1 
ATOM   5347 C CE1  . HIS   B 1 94  ? 48.865 -15.643 1.268   1.00 10.99 ?  94  HIS   B CE1  1 
ATOM   5348 N NE2  . HIS   B 1 94  ? 48.580 -14.417 0.855   1.00 11.01 ?  94  HIS   B NE2  1 
ATOM   5349 H H    . HIS   B 1 94  ? 44.358 -14.513 0.195   1.00 12.14 ?  94  HIS   B H    1 
ATOM   5350 H HA   . HIS   B 1 94  ? 44.938 -17.064 0.796   1.00 12.22 ?  94  HIS   B HA   1 
ATOM   5351 H HB2  . HIS   B 1 94  ? 44.951 -14.744 2.419   1.00 12.73 ?  94  HIS   B HB2  1 
ATOM   5352 H HB3  . HIS   B 1 94  ? 45.435 -16.167 2.930   1.00 12.73 ?  94  HIS   B HB3  1 
ATOM   5353 H HD2  . HIS   B 1 94  ? 46.799 -13.387 0.912   1.00 13.27 ?  94  HIS   B HD2  1 
ATOM   5354 H HE1  . HIS   B 1 94  ? 49.696 -16.059 1.204   1.00 13.21 ?  94  HIS   B HE1  1 
ATOM   5355 H HE2  . HIS   B 1 94  ? 49.135 -13.875 0.486   1.00 13.23 ?  94  HIS   B HE2  1 
ATOM   5356 N N    . VAL   B 1 95  ? 42.709 -17.867 1.541   1.00 10.42 ?  95  VAL   B N    1 
ATOM   5357 C CA   . VAL   B 1 95  ? 41.382 -18.304 1.974   1.00 10.70 ?  95  VAL   B CA   1 
ATOM   5358 C C    . VAL   B 1 95  ? 41.550 -19.339 3.073   1.00 11.15 ?  95  VAL   B C    1 
ATOM   5359 O O    . VAL   B 1 95  ? 42.324 -20.292 2.919   1.00 11.61 ?  95  VAL   B O    1 
ATOM   5360 C CB   . VAL   B 1 95  ? 40.560 -18.906 0.818   1.00 10.86 ?  95  VAL   B CB   1 
ATOM   5361 C CG1  . VAL   B 1 95  ? 39.180 -19.362 1.305   1.00 12.29 ?  95  VAL   B CG1  1 
ATOM   5362 C CG2  . VAL   B 1 95  ? 40.436 -17.924 -0.319  1.00 10.96 ?  95  VAL   B CG2  1 
ATOM   5363 H H    . VAL   B 1 95  ? 43.175 -18.499 1.185   1.00 12.52 ?  95  VAL   B H    1 
ATOM   5364 H HA   . VAL   B 1 95  ? 40.892 -17.550 2.338   1.00 12.86 ?  95  VAL   B HA   1 
ATOM   5365 H HB   . VAL   B 1 95  ? 41.018 -19.683 0.480   1.00 13.05 ?  95  VAL   B HB   1 
ATOM   5366 H HG11 . VAL   B 1 95  ? 38.616 -19.554 0.535   1.00 14.77 ?  95  VAL   B HG11 1 
ATOM   5367 H HG12 . VAL   B 1 95  ? 39.276 -20.162 1.844   1.00 14.77 ?  95  VAL   B HG12 1 
ATOM   5368 H HG13 . VAL   B 1 95  ? 38.773 -18.654 1.833   1.00 14.77 ?  95  VAL   B HG13 1 
ATOM   5369 H HG21 . VAL   B 1 95  ? 39.861 -18.306 -1.002  1.00 13.17 ?  95  VAL   B HG21 1 
ATOM   5370 H HG22 . VAL   B 1 95  ? 40.049 -17.100 0.015   1.00 13.17 ?  95  VAL   B HG22 1 
ATOM   5371 H HG23 . VAL   B 1 95  ? 41.317 -17.757 -0.683  1.00 13.17 ?  95  VAL   B HG23 1 
ATOM   5372 N N    . VAL   B 1 96  ? 40.812 -19.171 4.164   1.00 11.43 ?  96  VAL   B N    1 
ATOM   5373 C CA   . VAL   B 1 96  ? 40.894 -20.081 5.306   1.00 11.86 ?  96  VAL   B CA   1 
ATOM   5374 C C    . VAL   B 1 96  ? 39.706 -21.039 5.260   1.00 12.38 ?  96  VAL   B C    1 
ATOM   5375 O O    . VAL   B 1 96  ? 38.586 -20.686 5.643   1.00 12.93 ?  96  VAL   B O    1 
ATOM   5376 C CB   . VAL   B 1 96  ? 40.943 -19.327 6.638   1.00 12.35 ?  96  VAL   B CB   1 
ATOM   5377 C CG1  . VAL   B 1 96  ? 41.109 -20.312 7.791   1.00 13.32 ?  96  VAL   B CG1  1 
ATOM   5378 C CG2  . VAL   B 1 96  ? 42.060 -18.292 6.644   1.00 12.91 ?  96  VAL   B CG2  1 
ATOM   5379 H H    . VAL   B 1 96  ? 40.246 -18.535 4.273   1.00 13.74 ?  96  VAL   B H    1 
ATOM   5380 H HA   . VAL   B 1 96  ? 41.706 -20.610 5.236   1.00 14.25 ?  96  VAL   B HA   1 
ATOM   5381 H HB   . VAL   B 1 96  ? 40.100 -18.862 6.767   1.00 14.84 ?  96  VAL   B HB   1 
ATOM   5382 H HG11 . VAL   B 1 96  ? 41.291 -19.814 8.606   1.00 16.00 ?  96  VAL   B HG11 1 
ATOM   5383 H HG12 . VAL   B 1 96  ? 40.291 -20.823 7.896   1.00 16.00 ?  96  VAL   B HG12 1 
ATOM   5384 H HG13 . VAL   B 1 96  ? 41.849 -20.905 7.596   1.00 16.00 ?  96  VAL   B HG13 1 
ATOM   5385 H HG21 . VAL   B 1 96  ? 42.103 -17.875 7.522   1.00 15.52 ?  96  VAL   B HG21 1 
ATOM   5386 H HG22 . VAL   B 1 96  ? 42.900 -18.727 6.443   1.00 15.52 ?  96  VAL   B HG22 1 
ATOM   5387 H HG23 . VAL   B 1 96  ? 41.868 -17.614 5.973   1.00 15.52 ?  96  VAL   B HG23 1 
ATOM   5388 N N    . GLY   B 1 97  ? 39.941 -22.271 4.821   1.00 12.19 ?  97  GLY   B N    1 
ATOM   5389 C CA   . GLY   B 1 97  ? 38.960 -23.320 4.976   1.00 12.80 ?  97  GLY   B CA   1 
ATOM   5390 C C    . GLY   B 1 97  ? 39.084 -23.942 6.352   1.00 13.78 ?  97  GLY   B C    1 
ATOM   5391 O O    . GLY   B 1 97  ? 40.124 -23.820 7.014   1.00 14.24 ?  97  GLY   B O    1 
ATOM   5392 H H    . GLY   B 1 97  ? 40.672 -22.519 4.431   1.00 14.65 ?  97  GLY   B H    1 
ATOM   5393 H HA2  . GLY   B 1 97  ? 38.068 -22.944 4.866   1.00 15.38 ?  97  GLY   B HA2  1 
ATOM   5394 H HA3  . GLY   B 1 97  ? 39.095 -24.000 4.297   1.00 15.38 ?  97  GLY   B HA3  1 
ATOM   5395 N N    . PRO   B 1 98  ? 38.036 -24.629 6.809   1.00 14.57 ?  98  PRO   B N    1 
ATOM   5396 C CA   . PRO   B 1 98  ? 38.129 -25.324 8.096   1.00 15.33 ?  98  PRO   B CA   1 
ATOM   5397 C C    . PRO   B 1 98  ? 39.153 -26.445 8.053   1.00 14.91 ?  98  PRO   B C    1 
ATOM   5398 O O    . PRO   B 1 98  ? 39.262 -27.177 7.070   1.00 15.33 ?  98  PRO   B O    1 
ATOM   5399 C CB   . PRO   B 1 98  ? 36.711 -25.866 8.304   1.00 15.39 ?  98  PRO   B CB   1 
ATOM   5400 C CG   . PRO   B 1 98  ? 36.153 -25.997 6.932   1.00 15.15 ?  98  PRO   B CG   1 
ATOM   5401 C CD   . PRO   B 1 98  ? 36.719 -24.824 6.174   1.00 14.45 ?  98  PRO   B CD   1 
ATOM   5402 H HA   . PRO   B 1 98  ? 38.352 -24.700 8.800   1.00 18.41 ?  98  PRO   B HA   1 
ATOM   5403 H HB2  . PRO   B 1 98  ? 36.754 -26.732 8.740   1.00 18.49 ?  98  PRO   B HB2  1 
ATOM   5404 H HB3  . PRO   B 1 98  ? 36.193 -25.239 8.827   1.00 18.49 ?  98  PRO   B HB3  1 
ATOM   5405 H HG2  . PRO   B 1 98  ? 36.446 -26.835 6.538   1.00 18.20 ?  98  PRO   B HG2  1 
ATOM   5406 H HG3  . PRO   B 1 98  ? 35.186 -25.953 6.967   1.00 18.20 ?  98  PRO   B HG3  1 
ATOM   5407 H HD2  . PRO   B 1 98  ? 36.813 -25.044 5.230   1.00 17.35 ?  98  PRO   B HD2  1 
ATOM   5408 H HD3  . PRO   B 1 98  ? 36.162 -24.038 6.299   1.00 17.35 ?  98  PRO   B HD3  1 
ATOM   5409 N N    . ASN   B 1 99  ? 39.905 -26.574 9.138   1.00 16.04 ?  99  ASN   B N    1 
ATOM   5410 C CA   . ASN   B 1 99  ? 40.882 -27.647 9.299   1.00 16.68 ?  99  ASN   B CA   1 
ATOM   5411 C C    . ASN   B 1 99  ? 40.256 -28.736 10.170  1.00 19.22 ?  99  ASN   B C    1 
ATOM   5412 O O    . ASN   B 1 99  ? 40.182 -28.599 11.393  1.00 19.77 ?  99  ASN   B O    1 
ATOM   5413 C CB   . ASN   B 1 99  ? 42.152 -27.090 9.926   1.00 17.11 ?  99  ASN   B CB   1 
ATOM   5414 C CG   . ASN   B 1 99  ? 43.285 -28.092 9.932   1.00 17.96 ?  99  ASN   B CG   1 
ATOM   5415 O OD1  . ASN   B 1 99  ? 43.063 -29.287 10.088  1.00 18.65 ?  99  ASN   B OD1  1 
ATOM   5416 N ND2  . ASN   B 1 99  ? 44.503 -27.610 9.755   1.00 18.22 ?  99  ASN   B ND2  1 
ATOM   5417 H H    . ASN   B 1 99  ? 39.865 -26.039 9.807   1.00 19.27 ?  99  ASN   B H    1 
ATOM   5418 H HA   . ASN   B 1 99  ? 41.095 -28.030 8.434   1.00 20.03 ?  99  ASN   B HA   1 
ATOM   5419 H HB2  . ASN   B 1 99  ? 42.431 -26.314 9.425   1.00 20.55 ?  99  ASN   B HB2  1 
ATOM   5420 H HB3  . ASN   B 1 99  ? 41.959 -26.844 10.846  1.00 20.55 ?  99  ASN   B HB3  1 
ATOM   5421 H HD21 . ASN   B 1 99  ? 45.176 -28.142 9.747   1.00 21.88 ?  99  ASN   B HD21 1 
ATOM   5422 H HD22 . ASN   B 1 99  ? 44.615 -26.765 9.651   1.00 21.88 ?  99  ASN   B HD22 1 
ATOM   5423 N N    A VAL   B 1 100 ? 39.787 -29.812 9.532   0.72 21.14 ?  100 VAL   B N    1 
ATOM   5424 N N    B VAL   B 1 100 ? 39.806 -29.818 9.526   0.28 21.14 ?  100 VAL   B N    1 
ATOM   5425 C CA   A VAL   B 1 100 ? 39.174 -30.913 10.276  0.72 23.83 ?  100 VAL   B CA   1 
ATOM   5426 C CA   B VAL   B 1 100 ? 39.184 -30.925 10.251  0.28 23.33 ?  100 VAL   B CA   1 
ATOM   5427 C C    A VAL   B 1 100 ? 40.179 -31.577 11.210  0.72 24.24 ?  100 VAL   B C    1 
ATOM   5428 C C    B VAL   B 1 100 ? 40.178 -31.581 11.199  0.28 24.04 ?  100 VAL   B C    1 
ATOM   5429 O O    A VAL   B 1 100 ? 39.802 -32.094 12.270  0.72 24.66 ?  100 VAL   B O    1 
ATOM   5430 O O    B VAL   B 1 100 ? 39.794 -32.082 12.264  0.28 24.22 ?  100 VAL   B O    1 
ATOM   5431 C CB   A VAL   B 1 100 ? 38.522 -31.923 9.309   0.72 26.13 ?  100 VAL   B CB   1 
ATOM   5432 C CB   B VAL   B 1 100 ? 38.571 -31.935 9.258   0.28 24.74 ?  100 VAL   B CB   1 
ATOM   5433 C CG1  A VAL   B 1 100 ? 38.035 -33.152 10.063  0.72 27.15 ?  100 VAL   B CG1  1 
ATOM   5434 C CG1  B VAL   B 1 100 ? 38.063 -33.170 9.987   0.28 25.30 ?  100 VAL   B CG1  1 
ATOM   5435 C CG2  A VAL   B 1 100 ? 37.368 -31.273 8.562   0.72 26.79 ?  100 VAL   B CG2  1 
ATOM   5436 C CG2  B VAL   B 1 100 ? 37.445 -31.283 8.471   0.28 25.20 ?  100 VAL   B CG2  1 
ATOM   5437 H H    A VAL   B 1 100 ? 39.794 -29.916 8.677   0.72 25.39 ?  100 VAL   B H    1 
ATOM   5438 H H    B VAL   B 1 100 ? 39.847 -29.932 8.674   0.28 25.39 ?  100 VAL   B H    1 
ATOM   5439 H HA   A VAL   B 1 100 ? 38.461 -30.548 10.825  0.72 28.62 ?  100 VAL   B HA   1 
ATOM   5440 H HA   B VAL   B 1 100 ? 38.458 -30.573 10.786  0.28 28.02 ?  100 VAL   B HA   1 
ATOM   5441 H HB   A VAL   B 1 100 ? 39.181 -32.214 8.661   0.72 31.38 ?  100 VAL   B HB   1 
ATOM   5442 H HB   B VAL   B 1 100 ? 39.252 -32.219 8.629   0.28 29.71 ?  100 VAL   B HB   1 
ATOM   5443 H HG11 A VAL   B 1 100 ? 37.446 -33.663 9.483   0.72 32.60 ?  100 VAL   B HG11 1 
ATOM   5444 H HG11 B VAL   B 1 100 ? 37.496 -33.680 9.386   0.28 30.38 ?  100 VAL   B HG11 1 
ATOM   5445 H HG12 A VAL   B 1 100 ? 38.797 -33.697 10.317  0.72 32.60 ?  100 VAL   B HG12 1 
ATOM   5446 H HG12 B VAL   B 1 100 ? 38.818 -33.711 10.264  0.28 30.38 ?  100 VAL   B HG12 1 
ATOM   5447 H HG13 A VAL   B 1 100 ? 37.550 -32.868 10.854  0.72 32.60 ?  100 VAL   B HG13 1 
ATOM   5448 H HG13 B VAL   B 1 100 ? 37.551 -32.891 10.762  0.28 30.38 ?  100 VAL   B HG13 1 
ATOM   5449 H HG21 A VAL   B 1 100 ? 36.972 -31.926 7.962   0.72 32.17 ?  100 VAL   B HG21 1 
ATOM   5450 H HG21 B VAL   B 1 100 ? 37.063 -31.938 7.865   0.28 30.26 ?  100 VAL   B HG21 1 
ATOM   5451 H HG22 A VAL   B 1 100 ? 36.704 -30.973 9.205   0.72 32.17 ?  100 VAL   B HG22 1 
ATOM   5452 H HG22 B VAL   B 1 100 ? 36.766 -30.972 9.091   0.28 30.26 ?  100 VAL   B HG22 1 
ATOM   5453 H HG23 A VAL   B 1 100 ? 37.704 -30.519 8.056   0.72 32.17 ?  100 VAL   B HG23 1 
ATOM   5454 H HG23 B VAL   B 1 100 ? 37.802 -30.536 7.968   0.28 30.26 ?  100 VAL   B HG23 1 
ATOM   5455 N N    . ASN   B 1 101 ? 41.461 -31.602 10.834  1.00 24.62 ?  101 ASN   B N    1 
ATOM   5456 C CA   . ASN   B 1 101 ? 42.493 -32.138 11.720  1.00 26.31 ?  101 ASN   B CA   1 
ATOM   5457 C C    . ASN   B 1 101 ? 42.678 -31.305 12.982  1.00 28.57 ?  101 ASN   B C    1 
ATOM   5458 O O    . ASN   B 1 101 ? 43.311 -31.784 13.931  1.00 29.74 ?  101 ASN   B O    1 
ATOM   5459 C CB   . ASN   B 1 101 ? 43.827 -32.263 10.977  1.00 26.26 ?  101 ASN   B CB   1 
ATOM   5460 C CG   . ASN   B 1 101 ? 43.835 -33.411 9.986   1.00 25.93 ?  101 ASN   B CG   1 
ATOM   5461 O OD1  . ASN   B 1 101 ? 43.188 -34.428 10.205  1.00 26.85 ?  101 ASN   B OD1  1 
ATOM   5462 N ND2  . ASN   B 1 101 ? 44.562 -33.249 8.889   1.00 25.46 ?  101 ASN   B ND2  1 
ATOM   5463 H H    A ASN   B 1 101 ? 41.752 -31.333 10.070  0.72 29.57 ?  101 ASN   B H    1 
ATOM   5464 H H    B ASN   B 1 101 ? 41.756 -31.321 10.076  0.28 29.57 ?  101 ASN   B H    1 
ATOM   5465 H HA   . ASN   B 1 101 ? 42.229 -33.025 11.999  1.00 31.59 ?  101 ASN   B HA   1 
ATOM   5466 H HB2  . ASN   B 1 101 ? 44.002 -31.447 10.486  1.00 31.53 ?  101 ASN   B HB2  1 
ATOM   5467 H HB3  . ASN   B 1 101 ? 44.537 -32.417 11.624  1.00 31.53 ?  101 ASN   B HB3  1 
ATOM   5468 H HD21 . ASN   B 1 101 ? 44.597 -33.875 8.300   1.00 30.58 ?  101 ASN   B HD21 1 
ATOM   5469 H HD22 . ASN   B 1 101 ? 44.993 -32.516 8.765   1.00 30.58 ?  101 ASN   B HD22 1 
ATOM   5470 N N    . LYS   B 1 102 ? 42.157 -30.077 13.008  1.00 30.84 ?  102 LYS   B N    1 
ATOM   5471 C CA   . LYS   B 1 102 ? 42.126 -29.241 14.200  1.00 33.45 ?  102 LYS   B CA   1 
ATOM   5472 C C    . LYS   B 1 102 ? 40.746 -29.201 14.846  1.00 33.10 ?  102 LYS   B C    1 
ATOM   5473 O O    . LYS   B 1 102 ? 40.528 -28.410 15.768  1.00 33.90 ?  102 LYS   B O    1 
ATOM   5474 C CB   . LYS   B 1 102 ? 42.555 -27.812 13.859  1.00 36.60 ?  102 LYS   B CB   1 
ATOM   5475 C CG   . LYS   B 1 102 ? 44.015 -27.645 13.474  1.00 39.64 ?  102 LYS   B CG   1 
ATOM   5476 C CD   . LYS   B 1 102 ? 44.255 -26.232 12.962  1.00 42.39 ?  102 LYS   B CD   1 
ATOM   5477 C CE   . LYS   B 1 102 ? 45.728 -25.927 12.771  1.00 44.43 ?  102 LYS   B CE   1 
ATOM   5478 N NZ   . LYS   B 1 102 ? 45.923 -24.534 12.273  1.00 45.62 ?  102 LYS   B NZ   1 
ATOM   5479 H H    . LYS   B 1 102 ? 41.807 -29.695 12.322  1.00 37.03 ?  102 LYS   B H    1 
ATOM   5480 H HA   . LYS   B 1 102 ? 42.755 -29.591 14.850  1.00 40.16 ?  102 LYS   B HA   1 
ATOM   5481 H HB2  . LYS   B 1 102 ? 42.021 -27.499 13.113  1.00 43.94 ?  102 LYS   B HB2  1 
ATOM   5482 H HB3  . LYS   B 1 102 ? 42.393 -27.248 14.632  1.00 43.94 ?  102 LYS   B HB3  1 
ATOM   5483 H HG2  . LYS   B 1 102 ? 44.577 -27.790 14.252  1.00 47.58 ?  102 LYS   B HG2  1 
ATOM   5484 H HG3  . LYS   B 1 102 ? 44.241 -28.271 12.769  1.00 47.58 ?  102 LYS   B HG3  1 
ATOM   5485 H HD2  . LYS   B 1 102 ? 43.812 -26.126 12.105  1.00 50.89 ?  102 LYS   B HD2  1 
ATOM   5486 H HD3  . LYS   B 1 102 ? 43.896 -25.598 13.602  1.00 50.89 ?  102 LYS   B HD3  1 
ATOM   5487 H HE2  . LYS   B 1 102 ? 46.188 -26.016 13.622  1.00 53.33 ?  102 LYS   B HE2  1 
ATOM   5488 H HE3  . LYS   B 1 102 ? 46.103 -26.541 12.120  1.00 53.33 ?  102 LYS   B HE3  1 
ATOM   5489 H HZ1  . LYS   B 1 102 ? 46.790 -24.367 12.165  1.00 54.77 ?  102 LYS   B HZ1  1 
ATOM   5490 H HZ2  . LYS   B 1 102 ? 45.508 -24.431 11.492  1.00 54.77 ?  102 LYS   B HZ2  1 
ATOM   5491 H HZ3  . LYS   B 1 102 ? 45.586 -23.953 12.857  1.00 54.77 ?  102 LYS   B HZ3  1 
ATOM   5492 N N    . GLY   B 1 103 ? 39.806 -30.014 14.370  1.00 32.24 ?  103 GLY   B N    1 
ATOM   5493 C CA   . GLY   B 1 103 ? 38.478 -30.059 14.948  1.00 31.76 ?  103 GLY   B CA   1 
ATOM   5494 C C    . GLY   B 1 103 ? 37.539 -28.964 14.495  1.00 30.74 ?  103 GLY   B C    1 
ATOM   5495 O O    . GLY   B 1 103 ? 36.450 -28.829 15.066  1.00 31.15 ?  103 GLY   B O    1 
ATOM   5496 H H    . GLY   B 1 103 ? 39.917 -30.549 13.707  1.00 38.71 ?  103 GLY   B H    1 
ATOM   5497 H HA2  . GLY   B 1 103 ? 38.070 -30.910 14.727  1.00 38.13 ?  103 GLY   B HA2  1 
ATOM   5498 H HA3  . GLY   B 1 103 ? 38.556 -30.008 15.915  1.00 38.13 ?  103 GLY   B HA3  1 
ATOM   5499 N N    A GLU   B 1 104 ? 37.924 -28.179 13.492  0.72 29.50 ?  104 GLU   B N    1 
ATOM   5500 N N    B GLU   B 1 104 ? 37.913 -28.181 13.489  0.28 30.19 ?  104 GLU   B N    1 
ATOM   5501 C CA   A GLU   B 1 104 ? 37.086 -27.089 13.018  0.72 28.15 ?  104 GLU   B CA   1 
ATOM   5502 C CA   B GLU   B 1 104 ? 37.069 -27.089 13.030  0.28 29.43 ?  104 GLU   B CA   1 
ATOM   5503 C C    A GLU   B 1 104 ? 35.913 -27.631 12.200  0.72 28.55 ?  104 GLU   B C    1 
ATOM   5504 C C    B GLU   B 1 104 ? 35.903 -27.619 12.201  0.28 29.51 ?  104 GLU   B C    1 
ATOM   5505 O O    A GLU   B 1 104 ? 35.960 -28.730 11.638  0.72 29.23 ?  104 GLU   B O    1 
ATOM   5506 O O    B GLU   B 1 104 ? 35.983 -28.683 11.580  0.28 29.80 ?  104 GLU   B O    1 
ATOM   5507 C CB   A GLU   B 1 104 ? 37.927 -26.092 12.215  0.72 26.80 ?  104 GLU   B CB   1 
ATOM   5508 C CB   B GLU   B 1 104 ? 37.899 -26.088 12.227  0.28 28.62 ?  104 GLU   B CB   1 
ATOM   5509 C CG   A GLU   B 1 104 ? 39.032 -25.457 13.056  0.72 25.46 ?  104 GLU   B CG   1 
ATOM   5510 C CG   B GLU   B 1 104 ? 38.999 -25.442 13.061  0.28 27.88 ?  104 GLU   B CG   1 
ATOM   5511 C CD   A GLU   B 1 104 ? 39.967 -24.559 12.273  0.72 24.07 ?  104 GLU   B CD   1 
ATOM   5512 C CD   B GLU   B 1 104 ? 39.938 -24.577 12.245  0.28 27.23 ?  104 GLU   B CD   1 
ATOM   5513 O OE1  A GLU   B 1 104 ? 39.966 -24.605 11.025  0.72 22.32 ?  104 GLU   B OE1  1 
ATOM   5514 O OE1  B GLU   B 1 104 ? 39.856 -24.605 10.999  0.28 26.71 ?  104 GLU   B OE1  1 
ATOM   5515 O OE2  A GLU   B 1 104 ? 40.714 -23.800 12.925  0.72 24.28 -1 104 GLU   B OE2  1 
ATOM   5516 O OE2  B GLU   B 1 104 ? 40.763 -23.866 12.857  0.28 27.19 -1 104 GLU   B OE2  1 
ATOM   5517 H H    A GLU   B 1 104 ? 38.673 -28.254 13.077  0.72 35.42 ?  104 GLU   B H    1 
ATOM   5518 H H    B GLU   B 1 104 ? 38.652 -28.260 13.058  0.28 36.25 ?  104 GLU   B H    1 
ATOM   5519 H HA   A GLU   B 1 104 ? 36.726 -26.618 13.785  0.72 33.80 ?  104 GLU   B HA   1 
ATOM   5520 H HA   B GLU   B 1 104 ? 36.705 -26.624 13.800  0.28 35.34 ?  104 GLU   B HA   1 
ATOM   5521 H HB2  A GLU   B 1 104 ? 38.343 -26.551 11.469  0.72 32.18 ?  104 GLU   B HB2  1 
ATOM   5522 H HB2  B GLU   B 1 104 ? 38.316 -26.547 11.482  0.28 34.37 ?  104 GLU   B HB2  1 
ATOM   5523 H HB3  A GLU   B 1 104 ? 37.353 -25.381 11.890  0.72 32.18 ?  104 GLU   B HB3  1 
ATOM   5524 H HB3  B GLU   B 1 104 ? 37.317 -25.383 11.900  0.28 34.37 ?  104 GLU   B HB3  1 
ATOM   5525 H HG2  A GLU   B 1 104 ? 38.631 -24.913 13.750  0.72 30.57 ?  104 GLU   B HG2  1 
ATOM   5526 H HG2  B GLU   B 1 104 ? 38.591 -24.882 13.740  0.28 33.47 ?  104 GLU   B HG2  1 
ATOM   5527 H HG3  A GLU   B 1 104 ? 39.568 -26.159 13.458  0.72 30.57 ?  104 GLU   B HG3  1 
ATOM   5528 H HG3  B GLU   B 1 104 ? 39.525 -26.140 13.484  0.28 33.47 ?  104 GLU   B HG3  1 
ATOM   5529 N N    A ASP   B 1 105 ? 34.842 -26.841 12.150  0.72 28.23 ?  105 ASP   B N    1 
ATOM   5530 N N    B ASP   B 1 105 ? 34.808 -26.861 12.202  0.28 29.16 ?  105 ASP   B N    1 
ATOM   5531 C CA   A ASP   B 1 105 ? 33.565 -27.300 11.616  0.72 28.70 ?  105 ASP   B CA   1 
ATOM   5532 C CA   B ASP   B 1 105 ? 33.552 -27.333 11.632  0.28 28.98 ?  105 ASP   B CA   1 
ATOM   5533 C C    A ASP   B 1 105 ? 33.613 -27.341 10.093  0.72 26.98 ?  105 ASP   B C    1 
ATOM   5534 C C    B ASP   B 1 105 ? 33.632 -27.352 10.109  0.28 27.74 ?  105 ASP   B C    1 
ATOM   5535 O O    A ASP   B 1 105 ? 33.759 -26.302 9.441   0.72 26.17 ?  105 ASP   B O    1 
ATOM   5536 O O    B ASP   B 1 105 ? 33.839 -26.313 9.474   0.28 27.59 ?  105 ASP   B O    1 
ATOM   5537 C CB   A ASP   B 1 105 ? 32.447 -26.370 12.084  0.72 31.47 ?  105 ASP   B CB   1 
ATOM   5538 C CB   B ASP   B 1 105 ? 32.406 -26.435 12.098  0.28 30.03 ?  105 ASP   B CB   1 
ATOM   5539 C CG   A ASP   B 1 105 ? 31.071 -26.841 11.648  0.72 33.88 ?  105 ASP   B CG   1 
ATOM   5540 C CG   B ASP   B 1 105 ? 31.041 -27.017 11.773  0.28 30.91 ?  105 ASP   B CG   1 
ATOM   5541 O OD1  A ASP   B 1 105 ? 30.973 -27.925 11.034  0.72 34.22 ?  105 ASP   B OD1  1 
ATOM   5542 O OD1  B ASP   B 1 105 ? 30.979 -28.010 11.019  0.28 31.13 ?  105 ASP   B OD1  1 
ATOM   5543 O OD2  A ASP   B 1 105 ? 30.082 -26.124 11.919  0.72 35.24 -1 105 ASP   B OD2  1 
ATOM   5544 O OD2  B ASP   B 1 105 ? 30.030 -26.487 12.280  0.28 31.11 -1 105 ASP   B OD2  1 
ATOM   5545 H H    A ASP   B 1 105 ? 34.834 -26.026 12.424  0.72 33.89 ?  105 ASP   B H    1 
ATOM   5546 H H    B ASP   B 1 105 ? 34.769 -26.067 12.528  0.28 35.02 ?  105 ASP   B H    1 
ATOM   5547 H HA   A ASP   B 1 105 ? 33.382 -28.194 11.943  0.72 34.46 ?  105 ASP   B HA   1 
ATOM   5548 H HA   B ASP   B 1 105 ? 33.373 -28.235 11.942  0.28 34.80 ?  105 ASP   B HA   1 
ATOM   5549 H HB2  A ASP   B 1 105 ? 32.468 -26.316 13.053  0.72 37.79 ?  105 ASP   B HB2  1 
ATOM   5550 H HB2  B ASP   B 1 105 ? 32.462 -26.322 13.061  0.28 36.05 ?  105 ASP   B HB2  1 
ATOM   5551 H HB3  A ASP   B 1 105 ? 32.589 -25.490 11.701  0.72 37.79 ?  105 ASP   B HB3  1 
ATOM   5552 H HB3  B ASP   B 1 105 ? 32.482 -25.571 11.660  0.28 36.05 ?  105 ASP   B HB3  1 
ATOM   5553 N N    . ILE   B 1 106 ? 33.455 -28.542 9.527   1.00 26.69 ?  106 ILE   B N    1 
ATOM   5554 C CA   . ILE   B 1 106 ? 33.460 -28.703 8.076   1.00 25.18 ?  106 ILE   B CA   1 
ATOM   5555 C C    . ILE   B 1 106 ? 32.363 -27.881 7.402   1.00 23.82 ?  106 ILE   B C    1 
ATOM   5556 O O    . ILE   B 1 106 ? 32.466 -27.570 6.211   1.00 22.53 ?  106 ILE   B O    1 
ATOM   5557 C CB   . ILE   B 1 106 ? 33.371 -30.209 7.730   1.00 25.91 ?  106 ILE   B CB   1 
ATOM   5558 C CG1  . ILE   B 1 106 ? 33.645 -30.451 6.246   1.00 26.35 ?  106 ILE   B CG1  1 
ATOM   5559 C CG2  . ILE   B 1 106 ? 32.008 -30.776 8.112   1.00 26.91 ?  106 ILE   B CG2  1 
ATOM   5560 C CD1  . ILE   B 1 106 ? 35.008 -29.979 5.802   1.00 26.50 ?  106 ILE   B CD1  1 
ATOM   5561 H H    A ILE   B 1 106 ? 33.345 -29.274 9.964   0.72 32.05 ?  106 ILE   B H    1 
ATOM   5562 H H    B ILE   B 1 106 ? 33.337 -29.275 9.959   0.28 32.05 ?  106 ILE   B H    1 
ATOM   5563 H HA   . ILE   B 1 106 ? 34.307 -28.375 7.746   1.00 30.24 ?  106 ILE   B HA   1 
ATOM   5564 H HB   . ILE   B 1 106 ? 34.046 -30.679 8.244   1.00 31.12 ?  106 ILE   B HB   1 
ATOM   5565 H HG12 . ILE   B 1 106 ? 33.594 -31.406 6.070   1.00 31.64 ?  106 ILE   B HG12 1 
ATOM   5566 H HG13 . ILE   B 1 106 ? 32.981 -29.985 5.720   1.00 31.64 ?  106 ILE   B HG13 1 
ATOM   5567 H HG21 . ILE   B 1 106 ? 32.028 -31.741 8.011   1.00 32.32 ?  106 ILE   B HG21 1 
ATOM   5568 H HG22 . ILE   B 1 106 ? 31.817 -30.544 9.034   1.00 32.32 ?  106 ILE   B HG22 1 
ATOM   5569 H HG23 . ILE   B 1 106 ? 31.332 -30.397 7.529   1.00 32.32 ?  106 ILE   B HG23 1 
ATOM   5570 H HD11 . ILE   B 1 106 ? 35.220 -30.383 4.947   1.00 31.82 ?  106 ILE   B HD11 1 
ATOM   5571 H HD12 . ILE   B 1 106 ? 34.996 -29.012 5.716   1.00 31.82 ?  106 ILE   B HD12 1 
ATOM   5572 H HD13 . ILE   B 1 106 ? 35.667 -30.244 6.464   1.00 31.82 ?  106 ILE   B HD13 1 
ATOM   5573 N N    A GLN   B 1 107 ? 31.301 -27.536 8.132   0.72 24.22 ?  107 GLN   B N    1 
ATOM   5574 N N    B GLN   B 1 107 ? 31.319 -27.504 8.142   0.28 24.27 ?  107 GLN   B N    1 
ATOM   5575 C CA   A GLN   B 1 107 ? 30.236 -26.712 7.566   0.72 24.91 ?  107 GLN   B CA   1 
ATOM   5576 C CA   B GLN   B 1 107 ? 30.240 -26.708 7.568   0.28 24.71 ?  107 GLN   B CA   1 
ATOM   5577 C C    A GLN   B 1 107 ? 30.739 -25.363 7.065   0.72 22.92 ?  107 GLN   B C    1 
ATOM   5578 C C    B GLN   B 1 107 ? 30.720 -25.343 7.092   0.28 22.83 ?  107 GLN   B C    1 
ATOM   5579 O O    A GLN   B 1 107 ? 30.109 -24.776 6.180   0.72 23.48 ?  107 GLN   B O    1 
ATOM   5580 O O    B GLN   B 1 107 ? 30.050 -24.722 6.260   0.28 23.11 ?  107 GLN   B O    1 
ATOM   5581 C CB   A GLN   B 1 107 ? 29.128 -26.515 8.604   0.72 28.57 ?  107 GLN   B CB   1 
ATOM   5582 C CB   B GLN   B 1 107 ? 29.117 -26.542 8.596   0.28 27.31 ?  107 GLN   B CB   1 
ATOM   5583 C CG   A GLN   B 1 107 ? 27.807 -26.002 8.037   0.72 32.21 ?  107 GLN   B CG   1 
ATOM   5584 C CG   B GLN   B 1 107 ? 27.791 -26.049 8.024   0.28 29.74 ?  107 GLN   B CG   1 
ATOM   5585 C CD   A GLN   B 1 107 ? 27.742 -24.487 7.953   0.72 35.01 ?  107 GLN   B CD   1 
ATOM   5586 C CD   B GLN   B 1 107 ? 27.668 -24.535 8.029   0.28 31.62 ?  107 GLN   B CD   1 
ATOM   5587 O OE1  A GLN   B 1 107 ? 28.575 -23.783 8.526   0.72 36.04 ?  107 GLN   B OE1  1 
ATOM   5588 O OE1  B GLN   B 1 107 ? 28.496 -23.833 8.609   0.28 32.28 ?  107 GLN   B OE1  1 
ATOM   5589 N NE2  A GLN   B 1 107 ? 26.742 -23.976 7.237   0.72 35.97 ?  107 GLN   B NE2  1 
ATOM   5590 N NE2  B GLN   B 1 107 ? 26.624 -24.025 7.383   0.28 32.29 ?  107 GLN   B NE2  1 
ATOM   5591 H H    A GLN   B 1 107 ? 31.167 -27.778 8.942   0.72 29.08 ?  107 GLN   B H    1 
ATOM   5592 H H    B GLN   B 1 107 ? 31.214 -27.693 8.970   0.28 29.14 ?  107 GLN   B H    1 
ATOM   5593 H HA   A GLN   B 1 107 ? 29.849 -27.179 6.810   0.72 29.91 ?  107 GLN   B HA   1 
ATOM   5594 H HA   B GLN   B 1 107 ? 29.875 -27.179 6.802   0.28 29.68 ?  107 GLN   B HA   1 
ATOM   5595 H HB2  A GLN   B 1 107 ? 28.953 -27.366 9.028   0.72 34.31 ?  107 GLN   B HB2  1 
ATOM   5596 H HB2  B GLN   B 1 107 ? 28.953 -27.400 9.009   0.28 32.80 ?  107 GLN   B HB2  1 
ATOM   5597 H HB3  A GLN   B 1 107 ? 29.436 -25.876 9.265   0.72 34.31 ?  107 GLN   B HB3  1 
ATOM   5598 H HB3  B GLN   B 1 107 ? 29.404 -25.905 9.269   0.28 32.80 ?  107 GLN   B HB3  1 
ATOM   5599 H HG2  A GLN   B 1 107 ? 27.685 -26.355 7.143   0.72 38.67 ?  107 GLN   B HG2  1 
ATOM   5600 H HG2  B GLN   B 1 107 ? 27.708 -26.353 7.107   0.28 35.71 ?  107 GLN   B HG2  1 
ATOM   5601 H HG3  A GLN   B 1 107 ? 27.082 -26.303 8.611   0.72 38.67 ?  107 GLN   B HG3  1 
ATOM   5602 H HG3  B GLN   B 1 107 ? 27.065 -26.413 8.558   0.28 35.71 ?  107 GLN   B HG3  1 
ATOM   5603 H HE21 A GLN   B 1 107 ? 26.178 -24.499 6.849   0.72 43.19 ?  107 GLN   B HE21 1 
ATOM   5604 H HE21 B GLN   B 1 107 ? 26.064 -24.546 6.987   0.28 38.76 ?  107 GLN   B HE21 1 
ATOM   5605 H HE22 A GLN   B 1 107 ? 26.656 -23.123 7.161   0.72 43.19 ?  107 GLN   B HE22 1 
ATOM   5606 H HE22 B GLN   B 1 107 ? 26.507 -23.173 7.359   0.28 38.76 ?  107 GLN   B HE22 1 
ATOM   5607 N N    . LEU   B 1 108 ? 31.860 -24.862 7.592   1.00 20.87 ?  108 LEU   B N    1 
ATOM   5608 C CA   . LEU   B 1 108 ? 32.397 -23.564 7.183   1.00 18.52 ?  108 LEU   B CA   1 
ATOM   5609 C C    . LEU   B 1 108 ? 33.048 -23.587 5.809   1.00 16.20 ?  108 LEU   B C    1 
ATOM   5610 O O    . LEU   B 1 108 ? 33.482 -22.529 5.324   1.00 15.68 ?  108 LEU   B O    1 
ATOM   5611 C CB   . LEU   B 1 108 ? 33.401 -23.063 8.219   1.00 19.05 ?  108 LEU   B CB   1 
ATOM   5612 C CG   . LEU   B 1 108 ? 32.775 -22.596 9.531   1.00 20.47 ?  108 LEU   B CG   1 
ATOM   5613 C CD1  . LEU   B 1 108 ? 33.806 -22.560 10.644  1.00 20.57 ?  108 LEU   B CD1  1 
ATOM   5614 C CD2  . LEU   B 1 108 ? 32.149 -21.223 9.348   1.00 21.41 ?  108 LEU   B CD2  1 
ATOM   5615 H H    A LEU   B 1 108 ? 32.324 -25.256 8.197   0.72 25.06 ?  108 LEU   B H    1 
ATOM   5616 H H    B LEU   B 1 108 ? 32.335 -25.268 8.181   0.28 25.06 ?  108 LEU   B H    1 
ATOM   5617 H HA   . LEU   B 1 108 ? 31.666 -22.929 7.146   1.00 22.24 ?  108 LEU   B HA   1 
ATOM   5618 H HB2  . LEU   B 1 108 ? 34.016 -23.779 8.430   1.00 22.89 ?  108 LEU   B HB2  1 
ATOM   5619 H HB3  . LEU   B 1 108 ? 33.884 -22.311 7.844   1.00 22.89 ?  108 LEU   B HB3  1 
ATOM   5620 H HG   . LEU   B 1 108 ? 32.071 -23.213 9.790   1.00 24.58 ?  108 LEU   B HG   1 
ATOM   5621 H HD11 . LEU   B 1 108 ? 33.372 -22.289 11.469  1.00 24.70 ?  108 LEU   B HD11 1 
ATOM   5622 H HD12 . LEU   B 1 108 ? 34.189 -23.444 10.746  1.00 24.70 ?  108 LEU   B HD12 1 
ATOM   5623 H HD13 . LEU   B 1 108 ? 34.498 -21.922 10.410  1.00 24.70 ?  108 LEU   B HD13 1 
ATOM   5624 H HD21 . LEU   B 1 108 ? 31.793 -20.921 10.199  1.00 25.71 ?  108 LEU   B HD21 1 
ATOM   5625 H HD22 . LEU   B 1 108 ? 32.828 -20.606 9.036   1.00 25.71 ?  108 LEU   B HD22 1 
ATOM   5626 H HD23 . LEU   B 1 108 ? 31.433 -21.286 8.695   1.00 25.71 ?  108 LEU   B HD23 1 
ATOM   5627 N N    . LEU   B 1 109 ? 33.118 -24.756 5.177   1.00 15.38 ?  109 LEU   B N    1 
ATOM   5628 C CA   . LEU   B 1 109 ? 33.748 -24.862 3.869   1.00 14.59 ?  109 LEU   B CA   1 
ATOM   5629 C C    . LEU   B 1 109 ? 32.982 -24.076 2.810   1.00 13.96 ?  109 LEU   B C    1 
ATOM   5630 O O    . LEU   B 1 109 ? 33.596 -23.482 1.915   1.00 13.51 ?  109 LEU   B O    1 
ATOM   5631 C CB   . LEU   B 1 109 ? 33.866 -26.337 3.489   1.00 14.67 ?  109 LEU   B CB   1 
ATOM   5632 C CG   . LEU   B 1 109 ? 34.641 -26.677 2.221   1.00 14.46 ?  109 LEU   B CG   1 
ATOM   5633 C CD1  . LEU   B 1 109 ? 36.013 -26.027 2.225   1.00 14.26 ?  109 LEU   B CD1  1 
ATOM   5634 C CD2  . LEU   B 1 109 ? 34.772 -28.185 2.083   1.00 15.35 ?  109 LEU   B CD2  1 
ATOM   5635 H H    . LEU   B 1 109 ? 32.827 -25.505 5.489   1.00 18.48 ?  109 LEU   B H    1 
ATOM   5636 H HA   . LEU   B 1 109 ? 34.644 -24.497 3.920   1.00 17.52 ?  109 LEU   B HA   1 
ATOM   5637 H HB2  . LEU   B 1 109 ? 34.308 -26.803 4.218   1.00 17.62 ?  109 LEU   B HB2  1 
ATOM   5638 H HB3  . LEU   B 1 109 ? 32.972 -26.696 3.380   1.00 17.62 ?  109 LEU   B HB3  1 
ATOM   5639 H HG   . LEU   B 1 109 ? 34.150 -26.356 1.446   1.00 17.37 ?  109 LEU   B HG   1 
ATOM   5640 H HD11 . LEU   B 1 109 ? 36.538 -26.392 1.493   1.00 17.13 ?  109 LEU   B HD11 1 
ATOM   5641 H HD12 . LEU   B 1 109 ? 35.907 -25.073 2.113   1.00 17.13 ?  109 LEU   B HD12 1 
ATOM   5642 H HD13 . LEU   B 1 109 ? 36.447 -26.222 3.069   1.00 17.13 ?  109 LEU   B HD13 1 
ATOM   5643 H HD21 . LEU   B 1 109 ? 35.336 -28.389 1.319   1.00 18.44 ?  109 LEU   B HD21 1 
ATOM   5644 H HD22 . LEU   B 1 109 ? 35.168 -28.544 2.891   1.00 18.44 ?  109 LEU   B HD22 1 
ATOM   5645 H HD23 . LEU   B 1 109 ? 33.889 -28.572 1.950   1.00 18.44 ?  109 LEU   B HD23 1 
ATOM   5646 N N    . LYS   B 1 110 ? 31.648 -24.042 2.891   1.00 13.75 ?  110 LYS   B N    1 
ATOM   5647 C CA   . LYS   B 1 110 ? 30.895 -23.284 1.893   1.00 13.51 ?  110 LYS   B CA   1 
ATOM   5648 C C    . LYS   B 1 110 ? 31.228 -21.794 1.977   1.00 13.13 ?  110 LYS   B C    1 
ATOM   5649 O O    . LYS   B 1 110 ? 31.484 -21.146 0.957   1.00 12.80 ?  110 LYS   B O    1 
ATOM   5650 C CB   . LYS   B 1 110 ? 29.389 -23.529 2.038   1.00 14.10 ?  110 LYS   B CB   1 
ATOM   5651 C CG   . LYS   B 1 110 ? 28.577 -22.917 0.897   1.00 14.25 ?  110 LYS   B CG   1 
ATOM   5652 C CD   . LYS   B 1 110 ? 27.109 -23.339 0.927   1.00 14.78 ?  110 LYS   B CD   1 
ATOM   5653 C CE   . LYS   B 1 110 ? 26.350 -22.820 -0.293  1.00 15.35 ?  110 LYS   B CE   1 
ATOM   5654 N NZ   . LYS   B 1 110 ? 26.685 -23.549 -1.540  1.00 15.87 ?  110 LYS   B NZ   1 
ATOM   5655 H H    . LYS   B 1 110 ? 31.171 -24.436 3.485   1.00 16.52 ?  110 LYS   B H    1 
ATOM   5656 H HA   . LYS   B 1 110 ? 31.156 -23.592 1.008   1.00 16.24 ?  110 LYS   B HA   1 
ATOM   5657 H HB2  . LYS   B 1 110 ? 29.224 -24.489 2.042   1.00 16.94 ?  110 LYS   B HB2  1 
ATOM   5658 H HB3  . LYS   B 1 110 ? 29.083 -23.140 2.870   1.00 16.94 ?  110 LYS   B HB3  1 
ATOM   5659 H HG2  . LYS   B 1 110 ? 28.604 -21.951 0.968   1.00 17.12 ?  110 LYS   B HG2  1 
ATOM   5660 H HG3  . LYS   B 1 110 ? 28.948 -23.202 0.049   1.00 17.12 ?  110 LYS   B HG3  1 
ATOM   5661 H HD2  . LYS   B 1 110 ? 27.051 -24.313 0.928   1.00 17.76 ?  110 LYS   B HD2  1 
ATOM   5662 H HD3  . LYS   B 1 110 ? 26.683 -22.984 1.725   1.00 17.76 ?  110 LYS   B HD3  1 
ATOM   5663 H HE2  . LYS   B 1 110 ? 25.397 -22.915 -0.140  1.00 18.44 ?  110 LYS   B HE2  1 
ATOM   5664 H HE3  . LYS   B 1 110 ? 26.573 -21.885 -0.424  1.00 18.44 ?  110 LYS   B HE3  1 
ATOM   5665 H HZ1  . LYS   B 1 110 ? 26.230 -23.216 -2.224  1.00 19.06 ?  110 LYS   B HZ1  1 
ATOM   5666 H HZ2  . LYS   B 1 110 ? 27.559 -23.475 -1.710  1.00 19.06 ?  110 LYS   B HZ2  1 
ATOM   5667 H HZ3  . LYS   B 1 110 ? 26.486 -24.414 -1.451  1.00 19.06 ?  110 LYS   B HZ3  1 
ATOM   5668 N N    . SER   B 1 111 ? 31.240 -21.241 3.195   1.00 13.42 ?  111 SER   B N    1 
ATOM   5669 C CA   . SER   B 1 111 ? 31.637 -19.846 3.378   1.00 13.34 ?  111 SER   B CA   1 
ATOM   5670 C C    . SER   B 1 111 ? 33.015 -19.585 2.784   1.00 12.89 ?  111 SER   B C    1 
ATOM   5671 O O    . SER   B 1 111 ? 33.239 -18.551 2.135   1.00 12.99 ?  111 SER   B O    1 
ATOM   5672 C CB   . SER   B 1 111 ? 31.635 -19.494 4.865   1.00 14.27 ?  111 SER   B CB   1 
ATOM   5673 O OG   . SER   B 1 111 ? 30.324 -19.491 5.390   1.00 16.15 ?  111 SER   B OG   1 
ATOM   5674 H H    . SER   B 1 111 ? 31.030 -21.655 3.919   1.00 16.12 ?  111 SER   B H    1 
ATOM   5675 H HA   . SER   B 1 111 ? 31.004 -19.274 2.928   1.00 16.03 ?  111 SER   B HA   1 
ATOM   5676 H HB2  . SER   B 1 111 ? 32.160 -20.152 5.348   1.00 17.14 ?  111 SER   B HB2  1 
ATOM   5677 H HB3  . SER   B 1 111 ? 32.016 -18.614 4.982   1.00 17.14 ?  111 SER   B HB3  1 
ATOM   5678 H HG   . SER   B 1 111 ? 30.337 -19.298 6.213   1.00 19.40 ?  111 SER   B HG   1 
ATOM   5679 N N    . ALA   B 1 112 ? 33.956 -20.503 3.008   1.00 12.88 ?  112 ALA   B N    1 
ATOM   5680 C CA   . ALA   B 1 112 ? 35.299 -20.334 2.466   1.00 12.71 ?  112 ALA   B CA   1 
ATOM   5681 C C    . ALA   B 1 112 ? 35.269 -20.237 0.944   1.00 12.19 ?  112 ALA   B C    1 
ATOM   5682 O O    . ALA   B 1 112 ? 35.895 -19.348 0.353   1.00 12.41 ?  112 ALA   B O    1 
ATOM   5683 C CB   . ALA   B 1 112 ? 36.205 -21.475 2.941   1.00 13.25 ?  112 ALA   B CB   1 
ATOM   5684 H H    . ALA   B 1 112 ? 33.843 -21.228 3.469   1.00 15.47 ?  112 ALA   B H    1 
ATOM   5685 H HA   . ALA   B 1 112 ? 35.665 -19.506 2.808   1.00 15.28 ?  112 ALA   B HA   1 
ATOM   5686 H HB1  . ALA   B 1 112 ? 37.097 -21.335 2.578   1.00 15.92 ?  112 ALA   B HB1  1 
ATOM   5687 H HB2  . ALA   B 1 112 ? 36.244 -21.463 3.912   1.00 15.92 ?  112 ALA   B HB2  1 
ATOM   5688 H HB3  . ALA   B 1 112 ? 35.849 -22.316 2.632   1.00 15.92 ?  112 ALA   B HB3  1 
ATOM   5689 N N    . TYR   B 1 113 ? 34.541 -21.144 0.286   1.00 12.01 ?  113 TYR   B N    1 
ATOM   5690 C CA   . TYR   B 1 113 ? 34.464 -21.093 -1.167  1.00 11.79 ?  113 TYR   B CA   1 
ATOM   5691 C C    . TYR   B 1 113 ? 33.756 -19.843 -1.680  1.00 11.58 ?  113 TYR   B C    1 
ATOM   5692 O O    . TYR   B 1 113 ? 34.027 -19.412 -2.804  1.00 11.58 ?  113 TYR   B O    1 
ATOM   5693 C CB   . TYR   B 1 113 ? 33.792 -22.351 -1.716  1.00 11.99 ?  113 TYR   B CB   1 
ATOM   5694 C CG   . TYR   B 1 113 ? 34.754 -23.501 -1.975  1.00 12.19 ?  113 TYR   B CG   1 
ATOM   5695 C CD1  . TYR   B 1 113 ? 35.756 -23.394 -2.931  1.00 12.83 ?  113 TYR   B CD1  1 
ATOM   5696 C CD2  . TYR   B 1 113 ? 34.645 -24.697 -1.281  1.00 12.64 ?  113 TYR   B CD2  1 
ATOM   5697 C CE1  . TYR   B 1 113 ? 36.638 -24.426 -3.174  1.00 12.78 ?  113 TYR   B CE1  1 
ATOM   5698 C CE2  . TYR   B 1 113 ? 35.519 -25.749 -1.523  1.00 13.22 ?  113 TYR   B CE2  1 
ATOM   5699 C CZ   . TYR   B 1 113 ? 36.509 -25.610 -2.478  1.00 13.06 ?  113 TYR   B CZ   1 
ATOM   5700 O OH   . TYR   B 1 113 ? 37.395 -26.631 -2.744  1.00 13.81 ?  113 TYR   B OH   1 
ATOM   5701 H H    . TYR   B 1 113 ? 34.081 -21.778 0.655   1.00 14.43 ?  113 TYR   B H    1 
ATOM   5702 H HA   . TYR   B 1 113 ? 35.366 -21.078 -1.509  1.00 14.16 ?  113 TYR   B HA   1 
ATOM   5703 H HB2  . TYR   B 1 113 ? 33.129 -22.665 -1.076  1.00 14.41 ?  113 TYR   B HB2  1 
ATOM   5704 H HB3  . TYR   B 1 113 ? 33.355 -22.135 -2.555  1.00 14.41 ?  113 TYR   B HB3  1 
ATOM   5705 H HD1  . TYR   B 1 113 ? 35.847 -22.594 -3.405  1.00 15.42 ?  113 TYR   B HD1  1 
ATOM   5706 H HD2  . TYR   B 1 113 ? 33.972 -24.795 -0.650  1.00 15.18 ?  113 TYR   B HD2  1 
ATOM   5707 H HE1  . TYR   B 1 113 ? 37.304 -24.329 -3.821  1.00 15.36 ?  113 TYR   B HE1  1 
ATOM   5708 H HE2  . TYR   B 1 113 ? 35.426 -26.547 -1.058  1.00 15.88 ?  113 TYR   B HE2  1 
ATOM   5709 H HH   . TYR   B 1 113 ? 37.212 -27.300 -2.272  1.00 16.60 ?  113 TYR   B HH   1 
ATOM   5710 N N    . GLU   B 1 114 ? 32.835 -19.265 -0.901  1.00 11.69 ?  114 GLU   B N    1 
ATOM   5711 C CA   . GLU   B 1 114 ? 32.152 -18.061 -1.361  1.00 11.83 ?  114 GLU   B CA   1 
ATOM   5712 C C    . GLU   B 1 114 ? 33.134 -16.936 -1.656  1.00 11.80 ?  114 GLU   B C    1 
ATOM   5713 O O    . GLU   B 1 114 ? 32.852 -16.079 -2.497  1.00 11.79 ?  114 GLU   B O    1 
ATOM   5714 C CB   . GLU   B 1 114 ? 31.093 -17.636 -0.342  1.00 12.38 ?  114 GLU   B CB   1 
ATOM   5715 C CG   . GLU   B 1 114 ? 29.869 -18.547 -0.418  1.00 12.49 ?  114 GLU   B CG   1 
ATOM   5716 C CD   . GLU   B 1 114 ? 28.850 -18.371 0.700   1.00 12.86 ?  114 GLU   B CD   1 
ATOM   5717 O OE1  . GLU   B 1 114 ? 29.142 -17.749 1.742   1.00 12.82 ?  114 GLU   B OE1  1 
ATOM   5718 O OE2  . GLU   B 1 114 ? 27.728 -18.911 0.541   1.00 13.51 -1 114 GLU   B OE2  1 
ATOM   5719 H H    . GLU   B 1 114 ? 32.588 -19.554 -0.127  1.00 14.05 ?  114 GLU   B H    1 
ATOM   5720 H HA   . GLU   B 1 114 ? 31.695 -18.265 -2.188  1.00 14.22 ?  114 GLU   B HA   1 
ATOM   5721 H HB2  . GLU   B 1 114 ? 31.463 -17.697 0.554   1.00 14.88 ?  114 GLU   B HB2  1 
ATOM   5722 H HB3  . GLU   B 1 114 ? 30.810 -16.730 -0.530  1.00 14.88 ?  114 GLU   B HB3  1 
ATOM   5723 H HG2  . GLU   B 1 114 ? 29.417 -18.376 -1.256  1.00 15.01 ?  114 GLU   B HG2  1 
ATOM   5724 H HG3  . GLU   B 1 114 ? 30.175 -19.467 -0.393  1.00 15.01 ?  114 GLU   B HG3  1 
ATOM   5725 N N    . ASN   B 1 115 ? 34.297 -16.924 -0.998  1.00 11.52 ?  115 ASN   B N    1 
ATOM   5726 C CA   . ASN   B 1 115 ? 35.295 -15.900 -1.300  1.00 11.36 ?  115 ASN   B CA   1 
ATOM   5727 C C    . ASN   B 1 115 ? 35.701 -15.922 -2.768  1.00 10.89 ?  115 ASN   B C    1 
ATOM   5728 O O    . ASN   B 1 115 ? 36.085 -14.883 -3.326  1.00 11.89 ?  115 ASN   B O    1 
ATOM   5729 C CB   . ASN   B 1 115 ? 36.534 -16.074 -0.415  1.00 11.97 ?  115 ASN   B CB   1 
ATOM   5730 C CG   . ASN   B 1 115 ? 36.260 -15.812 1.043   1.00 12.40 ?  115 ASN   B CG   1 
ATOM   5731 O OD1  . ASN   B 1 115 ? 36.267 -14.665 1.487   1.00 14.19 ?  115 ASN   B OD1  1 
ATOM   5732 N ND2  . ASN   B 1 115 ? 36.087 -16.878 1.817   1.00 12.38 ?  115 ASN   B ND2  1 
ATOM   5733 H H    . ASN   B 1 115 ? 34.526 -17.482 -0.378  1.00 13.84 ?  115 ASN   B H    1 
ATOM   5734 H HA   . ASN   B 1 115 ? 34.921 -15.029 -1.110  1.00 13.65 ?  115 ASN   B HA   1 
ATOM   5735 H HB2  . ASN   B 1 115 ? 36.865 -16.981 -0.499  1.00 14.39 ?  115 ASN   B HB2  1 
ATOM   5736 H HB3  . ASN   B 1 115 ? 37.220 -15.446 -0.700  1.00 14.39 ?  115 ASN   B HB3  1 
ATOM   5737 H HD21 . ASN   B 1 115 ? 35.938 -16.781 2.659   1.00 14.88 ?  115 ASN   B HD21 1 
ATOM   5738 H HD22 . ASN   B 1 115 ? 36.111 -17.668 1.475   1.00 14.88 ?  115 ASN   B HD22 1 
ATOM   5739 N N    . PHE   B 1 116 ? 35.670 -17.100 -3.401  1.00 10.91 ?  116 PHE   B N    1 
ATOM   5740 C CA   . PHE   B 1 116 ? 36.105 -17.194 -4.790  1.00 11.20 ?  116 PHE   B CA   1 
ATOM   5741 C C    . PHE   B 1 116 ? 35.203 -16.370 -5.702  1.00 11.24 ?  116 PHE   B C    1 
ATOM   5742 O O    . PHE   B 1 116 ? 35.643 -15.937 -6.774  1.00 11.61 ?  116 PHE   B O    1 
ATOM   5743 C CB   . PHE   B 1 116 ? 36.075 -18.640 -5.314  1.00 11.12 ?  116 PHE   B CB   1 
ATOM   5744 C CG   . PHE   B 1 116 ? 37.138 -19.596 -4.762  1.00 11.05 ?  116 PHE   B CG   1 
ATOM   5745 C CD1  . PHE   B 1 116 ? 37.791 -19.408 -3.552  1.00 11.77 ?  116 PHE   B CD1  1 
ATOM   5746 C CD2  . PHE   B 1 116 ? 37.444 -20.733 -5.496  1.00 11.48 ?  116 PHE   B CD2  1 
ATOM   5747 C CE1  . PHE   B 1 116 ? 38.723 -20.344 -3.096  1.00 11.97 ?  116 PHE   B CE1  1 
ATOM   5748 C CE2  . PHE   B 1 116 ? 38.369 -21.669 -5.047  1.00 11.50 ?  116 PHE   B CE2  1 
ATOM   5749 C CZ   . PHE   B 1 116 ? 39.000 -21.480 -3.851  1.00 11.74 ?  116 PHE   B CZ   1 
ATOM   5750 H H    . PHE   B 1 116 ? 35.405 -17.845 -3.053  1.00 13.11 ?  116 PHE   B H    1 
ATOM   5751 H HA   . PHE   B 1 116 ? 37.012 -16.863 -4.867  1.00 13.46 ?  116 PHE   B HA   1 
ATOM   5752 H HB2  . PHE   B 1 116 ? 35.203 -19.020 -5.103  1.00 13.37 ?  116 PHE   B HB2  1 
ATOM   5753 H HB3  . PHE   B 1 116 ? 36.181 -18.613 -6.279  1.00 13.37 ?  116 PHE   B HB3  1 
ATOM   5754 H HD1  . PHE   B 1 116 ? 37.591 -18.657 -3.035  1.00 14.15 ?  116 PHE   B HD1  1 
ATOM   5755 H HD2  . PHE   B 1 116 ? 37.006 -20.883 -6.306  1.00 13.79 ?  116 PHE   B HD2  1 
ATOM   5756 H HE1  . PHE   B 1 116 ? 39.156 -20.210 -2.287  1.00 14.38 ?  116 PHE   B HE1  1 
ATOM   5757 H HE2  . PHE   B 1 116 ? 38.557 -22.419 -5.561  1.00 13.82 ?  116 PHE   B HE2  1 
ATOM   5758 H HZ   . PHE   B 1 116 ? 39.633 -22.092 -3.558  1.00 14.10 ?  116 PHE   B HZ   1 
ATOM   5759 N N    . ASN   B 1 117 ? 33.935 -16.167 -5.316  1.00 11.45 ?  117 ASN   B N    1 
ATOM   5760 C CA   . ASN   B 1 117 ? 32.992 -15.465 -6.184  1.00 11.70 ?  117 ASN   B CA   1 
ATOM   5761 C C    . ASN   B 1 117 ? 33.305 -13.986 -6.337  1.00 12.39 ?  117 ASN   B C    1 
ATOM   5762 O O    . ASN   B 1 117 ? 32.706 -13.334 -7.195  1.00 13.18 ?  117 ASN   B O    1 
ATOM   5763 C CB   . ASN   B 1 117 ? 31.564 -15.687 -5.699  1.00 11.78 ?  117 ASN   B CB   1 
ATOM   5764 C CG   . ASN   B 1 117 ? 31.113 -17.098 -5.952  1.00 12.03 ?  117 ASN   B CG   1 
ATOM   5765 O OD1  . ASN   B 1 117 ? 31.469 -17.689 -6.972  1.00 13.02 ?  117 ASN   B OD1  1 
ATOM   5766 N ND2  . ASN   B 1 117 ? 30.375 -17.671 -5.011  1.00 12.22 ?  117 ASN   B ND2  1 
ATOM   5767 H H    . ASN   B 1 117 ? 33.609 -16.421 -4.556  1.00 13.76 ?  117 ASN   B H    1 
ATOM   5768 H HA   . ASN   B 1 117 ? 33.057 -15.862 -7.061  1.00 14.06 ?  117 ASN   B HA   1 
ATOM   5769 H HB2  . ASN   B 1 117 ? 31.519 -15.518 -4.740  1.00 14.16 ?  117 ASN   B HB2  1 
ATOM   5770 H HB3  . ASN   B 1 117 ? 30.972 -15.077 -6.169  1.00 14.16 ?  117 ASN   B HB3  1 
ATOM   5771 H HD21 . ASN   B 1 117 ? 30.094 -18.476 -5.118  1.00 14.69 ?  117 ASN   B HD21 1 
ATOM   5772 H HD22 . ASN   B 1 117 ? 30.154 -17.228 -4.308  1.00 14.69 ?  117 ASN   B HD22 1 
ATOM   5773 N N    . GLN   B 1 118 ? 34.242 -13.458 -5.561  1.00 11.91 ?  118 GLN   B N    1 
ATOM   5774 C CA   . GLN   B 1 118 ? 34.668 -12.070 -5.707  1.00 12.41 ?  118 GLN   B CA   1 
ATOM   5775 C C    . GLN   B 1 118 ? 35.739 -11.880 -6.776  1.00 12.69 ?  118 GLN   B C    1 
ATOM   5776 O O    . GLN   B 1 118 ? 36.209 -10.754 -6.960  1.00 13.71 ?  118 GLN   B O    1 
ATOM   5777 C CB   . GLN   B 1 118 ? 35.144 -11.532 -4.356  1.00 13.11 ?  118 GLN   B CB   1 
ATOM   5778 C CG   . GLN   B 1 118 ? 34.062 -11.580 -3.291  1.00 13.20 ?  118 GLN   B CG   1 
ATOM   5779 C CD   . GLN   B 1 118 ? 32.895 -10.669 -3.611  1.00 13.06 ?  118 GLN   B CD   1 
ATOM   5780 O OE1  . GLN   B 1 118 ? 33.084 -9.523  -4.037  1.00 13.60 ?  118 GLN   B OE1  1 
ATOM   5781 N NE2  . GLN   B 1 118 ? 31.679 -11.165 -3.410  1.00 13.41 ?  118 GLN   B NE2  1 
ATOM   5782 H H    . GLN   B 1 118 ? 34.667 -13.880 -4.938  1.00 14.32 ?  118 GLN   B H    1 
ATOM   5783 H HA   . GLN   B 1 118 ? 33.901 -11.543 -5.980  1.00 14.91 ?  118 GLN   B HA   1 
ATOM   5784 H HB2  . GLN   B 1 118 ? 35.895 -12.055 -4.049  1.00 15.75 ?  118 GLN   B HB2  1 
ATOM   5785 H HB3  . GLN   B 1 118 ? 35.412 -10.599 -4.464  1.00 15.75 ?  118 GLN   B HB3  1 
ATOM   5786 H HG2  . GLN   B 1 118 ? 33.725 -12.487 -3.223  1.00 15.86 ?  118 GLN   B HG2  1 
ATOM   5787 H HG3  . GLN   B 1 118 ? 34.438 -11.300 -2.442  1.00 15.86 ?  118 GLN   B HG3  1 
ATOM   5788 H HE21 . GLN   B 1 118 ? 31.588 -11.966 -3.107  1.00 16.11 ?  118 GLN   B HE21 1 
ATOM   5789 H HE22 . GLN   B 1 118 ? 30.989 -10.686 -3.577  1.00 16.11 ?  118 GLN   B HE22 1 
ATOM   5790 N N    . HIS   B 1 119 ? 36.092 -12.939 -7.508  1.00 11.84 ?  119 HIS   B N    1 
ATOM   5791 C CA   . HIS   B 1 119 ? 37.133 -12.898 -8.526  1.00 12.13 ?  119 HIS   B CA   1 
ATOM   5792 C C    . HIS   B 1 119 ? 36.652 -13.628 -9.765  1.00 11.93 ?  119 HIS   B C    1 
ATOM   5793 O O    . HIS   B 1 119 ? 36.145 -14.746 -9.665  1.00 12.82 ?  119 HIS   B O    1 
ATOM   5794 C CB   . HIS   B 1 119 ? 38.410 -13.531 -7.974  1.00 12.85 ?  119 HIS   B CB   1 
ATOM   5795 C CG   . HIS   B 1 119 ? 38.893 -12.829 -6.749  1.00 13.97 ?  119 HIS   B CG   1 
ATOM   5796 N ND1  . HIS   B 1 119 ? 39.693 -11.708 -6.805  1.00 15.38 ?  119 HIS   B ND1  1 
ATOM   5797 C CD2  . HIS   B 1 119 ? 38.596 -13.019 -5.443  1.00 15.08 ?  119 HIS   B CD2  1 
ATOM   5798 C CE1  . HIS   B 1 119 ? 39.900 -11.263 -5.580  1.00 16.53 ?  119 HIS   B CE1  1 
ATOM   5799 N NE2  . HIS   B 1 119 ? 39.240 -12.035 -4.735  1.00 16.38 ?  119 HIS   B NE2  1 
ATOM   5800 H H    . HIS   B 1 119 ? 35.722 -13.719 -7.439  1.00 14.23 ?  119 HIS   B H    1 
ATOM   5801 H HA   . HIS   B 1 119 ? 37.319 -11.975 -8.765  1.00 14.58 ?  119 HIS   B HA   1 
ATOM   5802 H HB2  . HIS   B 1 119 ? 38.236 -14.457 -7.746  1.00 15.44 ?  119 HIS   B HB2  1 
ATOM   5803 H HB3  . HIS   B 1 119 ? 39.110 -13.479 -8.646  1.00 15.44 ?  119 HIS   B HB3  1 
ATOM   5804 H HD2  . HIS   B 1 119 ? 38.058 -13.695 -5.089  1.00 18.12 ?  119 HIS   B HD2  1 
ATOM   5805 H HE1  . HIS   B 1 119 ? 40.432 -10.540 -5.348  1.00 19.85 ?  119 HIS   B HE1  1 
ATOM   5806 H HE2  . HIS   B 1 119 ? 39.241 -11.956 -3.877  1.00 19.68 ?  119 HIS   B HE2  1 
ATOM   5807 N N    . GLU   B 1 120 ? 36.812 -13.009 -10.935 1.00 12.57 ?  120 GLU   B N    1 
ATOM   5808 C CA   . GLU   B 1 120 ? 36.221 -13.596 -12.134 1.00 14.11 ?  120 GLU   B CA   1 
ATOM   5809 C C    . GLU   B 1 120 ? 36.900 -14.895 -12.549 1.00 13.21 ?  120 GLU   B C    1 
ATOM   5810 O O    . GLU   B 1 120 ? 36.238 -15.770 -13.117 1.00 13.19 ?  120 GLU   B O    1 
ATOM   5811 C CB   . GLU   B 1 120 ? 36.213 -12.588 -13.279 1.00 18.49 ?  120 GLU   B CB   1 
ATOM   5812 C CG   . GLU   B 1 120 ? 35.233 -11.451 -13.057 1.00 24.39 ?  120 GLU   B CG   1 
ATOM   5813 C CD   . GLU   B 1 120 ? 35.066 -10.571 -14.276 1.00 29.81 ?  120 GLU   B CD   1 
ATOM   5814 O OE1  . GLU   B 1 120 ? 36.066 -10.341 -14.989 1.00 31.89 ?  120 GLU   B OE1  1 
ATOM   5815 O OE2  . GLU   B 1 120 ? 33.930 -10.111 -14.521 1.00 32.41 -1 120 GLU   B OE2  1 
ATOM   5816 H H    . GLU   B 1 120 ? 37.236 -12.268 -11.059 1.00 15.11 ?  120 GLU   B H    1 
ATOM   5817 H HA   . GLU   B 1 120 ? 35.297 -13.809 -11.939 1.00 16.95 ?  120 GLU   B HA   1 
ATOM   5818 H HB2  . GLU   B 1 120 ? 37.095 -12.203 -13.375 1.00 22.21 ?  120 GLU   B HB2  1 
ATOM   5819 H HB3  . GLU   B 1 120 ? 35.957 -13.042 -14.100 1.00 22.21 ?  120 GLU   B HB3  1 
ATOM   5820 H HG2  . GLU   B 1 120 ? 34.361 -11.820 -12.837 1.00 29.29 ?  120 GLU   B HG2  1 
ATOM   5821 H HG3  . GLU   B 1 120 ? 35.549 -10.896 -12.329 1.00 29.29 ?  120 GLU   B HG3  1 
ATOM   5822 N N    . VAL   B 1 121 ? 38.199 -15.041 -12.290 1.00 12.71 ?  121 VAL   B N    1 
ATOM   5823 C CA   . VAL   B 1 121 ? 38.942 -16.252 -12.635 1.00 12.55 ?  121 VAL   B CA   1 
ATOM   5824 C C    . VAL   B 1 121 ? 40.054 -16.453 -11.614 1.00 11.93 ?  121 VAL   B C    1 
ATOM   5825 O O    . VAL   B 1 121 ? 40.730 -15.495 -11.221 1.00 12.75 ?  121 VAL   B O    1 
ATOM   5826 C CB   . VAL   B 1 121 ? 39.460 -16.207 -14.092 1.00 14.16 ?  121 VAL   B CB   1 
ATOM   5827 C CG1  . VAL   B 1 121 ? 40.323 -14.971 -14.342 1.00 15.32 ?  121 VAL   B CG1  1 
ATOM   5828 C CG2  . VAL   B 1 121 ? 40.207 -17.492 -14.444 1.00 15.48 ?  121 VAL   B CG2  1 
ATOM   5829 H H    . VAL   B 1 121 ? 38.684 -14.436 -11.918 1.00 15.28 ?  121 VAL   B H    1 
ATOM   5830 H HA   . VAL   B 1 121 ? 38.335 -17.005 -12.569 1.00 15.08 ?  121 VAL   B HA   1 
ATOM   5831 H HB   . VAL   B 1 121 ? 38.693 -16.151 -14.689 1.00 17.01 ?  121 VAL   B HB   1 
ATOM   5832 H HG11 . VAL   B 1 121 ? 40.638 -14.987 -15.259 1.00 18.40 ?  121 VAL   B HG11 1 
ATOM   5833 H HG12 . VAL   B 1 121 ? 39.787 -14.177 -14.189 1.00 18.40 ?  121 VAL   B HG12 1 
ATOM   5834 H HG13 . VAL   B 1 121 ? 41.077 -14.986 -13.733 1.00 18.40 ?  121 VAL   B HG13 1 
ATOM   5835 H HG21 . VAL   B 1 121 ? 40.413 -17.490 -15.394 1.00 18.60 ?  121 VAL   B HG21 1 
ATOM   5836 H HG22 . VAL   B 1 121 ? 41.031 -17.532 -13.932 1.00 18.60 ?  121 VAL   B HG22 1 
ATOM   5837 H HG23 . VAL   B 1 121 ? 39.648 -18.256 -14.232 1.00 18.60 ?  121 VAL   B HG23 1 
ATOM   5838 N N    . LEU   B 1 122 ? 40.236 -17.705 -11.175 1.00 11.47 ?  122 LEU   B N    1 
ATOM   5839 C CA   . LEU   B 1 122 ? 41.220 -18.052 -10.153 1.00 11.18 ?  122 LEU   B CA   1 
ATOM   5840 C C    . LEU   B 1 122 ? 41.877 -19.383 -10.481 1.00 11.19 ?  122 LEU   B C    1 
ATOM   5841 O O    . LEU   B 1 122 ? 41.219 -20.305 -10.985 1.00 12.43 ?  122 LEU   B O    1 
ATOM   5842 C CB   . LEU   B 1 122 ? 40.568 -18.272 -8.774  1.00 12.88 ?  122 LEU   B CB   1 
ATOM   5843 C CG   . LEU   B 1 122 ? 39.535 -17.249 -8.287  1.00 13.03 ?  122 LEU   B CG   1 
ATOM   5844 C CD1  . LEU   B 1 122 ? 38.134 -17.605 -8.761  1.00 14.01 ?  122 LEU   B CD1  1 
ATOM   5845 C CD2  . LEU   B 1 122 ? 39.572 -17.137 -6.776  1.00 12.71 ?  122 LEU   B CD2  1 
ATOM   5846 H H    . LEU   B 1 122 ? 39.789 -18.385 -11.461 1.00 13.78 ?  122 LEU   B H    1 
ATOM   5847 H HA   . LEU   B 1 122 ? 41.896 -17.359 -10.083 1.00 13.43 ?  122 LEU   B HA   1 
ATOM   5848 H HB2  . LEU   B 1 122 ? 40.121 -19.130 -8.788  1.00 15.48 ?  122 LEU   B HB2  1 
ATOM   5849 H HB3  . LEU   B 1 122 ? 41.273 -18.290 -8.110  1.00 15.48 ?  122 LEU   B HB3  1 
ATOM   5850 H HG   . LEU   B 1 122 ? 39.760 -16.379 -8.650  1.00 15.65 ?  122 LEU   B HG   1 
ATOM   5851 H HD11 . LEU   B 1 122 ? 37.506 -16.958 -8.397  1.00 16.83 ?  122 LEU   B HD11 1 
ATOM   5852 H HD12 . LEU   B 1 122 ? 38.112 -17.572 -9.730  1.00 16.83 ?  122 LEU   B HD12 1 
ATOM   5853 H HD13 . LEU   B 1 122 ? 37.910 -18.493 -8.451  1.00 16.83 ?  122 LEU   B HD13 1 
ATOM   5854 H HD21 . LEU   B 1 122 ? 38.894 -16.508 -6.485  1.00 15.27 ?  122 LEU   B HD21 1 
ATOM   5855 H HD22 . LEU   B 1 122 ? 39.404 -18.009 -6.387  1.00 15.27 ?  122 LEU   B HD22 1 
ATOM   5856 H HD23 . LEU   B 1 122 ? 40.452 -16.821 -6.503  1.00 15.27 ?  122 LEU   B HD23 1 
ATOM   5857 N N    . LEU   B 1 123 ? 43.162 -19.487 -10.128 1.00 10.94 ?  123 LEU   B N    1 
ATOM   5858 C CA   . LEU   B 1 123 ? 43.872 -20.758 -9.999  1.00 11.16 ?  123 LEU   B CA   1 
ATOM   5859 C C    . LEU   B 1 123 ? 43.843 -21.151 -8.526  1.00 11.05 ?  123 LEU   B C    1 
ATOM   5860 O O    . LEU   B 1 123 ? 44.190 -20.326 -7.671  1.00 11.37 ?  123 LEU   B O    1 
ATOM   5861 C CB   . LEU   B 1 123 ? 45.320 -20.580 -10.461 1.00 11.54 ?  123 LEU   B CB   1 
ATOM   5862 C CG   . LEU   B 1 123 ? 46.266 -21.756 -10.209 1.00 11.76 ?  123 LEU   B CG   1 
ATOM   5863 C CD1  . LEU   B 1 123 ? 45.858 -23.009 -10.993 1.00 12.66 ?  123 LEU   B CD1  1 
ATOM   5864 C CD2  . LEU   B 1 123 ? 47.690 -21.359 -10.556 1.00 12.75 ?  123 LEU   B CD2  1 
ATOM   5865 H H    . LEU   B 1 123 ? 43.659 -18.808 -9.944  1.00 13.15 ?  123 LEU   B H    1 
ATOM   5866 H HA   . LEU   B 1 123 ? 43.434 -21.448 -10.527 1.00 13.42 ?  123 LEU   B HA   1 
ATOM   5867 H HB2  . LEU   B 1 123 ? 45.309 -20.422 -11.418 1.00 13.87 ?  123 LEU   B HB2  1 
ATOM   5868 H HB3  . LEU   B 1 123 ? 45.687 -19.809 -10.009 1.00 13.87 ?  123 LEU   B HB3  1 
ATOM   5869 H HG   . LEU   B 1 123 ? 46.251 -21.979 -9.265  1.00 14.14 ?  123 LEU   B HG   1 
ATOM   5870 H HD11 . LEU   B 1 123 ? 46.494 -23.716 -10.807 1.00 15.21 ?  123 LEU   B HD11 1 
ATOM   5871 H HD12 . LEU   B 1 123 ? 44.970 -23.278 -10.713 1.00 15.21 ?  123 LEU   B HD12 1 
ATOM   5872 H HD13 . LEU   B 1 123 ? 45.860 -22.800 -11.940 1.00 15.21 ?  123 LEU   B HD13 1 
ATOM   5873 H HD21 . LEU   B 1 123 ? 48.276 -22.112 -10.389 1.00 15.31 ?  123 LEU   B HD21 1 
ATOM   5874 H HD22 . LEU   B 1 123 ? 47.727 -21.108 -11.492 1.00 15.31 ?  123 LEU   B HD22 1 
ATOM   5875 H HD23 . LEU   B 1 123 ? 47.951 -20.606 -10.001 1.00 15.31 ?  123 LEU   B HD23 1 
ATOM   5876 N N    . ALA   B 1 124 ? 43.414 -22.382 -8.218  1.00 10.98 ?  124 ALA   B N    1 
ATOM   5877 C CA   . ALA   B 1 124 ? 43.156 -22.701 -6.821  1.00 11.06 ?  124 ALA   B CA   1 
ATOM   5878 C C    . ALA   B 1 124 ? 43.422 -24.162 -6.488  1.00 10.70 ?  124 ALA   B C    1 
ATOM   5879 O O    . ALA   B 1 124 ? 43.288 -25.041 -7.354  1.00 11.25 ?  124 ALA   B O    1 
ATOM   5880 C CB   . ALA   B 1 124 ? 41.697 -22.388 -6.454  1.00 11.54 ?  124 ALA   B CB   1 
ATOM   5881 H H    . ALA   B 1 124 ? 43.262 -23.025 -8.777  1.00 13.20 ?  124 ALA   B H    1 
ATOM   5882 H HA   . ALA   B 1 124 ? 43.727 -22.146 -6.271  1.00 13.29 ?  124 ALA   B HA   1 
ATOM   5883 H HB1  . ALA   B 1 124 ? 41.545 -22.604 -5.521  1.00 13.87 ?  124 ALA   B HB1  1 
ATOM   5884 H HB2  . ALA   B 1 124 ? 41.527 -21.442 -6.605  1.00 13.87 ?  124 ALA   B HB2  1 
ATOM   5885 H HB3  . ALA   B 1 124 ? 41.106 -22.918 -7.016  1.00 13.87 ?  124 ALA   B HB3  1 
ATOM   5886 N N    . PRO   B 1 125 ? 43.719 -24.453 -5.225  1.00 11.03 ?  125 PRO   B N    1 
ATOM   5887 C CA   . PRO   B 1 125 ? 43.660 -25.818 -4.703  1.00 11.65 ?  125 PRO   B CA   1 
ATOM   5888 C C    . PRO   B 1 125 ? 42.260 -26.089 -4.156  1.00 11.61 ?  125 PRO   B C    1 
ATOM   5889 O O    . PRO   B 1 125 ? 41.465 -25.172 -3.946  1.00 12.18 ?  125 PRO   B O    1 
ATOM   5890 C CB   . PRO   B 1 125 ? 44.645 -25.743 -3.531  1.00 12.85 ?  125 PRO   B CB   1 
ATOM   5891 C CG   . PRO   B 1 125 ? 44.397 -24.352 -2.961  1.00 12.76 ?  125 PRO   B CG   1 
ATOM   5892 C CD   . PRO   B 1 125 ? 44.045 -23.484 -4.162  1.00 11.64 ?  125 PRO   B CD   1 
ATOM   5893 H HA   . PRO   B 1 125 ? 43.934 -26.486 -5.353  1.00 14.00 ?  125 PRO   B HA   1 
ATOM   5894 H HB2  . PRO   B 1 125 ? 44.438 -26.428 -2.872  1.00 15.44 ?  125 PRO   B HB2  1 
ATOM   5895 H HB3  . PRO   B 1 125 ? 45.557 -25.830 -3.848  1.00 15.44 ?  125 PRO   B HB3  1 
ATOM   5896 H HG2  . PRO   B 1 125 ? 43.656 -24.378 -2.332  1.00 15.33 ?  125 PRO   B HG2  1 
ATOM   5897 H HG3  . PRO   B 1 125 ? 45.201 -24.025 -2.521  1.00 15.33 ?  125 PRO   B HG3  1 
ATOM   5898 H HD2  . PRO   B 1 125 ? 43.279 -22.925 -3.970  1.00 13.99 ?  125 PRO   B HD2  1 
ATOM   5899 H HD3  . PRO   B 1 125 ? 44.817 -22.943 -4.422  1.00 13.99 ?  125 PRO   B HD3  1 
ATOM   5900 N N    . LEU   B 1 126 ? 41.988 -27.365 -3.879  1.00 12.32 ?  126 LEU   B N    1 
ATOM   5901 C CA   . LEU   B 1 126 ? 40.763 -27.730 -3.171  1.00 12.74 ?  126 LEU   B CA   1 
ATOM   5902 C C    . LEU   B 1 126 ? 40.876 -27.337 -1.704  1.00 12.88 ?  126 LEU   B C    1 
ATOM   5903 O O    . LEU   B 1 126 ? 41.772 -27.796 -0.990  1.00 14.49 ?  126 LEU   B O    1 
ATOM   5904 C CB   . LEU   B 1 126 ? 40.509 -29.227 -3.294  1.00 14.30 ?  126 LEU   B CB   1 
ATOM   5905 C CG   . LEU   B 1 126 ? 39.980 -29.717 -4.645  1.00 15.26 ?  126 LEU   B CG   1 
ATOM   5906 C CD1  . LEU   B 1 126 ? 40.024 -31.224 -4.719  1.00 16.90 ?  126 LEU   B CD1  1 
ATOM   5907 C CD2  . LEU   B 1 126 ? 38.565 -29.231 -4.898  1.00 15.42 ?  126 LEU   B CD2  1 
ATOM   5908 H H    . LEU   B 1 126 ? 42.495 -28.032 -4.076  1.00 14.81 ?  126 LEU   B H    1 
ATOM   5909 H HA   . LEU   B 1 126 ? 40.014 -27.252 -3.558  1.00 15.31 ?  126 LEU   B HA   1 
ATOM   5910 H HB2  . LEU   B 1 126 ? 41.341 -29.691 -3.128  1.00 17.18 ?  126 LEU   B HB2  1 
ATOM   5911 H HB3  . LEU   B 1 126 ? 39.855 -29.480 -2.625  1.00 17.18 ?  126 LEU   B HB3  1 
ATOM   5912 H HG   . LEU   B 1 126 ? 40.549 -29.366 -5.351  1.00 18.33 ?  126 LEU   B HG   1 
ATOM   5913 H HD11 . LEU   B 1 126 ? 39.683 -31.507 -5.582  1.00 20.30 ?  126 LEU   B HD11 1 
ATOM   5914 H HD12 . LEU   B 1 126 ? 40.936 -31.521 -4.606  1.00 20.30 ?  126 LEU   B HD12 1 
ATOM   5915 H HD13 . LEU   B 1 126 ? 39.465 -31.588 -4.011  1.00 20.30 ?  126 LEU   B HD13 1 
ATOM   5916 H HD21 . LEU   B 1 126 ? 38.234 -29.630 -5.719  1.00 18.52 ?  126 LEU   B HD21 1 
ATOM   5917 H HD22 . LEU   B 1 126 ? 38.003 -29.488 -4.153  1.00 18.52 ?  126 LEU   B HD22 1 
ATOM   5918 H HD23 . LEU   B 1 126 ? 38.572 -28.261 -4.986  1.00 18.52 ?  126 LEU   B HD23 1 
ATOM   5919 N N    . LEU   B 1 127 ? 39.954 -26.498 -1.246  1.00 12.98 ?  127 LEU   B N    1 
ATOM   5920 C CA   . LEU   B 1 127 ? 40.011 -26.008 0.120   1.00 13.53 ?  127 LEU   B CA   1 
ATOM   5921 C C    . LEU   B 1 127 ? 39.736 -27.130 1.114   1.00 13.05 ?  127 LEU   B C    1 
ATOM   5922 O O    . LEU   B 1 127 ? 38.915 -28.028 0.885   1.00 13.62 ?  127 LEU   B O    1 
ATOM   5923 C CB   . LEU   B 1 127 ? 38.994 -24.885 0.337   1.00 13.93 ?  127 LEU   B CB   1 
ATOM   5924 C CG   . LEU   B 1 127 ? 39.167 -23.618 -0.503  1.00 14.28 ?  127 LEU   B CG   1 
ATOM   5925 C CD1  . LEU   B 1 127 ? 38.042 -22.649 -0.179  1.00 14.50 ?  127 LEU   B CD1  1 
ATOM   5926 C CD2  . LEU   B 1 127 ? 40.522 -22.966 -0.274  1.00 15.00 ?  127 LEU   B CD2  1 
ATOM   5927 H H    . LEU   B 1 127 ? 39.292 -26.189 -1.706  1.00 15.60 ?  127 LEU   B H    1 
ATOM   5928 H HA   . LEU   B 1 127 ? 40.897 -25.650 0.297   1.00 16.25 ?  127 LEU   B HA   1 
ATOM   5929 H HB2  . LEU   B 1 127 ? 38.111 -25.238 0.146   1.00 16.73 ?  127 LEU   B HB2  1 
ATOM   5930 H HB3  . LEU   B 1 127 ? 39.034 -24.617 1.269   1.00 16.73 ?  127 LEU   B HB3  1 
ATOM   5931 H HG   . LEU   B 1 127 ? 39.089 -23.846 -1.438  1.00 17.15 ?  127 LEU   B HG   1 
ATOM   5932 H HD11 . LEU   B 1 127 ? 38.153 -21.841 -0.710  1.00 17.42 ?  127 LEU   B HD11 1 
ATOM   5933 H HD12 . LEU   B 1 127 ? 37.187 -23.060 -0.389  1.00 17.42 ?  127 LEU   B HD12 1 
ATOM   5934 H HD13 . LEU   B 1 127 ? 38.073 -22.422 0.766   1.00 17.42 ?  127 LEU   B HD13 1 
ATOM   5935 H HD21 . LEU   B 1 127 ? 40.552 -22.121 -0.753  1.00 18.02 ?  127 LEU   B HD21 1 
ATOM   5936 H HD22 . LEU   B 1 127 ? 40.643 -22.809 0.677   1.00 18.02 ?  127 LEU   B HD22 1 
ATOM   5937 H HD23 . LEU   B 1 127 ? 41.213 -23.558 -0.603  1.00 18.02 ?  127 LEU   B HD23 1 
ATOM   5938 N N    . SER   B 1 128 ? 40.423 -27.047 2.245   1.00 13.20 ?  128 SER   B N    1 
ATOM   5939 C CA   . SER   B 1 128 ? 40.302 -27.966 3.364   1.00 13.73 ?  128 SER   B CA   1 
ATOM   5940 C C    . SER   B 1 128 ? 40.801 -29.372 3.045   1.00 14.44 ?  128 SER   B C    1 
ATOM   5941 O O    . SER   B 1 128 ? 40.704 -30.253 3.897   1.00 15.73 ?  128 SER   B O    1 
ATOM   5942 C CB   . SER   B 1 128 ? 38.895 -27.973 3.976   1.00 13.81 ?  128 SER   B CB   1 
ATOM   5943 O OG   . SER   B 1 128 ? 38.593 -26.699 4.529   1.00 14.65 ?  128 SER   B OG   1 
ATOM   5944 H H    . SER   B 1 128 ? 41.000 -26.426 2.395   1.00 15.86 ?  128 SER   B H    1 
ATOM   5945 H HA   . SER   B 1 128 ? 40.879 -27.635 4.055   1.00 16.50 ?  128 SER   B HA   1 
ATOM   5946 H HB2  . SER   B 1 128 ? 38.237 -28.191 3.291   1.00 16.59 ?  128 SER   B HB2  1 
ATOM   5947 H HB3  . SER   B 1 128 ? 38.856 -28.648 4.684   1.00 16.59 ?  128 SER   B HB3  1 
ATOM   5948 H HG   . SER   B 1 128 ? 39.152 -26.512 5.125   1.00 17.60 ?  128 SER   B HG   1 
ATOM   5949 N N    . ALA   B 1 129 ? 41.377 -29.591 1.863   1.00 15.79 ?  129 ALA   B N    1 
ATOM   5950 C CA   . ALA   B 1 129 ? 41.925 -30.887 1.500   1.00 16.72 ?  129 ALA   B CA   1 
ATOM   5951 C C    . ALA   B 1 129 ? 43.315 -31.067 2.099   1.00 15.86 ?  129 ALA   B C    1 
ATOM   5952 O O    . ALA   B 1 129 ? 43.874 -30.169 2.741   1.00 15.61 ?  129 ALA   B O    1 
ATOM   5953 C CB   . ALA   B 1 129 ? 41.988 -31.028 -0.018  1.00 18.56 ?  129 ALA   B CB   1 
ATOM   5954 H H    . ALA   B 1 129 ? 41.467 -28.994 1.248   1.00 18.97 ?  129 ALA   B H    1 
ATOM   5955 H HA   . ALA   B 1 129 ? 41.353 -31.584 1.849   1.00 20.08 ?  129 ALA   B HA   1 
ATOM   5956 H HB1  . ALA   B 1 129 ? 42.347 -31.904 -0.237  1.00 22.29 ?  129 ALA   B HB1  1 
ATOM   5957 H HB2  . ALA   B 1 129 ? 41.096 -30.936 -0.380  1.00 22.29 ?  129 ALA   B HB2  1 
ATOM   5958 H HB3  . ALA   B 1 129 ? 42.567 -30.336 -0.376  1.00 22.29 ?  129 ALA   B HB3  1 
ATOM   5959 N N    . GLY   B 1 130 ? 43.880 -32.252 1.870   1.00 15.70 ?  130 GLY   B N    1 
ATOM   5960 C CA   . GLY   B 1 130 ? 45.267 -32.490 2.231   1.00 16.14 ?  130 GLY   B CA   1 
ATOM   5961 C C    . GLY   B 1 130 ? 45.474 -32.398 3.725   1.00 16.30 ?  130 GLY   B C    1 
ATOM   5962 O O    . GLY   B 1 130 ? 44.770 -33.039 4.518   1.00 16.99 ?  130 GLY   B O    1 
ATOM   5963 H H    . GLY   B 1 130 ? 43.486 -32.921 1.503   1.00 18.86 ?  130 GLY   B H    1 
ATOM   5964 H HA2  . GLY   B 1 130 ? 45.534 -33.376 1.937   1.00 19.39 ?  130 GLY   B HA2  1 
ATOM   5965 H HA3  . GLY   B 1 130 ? 45.838 -31.836 1.796   1.00 19.39 ?  130 GLY   B HA3  1 
ATOM   5966 N N    . ILE   B 1 131 ? 46.449 -31.574 4.121   1.00 16.67 ?  131 ILE   B N    1 
ATOM   5967 C CA   . ILE   B 1 131 ? 46.802 -31.434 5.521   1.00 17.48 ?  131 ILE   B CA   1 
ATOM   5968 C C    . ILE   B 1 131 ? 45.682 -30.829 6.351   1.00 16.47 ?  131 ILE   B C    1 
ATOM   5969 O O    . ILE   B 1 131 ? 45.748 -30.891 7.581   1.00 17.95 ?  131 ILE   B O    1 
ATOM   5970 C CB   . ILE   B 1 131 ? 48.129 -30.654 5.695   1.00 19.38 ?  131 ILE   B CB   1 
ATOM   5971 C CG1  . ILE   B 1 131 ? 47.958 -29.175 5.313   1.00 20.35 ?  131 ILE   B CG1  1 
ATOM   5972 C CG2  . ILE   B 1 131 ? 49.242 -31.309 4.876   1.00 20.24 ?  131 ILE   B CG2  1 
ATOM   5973 C CD1  . ILE   B 1 131 ? 49.154 -28.303 5.655   1.00 21.40 ?  131 ILE   B CD1  1 
ATOM   5974 H H    . ILE   B 1 131 ? 46.916 -31.076 3.598   1.00 20.03 ?  131 ILE   B H    1 
ATOM   5975 H HA   . ILE   B 1 131 ? 46.951 -32.318 5.880   1.00 21.00 ?  131 ILE   B HA   1 
ATOM   5976 H HB   . ILE   B 1 131 ? 48.380 -30.692 6.630   1.00 23.28 ?  131 ILE   B HB   1 
ATOM   5977 H HG12 . ILE   B 1 131 ? 47.811 -29.119 4.357   1.00 24.44 ?  131 ILE   B HG12 1 
ATOM   5978 H HG13 . ILE   B 1 131 ? 47.190 -28.811 5.783   1.00 24.44 ?  131 ILE   B HG13 1 
ATOM   5979 H HG21 . ILE   B 1 131 ? 50.084 -30.895 5.108   1.00 24.31 ?  131 ILE   B HG21 1 
ATOM   5980 H HG22 . ILE   B 1 131 ? 49.261 -32.254 5.083   1.00 24.31 ?  131 ILE   B HG22 1 
ATOM   5981 H HG23 . ILE   B 1 131 ? 49.051 -31.178 3.933   1.00 24.31 ?  131 ILE   B HG23 1 
ATOM   5982 H HD11 . ILE   B 1 131 ? 48.937 -27.381 5.447   1.00 25.69 ?  131 ILE   B HD11 1 
ATOM   5983 H HD12 . ILE   B 1 131 ? 49.347 -28.393 6.601   1.00 25.69 ?  131 ILE   B HD12 1 
ATOM   5984 H HD13 . ILE   B 1 131 ? 49.914 -28.593 5.131   1.00 25.69 ?  131 ILE   B HD13 1 
ATOM   5985 N N    . PHE   B 1 132 ? 44.657 -30.247 5.715   1.00 15.30 ?  132 PHE   B N    1 
ATOM   5986 C CA   . PHE   B 1 132 ? 43.489 -29.745 6.433   1.00 15.73 ?  132 PHE   B CA   1 
ATOM   5987 C C    . PHE   B 1 132 ? 42.466 -30.836 6.760   1.00 17.11 ?  132 PHE   B C    1 
ATOM   5988 O O    . PHE   B 1 132 ? 41.557 -30.587 7.559   1.00 18.73 ?  132 PHE   B O    1 
ATOM   5989 C CB   . PHE   B 1 132 ? 42.816 -28.612 5.644   1.00 14.74 ?  132 PHE   B CB   1 
ATOM   5990 C CG   . PHE   B 1 132 ? 43.514 -27.271 5.759   1.00 15.05 ?  132 PHE   B CG   1 
ATOM   5991 C CD1  . PHE   B 1 132 ? 44.806 -27.089 5.289   1.00 15.81 ?  132 PHE   B CD1  1 
ATOM   5992 C CD2  . PHE   B 1 132 ? 42.847 -26.172 6.291   1.00 14.60 ?  132 PHE   B CD2  1 
ATOM   5993 C CE1  . PHE   B 1 132 ? 45.429 -25.847 5.382   1.00 16.24 ?  132 PHE   B CE1  1 
ATOM   5994 C CE2  . PHE   B 1 132 ? 43.461 -24.929 6.376   1.00 14.98 ?  132 PHE   B CE2  1 
ATOM   5995 C CZ   . PHE   B 1 132 ? 44.752 -24.773 5.927   1.00 15.86 ?  132 PHE   B CZ   1 
ATOM   5996 H H    . PHE   B 1 132 ? 44.614 -30.133 4.864   1.00 18.38 ?  132 PHE   B H    1 
ATOM   5997 H HA   . PHE   B 1 132 ? 43.784 -29.365 7.274   1.00 18.90 ?  132 PHE   B HA   1 
ATOM   5998 H HB2  . PHE   B 1 132 ? 42.807 -28.850 4.707   1.00 17.71 ?  132 PHE   B HB2  1 
ATOM   5999 H HB3  . PHE   B 1 132 ? 41.907 -28.498 5.966   1.00 17.71 ?  132 PHE   B HB3  1 
ATOM   6000 H HD1  . PHE   B 1 132 ? 45.267 -27.811 4.925   1.00 18.99 ?  132 PHE   B HD1  1 
ATOM   6001 H HD2  . PHE   B 1 132 ? 41.975 -26.271 6.599   1.00 17.54 ?  132 PHE   B HD2  1 
ATOM   6002 H HE1  . PHE   B 1 132 ? 46.300 -25.741 5.076   1.00 19.51 ?  132 PHE   B HE1  1 
ATOM   6003 H HE2  . PHE   B 1 132 ? 43.006 -24.206 6.748   1.00 18.00 ?  132 PHE   B HE2  1 
ATOM   6004 H HZ   . PHE   B 1 132 ? 45.166 -23.938 5.991   1.00 19.05 ?  132 PHE   B HZ   1 
ATOM   6005 N N    . GLY   B 1 133 ? 42.571 -32.027 6.160   1.00 16.94 ?  133 GLY   B N    1 
ATOM   6006 C CA   . GLY   B 1 133 ? 41.858 -33.194 6.650   1.00 17.66 ?  133 GLY   B CA   1 
ATOM   6007 C C    . GLY   B 1 133 ? 40.461 -33.452 6.115   1.00 17.81 ?  133 GLY   B C    1 
ATOM   6008 O O    . GLY   B 1 133 ? 39.871 -34.473 6.482   1.00 19.54 ?  133 GLY   B O    1 
ATOM   6009 H H    . GLY   B 1 133 ? 43.059 -32.175 5.466   1.00 20.34 ?  133 GLY   B H    1 
ATOM   6010 H HA2  . GLY   B 1 133 ? 42.396 -33.975 6.457   1.00 21.21 ?  133 GLY   B HA2  1 
ATOM   6011 H HA3  . GLY   B 1 133 ? 41.785 -33.116 7.613   1.00 21.21 ?  133 GLY   B HA3  1 
ATOM   6012 N N    . ALA   B 1 134 ? 39.900 -32.581 5.284   1.00 17.02 ?  134 ALA   B N    1 
ATOM   6013 C CA   . ALA   B 1 134 ? 38.577 -32.869 4.750   1.00 16.97 ?  134 ALA   B CA   1 
ATOM   6014 C C    . ALA   B 1 134 ? 38.667 -33.870 3.603   1.00 16.87 ?  134 ALA   B C    1 
ATOM   6015 O O    . ALA   B 1 134 ? 39.723 -34.071 2.997   1.00 18.09 ?  134 ALA   B O    1 
ATOM   6016 C CB   . ALA   B 1 134 ? 37.900 -31.588 4.263   1.00 17.38 ?  134 ALA   B CB   1 
ATOM   6017 H H    . ALA   B 1 134 ? 40.248 -31.832 5.029   1.00 20.45 ?  134 ALA   B H    1 
ATOM   6018 H HA   . ALA   B 1 134 ? 38.028 -33.250 5.454   1.00 20.38 ?  134 ALA   B HA   1 
ATOM   6019 H HB1  . ALA   B 1 134 ? 37.015 -31.809 3.929   1.00 20.88 ?  134 ALA   B HB1  1 
ATOM   6020 H HB2  . ALA   B 1 134 ? 37.826 -30.966 5.003   1.00 20.88 ?  134 ALA   B HB2  1 
ATOM   6021 H HB3  . ALA   B 1 134 ? 38.432 -31.198 3.554   1.00 20.88 ?  134 ALA   B HB3  1 
ATOM   6022 N N    . ASP   B 1 135 ? 37.531 -34.495 3.314   1.00 17.08 ?  135 ASP   B N    1 
ATOM   6023 C CA   . ASP   B 1 135 ? 37.429 -35.387 2.170   1.00 17.89 ?  135 ASP   B CA   1 
ATOM   6024 C C    . ASP   B 1 135 ? 37.533 -34.552 0.900   1.00 16.73 ?  135 ASP   B C    1 
ATOM   6025 O O    . ASP   B 1 135 ? 36.682 -33.679 0.675   1.00 16.76 ?  135 ASP   B O    1 
ATOM   6026 C CB   . ASP   B 1 135 ? 36.081 -36.105 2.224   1.00 20.00 ?  135 ASP   B CB   1 
ATOM   6027 C CG   . ASP   B 1 135 ? 35.897 -37.103 1.100   1.00 21.90 ?  135 ASP   B CG   1 
ATOM   6028 O OD1  . ASP   B 1 135 ? 36.757 -37.160 0.197   1.00 21.83 ?  135 ASP   B OD1  1 
ATOM   6029 O OD2  . ASP   B 1 135 ? 34.898 -37.857 1.135   1.00 24.55 -1 135 ASP   B OD2  1 
ATOM   6030 H H    . ASP   B 1 135 ? 36.801 -34.416 3.767   1.00 20.51 ?  135 ASP   B H    1 
ATOM   6031 H HA   . ASP   B 1 135 ? 38.141 -36.047 2.204   1.00 21.49 ?  135 ASP   B HA   1 
ATOM   6032 H HB2  . ASP   B 1 135 ? 36.017 -36.589 3.059   1.00 24.02 ?  135 ASP   B HB2  1 
ATOM   6033 H HB3  . ASP   B 1 135 ? 35.376 -35.444 2.163   1.00 24.02 ?  135 ASP   B HB3  1 
ATOM   6034 N N    . PRO   B 1 136 ? 38.542 -34.764 0.053   1.00 16.92 ?  136 PRO   B N    1 
ATOM   6035 C CA   . PRO   B 1 136 ? 38.643 -33.940 -1.161  1.00 16.07 ?  136 PRO   B CA   1 
ATOM   6036 C C    . PRO   B 1 136 ? 37.453 -34.091 -2.087  1.00 15.68 ?  136 PRO   B C    1 
ATOM   6037 O O    . PRO   B 1 136 ? 37.126 -33.147 -2.811  1.00 15.08 ?  136 PRO   B O    1 
ATOM   6038 C CB   . PRO   B 1 136 ? 39.954 -34.417 -1.804  1.00 17.26 ?  136 PRO   B CB   1 
ATOM   6039 C CG   . PRO   B 1 136 ? 40.141 -35.814 -1.276  1.00 18.24 ?  136 PRO   B CG   1 
ATOM   6040 C CD   . PRO   B 1 136 ? 39.616 -35.768 0.130   1.00 17.78 ?  136 PRO   B CD   1 
ATOM   6041 H HA   . PRO   B 1 136 ? 38.733 -33.006 -0.922  1.00 19.31 ?  136 PRO   B HA   1 
ATOM   6042 H HB2  . PRO   B 1 136 ? 39.864 -34.422 -2.771  1.00 20.73 ?  136 PRO   B HB2  1 
ATOM   6043 H HB3  . PRO   B 1 136 ? 40.683 -33.842 -1.527  1.00 20.73 ?  136 PRO   B HB3  1 
ATOM   6044 H HG2  . PRO   B 1 136 ? 39.629 -36.442 -1.811  1.00 21.91 ?  136 PRO   B HG2  1 
ATOM   6045 H HG3  . PRO   B 1 136 ? 41.083 -36.047 -1.283  1.00 21.91 ?  136 PRO   B HG3  1 
ATOM   6046 H HD2  . PRO   B 1 136 ? 39.256 -36.631 0.387   1.00 21.35 ?  136 PRO   B HD2  1 
ATOM   6047 H HD3  . PRO   B 1 136 ? 40.311 -35.476 0.745   1.00 21.35 ?  136 PRO   B HD3  1 
ATOM   6048 N N    . ILE   B 1 137 ? 36.798 -35.257 -2.091  1.00 16.28 ?  137 ILE   B N    1 
ATOM   6049 C CA   . ILE   B 1 137 ? 35.581 -35.424 -2.881  1.00 16.56 ?  137 ILE   B CA   1 
ATOM   6050 C C    . ILE   B 1 137 ? 34.510 -34.451 -2.406  1.00 16.45 ?  137 ILE   B C    1 
ATOM   6051 O O    . ILE   B 1 137 ? 33.795 -33.841 -3.211  1.00 16.01 ?  137 ILE   B O    1 
ATOM   6052 C CB   . ILE   B 1 137 ? 35.102 -36.889 -2.811  1.00 18.51 ?  137 ILE   B CB   1 
ATOM   6053 C CG1  . ILE   B 1 137 ? 36.107 -37.814 -3.506  1.00 20.81 ?  137 ILE   B CG1  1 
ATOM   6054 C CG2  . ILE   B 1 137 ? 33.702 -37.030 -3.414  1.00 18.81 ?  137 ILE   B CG2  1 
ATOM   6055 C CD1  . ILE   B 1 137 ? 35.754 -39.285 -3.416  1.00 22.92 ?  137 ILE   B CD1  1 
ATOM   6056 H H    . ILE   B 1 137 ? 37.031 -35.958 -1.653  1.00 19.56 ?  137 ILE   B H    1 
ATOM   6057 H HA   . ILE   B 1 137 ? 35.776 -35.223 -3.812  1.00 19.89 ?  137 ILE   B HA   1 
ATOM   6058 H HB   . ILE   B 1 137 ? 35.049 -37.147 -1.883  1.00 22.23 ?  137 ILE   B HB   1 
ATOM   6059 H HG12 . ILE   B 1 137 ? 36.157 -37.584 -4.447  1.00 24.99 ?  137 ILE   B HG12 1 
ATOM   6060 H HG13 . ILE   B 1 137 ? 36.977 -37.699 -3.093  1.00 24.99 ?  137 ILE   B HG13 1 
ATOM   6061 H HG21 . ILE   B 1 137 ? 33.439 -37.965 -3.417  1.00 22.59 ?  137 ILE   B HG21 1 
ATOM   6062 H HG22 . ILE   B 1 137 ? 33.067 -36.530 -2.879  1.00 22.59 ?  137 ILE   B HG22 1 
ATOM   6063 H HG23 . ILE   B 1 137 ? 33.710 -36.692 -4.323  1.00 22.59 ?  137 ILE   B HG23 1 
ATOM   6064 H HD11 . ILE   B 1 137 ? 36.415 -39.785 -3.916  1.00 27.52 ?  137 ILE   B HD11 1 
ATOM   6065 H HD12 . ILE   B 1 137 ? 35.760 -39.562 -2.485  1.00 27.52 ?  137 ILE   B HD12 1 
ATOM   6066 H HD13 . ILE   B 1 137 ? 34.879 -39.440 -3.804  1.00 27.52 ?  137 ILE   B HD13 1 
ATOM   6067 N N    . HIS   B 1 138 ? 34.376 -34.302 -1.091  1.00 16.30 ?  138 HIS   B N    1 
ATOM   6068 C CA   . HIS   B 1 138 ? 33.425 -33.336 -0.557  1.00 16.75 ?  138 HIS   B CA   1 
ATOM   6069 C C    . HIS   B 1 138 ? 33.846 -31.908 -0.878  1.00 15.85 ?  138 HIS   B C    1 
ATOM   6070 O O    . HIS   B 1 138 ? 33.000 -31.064 -1.195  1.00 16.22 ?  138 HIS   B O    1 
ATOM   6071 C CB   . HIS   B 1 138 ? 33.294 -33.513 0.949   1.00 18.08 ?  138 HIS   B CB   1 
ATOM   6072 C CG   . HIS   B 1 138 ? 32.357 -32.532 1.579   1.00 19.01 ?  138 HIS   B CG   1 
ATOM   6073 N ND1  . HIS   B 1 138 ? 31.021 -32.463 1.248   1.00 19.99 ?  138 HIS   B ND1  1 
ATOM   6074 C CD2  . HIS   B 1 138 ? 32.570 -31.557 2.493   1.00 19.55 ?  138 HIS   B CD2  1 
ATOM   6075 C CE1  . HIS   B 1 138 ? 30.447 -31.500 1.945   1.00 20.11 ?  138 HIS   B CE1  1 
ATOM   6076 N NE2  . HIS   B 1 138 ? 31.364 -30.938 2.712   1.00 19.73 ?  138 HIS   B NE2  1 
ATOM   6077 H H    . HIS   B 1 138 ? 34.817 -34.742 -0.501  1.00 19.58 ?  138 HIS   B H    1 
ATOM   6078 H HA   . HIS   B 1 138 ? 32.555 -33.494 -0.958  1.00 20.12 ?  138 HIS   B HA   1 
ATOM   6079 H HB2  . HIS   B 1 138 ? 32.954 -34.402 1.134   1.00 21.71 ?  138 HIS   B HB2  1 
ATOM   6080 H HB3  . HIS   B 1 138 ? 34.162 -33.395 1.358   1.00 21.71 ?  138 HIS   B HB3  1 
ATOM   6081 H HD1  . HIS   B 1 138 ? 30.621 -32.973 0.680   1.00 24.01 ?  138 HIS   B HD1  1 
ATOM   6082 H HD2  . HIS   B 1 138 ? 33.369 -31.353 2.912   1.00 23.48 ?  138 HIS   B HD2  1 
ATOM   6083 H HE1  . HIS   B 1 138 ? 29.543 -31.265 1.906   1.00 24.15 ?  138 HIS   B HE1  1 
ATOM   6084 N N    . SER   B 1 139 ? 35.141 -31.609 -0.794  1.00 15.33 ?  139 SER   B N    1 
ATOM   6085 C CA   . SER   B 1 139 ? 35.583 -30.261 -1.117  1.00 14.70 ?  139 SER   B CA   1 
ATOM   6086 C C    . SER   B 1 139 ? 35.248 -29.911 -2.559  1.00 14.03 ?  139 SER   B C    1 
ATOM   6087 O O    . SER   B 1 139 ? 34.799 -28.796 -2.841  1.00 13.97 ?  139 SER   B O    1 
ATOM   6088 C CB   . SER   B 1 139 ? 37.076 -30.119 -0.845  1.00 15.34 ?  139 SER   B CB   1 
ATOM   6089 O OG   . SER   B 1 139 ? 37.480 -28.788 -1.108  1.00 15.19 ?  139 SER   B OG   1 
ATOM   6090 H H    . SER   B 1 139 ? 35.759 -32.155 -0.562  1.00 18.41 ?  139 SER   B H    1 
ATOM   6091 H HA   . SER   B 1 139 ? 35.113 -29.635 -0.549  1.00 17.66 ?  139 SER   B HA   1 
ATOM   6092 H HB2  . SER   B 1 139 ? 37.250 -30.327 0.088   1.00 18.42 ?  139 SER   B HB2  1 
ATOM   6093 H HB3  . SER   B 1 139 ? 37.567 -30.724 -1.420  1.00 18.42 ?  139 SER   B HB3  1 
ATOM   6094 H HG   . SER   B 1 139 ? 38.308 -28.703 -0.956  1.00 18.25 ?  139 SER   B HG   1 
ATOM   6095 N N    . LEU   B 1 140 ? 35.435 -30.858 -3.481  1.00 13.81 ?  140 LEU   B N    1 
ATOM   6096 C CA   . LEU   B 1 140 ? 35.075 -30.612 -4.871  1.00 13.86 ?  140 LEU   B CA   1 
ATOM   6097 C C    . LEU   B 1 140 ? 33.573 -30.381 -5.011  1.00 14.13 ?  140 LEU   B C    1 
ATOM   6098 O O    . LEU   B 1 140 ? 33.140 -29.490 -5.750  1.00 14.07 ?  140 LEU   B O    1 
ATOM   6099 C CB   . LEU   B 1 140 ? 35.547 -31.776 -5.742  1.00 13.87 ?  140 LEU   B CB   1 
ATOM   6100 C CG   . LEU   B 1 140 ? 35.185 -31.668 -7.217  1.00 14.22 ?  140 LEU   B CG   1 
ATOM   6101 C CD1  . LEU   B 1 140 ? 35.759 -30.393 -7.811  1.00 15.16 ?  140 LEU   B CD1  1 
ATOM   6102 C CD2  . LEU   B 1 140 ? 35.659 -32.895 -7.963  1.00 15.30 ?  140 LEU   B CD2  1 
ATOM   6103 H H    . LEU   B 1 140 ? 35.760 -31.639 -3.329  1.00 16.59 ?  140 LEU   B H    1 
ATOM   6104 H HA   . LEU   B 1 140 ? 35.530 -29.810 -5.174  1.00 16.65 ?  140 LEU   B HA   1 
ATOM   6105 H HB2  . LEU   B 1 140 ? 36.513 -31.836 -5.685  1.00 16.66 ?  140 LEU   B HB2  1 
ATOM   6106 H HB3  . LEU   B 1 140 ? 35.150 -32.595 -5.408  1.00 16.66 ?  140 LEU   B HB3  1 
ATOM   6107 H HG   . LEU   B 1 140 ? 34.220 -31.621 -7.301  1.00 17.08 ?  140 LEU   B HG   1 
ATOM   6108 H HD11 . LEU   B 1 140 ? 35.655 -30.421 -8.773  1.00 18.21 ?  140 LEU   B HD11 1 
ATOM   6109 H HD12 . LEU   B 1 140 ? 35.279 -29.630 -7.448  1.00 18.21 ?  140 LEU   B HD12 1 
ATOM   6110 H HD13 . LEU   B 1 140 ? 36.699 -30.333 -7.580  1.00 18.21 ?  140 LEU   B HD13 1 
ATOM   6111 H HD21 . LEU   B 1 140 ? 35.412 -32.802 -8.897  1.00 18.38 ?  140 LEU   B HD21 1 
ATOM   6112 H HD22 . LEU   B 1 140 ? 36.615 -32.966 -7.872  1.00 18.38 ?  140 LEU   B HD22 1 
ATOM   6113 H HD23 . LEU   B 1 140 ? 35.222 -33.673 -7.581  1.00 18.38 ?  140 LEU   B HD23 1 
ATOM   6114 N N    . ARG   B 1 141 ? 32.766 -31.171 -4.297  1.00 14.32 ?  141 ARG   B N    1 
ATOM   6115 C CA   . ARG   B 1 141 ? 31.316 -30.992 -4.281  1.00 15.11 ?  141 ARG   B CA   1 
ATOM   6116 C C    . ARG   B 1 141 ? 30.938 -29.582 -3.852  1.00 14.63 ?  141 ARG   B C    1 
ATOM   6117 O O    . ARG   B 1 141 ? 30.131 -28.907 -4.509  1.00 14.90 ?  141 ARG   B O    1 
ATOM   6118 C CB   . ARG   B 1 141 ? 30.723 -32.017 -3.305  1.00 16.39 ?  141 ARG   B CB   1 
ATOM   6119 C CG   . ARG   B 1 141 ? 29.257 -31.891 -2.991  1.00 18.22 ?  141 ARG   B CG   1 
ATOM   6120 C CD   . ARG   B 1 141 ? 28.465 -32.535 -4.057  1.00 19.80 ?  141 ARG   B CD   1 
ATOM   6121 N NE   . ARG   B 1 141 ? 28.195 -31.623 -5.157  1.00 20.22 ?  141 ARG   B NE   1 
ATOM   6122 C CZ   . ARG   B 1 141 ? 28.195 -31.968 -6.437  1.00 19.81 ?  141 ARG   B CZ   1 
ATOM   6123 N NH1  . ARG   B 1 141 ? 28.633 -33.152 -6.838  1.00 19.72 ?  141 ARG   B NH1  1 
ATOM   6124 N NH2  . ARG   B 1 141 ? 27.735 -31.106 -7.338  1.00 20.63 ?  141 ARG   B NH2  1 
ATOM   6125 H H    . ARG   B 1 141 ? 33.041 -31.825 -3.813  1.00 17.21 ?  141 ARG   B H    1 
ATOM   6126 H HA   . ARG   B 1 141 ? 30.952 -31.155 -5.163  1.00 18.15 ?  141 ARG   B HA   1 
ATOM   6127 H HB2  . ARG   B 1 141 ? 30.875 -32.905 -3.669  1.00 19.69 ?  141 ARG   B HB2  1 
ATOM   6128 H HB3  . ARG   B 1 141 ? 31.200 -31.941 -2.464  1.00 19.69 ?  141 ARG   B HB3  1 
ATOM   6129 H HG2  . ARG   B 1 141 ? 29.073 -32.333 -2.150  1.00 21.88 ?  141 ARG   B HG2  1 
ATOM   6130 H HG3  . ARG   B 1 141 ? 29.004 -30.951 -2.936  1.00 21.88 ?  141 ARG   B HG3  1 
ATOM   6131 H HD2  . ARG   B 1 141 ? 28.952 -33.304 -4.397  1.00 23.78 ?  141 ARG   B HD2  1 
ATOM   6132 H HD3  . ARG   B 1 141 ? 27.622 -32.824 -3.686  1.00 23.78 ?  141 ARG   B HD3  1 
ATOM   6133 H HE   . ARG   B 1 141 ? 28.019 -30.802 -4.960  1.00 24.29 ?  141 ARG   B HE   1 
ATOM   6134 H HH11 . ARG   B 1 141 ? 28.924 -33.725 -6.269  1.00 23.69 ?  141 ARG   B HH11 1 
ATOM   6135 H HH12 . ARG   B 1 141 ? 28.631 -33.344 -7.674  1.00 23.69 ?  141 ARG   B HH12 1 
ATOM   6136 H HH21 . ARG   B 1 141 ? 27.453 -30.329 -7.090  1.00 24.77 ?  141 ARG   B HH21 1 
ATOM   6137 H HH22 . ARG   B 1 141 ? 27.748 -31.307 -8.174  1.00 24.77 ?  141 ARG   B HH22 1 
ATOM   6138 N N    . VAL   B 1 142 ? 31.484 -29.134 -2.724  1.00 14.12 ?  142 VAL   B N    1 
ATOM   6139 C CA   . VAL   B 1 142 ? 31.146 -27.803 -2.239  1.00 14.09 ?  142 VAL   B CA   1 
ATOM   6140 C C    . VAL   B 1 142 ? 31.621 -26.744 -3.226  1.00 13.73 ?  142 VAL   B C    1 
ATOM   6141 O O    . VAL   B 1 142 ? 30.925 -25.757 -3.481  1.00 14.23 ?  142 VAL   B O    1 
ATOM   6142 C CB   . VAL   B 1 142 ? 31.688 -27.577 -0.815  1.00 14.75 ?  142 VAL   B CB   1 
ATOM   6143 C CG1  . VAL   B 1 142 ? 31.380 -26.151 -0.356  1.00 14.41 ?  142 VAL   B CG1  1 
ATOM   6144 C CG2  . VAL   B 1 142 ? 31.094 -28.598 0.148   1.00 15.32 ?  142 VAL   B CG2  1 
ATOM   6145 H H    . VAL   B 1 142 ? 32.040 -29.570 -2.231  1.00 16.97 ?  142 VAL   B H    1 
ATOM   6146 H HA   . VAL   B 1 142 ? 30.186 -27.733 -2.187  1.00 16.92 ?  142 VAL   B HA   1 
ATOM   6147 H HB   . VAL   B 1 142 ? 32.653 -27.689 -0.815  1.00 17.71 ?  142 VAL   B HB   1 
ATOM   6148 H HG11 . VAL   B 1 142 ? 31.552 -26.083 0.595   1.00 17.31 ?  142 VAL   B HG11 1 
ATOM   6149 H HG12 . VAL   B 1 142 ? 31.954 -25.533 -0.839  1.00 17.31 ?  142 VAL   B HG12 1 
ATOM   6150 H HG13 . VAL   B 1 142 ? 30.451 -25.957 -0.542  1.00 17.31 ?  142 VAL   B HG13 1 
ATOM   6151 H HG21 . VAL   B 1 142 ? 31.413 -28.413 1.045   1.00 18.40 ?  142 VAL   B HG21 1 
ATOM   6152 H HG22 . VAL   B 1 142 ? 30.127 -28.531 0.120   1.00 18.40 ?  142 VAL   B HG22 1 
ATOM   6153 H HG23 . VAL   B 1 142 ? 31.371 -29.487 -0.125  1.00 18.40 ?  142 VAL   B HG23 1 
ATOM   6154 N N    . CYS   B 1 143 ? 32.805 -26.941 -3.812  1.00 13.56 ?  143 CYS   B N    1 
ATOM   6155 C CA   . CYS   B 1 143 ? 33.299 -26.003 -4.815  1.00 13.52 ?  143 CYS   B CA   1 
ATOM   6156 C C    . CYS   B 1 143 ? 32.299 -25.855 -5.956  1.00 13.32 ?  143 CYS   B C    1 
ATOM   6157 O O    . CYS   B 1 143 ? 31.899 -24.743 -6.317  1.00 13.58 ?  143 CYS   B O    1 
ATOM   6158 C CB   . CYS   B 1 143 ? 34.655 -26.489 -5.345  1.00 14.00 ?  143 CYS   B CB   1 
ATOM   6159 S SG   . CYS   B 1 143 ? 35.411 -25.389 -6.556  1.00 14.06 ?  143 CYS   B SG   1 
ATOM   6160 H H    . CYS   B 1 143 ? 33.336 -27.594 -3.643  1.00 16.29 ?  143 CYS   B H    1 
ATOM   6161 H HA   . CYS   B 1 143 ? 33.434 -25.131 -4.413  1.00 16.25 ?  143 CYS   B HA   1 
ATOM   6162 H HB2  . CYS   B 1 143 ? 35.276 -26.579 -4.603  1.00 16.82 ?  143 CYS   B HB2  1 
ATOM   6163 H HB3  . CYS   B 1 143 ? 34.536 -27.353 -5.768  1.00 16.82 ?  143 CYS   B HB3  1 
ATOM   6164 H HG   . CYS   B 1 143 ? 36.491 -25.827 -6.869  1.00 16.89 ?  143 CYS   B HG   1 
ATOM   6165 N N    . VAL   B 1 144 ? 31.902 -26.977 -6.552  1.00 13.88 ?  144 VAL   B N    1 
ATOM   6166 C CA   . VAL   B 1 144 ? 30.993 -26.925 -7.693  1.00 14.76 ?  144 VAL   B CA   1 
ATOM   6167 C C    . VAL   B 1 144 ? 29.654 -26.313 -7.317  1.00 14.84 ?  144 VAL   B C    1 
ATOM   6168 O O    . VAL   B 1 144 ? 29.043 -25.601 -8.124  1.00 16.18 ?  144 VAL   B O    1 
ATOM   6169 C CB   . VAL   B 1 144 ? 30.838 -28.337 -8.275  1.00 17.02 ?  144 VAL   B CB   1 
ATOM   6170 C CG1  . VAL   B 1 144 ? 29.570 -28.461 -9.117  1.00 19.65 ?  144 VAL   B CG1  1 
ATOM   6171 C CG2  . VAL   B 1 144 ? 32.084 -28.725 -9.063  1.00 17.13 ?  144 VAL   B CG2  1 
ATOM   6172 H H    . VAL   B 1 144 ? 32.144 -27.772 -6.324  1.00 16.68 ?  144 VAL   B H    1 
ATOM   6173 H HA   . VAL   B 1 144 ? 31.382 -26.367 -8.383  1.00 17.73 ?  144 VAL   B HA   1 
ATOM   6174 H HB   . VAL   B 1 144 ? 30.757 -28.965 -7.540  1.00 20.44 ?  144 VAL   B HB   1 
ATOM   6175 H HG11 . VAL   B 1 144 ? 29.652 -29.249 -9.685  1.00 23.59 ?  144 VAL   B HG11 1 
ATOM   6176 H HG12 . VAL   B 1 144 ? 28.808 -28.566 -8.528  1.00 23.59 ?  144 VAL   B HG12 1 
ATOM   6177 H HG13 . VAL   B 1 144 ? 29.472 -27.672 -9.664  1.00 23.59 ?  144 VAL   B HG13 1 
ATOM   6178 H HG21 . VAL   B 1 144 ? 31.971 -29.622 -9.415  1.00 20.57 ?  144 VAL   B HG21 1 
ATOM   6179 H HG22 . VAL   B 1 144 ? 32.202 -28.096 -9.795  1.00 20.57 ?  144 VAL   B HG22 1 
ATOM   6180 H HG23 . VAL   B 1 144 ? 32.852 -28.693 -8.474  1.00 20.57 ?  144 VAL   B HG23 1 
ATOM   6181 N N    . ASP   B 1 145 ? 29.187 -26.552 -6.096  1.00 15.06 ?  145 ASP   B N    1 
ATOM   6182 C CA   . ASP   B 1 145 ? 27.875 -26.084 -5.671  1.00 15.57 ?  145 ASP   B CA   1 
ATOM   6183 C C    . ASP   B 1 145 ? 27.905 -24.663 -5.120  1.00 15.32 ?  145 ASP   B C    1 
ATOM   6184 O O    . ASP   B 1 145 ? 26.846 -24.121 -4.785  1.00 16.99 ?  145 ASP   B O    1 
ATOM   6185 C CB   . ASP   B 1 145 ? 27.282 -27.008 -4.599  1.00 17.13 ?  145 ASP   B CB   1 
ATOM   6186 C CG   . ASP   B 1 145 ? 26.927 -28.385 -5.117  1.00 18.70 ?  145 ASP   B CG   1 
ATOM   6187 O OD1  . ASP   B 1 145 ? 26.845 -28.581 -6.346  1.00 19.07 ?  145 ASP   B OD1  1 
ATOM   6188 O OD2  . ASP   B 1 145 ? 26.725 -29.271 -4.266  1.00 20.97 -1 145 ASP   B OD2  1 
ATOM   6189 H H    . ASP   B 1 145 ? 29.620 -26.975 -5.487  1.00 18.09 ?  145 ASP   B H    1 
ATOM   6190 H HA   . ASP   B 1 145 ? 27.281 -26.073 -6.435  1.00 18.71 ?  145 ASP   B HA   1 
ATOM   6191 H HB2  . ASP   B 1 145 ? 27.923 -27.120 -3.892  1.00 20.58 ?  145 ASP   B HB2  1 
ATOM   6192 H HB3  . ASP   B 1 145 ? 26.467 -26.601 -4.258  1.00 20.58 ?  145 ASP   B HB3  1 
ATOM   6193 N N    . THR   B 1 146 ? 29.083 -24.046 -5.012  1.00 13.76 ?  146 THR   B N    1 
ATOM   6194 C CA   . THR   B 1 146 ? 29.210 -22.722 -4.405  1.00 13.07 ?  146 THR   B CA   1 
ATOM   6195 C C    . THR   B 1 146 ? 29.843 -21.693 -5.323  1.00 13.23 ?  146 THR   B C    1 
ATOM   6196 O O    . THR   B 1 146 ? 29.395 -20.531 -5.366  1.00 13.46 ?  146 THR   B O    1 
ATOM   6197 C CB   . THR   B 1 146 ? 30.039 -22.822 -3.115  1.00 13.59 ?  146 THR   B CB   1 
ATOM   6198 O OG1  . THR   B 1 146 ? 29.467 -23.817 -2.255  1.00 14.21 ?  146 THR   B OG1  1 
ATOM   6199 C CG2  . THR   B 1 146 ? 30.107 -21.484 -2.397  1.00 14.17 ?  146 THR   B CG2  1 
ATOM   6200 H H    . THR   B 1 146 ? 29.836 -24.367 -5.288  1.00 16.53 ?  146 THR   B H    1 
ATOM   6201 H HA   . THR   B 1 146 ? 28.332 -22.395 -4.167  1.00 15.71 ?  146 THR   B HA   1 
ATOM   6202 H HB   . THR   B 1 146 ? 30.947 -23.076 -3.340  1.00 16.33 ?  146 THR   B HB   1 
ATOM   6203 H HG1  . THR   B 1 146 ? 29.505 -24.574 -2.633  1.00 17.07 ?  146 THR   B HG1  1 
ATOM   6204 H HG21 . THR   B 1 146 ? 30.458 -21.602 -1.502  1.00 17.02 ?  146 THR   B HG21 1 
ATOM   6205 H HG22 . THR   B 1 146 ? 30.685 -20.870 -2.882  1.00 17.02 ?  146 THR   B HG22 1 
ATOM   6206 H HG23 . THR   B 1 146 ? 29.219 -21.093 -2.337  1.00 17.02 ?  146 THR   B HG23 1 
ATOM   6207 N N    . VAL   B 1 147 ? 30.905 -22.068 -6.027  1.00 13.21 ?  147 VAL   B N    1 
ATOM   6208 C CA   . VAL   B 1 147 ? 31.631 -21.128 -6.867  1.00 13.00 ?  147 VAL   B CA   1 
ATOM   6209 C C    . VAL   B 1 147 ? 30.901 -20.993 -8.191  1.00 12.99 ?  147 VAL   B C    1 
ATOM   6210 O O    . VAL   B 1 147 ? 30.531 -21.995 -8.817  1.00 13.97 ?  147 VAL   B O    1 
ATOM   6211 C CB   . VAL   B 1 147 ? 33.084 -21.590 -7.072  1.00 13.05 ?  147 VAL   B CB   1 
ATOM   6212 C CG1  . VAL   B 1 147 ? 33.844 -20.571 -7.902  1.00 13.00 ?  147 VAL   B CG1  1 
ATOM   6213 C CG2  . VAL   B 1 147 ? 33.767 -21.800 -5.731  1.00 12.99 ?  147 VAL   B CG2  1 
ATOM   6214 H H    . VAL   B 1 147 ? 31.227 -22.871 -6.042  1.00 15.87 ?  147 VAL   B H    1 
ATOM   6215 H HA   . VAL   B 1 147 ? 31.650 -20.261 -6.438  1.00 15.62 ?  147 VAL   B HA   1 
ATOM   6216 H HB   . VAL   B 1 147 ? 33.090 -22.435 -7.553  1.00 15.68 ?  147 VAL   B HB   1 
ATOM   6217 H HG11 . VAL   B 1 147 ? 34.789 -20.790 -7.886  1.00 15.62 ?  147 VAL   B HG11 1 
ATOM   6218 H HG12 . VAL   B 1 147 ? 33.517 -20.591 -8.814  1.00 15.62 ?  147 VAL   B HG12 1 
ATOM   6219 H HG13 . VAL   B 1 147 ? 33.706 -19.688 -7.520  1.00 15.62 ?  147 VAL   B HG13 1 
ATOM   6220 H HG21 . VAL   B 1 147 ? 34.706 -22.002 -5.882  1.00 15.61 ?  147 VAL   B HG21 1 
ATOM   6221 H HG22 . VAL   B 1 147 ? 33.685 -20.991 -5.205  1.00 15.61 ?  147 VAL   B HG22 1 
ATOM   6222 H HG23 . VAL   B 1 147 ? 33.342 -22.540 -5.271  1.00 15.61 ?  147 VAL   B HG23 1 
ATOM   6223 N N    . ARG   B 1 148 ? 30.697 -19.745 -8.615  1.00 13.03 ?  148 ARG   B N    1 
ATOM   6224 C CA   . ARG   B 1 148 ? 30.073 -19.431 -9.889  1.00 13.36 ?  148 ARG   B CA   1 
ATOM   6225 C C    . ARG   B 1 148 ? 31.031 -18.759 -10.863 1.00 13.47 ?  148 ARG   B C    1 
ATOM   6226 O O    . ARG   B 1 148 ? 30.750 -18.742 -12.064 1.00 14.66 ?  148 ARG   B O    1 
ATOM   6227 C CB   . ARG   B 1 148 ? 28.830 -18.547 -9.675  1.00 13.70 ?  148 ARG   B CB   1 
ATOM   6228 C CG   . ARG   B 1 148 ? 27.757 -19.251 -8.857  1.00 14.37 ?  148 ARG   B CG   1 
ATOM   6229 C CD   . ARG   B 1 148 ? 26.553 -18.360 -8.543  1.00 15.24 ?  148 ARG   B CD   1 
ATOM   6230 N NE   . ARG   B 1 148 ? 26.939 -17.160 -7.811  1.00 15.10 ?  148 ARG   B NE   1 
ATOM   6231 C CZ   . ARG   B 1 148 ? 27.231 -17.123 -6.517  1.00 13.99 ?  148 ARG   B CZ   1 
ATOM   6232 N NH1  . ARG   B 1 148 ? 27.160 -18.206 -5.757  1.00 14.17 ?  148 ARG   B NH1  1 
ATOM   6233 N NH2  . ARG   B 1 148 ? 27.630 -15.974 -5.975  1.00 13.90 ?  148 ARG   B NH2  1 
ATOM   6234 H H    . ARG   B 1 148 ? 30.924 -19.045 -8.164  1.00 15.66 ?  148 ARG   B H    1 
ATOM   6235 H HA   . ARG   B 1 148 ? 29.778 -20.256 -10.298 1.00 16.05 ?  148 ARG   B HA   1 
ATOM   6236 H HB2  . ARG   B 1 148 ? 29.091 -17.743 -9.201  1.00 16.46 ?  148 ARG   B HB2  1 
ATOM   6237 H HB3  . ARG   B 1 148 ? 28.453 -18.319 -10.538 1.00 16.46 ?  148 ARG   B HB3  1 
ATOM   6238 H HG2  . ARG   B 1 148 ? 27.434 -20.020 -9.359  1.00 17.26 ?  148 ARG   B HG2  1 
ATOM   6239 H HG3  . ARG   B 1 148 ? 28.139 -19.544 -8.017  1.00 17.26 ?  148 ARG   B HG3  1 
ATOM   6240 H HD2  . ARG   B 1 148 ? 26.134 -18.085 -9.373  1.00 18.31 ?  148 ARG   B HD2  1 
ATOM   6241 H HD3  . ARG   B 1 148 ? 25.921 -18.858 -7.999  1.00 18.31 ?  148 ARG   B HD3  1 
ATOM   6242 H HE   . ARG   B 1 148 ? 26.998 -16.427 -8.252  1.00 18.14 ?  148 ARG   B HE   1 
ATOM   6243 H HH11 . ARG   B 1 148 ? 26.900 -18.956 -6.091  1.00 17.02 ?  148 ARG   B HH11 1 
ATOM   6244 H HH12 . ARG   B 1 148 ? 27.346 -18.157 -4.916  1.00 17.02 ?  148 ARG   B HH12 1 
ATOM   6245 H HH21 . ARG   B 1 148 ? 27.690 -15.269 -6.461  1.00 16.70 ?  148 ARG   B HH21 1 
ATOM   6246 H HH22 . ARG   B 1 148 ? 27.822 -15.937 -5.137  1.00 16.70 ?  148 ARG   B HH22 1 
ATOM   6247 N N    . THR   B 1 149 ? 32.134 -18.200 -10.373 1.00 13.20 ?  149 THR   B N    1 
ATOM   6248 C CA   . THR   B 1 149 ? 33.177 -17.641 -11.217 1.00 13.16 ?  149 THR   B CA   1 
ATOM   6249 C C    . THR   B 1 149 ? 34.061 -18.783 -11.722 1.00 12.95 ?  149 THR   B C    1 
ATOM   6250 O O    . THR   B 1 149 ? 33.866 -19.952 -11.375 1.00 13.29 ?  149 THR   B O    1 
ATOM   6251 C CB   . THR   B 1 149 ? 33.946 -16.588 -10.428 1.00 13.10 ?  149 THR   B CB   1 
ATOM   6252 O OG1  . THR   B 1 149 ? 34.402 -17.183 -9.210  1.00 13.12 ?  149 THR   B OG1  1 
ATOM   6253 C CG2  . THR   B 1 149 ? 33.060 -15.374 -10.135 1.00 13.93 ?  149 THR   B CG2  1 
ATOM   6254 H H    . THR   B 1 149 ? 32.291 -18.122 -9.534  1.00 15.86 ?  149 THR   B H    1 
ATOM   6255 H HA   . THR   B 1 149 ? 32.773 -17.204 -11.982 1.00 15.81 ?  149 THR   B HA   1 
ATOM   6256 H HB   . THR   B 1 149 ? 34.712 -16.300 -10.939 1.00 15.74 ?  149 THR   B HB   1 
ATOM   6257 H HG1  . THR   B 1 149 ? 34.817 -16.612 -8.744  1.00 15.77 ?  149 THR   B HG1  1 
ATOM   6258 H HG21 . THR   B 1 149 ? 33.570 -14.708 -9.641  1.00 16.73 ?  149 THR   B HG21 1 
ATOM   6259 H HG22 . THR   B 1 149 ? 32.758 -14.980 -10.968 1.00 16.73 ?  149 THR   B HG22 1 
ATOM   6260 H HG23 . THR   B 1 149 ? 32.293 -15.637 -9.609  1.00 16.73 ?  149 THR   B HG23 1 
ATOM   6261 N N    . ASN   B 1 150 ? 35.027 -18.465 -12.574 1.00 12.92 ?  150 ASN   B N    1 
ATOM   6262 C CA   . ASN   B 1 150 ? 35.790 -19.494 -13.270 1.00 13.26 ?  150 ASN   B CA   1 
ATOM   6263 C C    . ASN   B 1 150 ? 36.953 -19.942 -12.394 1.00 12.87 ?  150 ASN   B C    1 
ATOM   6264 O O    . ASN   B 1 150 ? 37.884 -19.170 -12.137 1.00 13.37 ?  150 ASN   B O    1 
ATOM   6265 C CB   . ASN   B 1 150 ? 36.262 -18.970 -14.619 1.00 14.95 ?  150 ASN   B CB   1 
ATOM   6266 C CG   . ASN   B 1 150 ? 35.117 -18.737 -15.559 1.00 17.65 ?  150 ASN   B CG   1 
ATOM   6267 O OD1  . ASN   B 1 150 ? 34.232 -19.575 -15.673 1.00 18.93 ?  150 ASN   B OD1  1 
ATOM   6268 N ND2  . ASN   B 1 150 ? 35.097 -17.585 -16.205 1.00 18.97 ?  150 ASN   B ND2  1 
ATOM   6269 H H    . ASN   B 1 150 ? 35.270 -17.657 -12.762 1.00 15.52 ?  150 ASN   B H    1 
ATOM   6270 H HA   . ASN   B 1 150 ? 35.211 -20.260 -13.429 1.00 15.93 ?  150 ASN   B HA   1 
ATOM   6271 H HB2  . ASN   B 1 150 ? 36.719 -18.126 -14.489 1.00 17.96 ?  150 ASN   B HB2  1 
ATOM   6272 H HB3  . ASN   B 1 150 ? 36.855 -19.618 -15.022 1.00 17.96 ?  150 ASN   B HB3  1 
ATOM   6273 H HD21 . ASN   B 1 150 ? 34.456 -17.405 -16.752 1.00 22.79 ?  150 ASN   B HD21 1 
ATOM   6274 H HD22 . ASN   B 1 150 ? 35.731 -17.015 -16.088 1.00 22.79 ?  150 ASN   B HD22 1 
ATOM   6275 N N    . VAL   B 1 151 ? 36.908 -21.190 -11.938 1.00 12.76 ?  151 VAL   B N    1 
ATOM   6276 C CA   . VAL   B 1 151 ? 37.927 -21.719 -11.046 1.00 12.72 ?  151 VAL   B CA   1 
ATOM   6277 C C    . VAL   B 1 151 ? 38.635 -22.887 -11.721 1.00 12.55 ?  151 VAL   B C    1 
ATOM   6278 O O    . VAL   B 1 151 ? 37.994 -23.820 -12.228 1.00 13.42 ?  151 VAL   B O    1 
ATOM   6279 C CB   . VAL   B 1 151 ? 37.369 -22.057 -9.649  1.00 14.03 ?  151 VAL   B CB   1 
ATOM   6280 C CG1  . VAL   B 1 151 ? 36.205 -23.052 -9.727  1.00 14.85 ?  151 VAL   B CG1  1 
ATOM   6281 C CG2  . VAL   B 1 151 ? 38.484 -22.545 -8.734  1.00 14.43 ?  151 VAL   B CG2  1 
ATOM   6282 H H    . VAL   B 1 151 ? 36.285 -21.754 -12.141 1.00 15.34 ?  151 VAL   B H    1 
ATOM   6283 H HA   . VAL   B 1 151 ? 38.590 -21.023 -10.916 1.00 15.28 ?  151 VAL   B HA   1 
ATOM   6284 H HB   . VAL   B 1 151 ? 37.017 -21.240 -9.260  1.00 16.86 ?  151 VAL   B HB   1 
ATOM   6285 H HG11 . VAL   B 1 151 ? 35.889 -23.243 -8.828  1.00 17.84 ?  151 VAL   B HG11 1 
ATOM   6286 H HG12 . VAL   B 1 151 ? 35.485 -22.663 -10.251 1.00 17.84 ?  151 VAL   B HG12 1 
ATOM   6287 H HG13 . VAL   B 1 151 ? 36.511 -23.871 -10.148 1.00 17.84 ?  151 VAL   B HG13 1 
ATOM   6288 H HG21 . VAL   B 1 151 ? 38.137 -22.623 -7.831  1.00 17.33 ?  151 VAL   B HG21 1 
ATOM   6289 H HG22 . VAL   B 1 151 ? 38.795 -23.410 -9.043  1.00 17.33 ?  151 VAL   B HG22 1 
ATOM   6290 H HG23 . VAL   B 1 151 ? 39.212 -21.904 -8.752  1.00 17.33 ?  151 VAL   B HG23 1 
ATOM   6291 N N    . TYR   B 1 152 ? 39.965 -22.794 -11.744 1.00 11.90 ?  152 TYR   B N    1 
ATOM   6292 C CA   . TYR   B 1 152 ? 40.871 -23.777 -12.320 1.00 12.11 ?  152 TYR   B CA   1 
ATOM   6293 C C    . TYR   B 1 152 ? 41.591 -24.451 -11.157 1.00 11.53 ?  152 TYR   B C    1 
ATOM   6294 O O    . TYR   B 1 152 ? 42.441 -23.832 -10.508 1.00 12.07 ?  152 TYR   B O    1 
ATOM   6295 C CB   . TYR   B 1 152 ? 41.839 -23.078 -13.275 1.00 13.02 ?  152 TYR   B CB   1 
ATOM   6296 C CG   . TYR   B 1 152 ? 41.156 -22.614 -14.540 1.00 13.67 ?  152 TYR   B CG   1 
ATOM   6297 C CD1  . TYR   B 1 152 ? 40.485 -21.393 -14.601 1.00 14.06 ?  152 TYR   B CD1  1 
ATOM   6298 C CD2  . TYR   B 1 152 ? 41.149 -23.422 -15.666 1.00 14.75 ?  152 TYR   B CD2  1 
ATOM   6299 C CE1  . TYR   B 1 152 ? 39.841 -20.996 -15.757 1.00 15.30 ?  152 TYR   B CE1  1 
ATOM   6300 C CE2  . TYR   B 1 152 ? 40.514 -23.034 -16.820 1.00 15.55 ?  152 TYR   B CE2  1 
ATOM   6301 C CZ   . TYR   B 1 152 ? 39.863 -21.819 -16.865 1.00 15.69 ?  152 TYR   B CZ   1 
ATOM   6302 O OH   . TYR   B 1 152 ? 39.232 -21.453 -18.028 1.00 18.02 ?  152 TYR   B OH   1 
ATOM   6303 H H    . TYR   B 1 152 ? 40.394 -22.122 -11.403 1.00 14.30 ?  152 TYR   B H    1 
ATOM   6304 H HA   . TYR   B 1 152 ? 40.360 -24.446 -12.809 1.00 14.55 ?  152 TYR   B HA   1 
ATOM   6305 H HB2  . TYR   B 1 152 ? 42.213 -22.304 -12.828 1.00 15.65 ?  152 TYR   B HB2  1 
ATOM   6306 H HB3  . TYR   B 1 152 ? 42.545 -23.696 -13.517 1.00 15.65 ?  152 TYR   B HB3  1 
ATOM   6307 H HD1  . TYR   B 1 152 ? 40.464 -20.839 -13.854 1.00 16.89 ?  152 TYR   B HD1  1 
ATOM   6308 H HD2  . TYR   B 1 152 ? 41.586 -24.245 -15.640 1.00 17.72 ?  152 TYR   B HD2  1 
ATOM   6309 H HE1  . TYR   B 1 152 ? 39.401 -20.179 -15.792 1.00 18.38 ?  152 TYR   B HE1  1 
ATOM   6310 H HE2  . TYR   B 1 152 ? 40.529 -23.588 -17.568 1.00 18.68 ?  152 TYR   B HE2  1 
ATOM   6311 H HH   . TYR   B 1 152 ? 38.872 -20.699 -17.932 1.00 21.64 ?  152 TYR   B HH   1 
ATOM   6312 N N    . LEU   B 1 153 ? 41.219 -25.703 -10.877 1.00 11.83 ?  153 LEU   B N    1 
ATOM   6313 C CA   . LEU   B 1 153 ? 41.730 -26.452 -9.737  1.00 11.81 ?  153 LEU   B CA   1 
ATOM   6314 C C    . LEU   B 1 153 ? 42.961 -27.248 -10.135 1.00 12.16 ?  153 LEU   B C    1 
ATOM   6315 O O    . LEU   B 1 153 ? 42.942 -27.976 -11.131 1.00 13.25 ?  153 LEU   B O    1 
ATOM   6316 C CB   . LEU   B 1 153 ? 40.654 -27.413 -9.221  1.00 12.05 ?  153 LEU   B CB   1 
ATOM   6317 C CG   . LEU   B 1 153 ? 39.391 -26.755 -8.662  1.00 12.97 ?  153 LEU   B CG   1 
ATOM   6318 C CD1  . LEU   B 1 153 ? 38.283 -27.785 -8.497  1.00 13.78 ?  153 LEU   B CD1  1 
ATOM   6319 C CD2  . LEU   B 1 153 ? 39.687 -26.091 -7.326  1.00 13.74 ?  153 LEU   B CD2  1 
ATOM   6320 H H    . LEU   B 1 153 ? 40.640 -26.143 -11.342 1.00 14.22 ?  153 LEU   B H    1 
ATOM   6321 H HA   . LEU   B 1 153 ? 41.960 -25.838 -9.026  1.00 14.19 ?  153 LEU   B HA   1 
ATOM   6322 H HB2  . LEU   B 1 153 ? 40.377 -27.990 -9.947  1.00 14.48 ?  153 LEU   B HB2  1 
ATOM   6323 H HB3  . LEU   B 1 153 ? 41.037 -27.949 -8.507  1.00 14.48 ?  153 LEU   B HB3  1 
ATOM   6324 H HG   . LEU   B 1 153 ? 39.084 -26.066 -9.276  1.00 15.59 ?  153 LEU   B HG   1 
ATOM   6325 H HD11 . LEU   B 1 153 ? 37.472 -27.329 -8.211  1.00 16.56 ?  153 LEU   B HD11 1 
ATOM   6326 H HD12 . LEU   B 1 153 ? 38.136 -28.220 -9.345  1.00 16.56 ?  153 LEU   B HD12 1 
ATOM   6327 H HD13 . LEU   B 1 153 ? 38.553 -28.427 -7.826  1.00 16.56 ?  153 LEU   B HD13 1 
ATOM   6328 H HD21 . LEU   B 1 153 ? 38.871 -25.713 -6.965  1.00 16.50 ?  153 LEU   B HD21 1 
ATOM   6329 H HD22 . LEU   B 1 153 ? 40.045 -26.754 -6.715  1.00 16.50 ?  153 LEU   B HD22 1 
ATOM   6330 H HD23 . LEU   B 1 153 ? 40.344 -25.383 -7.460  1.00 16.50 ?  153 LEU   B HD23 1 
ATOM   6331 N N    . ALA   B 1 154 ? 44.012 -27.142 -9.332  1.00 12.14 ?  154 ALA   B N    1 
ATOM   6332 C CA   . ALA   B 1 154 ? 45.236 -27.908 -9.518  1.00 13.39 ?  154 ALA   B CA   1 
ATOM   6333 C C    . ALA   B 1 154 ? 45.301 -28.983 -8.442  1.00 13.57 ?  154 ALA   B C    1 
ATOM   6334 O O    . ALA   B 1 154 ? 45.227 -28.679 -7.245  1.00 14.85 ?  154 ALA   B O    1 
ATOM   6335 C CB   . ALA   B 1 154 ? 46.459 -26.996 -9.448  1.00 14.03 ?  154 ALA   B CB   1 
ATOM   6336 H H    . ALA   B 1 154 ? 44.034 -26.614 -8.651  1.00 14.59 ?  154 ALA   B H    1 
ATOM   6337 H HA   . ALA   B 1 154 ? 45.224 -28.334 -10.386 1.00 16.09 ?  154 ALA   B HA   1 
ATOM   6338 H HB1  . ALA   B 1 154 ? 47.261 -27.526 -9.573  1.00 16.85 ?  154 ALA   B HB1  1 
ATOM   6339 H HB2  . ALA   B 1 154 ? 46.398 -26.322 -10.146 1.00 16.85 ?  154 ALA   B HB2  1 
ATOM   6340 H HB3  . ALA   B 1 154 ? 46.486 -26.561 -8.578  1.00 16.85 ?  154 ALA   B HB3  1 
ATOM   6341 N N    . VAL   B 1 155 ? 45.427 -30.232 -8.872  1.00 12.99 ?  155 VAL   B N    1 
ATOM   6342 C CA   . VAL   B 1 155 ? 45.538 -31.378 -7.978  1.00 13.23 ?  155 VAL   B CA   1 
ATOM   6343 C C    . VAL   B 1 155 ? 46.878 -32.051 -8.252  1.00 13.25 ?  155 VAL   B C    1 
ATOM   6344 O O    . VAL   B 1 155 ? 47.121 -32.539 -9.364  1.00 15.05 ?  155 VAL   B O    1 
ATOM   6345 C CB   . VAL   B 1 155 ? 44.380 -32.369 -8.173  1.00 14.73 ?  155 VAL   B CB   1 
ATOM   6346 C CG1  . VAL   B 1 155 ? 44.559 -33.563 -7.257  1.00 14.67 ?  155 VAL   B CG1  1 
ATOM   6347 C CG2  . VAL   B 1 155 ? 43.040 -31.675 -7.914  1.00 15.54 ?  155 VAL   B CG2  1 
ATOM   6348 H H    . VAL   B 1 155 ? 45.464 -30.447 -9.706  1.00 15.61 ?  155 VAL   B H    1 
ATOM   6349 H HA   . VAL   B 1 155 ? 45.529 -31.074 -7.057  1.00 15.89 ?  155 VAL   B HA   1 
ATOM   6350 H HB   . VAL   B 1 155 ? 44.382 -32.684 -9.091  1.00 17.70 ?  155 VAL   B HB   1 
ATOM   6351 H HG11 . VAL   B 1 155 ? 43.729 -34.066 -7.222  1.00 17.62 ?  155 VAL   B HG11 1 
ATOM   6352 H HG12 . VAL   B 1 155 ? 45.269 -34.130 -7.601  1.00 17.62 ?  155 VAL   B HG12 1 
ATOM   6353 H HG13 . VAL   B 1 155 ? 44.790 -33.252 -6.366  1.00 17.62 ?  155 VAL   B HG13 1 
ATOM   6354 H HG21 . VAL   B 1 155 ? 42.326 -32.327 -8.002  1.00 18.67 ?  155 VAL   B HG21 1 
ATOM   6355 H HG22 . VAL   B 1 155 ? 43.043 -31.308 -7.016  1.00 18.67 ?  155 VAL   B HG22 1 
ATOM   6356 H HG23 . VAL   B 1 155 ? 42.919 -30.964 -8.562  1.00 18.67 ?  155 VAL   B HG23 1 
ATOM   6357 N N    . PHE   B 1 156 ? 47.739 -32.093 -7.235  1.00 13.77 ?  156 PHE   B N    1 
ATOM   6358 C CA   . PHE   B 1 156 ? 49.116 -32.543 -7.436  1.00 14.98 ?  156 PHE   B CA   1 
ATOM   6359 C C    . PHE   B 1 156 ? 49.215 -34.043 -7.721  1.00 15.79 ?  156 PHE   B C    1 
ATOM   6360 O O    . PHE   B 1 156 ? 49.939 -34.468 -8.633  1.00 17.79 ?  156 PHE   B O    1 
ATOM   6361 C CB   . PHE   B 1 156 ? 49.948 -32.169 -6.211  1.00 15.16 ?  156 PHE   B CB   1 
ATOM   6362 C CG   . PHE   B 1 156 ? 51.369 -32.633 -6.272  1.00 15.77 ?  156 PHE   B CG   1 
ATOM   6363 C CD1  . PHE   B 1 156 ? 52.248 -32.090 -7.190  1.00 17.33 ?  156 PHE   B CD1  1 
ATOM   6364 C CD2  . PHE   B 1 156 ? 51.829 -33.599 -5.401  1.00 16.39 ?  156 PHE   B CD2  1 
ATOM   6365 C CE1  . PHE   B 1 156 ? 53.564 -32.502 -7.244  1.00 18.13 ?  156 PHE   B CE1  1 
ATOM   6366 C CE2  . PHE   B 1 156 ? 53.146 -34.019 -5.451  1.00 17.68 ?  156 PHE   B CE2  1 
ATOM   6367 C CZ   . PHE   B 1 156 ? 54.007 -33.471 -6.378  1.00 18.08 ?  156 PHE   B CZ   1 
ATOM   6368 H H    . PHE   B 1 156 ? 47.549 -31.876 -6.426  1.00 16.54 ?  156 PHE   B H    1 
ATOM   6369 H HA   . PHE   B 1 156 ? 49.484 -32.075 -8.197  1.00 18.00 ?  156 PHE   B HA   1 
ATOM   6370 H HB2  . PHE   B 1 156 ? 49.957 -31.202 -6.126  1.00 18.22 ?  156 PHE   B HB2  1 
ATOM   6371 H HB3  . PHE   B 1 156 ? 49.542 -32.562 -5.422  1.00 18.22 ?  156 PHE   B HB3  1 
ATOM   6372 H HD1  . PHE   B 1 156 ? 51.949 -31.431 -7.777  1.00 20.82 ?  156 PHE   B HD1  1 
ATOM   6373 H HD2  . PHE   B 1 156 ? 51.244 -33.974 -4.779  1.00 19.68 ?  156 PHE   B HD2  1 
ATOM   6374 H HE1  . PHE   B 1 156 ? 54.145 -32.129 -7.869  1.00 21.78 ?  156 PHE   B HE1  1 
ATOM   6375 H HE2  . PHE   B 1 156 ? 53.443 -34.679 -4.865  1.00 21.24 ?  156 PHE   B HE2  1 
ATOM   6376 H HZ   . PHE   B 1 156 ? 54.893 -33.754 -6.413  1.00 21.72 ?  156 PHE   B HZ   1 
ATOM   6377 N N    . ASP   B 1 157 ? 48.549 -34.865 -6.920  1.00 16.08 ?  157 ASP   B N    1 
ATOM   6378 C CA   . ASP   B 1 157 ? 48.694 -36.313 -7.013  1.00 17.48 ?  157 ASP   B CA   1 
ATOM   6379 C C    . ASP   B 1 157 ? 47.780 -36.857 -8.107  1.00 17.82 ?  157 ASP   B C    1 
ATOM   6380 O O    . ASP   B 1 157 ? 46.553 -36.737 -8.011  1.00 17.19 ?  157 ASP   B O    1 
ATOM   6381 C CB   . ASP   B 1 157 ? 48.328 -36.924 -5.666  1.00 18.95 ?  157 ASP   B CB   1 
ATOM   6382 C CG   . ASP   B 1 157 ? 48.469 -38.433 -5.646  1.00 20.82 ?  157 ASP   B CG   1 
ATOM   6383 O OD1  . ASP   B 1 157 ? 48.819 -39.030 -6.689  1.00 21.32 ?  157 ASP   B OD1  1 
ATOM   6384 O OD2  . ASP   B 1 157 ? 48.231 -39.018 -4.572  1.00 22.75 -1 157 ASP   B OD2  1 
ATOM   6385 H H    . ASP   B 1 157 ? 48.009 -34.607 -6.308  1.00 19.32 ?  157 ASP   B H    1 
ATOM   6386 H HA   . ASP   B 1 157 ? 49.614 -36.545 -7.225  1.00 21.00 ?  157 ASP   B HA   1 
ATOM   6387 H HB2  . ASP   B 1 157 ? 48.899 -36.542 -4.984  1.00 22.76 ?  157 ASP   B HB2  1 
ATOM   6388 H HB3  . ASP   B 1 157 ? 47.398 -36.709 -5.471  1.00 22.76 ?  157 ASP   B HB3  1 
ATOM   6389 N N    . LYS   B 1 158 ? 48.378 -37.475 -9.134  1.00 18.65 ?  158 LYS   B N    1 
ATOM   6390 C CA   . LYS   B 1 158 ? 47.604 -38.092 -10.214 1.00 19.56 ?  158 LYS   B CA   1 
ATOM   6391 C C    . LYS   B 1 158 ? 46.545 -39.055 -9.681  1.00 19.37 ?  158 LYS   B C    1 
ATOM   6392 O O    . LYS   B 1 158 ? 45.438 -39.143 -10.230 1.00 19.67 ?  158 LYS   B O    1 
ATOM   6393 C CB   . LYS   B 1 158 ? 48.551 -38.820 -11.179 1.00 21.32 ?  158 LYS   B CB   1 
ATOM   6394 C CG   . LYS   B 1 158 ? 47.871 -39.707 -12.217 1.00 23.51 ?  158 LYS   B CG   1 
ATOM   6395 C CD   . LYS   B 1 158 ? 47.019 -38.912 -13.186 1.00 25.63 ?  158 LYS   B CD   1 
ATOM   6396 C CE   . LYS   B 1 158 ? 46.412 -39.819 -14.244 1.00 27.33 ?  158 LYS   B CE   1 
ATOM   6397 N NZ   . LYS   B 1 158 ? 45.346 -39.133 -15.026 1.00 27.71 ?  158 LYS   B NZ   1 
ATOM   6398 H H    . LYS   B 1 158 ? 49.233 -37.550 -9.229  1.00 22.40 ?  158 LYS   B H    1 
ATOM   6399 H HA   . LYS   B 1 158 ? 47.154 -37.397 -10.718 1.00 23.49 ?  158 LYS   B HA   1 
ATOM   6400 H HB2  . LYS   B 1 158 ? 49.070 -38.157 -11.667 1.00 25.60 ?  158 LYS   B HB2  1 
ATOM   6401 H HB3  . LYS   B 1 158 ? 49.150 -39.382 -10.665 1.00 25.60 ?  158 LYS   B HB3  1 
ATOM   6402 H HG2  . LYS   B 1 158 ? 48.555 -40.165 -12.732 1.00 28.23 ?  158 LYS   B HG2  1 
ATOM   6403 H HG3  . LYS   B 1 158 ? 47.307 -40.361 -11.775 1.00 28.23 ?  158 LYS   B HG3  1 
ATOM   6404 H HD2  . LYS   B 1 158 ? 46.298 -38.480 -12.702 1.00 30.78 ?  158 LYS   B HD2  1 
ATOM   6405 H HD3  . LYS   B 1 158 ? 47.571 -38.250 -13.632 1.00 30.78 ?  158 LYS   B HD3  1 
ATOM   6406 H HE2  . LYS   B 1 158 ? 47.105 -40.099 -14.860 1.00 32.82 ?  158 LYS   B HE2  1 
ATOM   6407 H HE3  . LYS   B 1 158 ? 46.017 -40.594 -13.811 1.00 32.82 ?  158 LYS   B HE3  1 
ATOM   6408 H HZ1  . LYS   B 1 158 ? 45.009 -39.687 -15.635 1.00 33.27 ?  158 LYS   B HZ1  1 
ATOM   6409 H HZ2  . LYS   B 1 158 ? 44.691 -38.868 -14.483 1.00 33.27 ?  158 LYS   B HZ2  1 
ATOM   6410 H HZ3  . LYS   B 1 158 ? 45.683 -38.420 -15.439 1.00 33.27 ?  158 LYS   B HZ3  1 
ATOM   6411 N N    . ASN   B 1 159 ? 46.869 -39.812 -8.631  1.00 19.71 ?  159 ASN   B N    1 
ATOM   6412 C CA   . ASN   B 1 159 ? 45.913 -40.794 -8.126  1.00 20.41 ?  159 ASN   B CA   1 
ATOM   6413 C C    . ASN   B 1 159 ? 44.713 -40.121 -7.456  1.00 19.33 ?  159 ASN   B C    1 
ATOM   6414 O O    . ASN   B 1 159 ? 43.580 -40.609 -7.567  1.00 19.69 ?  159 ASN   B O    1 
ATOM   6415 C CB   . ASN   B 1 159 ? 46.614 -41.774 -7.189  1.00 22.04 ?  159 ASN   B CB   1 
ATOM   6416 C CG   . ASN   B 1 159 ? 47.640 -42.621 -7.906  1.00 24.18 ?  159 ASN   B CG   1 
ATOM   6417 O OD1  . ASN   B 1 159 ? 47.395 -43.114 -9.014  1.00 24.95 ?  159 ASN   B OD1  1 
ATOM   6418 N ND2  . ASN   B 1 159 ? 48.798 -42.802 -7.279  1.00 24.97 ?  159 ASN   B ND2  1 
ATOM   6419 H H    . ASN   B 1 159 ? 47.613 -39.769 -8.207  1.00 23.67 ?  159 ASN   B H    1 
ATOM   6420 H HA   . ASN   B 1 159 ? 45.576 -41.302 -8.880  1.00 24.51 ?  159 ASN   B HA   1 
ATOM   6421 H HB2  . ASN   B 1 159 ? 47.069 -41.281 -6.492  1.00 26.47 ?  159 ASN   B HB2  1 
ATOM   6422 H HB3  . ASN   B 1 159 ? 45.954 -42.371 -6.805  1.00 26.47 ?  159 ASN   B HB3  1 
ATOM   6423 H HD21 . ASN   B 1 159 ? 49.418 -43.281 -7.643  1.00 29.99 ?  159 ASN   B HD21 1 
ATOM   6424 H HD22 . ASN   B 1 159 ? 48.928 -42.459 -6.501  1.00 29.99 ?  159 ASN   B HD22 1 
ATOM   6425 N N    . LEU   B 1 160 ? 44.928 -38.991 -6.771  1.00 18.14 ?  160 LEU   B N    1 
ATOM   6426 C CA   . LEU   B 1 160 ? 43.793 -38.254 -6.229  1.00 17.32 ?  160 LEU   B CA   1 
ATOM   6427 C C    . LEU   B 1 160 ? 43.005 -37.586 -7.344  1.00 16.79 ?  160 LEU   B C    1 
ATOM   6428 O O    . LEU   B 1 160 ? 41.769 -37.583 -7.322  1.00 16.47 ?  160 LEU   B O    1 
ATOM   6429 C CB   . LEU   B 1 160 ? 44.261 -37.225 -5.200  1.00 17.20 ?  160 LEU   B CB   1 
ATOM   6430 C CG   . LEU   B 1 160 ? 43.140 -36.326 -4.662  1.00 16.96 ?  160 LEU   B CG   1 
ATOM   6431 C CD1  . LEU   B 1 160 ? 42.018 -37.160 -4.055  1.00 17.66 ?  160 LEU   B CD1  1 
ATOM   6432 C CD2  . LEU   B 1 160 ? 43.676 -35.334 -3.644  1.00 17.28 ?  160 LEU   B CD2  1 
ATOM   6433 H H    . LEU   B 1 160 ? 45.703 -38.651 -6.610  1.00 21.79 ?  160 LEU   B H    1 
ATOM   6434 H HA   . LEU   B 1 160 ? 43.207 -38.882 -5.781  1.00 20.80 ?  160 LEU   B HA   1 
ATOM   6435 H HB2  . LEU   B 1 160 ? 44.656 -37.695 -4.447  1.00 20.66 ?  160 LEU   B HB2  1 
ATOM   6436 H HB3  . LEU   B 1 160 ? 44.929 -36.654 -5.613  1.00 20.66 ?  160 LEU   B HB3  1 
ATOM   6437 H HG   . LEU   B 1 160 ? 42.767 -35.821 -5.398  1.00 20.37 ?  160 LEU   B HG   1 
ATOM   6438 H HD11 . LEU   B 1 160 ? 41.393 -36.570 -3.611  1.00 21.21 ?  160 LEU   B HD11 1 
ATOM   6439 H HD12 . LEU   B 1 160 ? 41.564 -37.651 -4.760  1.00 21.21 ?  160 LEU   B HD12 1 
ATOM   6440 H HD13 . LEU   B 1 160 ? 42.397 -37.784 -3.413  1.00 21.21 ?  160 LEU   B HD13 1 
ATOM   6441 H HD21 . LEU   B 1 160 ? 42.951 -34.761 -3.355  1.00 20.76 ?  160 LEU   B HD21 1 
ATOM   6442 H HD22 . LEU   B 1 160 ? 44.036 -35.823 -2.887  1.00 20.76 ?  160 LEU   B HD22 1 
ATOM   6443 H HD23 . LEU   B 1 160 ? 44.375 -34.805 -4.059  1.00 20.76 ?  160 LEU   B HD23 1 
ATOM   6444 N N    . TYR   B 1 161 ? 43.705 -37.020 -8.331  1.00 16.76 ?  161 TYR   B N    1 
ATOM   6445 C CA   . TYR   B 1 161 ? 43.029 -36.448 -9.491  1.00 16.54 ?  161 TYR   B CA   1 
ATOM   6446 C C    . TYR   B 1 161 ? 42.083 -37.468 -10.113 1.00 16.61 ?  161 TYR   B C    1 
ATOM   6447 O O    . TYR   B 1 161 ? 40.911 -37.174 -10.374 1.00 16.51 ?  161 TYR   B O    1 
ATOM   6448 C CB   . TYR   B 1 161 ? 44.069 -35.969 -10.512 1.00 17.10 ?  161 TYR   B CB   1 
ATOM   6449 C CG   . TYR   B 1 161 ? 43.491 -35.500 -11.828 1.00 17.68 ?  161 TYR   B CG   1 
ATOM   6450 C CD1  . TYR   B 1 161 ? 43.097 -34.178 -11.999 1.00 18.00 ?  161 TYR   B CD1  1 
ATOM   6451 C CD2  . TYR   B 1 161 ? 43.324 -36.380 -12.896 1.00 18.14 ?  161 TYR   B CD2  1 
ATOM   6452 C CE1  . TYR   B 1 161 ? 42.565 -33.746 -13.187 1.00 18.99 ?  161 TYR   B CE1  1 
ATOM   6453 C CE2  . TYR   B 1 161 ? 42.788 -35.953 -14.090 1.00 19.39 ?  161 TYR   B CE2  1 
ATOM   6454 C CZ   . TYR   B 1 161 ? 42.412 -34.632 -14.230 1.00 19.70 ?  161 TYR   B CZ   1 
ATOM   6455 O OH   . TYR   B 1 161 ? 41.878 -34.189 -15.414 1.00 21.55 ?  161 TYR   B OH   1 
ATOM   6456 H H    . TYR   B 1 161 ? 44.560 -36.968 -8.359  1.00 20.13 ?  161 TYR   B H    1 
ATOM   6457 H HA   . TYR   B 1 161 ? 42.503 -35.687 -9.213  1.00 19.87 ?  161 TYR   B HA   1 
ATOM   6458 H HB2  . TYR   B 1 161 ? 44.559 -35.225 -10.126 1.00 20.54 ?  161 TYR   B HB2  1 
ATOM   6459 H HB3  . TYR   B 1 161 ? 44.679 -36.698 -10.704 1.00 20.54 ?  161 TYR   B HB3  1 
ATOM   6460 H HD1  . TYR   B 1 161 ? 43.197 -33.571 -11.300 1.00 21.62 ?  161 TYR   B HD1  1 
ATOM   6461 H HD2  . TYR   B 1 161 ? 43.573 -37.270 -12.804 1.00 21.79 ?  161 TYR   B HD2  1 
ATOM   6462 H HE1  . TYR   B 1 161 ? 42.310 -32.852 -13.283 1.00 22.81 ?  161 TYR   B HE1  1 
ATOM   6463 H HE2  . TYR   B 1 161 ? 42.680 -36.545 -14.798 1.00 23.29 ?  161 TYR   B HE2  1 
ATOM   6464 H HH   . TYR   B 1 161 ? 41.832 -34.823 -15.965 1.00 25.88 ?  161 TYR   B HH   1 
ATOM   6465 N N    . ASP   B 1 162 ? 42.579 -38.688 -10.338 1.00 17.08 ?  162 ASP   B N    1 
ATOM   6466 C CA   . ASP   B 1 162 ? 41.754 -39.726 -10.949 1.00 17.63 ?  162 ASP   B CA   1 
ATOM   6467 C C    . ASP   B 1 162 ? 40.546 -40.063 -10.082 1.00 17.02 ?  162 ASP   B C    1 
ATOM   6468 O O    . ASP   B 1 162 ? 39.440 -40.274 -10.598 1.00 17.43 ?  162 ASP   B O    1 
ATOM   6469 C CB   . ASP   B 1 162 ? 42.587 -40.986 -11.201 1.00 19.02 ?  162 ASP   B CB   1 
ATOM   6470 C CG   . ASP   B 1 162 ? 43.581 -40.820 -12.335 1.00 20.60 ?  162 ASP   B CG   1 
ATOM   6471 O OD1  . ASP   B 1 162 ? 43.450 -39.871 -13.133 1.00 20.89 ?  162 ASP   B OD1  1 
ATOM   6472 O OD2  . ASP   B 1 162 ? 44.488 -41.670 -12.442 1.00 22.25 -1 162 ASP   B OD2  1 
ATOM   6473 H H    . ASP   B 1 162 ? 43.382 -38.934 -10.152 1.00 20.52 ?  162 ASP   B H    1 
ATOM   6474 H HA   . ASP   B 1 162 ? 41.430 -39.415 -11.806 1.00 21.18 ?  162 ASP   B HA   1 
ATOM   6475 H HB2  . ASP   B 1 162 ? 43.096 -41.201 -10.404 1.00 22.84 ?  162 ASP   B HB2  1 
ATOM   6476 H HB3  . ASP   B 1 162 ? 41.998 -41.723 -11.428 1.00 22.84 ?  162 ASP   B HB3  1 
ATOM   6477 N N    A LYS   B 1 163 ? 40.739 -40.140 -8.764  0.72 16.36 ?  163 LYS   B N    1 
ATOM   6478 N N    B LYS   B 1 163 ? 40.734 -40.122 -8.761  0.28 17.14 ?  163 LYS   B N    1 
ATOM   6479 C CA   A LYS   B 1 163 ? 39.610 -40.407 -7.878  0.72 16.67 ?  163 LYS   B CA   1 
ATOM   6480 C CA   B LYS   B 1 163 ? 39.610 -40.408 -7.875  0.28 17.65 ?  163 LYS   B CA   1 
ATOM   6481 C C    A LYS   B 1 163 ? 38.571 -39.294 -7.954  0.72 15.82 ?  163 LYS   B C    1 
ATOM   6482 C C    B LYS   B 1 163 ? 38.572 -39.292 -7.921  0.28 16.26 ?  163 LYS   B C    1 
ATOM   6483 O O    A LYS   B 1 163 ? 37.361 -39.560 -7.975  0.72 16.66 ?  163 LYS   B O    1 
ATOM   6484 O O    B LYS   B 1 163 ? 37.364 -39.556 -7.885  0.28 16.50 ?  163 LYS   B O    1 
ATOM   6485 C CB   A LYS   B 1 163 ? 40.090 -40.588 -6.441  0.72 19.02 ?  163 LYS   B CB   1 
ATOM   6486 C CB   B LYS   B 1 163 ? 40.106 -40.615 -6.445  0.28 19.92 ?  163 LYS   B CB   1 
ATOM   6487 C CG   A LYS   B 1 163 ? 39.013 -41.140 -5.529  0.72 23.39 ?  163 LYS   B CG   1 
ATOM   6488 C CG   B LYS   B 1 163 ? 39.027 -41.117 -5.505  0.28 22.64 ?  163 LYS   B CG   1 
ATOM   6489 C CD   A LYS   B 1 163 ? 39.428 -41.160 -4.071  0.72 27.17 ?  163 LYS   B CD   1 
ATOM   6490 C CD   B LYS   B 1 163 ? 39.525 -41.255 -4.079  0.28 25.21 ?  163 LYS   B CD   1 
ATOM   6491 C CE   A LYS   B 1 163 ? 38.352 -41.834 -3.229  0.72 29.82 ?  163 LYS   B CE   1 
ATOM   6492 C CE   B LYS   B 1 163 ? 38.470 -41.919 -3.208  0.28 27.08 ?  163 LYS   B CE   1 
ATOM   6493 N NZ   A LYS   B 1 163 ? 38.458 -41.497 -1.783  0.72 31.44 ?  163 LYS   B NZ   1 
ATOM   6494 N NZ   B LYS   B 1 163 ? 38.688 -41.666 -1.758  0.28 28.08 ?  163 LYS   B NZ   1 
ATOM   6495 H H    A LYS   B 1 163 ? 41.498 -40.040 -8.369  0.72 19.65 ?  163 LYS   B H    1 
ATOM   6496 H H    B LYS   B 1 163 ? 41.488 -40.004 -8.364  0.28 20.59 ?  163 LYS   B H    1 
ATOM   6497 H HA   A LYS   B 1 163 ? 39.186 -41.231 -8.158  0.72 20.03 ?  163 LYS   B HA   1 
ATOM   6498 H HA   B LYS   B 1 163 ? 39.180 -41.226 -8.166  0.28 21.20 ?  163 LYS   B HA   1 
ATOM   6499 H HB2  A LYS   B 1 163 ? 40.837 -41.210 -6.434  0.72 22.84 ?  163 LYS   B HB2  1 
ATOM   6500 H HB2  B LYS   B 1 163 ? 40.823 -41.268 -6.452  0.28 23.92 ?  163 LYS   B HB2  1 
ATOM   6501 H HB3  A LYS   B 1 163 ? 40.370 -39.731 -6.090  0.72 22.84 ?  163 LYS   B HB3  1 
ATOM   6502 H HB3  B LYS   B 1 163 ? 40.433 -39.770 -6.099  0.28 23.92 ?  163 LYS   B HB3  1 
ATOM   6503 H HG2  A LYS   B 1 163 ? 38.218 -40.590 -5.606  0.72 28.09 ?  163 LYS   B HG2  1 
ATOM   6504 H HG2  B LYS   B 1 163 ? 38.287 -40.491 -5.504  0.28 27.19 ?  163 LYS   B HG2  1 
ATOM   6505 H HG3  A LYS   B 1 163 ? 38.810 -42.053 -5.796  0.72 28.09 ?  163 LYS   B HG3  1 
ATOM   6506 H HG3  B LYS   B 1 163 ? 38.725 -41.989 -5.805  0.28 27.19 ?  163 LYS   B HG3  1 
ATOM   6507 H HD2  A LYS   B 1 163 ? 40.252 -41.664 -3.975  0.72 32.62 ?  163 LYS   B HD2  1 
ATOM   6508 H HD2  B LYS   B 1 163 ? 40.324 -41.806 -4.067  0.28 30.27 ?  163 LYS   B HD2  1 
ATOM   6509 H HD3  A LYS   B 1 163 ? 39.545 -40.252 -3.754  0.72 32.62 ?  163 LYS   B HD3  1 
ATOM   6510 H HD3  B LYS   B 1 163 ? 39.715 -40.376 -3.716  0.28 30.27 ?  163 LYS   B HD3  1 
ATOM   6511 H HE2  A LYS   B 1 163 ? 37.477 -41.558 -3.545  0.72 35.80 ?  163 LYS   B HE2  1 
ATOM   6512 H HE2  B LYS   B 1 163 ? 37.596 -41.575 -3.450  0.28 32.52 ?  163 LYS   B HE2  1 
ATOM   6513 H HE3  A LYS   B 1 163 ? 38.442 -42.794 -3.318  0.72 35.80 ?  163 LYS   B HE3  1 
ATOM   6514 H HE3  B LYS   B 1 163 ? 38.500 -42.878 -3.354  0.28 32.52 ?  163 LYS   B HE3  1 
ATOM   6515 H HZ1  A LYS   B 1 163 ? 37.812 -41.907 -1.329  0.72 37.75 ?  163 LYS   B HZ1  1 
ATOM   6516 H HZ1  B LYS   B 1 163 ? 38.052 -42.068 -1.282  0.28 33.71 ?  163 LYS   B HZ1  1 
ATOM   6517 H HZ2  A LYS   B 1 163 ? 39.246 -41.761 -1.468  0.72 37.75 ?  163 LYS   B HZ2  1 
ATOM   6518 H HZ2  B LYS   B 1 163 ? 39.481 -41.983 -1.511  0.28 33.71 ?  163 LYS   B HZ2  1 
ATOM   6519 H HZ3  A LYS   B 1 163 ? 38.379 -40.618 -1.669  0.72 37.75 ?  163 LYS   B HZ3  1 
ATOM   6520 H HZ3  B LYS   B 1 163 ? 38.661 -40.791 -1.596  0.28 33.71 ?  163 LYS   B HZ3  1 
ATOM   6521 N N    . LEU   B 1 164 ? 39.027 -38.040 -7.995  1.00 15.03 ?  164 LEU   B N    1 
ATOM   6522 C CA   . LEU   B 1 164 ? 38.109 -36.906 -8.051  1.00 14.76 ?  164 LEU   B CA   1 
ATOM   6523 C C    . LEU   B 1 164 ? 37.327 -36.889 -9.360  1.00 14.86 ?  164 LEU   B C    1 
ATOM   6524 O O    . LEU   B 1 164 ? 36.102 -36.695 -9.365  1.00 16.02 ?  164 LEU   B O    1 
ATOM   6525 C CB   . LEU   B 1 164 ? 38.907 -35.613 -7.885  1.00 14.11 ?  164 LEU   B CB   1 
ATOM   6526 C CG   . LEU   B 1 164 ? 39.437 -35.335 -6.480  1.00 15.24 ?  164 LEU   B CG   1 
ATOM   6527 C CD1  . LEU   B 1 164 ? 40.519 -34.270 -6.530  1.00 15.13 ?  164 LEU   B CD1  1 
ATOM   6528 C CD2  . LEU   B 1 164 ? 38.314 -34.904 -5.551  1.00 17.12 ?  164 LEU   B CD2  1 
ATOM   6529 H H    A LEU   B 1 164 ? 39.863 -37.823 -7.986  0.72 18.06 ?  164 LEU   B H    1 
ATOM   6530 H H    B LEU   B 1 164 ? 39.863 -37.824 -8.015  0.28 18.06 ?  164 LEU   B H    1 
ATOM   6531 H HA   . LEU   B 1 164 ? 37.482 -36.969 -7.322  1.00 17.73 ?  164 LEU   B HA   1 
ATOM   6532 H HB2  . LEU   B 1 164 ? 39.679 -35.646 -8.480  1.00 16.96 ?  164 LEU   B HB2  1 
ATOM   6533 H HB3  . LEU   B 1 164 ? 38.345 -34.867 -8.135  1.00 16.96 ?  164 LEU   B HB3  1 
ATOM   6534 H HG   . LEU   B 1 164 ? 39.835 -36.142 -6.123  1.00 18.31 ?  164 LEU   B HG   1 
ATOM   6535 H HD11 . LEU   B 1 164 ? 40.837 -34.093 -5.629  1.00 18.17 ?  164 LEU   B HD11 1 
ATOM   6536 H HD12 . LEU   B 1 164 ? 41.255 -34.584 -7.081  1.00 18.17 ?  164 LEU   B HD12 1 
ATOM   6537 H HD13 . LEU   B 1 164 ? 40.150 -33.455 -6.911  1.00 18.17 ?  164 LEU   B HD13 1 
ATOM   6538 H HD21 . LEU   B 1 164 ? 38.686 -34.682 -4.684  1.00 20.56 ?  164 LEU   B HD21 1 
ATOM   6539 H HD22 . LEU   B 1 164 ? 37.869 -34.130 -5.929  1.00 20.56 ?  164 LEU   B HD22 1 
ATOM   6540 H HD23 . LEU   B 1 164 ? 37.683 -35.637 -5.462  1.00 20.56 ?  164 LEU   B HD23 1 
ATOM   6541 N N    . VAL   B 1 165 ? 38.021 -37.067 -10.486 1.00 16.65 ?  165 VAL   B N    1 
ATOM   6542 C CA   . VAL   B 1 165 ? 37.368 -37.002 -11.788 1.00 17.93 ?  165 VAL   B CA   1 
ATOM   6543 C C    . VAL   B 1 165 ? 36.446 -38.199 -11.974 1.00 19.44 ?  165 VAL   B C    1 
ATOM   6544 O O    . VAL   B 1 165 ? 35.283 -38.057 -12.369 1.00 20.66 ?  165 VAL   B O    1 
ATOM   6545 C CB   . VAL   B 1 165 ? 38.418 -36.920 -12.910 1.00 18.83 ?  165 VAL   B CB   1 
ATOM   6546 C CG1  . VAL   B 1 165 ? 37.762 -37.044 -14.266 1.00 19.99 ?  165 VAL   B CG1  1 
ATOM   6547 C CG2  . VAL   B 1 165 ? 39.194 -35.622 -12.813 1.00 18.58 ?  165 VAL   B CG2  1 
ATOM   6548 H H    . VAL   B 1 165 ? 38.867 -37.229 -10.523 1.00 20.00 ?  165 VAL   B H    1 
ATOM   6549 H HA   . VAL   B 1 165 ? 36.826 -36.204 -11.831 1.00 21.54 ?  165 VAL   B HA   1 
ATOM   6550 H HB   . VAL   B 1 165 ? 39.052 -37.649 -12.810 1.00 22.62 ?  165 VAL   B HB   1 
ATOM   6551 H HG11 . VAL   B 1 165 ? 38.382 -36.744 -14.945 1.00 24.00 ?  165 VAL   B HG11 1 
ATOM   6552 H HG12 . VAL   B 1 165 ? 37.537 -37.977 -14.419 1.00 24.00 ?  165 VAL   B HG12 1 
ATOM   6553 H HG13 . VAL   B 1 165 ? 36.961 -36.503 -14.279 1.00 24.00 ?  165 VAL   B HG13 1 
ATOM   6554 H HG21 . VAL   B 1 165 ? 39.834 -35.576 -13.542 1.00 22.32 ?  165 VAL   B HG21 1 
ATOM   6555 H HG22 . VAL   B 1 165 ? 38.573 -34.877 -12.875 1.00 22.32 ?  165 VAL   B HG22 1 
ATOM   6556 H HG23 . VAL   B 1 165 ? 39.661 -35.590 -11.963 1.00 22.32 ?  165 VAL   B HG23 1 
ATOM   6557 N N    . SER   B 1 166 ? 36.960 -39.399 -11.687 1.00 20.07 ?  166 SER   B N    1 
ATOM   6558 C CA   . SER   B 1 166 ? 36.205 -40.612 -11.968 1.00 20.97 ?  166 SER   B CA   1 
ATOM   6559 C C    . SER   B 1 166 ? 34.946 -40.698 -11.121 1.00 21.07 ?  166 SER   B C    1 
ATOM   6560 O O    . SER   B 1 166 ? 33.972 -41.314 -11.549 1.00 22.22 ?  166 SER   B O    1 
ATOM   6561 C CB   . SER   B 1 166 ? 37.071 -41.866 -11.784 1.00 21.98 ?  166 SER   B CB   1 
ATOM   6562 O OG   . SER   B 1 166 ? 37.437 -42.057 -10.428 1.00 22.21 ?  166 SER   B OG   1 
ATOM   6563 H H    . SER   B 1 166 ? 37.736 -39.537 -11.338 1.00 24.11 ?  166 SER   B H    1 
ATOM   6564 H HA   . SER   B 1 166 ? 35.926 -40.598 -12.896 1.00 25.18 ?  166 SER   B HA   1 
ATOM   6565 H HB2  . SER   B 1 166 ? 36.570 -42.643 -12.082 1.00 26.40 ?  166 SER   B HB2  1 
ATOM   6566 H HB3  . SER   B 1 166 ? 37.875 -41.774 -12.323 1.00 26.40 ?  166 SER   B HB3  1 
ATOM   6567 H HG   . SER   B 1 166 ? 37.889 -41.397 -10.161 1.00 26.67 ?  166 SER   B HG   1 
ATOM   6568 N N    . SER   B 1 167 ? 34.930 -40.089 -9.936  1.00 19.90 ?  167 SER   B N    1 
ATOM   6569 C CA   . SER   B 1 167 ? 33.776 -40.146 -9.047  1.00 19.68 ?  167 SER   B CA   1 
ATOM   6570 C C    . SER   B 1 167 ? 32.859 -38.927 -9.141  1.00 19.30 ?  167 SER   B C    1 
ATOM   6571 O O    . SER   B 1 167 ? 31.783 -38.931 -8.531  1.00 19.65 ?  167 SER   B O    1 
ATOM   6572 C CB   . SER   B 1 167 ? 34.226 -40.328 -7.591  1.00 19.60 ?  167 SER   B CB   1 
ATOM   6573 O OG   . SER   B 1 167 ? 34.886 -39.164 -7.113  1.00 19.33 ?  167 SER   B OG   1 
ATOM   6574 H H    . SER   B 1 167 ? 35.585 -39.637 -9.626  1.00 23.90 ?  167 SER   B H    1 
ATOM   6575 H HA   . SER   B 1 167 ? 33.243 -40.923 -9.283  1.00 23.64 ?  167 SER   B HA   1 
ATOM   6576 H HB2  . SER   B 1 167 ? 33.444 -40.504 -7.041  1.00 23.53 ?  167 SER   B HB2  1 
ATOM   6577 H HB3  . SER   B 1 167 ? 34.832 -41.090 -7.545  1.00 23.53 ?  167 SER   B HB3  1 
ATOM   6578 H HG   . SER   B 1 167 ? 35.568 -39.018 -7.578  1.00 23.21 ?  167 SER   B HG   1 
ATOM   6579 N N    . PHE   B 1 168 ? 33.233 -37.894 -9.896  1.00 19.02 ?  168 PHE   B N    1 
ATOM   6580 C CA   . PHE   B 1 168 ? 32.400 -36.693 -9.956  1.00 18.33 ?  168 PHE   B CA   1 
ATOM   6581 C C    . PHE   B 1 168 ? 31.087 -36.952 -10.688 1.00 16.27 ?  168 PHE   B C    1 
ATOM   6582 O O    . PHE   B 1 168 ? 30.049 -36.353 -10.351 1.00 17.25 ?  168 PHE   B O    1 
ATOM   6583 C CB   . PHE   B 1 168 ? 33.163 -35.554 -10.628 1.00 18.82 ?  168 PHE   B CB   1 
ATOM   6584 C CG   . PHE   B 1 168 ? 32.357 -34.304 -10.765 1.00 18.87 ?  168 PHE   B CG   1 
ATOM   6585 C CD1  . PHE   B 1 168 ? 32.024 -33.559 -9.644  1.00 20.00 ?  168 PHE   B CD1  1 
ATOM   6586 C CD2  . PHE   B 1 168 ? 31.913 -33.879 -12.003 1.00 18.34 ?  168 PHE   B CD2  1 
ATOM   6587 C CE1  . PHE   B 1 168 ? 31.260 -32.412 -9.752  1.00 20.49 ?  168 PHE   B CE1  1 
ATOM   6588 C CE2  . PHE   B 1 168 ? 31.162 -32.718 -12.124 1.00 19.41 ?  168 PHE   B CE2  1 
ATOM   6589 C CZ   . PHE   B 1 168 ? 30.831 -31.984 -10.995 1.00 19.73 ?  168 PHE   B CZ   1 
ATOM   6590 H H    . PHE   B 1 168 ? 33.947 -37.862 -10.370 1.00 22.84 ?  168 PHE   B H    1 
ATOM   6591 H HA   . PHE   B 1 168 ? 32.179 -36.416 -9.058  1.00 22.01 ?  168 PHE   B HA   1 
ATOM   6592 H HB2  . PHE   B 1 168 ? 33.944 -35.345 -10.096 1.00 22.60 ?  168 PHE   B HB2  1 
ATOM   6593 H HB3  . PHE   B 1 168 ? 33.429 -35.830 -11.518 1.00 22.60 ?  168 PHE   B HB3  1 
ATOM   6594 H HD1  . PHE   B 1 168 ? 32.305 -33.847 -8.806  1.00 24.02 ?  168 PHE   B HD1  1 
ATOM   6595 H HD2  . PHE   B 1 168 ? 32.132 -34.362 -12.763 1.00 22.03 ?  168 PHE   B HD2  1 
ATOM   6596 H HE1  . PHE   B 1 168 ? 31.043 -31.924 -8.992  1.00 24.61 ?  168 PHE   B HE1  1 
ATOM   6597 H HE2  . PHE   B 1 168 ? 30.870 -32.436 -12.964 1.00 23.31 ?  168 PHE   B HE2  1 
ATOM   6598 H HZ   . PHE   B 1 168 ? 30.320 -31.210 -11.075 1.00 23.69 ?  168 PHE   B HZ   1 
ATOM   6599 N N    . LEU   B 1 169 ? 31.114 -37.839 -11.680 1.00 16.41 ?  169 LEU   B N    1 
ATOM   6600 C CA   . LEU   B 1 169 ? 29.936 -38.142 -12.478 1.00 18.44 ?  169 LEU   B CA   1 
ATOM   6601 C C    . LEU   B 1 169 ? 29.936 -39.576 -12.989 1.00 20.89 ?  169 LEU   B C    1 
ATOM   6602 O O    . LEU   B 1 169 ? 29.025 -39.984 -13.709 1.00 23.23 ?  169 LEU   B O    1 
ATOM   6603 C CB   . LEU   B 1 169 ? 29.849 -37.184 -13.665 1.00 20.09 ?  169 LEU   B CB   1 
ATOM   6604 C CG   . LEU   B 1 169 ? 28.561 -36.371 -13.788 1.00 22.78 ?  169 LEU   B CG   1 
ATOM   6605 C CD1  . LEU   B 1 169 ? 28.497 -35.745 -15.163 1.00 23.75 ?  169 LEU   B CD1  1 
ATOM   6606 C CD2  . LEU   B 1 169 ? 27.324 -37.214 -13.520 1.00 22.53 ?  169 LEU   B CD2  1 
ATOM   6607 O OXT  . LEU   B 1 169 ? 30.851 -40.342 -12.699 1.00 21.77 -1 169 LEU   B OXT  1 
ATOM   6608 H H    . LEU   B 1 169 ? 31.817 -38.279 -11.924 1.00 19.72 ?  169 LEU   B H    1 
ATOM   6609 H HA   . LEU   B 1 169 ? 29.155 -38.016 -11.925 1.00 22.15 ?  169 LEU   B HA   1 
ATOM   6610 H HB2  . LEU   B 1 169 ? 30.581 -36.550 -13.604 1.00 24.13 ?  169 LEU   B HB2  1 
ATOM   6611 H HB3  . LEU   B 1 169 ? 29.938 -37.697 -14.485 1.00 24.13 ?  169 LEU   B HB3  1 
ATOM   6612 H HG   . LEU   B 1 169 ? 28.577 -35.651 -13.136 1.00 27.35 ?  169 LEU   B HG   1 
ATOM   6613 H HD11 . LEU   B 1 169 ? 27.695 -35.204 -15.225 1.00 28.52 ?  169 LEU   B HD11 1 
ATOM   6614 H HD12 . LEU   B 1 169 ? 29.283 -35.192 -15.291 1.00 28.52 ?  169 LEU   B HD12 1 
ATOM   6615 H HD13 . LEU   B 1 169 ? 28.475 -36.451 -15.826 1.00 28.52 ?  169 LEU   B HD13 1 
ATOM   6616 H HD21 . LEU   B 1 169 ? 26.555 -36.795 -13.930 1.00 27.05 ?  169 LEU   B HD21 1 
ATOM   6617 H HD22 . LEU   B 1 169 ? 27.459 -38.100 -13.895 1.00 27.05 ?  169 LEU   B HD22 1 
ATOM   6618 H HD23 . LEU   B 1 169 ? 27.194 -37.280 -12.561 1.00 27.05 ?  169 LEU   B HD23 1 
HETATM 6619 C C1   T TFA   C 2 .   ? 12.129 -1.304  1.447   0.40 12.13 ?  201 TFA   A C1   1 
HETATM 6620 C C2   T TFA   C 2 .   ? 12.749 -1.714  0.085   0.40 14.86 ?  201 TFA   A C2   1 
HETATM 6621 O O    T TFA   C 2 .   ? 12.848 -1.596  2.410   0.40 10.53 ?  201 TFA   A O    1 
HETATM 6622 F F1   T TFA   C 2 .   ? 12.819 -3.054  0.022   0.40 16.20 ?  201 TFA   A F1   1 
HETATM 6623 F F2   T TFA   C 2 .   ? 12.033 -1.321  -0.981  0.40 15.53 ?  201 TFA   A F2   1 
HETATM 6624 F F3   T TFA   C 2 .   ? 13.981 -1.228  -0.099  0.40 16.44 ?  201 TFA   A F3   1 
HETATM 6625 O OXT  T TFA   C 2 .   ? 11.029 -0.751  1.391   0.40 12.50 ?  201 TFA   A OXT  1 
HETATM 6626 N N2   B A1A9N D 3 .   ? 14.702 -0.145  3.932   0.28 19.10 ?  202 A1A9N A N2   1 
HETATM 6627 C C3   B A1A9N D 3 .   ? 14.282 -0.444  1.029   0.28 21.61 ?  202 A1A9N A C3   1 
HETATM 6628 C C6   B A1A9N D 3 .   ? 15.322 2.111   5.263   0.28 17.53 ?  202 A1A9N A C6   1 
HETATM 6629 C C9   B A1A9N D 3 .   ? 15.769 4.275   4.743   0.28 16.59 ?  202 A1A9N A C9   1 
HETATM 6630 C C12  B A1A9N D 3 .   ? 12.161 -1.789  0.454   0.28 23.00 ?  202 A1A9N A C12  1 
HETATM 6631 C C1   B A1A9N D 3 .   ? 16.679 -1.331  0.465   0.28 21.06 ?  202 A1A9N A C1   1 
HETATM 6632 C C10  B A1A9N D 3 .   ? 12.738 -0.359  0.434   0.28 22.70 ?  202 A1A9N A C10  1 
HETATM 6633 C C11  B A1A9N D 3 .   ? 11.853 0.599   1.318   0.28 23.03 ?  202 A1A9N A C11  1 
HETATM 6634 C C2   B A1A9N D 3 .   ? 15.298 -0.894  -0.091  0.28 21.32 ?  202 A1A9N A C2   1 
HETATM 6635 C C4   B A1A9N D 3 .   ? 14.890 0.971   3.143   0.28 19.28 ?  202 A1A9N A C4   1 
HETATM 6636 C C5   B A1A9N D 3 .   ? 14.832 -0.083  5.305   0.28 18.73 ?  202 A1A9N A C5   1 
HETATM 6637 C C7   B A1A9N D 3 .   ? 15.226 2.220   3.823   0.28 18.05 ?  202 A1A9N A C7   1 
HETATM 6638 C C8   B A1A9N D 3 .   ? 15.522 3.627   3.530   0.28 17.43 ?  202 A1A9N A C8   1 
HETATM 6639 N N1   B A1A9N D 3 .   ? 14.736 0.818   1.735   0.28 20.60 ?  202 A1A9N A N1   1 
HETATM 6640 N N3   B A1A9N D 3 .   ? 15.133 0.998   6.025   0.28 18.18 ?  202 A1A9N A N3   1 
HETATM 6641 N N4   B A1A9N D 3 .   ? 15.644 3.352   5.724   0.28 16.31 ?  202 A1A9N A N4   1 
HETATM 6642 O O1   B A1A9N D 3 .   ? 12.809 0.128   -0.880  0.28 22.87 ?  202 A1A9N A O1   1 
HETATM 6643 H H1   B A1A9N D 3 .   ? 14.267 -1.255  1.787   0.28 25.95 ?  202 A1A9N A H1   1 
HETATM 6644 H H10  B A1A9N D 3 .   ? 16.023 5.295   5.063   0.28 19.92 ?  202 A1A9N A H10  1 
HETATM 6645 H H17  B A1A9N D 3 .   ? 12.500 -2.421  -0.384  0.28 27.62 ?  202 A1A9N A H17  1 
HETATM 6646 H H15  B A1A9N D 3 .   ? 11.065 -1.821  0.403   0.28 27.62 ?  202 A1A9N A H15  1 
HETATM 6647 H H16  B A1A9N D 3 .   ? 12.416 -2.355  1.365   0.28 27.62 ?  202 A1A9N A H16  1 
HETATM 6648 H H2   B A1A9N D 3 .   ? 17.312 -1.837  -0.282  0.28 25.30 ?  202 A1A9N A H2   1 
HETATM 6649 H H3   B A1A9N D 3 .   ? 16.600 -2.031  1.309   0.28 25.30 ?  202 A1A9N A H3   1 
HETATM 6650 H H4   B A1A9N D 3 .   ? 17.307 -0.501  0.845   0.28 25.30 ?  202 A1A9N A H4   1 
HETATM 6651 H H14  B A1A9N D 3 .   ? 10.877 0.851   0.854   0.28 27.66 ?  202 A1A9N A H14  1 
HETATM 6652 H H13  B A1A9N D 3 .   ? 12.306 1.584   1.539   0.28 27.66 ?  202 A1A9N A H13  1 
HETATM 6653 H H12  B A1A9N D 3 .   ? 11.583 0.192   2.312   0.28 27.66 ?  202 A1A9N A H12  1 
HETATM 6654 H H5   B A1A9N D 3 .   ? 14.853 -1.715  -0.689  0.28 25.61 ?  202 A1A9N A H5   1 
HETATM 6655 H H6   B A1A9N D 3 .   ? 15.448 -0.074  -0.821  0.28 25.61 ?  202 A1A9N A H6   1 
HETATM 6656 H H8   B A1A9N D 3 .   ? 14.668 -1.011  5.905   0.28 22.50 ?  202 A1A9N A H8   1 
HETATM 6657 H H9   B A1A9N D 3 .   ? 15.550 4.130   2.586   0.28 20.93 ?  202 A1A9N A H9   1 
HETATM 6658 H H7   B A1A9N D 3 .   ? 14.935 1.598   1.112   0.28 24.74 ?  202 A1A9N A H7   1 
HETATM 6659 H H11  B A1A9N D 3 .   ? 15.783 3.591   6.761   0.28 19.59 ?  202 A1A9N A H11  1 
HETATM 6660 H H18  B A1A9N D 3 .   ? 11.942 0.285   -1.299  0.28 27.46 ?  202 A1A9N A H18  1 
HETATM 6661 O O    . HOH   E 4 .   ? 14.756 -4.649  20.534  1.00 45.36 ?  301 HOH   A O    1 
HETATM 6662 O O    A HOH   E 4 .   ? 4.678  3.930   0.597   0.72 21.55 ?  302 HOH   A O    1 
HETATM 6663 O O    . HOH   E 4 .   ? 34.319 -1.838  12.487  1.00 37.82 ?  303 HOH   A O    1 
HETATM 6664 O O    . HOH   E 4 .   ? 7.598  -6.279  -6.649  1.00 38.61 ?  304 HOH   A O    1 
HETATM 6665 O O    . HOH   E 4 .   ? 18.583 -2.382  -16.409 1.00 46.67 ?  305 HOH   A O    1 
HETATM 6666 O O    . HOH   E 4 .   ? 30.968 6.213   -12.300 1.00 27.62 ?  306 HOH   A O    1 
HETATM 6667 O O    B HOH   E 4 .   ? 5.436  4.022   0.483   0.28 33.04 ?  307 HOH   A O    1 
HETATM 6668 O O    . HOH   E 4 .   ? 11.981 0.337   14.775  1.00 32.88 ?  308 HOH   A O    1 
HETATM 6669 O O    . HOH   E 4 .   ? 14.686 -13.954 16.664  1.00 24.06 ?  309 HOH   A O    1 
HETATM 6670 O O    . HOH   E 4 .   ? 17.081 -18.007 15.048  1.00 25.09 ?  310 HOH   A O    1 
HETATM 6671 O O    . HOH   E 4 .   ? 15.025 -12.192 18.644  1.00 38.51 ?  311 HOH   A O    1 
HETATM 6672 O O    . HOH   E 4 .   ? -0.447 -2.994  2.997   1.00 37.93 ?  312 HOH   A O    1 
HETATM 6673 O O    . HOH   E 4 .   ? 28.938 0.470   -9.717  1.00 20.75 ?  313 HOH   A O    1 
HETATM 6674 O O    . HOH   E 4 .   ? 36.096 -5.129  -0.536  1.00 28.17 ?  314 HOH   A O    1 
HETATM 6675 O O    . HOH   E 4 .   ? 42.413 10.562  5.179   1.00 20.15 ?  315 HOH   A O    1 
HETATM 6676 O O    . HOH   E 4 .   ? 11.732 -10.840 -10.139 1.00 44.54 ?  316 HOH   A O    1 
HETATM 6677 O O    . HOH   E 4 .   ? 30.225 -13.316 -8.567  1.00 20.46 ?  317 HOH   A O    1 
HETATM 6678 O O    . HOH   E 4 .   ? 14.419 -24.695 11.605  1.00 36.00 ?  318 HOH   A O    1 
HETATM 6679 O O    . HOH   E 4 .   ? 9.152  -10.114 19.339  1.00 36.88 ?  319 HOH   A O    1 
HETATM 6680 O O    . HOH   E 4 .   ? 18.864 -21.989 6.961   1.00 31.87 ?  320 HOH   A O    1 
HETATM 6681 O O    B HOH   E 4 .   ? 18.865 -0.557  -1.942  0.28 19.08 ?  321 HOH   A O    1 
HETATM 6682 O O    . HOH   E 4 .   ? 15.057 3.971   17.743  1.00 40.37 ?  322 HOH   A O    1 
HETATM 6683 O O    . HOH   E 4 .   ? 19.881 -12.537 -8.952  1.00 24.86 ?  323 HOH   A O    1 
HETATM 6684 O O    . HOH   E 4 .   ? 28.175 -6.330  19.629  1.00 40.90 ?  324 HOH   A O    1 
HETATM 6685 O O    A HOH   E 4 .   ? 14.617 -3.644  3.083   0.72 14.01 ?  325 HOH   A O    1 
HETATM 6686 O O    . HOH   E 4 .   ? 14.133 -4.550  -11.915 1.00 31.96 ?  326 HOH   A O    1 
HETATM 6687 O O    . HOH   E 4 .   ? 7.992  -21.472 3.968   1.00 43.91 ?  327 HOH   A O    1 
HETATM 6688 O O    . HOH   E 4 .   ? 26.478 -19.332 -1.798  1.00 14.33 ?  328 HOH   A O    1 
HETATM 6689 O O    . HOH   E 4 .   ? 33.972 -0.995  -8.913  1.00 27.14 ?  329 HOH   A O    1 
HETATM 6690 O O    . HOH   E 4 .   ? 13.224 -1.450  -6.655  1.00 16.92 ?  330 HOH   A O    1 
HETATM 6691 O O    . HOH   E 4 .   ? 27.922 0.825   -7.137  1.00 13.58 ?  331 HOH   A O    1 
HETATM 6692 O O    . HOH   E 4 .   ? 8.837  -12.090 17.089  1.00 44.08 ?  332 HOH   A O    1 
HETATM 6693 O O    . HOH   E 4 .   ? 22.299 5.376   18.984  1.00 40.74 ?  333 HOH   A O    1 
HETATM 6694 O O    . HOH   E 4 .   ? 27.311 13.775  2.876   1.00 30.25 ?  334 HOH   A O    1 
HETATM 6695 O O    . HOH   E 4 .   ? 31.019 -18.107 7.833   1.00 20.51 ?  335 HOH   A O    1 
HETATM 6696 O O    . HOH   E 4 .   ? 37.514 2.829   10.224  1.00 28.35 ?  336 HOH   A O    1 
HETATM 6697 O O    . HOH   E 4 .   ? 22.706 12.485  1.617   1.00 14.96 ?  337 HOH   A O    1 
HETATM 6698 O O    . HOH   E 4 .   ? 21.272 -2.275  -2.364  1.00 16.73 ?  338 HOH   A O    1 
HETATM 6699 O O    . HOH   E 4 .   ? -0.596 -8.412  2.154   1.00 42.80 ?  339 HOH   A O    1 
HETATM 6700 O O    . HOH   E 4 .   ? 44.300 7.121   6.426   1.00 25.87 ?  340 HOH   A O    1 
HETATM 6701 O O    . HOH   E 4 .   ? 28.344 -0.134  -13.416 1.00 33.86 ?  341 HOH   A O    1 
HETATM 6702 O O    . HOH   E 4 .   ? 7.931  -12.571 -0.884  1.00 21.56 ?  342 HOH   A O    1 
HETATM 6703 O O    . HOH   E 4 .   ? 20.619 -19.711 -5.067  1.00 27.20 ?  343 HOH   A O    1 
HETATM 6704 O O    . HOH   E 4 .   ? 9.847  -21.393 5.689   1.00 18.83 ?  344 HOH   A O    1 
HETATM 6705 O O    . HOH   E 4 .   ? 38.268 10.106  7.201   1.00 38.43 ?  345 HOH   A O    1 
HETATM 6706 O O    . HOH   E 4 .   ? 6.402  -5.477  11.043  1.00 19.12 ?  346 HOH   A O    1 
HETATM 6707 O O    . HOH   E 4 .   ? 18.623 -19.355 13.541  1.00 36.17 ?  347 HOH   A O    1 
HETATM 6708 O O    A HOH   E 4 .   ? 3.575  -9.453  9.706   0.72 23.06 ?  348 HOH   A O    1 
HETATM 6709 O O    . HOH   E 4 .   ? 13.539 -15.228 -7.472  1.00 25.70 ?  349 HOH   A O    1 
HETATM 6710 O O    . HOH   E 4 .   ? 26.831 11.413  1.645   1.00 16.64 ?  350 HOH   A O    1 
HETATM 6711 O O    . HOH   E 4 .   ? 39.746 -1.017  -5.177  1.00 20.34 ?  351 HOH   A O    1 
HETATM 6712 O O    . HOH   E 4 .   ? 42.569 4.318   5.411   1.00 30.58 ?  352 HOH   A O    1 
HETATM 6713 O O    A HOH   E 4 .   ? 6.923  -8.153  11.827  0.72 17.72 ?  353 HOH   A O    1 
HETATM 6714 O O    A HOH   E 4 .   ? 14.255 0.583   6.787   0.72 16.67 ?  354 HOH   A O    1 
HETATM 6715 O O    . HOH   E 4 .   ? 38.538 4.965   6.981   1.00 15.72 ?  355 HOH   A O    1 
HETATM 6716 O O    A HOH   E 4 .   ? 17.480 -1.703  0.431   0.72 17.10 ?  356 HOH   A O    1 
HETATM 6717 O O    . HOH   E 4 .   ? 0.644  -4.422  0.090   1.00 32.39 ?  357 HOH   A O    1 
HETATM 6718 O O    . HOH   E 4 .   ? 24.018 -2.092  -2.081  1.00 10.65 ?  358 HOH   A O    1 
HETATM 6719 O O    . HOH   E 4 .   ? 14.346 -21.197 -4.262  1.00 29.69 ?  359 HOH   A O    1 
HETATM 6720 O O    . HOH   E 4 .   ? 25.691 -0.798  -7.380  1.00 15.09 ?  360 HOH   A O    1 
HETATM 6721 O O    . HOH   E 4 .   ? 22.160 -19.280 11.387  1.00 33.32 ?  361 HOH   A O    1 
HETATM 6722 O O    . HOH   E 4 .   ? 35.755 -12.646 6.851   1.00 16.04 ?  362 HOH   A O    1 
HETATM 6723 O O    . HOH   E 4 .   ? 31.073 -13.946 -2.484  1.00 14.01 ?  363 HOH   A O    1 
HETATM 6724 O O    . HOH   E 4 .   ? 17.122 -17.761 -5.065  1.00 26.23 ?  364 HOH   A O    1 
HETATM 6725 O O    . HOH   E 4 .   ? 16.974 -19.272 4.880   1.00 15.27 ?  365 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? 37.212 -2.819  9.711   1.00 40.04 ?  366 HOH   A O    1 
HETATM 6727 O O    . HOH   E 4 .   ? 37.355 11.957  4.955   1.00 29.99 ?  367 HOH   A O    1 
HETATM 6728 O O    . HOH   E 4 .   ? 43.933 8.436   -3.084  1.00 26.43 ?  368 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 30.787 3.088   8.282   1.00 12.15 ?  369 HOH   A O    1 
HETATM 6730 O O    . HOH   E 4 .   ? 31.671 8.186   14.906  1.00 23.32 ?  370 HOH   A O    1 
HETATM 6731 O O    . HOH   E 4 .   ? 33.625 -7.160  4.316   1.00 17.15 ?  371 HOH   A O    1 
HETATM 6732 O O    . HOH   E 4 .   ? 21.858 -21.903 8.418   1.00 28.57 ?  372 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 27.429 -10.610 14.059  1.00 17.45 ?  373 HOH   A O    1 
HETATM 6734 O O    . HOH   E 4 .   ? 18.550 9.456   9.010   1.00 21.20 ?  374 HOH   A O    1 
HETATM 6735 O O    . HOH   E 4 .   ? 31.882 -9.329  -6.636  1.00 22.12 ?  375 HOH   A O    1 
HETATM 6736 O O    . HOH   E 4 .   ? 31.744 -7.312  -9.860  1.00 21.50 ?  376 HOH   A O    1 
HETATM 6737 O O    . HOH   E 4 .   ? 24.669 -17.499 12.730  1.00 24.06 ?  377 HOH   A O    1 
HETATM 6738 O O    . HOH   E 4 .   ? 16.516 -22.061 0.954   1.00 27.72 ?  378 HOH   A O    1 
HETATM 6739 O O    . HOH   E 4 .   ? 14.031 -23.039 7.434   1.00 18.06 ?  379 HOH   A O    1 
HETATM 6740 O O    . HOH   E 4 .   ? 13.921 -4.981  17.453  1.00 26.59 ?  380 HOH   A O    1 
HETATM 6741 O O    . HOH   E 4 .   ? 43.347 7.836   2.712   1.00 25.35 ?  381 HOH   A O    1 
HETATM 6742 O O    B HOH   E 4 .   ? 14.859 -2.924  3.374   0.28 22.07 ?  382 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 15.519 11.812  7.928   1.00 38.27 ?  383 HOH   A O    1 
HETATM 6744 O O    . HOH   E 4 .   ? 24.390 3.602   -1.811  1.00 15.00 ?  384 HOH   A O    1 
HETATM 6745 O O    T HOH   E 4 .   ? 15.390 -0.411  2.374   0.40 12.66 ?  385 HOH   A O    1 
HETATM 6746 O O    . HOH   E 4 .   ? 22.582 -11.917 21.789  1.00 44.90 ?  386 HOH   A O    1 
HETATM 6747 O O    . HOH   E 4 .   ? 24.191 -7.755  14.446  1.00 17.14 ?  387 HOH   A O    1 
HETATM 6748 O O    A HOH   E 4 .   ? 11.050 -0.368  1.918   0.32 17.40 ?  388 HOH   A O    1 
HETATM 6749 O O    . HOH   E 4 .   ? 21.185 10.296  15.034  1.00 33.42 ?  389 HOH   A O    1 
HETATM 6750 O O    . HOH   E 4 .   ? 32.762 -9.250  5.970   1.00 20.17 ?  390 HOH   A O    1 
HETATM 6751 O O    . HOH   E 4 .   ? 27.469 -6.149  -13.991 1.00 36.71 ?  391 HOH   A O    1 
HETATM 6752 O O    . HOH   E 4 .   ? 37.522 -2.021  5.811   1.00 26.78 ?  392 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 21.313 3.089   -0.315  1.00 13.17 ?  393 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 30.659 1.904   16.697  1.00 21.28 ?  394 HOH   A O    1 
HETATM 6755 O O    . HOH   E 4 .   ? 10.943 1.679   12.634  1.00 24.48 ?  395 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 15.153 -8.085  -9.742  1.00 22.65 ?  396 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 24.575 1.984   -7.045  1.00 19.80 ?  397 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 15.179 -21.527 14.224  1.00 18.23 ?  398 HOH   A O    1 
HETATM 6759 O O    . HOH   E 4 .   ? 6.651  -3.227  12.765  1.00 28.98 ?  399 HOH   A O    1 
HETATM 6760 O O    . HOH   E 4 .   ? 20.529 -20.012 2.769   1.00 17.83 ?  400 HOH   A O    1 
HETATM 6761 O O    A HOH   E 4 .   ? 15.781 -0.936  5.258   0.72 16.78 ?  401 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 23.448 11.379  4.074   1.00 12.43 ?  402 HOH   A O    1 
HETATM 6763 O O    . HOH   E 4 .   ? 23.928 -15.682 -9.164  1.00 34.72 ?  403 HOH   A O    1 
HETATM 6764 O O    . HOH   E 4 .   ? 27.253 2.334   18.736  1.00 31.66 ?  404 HOH   A O    1 
HETATM 6765 O O    B HOH   E 4 .   ? 18.735 1.996   -0.600  0.28 8.58  ?  405 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 14.553 -0.540  -12.152 1.00 23.21 ?  406 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 40.891 -8.292  -6.766  1.00 35.68 ?  407 HOH   A O    1 
HETATM 6768 O O    . HOH   E 4 .   ? 26.910 4.179   -0.654  1.00 12.64 ?  408 HOH   A O    1 
HETATM 6769 O O    . HOH   E 4 .   ? 23.917 -20.275 -1.365  1.00 16.73 ?  409 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 32.526 -10.653 3.171   1.00 31.05 ?  410 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 38.083 -1.342  -1.934  1.00 19.08 ?  411 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 30.286 -12.925 13.521  1.00 20.04 ?  412 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 30.007 -10.082 13.026  1.00 21.61 ?  413 HOH   A O    1 
HETATM 6774 O O    . HOH   E 4 .   ? 32.652 -4.305  -9.885  1.00 28.65 ?  414 HOH   A O    1 
HETATM 6775 O O    . HOH   E 4 .   ? 35.076 -5.212  -3.113  1.00 18.01 ?  415 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 16.159 16.627  8.672   1.00 31.08 ?  416 HOH   A O    1 
HETATM 6777 O O    . HOH   E 4 .   ? 24.026 3.963   -4.857  1.00 22.92 ?  417 HOH   A O    1 
HETATM 6778 O O    . HOH   E 4 .   ? 41.550 1.508   5.025   1.00 35.98 ?  418 HOH   A O    1 
HETATM 6779 O O    A HOH   E 4 .   ? 18.944 -0.657  -1.636  0.72 12.44 ?  419 HOH   A O    1 
HETATM 6780 O O    . HOH   E 4 .   ? 36.695 -4.982  5.404   1.00 23.91 ?  420 HOH   A O    1 
HETATM 6781 O O    . HOH   E 4 .   ? 5.424  2.862   5.021   1.00 34.75 ?  421 HOH   A O    1 
HETATM 6782 O O    . HOH   E 4 .   ? 16.205 -14.187 20.184  1.00 49.85 ?  422 HOH   A O    1 
HETATM 6783 O O    . HOH   E 4 .   ? 28.615 -10.604 -14.006 1.00 42.97 ?  423 HOH   A O    1 
HETATM 6784 O O    . HOH   E 4 .   ? 44.938 -0.605  3.021   1.00 40.96 ?  424 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 10.373 -13.701 -1.695  1.00 17.11 ?  425 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 15.871 2.105   24.768  1.00 44.37 ?  426 HOH   A O    1 
HETATM 6787 O O    . HOH   E 4 .   ? 21.718 -13.840 -8.182  1.00 41.23 ?  427 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 10.354 -22.174 -1.250  1.00 45.11 ?  428 HOH   A O    1 
HETATM 6789 O O    . HOH   E 4 .   ? 11.627 -10.691 16.920  1.00 23.12 ?  429 HOH   A O    1 
HETATM 6790 O O    . HOH   E 4 .   ? 22.618 8.170   18.368  1.00 44.70 ?  430 HOH   A O    1 
HETATM 6791 O O    A HOH   E 4 .   ? 20.089 4.556   -7.553  0.72 16.32 ?  431 HOH   A O    1 
HETATM 6792 O O    . HOH   E 4 .   ? 15.933 6.837   2.978   1.00 16.79 ?  432 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 20.557 -17.696 24.785  1.00 50.97 ?  433 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 23.487 -8.021  17.095  1.00 22.07 ?  434 HOH   A O    1 
HETATM 6795 O O    B HOH   E 4 .   ? 10.599 4.406   2.526   0.28 27.56 ?  435 HOH   A O    1 
HETATM 6796 O O    . HOH   E 4 .   ? 27.082 -3.180  19.375  1.00 38.33 ?  436 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 23.327 -20.920 1.317   1.00 18.62 ?  437 HOH   A O    1 
HETATM 6798 O O    B HOH   E 4 .   ? 7.364  1.910   6.939   0.28 29.02 ?  438 HOH   A O    1 
HETATM 6799 O O    . HOH   E 4 .   ? 37.723 -8.840  -3.464  1.00 24.02 ?  439 HOH   A O    1 
HETATM 6800 O O    A HOH   E 4 .   ? 16.244 2.960   -1.451  0.72 13.83 ?  440 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 9.449  -16.298 -1.978  1.00 39.92 ?  441 HOH   A O    1 
HETATM 6802 O O    . HOH   E 4 .   ? 21.231 -9.216  21.325  1.00 46.05 ?  442 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 34.409 -8.070  -0.566  1.00 28.20 ?  443 HOH   A O    1 
HETATM 6804 O O    . HOH   E 4 .   ? 18.372 -15.996 16.383  1.00 36.74 ?  444 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 18.438 4.907   -15.190 1.00 46.34 ?  445 HOH   A O    1 
HETATM 6806 O O    . HOH   E 4 .   ? 30.567 14.784  2.789   1.00 18.40 ?  446 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 23.202 7.566   -3.219  1.00 30.00 ?  447 HOH   A O    1 
HETATM 6808 O O    A HOH   E 4 .   ? 14.009 -0.328  3.448   0.32 22.91 ?  448 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 19.283 -10.991 24.064  1.00 63.58 ?  449 HOH   A O    1 
HETATM 6810 O O    . HOH   E 4 .   ? 31.339 -12.761 0.004   1.00 19.92 ?  450 HOH   A O    1 
HETATM 6811 O O    . HOH   E 4 .   ? 21.476 -14.694 18.014  1.00 51.52 ?  451 HOH   A O    1 
HETATM 6812 O O    A HOH   E 4 .   ? 18.848 2.045   -0.760  0.72 15.65 ?  452 HOH   A O    1 
HETATM 6813 O O    . HOH   E 4 .   ? 29.784 -1.955  -12.750 1.00 44.50 ?  453 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 29.795 -16.041 10.690  1.00 36.16 ?  454 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 27.808 7.058   -6.430  1.00 34.05 ?  455 HOH   A O    1 
HETATM 6816 O O    A HOH   E 4 .   ? -1.451 -4.932  7.618   0.72 36.37 ?  456 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 32.461 -15.888 10.844  1.00 31.62 ?  457 HOH   A O    1 
HETATM 6818 O O    . HOH   E 4 .   ? 25.428 8.256   -4.823  1.00 29.56 ?  458 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 19.897 -17.354 -5.053  1.00 24.15 ?  459 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 24.819 5.614   20.743  1.00 50.36 ?  460 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 23.127 -22.288 -3.400  1.00 35.53 ?  461 HOH   A O    1 
HETATM 6822 O O    B HOH   E 4 .   ? 16.138 2.972   -1.000  0.28 19.73 ?  462 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 24.573 14.651  7.815   1.00 36.22 ?  463 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 26.916 11.606  -1.337  1.00 31.48 ?  464 HOH   A O    1 
HETATM 6825 O O    . HOH   E 4 .   ? 15.712 -21.527 3.670   1.00 23.69 ?  465 HOH   A O    1 
HETATM 6826 O O    . HOH   E 4 .   ? 18.752 10.909  11.284  1.00 31.99 ?  466 HOH   A O    1 
HETATM 6827 O O    . HOH   E 4 .   ? 21.852 5.164   -5.778  1.00 30.91 ?  467 HOH   A O    1 
HETATM 6828 O O    . HOH   E 4 .   ? 39.639 -7.000  -3.492  1.00 42.71 ?  468 HOH   A O    1 
HETATM 6829 O O    . HOH   E 4 .   ? 27.465 -11.421 16.550  1.00 37.04 ?  469 HOH   A O    1 
HETATM 6830 O O    . HOH   E 4 .   ? 25.810 10.775  -3.746  1.00 24.75 ?  470 HOH   A O    1 
HETATM 6831 O O    . HOH   E 4 .   ? 12.306 1.559   17.324  1.00 39.03 ?  471 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 23.479 13.722  5.495   1.00 18.38 ?  472 HOH   A O    1 
HETATM 6833 O O    . HOH   E 4 .   ? 11.899 -13.460 16.386  1.00 52.46 ?  473 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 13.984 -10.354 -10.894 1.00 32.44 ?  474 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 10.991 -15.092 -6.120  1.00 34.81 ?  475 HOH   A O    1 
HETATM 6836 O O    . HOH   E 4 .   ? 18.074 -16.247 -8.847  1.00 40.18 ?  476 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 23.115 11.819  -4.067  1.00 18.95 ?  477 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 15.693 -17.117 -7.003  1.00 30.21 ?  478 HOH   A O    1 
HETATM 6839 O O    . HOH   E 4 .   ? 35.177 7.425   12.251  1.00 42.21 ?  479 HOH   A O    1 
HETATM 6840 O O    . HOH   E 4 .   ? 28.569 -4.668  -12.265 1.00 37.14 ?  480 HOH   A O    1 
HETATM 6841 O O    . HOH   E 4 .   ? 28.836 9.012   17.516  1.00 39.57 ?  481 HOH   A O    1 
HETATM 6842 O O    . HOH   E 4 .   ? 17.350 -18.687 19.832  1.00 49.77 ?  482 HOH   A O    1 
HETATM 6843 O O    . HOH   E 4 .   ? 20.497 -16.085 -7.384  1.00 28.40 ?  483 HOH   A O    1 
HETATM 6844 O O    B HOH   E 4 .   ? 10.397 3.399   0.061   0.28 30.68 ?  484 HOH   A O    1 
HETATM 6845 O O    . HOH   E 4 .   ? 30.882 0.702   19.134  1.00 38.85 ?  485 HOH   A O    1 
HETATM 6846 O O    . HOH   E 4 .   ? 40.957 -3.985  -0.347  1.00 34.86 ?  486 HOH   A O    1 
HETATM 6847 O O    . HOH   E 4 .   ? 16.789 -20.509 16.180  1.00 28.13 ?  487 HOH   A O    1 
HETATM 6848 O O    . HOH   E 4 .   ? 28.652 -7.966  -15.316 1.00 48.39 ?  488 HOH   A O    1 
HETATM 6849 O O    . HOH   E 4 .   ? 41.743 9.378   -4.006  1.00 30.27 ?  489 HOH   A O    1 
HETATM 6850 O O    . HOH   E 4 .   ? 44.542 10.456  -1.575  1.00 30.43 ?  490 HOH   A O    1 
HETATM 6851 O O    . HOH   E 4 .   ? 31.478 -0.578  -10.534 1.00 27.68 ?  491 HOH   A O    1 
HETATM 6852 O O    . HOH   E 4 .   ? 23.218 -12.853 19.297  1.00 43.33 ?  492 HOH   A O    1 
HETATM 6853 O O    . HOH   E 4 .   ? 18.414 -23.188 1.901   1.00 41.72 ?  493 HOH   A O    1 
HETATM 6854 O O    . HOH   E 4 .   ? 39.134 2.429   7.522   1.00 31.73 ?  494 HOH   A O    1 
HETATM 6855 O O    . HOH   E 4 .   ? 16.020 -6.779  -11.876 1.00 41.51 ?  495 HOH   A O    1 
HETATM 6856 O O    B HOH   E 4 .   ? 2.247  4.318   1.291   0.28 28.98 ?  496 HOH   A O    1 
HETATM 6857 O O    . HOH   E 4 .   ? 13.918 -25.275 8.893   1.00 31.28 ?  497 HOH   A O    1 
HETATM 6858 O O    . HOH   E 4 .   ? 30.724 5.803   -14.748 1.00 34.24 ?  498 HOH   A O    1 
HETATM 6859 O O    . HOH   E 4 .   ? 40.545 -0.260  -7.797  1.00 33.49 ?  499 HOH   A O    1 
HETATM 6860 O O    . HOH   E 4 .   ? 19.997 -22.355 4.173   1.00 27.01 ?  500 HOH   A O    1 
HETATM 6861 O O    . HOH   E 4 .   ? 16.169 -23.381 5.731   1.00 27.04 ?  501 HOH   A O    1 
HETATM 6862 O O    . HOH   E 4 .   ? 30.741 -5.851  -11.849 1.00 47.87 ?  502 HOH   A O    1 
HETATM 6863 O O    . HOH   E 4 .   ? 8.043  -3.143  -5.708  1.00 45.14 ?  503 HOH   A O    1 
HETATM 6864 O O    . HOH   E 4 .   ? 37.361 -6.643  7.580   1.00 25.84 ?  504 HOH   A O    1 
HETATM 6865 O O    . HOH   E 4 .   ? 23.149 -23.751 1.584   1.00 30.75 ?  505 HOH   A O    1 
HETATM 6866 O O    . HOH   E 4 .   ? 39.510 -0.008  6.597   1.00 29.48 ?  506 HOH   A O    1 
HETATM 6867 O O    . HOH   E 4 .   ? 37.994 13.921  6.804   1.00 47.40 ?  507 HOH   A O    1 
HETATM 6868 O O    . HOH   E 4 .   ? 28.992 14.475  0.861   1.00 46.63 ?  508 HOH   A O    1 
HETATM 6869 O O    B HOH   E 4 .   ? 15.109 8.136   4.905   0.28 28.67 ?  509 HOH   A O    1 
HETATM 6870 O O    B HOH   E 4 .   ? 9.925  1.026   -5.413  0.28 19.51 ?  510 HOH   A O    1 
HETATM 6871 O O    . HOH   E 4 .   ? 22.000 -24.002 4.496   1.00 26.50 ?  511 HOH   A O    1 
HETATM 6872 O O    . HOH   E 4 .   ? 36.430 -6.505  10.147  1.00 44.39 ?  512 HOH   A O    1 
HETATM 6873 O O    T HOH   E 4 .   ? 11.909 -2.135  -3.670  0.40 12.93 ?  513 HOH   A O    1 
HETATM 6874 O O    A HOH   E 4 .   ? 14.832 8.661   4.879   0.72 45.29 ?  514 HOH   A O    1 
HETATM 6875 O O    . HOH   E 4 .   ? 17.324 -6.507  -14.208 1.00 38.66 ?  515 HOH   A O    1 
HETATM 6876 O O    . HOH   E 4 .   ? 24.089 8.969   -7.221  1.00 36.61 ?  516 HOH   A O    1 
HETATM 6877 O O    B HOH   E 4 .   ? 8.451  7.264   1.938   0.28 32.90 ?  517 HOH   A O    1 
HETATM 6878 O O    . HOH   E 4 .   ? 16.355 -21.099 18.767  1.00 35.23 ?  518 HOH   A O    1 
HETATM 6879 O O    . HOH   E 4 .   ? 15.866 -12.220 27.476  1.00 44.62 ?  519 HOH   A O    1 
HETATM 6880 O O    . HOH   E 4 .   ? 14.728 -22.773 19.831  1.00 33.97 ?  520 HOH   A O    1 
HETATM 6881 O O    . HOH   F 4 .   ? 29.808 -22.434 5.490   1.00 20.62 ?  201 HOH   B O    1 
HETATM 6882 O O    . HOH   F 4 .   ? 41.816 -35.982 -17.227 1.00 31.09 ?  202 HOH   B O    1 
HETATM 6883 O O    . HOH   F 4 .   ? 48.086 -6.869  15.580  1.00 36.28 ?  203 HOH   B O    1 
HETATM 6884 O O    . HOH   F 4 .   ? 49.391 -22.651 -19.731 1.00 48.80 ?  204 HOH   B O    1 
HETATM 6885 O O    . HOH   F 4 .   ? 47.399 -7.445  -3.946  1.00 38.91 ?  205 HOH   B O    1 
HETATM 6886 O O    . HOH   F 4 .   ? 41.348 -7.814  5.477   1.00 38.98 ?  206 HOH   B O    1 
HETATM 6887 O O    . HOH   F 4 .   ? 59.148 -18.702 6.862   1.00 37.51 ?  207 HOH   B O    1 
HETATM 6888 O O    . HOH   F 4 .   ? 27.857 -41.787 -15.179 1.00 35.84 ?  208 HOH   B O    1 
HETATM 6889 O O    . HOH   F 4 .   ? 52.908 -13.456 -20.422 1.00 36.44 ?  209 HOH   B O    1 
HETATM 6890 O O    . HOH   F 4 .   ? 27.732 -29.187 -1.863  1.00 36.87 ?  210 HOH   B O    1 
HETATM 6891 O O    . HOH   F 4 .   ? 37.953 -39.452 -0.188  1.00 40.03 ?  211 HOH   B O    1 
HETATM 6892 O O    . HOH   F 4 .   ? 56.343 -19.699 7.317   1.00 32.72 ?  212 HOH   B O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 29.906 -26.272 4.038   1.00 27.71 ?  213 HOH   B O    1 
HETATM 6894 O O    . HOH   F 4 .   ? 54.480 -9.364  -8.738  1.00 19.29 ?  214 HOH   B O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 30.216 -41.010 -8.108  1.00 16.70 ?  215 HOH   B O    1 
HETATM 6896 O O    . HOH   F 4 .   ? 57.704 -24.472 5.028   1.00 35.78 ?  216 HOH   B O    1 
HETATM 6897 O O    . HOH   F 4 .   ? 58.208 -12.992 8.423   1.00 31.87 ?  217 HOH   B O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 50.220 -3.381  7.196   1.00 34.35 ?  218 HOH   B O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 56.669 -30.735 -7.779  1.00 33.47 ?  219 HOH   B O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 55.399 -16.532 -14.348 1.00 34.16 ?  220 HOH   B O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 44.427 -7.250  2.089   1.00 33.47 ?  221 HOH   B O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 50.728 -6.120  0.217   1.00 26.67 ?  222 HOH   B O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 57.154 -26.848 -7.651  1.00 40.70 ?  223 HOH   B O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 35.975 -43.265 -8.511  1.00 31.60 ?  224 HOH   B O    1 
HETATM 6905 O O    . HOH   F 4 .   ? 37.105 -19.798 -18.127 1.00 37.90 ?  225 HOH   B O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 34.532 -36.371 -7.178  1.00 18.44 ?  226 HOH   B O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 57.404 -16.243 -12.209 1.00 19.27 ?  227 HOH   B O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 25.427 -25.951 -1.344  1.00 31.95 ?  228 HOH   B O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 35.094 -7.990  -3.034  1.00 18.00 ?  229 HOH   B O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 29.821 -34.227 -0.439  1.00 35.46 ?  230 HOH   B O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 39.288 -10.900 6.121   1.00 27.03 ?  231 HOH   B O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 48.592 -36.444 -15.473 1.00 42.41 ?  232 HOH   B O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 41.502 -39.154 -14.896 1.00 22.32 ?  233 HOH   B O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 51.677 -6.478  4.405   1.00 20.09 ?  234 HOH   B O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 30.904 -28.762 4.322   1.00 26.84 ?  235 HOH   B O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 45.130 -34.973 6.852   1.00 42.20 ?  236 HOH   B O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 50.729 -12.973 -0.479  1.00 12.17 ?  237 HOH   B O    1 
HETATM 6918 O O    . HOH   F 4 .   ? 44.925 -43.558 -10.507 1.00 28.47 ?  238 HOH   B O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 41.371 -9.622  13.107  1.00 22.40 ?  239 HOH   B O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 42.558 -25.372 2.648   1.00 15.65 ?  240 HOH   B O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 46.409 -1.573  13.257  1.00 27.35 ?  241 HOH   B O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 28.391 -19.676 -13.119 1.00 24.79 ?  242 HOH   B O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 32.820 -43.798 -11.313 1.00 20.26 ?  243 HOH   B O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 40.645 -16.043 14.161  1.00 24.58 ?  244 HOH   B O    1 
HETATM 6925 O O    . HOH   F 4 .   ? 42.619 -22.862 3.850   1.00 12.09 ?  245 HOH   B O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 39.488 -11.108 0.362   1.00 17.12 ?  246 HOH   B O    1 
HETATM 6927 O O    . HOH   F 4 .   ? 57.604 -24.379 -3.792  1.00 21.56 ?  247 HOH   B O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 44.512 -27.766 -0.708  1.00 22.57 ?  248 HOH   B O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 34.212 -18.484 11.400  1.00 24.41 ?  249 HOH   B O    1 
HETATM 6930 O O    . HOH   F 4 .   ? 48.071 -24.532 -17.749 1.00 30.23 ?  250 HOH   B O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 34.867 -24.635 13.838  1.00 31.94 ?  251 HOH   B O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 43.079 -43.244 -8.245  1.00 29.42 ?  252 HOH   B O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 51.540 -13.847 11.025  1.00 28.69 ?  253 HOH   B O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 50.940 -39.973 -8.217  1.00 32.40 ?  254 HOH   B O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 27.117 -31.824 -9.951  1.00 20.34 ?  255 HOH   B O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 40.322 -12.762 -11.526 1.00 15.66 ?  256 HOH   B O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 31.780 -17.912 -14.510 1.00 29.99 ?  257 HOH   B O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 43.210 -32.382 -17.065 1.00 23.66 ?  258 HOH   B O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 29.732 -25.229 -10.804 1.00 17.17 ?  259 HOH   B O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 38.473 -11.063 -2.232  1.00 18.91 ?  260 HOH   B O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 33.499 -16.991 8.089   1.00 19.93 ?  261 HOH   B O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 58.176 -10.650 -4.073  1.00 20.08 ?  262 HOH   B O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 41.872 -23.514 9.288   1.00 17.41 ?  263 HOH   B O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 57.501 -9.239  1.465   1.00 19.76 ?  264 HOH   B O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 30.857 -15.731 2.668   1.00 14.13 ?  265 HOH   B O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 38.895 -11.961 12.364  1.00 35.20 ?  266 HOH   B O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 49.726 -0.490  10.261  1.00 30.96 ?  267 HOH   B O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 34.932 -33.346 -19.185 1.00 31.58 ?  268 HOH   B O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 42.332 -9.901  9.396   1.00 20.73 ?  269 HOH   B O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 43.361 -15.794 -12.179 1.00 14.61 ?  270 HOH   B O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 56.157 -23.556 -14.705 1.00 26.62 ?  271 HOH   B O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 47.988 -22.760 5.862   1.00 18.00 ?  272 HOH   B O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 49.326 -28.711 -6.884  1.00 15.57 ?  273 HOH   B O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 42.365 -34.700 3.776   1.00 26.22 ?  274 HOH   B O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 46.837 -29.566 9.831   1.00 32.22 ?  275 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 56.930 -8.648  8.467   1.00 19.22 ?  276 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 28.473 -30.897 -14.697 1.00 30.12 ?  277 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 30.561 -42.237 -10.609 1.00 29.88 ?  278 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 46.601 -31.261 -4.770  1.00 23.36 ?  279 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 27.962 -22.889 -7.982  1.00 18.08 ?  280 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 28.255 -34.353 -9.414  1.00 20.27 ?  281 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 57.079 -12.122 12.384  1.00 37.35 ?  282 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 45.928 -40.369 -3.555  1.00 27.82 ?  283 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 34.447 -12.761 2.600   1.00 25.33 ?  284 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 41.140 -5.539  11.532  1.00 44.19 ?  285 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 48.401 -25.042 3.115   1.00 13.67 ?  286 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 59.759 -15.319 8.163   1.00 32.06 ?  287 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 42.321 -9.948  -14.900 1.00 35.72 ?  288 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 36.836 -12.755 -1.534  1.00 26.07 ?  289 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 48.695 -20.021 5.957   1.00 14.30 ?  290 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 33.512 -15.315 -13.954 1.00 21.37 ?  291 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 47.068 -33.995 -4.595  1.00 17.45 ?  292 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 51.235 -37.610 -9.572  1.00 26.47 ?  293 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 37.526 -18.137 13.105  1.00 30.78 ?  294 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 27.561 -26.702 -15.631 1.00 32.32 ?  295 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 45.343 -33.386 -15.922 1.00 23.93 ?  296 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 52.510 -10.402 13.036  1.00 21.70 ?  297 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 42.891 -20.321 -20.783 1.00 34.57 ?  298 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 50.001 -24.593 5.826   1.00 33.32 ?  299 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 37.318 -35.663 7.213   1.00 33.20 ?  300 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 42.689 -12.308 -18.521 1.00 29.91 ?  301 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 44.051 -29.349 -4.666  1.00 23.35 ?  302 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 44.623 -27.452 2.003   1.00 16.00 ?  303 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 52.602 -35.657 -8.580  1.00 28.59 ?  304 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 35.081 -33.533 4.576   1.00 29.90 ?  305 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 52.519 -29.259 -13.011 1.00 25.21 ?  306 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 53.466 -30.198 4.512   1.00 19.39 ?  307 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 40.246 -10.840 -9.555  1.00 17.25 ?  308 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 32.816 -34.595 -5.879  1.00 17.50 ?  309 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 53.218 -16.110 -12.722 1.00 28.67 ?  310 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 43.498 -15.409 18.217  1.00 29.72 ?  311 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 37.851 -10.250 -10.787 1.00 17.29 ?  312 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 62.706 -13.575 4.747   1.00 26.96 ?  313 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 25.942 -21.483 -3.541  1.00 16.89 ?  314 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 51.400 -32.986 -10.759 1.00 39.77 ?  315 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 51.721 -5.933  -7.895  1.00 46.88 ?  316 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 43.195 -21.437 10.681  1.00 16.23 ?  317 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 48.105 -32.647 -16.594 1.00 41.83 ?  318 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 37.155 -30.603 -21.010 1.00 31.54 ?  319 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 41.736 -8.053  1.389   1.00 24.76 ?  320 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 62.850 -20.236 -0.772  1.00 37.67 ?  321 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 44.133 -1.789  7.599   1.00 46.61 ?  322 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 26.340 -21.042 -6.246  1.00 16.76 ?  323 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 59.976 -17.107 -10.461 1.00 33.38 ?  324 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 38.325 -12.749 7.922   1.00 18.69 ?  325 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 53.640 -12.571 -22.285 1.00 33.26 ?  326 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 36.720 -12.419 4.291   1.00 18.09 ?  327 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 44.576 -24.605 9.578   1.00 20.36 ?  328 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 57.628 -22.045 3.241   1.00 29.21 ?  329 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 38.395 -9.378  -13.294 1.00 27.21 ?  330 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 27.935 -14.797 -9.440  1.00 35.00 ?  331 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 41.205 -24.470 15.862  1.00 44.54 ?  332 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 48.596 -11.969 -14.014 1.00 26.76 ?  333 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 43.094 -34.645 0.113   1.00 20.04 ?  334 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 47.151 -24.499 8.189   1.00 26.10 ?  335 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 33.571 -31.208 11.055  1.00 33.59 ?  336 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 45.711 -36.258 -16.100 1.00 34.70 ?  337 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 39.461 -23.492 -20.343 1.00 36.40 ?  338 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 42.834 -43.481 -14.341 1.00 44.93 ?  339 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 47.463 -27.438 2.031   1.00 15.21 ?  340 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 46.824 -19.864 12.289  1.00 29.47 ?  341 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 37.020 -15.129 -16.510 1.00 41.67 ?  342 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 28.856 -42.921 -12.346 1.00 37.30 ?  343 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 37.103 -45.241 -9.801  1.00 37.10 ?  344 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 32.983 -14.666 1.064   1.00 18.82 ?  345 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 38.458 -12.279 -16.288 1.00 41.36 ?  346 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 27.771 -26.569 -0.584  1.00 29.66 ?  347 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 38.520 -22.336 15.022  1.00 38.86 ?  348 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 33.728 -9.455  -8.839  1.00 32.09 ?  349 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 39.833 -44.298 -11.212 1.00 38.08 ?  350 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 40.435 -43.491 -9.126  1.00 25.83 ?  351 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 62.564 -20.119 -4.765  1.00 42.04 ?  352 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 34.555 -10.328 7.652   1.00 23.75 ?  353 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 55.636 -8.260  10.829  1.00 24.58 ?  354 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 44.191 -37.341 -17.727 1.00 32.56 ?  355 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 23.212 -23.662 6.841   1.00 36.70 ?  356 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 36.061 -8.594  -9.698  1.00 33.70 ?  357 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 56.575 -7.300  3.155   1.00 26.11 ?  358 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 43.198 -12.664 -21.210 1.00 39.92 ?  359 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 61.509 -19.899 1.693   1.00 36.16 ?  360 HOH   B O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 34.103 -7.718  11.463  1.00 39.80 ?  361 HOH   B O    1 
HETATM 7042 O O    . HOH   F 4 .   ? 56.912 -21.553 -16.351 1.00 39.21 ?  362 HOH   B O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 27.150 -25.941 -11.398 1.00 33.72 ?  363 HOH   B O    1 
HETATM 7044 O O    . HOH   F 4 .   ? 40.228 -8.853  9.905   1.00 37.35 ?  364 HOH   B O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 54.185 -5.732  3.021   1.00 35.38 ?  365 HOH   B O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 40.103 -11.365 -13.951 1.00 33.29 ?  366 HOH   B O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 32.531 -23.645 14.093  1.00 39.39 ?  367 HOH   B O    1 
HETATM 7048 O O    . HOH   F 4 .   ? 58.938 -10.431 9.219   1.00 37.59 ?  368 HOH   B O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 48.355 -26.515 8.818   1.00 38.80 ?  369 HOH   B O    1 
HETATM 7050 O O    . HOH   F 4 .   ? 36.159 -8.679  9.002   1.00 37.29 ?  370 HOH   B O    1 
HETATM 7051 O O    . HOH   F 4 .   ? 56.099 -7.848  -0.597  1.00 33.29 ?  371 HOH   B O    1 
HETATM 7052 O O    . HOH   F 4 .   ? 39.844 -7.005  7.843   1.00 38.76 ?  372 HOH   B O    1 
HETATM 7053 O O    . HOH   F 4 .   ? 41.805 -10.012 -17.477 1.00 49.90 ?  373 HOH   B O    1 
HETATM 7054 O O    . HOH   F 4 .   ? 52.049 -12.888 13.385  1.00 31.18 ?  374 HOH   B O    1 
HETATM 7055 O O    . HOH   F 4 .   ? 62.981 -12.334 6.934   1.00 37.63 ?  375 HOH   B O    1 
HETATM 7056 O O    . HOH   F 4 .   ? 38.015 -10.594 10.097  1.00 30.02 ?  376 HOH   B O    1 
HETATM 7057 O O    . HOH   F 4 .   ? 41.845 -6.754  -4.870  1.00 46.38 ?  377 HOH   B O    1 
HETATM 7058 O O    . HOH   F 4 .   ? 36.530 -22.811 13.313  1.00 27.07 ?  378 HOH   B O    1 
HETATM 7059 O O    . HOH   F 4 .   ? 42.651 -17.072 -23.176 1.00 42.33 ?  379 HOH   B O    1 
HETATM 7060 O O    . HOH   F 4 .   ? 44.054 -5.591  -3.532  1.00 41.62 ?  380 HOH   B O    1 
HETATM 7061 O O    . HOH   F 4 .   ? 40.079 -7.632  3.227   1.00 33.58 ?  381 HOH   B O    1 
HETATM 7062 O O    . HOH   F 4 .   ? 39.685 -14.052 15.725  1.00 48.10 ?  382 HOH   B O    1 
HETATM 7063 O O    . HOH   F 4 .   ? 52.817 -29.874 7.215   1.00 23.99 ?  383 HOH   B O    1 
HETATM 7064 O O    . HOH   F 4 .   ? 60.455 -22.240 2.868   1.00 49.08 ?  384 HOH   B O    1 
HETATM 7065 O O    . HOH   F 4 .   ? 25.824 -18.882 -11.858 1.00 38.27 ?  385 HOH   B O    1 
HETATM 7066 O O    . HOH   F 4 .   ? 46.785 -5.334  2.888   1.00 39.49 ?  386 HOH   B O    1 
HETATM 7067 O O    . HOH   F 4 .   ? 35.382 -33.732 7.310   1.00 41.23 ?  387 HOH   B O    1 
HETATM 7068 O O    . HOH   F 4 .   ? 23.916 -20.850 -7.672  1.00 28.23 ?  388 HOH   B O    1 
HETATM 7069 O O    . HOH   F 4 .   ? 40.929 -9.785  15.849  1.00 44.87 ?  389 HOH   B O    1 
HETATM 7070 O O    . HOH   F 4 .   ? 35.284 -20.342 13.317  1.00 31.57 ?  390 HOH   B O    1 
HETATM 7071 O O    . HOH   F 4 .   ? 40.665 -6.647  -0.853  1.00 24.70 ?  391 HOH   B O    1 
HETATM 7072 O O    . HOH   F 4 .   ? 44.083 -31.775 -3.782  1.00 35.18 ?  392 HOH   B O    1 
HETATM 7073 O O    . HOH   F 4 .   ? 26.632 -28.005 -13.503 1.00 35.48 ?  393 HOH   B O    1 
HETATM 7074 O O    . HOH   F 4 .   ? 27.896 -27.076 2.162   1.00 30.66 ?  394 HOH   B O    1 
HETATM 7075 O O    . HOH   F 4 .   ? 24.612 -20.642 -10.491 1.00 37.55 ?  395 HOH   B O    1 
HETATM 7076 O O    . HOH   F 4 .   ? 34.376 -33.451 9.666   1.00 34.01 ?  396 HOH   B O    1 
HETATM 7077 O O    . HOH   F 4 .   ? 50.638 -30.788 8.704   1.00 29.28 ?  397 HOH   B O    1 
HETATM 7078 O O    . HOH   F 4 .   ? 26.861 -30.698 -12.639 1.00 29.31 ?  398 HOH   B O    1 
HETATM 7079 O O    . HOH   F 4 .   ? 57.703 -6.551  -2.385  1.00 34.32 ?  399 HOH   B O    1 
HETATM 7080 O O    . HOH   F 4 .   ? 45.738 -20.187 15.204  1.00 48.89 ?  400 HOH   B O    1 
HETATM 7081 O O    . HOH   F 4 .   ? 40.911 -11.782 -22.323 1.00 41.17 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.6197 0.6259 0.6864 -0.0106 -0.0281 0.0822  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6150 0.6225 0.6555 -0.0125 -0.0209 0.0571  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6178 0.6243 0.6758 -0.0122 -0.0271 0.0813  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6132 0.6212 0.6493 -0.0137 -0.0211 0.0583  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6050 0.6158 0.6455 -0.0187 -0.0294 0.0813  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6027 0.6141 0.6300 -0.0194 -0.0256 0.0684  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6074 0.6176 0.6562 -0.0176 -0.0313 0.0834  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6053 0.6158 0.6386 -0.0183 -0.0267 0.0686  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6264 0.6299 0.6882 -0.0088 -0.0237 0.0802  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6198 0.6256 0.6574 -0.0104 -0.0171 0.0509  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6295 0.6317 0.6907 -0.0073 -0.0226 0.0796  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6221 0.6271 0.6589 -0.0092 -0.0157 0.0482  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6291 0.6319 0.6912 -0.0079 -0.0222 0.0801  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6219 0.6272 0.6591 -0.0094 -0.0156 0.0485  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.5869 0.6037 0.5965 -0.0270 -0.0292 0.0787  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5512 0.5791 0.5082 -0.0443 -0.0324 0.0841  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.5081 0.5540 0.4581 -0.0604 -0.0217 0.0624  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.5091 0.5562 0.4516 -0.0615 -0.0231 0.0659  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5554 0.5776 0.4647 -0.0463 -0.0456 0.1106  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5575 0.5743 0.4235 -0.0495 -0.0567 0.1360  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5595 0.5717 0.4052 -0.0517 -0.0610 0.1475  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5567 0.5732 0.4128 -0.0493 -0.0610 0.1467  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4627 0.5232 0.4125 -0.0766 -0.0106 0.0372  5   SER   A N   
47   C CA  . SER   A 5   ? 0.4162 0.4908 0.3730 -0.0917 0.0024  0.0109  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3688 0.4491 0.3240 -0.0980 0.0162  -0.0034 5   SER   A C   
49   O O   . SER   A 5   ? 0.3721 0.4573 0.3216 -0.0908 0.0141  -0.0161 5   SER   A O   
50   C CB  . SER   A 5   ? 0.4200 0.4993 0.3908 -0.0982 0.0043  0.0016  5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4228 0.5042 0.4012 -0.1021 0.0075  -0.0030 5   SER   A OG  
57   N N   . PHE   A 6   ? 0.3138 0.3966 0.2730 -0.1104 0.0304  0.0005  6   PHE   A N   
58   C CA  . PHE   A 6   ? 0.2680 0.3441 0.2335 -0.1121 0.0362  0.0178  6   PHE   A CA  
59   C C   . PHE   A 6   ? 0.2642 0.3336 0.2390 -0.1071 0.0468  0.0109  6   PHE   A C   
60   O O   . PHE   A 6   ? 0.2730 0.3390 0.2734 -0.1122 0.0516  0.0240  6   PHE   A O   
61   C CB  . PHE   A 6   ? 0.2481 0.3087 0.2175 -0.0998 0.0193  0.0323  6   PHE   A CB  
62   C CG  . PHE   A 6   ? 0.2336 0.2828 0.2044 -0.0821 0.0086  0.0347  6   PHE   A CG  
63   C CD1 . PHE   A 6   ? 0.2244 0.2693 0.2049 -0.0724 0.0059  0.0368  6   PHE   A CD1 
64   C CD2 . PHE   A 6   ? 0.2379 0.2756 0.2181 -0.0657 0.0131  0.0362  6   PHE   A CD2 
65   C CE1 . PHE   A 6   ? 0.2245 0.2615 0.2148 -0.0671 0.0068  0.0378  6   PHE   A CE1 
66   C CE2 . PHE   A 6   ? 0.2368 0.2696 0.2325 -0.0580 0.0128  0.0284  6   PHE   A CE2 
67   C CZ  . PHE   A 6   ? 0.2303 0.2635 0.2224 -0.0611 0.0098  0.0306  6   PHE   A CZ  
77   N N   A SER   A 7   ? 0.2569 0.3253 0.2248 -0.1088 0.0525  0.0027  7   SER   A N   
78   N N   B SER   A 7   ? 0.2586 0.3253 0.2426 -0.0893 0.0450  0.0037  7   SER   A N   
79   C CA  A SER   A 7   ? 0.2587 0.3216 0.2354 -0.1003 0.0553  -0.0114 7   SER   A CA  
80   C CA  B SER   A 7   ? 0.2563 0.3163 0.2535 -0.0681 0.0413  -0.0030 7   SER   A CA  
81   C C   A SER   A 7   ? 0.2417 0.2819 0.2123 -0.0978 0.0661  -0.0111 7   SER   A C   
82   C C   B SER   A 7   ? 0.2441 0.2922 0.2331 -0.0528 0.0446  -0.0005 7   SER   A C   
83   O O   A SER   A 7   ? 0.2538 0.2743 0.2136 -0.1041 0.0660  -0.0138 7   SER   A O   
84   O O   B SER   A 7   ? 0.2511 0.2924 0.2359 -0.0524 0.0426  -0.0027 7   SER   A O   
85   C CB  A SER   A 7   ? 0.2802 0.3503 0.2688 -0.0892 0.0556  -0.0093 7   SER   A CB  
86   C CB  B SER   A 7   ? 0.2668 0.3282 0.2820 -0.0607 0.0360  -0.0046 7   SER   A CB  
87   O OG  A SER   A 7   ? 0.2989 0.3683 0.2977 -0.0803 0.0546  -0.0088 7   SER   A OG  
88   O OG  B SER   A 7   ? 0.2759 0.3359 0.3052 -0.0545 0.0311  -0.0035 7   SER   A OG  
99   N N   A GLY   A 8   ? 0.2173 0.2499 0.2133 -0.0863 0.0588  -0.0179 8   GLY   A N   
100  N N   B GLY   A 8   ? 0.2245 0.2676 0.2149 -0.0379 0.0441  0.0028  8   GLY   A N   
101  C CA  A GLY   A 8   ? 0.2034 0.2257 0.2161 -0.0548 0.0526  -0.0153 8   GLY   A CA  
102  C CA  B GLY   A 8   ? 0.2065 0.2427 0.2027 -0.0235 0.0378  0.0080  8   GLY   A CA  
103  C C   A GLY   A 8   ? 0.1791 0.2056 0.2130 -0.0361 0.0456  -0.0087 8   GLY   A C   
104  C C   B GLY   A 8   ? 0.1848 0.2184 0.1856 -0.0099 0.0329  0.0138  8   GLY   A C   
105  O O   A GLY   A 8   ? 0.1822 0.2055 0.2313 -0.0158 0.0476  -0.0279 8   GLY   A O   
106  O O   B GLY   A 8   ? 0.1839 0.2195 0.1941 -0.0018 0.0281  0.0057  8   GLY   A O   
113  N N   A TYR   A 9   ? 0.1588 0.1857 0.2060 -0.0252 0.0395  0.0084  9   TYR   A N   
114  N N   B TYR   A 9   ? 0.1697 0.1971 0.1806 -0.0023 0.0329  0.0255  9   TYR   A N   
115  C CA  A TYR   A 9   ? 0.1453 0.1743 0.1867 -0.0219 0.0324  0.0104  9   TYR   A CA  
116  C CA  B TYR   A 9   ? 0.1597 0.1807 0.1695 -0.0005 0.0310  0.0265  9   TYR   A CA  
117  C C   A TYR   A 9   ? 0.1447 0.1558 0.1838 -0.0135 0.0432  0.0194  9   TYR   A C   
118  C C   B TYR   A 9   ? 0.1529 0.1631 0.1662 0.0085  0.0348  0.0227  9   TYR   A C   
119  O O   A TYR   A 9   ? 0.1699 0.1591 0.1916 -0.0128 0.0298  0.0135  9   TYR   A O   
120  O O   B TYR   A 9   ? 0.1585 0.1671 0.1792 0.0151  0.0321  0.0206  9   TYR   A O   
121  C CB  A TYR   A 9   ? 0.1391 0.1953 0.1873 -0.0167 0.0262  0.0059  9   TYR   A CB  
122  C CB  B TYR   A 9   ? 0.1626 0.1879 0.1745 -0.0066 0.0233  0.0258  9   TYR   A CB  
123  C CG  A TYR   A 9   ? 0.1415 0.2075 0.1873 -0.0124 0.0367  0.0007  9   TYR   A CG  
124  C CG  B TYR   A 9   ? 0.1696 0.1921 0.1833 -0.0170 0.0172  0.0269  9   TYR   A CG  
125  C CD1 A TYR   A 9   ? 0.1460 0.2136 0.1922 -0.0217 0.0416  0.0061  9   TYR   A CD1 
126  C CD1 B TYR   A 9   ? 0.1732 0.1944 0.1889 -0.0265 0.0156  0.0289  9   TYR   A CD1 
127  C CD2 A TYR   A 9   ? 0.1418 0.2129 0.1947 -0.0070 0.0287  0.0092  9   TYR   A CD2 
128  C CD2 B TYR   A 9   ? 0.1704 0.1908 0.1812 -0.0196 0.0121  0.0314  9   TYR   A CD2 
129  C CE1 A TYR   A 9   ? 0.1549 0.2210 0.2009 -0.0256 0.0421  0.0080  9   TYR   A CE1 
130  C CE1 B TYR   A 9   ? 0.1765 0.1969 0.1920 -0.0330 0.0141  0.0277  9   TYR   A CE1 
131  C CE2 A TYR   A 9   ? 0.1441 0.2228 0.1931 -0.0105 0.0324  0.0057  9   TYR   A CE2 
132  C CE2 B TYR   A 9   ? 0.1714 0.1934 0.1785 -0.0251 0.0121  0.0308  9   TYR   A CE2 
133  C CZ  A TYR   A 9   ? 0.1502 0.2273 0.2093 -0.0301 0.0554  0.0031  9   TYR   A CZ  
134  C CZ  B TYR   A 9   ? 0.1739 0.1954 0.1866 -0.0351 0.0174  0.0293  9   TYR   A CZ  
135  O OH  A TYR   A 9   ? 0.1636 0.2423 0.2277 -0.0444 0.0636  0.0008  9   TYR   A OH  
136  O OH  B TYR   A 9   ? 0.1775 0.2005 0.1904 -0.0449 0.0211  0.0277  9   TYR   A OH  
155  N N   A LEU   A 10  ? 0.1415 0.1452 0.1948 -0.0133 0.0310  0.0238  10  LEU   A N   
156  N N   B LEU   A 10  ? 0.1482 0.1520 0.1617 0.0064  0.0328  0.0107  10  LEU   A N   
157  C CA  A LEU   A 10  ? 0.1346 0.1487 0.1928 -0.0196 0.0230  0.0348  10  LEU   A CA  
158  C CA  B LEU   A 10  ? 0.1385 0.1456 0.1574 0.0017  0.0263  0.0082  10  LEU   A CA  
159  C C   A LEU   A 10  ? 0.1281 0.1406 0.1930 -0.0177 0.0187  0.0328  10  LEU   A C   
160  C C   B LEU   A 10  ? 0.1383 0.1357 0.1547 -0.0047 0.0316  0.0112  10  LEU   A C   
161  O O   A LEU   A 10  ? 0.1341 0.1382 0.2096 -0.0093 0.0314  0.0357  10  LEU   A O   
162  O O   B LEU   A 10  ? 0.1416 0.1271 0.1592 -0.0036 0.0461  0.0168  10  LEU   A O   
163  C CB  A LEU   A 10  ? 0.1505 0.1616 0.2178 -0.0137 0.0164  0.0505  10  LEU   A CB  
164  C CB  B LEU   A 10  ? 0.1366 0.1493 0.1564 0.0022  0.0161  0.0085  10  LEU   A CB  
165  C CG  A LEU   A 10  ? 0.1818 0.1795 0.2591 -0.0139 -0.0079 0.0538  10  LEU   A CG  
166  C CG  B LEU   A 10  ? 0.1378 0.1591 0.1630 0.0037  0.0077  0.0036  10  LEU   A CG  
167  C CD1 A LEU   A 10  ? 0.1946 0.1808 0.2820 -0.0275 -0.0157 0.0564  10  LEU   A CD1 
168  C CD1 B LEU   A 10  ? 0.1381 0.1647 0.1678 0.0060  0.0057  -0.0063 10  LEU   A CD1 
169  C CD2 A LEU   A 10  ? 0.1976 0.1971 0.2689 -0.0123 -0.0117 0.0422  10  LEU   A CD2 
170  C CD2 B LEU   A 10  ? 0.1373 0.1663 0.1624 -0.0046 0.0094  0.0157  10  LEU   A CD2 
193  N N   A LYS   A 11  ? 0.1318 0.1378 0.1870 -0.0194 0.0228  0.0324  11  LYS   A N   
194  N N   B LYS   A 11  ? 0.1421 0.1346 0.1544 -0.0118 0.0227  0.0132  11  LYS   A N   
195  C CA  A LYS   A 11  ? 0.1345 0.1349 0.1930 -0.0244 0.0179  0.0277  11  LYS   A CA  
196  C CA  B LYS   A 11  ? 0.1434 0.1278 0.1500 -0.0139 0.0180  0.0123  11  LYS   A CA  
197  C C   A LYS   A 11  ? 0.1304 0.1403 0.1974 -0.0235 0.0187  0.0192  11  LYS   A C   
198  C C   B LYS   A 11  ? 0.1384 0.1202 0.1530 -0.0132 0.0159  0.0097  11  LYS   A C   
199  O O   A LYS   A 11  ? 0.1373 0.1634 0.2350 -0.0424 0.0231  0.0120  11  LYS   A O   
200  O O   B LYS   A 11  ? 0.1359 0.1114 0.1674 -0.0160 0.0173  -0.0071 11  LYS   A O   
201  C CB  A LYS   A 11  ? 0.1405 0.1319 0.1836 -0.0196 0.0183  0.0240  11  LYS   A CB  
202  C CB  B LYS   A 11  ? 0.1549 0.1223 0.1408 -0.0156 0.0176  0.0077  11  LYS   A CB  
203  C CG  A LYS   A 11  ? 0.1562 0.1309 0.1846 -0.0203 0.0184  0.0195  11  LYS   A CG  
204  C CG  B LYS   A 11  ? 0.1669 0.1248 0.1332 -0.0115 0.0172  0.0093  11  LYS   A CG  
205  C CD  A LYS   A 11  ? 0.1688 0.1323 0.1952 -0.0170 0.0153  0.0204  11  LYS   A CD  
206  C CD  B LYS   A 11  ? 0.1760 0.1305 0.1357 -0.0112 0.0210  0.0080  11  LYS   A CD  
207  C CE  A LYS   A 11  ? 0.1811 0.1235 0.1972 -0.0153 0.0106  0.0198  11  LYS   A CE  
208  C CE  B LYS   A 11  ? 0.1844 0.1384 0.1343 -0.0075 0.0264  0.0096  11  LYS   A CE  
209  N NZ  A LYS   A 11  ? 0.1791 0.1165 0.1964 -0.0031 -0.0005 0.0101  11  LYS   A NZ  
210  N NZ  B LYS   A 11  ? 0.1895 0.1435 0.1323 -0.0030 0.0265  0.0104  11  LYS   A NZ  
237  N N   A LEU   A 12  ? 0.1264 0.1313 0.1791 -0.0226 0.0226  0.0228  12  LEU   A N   
238  N N   B LEU   A 12  ? 0.1373 0.1313 0.1557 -0.0020 0.0084  0.0073  12  LEU   A N   
239  C CA  A LEU   A 12  ? 0.1314 0.1365 0.1813 -0.0187 0.0124  0.0279  12  LEU   A CA  
240  C CA  B LEU   A 12  ? 0.1405 0.1413 0.1603 0.0018  0.0117  0.0078  12  LEU   A CA  
241  C C   A LEU   A 12  ? 0.1373 0.1286 0.1870 -0.0225 0.0135  0.0316  12  LEU   A C   
242  C C   B LEU   A 12  ? 0.1400 0.1407 0.1561 0.0039  0.0171  0.0020  12  LEU   A C   
243  O O   A LEU   A 12  ? 0.1391 0.1279 0.1965 -0.0146 0.0177  0.0149  12  LEU   A O   
244  O O   B LEU   A 12  ? 0.1468 0.1426 0.1448 0.0082  0.0156  -0.0024 12  LEU   A O   
245  C CB  A LEU   A 12  ? 0.1367 0.1394 0.1806 -0.0157 0.0093  0.0321  12  LEU   A CB  
246  C CB  B LEU   A 12  ? 0.1492 0.1535 0.1796 -0.0009 0.0110  0.0180  12  LEU   A CB  
247  C CG  A LEU   A 12  ? 0.1460 0.1510 0.2086 -0.0064 0.0175  0.0428  12  LEU   A CG  
248  C CG  B LEU   A 12  ? 0.1552 0.1614 0.2022 -0.0042 0.0193  0.0293  12  LEU   A CG  
249  C CD1 A LEU   A 12  ? 0.1633 0.1490 0.2175 -0.0010 0.0253  0.0458  12  LEU   A CD1 
250  C CD1 B LEU   A 12  ? 0.1608 0.1657 0.2080 -0.0059 0.0227  0.0247  12  LEU   A CD1 
251  C CD2 A LEU   A 12  ? 0.1482 0.1710 0.2363 -0.0138 0.0114  0.0594  12  LEU   A CD2 
252  C CD2 B LEU   A 12  ? 0.1573 0.1668 0.2173 -0.0087 0.0192  0.0426  12  LEU   A CD2 
275  N N   A THR   A 13  ? 0.1332 0.1257 0.2017 -0.0173 0.0128  0.0272  13  THR   A N   
276  N N   B THR   A 13  ? 0.1351 0.1364 0.1666 -0.0004 0.0171  0.0057  13  THR   A N   
277  C CA  A THR   A 13  ? 0.1334 0.1325 0.1985 -0.0137 0.0218  0.0185  13  THR   A CA  
278  C CA  B THR   A 13  ? 0.1314 0.1393 0.1658 -0.0062 0.0227  0.0112  13  THR   A CA  
279  C C   A THR   A 13  ? 0.1343 0.1309 0.2053 -0.0098 0.0109  0.0295  13  THR   A C   
280  C C   B THR   A 13  ? 0.1350 0.1416 0.1720 -0.0103 0.0259  0.0142  13  THR   A C   
281  O O   A THR   A 13  ? 0.1279 0.1373 0.1958 -0.0025 0.0082  0.0307  13  THR   A O   
282  O O   B THR   A 13  ? 0.1423 0.1425 0.1795 -0.0099 0.0286  0.0170  13  THR   A O   
283  C CB  A THR   A 13  ? 0.1404 0.1449 0.2181 -0.0049 0.0155  0.0227  13  THR   A CB  
284  C CB  B THR   A 13  ? 0.1287 0.1469 0.1682 -0.0045 0.0285  0.0125  13  THR   A CB  
285  O OG1 A THR   A 13  ? 0.1413 0.1419 0.2277 -0.0149 0.0013  0.0319  13  THR   A OG1 
286  O OG1 B THR   A 13  ? 0.1136 0.1473 0.1714 -0.0058 0.0498  0.0254  13  THR   A OG1 
287  C CG2 A THR   A 13  ? 0.1527 0.1681 0.2312 0.0001  0.0243  0.0115  13  THR   A CG2 
288  C CG2 B THR   A 13  ? 0.1355 0.1556 0.1779 0.0032  0.0227  0.0083  13  THR   A CG2 
303  N N   A ASP   A 14  ? 0.1414 0.1330 0.2281 -0.0161 0.0106  0.0375  14  ASP   A N   
304  N N   B ASP   A 14  ? 0.1334 0.1427 0.1764 -0.0133 0.0203  0.0175  14  ASP   A N   
305  C CA  A ASP   A 14  ? 0.1411 0.1429 0.2437 -0.0097 0.0080  0.0532  14  ASP   A CA  
306  C CA  B ASP   A 14  ? 0.1386 0.1469 0.1886 -0.0127 0.0142  0.0392  14  ASP   A CA  
307  C C   A ASP   A 14  ? 0.1452 0.1466 0.2269 -0.0148 0.0017  0.0394  14  ASP   A C   
308  C C   B ASP   A 14  ? 0.1391 0.1472 0.1728 -0.0194 0.0007  0.0537  14  ASP   A C   
309  O O   A ASP   A 14  ? 0.1684 0.1649 0.2381 -0.0270 -0.0067 0.0394  14  ASP   A O   
310  O O   B ASP   A 14  ? 0.1475 0.1511 0.1730 -0.0310 -0.0063 0.0619  14  ASP   A O   
311  C CB  A ASP   A 14  ? 0.1564 0.1710 0.3022 -0.0085 0.0112  0.0720  14  ASP   A CB  
312  C CB  B ASP   A 14  ? 0.1469 0.1521 0.2312 -0.0112 0.0020  0.0355  14  ASP   A CB  
313  C CG  A ASP   A 14  ? 0.1794 0.2236 0.3814 -0.0054 0.0138  0.0697  14  ASP   A CG  
314  C CG  B ASP   A 14  ? 0.1533 0.1704 0.2727 -0.0125 0.0015  0.0319  14  ASP   A CG  
315  O OD1 A ASP   A 14  ? 0.1962 0.2450 0.4127 -0.0026 -0.0010 0.0763  14  ASP   A OD1 
316  O OD1 B ASP   A 14  ? 0.1585 0.1771 0.2870 -0.0317 0.0056  0.0358  14  ASP   A OD1 
317  O OD2 A ASP   A 14  ? 0.1965 0.2511 0.4173 0.0152  0.0098  0.0522  14  ASP   A OD2 
318  O OD2 B ASP   A 14  ? 0.1575 0.1762 0.2927 0.0039  -0.0126 0.0234  14  ASP   A OD2 
327  N N   A ASN   A 15  ? 0.1269 0.1324 0.2199 -0.0163 0.0074  0.0441  15  ASN   A N   
328  N N   B ASN   A 15  ? 0.1340 0.1368 0.1754 -0.0130 0.0052  0.0570  15  ASN   A N   
329  C CA  A ASN   A 15  ? 0.1320 0.1364 0.2356 -0.0130 -0.0016 0.0364  15  ASN   A CA  
330  C CA  B ASN   A 15  ? 0.1343 0.1400 0.1808 -0.0082 0.0062  0.0480  15  ASN   A CA  
331  C C   A ASN   A 15  ? 0.1353 0.1372 0.2458 -0.0209 -0.0057 0.0394  15  ASN   A C   
332  C C   B ASN   A 15  ? 0.1371 0.1373 0.1931 -0.0133 0.0092  0.0463  15  ASN   A C   
333  O O   A ASN   A 15  ? 0.1426 0.1464 0.2504 -0.0288 -0.0170 0.0528  15  ASN   A O   
334  O O   B ASN   A 15  ? 0.1468 0.1466 0.2026 -0.0189 0.0027  0.0521  15  ASN   A O   
335  C CB  A ASN   A 15  ? 0.1268 0.1420 0.2225 -0.0080 0.0078  0.0328  15  ASN   A CB  
336  C CB  B ASN   A 15  ? 0.1344 0.1459 0.1723 -0.0021 0.0028  0.0495  15  ASN   A CB  
337  C CG  A ASN   A 15  ? 0.1326 0.1528 0.2329 -0.0130 0.0117  0.0226  15  ASN   A CG  
338  C CG  B ASN   A 15  ? 0.1357 0.1504 0.1714 0.0007  0.0078  0.0414  15  ASN   A CG  
339  O OD1 A ASN   A 15  ? 0.1463 0.1547 0.2564 -0.0254 0.0121  0.0173  15  ASN   A OD1 
340  O OD1 B ASN   A 15  ? 0.1382 0.1445 0.1823 0.0013  0.0168  0.0460  15  ASN   A OD1 
341  N ND2 A ASN   A 15  ? 0.1370 0.1700 0.2186 -0.0160 0.0091  0.0248  15  ASN   A ND2 
342  N ND2 B ASN   A 15  ? 0.1396 0.1594 0.1673 -0.0015 0.0048  0.0398  15  ASN   A ND2 
355  N N   A VAL   A 16  ? 0.1287 0.1313 0.2341 -0.0076 0.0063  0.0352  16  VAL   A N   
356  N N   B VAL   A 16  ? 0.1303 0.1304 0.1833 -0.0098 0.0196  0.0425  16  VAL   A N   
357  C CA  A VAL   A 16  ? 0.1210 0.1347 0.2229 -0.0100 0.0125  0.0353  16  VAL   A CA  
358  C CA  B VAL   A 16  ? 0.1305 0.1323 0.1736 -0.0044 0.0244  0.0393  16  VAL   A CA  
359  C C   A VAL   A 16  ? 0.1198 0.1317 0.2181 -0.0103 0.0062  0.0341  16  VAL   A C   
360  C C   B VAL   A 16  ? 0.1252 0.1387 0.1690 -0.0019 0.0173  0.0286  16  VAL   A C   
361  O O   A VAL   A 16  ? 0.1126 0.1225 0.2399 -0.0108 0.0181  0.0255  16  VAL   A O   
362  O O   B VAL   A 16  ? 0.1214 0.1347 0.1781 -0.0007 0.0224  0.0304  16  VAL   A O   
363  C CB  A VAL   A 16  ? 0.1284 0.1568 0.2248 0.0044  0.0279  0.0412  16  VAL   A CB  
364  C CB  B VAL   A 16  ? 0.1421 0.1373 0.1743 0.0042  0.0366  0.0387  16  VAL   A CB  
365  C CG1 A VAL   A 16  ? 0.1438 0.1709 0.2405 0.0090  0.0177  0.0467  16  VAL   A CG1 
366  C CG1 B VAL   A 16  ? 0.1480 0.1404 0.1784 0.0118  0.0347  0.0402  16  VAL   A CG1 
367  C CG2 A VAL   A 16  ? 0.1379 0.1704 0.2341 0.0110  0.0378  0.0324  16  VAL   A CG2 
368  C CG2 B VAL   A 16  ? 0.1461 0.1425 0.1879 0.0088  0.0415  0.0374  16  VAL   A CG2 
387  N N   A TYR   A 17  ? 0.1241 0.1310 0.2137 -0.0155 0.0161  0.0392  17  TYR   A N   
388  N N   B TYR   A 17  ? 0.1294 0.1418 0.1615 -0.0064 0.0142  0.0193  17  TYR   A N   
389  C CA  A TYR   A 17  ? 0.1256 0.1290 0.2005 -0.0184 0.0167  0.0384  17  TYR   A CA  
390  C CA  B TYR   A 17  ? 0.1378 0.1447 0.1585 -0.0123 0.0190  0.0174  17  TYR   A CA  
391  C C   A TYR   A 17  ? 0.1302 0.1260 0.2080 -0.0137 0.0186  0.0250  17  TYR   A C   
392  C C   B TYR   A 17  ? 0.1313 0.1459 0.1469 -0.0157 0.0304  0.0184  17  TYR   A C   
393  O O   A TYR   A 17  ? 0.1302 0.1210 0.2030 -0.0129 0.0221  0.0287  17  TYR   A O   
394  O O   B TYR   A 17  ? 0.1276 0.1497 0.1386 -0.0208 0.0323  0.0190  17  TYR   A O   
395  C CB  A TYR   A 17  ? 0.1362 0.1309 0.2014 -0.0182 0.0145  0.0325  17  TYR   A CB  
396  C CB  B TYR   A 17  ? 0.1598 0.1477 0.1631 -0.0182 0.0191  0.0203  17  TYR   A CB  
397  C CG  A TYR   A 17  ? 0.1612 0.1424 0.2033 -0.0287 -0.0041 0.0300  17  TYR   A CG  
398  C CG  B TYR   A 17  ? 0.1842 0.1547 0.1692 -0.0163 0.0030  0.0135  17  TYR   A CG  
399  C CD1 A TYR   A 17  ? 0.1782 0.1443 0.2011 -0.0113 -0.0174 0.0248  17  TYR   A CD1 
400  C CD1 B TYR   A 17  ? 0.1979 0.1590 0.1811 -0.0098 -0.0011 0.0150  17  TYR   A CD1 
401  C CD2 A TYR   A 17  ? 0.1784 0.1518 0.1915 -0.0446 -0.0072 0.0351  17  TYR   A CD2 
402  C CD2 B TYR   A 17  ? 0.1971 0.1655 0.1710 -0.0181 -0.0043 0.0130  17  TYR   A CD2 
403  C CE1 A TYR   A 17  ? 0.1935 0.1465 0.2038 -0.0242 -0.0368 0.0277  17  TYR   A CE1 
404  C CE1 B TYR   A 17  ? 0.2081 0.1655 0.1934 -0.0071 -0.0071 0.0149  17  TYR   A CE1 
405  C CE2 A TYR   A 17  ? 0.1977 0.1507 0.1927 -0.0519 -0.0252 0.0271  17  TYR   A CE2 
406  C CE2 B TYR   A 17  ? 0.2098 0.1721 0.1826 -0.0165 -0.0111 0.0132  17  TYR   A CE2 
407  C CZ  A TYR   A 17  ? 0.2109 0.1462 0.1947 -0.0432 -0.0411 0.0349  17  TYR   A CZ  
408  C CZ  B TYR   A 17  ? 0.2171 0.1744 0.1928 -0.0098 -0.0138 0.0146  17  TYR   A CZ  
409  O OH  A TYR   A 17  ? 0.2309 0.1469 0.2057 -0.0508 -0.0408 0.0335  17  TYR   A OH  
410  O OH  B TYR   A 17  ? 0.2264 0.1802 0.2112 -0.0069 -0.0110 0.0150  17  TYR   A OH  
429  N N   A ILE   A 18  ? 0.1335 0.1338 0.2109 -0.0144 0.0206  0.0394  18  ILE   A N   
430  N N   B ILE   A 18  ? 0.1274 0.1427 0.1381 -0.0150 0.0363  0.0256  18  ILE   A N   
431  C CA  A ILE   A 18  ? 0.1376 0.1335 0.2010 -0.0094 0.0215  0.0288  18  ILE   A CA  
432  C CA  B ILE   A 18  ? 0.1276 0.1408 0.1382 -0.0073 0.0375  0.0226  18  ILE   A CA  
433  C C   A ILE   A 18  ? 0.1394 0.1424 0.2009 -0.0230 0.0198  0.0238  18  ILE   A C   
434  C C   B ILE   A 18  ? 0.1318 0.1491 0.1246 -0.0116 0.0295  0.0184  18  ILE   A C   
435  O O   A ILE   A 18  ? 0.1380 0.1541 0.2184 -0.0266 0.0249  0.0321  18  ILE   A O   
436  O O   B ILE   A 18  ? 0.1259 0.1565 0.1346 -0.0095 0.0310  0.0231  18  ILE   A O   
437  C CB  A ILE   A 18  ? 0.1384 0.1335 0.1794 0.0018  0.0253  0.0354  18  ILE   A CB  
438  C CB  B ILE   A 18  ? 0.1291 0.1367 0.1430 0.0031  0.0478  0.0197  18  ILE   A CB  
439  C CG1 A ILE   A 18  ? 0.1482 0.1320 0.1750 0.0200  0.0296  0.0361  18  ILE   A CG1 
440  C CG1 B ILE   A 18  ? 0.1442 0.1468 0.1614 0.0028  0.0500  0.0207  18  ILE   A CG1 
441  C CG2 A ILE   A 18  ? 0.1413 0.1373 0.1861 0.0025  0.0160  0.0256  18  ILE   A CG2 
442  C CG2 B ILE   A 18  ? 0.1312 0.1365 0.1512 0.0067  0.0475  0.0161  18  ILE   A CG2 
443  C CD1 A ILE   A 18  ? 0.1706 0.1479 0.1867 0.0273  0.0213  0.0406  18  ILE   A CD1 
444  C CD1 B ILE   A 18  ? 0.1520 0.1551 0.1778 0.0084  0.0554  0.0070  18  ILE   A CD1 
467  N N   A LYS   A 19  ? 0.1415 0.1415 0.1771 -0.0171 0.0292  0.0194  19  LYS   A N   
468  N N   B LYS   A 19  ? 0.1407 0.1515 0.1186 -0.0111 0.0368  0.0051  19  LYS   A N   
469  C CA  A LYS   A 19  ? 0.1553 0.1585 0.1777 -0.0181 0.0307  0.0205  19  LYS   A CA  
470  C CA  B LYS   A 19  ? 0.1583 0.1665 0.1379 -0.0080 0.0423  -0.0078 19  LYS   A CA  
471  C C   A LYS   A 19  ? 0.1465 0.1506 0.1833 -0.0070 0.0377  0.0333  19  LYS   A C   
472  C C   B LYS   A 19  ? 0.1679 0.1729 0.1558 -0.0018 0.0426  -0.0105 19  LYS   A C   
473  O O   A LYS   A 19  ? 0.1429 0.1463 0.1804 -0.0024 0.0316  0.0335  19  LYS   A O   
474  O O   B LYS   A 19  ? 0.1710 0.1702 0.1572 -0.0044 0.0416  -0.0099 19  LYS   A O   
475  C CB  A LYS   A 19  ? 0.1820 0.1831 0.1879 -0.0206 0.0269  0.0137  19  LYS   A CB  
476  C CB  B LYS   A 19  ? 0.1615 0.1760 0.1450 -0.0075 0.0493  -0.0195 19  LYS   A CB  
477  C CG  A LYS   A 19  ? 0.2151 0.2011 0.1946 -0.0226 0.0275  0.0003  19  LYS   A CG  
478  C CG  B LYS   A 19  ? 0.1823 0.1913 0.1570 -0.0068 0.0468  -0.0183 19  LYS   A CG  
479  C CD  A LYS   A 19  ? 0.2452 0.2197 0.2086 -0.0295 0.0263  -0.0092 19  LYS   A CD  
480  C CD  B LYS   A 19  ? 0.2015 0.2046 0.1730 -0.0112 0.0437  -0.0162 19  LYS   A CD  
481  C CE  A LYS   A 19  ? 0.2684 0.2297 0.2258 -0.0370 0.0297  -0.0157 19  LYS   A CE  
482  C CE  B LYS   A 19  ? 0.2132 0.2139 0.1828 -0.0173 0.0403  -0.0159 19  LYS   A CE  
483  N NZ  A LYS   A 19  ? 0.2818 0.2361 0.2279 -0.0446 0.0382  -0.0215 19  LYS   A NZ  
484  N NZ  B LYS   A 19  ? 0.2220 0.2204 0.1893 -0.0230 0.0406  -0.0205 19  LYS   A NZ  
511  N N   A ASN   A 20  ? 0.1513 0.1598 0.2039 -0.0136 0.0389  0.0482  20  ASN   A N   
512  N N   B ASN   A 20  ? 0.1779 0.1855 0.1780 0.0027  0.0432  -0.0157 20  ASN   A N   
513  C CA  A ASN   A 20  ? 0.1691 0.1801 0.2332 0.0122  0.0629  0.0446  20  ASN   A CA  
514  C CA  B ASN   A 20  ? 0.1890 0.2024 0.1997 0.0070  0.0416  -0.0161 20  ASN   A CA  
515  C C   A ASN   A 20  ? 0.1889 0.1826 0.2499 0.0003  0.0846  0.0329  20  ASN   A C   
516  C C   B ASN   A 20  ? 0.1975 0.2023 0.2062 -0.0024 0.0497  -0.0202 20  ASN   A C   
517  O O   A ASN   A 20  ? 0.2148 0.1922 0.2602 -0.0225 0.0876  0.0111  20  ASN   A O   
518  O O   B ASN   A 20  ? 0.2052 0.2053 0.2124 -0.0102 0.0535  -0.0303 20  ASN   A O   
519  C CB  A ASN   A 20  ? 0.1774 0.1941 0.2468 0.0306  0.0668  0.0600  20  ASN   A CB  
520  C CB  B ASN   A 20  ? 0.1956 0.2175 0.2153 0.0178  0.0360  -0.0122 20  ASN   A CB  
521  C CG  A ASN   A 20  ? 0.1926 0.2030 0.2677 0.0480  0.0801  0.0678  20  ASN   A CG  
522  C CG  B ASN   A 20  ? 0.2038 0.2293 0.2337 0.0278  0.0353  -0.0068 20  ASN   A CG  
523  O OD1 A ASN   A 20  ? 0.2247 0.2145 0.3025 0.0609  0.0924  0.0601  20  ASN   A OD1 
524  O OD1 B ASN   A 20  ? 0.2160 0.2382 0.2420 0.0291  0.0307  -0.0019 20  ASN   A OD1 
525  N ND2 A ASN   A 20  ? 0.1904 0.2020 0.2746 0.0491  0.0682  0.0816  20  ASN   A ND2 
526  N ND2 B ASN   A 20  ? 0.2033 0.2269 0.2359 0.0379  0.0398  -0.0099 20  ASN   A ND2 
539  N N   A ALA   A 21  ? 0.1890 0.1819 0.2573 0.0037  0.0732  0.0269  21  ALA   A N   
540  N N   B ALA   A 21  ? 0.1992 0.2000 0.2126 -0.0047 0.0434  -0.0126 21  ALA   A N   
541  C CA  A ALA   A 21  ? 0.1906 0.1800 0.2598 -0.0017 0.0643  0.0302  21  ALA   A CA  
542  C CA  B ALA   A 21  ? 0.1989 0.1975 0.2117 -0.0098 0.0463  -0.0048 21  ALA   A CA  
543  C C   A ALA   A 21  ? 0.1747 0.1794 0.2564 -0.0021 0.0626  0.0356  21  ALA   A C   
544  C C   B ALA   A 21  ? 0.1898 0.1960 0.2061 -0.0114 0.0572  0.0053  21  ALA   A C   
545  O O   A ALA   A 21  ? 0.1737 0.1910 0.2744 0.0043  0.0532  0.0380  21  ALA   A O   
546  O O   B ALA   A 21  ? 0.1855 0.1962 0.2157 -0.0086 0.0580  0.0052  21  ALA   A O   
547  C CB  A ALA   A 21  ? 0.2053 0.1817 0.2721 -0.0113 0.0544  0.0330  21  ALA   A CB  
548  C CB  B ALA   A 21  ? 0.2045 0.1949 0.2234 -0.0114 0.0406  -0.0082 21  ALA   A CB  
559  N N   A ASP   A 22  ? 0.1736 0.1713 0.2564 -0.0052 0.0560  0.0369  22  ASP   A N   
560  N N   B ASP   A 22  ? 0.1908 0.1943 0.2047 -0.0167 0.0625  0.0160  22  ASP   A N   
561  C CA  A ASP   A 22  ? 0.1744 0.1733 0.2375 -0.0021 0.0485  0.0349  22  ASP   A CA  
562  C CA  B ASP   A 22  ? 0.1926 0.1934 0.2099 -0.0172 0.0586  0.0163  22  ASP   A CA  
563  C C   A ASP   A 22  ? 0.1634 0.1778 0.1989 0.0000  0.0486  0.0259  22  ASP   A C   
564  C C   B ASP   A 22  ? 0.1834 0.1897 0.1941 -0.0206 0.0640  0.0039  22  ASP   A C   
565  O O   A ASP   A 22  ? 0.1700 0.1871 0.2043 -0.0029 0.0515  0.0148  22  ASP   A O   
566  O O   B ASP   A 22  ? 0.1827 0.1944 0.1978 -0.0242 0.0620  -0.0118 22  ASP   A O   
567  C CB  A ASP   A 22  ? 0.1931 0.1746 0.2842 -0.0074 0.0298  0.0372  22  ASP   A CB  
568  C CB  B ASP   A 22  ? 0.2057 0.1968 0.2432 -0.0113 0.0456  0.0167  22  ASP   A CB  
569  C CG  A ASP   A 22  ? 0.2155 0.1853 0.3395 -0.0090 0.0003  0.0443  22  ASP   A CG  
570  C CG  B ASP   A 22  ? 0.2146 0.1990 0.2709 -0.0117 0.0320  0.0172  22  ASP   A CG  
571  O OD1 A ASP   A 22  ? 0.2137 0.1846 0.3639 -0.0201 -0.0138 0.0492  22  ASP   A OD1 
572  O OD1 B ASP   A 22  ? 0.2180 0.1994 0.2800 -0.0126 0.0339  0.0106  22  ASP   A OD1 
573  O OD2 A ASP   A 22  ? 0.2411 0.1974 0.3783 -0.0018 0.0004  0.0358  22  ASP   A OD2 
574  O OD2 B ASP   A 22  ? 0.2170 0.2049 0.2913 -0.0139 0.0232  0.0168  22  ASP   A OD2 
583  N N   A ILE   A 23  ? 0.1633 0.1768 0.1871 -0.0009 0.0476  0.0209  23  ILE   A N   
584  N N   B ILE   A 23  ? 0.1796 0.1823 0.1867 -0.0205 0.0620  0.0032  23  ILE   A N   
585  C CA  A ILE   A 23  ? 0.1638 0.1649 0.1813 -0.0025 0.0412  0.0187  23  ILE   A CA  
586  C CA  B ILE   A 23  ? 0.1803 0.1811 0.1778 -0.0213 0.0498  0.0005  23  ILE   A CA  
587  C C   A ILE   A 23  ? 0.1648 0.1691 0.1805 -0.0027 0.0510  0.0107  23  ILE   A C   
588  C C   B ILE   A 23  ? 0.1854 0.1860 0.1810 -0.0319 0.0494  -0.0087 23  ILE   A C   
589  O O   A ILE   A 23  ? 0.1786 0.1722 0.1818 0.0009  0.0387  -0.0001 23  ILE   A O   
590  O O   B ILE   A 23  ? 0.1839 0.1777 0.1805 -0.0355 0.0430  -0.0151 23  ILE   A O   
591  C CB  A ILE   A 23  ? 0.1719 0.1613 0.1677 -0.0002 0.0367  0.0202  23  ILE   A CB  
592  C CB  B ILE   A 23  ? 0.1791 0.1750 0.1659 -0.0153 0.0384  0.0039  23  ILE   A CB  
593  C CG1 A ILE   A 23  ? 0.1754 0.1612 0.1656 0.0018  0.0288  0.0133  23  ILE   A CG1 
594  C CG1 B ILE   A 23  ? 0.1786 0.1710 0.1536 -0.0167 0.0272  0.0061  23  ILE   A CG1 
595  C CG2 A ILE   A 23  ? 0.1732 0.1649 0.1698 0.0006  0.0394  0.0286  23  ILE   A CG2 
596  C CG2 B ILE   A 23  ? 0.1785 0.1711 0.1673 -0.0133 0.0368  -0.0001 23  ILE   A CG2 
597  C CD1 A ILE   A 23  ? 0.1815 0.1674 0.1753 -0.0008 0.0193  0.0017  23  ILE   A CD1 
598  C CD1 B ILE   A 23  ? 0.1768 0.1696 0.1473 -0.0134 0.0151  0.0024  23  ILE   A CD1 
621  N N   A VAL   A 24  ? 0.1689 0.1742 0.1948 -0.0060 0.0560  0.0077  24  VAL   A N   
622  N N   B VAL   A 24  ? 0.1958 0.1985 0.1976 -0.0363 0.0468  -0.0122 24  VAL   A N   
623  C CA  A VAL   A 24  ? 0.1854 0.1868 0.2148 -0.0165 0.0539  0.0003  24  VAL   A CA  
624  C CA  B VAL   A 24  ? 0.2106 0.2105 0.2133 -0.0360 0.0449  -0.0125 24  VAL   A CA  
625  C C   A VAL   A 24  ? 0.1899 0.2014 0.2155 -0.0272 0.0428  -0.0060 24  VAL   A C   
626  C C   B VAL   A 24  ? 0.2181 0.2268 0.2199 -0.0395 0.0456  -0.0151 24  VAL   A C   
627  O O   A VAL   A 24  ? 0.2034 0.2081 0.2250 -0.0237 0.0429  -0.0078 24  VAL   A O   
628  O O   B VAL   A 24  ? 0.2258 0.2298 0.2313 -0.0367 0.0438  -0.0137 24  VAL   A O   
629  C CB  A VAL   A 24  ? 0.1961 0.1928 0.2381 -0.0130 0.0654  0.0021  24  VAL   A CB  
630  C CB  B VAL   A 24  ? 0.2157 0.2099 0.2227 -0.0310 0.0433  -0.0120 24  VAL   A CB  
631  C CG1 A VAL   A 24  ? 0.2008 0.2032 0.2494 -0.0087 0.0670  -0.0048 24  VAL   A CG1 
632  C CG1 B VAL   A 24  ? 0.2214 0.2130 0.2319 -0.0249 0.0415  -0.0113 24  VAL   A CG1 
633  C CG2 A VAL   A 24  ? 0.2091 0.2025 0.2485 -0.0111 0.0754  0.0185  24  VAL   A CG2 
634  C CG2 B VAL   A 24  ? 0.2152 0.2066 0.2163 -0.0317 0.0438  -0.0159 24  VAL   A CG2 
653  N N   A GLU   A 25  ? 0.1910 0.2218 0.2121 -0.0345 0.0503  -0.0125 25  GLU   A N   
654  N N   B GLU   A 25  ? 0.2188 0.2406 0.2179 -0.0425 0.0549  -0.0186 25  GLU   A N   
655  C CA  A GLU   A 25  ? 0.2134 0.2499 0.2100 -0.0268 0.0588  -0.0180 25  GLU   A CA  
656  C CA  B GLU   A 25  ? 0.2243 0.2517 0.2267 -0.0477 0.0519  -0.0205 25  GLU   A CA  
657  C C   A GLU   A 25  ? 0.2031 0.2525 0.1827 -0.0388 0.0673  -0.0196 25  GLU   A C   
658  C C   B GLU   A 25  ? 0.2242 0.2515 0.2165 -0.0512 0.0569  -0.0245 25  GLU   A C   
659  O O   A GLU   A 25  ? 0.2048 0.2631 0.2020 -0.0394 0.0589  -0.0227 25  GLU   A O   
660  O O   B GLU   A 25  ? 0.2269 0.2540 0.2185 -0.0503 0.0560  -0.0323 25  GLU   A O   
661  C CB  A GLU   A 25  ? 0.2408 0.2783 0.2424 -0.0147 0.0650  -0.0142 25  GLU   A CB  
662  C CB  B GLU   A 25  ? 0.2303 0.2621 0.2537 -0.0478 0.0456  -0.0189 25  GLU   A CB  
663  C CG  A GLU   A 25  ? 0.2716 0.3039 0.3057 -0.0111 0.0472  -0.0190 25  GLU   A CG  
664  C CG  B GLU   A 25  ? 0.2427 0.2735 0.2893 -0.0441 0.0363  -0.0188 25  GLU   A CG  
665  C CD  A GLU   A 25  ? 0.2919 0.3255 0.3605 -0.0084 0.0293  -0.0211 25  GLU   A CD  
666  C CD  B GLU   A 25  ? 0.2518 0.2812 0.3216 -0.0403 0.0259  -0.0162 25  GLU   A CD  
667  O OE1 A GLU   A 25  ? 0.3004 0.3354 0.3712 -0.0037 0.0170  -0.0271 25  GLU   A OE1 
668  O OE1 B GLU   A 25  ? 0.2566 0.2822 0.3372 -0.0417 0.0196  -0.0162 25  GLU   A OE1 
669  O OE2 A GLU   A 25  ? 0.2980 0.3321 0.3940 -0.0116 0.0238  -0.0258 25  GLU   A OE2 
670  O OE2 B GLU   A 25  ? 0.2536 0.2864 0.3324 -0.0349 0.0252  -0.0121 25  GLU   A OE2 
683  N N   A GLU   A 26  ? 0.1922 0.2468 0.1938 -0.0569 0.0686  -0.0243 26  GLU   A N   
684  N N   B GLU   A 26  ? 0.2209 0.2456 0.2053 -0.0566 0.0674  -0.0257 26  GLU   A N   
685  C CA  A GLU   A 26  ? 0.2043 0.2485 0.1763 -0.0692 0.0664  -0.0171 26  GLU   A CA  
686  C CA  B GLU   A 26  ? 0.2238 0.2391 0.2045 -0.0585 0.0706  -0.0230 26  GLU   A CA  
687  C C   A GLU   A 26  ? 0.2090 0.2351 0.1674 -0.0659 0.0624  -0.0115 26  GLU   A C   
688  C C   B GLU   A 26  ? 0.2168 0.2335 0.1882 -0.0604 0.0651  -0.0144 26  GLU   A C   
689  O O   A GLU   A 26  ? 0.2188 0.2267 0.1651 -0.0724 0.0606  -0.0152 26  GLU   A O   
690  O O   B GLU   A 26  ? 0.2234 0.2350 0.1833 -0.0553 0.0680  -0.0148 26  GLU   A O   
691  C CB  A GLU   A 26  ? 0.2244 0.2591 0.2026 -0.0843 0.0569  -0.0055 26  GLU   A CB  
692  C CB  B GLU   A 26  ? 0.2337 0.2332 0.2170 -0.0625 0.0746  -0.0317 26  GLU   A CB  
693  C CG  A GLU   A 26  ? 0.2548 0.2884 0.2746 -0.0875 0.0492  -0.0132 26  GLU   A CG  
694  C CG  B GLU   A 26  ? 0.2408 0.2193 0.2175 -0.0737 0.0900  -0.0406 26  GLU   A CG  
695  C CD  A GLU   A 26  ? 0.2726 0.3103 0.3195 -0.0985 0.0526  -0.0155 26  GLU   A CD  
696  C CD  B GLU   A 26  ? 0.2448 0.2012 0.2097 -0.0931 0.1065  -0.0513 26  GLU   A CD  
697  O OE1 A GLU   A 26  ? 0.2709 0.3340 0.3254 -0.0935 0.0558  -0.0327 26  GLU   A OE1 
698  O OE1 B GLU   A 26  ? 0.2422 0.1938 0.2229 -0.1052 0.1127  -0.0695 26  GLU   A OE1 
699  O OE2 A GLU   A 26  ? 0.3042 0.3193 0.3534 -0.0927 0.0427  -0.0120 26  GLU   A OE2 
700  O OE2 B GLU   A 26  ? 0.2531 0.1961 0.1822 -0.0857 0.1137  -0.0517 26  GLU   A OE2 
713  N N   . ALA   A 27  ? 0.2014 0.2281 0.1757 -0.0657 0.0592  -0.0065 27  ALA   A N   
714  C CA  . ALA   A 27  ? 0.2100 0.2436 0.1763 -0.0620 0.0507  -0.0092 27  ALA   A CA  
715  C C   . ALA   A 27  ? 0.2522 0.2734 0.1883 -0.0728 0.0551  -0.0226 27  ALA   A C   
716  O O   . ALA   A 27  ? 0.2544 0.2618 0.1900 -0.0824 0.0439  -0.0173 27  ALA   A O   
717  C CB  . ALA   A 27  ? 0.1863 0.2354 0.1818 -0.0611 0.0386  -0.0078 27  ALA   A CB  
724  N N   A LYS   A 28  ? 0.2798 0.2957 0.2059 -0.0723 0.0547  -0.0461 28  LYS   A N   
725  N N   B LYS   A 28  ? 0.2837 0.3012 0.2235 -0.0668 0.0483  -0.0257 28  LYS   A N   
726  C CA  A LYS   A 28  ? 0.3160 0.3293 0.2365 -0.0646 0.0581  -0.0591 28  LYS   A CA  
727  C CA  B LYS   A 28  ? 0.3173 0.3323 0.2660 -0.0589 0.0425  -0.0262 28  LYS   A CA  
728  C C   A LYS   A 28  ? 0.3318 0.3566 0.2255 -0.0705 0.0765  -0.0468 28  LYS   A C   
729  C C   B LYS   A 28  ? 0.3352 0.3530 0.2718 -0.0607 0.0470  -0.0205 28  LYS   A C   
730  O O   A LYS   A 28  ? 0.3380 0.3656 0.2607 -0.0690 0.0605  -0.0475 28  LYS   A O   
731  O O   B LYS   A 28  ? 0.3389 0.3575 0.2835 -0.0590 0.0418  -0.0218 28  LYS   A O   
732  C CB  A LYS   A 28  ? 0.3375 0.3416 0.2961 -0.0485 0.0450  -0.0712 28  LYS   A CB  
733  C CB  B LYS   A 28  ? 0.3324 0.3437 0.3064 -0.0494 0.0327  -0.0286 28  LYS   A CB  
734  C CG  A LYS   A 28  ? 0.3567 0.3523 0.3591 -0.0355 0.0356  -0.0768 28  LYS   A CG  
735  C CG  B LYS   A 28  ? 0.3464 0.3533 0.3471 -0.0412 0.0250  -0.0293 28  LYS   A CG  
736  C CD  A LYS   A 28  ? 0.3732 0.3671 0.4306 -0.0244 0.0247  -0.0751 28  LYS   A CD  
737  C CD  B LYS   A 28  ? 0.3586 0.3631 0.3896 -0.0343 0.0175  -0.0283 28  LYS   A CD  
738  C CE  A LYS   A 28  ? 0.3854 0.3777 0.4810 -0.0177 0.0177  -0.0774 28  LYS   A CE  
739  C CE  B LYS   A 28  ? 0.3676 0.3701 0.4194 -0.0303 0.0125  -0.0287 28  LYS   A CE  
740  N NZ  A LYS   A 28  ? 0.3939 0.3837 0.5129 -0.0127 0.0156  -0.0810 28  LYS   A NZ  
741  N NZ  B LYS   A 28  ? 0.3730 0.3739 0.4385 -0.0275 0.0107  -0.0300 28  LYS   A NZ  
768  N N   A LYS   A 29  ? 0.3374 0.3756 0.2152 -0.0789 0.1085  -0.0275 29  LYS   A N   
769  N N   B LYS   A 29  ? 0.3469 0.3683 0.2765 -0.0652 0.0571  -0.0120 29  LYS   A N   
770  C CA  A LYS   A 29  ? 0.3524 0.3989 0.2351 -0.0827 0.1214  -0.0094 29  LYS   A CA  
771  C CA  B LYS   A 29  ? 0.3593 0.3839 0.2893 -0.0694 0.0650  -0.0038 29  LYS   A CA  
772  C C   A LYS   A 29  ? 0.3571 0.3949 0.2194 -0.0898 0.1011  0.0004  29  LYS   A C   
773  C C   B LYS   A 29  ? 0.3573 0.3841 0.2528 -0.0835 0.0740  0.0033  29  LYS   A C   
774  O O   A LYS   A 29  ? 0.3689 0.4065 0.2311 -0.0827 0.0933  -0.0056 29  LYS   A O   
775  O O   B LYS   A 29  ? 0.3625 0.3886 0.2560 -0.0806 0.0724  0.0027  29  LYS   A O   
776  C CB  A LYS   A 29  ? 0.3645 0.4264 0.2852 -0.0729 0.1370  -0.0048 29  LYS   A CB  
777  C CB  B LYS   A 29  ? 0.3725 0.3985 0.3376 -0.0585 0.0608  -0.0027 29  LYS   A CB  
778  C CG  A LYS   A 29  ? 0.3815 0.4501 0.3474 -0.0619 0.1379  -0.0030 29  LYS   A CG  
779  C CG  B LYS   A 29  ? 0.3854 0.4109 0.3840 -0.0488 0.0561  -0.0016 29  LYS   A CG  
780  C CD  A LYS   A 29  ? 0.3977 0.4702 0.4145 -0.0520 0.1318  -0.0039 29  LYS   A CD  
781  C CD  B LYS   A 29  ? 0.3961 0.4213 0.4265 -0.0411 0.0518  -0.0005 29  LYS   A CD  
782  C CE  A LYS   A 29  ? 0.4091 0.4841 0.4613 -0.0453 0.1285  -0.0063 29  LYS   A CE  
783  C CE  B LYS   A 29  ? 0.4038 0.4286 0.4567 -0.0358 0.0493  -0.0008 29  LYS   A CE  
784  N NZ  A LYS   A 29  ? 0.4148 0.4918 0.4919 -0.0415 0.1251  -0.0087 29  LYS   A NZ  
785  N NZ  B LYS   A 29  ? 0.4077 0.4324 0.4748 -0.0331 0.0473  -0.0008 29  LYS   A NZ  
812  N N   . VAL   A 30  ? 0.3477 0.3787 0.2172 -0.1009 0.0863  0.0098  30  VAL   A N   
813  C CA  . VAL   A 30  ? 0.3404 0.3603 0.1931 -0.1201 0.0549  0.0298  30  VAL   A CA  
814  C C   . VAL   A 30  ? 0.3400 0.3466 0.1589 -0.1260 0.0374  0.0395  30  VAL   A C   
815  O O   . VAL   A 30  ? 0.3479 0.3500 0.1654 -0.1276 0.0307  0.0403  30  VAL   A O   
816  C CB  . VAL   A 30  ? 0.3371 0.3519 0.2295 -0.1307 0.0311  0.0324  30  VAL   A CB  
817  C CG1 . VAL   A 30  ? 0.3407 0.3474 0.2457 -0.1332 0.0175  0.0355  30  VAL   A CG1 
818  C CG2 . VAL   A 30  ? 0.3335 0.3530 0.2540 -0.1365 0.0297  0.0320  30  VAL   A CG2 
829  N N   . LYS   A 31  ? 0.3336 0.3299 0.1477 -0.1247 0.0106  0.0258  31  LYS   A N   
830  C CA  . LYS   A 31  ? 0.3440 0.3288 0.1647 -0.1080 -0.0096 0.0260  31  LYS   A CA  
831  C C   . LYS   A 31  ? 0.3179 0.3021 0.1258 -0.0868 -0.0140 0.0601  31  LYS   A C   
832  O O   . LYS   A 31  ? 0.3259 0.3151 0.1406 -0.0827 -0.0253 0.0714  31  LYS   A O   
833  C CB  . LYS   A 31  ? 0.3867 0.3605 0.2747 -0.1027 -0.0244 0.0019  31  LYS   A CB  
834  C CG  . LYS   A 31  ? 0.4320 0.3933 0.4031 -0.0915 -0.0417 -0.0145 31  LYS   A CG  
835  C CD  . LYS   A 31  ? 0.4693 0.4239 0.5023 -0.0816 -0.0585 -0.0296 31  LYS   A CD  
836  C CE  . LYS   A 31  ? 0.4948 0.4463 0.5663 -0.0739 -0.0698 -0.0403 31  LYS   A CE  
837  N NZ  . LYS   A 31  ? 0.5078 0.4543 0.6014 -0.0701 -0.0764 -0.0470 31  LYS   A NZ  
851  N N   . PRO   A 32  ? 0.2790 0.2637 0.1262 -0.0788 -0.0099 0.0415  32  PRO   A N   
852  C CA  . PRO   A 32  ? 0.2668 0.2457 0.1543 -0.0717 -0.0230 0.0505  32  PRO   A CA  
853  C C   . PRO   A 32  ? 0.2589 0.2379 0.1661 -0.0599 -0.0286 0.0602  32  PRO   A C   
854  O O   . PRO   A 32  ? 0.2516 0.2317 0.1760 -0.0606 -0.0407 0.0561  32  PRO   A O   
855  C CB  . PRO   A 32  ? 0.2597 0.2491 0.1705 -0.0691 -0.0209 0.0426  32  PRO   A CB  
856  C CG  . PRO   A 32  ? 0.2550 0.2497 0.1297 -0.0661 -0.0301 0.0294  32  PRO   A CG  
857  C CD  . PRO   A 32  ? 0.2608 0.2525 0.1213 -0.0712 -0.0176 0.0355  32  PRO   A CD  
865  N N   . THR   A 33  ? 0.2649 0.2347 0.1604 -0.0537 -0.0307 0.0572  33  THR   A N   
866  C CA  . THR   A 33  ? 0.2626 0.2371 0.1671 -0.0467 -0.0372 0.0557  33  THR   A CA  
867  C C   . THR   A 33  ? 0.2340 0.2194 0.1494 -0.0496 -0.0352 0.0424  33  THR   A C   
868  O O   . THR   A 33  ? 0.2326 0.2202 0.1672 -0.0469 -0.0502 0.0482  33  THR   A O   
869  C CB  . THR   A 33  ? 0.2876 0.2621 0.1877 -0.0361 -0.0453 0.0763  33  THR   A CB  
870  O OG1 . THR   A 33  ? 0.3093 0.2756 0.2057 -0.0234 -0.0397 0.0902  33  THR   A OG1 
871  C CG2 . THR   A 33  ? 0.2928 0.2739 0.2057 -0.0264 -0.0545 0.0765  33  THR   A CG2 
879  N N   . VAL   A 34  ? 0.2043 0.1987 0.1356 -0.0442 -0.0272 0.0394  34  VAL   A N   
880  C CA  . VAL   A 34  ? 0.1805 0.1799 0.1295 -0.0339 -0.0191 0.0371  34  VAL   A CA  
881  C C   . VAL   A 34  ? 0.1667 0.1668 0.1301 -0.0283 -0.0060 0.0271  34  VAL   A C   
882  O O   . VAL   A 34  ? 0.1700 0.1666 0.1610 -0.0330 -0.0068 0.0410  34  VAL   A O   
883  C CB  . VAL   A 34  ? 0.1826 0.1794 0.1566 -0.0282 -0.0068 0.0270  34  VAL   A CB  
884  C CG1 . VAL   A 34  ? 0.1871 0.1806 0.1663 -0.0243 0.0046  0.0167  34  VAL   A CG1 
885  C CG2 . VAL   A 34  ? 0.1864 0.1902 0.1765 -0.0224 -0.0158 0.0273  34  VAL   A CG2 
895  N N   . VAL   A 35  ? 0.1493 0.1587 0.1390 -0.0320 -0.0082 0.0277  35  VAL   A N   
896  C CA  . VAL   A 35  ? 0.1463 0.1556 0.1329 -0.0276 -0.0036 0.0220  35  VAL   A CA  
897  C C   . VAL   A 35  ? 0.1370 0.1435 0.1260 -0.0211 -0.0007 0.0215  35  VAL   A C   
898  O O   . VAL   A 35  ? 0.1304 0.1560 0.1552 -0.0251 0.0105  0.0163  35  VAL   A O   
899  C CB  . VAL   A 35  ? 0.1490 0.1609 0.1471 -0.0193 0.0105  0.0089  35  VAL   A CB  
900  C CG1 . VAL   A 35  ? 0.1554 0.1661 0.1618 -0.0134 0.0026  0.0014  35  VAL   A CG1 
901  C CG2 . VAL   A 35  ? 0.1443 0.1628 0.1792 -0.0110 0.0122  0.0046  35  VAL   A CG2 
911  N N   . VAL   A 36  ? 0.1232 0.1386 0.1289 -0.0208 0.0074  0.0250  36  VAL   A N   
912  C CA  . VAL   A 36  ? 0.1189 0.1281 0.1315 -0.0108 0.0048  0.0218  36  VAL   A CA  
913  C C   . VAL   A 36  ? 0.1175 0.1306 0.1398 -0.0145 0.0059  0.0154  36  VAL   A C   
914  O O   . VAL   A 36  ? 0.1219 0.1296 0.1657 -0.0084 0.0207  0.0196  36  VAL   A O   
915  C CB  . VAL   A 36  ? 0.1227 0.1229 0.1417 -0.0148 0.0038  0.0251  36  VAL   A CB  
916  C CG1 . VAL   A 36  ? 0.1315 0.1262 0.1587 -0.0168 0.0054  0.0090  36  VAL   A CG1 
917  C CG2 . VAL   A 36  ? 0.1402 0.1279 0.1612 -0.0101 -0.0042 0.0207  36  VAL   A CG2 
927  N N   . ASN   A 37  ? 0.1147 0.1208 0.1309 -0.0081 0.0021  0.0154  37  ASN   A N   
928  C CA  . ASN   A 37  ? 0.1133 0.1195 0.1266 -0.0014 0.0018  0.0189  37  ASN   A CA  
929  C C   . ASN   A 37  ? 0.1099 0.1174 0.1279 -0.0048 0.0095  0.0260  37  ASN   A C   
930  O O   . ASN   A 37  ? 0.1271 0.1249 0.1353 0.0044  0.0086  0.0089  37  ASN   A O   
931  C CB  . ASN   A 37  ? 0.1163 0.1175 0.1341 -0.0028 0.0058  0.0157  37  ASN   A CB  
932  C CG  . ASN   A 37  ? 0.1144 0.1170 0.1473 -0.0028 0.0040  0.0106  37  ASN   A CG  
933  O OD1 . ASN   A 37  ? 0.1177 0.1194 0.1685 -0.0008 0.0032  0.0131  37  ASN   A OD1 
934  N ND2 . ASN   A 37  ? 0.1199 0.1185 0.1606 -0.0044 -0.0017 0.0241  37  ASN   A ND2 
941  N N   A ALA   A 38  ? 0.1134 0.1262 0.1404 -0.0032 0.0109  0.0060  38  ALA   A N   
942  N N   B ALA   A 38  ? 0.1164 0.1266 0.1292 -0.0060 0.0023  0.0175  38  ALA   A N   
943  C CA  A ALA   A 38  ? 0.1215 0.1266 0.1358 -0.0041 0.0016  0.0044  38  ALA   A CA  
944  C CA  B ALA   A 38  ? 0.1240 0.1324 0.1310 -0.0078 -0.0065 0.0183  38  ALA   A CA  
945  C C   A ALA   A 38  ? 0.1204 0.1238 0.1395 -0.0037 -0.0035 -0.0019 38  ALA   A C   
946  C C   B ALA   A 38  ? 0.1207 0.1290 0.1373 -0.0093 -0.0118 0.0129  38  ALA   A C   
947  O O   A ALA   A 38  ? 0.1211 0.1153 0.1404 0.0009  -0.0121 -0.0067 38  ALA   A O   
948  O O   B ALA   A 38  ? 0.1091 0.1237 0.1379 -0.0133 -0.0206 0.0165  38  ALA   A O   
949  C CB  A ALA   A 38  ? 0.1215 0.1494 0.1562 -0.0183 0.0014  -0.0007 38  ALA   A CB  
950  C CB  B ALA   A 38  ? 0.1302 0.1438 0.1399 -0.0090 -0.0082 0.0108  38  ALA   A CB  
961  N N   A ALA   A 39  ? 0.1103 0.1164 0.1454 0.0023  0.0056  0.0090  39  ALA   A N   
962  N N   B ALA   A 39  ? 0.1251 0.1263 0.1441 -0.0074 -0.0075 0.0103  39  ALA   A N   
963  C CA  A ALA   A 39  ? 0.1166 0.1137 0.1382 0.0013  0.0102  -0.0065 39  ALA   A CA  
964  C CA  B ALA   A 39  ? 0.1362 0.1322 0.1427 -0.0062 -0.0004 0.0108  39  ALA   A CA  
965  C C   A ALA   A 39  ? 0.1171 0.1159 0.1456 0.0006  0.0025  -0.0031 39  ALA   A C   
966  C C   B ALA   A 39  ? 0.1329 0.1241 0.1225 -0.0070 0.0079  0.0096  39  ALA   A C   
967  O O   A ALA   A 39  ? 0.1288 0.1225 0.1417 -0.0064 0.0014  0.0050  39  ALA   A O   
968  O O   B ALA   A 39  ? 0.1373 0.1254 0.1100 -0.0116 0.0090  0.0153  39  ALA   A O   
969  C CB  A ALA   A 39  ? 0.1189 0.1223 0.1483 -0.0002 -0.0028 -0.0137 39  ALA   A CB  
970  C CB  B ALA   A 39  ? 0.1480 0.1446 0.1610 -0.0040 -0.0006 0.0040  39  ALA   A CB  
981  N N   A ASN   A 40  ? 0.1243 0.1218 0.1492 -0.0077 0.0159  0.0038  40  ASN   A N   
982  N N   B ASN   A 40  ? 0.1352 0.1190 0.1248 -0.0048 0.0173  0.0076  40  ASN   A N   
983  C CA  A ASN   A 40  ? 0.1265 0.1219 0.1529 -0.0031 0.0115  0.0056  40  ASN   A CA  
984  C CA  B ASN   A 40  ? 0.1364 0.1155 0.1351 0.0003  0.0104  0.0105  40  ASN   A CA  
985  C C   A ASN   A 40  ? 0.1256 0.1114 0.1332 -0.0083 0.0145  0.0127  40  ASN   A C   
986  C C   B ASN   A 40  ? 0.1341 0.1149 0.1308 0.0004  0.0081  0.0173  40  ASN   A C   
987  O O   A ASN   A 40  ? 0.1246 0.1210 0.1374 -0.0121 0.0151  0.0181  40  ASN   A O   
988  O O   B ASN   A 40  ? 0.1341 0.1190 0.1384 -0.0004 0.0093  0.0160  40  ASN   A O   
989  C CB  A ASN   A 40  ? 0.1356 0.1278 0.1600 0.0023  -0.0019 0.0074  40  ASN   A CB  
990  C CB  B ASN   A 40  ? 0.1449 0.1150 0.1553 0.0001  0.0122  0.0105  40  ASN   A CB  
991  C CG  A ASN   A 40  ? 0.1437 0.1368 0.1781 0.0031  0.0013  0.0097  40  ASN   A CG  
992  C CG  B ASN   A 40  ? 0.1519 0.1224 0.1839 -0.0035 0.0131  0.0075  40  ASN   A CG  
993  O OD1 A ASN   A 40  ? 0.1536 0.1377 0.2001 0.0029  -0.0045 0.0057  40  ASN   A OD1 
994  O OD1 B ASN   A 40  ? 0.1606 0.1257 0.2038 -0.0015 0.0035  -0.0007 40  ASN   A OD1 
995  N ND2 A ASN   A 40  ? 0.1466 0.1493 0.1700 0.0039  0.0105  -0.0007 40  ASN   A ND2 
996  N ND2 B ASN   A 40  ? 0.1472 0.1310 0.1859 -0.0124 0.0298  0.0051  40  ASN   A ND2 
1009 N N   A VAL   A 41  ? 0.1254 0.1181 0.1393 -0.0048 0.0173  0.0106  41  VAL   A N   
1010 N N   B VAL   A 41  ? 0.1341 0.1201 0.1260 0.0041  0.0042  0.0245  41  VAL   A N   
1011 C CA  A VAL   A 41  ? 0.1267 0.1217 0.1481 -0.0058 0.0186  0.0111  41  VAL   A CA  
1012 C CA  B VAL   A 41  ? 0.1330 0.1249 0.1307 0.0033  0.0115  0.0224  41  VAL   A CA  
1013 C C   A VAL   A 41  ? 0.1221 0.1206 0.1588 -0.0023 0.0108  0.0145  41  VAL   A C   
1014 C C   B VAL   A 41  ? 0.1349 0.1250 0.1303 -0.0023 0.0155  0.0213  41  VAL   A C   
1015 O O   A VAL   A 41  ? 0.1236 0.1188 0.1760 0.0019  -0.0009 0.0078  41  VAL   A O   
1016 O O   B VAL   A 41  ? 0.1381 0.1165 0.1228 -0.0040 0.0096  0.0217  41  VAL   A O   
1017 C CB  A VAL   A 41  ? 0.1304 0.1281 0.1408 -0.0027 0.0204  0.0093  41  VAL   A CB  
1018 C CB  B VAL   A 41  ? 0.1303 0.1347 0.1357 0.0060  0.0148  0.0256  41  VAL   A CB  
1019 C CG1 A VAL   A 41  ? 0.1428 0.1393 0.1577 0.0055  0.0081  0.0087  41  VAL   A CG1 
1020 C CG1 B VAL   A 41  ? 0.1374 0.1418 0.1421 0.0007  0.0262  0.0160  41  VAL   A CG1 
1021 C CG2 A VAL   A 41  ? 0.1373 0.1293 0.1319 -0.0067 0.0265  0.0066  41  VAL   A CG2 
1022 C CG2 B VAL   A 41  ? 0.1301 0.1400 0.1428 0.0073  -0.0027 0.0251  41  VAL   A CG2 
1041 N N   A TYR   A 42  ? 0.1162 0.1141 0.1664 -0.0036 0.0153  0.0232  42  TYR   A N   
1042 N N   B TYR   A 42  ? 0.1310 0.1274 0.1365 -0.0026 0.0146  0.0266  42  TYR   A N   
1043 C CA  A TYR   A 42  ? 0.1208 0.1121 0.1716 -0.0077 0.0217  0.0226  42  TYR   A CA  
1044 C CA  B TYR   A 42  ? 0.1333 0.1351 0.1393 0.0034  0.0157  0.0273  42  TYR   A CA  
1045 C C   A TYR   A 42  ? 0.1100 0.1085 0.1799 -0.0059 0.0179  0.0225  42  TYR   A C   
1046 C C   B TYR   A 42  ? 0.1335 0.1375 0.1281 0.0054  0.0127  0.0323  42  TYR   A C   
1047 O O   A TYR   A 42  ? 0.1169 0.1140 0.1962 -0.0189 0.0128  0.0030  42  TYR   A O   
1048 O O   B TYR   A 42  ? 0.1310 0.1419 0.1359 0.0030  0.0108  0.0275  42  TYR   A O   
1049 C CB  A TYR   A 42  ? 0.1406 0.1215 0.1689 -0.0116 0.0311  0.0307  42  TYR   A CB  
1050 C CB  B TYR   A 42  ? 0.1414 0.1387 0.1445 0.0102  0.0047  0.0286  42  TYR   A CB  
1051 C CG  A TYR   A 42  ? 0.1589 0.1342 0.1702 -0.0070 0.0176  0.0353  42  TYR   A CG  
1052 C CG  B TYR   A 42  ? 0.1531 0.1462 0.1505 0.0186  -0.0037 0.0289  42  TYR   A CG  
1053 C CD1 A TYR   A 42  ? 0.1693 0.1496 0.1774 -0.0141 0.0194  0.0236  42  TYR   A CD1 
1054 C CD1 B TYR   A 42  ? 0.1548 0.1483 0.1471 0.0188  -0.0046 0.0334  42  TYR   A CD1 
1055 C CD2 A TYR   A 42  ? 0.1732 0.1523 0.1841 -0.0001 0.0062  0.0283  42  TYR   A CD2 
1056 C CD2 B TYR   A 42  ? 0.1642 0.1577 0.1608 0.0224  -0.0036 0.0229  42  TYR   A CD2 
1057 C CE1 A TYR   A 42  ? 0.1815 0.1592 0.1703 -0.0163 0.0222  0.0210  42  TYR   A CE1 
1058 C CE1 B TYR   A 42  ? 0.1595 0.1552 0.1485 0.0161  -0.0076 0.0318  42  TYR   A CE1 
1059 C CE2 A TYR   A 42  ? 0.1884 0.1647 0.1906 -0.0096 0.0086  0.0309  42  TYR   A CE2 
1060 C CE2 B TYR   A 42  ? 0.1707 0.1657 0.1641 0.0209  -0.0035 0.0260  42  TYR   A CE2 
1061 C CZ  A TYR   A 42  ? 0.1951 0.1688 0.1787 -0.0175 0.0171  0.0259  42  TYR   A CZ  
1062 C CZ  B TYR   A 42  ? 0.1686 0.1655 0.1547 0.0156  -0.0039 0.0254  42  TYR   A CZ  
1063 O OH  A TYR   A 42  ? 0.2094 0.1837 0.1997 -0.0213 0.0084  0.0228  42  TYR   A OH  
1064 O OH  B TYR   A 42  ? 0.1718 0.1762 0.1626 0.0098  -0.0019 0.0172  42  TYR   A OH  
1083 N N   A LEU   A 43  ? 0.1188 0.1109 0.1707 -0.0090 0.0156  0.0048  43  LEU   A N   
1084 N N   B LEU   A 43  ? 0.1282 0.1367 0.1180 0.0077  0.0043  0.0281  43  LEU   A N   
1085 C CA  A LEU   A 43  ? 0.1127 0.1090 0.1725 -0.0111 0.0153  0.0008  43  LEU   A CA  
1086 C CA  B LEU   A 43  ? 0.1285 0.1362 0.1298 0.0042  0.0034  0.0240  43  LEU   A CA  
1087 C C   A LEU   A 43  ? 0.1134 0.1176 0.1731 -0.0017 0.0063  0.0006  43  LEU   A C   
1088 C C   B LEU   A 43  ? 0.1321 0.1405 0.1417 0.0031  -0.0012 0.0186  43  LEU   A C   
1089 O O   A LEU   A 43  ? 0.1331 0.1171 0.1952 -0.0011 -0.0075 -0.0014 43  LEU   A O   
1090 O O   B LEU   A 43  ? 0.1357 0.1410 0.1435 0.0001  -0.0097 0.0189  43  LEU   A O   
1091 C CB  A LEU   A 43  ? 0.1201 0.1065 0.1831 -0.0145 0.0133  0.0005  43  LEU   A CB  
1092 C CB  B LEU   A 43  ? 0.1264 0.1306 0.1383 0.0019  -0.0003 0.0225  43  LEU   A CB  
1093 C CG  A LEU   A 43  ? 0.1272 0.1120 0.1841 -0.0084 0.0064  0.0050  43  LEU   A CG  
1094 C CG  B LEU   A 43  ? 0.1240 0.1294 0.1459 0.0006  0.0010  0.0172  43  LEU   A CG  
1095 C CD1 A LEU   A 43  ? 0.1327 0.1231 0.2028 -0.0062 -0.0072 0.0098  43  LEU   A CD1 
1096 C CD1 B LEU   A 43  ? 0.1256 0.1320 0.1557 -0.0012 -0.0072 0.0164  43  LEU   A CD1 
1097 C CD2 A LEU   A 43  ? 0.1434 0.1189 0.1763 -0.0004 0.0050  0.0158  43  LEU   A CD2 
1098 C CD2 B LEU   A 43  ? 0.1299 0.1283 0.1451 0.0031  0.0031  0.0259  43  LEU   A CD2 
1121 N N   A LYS   A 44  ? 0.1225 0.1138 0.1636 -0.0054 0.0109  0.0105  44  LYS   A N   
1122 N N   B LYS   A 44  ? 0.1376 0.1412 0.1503 0.0019  -0.0028 0.0167  44  LYS   A N   
1123 C CA  A LYS   A 44  ? 0.1344 0.1129 0.1650 -0.0066 0.0148  0.0148  44  LYS   A CA  
1124 C CA  B LYS   A 44  ? 0.1462 0.1431 0.1597 0.0016  -0.0046 0.0143  44  LYS   A CA  
1125 C C   A LYS   A 44  ? 0.1246 0.1178 0.1519 0.0017  0.0036  0.0152  44  LYS   A C   
1126 C C   B LYS   A 44  ? 0.1333 0.1310 0.1494 0.0020  -0.0046 0.0135  44  LYS   A C   
1127 O O   A LYS   A 44  ? 0.1317 0.1355 0.1672 0.0010  -0.0010 -0.0004 44  LYS   A O   
1128 O O   B LYS   A 44  ? 0.1368 0.1378 0.1502 0.0013  -0.0044 0.0018  44  LYS   A O   
1129 C CB  A LYS   A 44  ? 0.1618 0.1276 0.2003 0.0001  0.0275  0.0282  44  LYS   A CB  
1130 C CB  B LYS   A 44  ? 0.1683 0.1637 0.1999 0.0056  -0.0017 0.0124  44  LYS   A CB  
1131 C CG  A LYS   A 44  ? 0.1930 0.1553 0.2696 -0.0059 0.0412  0.0455  44  LYS   A CG  
1132 C CG  B LYS   A 44  ? 0.1879 0.1876 0.2525 0.0059  0.0018  0.0131  44  LYS   A CG  
1133 C CD  A LYS   A 44  ? 0.2297 0.2087 0.3663 -0.0098 0.0330  0.0342  44  LYS   A CD  
1134 C CD  B LYS   A 44  ? 0.2091 0.2187 0.3060 -0.0003 -0.0047 0.0117  44  LYS   A CD  
1135 C CE  A LYS   A 44  ? 0.2489 0.2414 0.4297 -0.0121 0.0339  0.0288  44  LYS   A CE  
1136 C CE  B LYS   A 44  ? 0.2208 0.2389 0.3416 -0.0064 -0.0090 0.0138  44  LYS   A CE  
1137 N NZ  A LYS   A 44  ? 0.2559 0.2644 0.4610 -0.0129 0.0349  0.0255  44  LYS   A NZ  
1138 N NZ  B LYS   A 44  ? 0.2294 0.2526 0.3602 -0.0135 -0.0097 0.0143  44  LYS   A NZ  
1165 N N   . HIS   A 45  ? 0.1193 0.1173 0.1569 0.0007  -0.0039 0.0167  45  HIS   A N   
1166 C CA  . HIS   A 45  ? 0.1148 0.1204 0.1626 -0.0010 -0.0037 0.0120  45  HIS   A CA  
1167 C C   . HIS   A 45  ? 0.1230 0.1318 0.1724 0.0058  -0.0035 0.0129  45  HIS   A C   
1168 O O   . HIS   A 45  ? 0.1494 0.1467 0.1962 0.0231  -0.0093 -0.0018 45  HIS   A O   
1169 C CB  . HIS   A 45  ? 0.1197 0.1137 0.1619 -0.0017 -0.0024 0.0093  45  HIS   A CB  
1170 C CG  . HIS   A 45  ? 0.1165 0.1176 0.1493 -0.0073 0.0030  0.0120  45  HIS   A CG  
1171 N ND1 . HIS   A 45  ? 0.1103 0.1247 0.1607 -0.0069 -0.0022 0.0186  45  HIS   A ND1 
1172 C CD2 . HIS   A 45  ? 0.1212 0.1213 0.1474 -0.0139 -0.0089 0.0195  45  HIS   A CD2 
1173 C CE1 . HIS   A 45  ? 0.1163 0.1294 0.1369 -0.0103 -0.0064 0.0226  45  HIS   A CE1 
1174 N NE2 . HIS   A 45  ? 0.1188 0.1302 0.1437 -0.0061 -0.0021 0.0194  45  HIS   A NE2 
1183 N N   A GLY   A 46  ? 0.1367 0.1303 0.1937 0.0084  -0.0150 0.0162  46  GLY   A N   
1184 N N   B GLY   A 46  ? 0.1298 0.1368 0.1701 0.0125  -0.0119 0.0163  46  GLY   A N   
1185 C CA  A GLY   A 46  ? 0.1421 0.1356 0.2006 0.0069  -0.0114 0.0188  46  GLY   A CA  
1186 C CA  B GLY   A 46  ? 0.1372 0.1373 0.1671 0.0106  -0.0155 0.0243  46  GLY   A CA  
1187 C C   A GLY   A 46  ? 0.1404 0.1312 0.2060 0.0178  -0.0157 0.0271  46  GLY   A C   
1188 C C   B GLY   A 46  ? 0.1405 0.1287 0.1617 0.0104  -0.0251 0.0342  46  GLY   A C   
1189 O O   A GLY   A 46  ? 0.1398 0.1397 0.2274 0.0105  -0.0193 0.0182  46  GLY   A O   
1190 O O   B GLY   A 46  ? 0.1452 0.1234 0.1758 0.0087  -0.0262 0.0418  46  GLY   A O   
1197 N N   A GLY   A 47  ? 0.1494 0.1358 0.1945 0.0153  -0.0169 0.0062  47  GLY   A N   
1198 N N   B GLY   A 47  ? 0.1354 0.1266 0.1470 0.0078  -0.0312 0.0315  47  GLY   A N   
1199 C CA  A GLY   A 47  ? 0.1461 0.1410 0.1913 0.0162  -0.0377 -0.0092 47  GLY   A CA  
1200 C CA  B GLY   A 47  ? 0.1368 0.1309 0.1559 0.0078  -0.0395 0.0211  47  GLY   A CA  
1201 C C   A GLY   A 47  ? 0.1350 0.1317 0.1904 0.0158  -0.0431 -0.0104 47  GLY   A C   
1202 C C   B GLY   A 47  ? 0.1305 0.1349 0.1520 0.0071  -0.0379 0.0113  47  GLY   A C   
1203 O O   A GLY   A 47  ? 0.1305 0.1266 0.1936 0.0144  -0.0407 0.0039  47  GLY   A O   
1204 O O   B GLY   A 47  ? 0.1352 0.1337 0.1620 0.0094  -0.0328 0.0178  47  GLY   A O   
1211 N N   A GLY   A 48  ? 0.1323 0.1364 0.2076 0.0107  -0.0507 -0.0053 48  GLY   A N   
1212 N N   B GLY   A 48  ? 0.1266 0.1426 0.1617 0.0025  -0.0388 -0.0012 48  GLY   A N   
1213 C CA  A GLY   A 48  ? 0.1261 0.1274 0.2121 0.0059  -0.0354 -0.0118 48  GLY   A CA  
1214 C CA  B GLY   A 48  ? 0.1217 0.1414 0.1671 -0.0027 -0.0253 -0.0072 48  GLY   A CA  
1215 C C   A GLY   A 48  ? 0.1263 0.1281 0.1948 0.0033  -0.0105 -0.0098 48  GLY   A C   
1216 C C   B GLY   A 48  ? 0.1187 0.1398 0.1534 -0.0016 -0.0061 -0.0083 48  GLY   A C   
1217 O O   A GLY   A 48  ? 0.1468 0.1252 0.2097 0.0088  -0.0125 -0.0107 48  GLY   A O   
1218 O O   B GLY   A 48  ? 0.1323 0.1430 0.1595 -0.0049 -0.0098 -0.0170 48  GLY   A O   
1225 N N   A VAL   A 49  ? 0.1185 0.1236 0.1824 -0.0051 -0.0042 -0.0102 49  VAL   A N   
1226 N N   B VAL   A 49  ? 0.1095 0.1310 0.1488 -0.0039 0.0009  0.0006  49  VAL   A N   
1227 C CA  A VAL   A 49  ? 0.1357 0.1278 0.1660 -0.0081 0.0184  -0.0139 49  VAL   A CA  
1228 C CA  B VAL   A 49  ? 0.1079 0.1235 0.1410 -0.0073 0.0034  0.0041  49  VAL   A CA  
1229 C C   A VAL   A 49  ? 0.1309 0.1177 0.1421 -0.0014 0.0127  -0.0059 49  VAL   A C   
1230 C C   B VAL   A 49  ? 0.1057 0.1151 0.1322 -0.0056 0.0111  0.0055  49  VAL   A C   
1231 O O   A VAL   A 49  ? 0.1426 0.1249 0.1425 -0.0036 0.0136  -0.0055 49  VAL   A O   
1232 O O   B VAL   A 49  ? 0.1049 0.1074 0.1438 -0.0115 0.0114  -0.0035 49  VAL   A O   
1233 C CB  A VAL   A 49  ? 0.1585 0.1377 0.1708 -0.0156 0.0272  -0.0166 49  VAL   A CB  
1234 C CB  B VAL   A 49  ? 0.1066 0.1185 0.1328 -0.0027 0.0046  0.0023  49  VAL   A CB  
1235 C CG1 A VAL   A 49  ? 0.1684 0.1326 0.1669 -0.0098 0.0283  -0.0065 49  VAL   A CG1 
1236 C CG1 B VAL   A 49  ? 0.1046 0.1165 0.1382 0.0072  0.0072  0.0011  49  VAL   A CG1 
1237 C CG2 A VAL   A 49  ? 0.1725 0.1504 0.2150 -0.0312 0.0277  -0.0185 49  VAL   A CG2 
1238 C CG2 B VAL   A 49  ? 0.1099 0.1225 0.1295 -0.0062 0.0214  0.0008  49  VAL   A CG2 
1257 N N   A ALA   A 50  ? 0.1211 0.1141 0.1400 -0.0036 -0.0063 0.0056  50  ALA   A N   
1258 N N   B ALA   A 50  ? 0.1077 0.1175 0.1206 -0.0007 0.0058  0.0093  50  ALA   A N   
1259 C CA  A ALA   A 50  ? 0.1160 0.1137 0.1480 -0.0115 -0.0027 0.0127  50  ALA   A CA  
1260 C CA  B ALA   A 50  ? 0.1133 0.1215 0.1224 -0.0044 0.0016  0.0088  50  ALA   A CA  
1261 C C   A ALA   A 50  ? 0.1142 0.1154 0.1529 -0.0118 -0.0022 0.0036  50  ALA   A C   
1262 C C   B ALA   A 50  ? 0.1156 0.1237 0.1219 -0.0043 0.0010  0.0032  50  ALA   A C   
1263 O O   A ALA   A 50  ? 0.1140 0.1180 0.1651 -0.0048 -0.0010 0.0019  50  ALA   A O   
1264 O O   B ALA   A 50  ? 0.1157 0.1244 0.1233 -0.0010 0.0025  0.0038  50  ALA   A O   
1265 C CB  A ALA   A 50  ? 0.1125 0.1161 0.1449 -0.0111 0.0023  0.0014  50  ALA   A CB  
1266 C CB  B ALA   A 50  ? 0.1157 0.1228 0.1235 -0.0046 0.0052  -0.0009 50  ALA   A CB  
1277 N N   A GLY   A 51  ? 0.1179 0.1057 0.1624 0.0001  -0.0097 0.0043  51  GLY   A N   
1278 N N   B GLY   A 51  ? 0.1185 0.1224 0.1313 0.0005  -0.0054 -0.0006 51  GLY   A N   
1279 C CA  A GLY   A 51  ? 0.1336 0.1080 0.1727 0.0024  -0.0172 0.0046  51  GLY   A CA  
1280 C CA  B GLY   A 51  ? 0.1265 0.1249 0.1428 0.0013  -0.0110 -0.0046 51  GLY   A CA  
1281 C C   A GLY   A 51  ? 0.1175 0.1198 0.1713 0.0046  -0.0051 -0.0041 51  GLY   A C   
1282 C C   B GLY   A 51  ? 0.1189 0.1296 0.1492 0.0029  -0.0093 -0.0084 51  GLY   A C   
1283 O O   A GLY   A 51  ? 0.1258 0.1236 0.1831 0.0007  -0.0036 -0.0090 51  GLY   A O   
1284 O O   B GLY   A 51  ? 0.1211 0.1328 0.1470 0.0045  -0.0187 -0.0097 51  GLY   A O   
1291 N N   . ALA   A 52  ? 0.1151 0.1325 0.1606 -0.0006 -0.0004 -0.0153 52  ALA   A N   
1292 C CA  . ALA   A 52  ? 0.1154 0.1433 0.1693 -0.0036 0.0066  -0.0158 52  ALA   A CA  
1293 C C   . ALA   A 52  ? 0.1168 0.1374 0.1506 -0.0108 0.0110  -0.0090 52  ALA   A C   
1294 O O   . ALA   A 52  ? 0.1279 0.1490 0.1655 -0.0059 0.0061  -0.0150 52  ALA   A O   
1295 C CB  . ALA   A 52  ? 0.1265 0.1765 0.1886 -0.0120 0.0034  -0.0125 52  ALA   A CB  
1302 N N   A LEU   A 53  ? 0.1190 0.1378 0.1515 -0.0092 0.0074  -0.0056 53  LEU   A N   
1303 N N   B LEU   A 53  ? 0.1180 0.1353 0.1421 -0.0082 0.0073  -0.0024 53  LEU   A N   
1304 C CA  A LEU   A 53  ? 0.1383 0.1416 0.1456 -0.0036 0.0065  0.0022  53  LEU   A CA  
1305 C CA  B LEU   A 53  ? 0.1256 0.1335 0.1344 -0.0034 0.0056  0.0037  53  LEU   A CA  
1306 C C   A LEU   A 53  ? 0.1340 0.1443 0.1132 0.0029  0.0065  0.0065  53  LEU   A C   
1307 C C   B LEU   A 53  ? 0.1247 0.1367 0.1220 -0.0006 0.0045  0.0015  53  LEU   A C   
1308 O O   A LEU   A 53  ? 0.1463 0.1537 0.1271 -0.0081 0.0028  0.0075  53  LEU   A O   
1309 O O   B LEU   A 53  ? 0.1270 0.1420 0.1301 -0.0102 -0.0007 0.0008  53  LEU   A O   
1310 C CB  A LEU   A 53  ? 0.1495 0.1428 0.1508 -0.0098 0.0068  0.0031  53  LEU   A CB  
1311 C CB  B LEU   A 53  ? 0.1286 0.1269 0.1306 -0.0045 0.0046  0.0099  53  LEU   A CB  
1312 C CG  A LEU   A 53  ? 0.1693 0.1494 0.1641 -0.0169 0.0089  0.0015  53  LEU   A CG  
1313 C CG  B LEU   A 53  ? 0.1339 0.1218 0.1219 -0.0081 0.0011  0.0127  53  LEU   A CG  
1314 C CD1 A LEU   A 53  ? 0.1846 0.1571 0.1668 -0.0128 0.0089  0.0020  53  LEU   A CD1 
1315 C CD1 B LEU   A 53  ? 0.1452 0.1248 0.1336 -0.0041 -0.0002 0.0150  53  LEU   A CD1 
1316 C CD2 A LEU   A 53  ? 0.1739 0.1647 0.1711 -0.0174 0.0027  0.0047  53  LEU   A CD2 
1317 C CD2 B LEU   A 53  ? 0.1293 0.1187 0.1099 -0.0103 -0.0008 0.0142  53  LEU   A CD2 
1340 N N   . ASN   A 54  ? 0.1255 0.1339 0.1269 -0.0004 -0.0008 0.0033  54  ASN   A N   
1341 C CA  . ASN   A 54  ? 0.1170 0.1297 0.1416 -0.0037 -0.0061 0.0021  54  ASN   A CA  
1342 C C   . ASN   A 54  ? 0.1237 0.1283 0.1526 -0.0068 0.0019  -0.0040 54  ASN   A C   
1343 O O   . ASN   A 54  ? 0.1249 0.1409 0.1582 -0.0065 -0.0057 -0.0147 54  ASN   A O   
1344 C CB  . ASN   A 54  ? 0.1138 0.1295 0.1547 -0.0060 -0.0067 0.0010  54  ASN   A CB  
1345 C CG  . ASN   A 54  ? 0.1125 0.1294 0.1539 -0.0031 -0.0025 0.0014  54  ASN   A CG  
1346 O OD1 . ASN   A 54  ? 0.1153 0.1333 0.1576 -0.0022 -0.0103 0.0013  54  ASN   A OD1 
1347 N ND2 . ASN   A 54  ? 0.1231 0.1352 0.1753 -0.0133 -0.0101 0.0108  54  ASN   A ND2 
1355 N N   . LYS   A 55  ? 0.1198 0.1353 0.1544 -0.0049 -0.0052 -0.0135 55  LYS   A N   
1356 C CA  . LYS   A 55  ? 0.1283 0.1435 0.1658 0.0035  -0.0081 -0.0221 55  LYS   A CA  
1357 C C   . LYS   A 55  ? 0.1266 0.1488 0.1710 -0.0016 -0.0014 -0.0263 55  LYS   A C   
1358 O O   . LYS   A 55  ? 0.1400 0.1605 0.1734 0.0012  -0.0036 -0.0333 55  LYS   A O   
1359 C CB  . LYS   A 55  ? 0.1349 0.1482 0.1801 0.0138  -0.0029 -0.0268 55  LYS   A CB  
1360 C CG  . LYS   A 55  ? 0.1544 0.1813 0.1914 0.0234  -0.0136 -0.0265 55  LYS   A CG  
1361 C CD  . LYS   A 55  ? 0.1631 0.2058 0.1946 0.0363  -0.0105 -0.0240 55  LYS   A CD  
1362 C CE  . LYS   A 55  ? 0.1855 0.2338 0.2133 0.0490  -0.0142 -0.0256 55  LYS   A CE  
1363 N NZ  . LYS   A 55  ? 0.1957 0.2455 0.2252 0.0569  -0.0189 -0.0220 55  LYS   A NZ  
1377 N N   . ALA   A 56  ? 0.1349 0.1563 0.1691 -0.0086 0.0047  -0.0255 56  ALA   A N   
1378 C CA  . ALA   A 56  ? 0.1464 0.1768 0.1643 -0.0139 0.0159  -0.0202 56  ALA   A CA  
1379 C C   . ALA   A 56  ? 0.1500 0.1870 0.1388 -0.0116 0.0159  -0.0187 56  ALA   A C   
1380 O O   . ALA   A 56  ? 0.1552 0.2204 0.1521 0.0030  0.0152  -0.0146 56  ALA   A O   
1381 C CB  . ALA   A 56  ? 0.1527 0.1983 0.1745 -0.0188 0.0159  -0.0139 56  ALA   A CB  
1387 N N   . THR   A 57  ? 0.1376 0.1660 0.1402 -0.0104 0.0075  -0.0204 57  THR   A N   
1388 C CA  . THR   A 57  ? 0.1441 0.1599 0.1436 -0.0116 0.0002  -0.0104 57  THR   A CA  
1389 C C   . THR   A 57  ? 0.1440 0.1709 0.1535 -0.0050 -0.0038 -0.0184 57  THR   A C   
1390 O O   . THR   A 57  ? 0.1376 0.1763 0.1693 -0.0111 -0.0165 -0.0274 57  THR   A O   
1391 C CB  . THR   A 57  ? 0.1369 0.1603 0.1429 -0.0111 0.0011  -0.0094 57  THR   A CB  
1392 O OG1 . THR   A 57  ? 0.1284 0.1563 0.1494 -0.0068 0.0009  -0.0072 57  THR   A OG1 
1393 C CG2 . THR   A 57  ? 0.1433 0.1628 0.1288 -0.0058 0.0004  -0.0015 57  THR   A CG2 
1401 N N   . ASN   A 58  ? 0.1432 0.1691 0.1769 -0.0065 0.0027  -0.0334 58  ASN   A N   
1402 C CA  . ASN   A 58  ? 0.1631 0.1585 0.1974 -0.0142 0.0108  -0.0388 58  ASN   A CA  
1403 C C   . ASN   A 58  ? 0.1433 0.1440 0.1922 -0.0031 -0.0029 -0.0253 58  ASN   A C   
1404 O O   . ASN   A 58  ? 0.1463 0.1576 0.2011 -0.0116 -0.0034 -0.0309 58  ASN   A O   
1405 C CB  . ASN   A 58  ? 0.2114 0.1747 0.2358 -0.0212 0.0326  -0.0588 58  ASN   A CB  
1406 C CG  . ASN   A 58  ? 0.2583 0.1993 0.3092 -0.0214 0.0392  -0.0484 58  ASN   A CG  
1407 O OD1 . ASN   A 58  ? 0.2847 0.1936 0.3459 0.0092  0.0740  -0.0330 58  ASN   A OD1 
1408 N ND2 . ASN   A 58  ? 0.2707 0.2134 0.3389 -0.0267 0.0286  -0.0530 58  ASN   A ND2 
1415 N N   . ASN   A 59  ? 0.1272 0.1372 0.1754 -0.0089 -0.0139 -0.0133 59  ASN   A N   
1416 C CA  . ASN   A 59  ? 0.1222 0.1307 0.1721 -0.0061 -0.0080 -0.0089 59  ASN   A CA  
1417 C C   . ASN   A 59  ? 0.1248 0.1326 0.1553 -0.0036 -0.0084 -0.0103 59  ASN   A C   
1418 O O   . ASN   A 59  ? 0.1268 0.1312 0.1637 -0.0098 0.0014  -0.0016 59  ASN   A O   
1419 C CB  . ASN   A 59  ? 0.1289 0.1297 0.1786 -0.0014 -0.0159 -0.0130 59  ASN   A CB  
1420 C CG  . ASN   A 59  ? 0.1342 0.1368 0.1751 -0.0039 -0.0256 0.0041  59  ASN   A CG  
1421 O OD1 . ASN   A 59  ? 0.1478 0.1403 0.1665 -0.0119 -0.0192 0.0044  59  ASN   A OD1 
1422 N ND2 . ASN   A 59  ? 0.1448 0.1383 0.1884 -0.0142 -0.0156 -0.0002 59  ASN   A ND2 
1429 N N   . ALA   A 60  ? 0.1250 0.1374 0.1529 -0.0030 -0.0049 -0.0030 60  ALA   A N   
1430 C CA  . ALA   A 60  ? 0.1217 0.1378 0.1664 -0.0053 -0.0151 -0.0013 60  ALA   A CA  
1431 C C   . ALA   A 60  ? 0.1215 0.1310 0.1717 -0.0030 -0.0085 -0.0022 60  ALA   A C   
1432 O O   . ALA   A 60  ? 0.1159 0.1341 0.1897 -0.0037 -0.0113 -0.0058 60  ALA   A O   
1433 C CB  . ALA   A 60  ? 0.1322 0.1525 0.1779 -0.0049 -0.0146 -0.0181 60  ALA   A CB  
1439 N N   . MET   A 61  ? 0.1184 0.1299 0.1626 -0.0052 -0.0055 -0.0079 61  MET   A N   
1440 C CA  . MET   A 61  ? 0.1184 0.1261 0.1575 -0.0088 -0.0019 0.0009  61  MET   A CA  
1441 C C   . MET   A 61  ? 0.1152 0.1200 0.1610 -0.0081 -0.0081 -0.0023 61  MET   A C   
1442 O O   . MET   A 61  ? 0.1209 0.1219 0.1671 -0.0075 0.0045  0.0013  61  MET   A O   
1443 C CB  . MET   A 61  ? 0.1254 0.1276 0.1415 -0.0079 0.0002  -0.0029 61  MET   A CB  
1444 C CG  . MET   A 61  ? 0.1269 0.1353 0.1609 -0.0031 0.0013  0.0013  61  MET   A CG  
1445 S SD  . MET   A 61  ? 0.1292 0.1337 0.1893 -0.0109 -0.0012 -0.0161 61  MET   A SD  
1446 C CE  . MET   A 61  ? 0.1505 0.1473 0.2108 -0.0108 0.0213  -0.0123 61  MET   A CE  
1456 N N   . GLN   A 62  ? 0.1196 0.1186 0.1628 -0.0099 -0.0058 -0.0045 62  GLN   A N   
1457 C CA  . GLN   A 62  ? 0.1171 0.1165 0.1687 -0.0022 0.0001  0.0030  62  GLN   A CA  
1458 C C   . GLN   A 62  ? 0.1189 0.1086 0.1743 -0.0018 0.0062  0.0004  62  GLN   A C   
1459 O O   . GLN   A 62  ? 0.1218 0.1243 0.1666 -0.0038 0.0021  -0.0016 62  GLN   A O   
1460 C CB  . GLN   A 62  ? 0.1193 0.1161 0.1771 -0.0063 0.0036  0.0052  62  GLN   A CB  
1461 C CG  . GLN   A 62  ? 0.1262 0.1143 0.1690 -0.0073 -0.0007 0.0149  62  GLN   A CG  
1462 C CD  . GLN   A 62  ? 0.1304 0.1188 0.1724 -0.0033 0.0061  0.0108  62  GLN   A CD  
1463 O OE1 . GLN   A 62  ? 0.1343 0.1312 0.1797 -0.0038 0.0006  0.0009  62  GLN   A OE1 
1464 N NE2 . GLN   A 62  ? 0.1352 0.1262 0.1730 0.0013  -0.0019 -0.0071 62  GLN   A NE2 
1473 N N   . VAL   A 63  ? 0.1164 0.1157 0.1888 -0.0074 0.0063  -0.0178 63  VAL   A N   
1474 C CA  . VAL   A 63  ? 0.1195 0.1252 0.2094 -0.0134 -0.0002 -0.0149 63  VAL   A CA  
1475 C C   . VAL   A 63  ? 0.1066 0.1275 0.1927 -0.0127 -0.0097 -0.0138 63  VAL   A C   
1476 O O   . VAL   A 63  ? 0.1106 0.1282 0.2102 -0.0143 -0.0067 -0.0064 63  VAL   A O   
1477 C CB  . VAL   A 63  ? 0.1318 0.1466 0.2339 -0.0137 0.0002  -0.0381 63  VAL   A CB  
1478 C CG1 . VAL   A 63  ? 0.1460 0.1647 0.2626 -0.0158 -0.0073 -0.0578 63  VAL   A CG1 
1479 C CG2 . VAL   A 63  ? 0.1409 0.1432 0.2432 -0.0157 0.0121  -0.0350 63  VAL   A CG2 
1489 N N   . GLU   A 64  ? 0.1142 0.1319 0.1782 -0.0039 -0.0063 -0.0085 64  GLU   A N   
1490 C CA  . GLU   A 64  ? 0.1144 0.1306 0.1840 -0.0076 -0.0078 0.0002  64  GLU   A CA  
1491 C C   . GLU   A 64  ? 0.1103 0.1214 0.1861 -0.0069 -0.0004 0.0037  64  GLU   A C   
1492 O O   . GLU   A 64  ? 0.1167 0.1302 0.1881 -0.0023 -0.0017 -0.0026 64  GLU   A O   
1493 C CB  . GLU   A 64  ? 0.1236 0.1393 0.1808 -0.0102 -0.0018 -0.0073 64  GLU   A CB  
1494 C CG  . GLU   A 64  ? 0.1370 0.1474 0.1885 -0.0124 -0.0035 -0.0001 64  GLU   A CG  
1495 C CD  . GLU   A 64  ? 0.1454 0.1550 0.1954 -0.0170 0.0054  -0.0026 64  GLU   A CD  
1496 O OE1 . GLU   A 64  ? 0.1430 0.1665 0.2137 -0.0238 0.0144  -0.0009 64  GLU   A OE1 
1497 O OE2 . GLU   A 64  ? 0.1635 0.1559 0.1894 -0.0239 -0.0063 0.0075  64  GLU   A OE2 
1504 N N   . SER   A 65  ? 0.1065 0.1259 0.1739 0.0027  0.0000  0.0038  65  SER   A N   
1505 C CA  . SER   A 65  ? 0.1184 0.1194 0.1699 -0.0044 -0.0066 -0.0019 65  SER   A CA  
1506 C C   . SER   A 65  ? 0.1147 0.1287 0.1660 -0.0073 -0.0026 -0.0019 65  SER   A C   
1507 O O   . SER   A 65  ? 0.1270 0.1292 0.1836 -0.0011 0.0085  -0.0055 65  SER   A O   
1508 C CB  . SER   A 65  ? 0.1178 0.1211 0.1670 -0.0103 0.0004  0.0078  65  SER   A CB  
1509 O OG  . SER   A 65  ? 0.1154 0.1384 0.1774 -0.0107 -0.0087 0.0131  65  SER   A OG  
1515 N N   . ASP   A 66  ? 0.1167 0.1231 0.1750 -0.0047 0.0129  0.0037  66  ASP   A N   
1516 C CA  . ASP   A 66  ? 0.1303 0.1369 0.1902 -0.0033 0.0097  0.0169  66  ASP   A CA  
1517 C C   . ASP   A 66  ? 0.1287 0.1320 0.1835 -0.0055 0.0094  0.0122  66  ASP   A C   
1518 O O   . ASP   A 66  ? 0.1343 0.1410 0.2054 -0.0034 0.0219  0.0156  66  ASP   A O   
1519 C CB  . ASP   A 66  ? 0.1360 0.1458 0.2211 0.0031  0.0165  0.0333  66  ASP   A CB  
1520 C CG  . ASP   A 66  ? 0.1639 0.1563 0.2504 -0.0032 0.0053  0.0482  66  ASP   A CG  
1521 O OD1 . ASP   A 66  ? 0.1615 0.1832 0.2332 -0.0085 -0.0064 0.0538  66  ASP   A OD1 
1522 O OD2 . ASP   A 66  ? 0.1826 0.1706 0.3235 0.0201  -0.0157 0.0289  66  ASP   A OD2 
1527 N N   . ASP   A 67  ? 0.1188 0.1383 0.1937 -0.0059 0.0130  0.0167  67  ASP   A N   
1528 C CA  . ASP   A 67  ? 0.1177 0.1488 0.2116 -0.0049 0.0047  0.0181  67  ASP   A CA  
1529 C C   . ASP   A 67  ? 0.1225 0.1489 0.2181 0.0002  0.0075  0.0242  67  ASP   A C   
1530 O O   . ASP   A 67  ? 0.1186 0.1537 0.2337 0.0023  0.0215  0.0299  67  ASP   A O   
1531 C CB  . ASP   A 67  ? 0.1305 0.1599 0.2481 -0.0091 -0.0114 0.0246  67  ASP   A CB  
1532 C CG  . ASP   A 67  ? 0.1263 0.1731 0.2800 -0.0105 -0.0276 0.0389  67  ASP   A CG  
1533 O OD1 . ASP   A 67  ? 0.1323 0.1928 0.3521 -0.0145 -0.0359 0.0513  67  ASP   A OD1 
1534 O OD2 . ASP   A 67  ? 0.1312 0.1772 0.2713 0.0047  -0.0191 0.0274  67  ASP   A OD2 
1539 N N   . TYR   A 68  ? 0.1238 0.1348 0.2119 -0.0004 0.0136  0.0276  68  TYR   A N   
1540 C CA  . TYR   A 68  ? 0.1310 0.1378 0.2064 0.0017  0.0197  0.0280  68  TYR   A CA  
1541 C C   . TYR   A 68  ? 0.1218 0.1348 0.2035 -0.0021 0.0241  0.0182  68  TYR   A C   
1542 O O   . TYR   A 68  ? 0.1282 0.1379 0.2143 0.0081  0.0263  0.0183  68  TYR   A O   
1543 C CB  . TYR   A 68  ? 0.1326 0.1347 0.2233 0.0077  0.0440  0.0323  68  TYR   A CB  
1544 C CG  . TYR   A 68  ? 0.1410 0.1513 0.2593 0.0042  0.0542  0.0326  68  TYR   A CG  
1545 C CD1 . TYR   A 68  ? 0.1537 0.1596 0.2948 -0.0186 0.0435  -0.0106 68  TYR   A CD1 
1546 C CD2 . TYR   A 68  ? 0.1645 0.1546 0.2951 0.0134  0.0534  0.0390  68  TYR   A CD2 
1547 C CE1 . TYR   A 68  ? 0.1636 0.1649 0.3272 -0.0201 0.0506  -0.0193 68  TYR   A CE1 
1548 C CE2 . TYR   A 68  ? 0.1630 0.1575 0.3174 0.0016  0.0656  0.0139  68  TYR   A CE2 
1549 C CZ  . TYR   A 68  ? 0.1676 0.1590 0.3318 -0.0188 0.0533  -0.0177 68  TYR   A CZ  
1550 O OH  . TYR   A 68  ? 0.1975 0.1573 0.3451 -0.0087 0.0286  -0.0351 68  TYR   A OH  
1560 N N   . ILE   A 69  ? 0.1193 0.1265 0.1939 -0.0021 0.0218  0.0169  69  ILE   A N   
1561 C CA  . ILE   A 69  ? 0.1279 0.1339 0.1823 0.0031  0.0133  0.0079  69  ILE   A CA  
1562 C C   . ILE   A 69  ? 0.1271 0.1344 0.1849 0.0041  0.0194  0.0202  69  ILE   A C   
1563 O O   . ILE   A 69  ? 0.1362 0.1403 0.1882 -0.0031 0.0224  0.0238  69  ILE   A O   
1564 C CB  . ILE   A 69  ? 0.1332 0.1581 0.1961 0.0039  0.0134  0.0053  69  ILE   A CB  
1565 C CG1 . ILE   A 69  ? 0.1344 0.1641 0.2016 0.0075  0.0146  -0.0124 69  ILE   A CG1 
1566 C CG2 . ILE   A 69  ? 0.1561 0.1764 0.2162 0.0130  -0.0033 -0.0094 69  ILE   A CG2 
1567 C CD1 . ILE   A 69  ? 0.1380 0.1754 0.2253 -0.0035 0.0115  -0.0180 69  ILE   A CD1 
1579 N N   . ALA   A 70  ? 0.1355 0.1345 0.1928 -0.0043 0.0195  0.0198  70  ALA   A N   
1580 C CA  . ALA   A 70  ? 0.1396 0.1448 0.2124 -0.0146 0.0293  0.0216  70  ALA   A CA  
1581 C C   . ALA   A 70  ? 0.1390 0.1565 0.2074 -0.0129 0.0271  0.0190  70  ALA   A C   
1582 O O   . ALA   A 70  ? 0.1557 0.1945 0.2304 0.0071  0.0453  0.0379  70  ALA   A O   
1583 C CB  . ALA   A 70  ? 0.1448 0.1372 0.2358 -0.0158 0.0249  0.0168  70  ALA   A CB  
1589 N N   . THR   A 71  ? 0.1315 0.1538 0.2061 -0.0050 0.0223  0.0195  71  THR   A N   
1590 C CA  . THR   A 71  ? 0.1420 0.1735 0.2284 0.0071  0.0183  0.0214  71  THR   A CA  
1591 C C   . THR   A 71  ? 0.1325 0.1659 0.2438 0.0151  0.0288  0.0214  71  THR   A C   
1592 O O   . THR   A 71  ? 0.1397 0.1957 0.2859 0.0118  0.0405  -0.0037 71  THR   A O   
1593 C CB  . THR   A 71  ? 0.1702 0.1992 0.2484 0.0154  -0.0134 0.0309  71  THR   A CB  
1594 O OG1 . THR   A 71  ? 0.1970 0.2173 0.2526 0.0076  -0.0301 0.0197  71  THR   A OG1 
1595 C CG2 . THR   A 71  ? 0.1841 0.2132 0.2712 0.0237  -0.0219 0.0451  71  THR   A CG2 
1603 N N   . ASN   A 72  ? 0.1365 0.1518 0.2292 0.0086  0.0288  0.0252  72  ASN   A N   
1604 C CA  . ASN   A 72  ? 0.1404 0.1514 0.2279 0.0118  0.0315  0.0205  72  ASN   A CA  
1605 C C   . ASN   A 72  ? 0.1525 0.1499 0.2287 0.0037  0.0443  0.0164  72  ASN   A C   
1606 O O   . ASN   A 72  ? 0.1717 0.1511 0.2587 0.0092  0.0422  0.0042  72  ASN   A O   
1607 C CB  . ASN   A 72  ? 0.1622 0.1553 0.2272 0.0096  0.0314  0.0208  72  ASN   A CB  
1608 C CG  . ASN   A 72  ? 0.1851 0.1676 0.2331 0.0200  0.0297  0.0306  72  ASN   A CG  
1609 O OD1 . ASN   A 72  ? 0.2029 0.2062 0.2474 0.0246  0.0338  0.0313  72  ASN   A OD1 
1610 N ND2 . ASN   A 72  ? 0.1985 0.1670 0.2400 0.0443  0.0174  0.0217  72  ASN   A ND2 
1617 N N   . GLY   A 73  ? 0.1492 0.1503 0.2132 0.0018  0.0397  0.0127  73  GLY   A N   
1618 C CA  . GLY   A 73  ? 0.1570 0.1491 0.1967 -0.0091 0.0357  0.0092  73  GLY   A CA  
1619 C C   . GLY   A 73  ? 0.1583 0.1372 0.1847 -0.0014 0.0444  0.0254  73  GLY   A C   
1620 O O   . GLY   A 73  ? 0.1549 0.1441 0.2048 0.0115  0.0377  0.0274  73  GLY   A O   
1624 N N   . PRO   A 74  ? 0.1637 0.1397 0.1941 -0.0165 0.0462  0.0176  74  PRO   A N   
1625 C CA  . PRO   A 74  ? 0.1613 0.1374 0.2052 -0.0025 0.0388  0.0183  74  PRO   A CA  
1626 C C   . PRO   A 74  ? 0.1527 0.1270 0.2017 -0.0022 0.0270  0.0049  74  PRO   A C   
1627 O O   . PRO   A 74  ? 0.1622 0.1319 0.2196 0.0035  0.0325  -0.0066 74  PRO   A O   
1628 C CB  . PRO   A 74  ? 0.1776 0.1687 0.2246 -0.0004 0.0428  0.0257  74  PRO   A CB  
1629 C CG  . PRO   A 74  ? 0.2021 0.2012 0.2580 -0.0176 0.0310  0.0132  74  PRO   A CG  
1630 C CD  . PRO   A 74  ? 0.1842 0.1747 0.2097 -0.0236 0.0336  0.0081  74  PRO   A CD  
1638 N N   . LEU   A 75  ? 0.1499 0.1176 0.1799 -0.0012 0.0195  0.0023  75  LEU   A N   
1639 C CA  . LEU   A 75  ? 0.1527 0.1170 0.1650 0.0011  0.0086  0.0093  75  LEU   A CA  
1640 C C   . LEU   A 75  ? 0.1630 0.1301 0.1663 0.0052  0.0115  0.0166  75  LEU   A C   
1641 O O   . LEU   A 75  ? 0.1943 0.1470 0.1648 0.0126  0.0059  0.0071  75  LEU   A O   
1642 C CB  . LEU   A 75  ? 0.1599 0.1261 0.1602 -0.0135 0.0137  0.0210  75  LEU   A CB  
1643 C CG  . LEU   A 75  ? 0.1794 0.1619 0.1677 -0.0390 0.0078  0.0134  75  LEU   A CG  
1644 C CD1 . LEU   A 75  ? 0.1942 0.2117 0.1798 -0.0384 0.0100  -0.0017 75  LEU   A CD1 
1645 C CD2 . LEU   A 75  ? 0.2062 0.2053 0.2243 -0.0154 0.0034  0.0127  75  LEU   A CD2 
1657 N N   . LYS   A 76  ? 0.1658 0.1292 0.1829 -0.0075 0.0094  0.0011  76  LYS   A N   
1658 C CA  . LYS   A 76  ? 0.1638 0.1472 0.1858 -0.0093 0.0143  -0.0141 76  LYS   A CA  
1659 C C   . LYS   A 76  ? 0.1569 0.1300 0.1575 -0.0039 0.0107  0.0057  76  LYS   A C   
1660 O O   . LYS   A 76  ? 0.1620 0.1260 0.1607 -0.0012 0.0179  0.0103  76  LYS   A O   
1661 C CB  . LYS   A 76  ? 0.1621 0.1723 0.2294 0.0026  0.0139  -0.0355 76  LYS   A CB  
1662 C CG  . LYS   A 76  ? 0.1746 0.1680 0.2680 0.0086  0.0096  -0.0335 76  LYS   A CG  
1663 C CD  . LYS   A 76  ? 0.1803 0.1713 0.3109 0.0102  -0.0048 -0.0400 76  LYS   A CD  
1664 C CE  . LYS   A 76  ? 0.2008 0.1921 0.3614 0.0048  -0.0015 -0.0489 76  LYS   A CE  
1665 N NZ  . LYS   A 76  ? 0.2003 0.1846 0.3947 -0.0104 -0.0029 -0.0581 76  LYS   A NZ  
1679 N N   . VAL   A 77  ? 0.1684 0.1371 0.1511 -0.0037 0.0234  0.0135  77  VAL   A N   
1680 C CA  . VAL   A 77  ? 0.1631 0.1435 0.1543 0.0037  0.0183  0.0089  77  VAL   A CA  
1681 C C   . VAL   A 77  ? 0.1566 0.1359 0.1584 0.0033  0.0136  0.0009  77  VAL   A C   
1682 O O   . VAL   A 77  ? 0.1683 0.1410 0.1557 0.0071  0.0257  -0.0069 77  VAL   A O   
1683 C CB  . VAL   A 77  ? 0.1810 0.1617 0.1582 -0.0014 0.0084  0.0122  77  VAL   A CB  
1684 C CG1 . VAL   A 77  ? 0.1767 0.1775 0.1724 0.0060  -0.0004 0.0024  77  VAL   A CG1 
1685 C CG2 . VAL   A 77  ? 0.2032 0.1723 0.1870 -0.0057 -0.0014 0.0189  77  VAL   A CG2 
1695 N N   . GLY   A 78  ? 0.1507 0.1336 0.1543 0.0011  0.0216  0.0039  78  GLY   A N   
1696 C CA  . GLY   A 78  ? 0.1507 0.1283 0.1620 -0.0003 0.0291  0.0101  78  GLY   A CA  
1697 C C   . GLY   A 78  ? 0.1402 0.1227 0.1616 0.0017  0.0225  0.0095  78  GLY   A C   
1698 O O   . GLY   A 78  ? 0.1382 0.1329 0.1900 -0.0005 0.0178  0.0225  78  GLY   A O   
1702 N N   . GLY   A 79  ? 0.1451 0.1245 0.1576 0.0016  0.0169  0.0128  79  GLY   A N   
1703 C CA  . GLY   A 79  ? 0.1425 0.1268 0.1738 0.0017  0.0199  0.0120  79  GLY   A CA  
1704 C C   . GLY   A 79  ? 0.1303 0.1229 0.1669 -0.0011 0.0103  0.0082  79  GLY   A C   
1705 O O   . GLY   A 79  ? 0.1316 0.1312 0.1746 0.0159  0.0106  0.0077  79  GLY   A O   
1709 N N   . SER   A 80  ? 0.1238 0.1368 0.1837 -0.0019 0.0104  -0.0008 80  SER   A N   
1710 C CA  . SER   A 80  ? 0.1238 0.1301 0.1712 -0.0006 0.0028  0.0055  80  SER   A CA  
1711 C C   . SER   A 80  ? 0.1188 0.1304 0.1668 -0.0075 0.0068  0.0125  80  SER   A C   
1712 O O   . SER   A 80  ? 0.1216 0.1557 0.1936 0.0041  0.0098  -0.0022 80  SER   A O   
1713 C CB  . SER   A 80  ? 0.1411 0.1286 0.1973 -0.0046 0.0065  0.0105  80  SER   A CB  
1714 O OG  . SER   A 80  ? 0.1650 0.1321 0.2330 0.0040  -0.0028 0.0304  80  SER   A OG  
1720 N N   . CYS   A 81  ? 0.1170 0.1271 0.1645 -0.0008 -0.0024 0.0172  81  CYS   A N   
1721 C CA  . CYS   A 81  ? 0.1144 0.1340 0.1702 -0.0038 -0.0080 0.0215  81  CYS   A CA  
1722 C C   . CYS   A 81  ? 0.1164 0.1288 0.1749 -0.0072 -0.0046 0.0267  81  CYS   A C   
1723 O O   . CYS   A 81  ? 0.1149 0.1612 0.1923 -0.0004 -0.0011 0.0404  81  CYS   A O   
1724 C CB  . CYS   A 81  ? 0.1252 0.1373 0.1907 -0.0132 -0.0017 0.0248  81  CYS   A CB  
1725 S SG  . CYS   A 81  ? 0.1386 0.1305 0.1809 -0.0143 0.0001  0.0165  81  CYS   A SG  
1731 N N   . VAL   A 82  ? 0.1199 0.1345 0.1739 -0.0020 -0.0106 0.0240  82  VAL   A N   
1732 C CA  . VAL   A 82  ? 0.1349 0.1439 0.1698 -0.0010 -0.0067 0.0337  82  VAL   A CA  
1733 C C   . VAL   A 82  ? 0.1287 0.1475 0.1754 -0.0040 -0.0103 0.0289  82  VAL   A C   
1734 O O   . VAL   A 82  ? 0.1238 0.1585 0.2005 -0.0049 -0.0072 0.0048  82  VAL   A O   
1735 C CB  . VAL   A 82  ? 0.1614 0.1598 0.1799 0.0001  -0.0052 0.0307  82  VAL   A CB  
1736 C CG1 . VAL   A 82  ? 0.1854 0.1727 0.1977 0.0001  -0.0026 0.0277  82  VAL   A CG1 
1737 C CG2 . VAL   A 82  ? 0.1683 0.1641 0.2157 -0.0016 -0.0112 0.0294  82  VAL   A CG2 
1747 N N   . LEU   A 83  ? 0.1240 0.1448 0.1626 -0.0151 -0.0128 0.0140  83  LEU   A N   
1748 C CA  . LEU   A 83  ? 0.1302 0.1448 0.1624 -0.0149 -0.0085 0.0119  83  LEU   A CA  
1749 C C   . LEU   A 83  ? 0.1340 0.1474 0.1521 -0.0135 -0.0163 0.0162  83  LEU   A C   
1750 O O   . LEU   A 83  ? 0.1448 0.1470 0.1676 -0.0169 -0.0137 0.0176  83  LEU   A O   
1751 C CB  . LEU   A 83  ? 0.1412 0.1489 0.1622 -0.0135 -0.0149 0.0144  83  LEU   A CB  
1752 C CG  . LEU   A 83  ? 0.1515 0.1569 0.1614 -0.0147 -0.0019 0.0076  83  LEU   A CG  
1753 C CD1 . LEU   A 83  ? 0.1609 0.1631 0.1732 -0.0266 -0.0052 0.0173  83  LEU   A CD1 
1754 C CD2 . LEU   A 83  ? 0.1430 0.1709 0.1818 -0.0157 0.0125  0.0093  83  LEU   A CD2 
1766 N N   . SER   A 84  ? 0.1512 0.1553 0.1516 -0.0185 -0.0168 0.0212  84  SER   A N   
1767 C CA  . SER   A 84  ? 0.1626 0.1606 0.1429 -0.0193 -0.0109 0.0204  84  SER   A CA  
1768 C C   . SER   A 84  ? 0.1641 0.1590 0.1389 -0.0252 0.0005  0.0129  84  SER   A C   
1769 O O   . SER   A 84  ? 0.1604 0.1677 0.1318 -0.0148 -0.0109 0.0151  84  SER   A O   
1770 C CB  . SER   A 84  ? 0.1627 0.1822 0.1531 -0.0130 -0.0135 0.0076  84  SER   A CB  
1771 O OG  . SER   A 84  ? 0.1669 0.2028 0.1709 -0.0133 -0.0180 -0.0066 84  SER   A OG  
1777 N N   . GLY   A 85  ? 0.1760 0.1744 0.1443 -0.0257 0.0048  0.0119  85  GLY   A N   
1778 C CA  . GLY   A 85  ? 0.1760 0.1781 0.1531 -0.0313 0.0112  0.0021  85  GLY   A CA  
1779 C C   . GLY   A 85  ? 0.1734 0.1837 0.1408 -0.0269 -0.0019 0.0017  85  GLY   A C   
1780 O O   . GLY   A 85  ? 0.1733 0.1980 0.1593 -0.0367 0.0096  -0.0118 85  GLY   A O   
1784 N N   . HIS   A 86  ? 0.1724 0.1783 0.1319 -0.0245 -0.0044 0.0043  86  HIS   A N   
1785 C CA  . HIS   A 86  ? 0.1906 0.1876 0.1357 -0.0280 -0.0024 0.0022  86  HIS   A CA  
1786 C C   . HIS   A 86  ? 0.2113 0.2031 0.1360 -0.0274 -0.0100 0.0006  86  HIS   A C   
1787 O O   . HIS   A 86  ? 0.2183 0.2242 0.1413 -0.0193 0.0035  0.0011  86  HIS   A O   
1788 C CB  . HIS   A 86  ? 0.1880 0.1817 0.1429 -0.0198 -0.0020 0.0084  86  HIS   A CB  
1789 C CG  . HIS   A 86  ? 0.1795 0.1807 0.1533 -0.0117 -0.0020 0.0107  86  HIS   A CG  
1790 N ND1 . HIS   A 86  ? 0.1849 0.1783 0.1945 -0.0240 -0.0017 0.0089  86  HIS   A ND1 
1791 C CD2 . HIS   A 86  ? 0.1780 0.1708 0.1489 -0.0054 0.0031  0.0161  86  HIS   A CD2 
1792 C CE1 . HIS   A 86  ? 0.1797 0.1777 0.1866 -0.0165 0.0124  0.0161  86  HIS   A CE1 
1793 N NE2 . HIS   A 86  ? 0.1756 0.1706 0.1582 -0.0012 0.0086  0.0277  86  HIS   A NE2 
1801 N N   . ASN   A 87  ? 0.2271 0.2128 0.1466 -0.0207 0.0130  -0.0089 87  ASN   A N   
1802 C CA  . ASN   A 87  ? 0.2472 0.2245 0.1569 -0.0197 0.0358  -0.0123 87  ASN   A CA  
1803 C C   . ASN   A 87  ? 0.2452 0.2364 0.1907 -0.0283 0.0562  -0.0048 87  ASN   A C   
1804 O O   . ASN   A 87  ? 0.2655 0.2515 0.2301 -0.0407 0.0829  -0.0161 87  ASN   A O   
1805 C CB  . ASN   A 87  ? 0.2668 0.2319 0.1626 -0.0065 0.0350  -0.0108 87  ASN   A CB  
1806 C CG  . ASN   A 87  ? 0.2785 0.2421 0.1684 0.0065  0.0511  -0.0060 87  ASN   A CG  
1807 O OD1 . ASN   A 87  ? 0.2940 0.2416 0.1720 0.0210  0.0494  0.0037  87  ASN   A OD1 
1808 N ND2 . ASN   A 87  ? 0.2800 0.2608 0.1807 0.0051  0.0506  -0.0000 87  ASN   A ND2 
1815 N N   . LEU   A 88  ? 0.2181 0.2251 0.1830 -0.0347 0.0393  0.0085  88  LEU   A N   
1816 C CA  . LEU   A 88  ? 0.1950 0.2203 0.1955 -0.0369 0.0360  0.0196  88  LEU   A CA  
1817 C C   . LEU   A 88  ? 0.1899 0.2222 0.1869 -0.0369 0.0340  0.0285  88  LEU   A C   
1818 O O   . LEU   A 88  ? 0.1941 0.2270 0.2163 -0.0305 0.0344  0.0477  88  LEU   A O   
1819 C CB  . LEU   A 88  ? 0.1944 0.2251 0.2043 -0.0433 -0.0021 0.0277  88  LEU   A CB  
1820 C CG  . LEU   A 88  ? 0.2173 0.2417 0.2327 -0.0370 -0.0119 0.0292  88  LEU   A CG  
1821 C CD1 . LEU   A 88  ? 0.2278 0.2497 0.2243 -0.0343 -0.0101 0.0223  88  LEU   A CD1 
1822 C CD2 . LEU   A 88  ? 0.2279 0.2526 0.2709 -0.0293 -0.0146 0.0202  88  LEU   A CD2 
1834 N N   . ALA   A 89  ? 0.1899 0.2151 0.1633 -0.0354 0.0202  0.0099  89  ALA   A N   
1835 C CA  . ALA   A 89  ? 0.1980 0.2114 0.1522 -0.0280 0.0053  0.0186  89  ALA   A CA  
1836 C C   . ALA   A 89  ? 0.2063 0.2129 0.1523 -0.0257 -0.0124 0.0159  89  ALA   A C   
1837 O O   . ALA   A 89  ? 0.2014 0.2098 0.1855 -0.0355 -0.0181 -0.0088 89  ALA   A O   
1838 C CB  . ALA   A 89  ? 0.1892 0.2100 0.1439 -0.0316 0.0002  0.0232  89  ALA   A CB  
1844 N N   . LYS   A 90  ? 0.2179 0.2294 0.1580 -0.0336 -0.0277 0.0211  90  LYS   A N   
1845 C CA  . LYS   A 90  ? 0.2288 0.2454 0.1545 -0.0300 -0.0383 0.0276  90  LYS   A CA  
1846 C C   . LYS   A 90  ? 0.2023 0.2251 0.1519 -0.0332 -0.0343 0.0133  90  LYS   A C   
1847 O O   . LYS   A 90  ? 0.2056 0.2449 0.1870 -0.0339 -0.0397 0.0011  90  LYS   A O   
1848 C CB  . LYS   A 90  ? 0.2568 0.2823 0.1945 -0.0248 -0.0495 0.0527  90  LYS   A CB  
1849 C CG  . LYS   A 90  ? 0.2930 0.3169 0.2941 -0.0224 -0.0478 0.0582  90  LYS   A CG  
1850 C CD  . LYS   A 90  ? 0.3347 0.3519 0.3908 -0.0253 -0.0321 0.0637  90  LYS   A CD  
1851 C CE  . LYS   A 90  ? 0.3669 0.3807 0.4636 -0.0261 -0.0190 0.0632  90  LYS   A CE  
1852 N NZ  . LYS   A 90  ? 0.3825 0.3962 0.5135 -0.0265 -0.0111 0.0595  90  LYS   A NZ  
1866 N N   . HIS   A 91  ? 0.1890 0.1968 0.1230 -0.0304 -0.0345 0.0220  91  HIS   A N   
1867 C CA  . HIS   A 91  ? 0.1756 0.1764 0.1410 -0.0157 -0.0323 0.0218  91  HIS   A CA  
1868 C C   . HIS   A 91  ? 0.1543 0.1624 0.1349 -0.0214 -0.0154 0.0278  91  HIS   A C   
1869 O O   . HIS   A 91  ? 0.1536 0.1796 0.1477 -0.0262 -0.0057 0.0277  91  HIS   A O   
1870 C CB  . HIS   A 91  ? 0.1979 0.2063 0.1876 0.0121  -0.0438 0.0261  91  HIS   A CB  
1871 C CG  . HIS   A 91  ? 0.2415 0.2580 0.2550 0.0200  -0.0703 0.0118  91  HIS   A CG  
1872 N ND1 . HIS   A 91  ? 0.2544 0.2847 0.2971 0.0228  -0.0802 -0.0096 91  HIS   A ND1 
1873 C CD2 . HIS   A 91  ? 0.2658 0.2801 0.2727 0.0234  -0.0875 0.0167  91  HIS   A CD2 
1874 C CE1 . HIS   A 91  ? 0.2694 0.2944 0.3067 0.0256  -0.0804 -0.0016 91  HIS   A CE1 
1875 N NE2 . HIS   A 91  ? 0.2778 0.2938 0.2954 0.0286  -0.0910 0.0081  91  HIS   A NE2 
1883 N N   . CYS   A 92  ? 0.1427 0.1534 0.1420 -0.0214 -0.0151 0.0270  92  CYS   A N   
1884 C CA  . CYS   A 92  ? 0.1343 0.1478 0.1478 -0.0138 -0.0035 0.0173  92  CYS   A CA  
1885 C C   . CYS   A 92  ? 0.1306 0.1397 0.1452 -0.0150 -0.0005 0.0170  92  CYS   A C   
1886 O O   . CYS   A 92  ? 0.1310 0.1470 0.1634 -0.0138 -0.0036 0.0173  92  CYS   A O   
1887 C CB  . CYS   A 92  ? 0.1347 0.1506 0.1537 -0.0064 -0.0115 0.0140  92  CYS   A CB  
1888 S SG  . CYS   A 92  ? 0.1359 0.1360 0.1546 -0.0120 -0.0059 0.0149  92  CYS   A SG  
1894 N N   . LEU   A 93  ? 0.1301 0.1261 0.1569 -0.0101 0.0020  0.0170  93  LEU   A N   
1895 C CA  . LEU   A 93  ? 0.1179 0.1257 0.1550 -0.0055 -0.0016 0.0170  93  LEU   A CA  
1896 C C   . LEU   A 93  ? 0.1175 0.1200 0.1424 -0.0009 0.0038  0.0116  93  LEU   A C   
1897 O O   . LEU   A 93  ? 0.1132 0.1300 0.1440 -0.0035 -0.0002 0.0127  93  LEU   A O   
1898 C CB  . LEU   A 93  ? 0.1243 0.1257 0.1692 -0.0057 -0.0091 0.0267  93  LEU   A CB  
1899 C CG  . LEU   A 93  ? 0.1331 0.1260 0.1719 -0.0030 -0.0004 0.0253  93  LEU   A CG  
1900 C CD1 . LEU   A 93  ? 0.1356 0.1302 0.1962 -0.0028 0.0069  0.0163  93  LEU   A CD1 
1901 C CD2 . LEU   A 93  ? 0.1458 0.1235 0.1880 -0.0102 -0.0035 0.0142  93  LEU   A CD2 
1913 N N   . HIS   A 94  ? 0.1103 0.1160 0.1484 -0.0040 0.0039  0.0194  94  HIS   A N   
1914 C CA  . HIS   A 94  ? 0.1112 0.1191 0.1486 -0.0095 -0.0001 0.0182  94  HIS   A CA  
1915 C C   . HIS   A 94  ? 0.1074 0.1116 0.1604 -0.0110 -0.0051 0.0094  94  HIS   A C   
1916 O O   . HIS   A 94  ? 0.1095 0.1389 0.1871 -0.0035 0.0002  -0.0098 94  HIS   A O   
1917 C CB  . HIS   A 94  ? 0.1111 0.1136 0.1532 -0.0081 -0.0065 0.0114  94  HIS   A CB  
1918 C CG  . HIS   A 94  ? 0.1138 0.1139 0.1472 -0.0078 -0.0091 0.0178  94  HIS   A CG  
1919 N ND1 . HIS   A 94  ? 0.1141 0.1159 0.1563 -0.0053 -0.0034 0.0164  94  HIS   A ND1 
1920 C CD2 . HIS   A 94  ? 0.1220 0.1251 0.1530 -0.0088 -0.0089 0.0105  94  HIS   A CD2 
1921 C CE1 . HIS   A 94  ? 0.1211 0.1207 0.1509 -0.0118 -0.0149 0.0121  94  HIS   A CE1 
1922 N NE2 . HIS   A 94  ? 0.1271 0.1207 0.1626 -0.0144 -0.0100 0.0064  94  HIS   A NE2 
1930 N N   . VAL   A 95  ? 0.1085 0.1125 0.1330 -0.0031 0.0056  0.0087  95  VAL   A N   
1931 C CA  . VAL   A 95  ? 0.1177 0.1173 0.1379 -0.0028 0.0091  0.0119  95  VAL   A CA  
1932 C C   . VAL   A 95  ? 0.1168 0.1134 0.1296 -0.0123 0.0046  0.0102  95  VAL   A C   
1933 O O   . VAL   A 95  ? 0.1187 0.1271 0.1419 0.0035  0.0056  0.0049  95  VAL   A O   
1934 C CB  . VAL   A 95  ? 0.1172 0.1170 0.1585 -0.0116 0.0030  0.0096  95  VAL   A CB  
1935 C CG1 . VAL   A 95  ? 0.1313 0.1196 0.1673 -0.0183 0.0001  0.0061  95  VAL   A CG1 
1936 C CG2 . VAL   A 95  ? 0.1216 0.1273 0.1515 -0.0125 0.0042  0.0232  95  VAL   A CG2 
1946 N N   . VAL   A 96  ? 0.1230 0.1162 0.1227 -0.0056 0.0048  0.0091  96  VAL   A N   
1947 C CA  . VAL   A 96  ? 0.1321 0.1162 0.1400 -0.0038 0.0081  0.0157  96  VAL   A CA  
1948 C C   . VAL   A 96  ? 0.1324 0.1229 0.1425 -0.0024 0.0140  0.0143  96  VAL   A C   
1949 O O   . VAL   A 96  ? 0.1383 0.1322 0.1640 -0.0063 0.0180  0.0003  96  VAL   A O   
1950 C CB  . VAL   A 96  ? 0.1286 0.1226 0.1464 -0.0060 0.0177  0.0141  96  VAL   A CB  
1951 C CG1 . VAL   A 96  ? 0.1429 0.1354 0.1393 -0.0065 0.0159  0.0062  96  VAL   A CG1 
1952 C CG2 . VAL   A 96  ? 0.1295 0.1291 0.1628 -0.0182 0.0134  0.0121  96  VAL   A CG2 
1962 N N   A GLY   A 97  ? 0.1292 0.1226 0.1480 -0.0062 0.0121  0.0080  97  GLY   A N   
1963 N N   B GLY   A 97  ? 0.1358 0.1287 0.1389 -0.0027 0.0083  0.0078  97  GLY   A N   
1964 C CA  A GLY   A 97  ? 0.1368 0.1379 0.1512 -0.0090 0.0027  0.0112  97  GLY   A CA  
1965 C CA  B GLY   A 97  ? 0.1425 0.1364 0.1368 -0.0031 0.0037  0.0088  97  GLY   A CA  
1966 C C   A GLY   A 97  ? 0.1373 0.1507 0.1435 -0.0148 0.0061  0.0078  97  GLY   A C   
1967 C C   B GLY   A 97  ? 0.1470 0.1426 0.1351 -0.0045 0.0017  0.0086  97  GLY   A C   
1968 O O   A GLY   A 97  ? 0.1506 0.1487 0.1616 -0.0149 0.0031  0.0147  97  GLY   A O   
1969 O O   B GLY   A 97  ? 0.1501 0.1438 0.1409 -0.0029 -0.0021 0.0115  97  GLY   A O   
1976 N N   A PRO   A 98  ? 0.1411 0.1590 0.1280 -0.0065 0.0006  0.0050  98  PRO   A N   
1977 N N   B PRO   A 98  ? 0.1535 0.1440 0.1353 -0.0037 -0.0022 0.0105  98  PRO   A N   
1978 C CA  A PRO   A 98  ? 0.1553 0.1808 0.1348 -0.0111 0.0047  0.0047  98  PRO   A CA  
1979 C CA  B PRO   A 98  ? 0.1648 0.1524 0.1420 -0.0077 -0.0026 0.0081  98  PRO   A CA  
1980 C C   A PRO   A 98  ? 0.1546 0.1907 0.1278 -0.0226 0.0046  0.0211  98  PRO   A C   
1981 C C   B PRO   A 98  ? 0.1807 0.1547 0.1407 -0.0128 -0.0041 0.0161  98  PRO   A C   
1982 O O   A PRO   A 98  ? 0.1455 0.1761 0.1500 -0.0152 -0.0004 0.0236  98  PRO   A O   
1983 O O   B PRO   A 98  ? 0.1768 0.1502 0.1541 -0.0083 -0.0023 0.0156  98  PRO   A O   
1984 C CB  A PRO   A 98  ? 0.1694 0.1897 0.1248 -0.0005 -0.0049 -0.0122 98  PRO   A CB  
1985 C CB  B PRO   A 98  ? 0.1649 0.1536 0.1377 -0.0028 -0.0064 0.0083  98  PRO   A CB  
1986 C CG  A PRO   A 98  ? 0.1670 0.1842 0.1416 0.0021  -0.0081 -0.0141 98  PRO   A CG  
1987 C CG  B PRO   A 98  ? 0.1647 0.1515 0.1417 -0.0025 -0.0064 0.0077  98  PRO   A CG  
1988 C CD  A PRO   A 98  ? 0.1528 0.1646 0.1345 0.0027  -0.0004 -0.0070 98  PRO   A CD  
1989 C CD  B PRO   A 98  ? 0.1579 0.1437 0.1356 -0.0010 -0.0025 0.0102  98  PRO   A CD  
2004 N N   A ASN   A 99  ? 0.1589 0.2163 0.1166 -0.0223 0.0065  0.0373  99  ASN   A N   
2005 N N   B ASN   A 99  ? 0.2024 0.1598 0.1271 -0.0150 -0.0120 0.0241  99  ASN   A N   
2006 C CA  A ASN   A 99  ? 0.1810 0.2377 0.1118 -0.0210 0.0023  0.0506  99  ASN   A CA  
2007 C CA  B ASN   A 99  ? 0.2255 0.1683 0.1328 -0.0158 -0.0149 0.0346  99  ASN   A CA  
2008 C C   A ASN   A 99  ? 0.1934 0.2725 0.1156 -0.0409 -0.0010 0.0573  99  ASN   A C   
2009 C C   B ASN   A 99  ? 0.2389 0.1835 0.1417 -0.0141 -0.0236 0.0294  99  ASN   A C   
2010 O O   A ASN   A 99  ? 0.2036 0.2880 0.1230 -0.0383 -0.0095 0.0416  99  ASN   A O   
2011 O O   B ASN   A 99  ? 0.2411 0.1677 0.1347 -0.0114 -0.0378 0.0153  99  ASN   A O   
2012 C CB  A ASN   A 99  ? 0.1762 0.2296 0.1233 -0.0148 0.0076  0.0472  99  ASN   A CB  
2013 C CB  B ASN   A 99  ? 0.2329 0.1648 0.1479 -0.0192 -0.0113 0.0445  99  ASN   A CB  
2014 C CG  A ASN   A 99  ? 0.1745 0.2238 0.1375 -0.0066 0.0000  0.0316  99  ASN   A CG  
2015 C CG  B ASN   A 99  ? 0.2397 0.1667 0.1630 -0.0250 -0.0094 0.0576  99  ASN   A CG  
2016 O OD1 A ASN   A 99  ? 0.1830 0.2325 0.1378 0.0004  -0.0008 0.0153  99  ASN   A OD1 
2017 O OD1 B ASN   A 99  ? 0.2430 0.1704 0.1514 -0.0240 -0.0066 0.0700  99  ASN   A OD1 
2018 N ND2 A ASN   A 99  ? 0.1758 0.2127 0.1642 -0.0063 -0.0098 0.0495  99  ASN   A ND2 
2019 N ND2 B ASN   A 99  ? 0.2424 0.1667 0.1907 -0.0242 -0.0181 0.0495  99  ASN   A ND2 
2032 N N   A VAL   A 100 ? 0.2092 0.2947 0.1354 -0.0551 -0.0273 0.0569  100 VAL   A N   
2033 N N   B VAL   A 100 ? 0.2494 0.2172 0.1705 -0.0138 -0.0235 0.0242  100 VAL   A N   
2034 C CA  A VAL   A 100 ? 0.2310 0.3183 0.1559 -0.0601 -0.0352 0.0554  100 VAL   A CA  
2035 C CA  B VAL   A 100 ? 0.2596 0.2494 0.2082 -0.0110 -0.0192 0.0192  100 VAL   A CA  
2036 C C   A VAL   A 100 ? 0.2455 0.3351 0.1465 -0.0645 -0.0387 0.0821  100 VAL   A C   
2037 C C   B VAL   A 100 ? 0.2733 0.2775 0.2341 -0.0053 -0.0167 0.0266  100 VAL   A C   
2038 O O   A VAL   A 100 ? 0.2578 0.3480 0.1723 -0.0586 -0.0152 0.0736  100 VAL   A O   
2039 O O   B VAL   A 100 ? 0.2756 0.2851 0.2450 -0.0041 -0.0146 0.0243  100 VAL   A O   
2040 C CB  A VAL   A 100 ? 0.2430 0.3193 0.1890 -0.0619 -0.0380 0.0369  100 VAL   A CB  
2041 C CB  B VAL   A 100 ? 0.2580 0.2488 0.2208 -0.0131 -0.0197 0.0104  100 VAL   A CB  
2042 C CG1 A VAL   A 100 ? 0.2442 0.3212 0.2080 -0.0646 -0.0345 0.0340  100 VAL   A CG1 
2043 C CG1 B VAL   A 100 ? 0.2571 0.2490 0.2259 -0.0123 -0.0171 0.0073  100 VAL   A CG1 
2044 C CG2 A VAL   A 100 ? 0.2484 0.3203 0.1993 -0.0613 -0.0418 0.0238  100 VAL   A CG2 
2045 C CG2 B VAL   A 100 ? 0.2573 0.2490 0.2257 -0.0152 -0.0211 0.0041  100 VAL   A CG2 
2064 N N   A ASN   A 101 ? 0.2499 0.3409 0.1651 -0.0729 -0.0394 0.1123  101 ASN   A N   
2065 N N   B ASN   A 101 ? 0.2834 0.2903 0.2542 0.0004  -0.0129 0.0327  101 ASN   A N   
2066 C CA  A ASN   A 101 ? 0.2714 0.3478 0.1889 -0.0774 -0.0378 0.1289  101 ASN   A CA  
2067 C CA  B ASN   A 101 ? 0.2944 0.2975 0.2685 0.0076  -0.0041 0.0360  101 ASN   A CA  
2068 C C   A ASN   A 101 ? 0.2967 0.3728 0.2209 -0.0772 -0.0078 0.1424  101 ASN   A C   
2069 C C   B ASN   A 101 ? 0.3039 0.2991 0.2834 0.0123  0.0080  0.0389  101 ASN   A C   
2070 O O   A ASN   A 101 ? 0.3097 0.3786 0.2658 -0.0702 -0.0092 0.1306  101 ASN   A O   
2071 O O   B ASN   A 101 ? 0.3070 0.3027 0.2923 0.0145  0.0124  0.0390  101 ASN   A O   
2072 C CB  A ASN   A 101 ? 0.2733 0.3334 0.1920 -0.0785 -0.0629 0.1224  101 ASN   A CB  
2073 C CB  B ASN   A 101 ? 0.2951 0.3009 0.2712 0.0113  -0.0040 0.0286  101 ASN   A CB  
2074 C CG  A ASN   A 101 ? 0.2764 0.3209 0.1926 -0.0812 -0.0754 0.0941  101 ASN   A CG  
2075 C CG  B ASN   A 101 ? 0.2957 0.3008 0.2750 0.0156  -0.0059 0.0230  101 ASN   A CG  
2076 O OD1 A ASN   A 101 ? 0.2756 0.3273 0.2140 -0.0719 -0.0731 0.0610  101 ASN   A OD1 
2077 O OD1 B ASN   A 101 ? 0.2988 0.3030 0.2764 0.0156  -0.0017 0.0163  101 ASN   A OD1 
2078 N ND2 A ASN   A 101 ? 0.2818 0.3084 0.1918 -0.0875 -0.0740 0.0968  101 ASN   A ND2 
2079 N ND2 B ASN   A 101 ? 0.2950 0.2998 0.2794 0.0203  -0.0096 0.0204  101 ASN   A ND2 
2092 N N   A LYS   A 102 ? 0.3047 0.3967 0.2478 -0.0823 0.0114  0.1304  102 LYS   A N   
2093 N N   B LYS   A 102 ? 0.3090 0.2953 0.2851 0.0119  0.0138  0.0358  102 LYS   A N   
2094 C CA  A LYS   A 102 ? 0.3180 0.4188 0.2534 -0.0816 0.0151  0.1124  102 LYS   A CA  
2095 C CA  B LYS   A 102 ? 0.3149 0.2940 0.2792 0.0081  0.0178  0.0323  102 LYS   A CA  
2096 C C   A LYS   A 102 ? 0.3260 0.4385 0.2377 -0.0700 0.0168  0.0994  102 LYS   A C   
2097 C C   B LYS   A 102 ? 0.3144 0.2857 0.2545 0.0090  0.0114  0.0442  102 LYS   A C   
2098 O O   A LYS   A 102 ? 0.3277 0.4512 0.2329 -0.0660 0.0240  0.0920  102 LYS   A O   
2099 O O   B LYS   A 102 ? 0.3173 0.2835 0.2534 0.0123  0.0126  0.0508  102 LYS   A O   
2100 C CB  A LYS   A 102 ? 0.3282 0.4205 0.2811 -0.0882 0.0096  0.0975  102 LYS   A CB  
2101 C CB  B LYS   A 102 ? 0.3209 0.2997 0.3013 0.0059  0.0222  0.0178  102 LYS   A CB  
2102 C CG  A LYS   A 102 ? 0.3387 0.4207 0.3005 -0.0932 0.0034  0.0795  102 LYS   A CG  
2103 C CG  B LYS   A 102 ? 0.3266 0.3057 0.3234 0.0032  0.0258  0.0048  102 LYS   A CG  
2104 C CD  A LYS   A 102 ? 0.3511 0.4222 0.3179 -0.0957 -0.0008 0.0584  102 LYS   A CD  
2105 C CD  B LYS   A 102 ? 0.3335 0.3128 0.3513 0.0006  0.0287  -0.0066 102 LYS   A CD  
2106 C CE  A LYS   A 102 ? 0.3619 0.4238 0.3378 -0.0954 -0.0065 0.0436  102 LYS   A CE  
2107 C CE  B LYS   A 102 ? 0.3394 0.3190 0.3700 -0.0013 0.0302  -0.0130 102 LYS   A CE  
2108 N NZ  A LYS   A 102 ? 0.3673 0.4232 0.3478 -0.0983 -0.0076 0.0343  102 LYS   A NZ  
2109 N NZ  B LYS   A 102 ? 0.3438 0.3229 0.3789 -0.0028 0.0301  -0.0147 102 LYS   A NZ  
2136 N N   A GLY   A 103 ? 0.3309 0.4460 0.2456 -0.0574 0.0059  0.0777  103 GLY   A N   
2137 N N   B GLY   A 103 ? 0.3095 0.2828 0.2340 0.0090  0.0007  0.0431  103 GLY   A N   
2138 C CA  A GLY   A 103 ? 0.3365 0.4489 0.2423 -0.0455 0.0055  0.0618  103 GLY   A CA  
2139 C CA  B GLY   A 103 ? 0.3035 0.2749 0.2243 0.0098  -0.0088 0.0513  103 GLY   A CA  
2140 C C   A GLY   A 103 ? 0.3367 0.4518 0.2441 -0.0378 0.0128  0.0484  103 GLY   A C   
2141 C C   B GLY   A 103 ? 0.2943 0.2646 0.2092 0.0075  -0.0159 0.0553  103 GLY   A C   
2142 O O   A GLY   A 103 ? 0.3474 0.4582 0.2662 -0.0308 0.0109  0.0410  103 GLY   A O   
2143 O O   B GLY   A 103 ? 0.2997 0.2625 0.2083 0.0071  -0.0190 0.0605  103 GLY   A O   
2150 N N   A GLU   A 104 ? 0.3208 0.4440 0.2097 -0.0424 0.0269  0.0395  104 GLU   A N   
2151 N N   B GLU   A 104 ? 0.2776 0.2536 0.1932 0.0038  -0.0244 0.0565  104 GLU   A N   
2152 C CA  A GLU   A 104 ? 0.3021 0.4325 0.1875 -0.0518 0.0325  0.0325  104 GLU   A CA  
2153 C CA  B GLU   A 104 ? 0.2639 0.2431 0.1783 -0.0037 -0.0317 0.0488  104 GLU   A CA  
2154 C C   A GLU   A 104 ? 0.3063 0.4411 0.1859 -0.0558 0.0309  0.0076  104 GLU   A C   
2155 C C   B GLU   A 104 ? 0.2668 0.2435 0.1886 -0.0015 -0.0257 0.0349  104 GLU   A C   
2156 O O   A GLU   A 104 ? 0.3004 0.4441 0.1959 -0.0578 0.0116  0.0028  104 GLU   A O   
2157 O O   B GLU   A 104 ? 0.2642 0.2327 0.1950 0.0026  -0.0270 0.0413  104 GLU   A O   
2158 C CB  A GLU   A 104 ? 0.2744 0.4115 0.1711 -0.0564 0.0369  0.0530  104 GLU   A CB  
2159 C CB  B GLU   A 104 ? 0.2518 0.2361 0.1672 -0.0133 -0.0377 0.0488  104 GLU   A CB  
2160 C CG  A GLU   A 104 ? 0.2524 0.3923 0.1794 -0.0566 0.0323  0.0665  104 GLU   A CG  
2161 C CG  B GLU   A 104 ? 0.2447 0.2356 0.1737 -0.0198 -0.0462 0.0444  104 GLU   A CG  
2162 C CD  A GLU   A 104 ? 0.2294 0.3727 0.1766 -0.0570 0.0320  0.0791  104 GLU   A CD  
2163 C CD  B GLU   A 104 ? 0.2374 0.2345 0.1744 -0.0249 -0.0546 0.0403  104 GLU   A CD  
2164 O OE1 A GLU   A 104 ? 0.2080 0.3583 0.1552 -0.0583 0.0245  0.0810  104 GLU   A OE1 
2165 O OE1 B GLU   A 104 ? 0.2333 0.2349 0.1639 -0.0230 -0.0658 0.0390  104 GLU   A OE1 
2166 O OE2 A GLU   A 104 ? 0.2419 0.3686 0.1917 -0.0543 0.0295  0.0964  104 GLU   A OE2 
2167 O OE2 B GLU   A 104 ? 0.2399 0.2336 0.1939 -0.0298 -0.0462 0.0366  104 GLU   A OE2 
2180 N N   A ASP   A 105 ? 0.3157 0.4449 0.1937 -0.0559 0.0419  -0.0193 105 ASP   A N   
2181 N N   B ASP   A 105 ? 0.2784 0.2575 0.2087 -0.0095 -0.0189 0.0166  105 ASP   A N   
2182 C CA  A ASP   A 105 ? 0.3196 0.4472 0.2298 -0.0543 0.0492  -0.0444 105 ASP   A CA  
2183 C CA  B ASP   A 105 ? 0.2887 0.2732 0.2361 -0.0147 -0.0092 -0.0071 105 ASP   A CA  
2184 C C   A ASP   A 105 ? 0.2898 0.4325 0.1939 -0.0663 0.0367  -0.0648 105 ASP   A C   
2185 C C   B ASP   A 105 ? 0.2849 0.2809 0.2334 -0.0199 -0.0076 -0.0177 105 ASP   A C   
2186 O O   A ASP   A 105 ? 0.2730 0.4224 0.1458 -0.0675 0.0383  -0.0859 105 ASP   A O   
2187 O O   B ASP   A 105 ? 0.2804 0.2869 0.2177 -0.0219 -0.0080 -0.0240 105 ASP   A O   
2188 C CB  A ASP   A 105 ? 0.3488 0.4647 0.2984 -0.0428 0.0625  -0.0479 105 ASP   A CB  
2189 C CB  B ASP   A 105 ? 0.3024 0.2823 0.2672 -0.0144 -0.0015 -0.0175 105 ASP   A CB  
2190 C CG  A ASP   A 105 ? 0.3715 0.4785 0.3540 -0.0331 0.0684  -0.0522 105 ASP   A CG  
2191 C CG  B ASP   A 105 ? 0.3137 0.2899 0.2917 -0.0108 0.0014  -0.0247 105 ASP   A CG  
2192 O OD1 A ASP   A 105 ? 0.3788 0.4844 0.3683 -0.0327 0.0676  -0.0599 105 ASP   A OD1 
2193 O OD1 B ASP   A 105 ? 0.3184 0.2894 0.2913 -0.0121 0.0013  -0.0285 105 ASP   A OD1 
2194 O OD2 A ASP   A 105 ? 0.3824 0.4836 0.3809 -0.0298 0.0744  -0.0460 105 ASP   A OD2 
2195 O OD2 B ASP   A 105 ? 0.3195 0.2971 0.3129 -0.0103 -0.0016 -0.0237 105 ASP   A OD2 
2204 N N   A ILE   A 106 ? 0.2734 0.4185 0.2184 -0.0756 0.0094  -0.0665 106 ILE   A N   
2205 N N   B ILE   A 106 ? 0.2842 0.2814 0.2455 -0.0213 -0.0088 -0.0186 106 ILE   A N   
2206 C CA  A ILE   A 106 ? 0.2480 0.4011 0.2333 -0.0866 -0.0142 -0.0805 106 ILE   A CA  
2207 C CA  B ILE   A 106 ? 0.2830 0.2847 0.2601 -0.0253 -0.0105 -0.0197 106 ILE   A CA  
2208 C C   A ILE   A 106 ? 0.2336 0.3694 0.2434 -0.1039 -0.0060 -0.0993 106 ILE   A C   
2209 C C   B ILE   A 106 ? 0.2809 0.2777 0.2589 -0.0261 -0.0051 -0.0154 106 ILE   A C   
2210 O O   A ILE   A 106 ? 0.2121 0.3534 0.2492 -0.1160 0.0094  -0.0993 106 ILE   A O   
2211 O O   B ILE   A 106 ? 0.2774 0.2776 0.2601 -0.0274 -0.0039 -0.0174 106 ILE   A O   
2212 C CB  A ILE   A 106 ? 0.2477 0.4155 0.2678 -0.0717 -0.0357 -0.0553 106 ILE   A CB  
2213 C CB  B ILE   A 106 ? 0.2861 0.2962 0.2826 -0.0269 -0.0175 -0.0175 106 ILE   A CB  
2214 C CG1 A ILE   A 106 ? 0.2392 0.4194 0.2944 -0.0576 -0.0402 -0.0335 106 ILE   A CG1 
2215 C CG1 B ILE   A 106 ? 0.2856 0.3032 0.2978 -0.0236 -0.0201 -0.0118 106 ILE   A CG1 
2216 C CG2 A ILE   A 106 ? 0.2540 0.4203 0.2780 -0.0690 -0.0419 -0.0532 106 ILE   A CG2 
2217 C CG2 B ILE   A 106 ? 0.2883 0.2985 0.2855 -0.0287 -0.0192 -0.0190 106 ILE   A CG2 
2218 C CD1 A ILE   A 106 ? 0.2370 0.4193 0.3072 -0.0450 -0.0342 -0.0208 106 ILE   A CD1 
2219 C CD1 B ILE   A 106 ? 0.2864 0.3057 0.3059 -0.0200 -0.0191 -0.0083 106 ILE   A CD1 
2242 N N   A GLN   A 107 ? 0.2504 0.3538 0.2695 -0.0972 0.0094  -0.1097 107 GLN   A N   
2243 N N   B GLN   A 107 ? 0.2822 0.2679 0.2613 -0.0241 0.0009  -0.0085 107 GLN   A N   
2244 C CA  A GLN   A 107 ? 0.2723 0.3353 0.3383 -0.0772 0.0325  -0.1020 107 GLN   A CA  
2245 C CA  B GLN   A 107 ? 0.2850 0.2629 0.2838 -0.0228 0.0080  -0.0064 107 GLN   A CA  
2246 C C   A GLN   A 107 ? 0.2426 0.2818 0.3241 -0.0642 0.0534  -0.0832 107 GLN   A C   
2247 C C   B GLN   A 107 ? 0.2598 0.2350 0.2575 -0.0209 0.0173  -0.0010 107 GLN   A C   
2248 O O   A GLN   A 107 ? 0.2524 0.2784 0.3774 -0.0585 0.0650  -0.0841 107 GLN   A O   
2249 O O   B GLN   A 107 ? 0.2622 0.2323 0.2570 -0.0211 0.0173  -0.0060 107 GLN   A O   
2250 C CB  A GLN   A 107 ? 0.3145 0.3641 0.4241 -0.0770 0.0254  -0.1015 107 GLN   A CB  
2251 C CB  B GLN   A 107 ? 0.3094 0.2858 0.3332 -0.0261 0.0020  -0.0065 107 GLN   A CB  
2252 C CG  A GLN   A 107 ? 0.3591 0.3923 0.5180 -0.0709 0.0175  -0.0926 107 GLN   A CG  
2253 C CG  B GLN   A 107 ? 0.3306 0.3059 0.3844 -0.0282 -0.0045 -0.0015 107 GLN   A CG  
2254 C CD  A GLN   A 107 ? 0.3913 0.4129 0.5987 -0.0661 0.0131  -0.0808 107 GLN   A CD  
2255 C CD  B GLN   A 107 ? 0.3492 0.3240 0.4306 -0.0282 -0.0090 0.0038  107 GLN   A CD  
2256 O OE1 A GLN   A 107 ? 0.4059 0.4202 0.6312 -0.0648 0.0118  -0.0781 107 GLN   A OE1 
2257 O OE1 B GLN   A 107 ? 0.3559 0.3309 0.4436 -0.0285 -0.0091 0.0073  107 GLN   A OE1 
2258 N NE2 A GLN   A 107 ? 0.4033 0.4203 0.6270 -0.0648 0.0110  -0.0784 107 GLN   A NE2 
2259 N NE2 B GLN   A 107 ? 0.3546 0.3302 0.4449 -0.0282 -0.0134 0.0054  107 GLN   A NE2 
2276 N N   A LEU   A 108 ? 0.2014 0.2268 0.2643 -0.0560 0.0519  -0.0760 108 LEU   A N   
2277 N N   B LEU   A 108 ? 0.2312 0.2097 0.2352 -0.0218 0.0239  -0.0016 108 LEU   A N   
2278 C CA  A LEU   A 108 ? 0.1840 0.1843 0.2337 -0.0224 0.0439  -0.0369 108 LEU   A CA  
2279 C CA  B LEU   A 108 ? 0.2048 0.1851 0.2181 -0.0156 0.0266  -0.0000 108 LEU   A CA  
2280 C C   A LEU   A 108 ? 0.1609 0.1422 0.2226 -0.0106 0.0403  -0.0058 108 LEU   A C   
2281 C C   B LEU   A 108 ? 0.1777 0.1577 0.2122 -0.0064 0.0290  0.0091  108 LEU   A C   
2282 O O   A LEU   A 108 ? 0.1542 0.1391 0.2451 -0.0013 0.0385  -0.0012 108 LEU   A O   
2283 O O   B LEU   A 108 ? 0.1773 0.1582 0.2171 -0.0021 0.0305  0.0111  108 LEU   A O   
2284 C CB  A LEU   A 108 ? 0.1907 0.1930 0.2242 -0.0236 0.0472  -0.0254 108 LEU   A CB  
2285 C CB  B LEU   A 108 ? 0.2057 0.1915 0.2107 -0.0252 0.0276  -0.0082 108 LEU   A CB  
2286 C CG  A LEU   A 108 ? 0.2101 0.2158 0.2435 -0.0173 0.0528  -0.0155 108 LEU   A CG  
2287 C CG  B LEU   A 108 ? 0.2094 0.2019 0.2174 -0.0316 0.0302  -0.0162 108 LEU   A CG  
2288 C CD1 A LEU   A 108 ? 0.2227 0.2201 0.2479 -0.0228 0.0548  -0.0103 108 LEU   A CD1 
2289 C CD1 B LEU   A 108 ? 0.2107 0.2047 0.2184 -0.0354 0.0321  -0.0177 108 LEU   A CD1 
2290 C CD2 A LEU   A 108 ? 0.2158 0.2317 0.2759 -0.0100 0.0502  -0.0103 108 LEU   A CD2 
2291 C CD2 B LEU   A 108 ? 0.2108 0.2067 0.2297 -0.0348 0.0306  -0.0157 108 LEU   A CD2 
2314 N N   . LEU   A 109 ? 0.1537 0.1427 0.2161 -0.0005 0.0289  0.0156  109 LEU   A N   
2315 C CA  . LEU   A 109 ? 0.1483 0.1346 0.2016 -0.0027 0.0184  0.0157  109 LEU   A CA  
2316 C C   . LEU   A 109 ? 0.1363 0.1285 0.1942 -0.0098 0.0143  0.0102  109 LEU   A C   
2317 O O   . LEU   A 109 ? 0.1443 0.1202 0.2076 -0.0039 -0.0003 0.0054  109 LEU   A O   
2318 C CB  . LEU   A 109 ? 0.1498 0.1402 0.2168 0.0080  0.0114  0.0308  109 LEU   A CB  
2319 C CG  . LEU   A 109 ? 0.1414 0.1507 0.2228 0.0060  0.0103  0.0370  109 LEU   A CG  
2320 C CD1 . LEU   A 109 ? 0.1488 0.1426 0.2364 0.0023  0.0156  0.0192  109 LEU   A CD1 
2321 C CD2 . LEU   A 109 ? 0.1430 0.1730 0.2481 0.0049  0.0070  0.0312  109 LEU   A CD2 
2334 N N   . LYS   A 110 ? 0.1378 0.1285 0.1881 -0.0103 0.0055  0.0099  110 LYS   A N   
2335 C CA  . LYS   A 110 ? 0.1366 0.1239 0.1982 -0.0105 -0.0014 0.0134  110 LYS   A CA  
2336 C C   . LYS   A 110 ? 0.1365 0.1180 0.1944 -0.0113 0.0029  0.0056  110 LYS   A C   
2337 O O   . LYS   A 110 ? 0.1295 0.1170 0.2065 -0.0105 0.0099  -0.0020 110 LYS   A O   
2338 C CB  . LYS   A 110 ? 0.1405 0.1268 0.2136 -0.0101 -0.0079 0.0035  110 LYS   A CB  
2339 C CG  . LYS   A 110 ? 0.1466 0.1289 0.2234 -0.0049 -0.0066 -0.0021 110 LYS   A CG  
2340 C CD  . LYS   A 110 ? 0.1513 0.1344 0.2353 -0.0108 -0.0002 -0.0068 110 LYS   A CD  
2341 C CE  . LYS   A 110 ? 0.1571 0.1412 0.2562 -0.0080 0.0099  -0.0119 110 LYS   A CE  
2342 N NZ  . LYS   A 110 ? 0.1584 0.1460 0.2631 -0.0184 0.0187  -0.0077 110 LYS   A NZ  
2356 N N   . SER   A 111 ? 0.1346 0.1207 0.1953 -0.0061 0.0039  0.0026  111 SER   A N   
2357 C CA  . SER   A 111 ? 0.1264 0.1237 0.2038 -0.0034 0.0069  0.0022  111 SER   A CA  
2358 C C   . SER   A 111 ? 0.1213 0.1186 0.1999 -0.0086 0.0081  0.0074  111 SER   A C   
2359 O O   . SER   A 111 ? 0.1354 0.1142 0.2055 -0.0061 0.0096  0.0046  111 SER   A O   
2360 C CB  . SER   A 111 ? 0.1424 0.1434 0.2111 -0.0034 0.0213  -0.0076 111 SER   A CB  
2361 O OG  . SER   A 111 ? 0.1877 0.1657 0.2250 0.0041  0.0244  -0.0116 111 SER   A OG  
2367 N N   . ALA   A 112 ? 0.1310 0.1132 0.2021 -0.0023 0.0180  0.0064  112 ALA   A N   
2368 C CA  . ALA   A 112 ? 0.1328 0.1152 0.1932 -0.0070 0.0186  -0.0019 112 ALA   A CA  
2369 C C   . ALA   A 112 ? 0.1263 0.1123 0.2002 -0.0046 0.0092  0.0063  112 ALA   A C   
2370 O O   . ALA   A 112 ? 0.1273 0.1114 0.2108 -0.0129 0.0166  0.0061  112 ALA   A O   
2371 C CB  . ALA   A 112 ? 0.1424 0.1203 0.1942 -0.0064 0.0137  0.0040  112 ALA   A CB  
2377 N N   . TYR   A 113 ? 0.1191 0.1191 0.1956 -0.0042 0.0133  0.0113  113 TYR   A N   
2378 C CA  . TYR   A 113 ? 0.1161 0.1158 0.1863 -0.0043 0.0155  0.0150  113 TYR   A CA  
2379 C C   . TYR   A 113 ? 0.1128 0.1149 0.1867 -0.0129 0.0150  0.0076  113 TYR   A C   
2380 O O   . TYR   A 113 ? 0.1217 0.1197 0.1966 -0.0066 0.0154  0.0047  113 TYR   A O   
2381 C CB  . TYR   A 113 ? 0.1181 0.1233 0.1907 -0.0056 -0.0023 0.0230  113 TYR   A CB  
2382 C CG  . TYR   A 113 ? 0.1214 0.1268 0.1785 -0.0131 0.0079  0.0194  113 TYR   A CG  
2383 C CD1 . TYR   A 113 ? 0.1229 0.1338 0.1713 -0.0042 0.0124  0.0249  113 TYR   A CD1 
2384 C CD2 . TYR   A 113 ? 0.1234 0.1322 0.1822 -0.0154 0.0093  0.0209  113 TYR   A CD2 
2385 C CE1 . TYR   A 113 ? 0.1272 0.1430 0.1722 -0.0037 0.0097  0.0225  113 TYR   A CE1 
2386 C CE2 . TYR   A 113 ? 0.1243 0.1415 0.1825 -0.0140 0.0009  0.0202  113 TYR   A CE2 
2387 C CZ  . TYR   A 113 ? 0.1258 0.1401 0.1725 -0.0004 0.0094  0.0248  113 TYR   A CZ  
2388 O OH  . TYR   A 113 ? 0.1249 0.1474 0.1968 0.0038  0.0114  0.0292  113 TYR   A OH  
2398 N N   . GLU   A 114 ? 0.1187 0.1139 0.1934 -0.0065 0.0172  0.0161  114 GLU   A N   
2399 C CA  . GLU   A 114 ? 0.1235 0.1103 0.1993 0.0006  0.0106  0.0206  114 GLU   A CA  
2400 C C   . GLU   A 114 ? 0.1179 0.1168 0.1959 -0.0026 0.0123  0.0064  114 GLU   A C   
2401 O O   . GLU   A 114 ? 0.1279 0.1205 0.1936 -0.0019 0.0043  0.0091  114 GLU   A O   
2402 C CB  . GLU   A 114 ? 0.1249 0.1109 0.1960 -0.0088 0.0095  0.0170  114 GLU   A CB  
2403 C CG  . GLU   A 114 ? 0.1336 0.1139 0.2030 -0.0020 0.0098  0.0064  114 GLU   A CG  
2404 C CD  . GLU   A 114 ? 0.1417 0.1158 0.2153 -0.0054 0.0029  -0.0002 114 GLU   A CD  
2405 O OE1 . GLU   A 114 ? 0.1403 0.1187 0.2181 -0.0093 0.0152  -0.0075 114 GLU   A OE1 
2406 O OE2 . GLU   A 114 ? 0.1602 0.1235 0.2271 -0.0100 0.0040  -0.0082 114 GLU   A OE2 
2413 N N   . ASN   A 115 ? 0.1208 0.1167 0.1852 -0.0079 0.0094  0.0025  115 ASN   A N   
2414 C CA  . ASN   A 115 ? 0.1238 0.1244 0.1956 -0.0128 0.0136  0.0087  115 ASN   A CA  
2415 C C   . ASN   A 115 ? 0.1219 0.1206 0.1880 -0.0144 0.0060  0.0103  115 ASN   A C   
2416 O O   . ASN   A 115 ? 0.1270 0.1293 0.1880 -0.0096 0.0131  0.0139  115 ASN   A O   
2417 C CB  . ASN   A 115 ? 0.1337 0.1302 0.1817 -0.0194 0.0147  0.0074  115 ASN   A CB  
2418 C CG  . ASN   A 115 ? 0.1299 0.1491 0.1908 -0.0242 0.0198  0.0021  115 ASN   A CG  
2419 O OD1 . ASN   A 115 ? 0.1361 0.2430 0.2173 -0.0192 0.0257  0.0196  115 ASN   A OD1 
2420 N ND2 . ASN   A 115 ? 0.1325 0.1296 0.1843 -0.0150 0.0275  0.0093  115 ASN   A ND2 
2427 N N   . PHE   A 116 ? 0.1201 0.1185 0.1918 -0.0069 0.0092  0.0205  116 PHE   A N   
2428 C CA  . PHE   A 116 ? 0.1218 0.1294 0.1784 -0.0030 0.0133  0.0175  116 PHE   A CA  
2429 C C   . PHE   A 116 ? 0.1167 0.1314 0.1815 -0.0116 0.0146  0.0205  116 PHE   A C   
2430 O O   . PHE   A 116 ? 0.1229 0.1391 0.1944 -0.0034 0.0053  0.0275  116 PHE   A O   
2431 C CB  . PHE   A 116 ? 0.1183 0.1170 0.1955 -0.0054 0.0188  0.0212  116 PHE   A CB  
2432 C CG  . PHE   A 116 ? 0.1220 0.1191 0.1858 -0.0086 0.0142  0.0134  116 PHE   A CG  
2433 C CD1 . PHE   A 116 ? 0.1259 0.1190 0.1826 -0.0089 0.0094  0.0109  116 PHE   A CD1 
2434 C CD2 . PHE   A 116 ? 0.1306 0.1258 0.1936 -0.0105 0.0146  0.0220  116 PHE   A CD2 
2435 C CE1 . PHE   A 116 ? 0.1312 0.1182 0.1959 -0.0173 0.0030  0.0108  116 PHE   A CE1 
2436 C CE2 . PHE   A 116 ? 0.1284 0.1229 0.1975 -0.0066 0.0156  0.0125  116 PHE   A CE2 
2437 C CZ  . PHE   A 116 ? 0.1307 0.1087 0.1888 -0.0004 0.0032  0.0120  116 PHE   A CZ  
2447 N N   . ASN   A 117 ? 0.1195 0.1229 0.2012 -0.0055 0.0129  0.0221  117 ASN   A N   
2448 C CA  . ASN   A 117 ? 0.1222 0.1221 0.2071 -0.0013 0.0130  0.0264  117 ASN   A CA  
2449 C C   . ASN   A 117 ? 0.1236 0.1309 0.2218 -0.0018 0.0180  0.0259  117 ASN   A C   
2450 O O   . ASN   A 117 ? 0.1334 0.1401 0.2399 -0.0084 -0.0062 0.0366  117 ASN   A O   
2451 C CB  . ASN   A 117 ? 0.1233 0.1273 0.2111 -0.0028 0.0072  0.0285  117 ASN   A CB  
2452 C CG  . ASN   A 117 ? 0.1210 0.1299 0.2030 -0.0034 0.0177  0.0279  117 ASN   A CG  
2453 O OD1 . ASN   A 117 ? 0.1261 0.1462 0.2151 -0.0133 0.0093  0.0188  117 ASN   A OD1 
2454 N ND2 . ASN   A 117 ? 0.1210 0.1288 0.2054 -0.0040 0.0103  0.0235  117 ASN   A ND2 
2461 N N   . GLN   A 118 ? 0.1236 0.1336 0.2151 -0.0104 -0.0042 0.0294  118 GLN   A N   
2462 C CA  . GLN   A 118 ? 0.1269 0.1447 0.2185 -0.0062 -0.0092 0.0243  118 GLN   A CA  
2463 C C   . GLN   A 118 ? 0.1326 0.1569 0.2055 -0.0101 -0.0026 0.0270  118 GLN   A C   
2464 O O   . GLN   A 118 ? 0.1311 0.1874 0.2311 -0.0008 -0.0132 0.0091  118 GLN   A O   
2465 C CB  . GLN   A 118 ? 0.1243 0.1523 0.2263 -0.0057 0.0065  0.0245  118 GLN   A CB  
2466 C CG  . GLN   A 118 ? 0.1232 0.1525 0.2232 -0.0057 0.0086  0.0279  118 GLN   A CG  
2467 C CD  . GLN   A 118 ? 0.1226 0.1525 0.2439 -0.0023 0.0076  0.0238  118 GLN   A CD  
2468 O OE1 . GLN   A 118 ? 0.1281 0.1646 0.2618 0.0084  -0.0021 0.0136  118 GLN   A OE1 
2469 N NE2 . GLN   A 118 ? 0.1357 0.1507 0.2420 -0.0020 0.0028  0.0212  118 GLN   A NE2 
2478 N N   . HIS   A 119 ? 0.1386 0.1491 0.1923 -0.0054 -0.0019 0.0299  119 HIS   A N   
2479 C CA  . HIS   A 119 ? 0.1409 0.1540 0.1941 -0.0078 -0.0065 0.0319  119 HIS   A CA  
2480 C C   . HIS   A 119 ? 0.1510 0.1605 0.1932 -0.0119 -0.0002 0.0389  119 HIS   A C   
2481 O O   . HIS   A 119 ? 0.1525 0.1706 0.1972 -0.0256 -0.0050 0.0406  119 HIS   A O   
2482 C CB  . HIS   A 119 ? 0.1469 0.1504 0.2169 -0.0063 0.0122  0.0311  119 HIS   A CB  
2483 C CG  . HIS   A 119 ? 0.1499 0.1549 0.2588 -0.0028 0.0112  0.0403  119 HIS   A CG  
2484 N ND1 . HIS   A 119 ? 0.1633 0.1772 0.3120 -0.0147 0.0051  0.0255  119 HIS   A ND1 
2485 C CD2 . HIS   A 119 ? 0.1625 0.1660 0.2716 0.0115  0.0279  0.0576  119 HIS   A CD2 
2486 C CE1 . HIS   A 119 ? 0.1557 0.1760 0.3157 -0.0218 0.0181  0.0460  119 HIS   A CE1 
2487 N NE2 . HIS   A 119 ? 0.1712 0.1756 0.3068 -0.0033 0.0397  0.0602  119 HIS   A NE2 
2495 N N   . GLU   A 120 ? 0.1571 0.1844 0.2028 -0.0097 -0.0097 0.0599  120 GLU   A N   
2496 C CA  . GLU   A 120 ? 0.1809 0.2156 0.2297 0.0014  -0.0119 0.1012  120 GLU   A CA  
2497 C C   . GLU   A 120 ? 0.1606 0.2002 0.2010 -0.0154 -0.0095 0.0882  120 GLU   A C   
2498 O O   . GLU   A 120 ? 0.1585 0.1887 0.2198 -0.0186 -0.0132 0.0802  120 GLU   A O   
2499 C CB  . GLU   A 120 ? 0.2557 0.2876 0.2964 0.0252  -0.0095 0.1491  120 GLU   A CB  
2500 C CG  . GLU   A 120 ? 0.3511 0.3660 0.4018 0.0415  -0.0065 0.1591  120 GLU   A CG  
2501 C CD  . GLU   A 120 ? 0.4342 0.4340 0.5190 0.0532  0.0046  0.1487  120 GLU   A CD  
2502 O OE1 . GLU   A 120 ? 0.4590 0.4552 0.5456 0.0560  0.0070  0.1445  120 GLU   A OE1 
2503 O OE2 . GLU   A 120 ? 0.4883 0.4883 0.5715 0.0566  0.0092  0.1445  120 GLU   A OE2 
2510 N N   . VAL   A 121 ? 0.1592 0.2031 0.1777 -0.0148 -0.0005 0.0686  121 VAL   A N   
2511 C CA  . VAL   A 121 ? 0.1672 0.2067 0.1680 -0.0189 0.0059  0.0652  121 VAL   A CA  
2512 C C   . VAL   A 121 ? 0.1532 0.1886 0.1534 -0.0250 0.0011  0.0495  121 VAL   A C   
2513 O O   . VAL   A 121 ? 0.1575 0.1944 0.1677 -0.0337 -0.0106 0.0450  121 VAL   A O   
2514 C CB  . VAL   A 121 ? 0.2034 0.2437 0.1973 -0.0056 0.0146  0.0746  121 VAL   A CB  
2515 C CG1 . VAL   A 121 ? 0.2087 0.2593 0.2001 -0.0027 0.0258  0.0771  121 VAL   A CG1 
2516 C CG2 . VAL   A 121 ? 0.2266 0.2597 0.2335 -0.0130 0.0118  0.0620  121 VAL   A CG2 
2526 N N   . LEU   A 122 ? 0.1425 0.1689 0.1622 -0.0218 0.0017  0.0423  122 LEU   A N   
2527 C CA  . LEU   A 122 ? 0.1525 0.1519 0.1605 -0.0209 0.0186  0.0401  122 LEU   A CA  
2528 C C   . LEU   A 122 ? 0.1477 0.1500 0.1677 -0.0257 0.0062  0.0357  122 LEU   A C   
2529 O O   . LEU   A 122 ? 0.1460 0.1581 0.1957 -0.0304 0.0068  0.0359  122 LEU   A O   
2530 C CB  . LEU   A 122 ? 0.1689 0.1525 0.1824 -0.0109 0.0057  0.0420  122 LEU   A CB  
2531 C CG  . LEU   A 122 ? 0.1674 0.1620 0.1794 -0.0127 0.0177  0.0331  122 LEU   A CG  
2532 C CD1 . LEU   A 122 ? 0.1901 0.1646 0.1946 -0.0209 0.0214  0.0355  122 LEU   A CD1 
2533 C CD2 . LEU   A 122 ? 0.1654 0.1553 0.1814 -0.0112 0.0288  0.0323  122 LEU   A CD2 
2545 N N   . LEU   A 123 ? 0.1362 0.1539 0.1601 -0.0248 0.0043  0.0295  123 LEU   A N   
2546 C CA  . LEU   A 123 ? 0.1377 0.1525 0.1546 -0.0260 0.0030  0.0306  123 LEU   A CA  
2547 C C   . LEU   A 123 ? 0.1344 0.1441 0.1458 -0.0181 0.0045  0.0319  123 LEU   A C   
2548 O O   . LEU   A 123 ? 0.1330 0.1583 0.1643 -0.0259 -0.0008 0.0398  123 LEU   A O   
2549 C CB  . LEU   A 123 ? 0.1498 0.1614 0.1527 -0.0288 0.0130  0.0274  123 LEU   A CB  
2550 C CG  . LEU   A 123 ? 0.1532 0.1734 0.1676 -0.0233 0.0181  0.0153  123 LEU   A CG  
2551 C CD1 . LEU   A 123 ? 0.1557 0.1784 0.1851 -0.0076 0.0208  0.0093  123 LEU   A CD1 
2552 C CD2 . LEU   A 123 ? 0.1655 0.1817 0.1821 -0.0188 0.0100  0.0148  123 LEU   A CD2 
2564 N N   A ALA   A 124 ? 0.1301 0.1313 0.1462 -0.0143 0.0094  0.0275  124 ALA   A N   
2565 N N   B ALA   A 124 ? 0.1412 0.1405 0.1387 -0.0152 0.0048  0.0255  124 ALA   A N   
2566 C CA  A ALA   A 124 ? 0.1242 0.1258 0.1519 -0.0130 0.0046  0.0225  124 ALA   A CA  
2567 C CA  B ALA   A 124 ? 0.1473 0.1419 0.1397 -0.0160 0.0004  0.0239  124 ALA   A CA  
2568 C C   A ALA   A 124 ? 0.1123 0.1274 0.1541 -0.0094 0.0117  0.0228  124 ALA   A C   
2569 C C   B ALA   A 124 ? 0.1461 0.1376 0.1325 -0.0099 0.0023  0.0244  124 ALA   A C   
2570 O O   A ALA   A 124 ? 0.1131 0.1373 0.1850 -0.0153 0.0197  0.0308  124 ALA   A O   
2571 O O   B ALA   A 124 ? 0.1486 0.1424 0.1365 -0.0062 0.0040  0.0300  124 ALA   A O   
2572 C CB  A ALA   A 124 ? 0.1191 0.1159 0.1749 -0.0090 0.0034  0.0229  124 ALA   A CB  
2573 C CB  B ALA   A 124 ? 0.1505 0.1414 0.1556 -0.0201 0.0024  0.0206  124 ALA   A CB  
2584 N N   A PRO   A 125 ? 0.1116 0.1265 0.1638 -0.0079 0.0131  0.0330  125 PRO   A N   
2585 N N   B PRO   A 125 ? 0.1402 0.1276 0.1252 -0.0047 0.0005  0.0253  125 PRO   A N   
2586 C CA  A PRO   A 125 ? 0.1190 0.1296 0.1726 -0.0082 0.0124  0.0310  125 PRO   A CA  
2587 C CA  B PRO   A 125 ? 0.1433 0.1346 0.1332 -0.0034 0.0034  0.0244  125 PRO   A CA  
2588 C C   A PRO   A 125 ? 0.1163 0.1306 0.1638 -0.0067 0.0065  0.0263  125 PRO   A C   
2589 C C   B PRO   A 125 ? 0.1435 0.1434 0.1371 -0.0043 0.0071  0.0278  125 PRO   A C   
2590 O O   A PRO   A 125 ? 0.1185 0.1285 0.1727 -0.0027 -0.0034 0.0209  125 PRO   A O   
2591 O O   B PRO   A 125 ? 0.1461 0.1473 0.1466 -0.0010 0.0070  0.0270  125 PRO   A O   
2592 C CB  A PRO   A 125 ? 0.1345 0.1293 0.1632 -0.0162 0.0133  0.0241  125 PRO   A CB  
2593 C CB  B PRO   A 125 ? 0.1471 0.1304 0.1308 -0.0039 0.0009  0.0204  125 PRO   A CB  
2594 C CG  A PRO   A 125 ? 0.1319 0.1277 0.1762 -0.0176 0.0128  0.0334  125 PRO   A CG  
2595 C CG  B PRO   A 125 ? 0.1463 0.1227 0.1377 -0.0047 -0.0001 0.0250  125 PRO   A CG  
2596 C CD  A PRO   A 125 ? 0.1192 0.1319 0.1752 -0.0156 0.0232  0.0300  125 PRO   A CD  
2597 C CD  B PRO   A 125 ? 0.1385 0.1142 0.1254 -0.0045 0.0033  0.0219  125 PRO   A CD  
2612 N N   A LEU   A 126 ? 0.1075 0.1384 0.1675 -0.0015 0.0090  0.0224  126 LEU   A N   
2613 N N   B LEU   A 126 ? 0.1419 0.1455 0.1473 -0.0049 0.0062  0.0283  126 LEU   A N   
2614 C CA  A LEU   A 126 ? 0.1106 0.1305 0.1723 -0.0030 0.0052  0.0250  126 LEU   A CA  
2615 C CA  B LEU   A 126 ? 0.1363 0.1407 0.1494 -0.0016 0.0026  0.0293  126 LEU   A CA  
2616 C C   A LEU   A 126 ? 0.1196 0.1270 0.1631 0.0023  -0.0011 0.0216  126 LEU   A C   
2617 C C   B LEU   A 126 ? 0.1277 0.1346 0.1492 -0.0054 0.0011  0.0253  126 LEU   A C   
2618 O O   A LEU   A 126 ? 0.1344 0.1341 0.1740 0.0098  0.0093  0.0279  126 LEU   A O   
2619 O O   B LEU   A 126 ? 0.1265 0.1321 0.1589 -0.0139 -0.0065 0.0339  126 LEU   A O   
2620 C CB  A LEU   A 126 ? 0.1191 0.1322 0.1832 -0.0004 0.0043  0.0210  126 LEU   A CB  
2621 C CB  B LEU   A 126 ? 0.1445 0.1470 0.1720 0.0027  0.0012  0.0179  126 LEU   A CB  
2622 C CG  A LEU   A 126 ? 0.1168 0.1380 0.1973 -0.0028 0.0190  0.0188  126 LEU   A CG  
2623 C CG  B LEU   A 126 ? 0.1482 0.1454 0.1853 0.0074  -0.0000 0.0041  126 LEU   A CG  
2624 C CD1 A LEU   A 126 ? 0.1241 0.1539 0.2267 -0.0041 0.0108  0.0263  126 LEU   A CD1 
2625 C CD1 B LEU   A 126 ? 0.1509 0.1414 0.1948 0.0102  -0.0045 -0.0084 126 LEU   A CD1 
2626 C CD2 A LEU   A 126 ? 0.1293 0.1354 0.1919 -0.0090 0.0247  0.0190  126 LEU   A CD2 
2627 C CD2 B LEU   A 126 ? 0.1475 0.1478 0.1896 0.0087  -0.0035 0.0093  126 LEU   A CD2 
2650 N N   A LEU   A 127 ? 0.1228 0.1281 0.1627 -0.0002 0.0019  0.0152  127 LEU   A N   
2651 N N   B LEU   A 127 ? 0.1229 0.1345 0.1410 -0.0043 0.0054  0.0241  127 LEU   A N   
2652 C CA  A LEU   A 127 ? 0.1248 0.1297 0.1527 -0.0082 -0.0007 0.0090  127 LEU   A CA  
2653 C CA  B LEU   A 127 ? 0.1207 0.1396 0.1367 -0.0019 0.0055  0.0304  127 LEU   A CA  
2654 C C   A LEU   A 127 ? 0.1262 0.1231 0.1498 -0.0083 -0.0009 0.0028  127 LEU   A C   
2655 C C   B LEU   A 127 ? 0.1230 0.1415 0.1460 0.0031  0.0057  0.0225  127 LEU   A C   
2656 O O   A LEU   A 127 ? 0.1330 0.1253 0.1558 -0.0195 -0.0059 0.0051  127 LEU   A O   
2657 O O   B LEU   A 127 ? 0.1277 0.1442 0.1526 0.0021  0.0137  0.0371  127 LEU   A O   
2658 C CB  A LEU   A 127 ? 0.1272 0.1373 0.1624 0.0013  0.0073  0.0057  127 LEU   A CB  
2659 C CB  B LEU   A 127 ? 0.1201 0.1504 0.1356 -0.0033 0.0070  0.0235  127 LEU   A CB  
2660 C CG  A LEU   A 127 ? 0.1323 0.1451 0.1748 0.0039  -0.0058 0.0182  127 LEU   A CG  
2661 C CG  B LEU   A 127 ? 0.1205 0.1592 0.1359 -0.0000 -0.0008 0.0197  127 LEU   A CG  
2662 C CD1 A LEU   A 127 ? 0.1362 0.1405 0.1849 0.0003  -0.0032 0.0159  127 LEU   A CD1 
2663 C CD1 B LEU   A 127 ? 0.1214 0.1655 0.1488 0.0034  -0.0005 0.0186  127 LEU   A CD1 
2664 C CD2 A LEU   A 127 ? 0.1436 0.1396 0.1919 0.0065  -0.0165 0.0197  127 LEU   A CD2 
2665 C CD2 B LEU   A 127 ? 0.1266 0.1631 0.1326 0.0003  -0.0127 0.0091  127 LEU   A CD2 
2688 N N   A SER   A 128 ? 0.1280 0.1249 0.1471 -0.0099 -0.0027 0.0142  128 SER   A N   
2689 N N   B SER   A 128 ? 0.1220 0.1412 0.1489 -0.0013 -0.0048 0.0164  128 SER   A N   
2690 C CA  A SER   A 128 ? 0.1437 0.1337 0.1451 -0.0079 0.0058  0.0139  128 SER   A CA  
2691 C CA  B SER   A 128 ? 0.1249 0.1384 0.1448 -0.0056 -0.0133 0.0114  128 SER   A CA  
2692 C C   A SER   A 128 ? 0.1489 0.1346 0.1519 -0.0024 0.0045  0.0204  128 SER   A C   
2693 C C   B SER   A 128 ? 0.1275 0.1298 0.1387 -0.0095 -0.0294 0.0162  128 SER   A C   
2694 O O   A SER   A 128 ? 0.1646 0.1473 0.1715 -0.0016 0.0074  0.0129  128 SER   A O   
2695 O O   B SER   A 128 ? 0.1284 0.1292 0.1473 -0.0078 -0.0371 0.0153  128 SER   A O   
2696 C CB  A SER   A 128 ? 0.1449 0.1415 0.1450 -0.0139 0.0049  0.0148  128 SER   A CB  
2697 C CB  B SER   A 128 ? 0.1222 0.1428 0.1432 -0.0068 -0.0136 0.0098  128 SER   A CB  
2698 O OG  A SER   A 128 ? 0.1490 0.1507 0.1584 -0.0085 0.0110  0.0169  128 SER   A OG  
2699 O OG  B SER   A 128 ? 0.1200 0.1475 0.1519 -0.0045 -0.0080 0.0106  128 SER   A OG  
2710 N N   A ALA   A 129 ? 0.1409 0.1432 0.1715 -0.0005 0.0016  0.0322  129 ALA   A N   
2711 N N   B ALA   A 129 ? 0.1303 0.1327 0.1423 -0.0093 -0.0285 0.0184  129 ALA   A N   
2712 C CA  A ALA   A 129 ? 0.1326 0.1440 0.1804 0.0001  0.0056  0.0412  129 ALA   A CA  
2713 C CA  B ALA   A 129 ? 0.1349 0.1325 0.1472 -0.0101 -0.0248 0.0198  129 ALA   A CA  
2714 C C   A ALA   A 129 ? 0.1357 0.1415 0.1771 0.0007  0.0056  0.0265  129 ALA   A C   
2715 C C   B ALA   A 129 ? 0.1424 0.1317 0.1602 -0.0111 -0.0234 0.0122  129 ALA   A C   
2716 O O   A ALA   A 129 ? 0.1379 0.1491 0.1666 -0.0017 0.0034  0.0284  129 ALA   A O   
2717 O O   B ALA   A 129 ? 0.1445 0.1336 0.1583 -0.0131 -0.0224 0.0110  129 ALA   A O   
2718 C CB  A ALA   A 129 ? 0.1354 0.1609 0.2005 0.0061  0.0050  0.0510  129 ALA   A CB  
2719 C CB  B ALA   A 129 ? 0.1349 0.1419 0.1451 -0.0070 -0.0243 0.0228  129 ALA   A CB  
2730 N N   A GLY   A 130 ? 0.1382 0.1373 0.2024 -0.0004 0.0127  0.0192  130 GLY   A N   
2731 N N   B GLY   A 130 ? 0.1467 0.1349 0.1694 -0.0079 -0.0178 0.0149  130 GLY   A N   
2732 C CA  A GLY   A 130 ? 0.1485 0.1391 0.1978 -0.0058 0.0076  0.0119  130 GLY   A CA  
2733 C CA  B GLY   A 130 ? 0.1510 0.1366 0.1753 -0.0061 -0.0165 0.0142  130 GLY   A CA  
2734 C C   A GLY   A 130 ? 0.1523 0.1338 0.1705 -0.0033 -0.0019 0.0125  130 GLY   A C   
2735 C C   B GLY   A 130 ? 0.1565 0.1348 0.1803 -0.0042 -0.0254 0.0200  130 GLY   A C   
2736 O O   A GLY   A 130 ? 0.1586 0.1325 0.1827 -0.0110 -0.0116 0.0059  130 GLY   A O   
2737 O O   B GLY   A 130 ? 0.1663 0.1343 0.1910 0.0056  -0.0380 0.0276  130 GLY   A O   
2744 N N   A ILE   A 131 ? 0.1570 0.1315 0.1647 -0.0029 -0.0058 0.0146  131 ILE   A N   
2745 N N   B ILE   A 131 ? 0.1519 0.1342 0.1768 -0.0117 -0.0221 0.0241  131 ILE   A N   
2746 C CA  A ILE   A 131 ? 0.1652 0.1350 0.1464 -0.0067 -0.0171 0.0077  131 ILE   A CA  
2747 C CA  B ILE   A 131 ? 0.1538 0.1363 0.1680 -0.0085 -0.0279 0.0218  131 ILE   A CA  
2748 C C   A ILE   A 131 ? 0.1592 0.1395 0.1461 -0.0102 -0.0097 0.0219  131 ILE   A C   
2749 C C   B ILE   A 131 ? 0.1556 0.1385 0.1551 -0.0134 -0.0267 0.0246  131 ILE   A C   
2750 O O   A ILE   A 131 ? 0.1655 0.1505 0.1688 -0.0046 -0.0112 0.0297  131 ILE   A O   
2751 O O   B ILE   A 131 ? 0.1641 0.1424 0.1599 -0.0166 -0.0183 0.0279  131 ILE   A O   
2752 C CB  A ILE   A 131 ? 0.1796 0.1482 0.1556 -0.0140 -0.0186 -0.0003 131 ILE   A CB  
2753 C CB  B ILE   A 131 ? 0.1495 0.1422 0.1730 -0.0012 -0.0391 0.0117  131 ILE   A CB  
2754 C CG1 A ILE   A 131 ? 0.1848 0.1802 0.1657 -0.0195 -0.0291 -0.0056 131 ILE   A CG1 
2755 C CG1 B ILE   A 131 ? 0.1488 0.1538 0.1769 0.0053  -0.0393 0.0042  131 ILE   A CG1 
2756 C CG2 A ILE   A 131 ? 0.1942 0.1398 0.1803 -0.0062 -0.0142 -0.0107 131 ILE   A CG2 
2757 C CG2 B ILE   A 131 ? 0.1456 0.1418 0.1725 -0.0025 -0.0365 0.0020  131 ILE   A CG2 
2758 C CD1 A ILE   A 131 ? 0.1899 0.1973 0.1973 -0.0201 -0.0314 -0.0149 131 ILE   A CD1 
2759 C CD1 B ILE   A 131 ? 0.1501 0.1578 0.1790 0.0090  -0.0393 -0.0056 131 ILE   A CD1 
2782 N N   A PHE   A 132 ? 0.1563 0.1391 0.1496 -0.0069 0.0017  0.0199  132 PHE   A N   
2783 N N   B PHE   A 132 ? 0.1524 0.1379 0.1541 -0.0064 -0.0241 0.0188  132 PHE   A N   
2784 C CA  A PHE   A 132 ? 0.1551 0.1475 0.1338 -0.0108 0.0063  0.0147  132 PHE   A CA  
2785 C CA  B PHE   A 132 ? 0.1533 0.1391 0.1598 -0.0076 -0.0225 0.0151  132 PHE   A CA  
2786 C C   A PHE   A 132 ? 0.1547 0.1639 0.1370 -0.0136 0.0045  0.0105  132 PHE   A C   
2787 C C   B PHE   A 132 ? 0.1590 0.1519 0.1725 -0.0066 -0.0188 0.0097  132 PHE   A C   
2788 O O   A PHE   A 132 ? 0.1597 0.1766 0.1472 -0.0222 0.0007  0.0128  132 PHE   A O   
2789 O O   B PHE   A 132 ? 0.1651 0.1637 0.1810 -0.0101 -0.0043 0.0160  132 PHE   A O   
2790 C CB  A PHE   A 132 ? 0.1510 0.1420 0.1378 -0.0093 0.0005  0.0150  132 PHE   A CB  
2791 C CB  B PHE   A 132 ? 0.1462 0.1307 0.1472 -0.0106 -0.0181 0.0249  132 PHE   A CB  
2792 C CG  A PHE   A 132 ? 0.1554 0.1434 0.1454 -0.0023 0.0042  0.0141  132 PHE   A CG  
2793 C CG  B PHE   A 132 ? 0.1466 0.1321 0.1450 -0.0085 -0.0206 0.0197  132 PHE   A CG  
2794 C CD1 A PHE   A 132 ? 0.1572 0.1560 0.1714 0.0023  0.0051  -0.0055 132 PHE   A CD1 
2795 C CD1 B PHE   A 132 ? 0.1472 0.1399 0.1583 -0.0030 -0.0194 0.0109  132 PHE   A CD1 
2796 C CD2 A PHE   A 132 ? 0.1547 0.1535 0.1576 -0.0027 0.0060  0.0077  132 PHE   A CD2 
2797 C CD2 B PHE   A 132 ? 0.1456 0.1407 0.1534 -0.0060 -0.0299 0.0108  132 PHE   A CD2 
2798 C CE1 A PHE   A 132 ? 0.1605 0.1573 0.1820 -0.0030 -0.0027 -0.0109 132 PHE   A CE1 
2799 C CE1 B PHE   A 132 ? 0.1481 0.1442 0.1637 -0.0027 -0.0288 0.0048  132 PHE   A CE1 
2800 C CE2 A PHE   A 132 ? 0.1517 0.1533 0.1684 0.0037  -0.0001 0.0077  132 PHE   A CE2 
2801 C CE2 B PHE   A 132 ? 0.1417 0.1459 0.1609 -0.0012 -0.0357 0.0101  132 PHE   A CE2 
2802 C CZ  A PHE   A 132 ? 0.1525 0.1534 0.1791 -0.0092 -0.0043 0.0040  132 PHE   A CZ  
2803 C CZ  B PHE   A 132 ? 0.1443 0.1463 0.1672 -0.0055 -0.0378 0.0056  132 PHE   A CZ  
2822 N N   A GLY   A 133 ? 0.1617 0.1684 0.1279 -0.0084 -0.0097 0.0168  133 GLY   A N   
2823 N N   B GLY   A 133 ? 0.1617 0.1523 0.1672 -0.0062 -0.0224 0.0080  133 GLY   A N   
2824 C CA  A GLY   A 133 ? 0.1716 0.1808 0.1447 -0.0122 -0.0203 0.0104  133 GLY   A CA  
2825 C CA  B GLY   A 133 ? 0.1673 0.1571 0.1624 -0.0054 -0.0238 0.0023  133 GLY   A CA  
2826 C C   A GLY   A 133 ? 0.1812 0.1893 0.1583 -0.0170 -0.0400 0.0026  133 GLY   A C   
2827 C C   B GLY   A 133 ? 0.1706 0.1641 0.1612 -0.0015 -0.0273 -0.0074 133 GLY   A C   
2828 O O   A GLY   A 133 ? 0.1991 0.2047 0.1769 -0.0161 -0.0363 -0.0189 133 GLY   A O   
2829 O O   B GLY   A 133 ? 0.1730 0.1719 0.1533 0.0045  -0.0249 -0.0231 133 GLY   A O   
2836 N N   A ALA   A 134 ? 0.1802 0.1775 0.1575 -0.0241 -0.0316 0.0011  134 ALA   A N   
2837 N N   B ALA   A 134 ? 0.1739 0.1606 0.1672 -0.0039 -0.0217 -0.0087 134 ALA   A N   
2838 C CA  A ALA   A 134 ? 0.1780 0.1739 0.1812 -0.0217 -0.0240 0.0031  134 ALA   A CA  
2839 C CA  B ALA   A 134 ? 0.1752 0.1582 0.1783 -0.0044 -0.0146 -0.0092 134 ALA   A CA  
2840 C C   A ALA   A 134 ? 0.1776 0.1732 0.1761 -0.0217 -0.0213 0.0033  134 ALA   A C   
2841 C C   B ALA   A 134 ? 0.1759 0.1551 0.1779 -0.0046 -0.0156 -0.0121 134 ALA   A C   
2842 O O   A ALA   A 134 ? 0.1861 0.1809 0.1931 -0.0239 -0.0164 -0.0029 134 ALA   A O   
2843 O O   B ALA   A 134 ? 0.1769 0.1558 0.1871 -0.0083 -0.0083 -0.0196 134 ALA   A O   
2844 C CB  A ALA   A 134 ? 0.1853 0.1710 0.2124 -0.0176 -0.0219 -0.0038 134 ALA   A CB  
2845 C CB  B ALA   A 134 ? 0.1757 0.1563 0.1906 -0.0052 -0.0143 -0.0101 134 ALA   A CB  
2856 N N   A ASP   A 135 ? 0.1798 0.1658 0.1819 -0.0188 -0.0182 0.0086  135 ASP   A N   
2857 N N   B ASP   A 135 ? 0.1805 0.1574 0.1782 -0.0075 -0.0227 -0.0050 135 ASP   A N   
2858 C CA  A ASP   A 135 ? 0.1797 0.1702 0.2041 -0.0223 -0.0282 0.0044  135 ASP   A CA  
2859 C CA  B ASP   A 135 ? 0.1800 0.1587 0.1816 -0.0083 -0.0303 -0.0060 135 ASP   A CA  
2860 C C   A ASP   A 135 ? 0.1654 0.1587 0.2080 -0.0130 -0.0196 0.0116  135 ASP   A C   
2861 C C   B ASP   A 135 ? 0.1660 0.1482 0.1770 -0.0032 -0.0220 -0.0073 135 ASP   A C   
2862 O O   A ASP   A 135 ? 0.1586 0.1517 0.2154 -0.0069 -0.0136 0.0228  135 ASP   A O   
2863 O O   B ASP   A 135 ? 0.1636 0.1409 0.1780 -0.0035 -0.0183 -0.0009 135 ASP   A O   
2864 C CB  A ASP   A 135 ? 0.2057 0.1990 0.2437 -0.0384 -0.0431 -0.0024 135 ASP   A CB  
2865 C CB  B ASP   A 135 ? 0.1899 0.1718 0.1845 -0.0111 -0.0449 -0.0085 135 ASP   A CB  
2866 C CG  A ASP   A 135 ? 0.2268 0.2244 0.2805 -0.0558 -0.0489 -0.0029 135 ASP   A CG  
2867 C CG  B ASP   A 135 ? 0.1989 0.1881 0.2039 -0.0123 -0.0507 -0.0044 135 ASP   A CG  
2868 O OD1 A ASP   A 135 ? 0.2210 0.2312 0.2771 -0.0643 -0.0535 0.0147  135 ASP   A OD1 
2869 O OD1 B ASP   A 135 ? 0.2003 0.1906 0.2119 -0.0083 -0.0514 -0.0043 135 ASP   A OD1 
2870 O OD2 A ASP   A 135 ? 0.2525 0.2464 0.3235 -0.0593 -0.0357 -0.0059 135 ASP   A OD2 
2871 O OD2 B ASP   A 135 ? 0.2058 0.1987 0.2199 -0.0162 -0.0549 -0.0031 135 ASP   A OD2 
2880 N N   A PRO   A 136 ? 0.1567 0.1540 0.2156 -0.0025 -0.0134 0.0186  136 PRO   A N   
2881 N N   B PRO   A 136 ? 0.1579 0.1413 0.1730 0.0024  -0.0117 -0.0153 136 PRO   A N   
2882 C CA  A PRO   A 136 ? 0.1495 0.1578 0.2314 -0.0074 -0.0093 0.0052  136 PRO   A CA  
2883 C CA  B PRO   A 136 ? 0.1546 0.1489 0.1747 -0.0012 -0.0007 -0.0221 136 PRO   A CA  
2884 C C   A PRO   A 136 ? 0.1280 0.1566 0.2303 -0.0031 -0.0040 0.0055  136 PRO   A C   
2885 C C   B PRO   A 136 ? 0.1473 0.1563 0.1690 0.0003  0.0042  -0.0150 136 PRO   A C   
2886 O O   A PRO   A 136 ? 0.1221 0.1628 0.2290 -0.0115 0.0012  0.0079  136 PRO   A O   
2887 O O   B PRO   A 136 ? 0.1438 0.1518 0.1492 0.0079  0.0217  -0.0133 136 PRO   A O   
2888 C CB  A PRO   A 136 ? 0.1679 0.1617 0.2431 -0.0049 -0.0071 0.0030  136 PRO   A CB  
2889 C CB  B PRO   A 136 ? 0.1631 0.1473 0.1820 0.0017  0.0014  -0.0272 136 PRO   A CB  
2890 C CG  A PRO   A 136 ? 0.1754 0.1605 0.2542 0.0017  -0.0078 0.0037  136 PRO   A CG  
2891 C CG  B PRO   A 136 ? 0.1675 0.1455 0.1838 0.0062  -0.0003 -0.0282 136 PRO   A CG  
2892 C CD  A PRO   A 136 ? 0.1674 0.1551 0.2367 0.0074  -0.0126 0.0195  136 PRO   A CD  
2893 C CD  B PRO   A 136 ? 0.1603 0.1391 0.1774 0.0058  -0.0031 -0.0164 136 PRO   A CD  
2908 N N   A ILE   A 137 ? 0.1295 0.1504 0.2392 -0.0022 -0.0135 0.0179  137 ILE   A N   
2909 N N   B ILE   A 137 ? 0.1502 0.1611 0.1838 -0.0044 -0.0042 -0.0114 137 ILE   A N   
2910 C CA  A ILE   A 137 ? 0.1332 0.1522 0.2408 -0.0122 -0.0200 0.0271  137 ILE   A CA  
2911 C CA  B ILE   A 137 ? 0.1518 0.1680 0.1903 -0.0033 -0.0027 -0.0092 137 ILE   A CA  
2912 C C   A ILE   A 137 ? 0.1368 0.1530 0.2254 -0.0191 -0.0202 0.0237  137 ILE   A C   
2913 C C   B ILE   A 137 ? 0.1460 0.1737 0.1828 -0.0067 0.0078  -0.0058 137 ILE   A C   
2914 O O   A ILE   A 137 ? 0.1460 0.1498 0.2318 -0.0151 -0.0130 0.0214  137 ILE   A O   
2915 O O   B ILE   A 137 ? 0.1416 0.1758 0.1822 -0.0055 0.0153  -0.0090 137 ILE   A O   
2916 C CB  A ILE   A 137 ? 0.1394 0.1670 0.2658 -0.0177 -0.0317 0.0281  137 ILE   A CB  
2917 C CB  B ILE   A 137 ? 0.1592 0.1646 0.2063 -0.0016 -0.0115 -0.0075 137 ILE   A CB  
2918 C CG1 A ILE   A 137 ? 0.1503 0.1918 0.2974 -0.0159 -0.0354 0.0370  137 ILE   A CG1 
2919 C CG1 B ILE   A 137 ? 0.1693 0.1683 0.2294 0.0026  -0.0238 -0.0031 137 ILE   A CG1 
2920 C CG2 A ILE   A 137 ? 0.1462 0.1681 0.2718 -0.0189 -0.0310 0.0161  137 ILE   A CG2 
2921 C CG2 B ILE   A 137 ? 0.1617 0.1598 0.2051 0.0006  -0.0115 -0.0082 137 ILE   A CG2 
2922 C CD1 A ILE   A 137 ? 0.1685 0.2045 0.3194 -0.0101 -0.0298 0.0411  137 ILE   A CD1 
2923 C CD1 B ILE   A 137 ? 0.1779 0.1688 0.2455 0.0016  -0.0282 0.0030  137 ILE   A CD1 
2946 N N   A HIS   A 138 ? 0.1370 0.1657 0.2143 -0.0126 -0.0144 0.0223  138 HIS   A N   
2947 N N   B HIS   A 138 ? 0.1448 0.1789 0.1848 -0.0079 0.0127  0.0003  138 HIS   A N   
2948 C CA  A HIS   A 138 ? 0.1428 0.1766 0.2060 -0.0135 -0.0035 0.0225  138 HIS   A CA  
2949 C CA  B HIS   A 138 ? 0.1448 0.1754 0.1866 -0.0071 0.0134  0.0075  138 HIS   A CA  
2950 C C   A HIS   A 138 ? 0.1337 0.1726 0.2012 -0.0128 -0.0043 0.0229  138 HIS   A C   
2951 C C   B HIS   A 138 ? 0.1380 0.1705 0.1909 -0.0079 0.0093  0.0216  138 HIS   A C   
2952 O O   A HIS   A 138 ? 0.1409 0.1790 0.2018 -0.0162 -0.0036 0.0195  138 HIS   A O   
2953 O O   B HIS   A 138 ? 0.1423 0.1728 0.1918 -0.0107 0.0128  0.0261  138 HIS   A O   
2954 C CB  A HIS   A 138 ? 0.1593 0.1961 0.2061 -0.0118 -0.0131 0.0203  138 HIS   A CB  
2955 C CB  B HIS   A 138 ? 0.1473 0.1775 0.1864 0.0013  0.0144  -0.0070 138 HIS   A CB  
2956 C CG  A HIS   A 138 ? 0.1811 0.2083 0.2081 -0.0186 -0.0139 0.0063  138 HIS   A CG  
2957 C CG  B HIS   A 138 ? 0.1538 0.1775 0.1888 0.0036  0.0103  -0.0234 138 HIS   A CG  
2958 N ND1 A HIS   A 138 ? 0.1960 0.2165 0.2313 -0.0202 -0.0097 0.0001  138 HIS   A ND1 
2959 N ND1 B HIS   A 138 ? 0.1623 0.1804 0.2043 0.0051  0.0050  -0.0285 138 HIS   A ND1 
2960 C CD2 A HIS   A 138 ? 0.1871 0.2149 0.2046 -0.0169 -0.0063 0.0040  138 HIS   A CD2 
2961 C CD2 B HIS   A 138 ? 0.1527 0.1749 0.1887 0.0063  0.0091  -0.0257 138 HIS   A CD2 
2962 C CE1 A HIS   A 138 ? 0.2041 0.2234 0.2315 -0.0108 -0.0095 0.0013  138 HIS   A CE1 
2963 C CE1 B HIS   A 138 ? 0.1629 0.1789 0.2051 0.0078  0.0017  -0.0283 138 HIS   A CE1 
2964 N NE2 A HIS   A 138 ? 0.1966 0.2238 0.2125 -0.0085 0.0013  -0.0011 138 HIS   A NE2 
2965 N NE2 B HIS   A 138 ? 0.1583 0.1765 0.2003 0.0089  0.0060  -0.0300 138 HIS   A NE2 
2980 N N   . SER   A 139 ? 0.1318 0.1640 0.2015 -0.0095 -0.0068 0.0290  139 SER   A N   
2981 C CA  . SER   A 139 ? 0.1299 0.1597 0.2031 -0.0119 -0.0005 0.0350  139 SER   A CA  
2982 C C   . SER   A 139 ? 0.1248 0.1501 0.2045 -0.0083 0.0032  0.0210  139 SER   A C   
2983 O O   . SER   A 139 ? 0.1183 0.1493 0.2107 -0.0139 0.0015  0.0268  139 SER   A O   
2984 C CB  . SER   A 139 ? 0.1263 0.1564 0.1986 -0.0172 -0.0062 0.0364  139 SER   A CB  
2985 O OG  . SER   A 139 ? 0.1356 0.1565 0.1958 -0.0187 -0.0103 0.0362  139 SER   A OG  
2992 N N   . LEU   A 140 ? 0.1218 0.1556 0.1903 -0.0096 -0.0028 0.0350  140 LEU   A N   
2993 C CA  . LEU   A 140 ? 0.1204 0.1521 0.1878 -0.0126 0.0026  0.0306  140 LEU   A CA  
2994 C C   . LEU   A 140 ? 0.1150 0.1581 0.1935 -0.0177 -0.0007 0.0323  140 LEU   A C   
2995 O O   . LEU   A 140 ? 0.1253 0.1575 0.2201 -0.0127 -0.0031 0.0353  140 LEU   A O   
2996 C CB  . LEU   A 140 ? 0.1243 0.1614 0.2061 -0.0175 0.0019  0.0332  140 LEU   A CB  
2997 C CG  . LEU   A 140 ? 0.1290 0.1749 0.2055 -0.0230 0.0033  0.0471  140 LEU   A CG  
2998 C CD1 . LEU   A 140 ? 0.1346 0.1808 0.2106 -0.0163 0.0025  0.0440  140 LEU   A CD1 
2999 C CD2 . LEU   A 140 ? 0.1301 0.1929 0.2253 -0.0186 0.0089  0.0490  140 LEU   A CD2 
3011 N N   . ARG   A 141 ? 0.1205 0.1572 0.2037 -0.0155 -0.0045 0.0294  141 ARG   A N   
3012 C CA  . ARG   A 141 ? 0.1386 0.1676 0.2224 -0.0228 -0.0096 0.0127  141 ARG   A CA  
3013 C C   . ARG   A 141 ? 0.1409 0.1545 0.2145 -0.0199 -0.0081 0.0140  141 ARG   A C   
3014 O O   . ARG   A 141 ? 0.1373 0.1510 0.2319 -0.0187 0.0033  0.0174  141 ARG   A O   
3015 C CB  . ARG   A 141 ? 0.1505 0.1937 0.2496 -0.0285 -0.0105 -0.0059 141 ARG   A CB  
3016 C CG  . ARG   A 141 ? 0.1881 0.2276 0.2857 -0.0331 0.0032  -0.0153 141 ARG   A CG  
3017 C CD  . ARG   A 141 ? 0.2175 0.2524 0.3134 -0.0419 0.0031  -0.0242 141 ARG   A CD  
3018 N NE  . ARG   A 141 ? 0.2098 0.2750 0.3271 -0.0451 -0.0096 -0.0216 141 ARG   A NE  
3019 C CZ  . ARG   A 141 ? 0.2126 0.2981 0.3341 -0.0549 0.0019  -0.0070 141 ARG   A CZ  
3020 N NH1 . ARG   A 141 ? 0.2018 0.3031 0.3201 -0.0673 0.0199  -0.0223 141 ARG   A NH1 
3021 N NH2 . ARG   A 141 ? 0.2194 0.3116 0.3534 -0.0472 -0.0117 0.0072  141 ARG   A NH2 
3035 N N   . VAL   A 142 ? 0.1331 0.1516 0.2018 -0.0161 -0.0037 0.0090  142 VAL   A N   
3036 C CA  . VAL   A 142 ? 0.1340 0.1458 0.1980 -0.0124 0.0123  0.0063  142 VAL   A CA  
3037 C C   . VAL   A 142 ? 0.1198 0.1417 0.1960 -0.0162 0.0095  0.0092  142 VAL   A C   
3038 O O   . VAL   A 142 ? 0.1267 0.1462 0.2110 -0.0041 0.0050  0.0163  142 VAL   A O   
3039 C CB  . VAL   A 142 ? 0.1399 0.1567 0.1985 -0.0152 0.0109  0.0122  142 VAL   A CB  
3040 C CG1 . VAL   A 142 ? 0.1397 0.1534 0.1979 -0.0192 0.0178  0.0128  142 VAL   A CG1 
3041 C CG2 . VAL   A 142 ? 0.1529 0.1706 0.2217 -0.0057 0.0105  0.0146  142 VAL   A CG2 
3051 N N   . CYS   A 143 ? 0.1249 0.1406 0.1841 -0.0170 0.0072  0.0112  143 CYS   A N   
3052 C CA  . CYS   A 143 ? 0.1241 0.1433 0.1970 -0.0150 0.0100  0.0214  143 CYS   A CA  
3053 C C   . CYS   A 143 ? 0.1226 0.1466 0.2037 -0.0161 0.0038  0.0305  143 CYS   A C   
3054 O O   . CYS   A 143 ? 0.1190 0.1466 0.2049 -0.0107 0.0025  0.0299  143 CYS   A O   
3055 C CB  . CYS   A 143 ? 0.1345 0.1465 0.1989 -0.0132 0.0133  0.0259  143 CYS   A CB  
3056 S SG  . CYS   A 143 ? 0.1507 0.1534 0.1853 -0.0013 0.0097  0.0178  143 CYS   A SG  
3062 N N   . VAL   A 144 ? 0.1218 0.1486 0.2311 -0.0158 0.0079  0.0376  144 VAL   A N   
3063 C CA  . VAL   A 144 ? 0.1295 0.1576 0.2564 -0.0188 0.0182  0.0397  144 VAL   A CA  
3064 C C   . VAL   A 144 ? 0.1362 0.1481 0.2465 -0.0237 -0.0074 0.0310  144 VAL   A C   
3065 O O   . VAL   A 144 ? 0.1560 0.1493 0.2460 -0.0123 -0.0160 0.0336  144 VAL   A O   
3066 C CB  . VAL   A 144 ? 0.1528 0.1826 0.3136 -0.0039 0.0308  0.0476  144 VAL   A CB  
3067 C CG1 . VAL   A 144 ? 0.1694 0.2003 0.3547 -0.0146 0.0114  0.0531  144 VAL   A CG1 
3068 C CG2 . VAL   A 144 ? 0.1333 0.1871 0.3165 -0.0042 0.0398  0.0593  144 VAL   A CG2 
3078 N N   . ASP   A 145 ? 0.1380 0.1405 0.2540 -0.0227 -0.0051 0.0252  145 ASP   A N   
3079 C CA  . ASP   A 145 ? 0.1508 0.1433 0.2578 -0.0224 -0.0030 0.0097  145 ASP   A CA  
3080 C C   . ASP   A 145 ? 0.1494 0.1382 0.2558 -0.0149 0.0001  0.0071  145 ASP   A C   
3081 O O   . ASP   A 145 ? 0.1623 0.1458 0.3062 -0.0143 -0.0059 -0.0225 145 ASP   A O   
3082 C CB  . ASP   A 145 ? 0.1643 0.1738 0.2736 -0.0289 -0.0166 0.0073  145 ASP   A CB  
3083 C CG  . ASP   A 145 ? 0.1843 0.2155 0.2911 -0.0432 -0.0346 0.0198  145 ASP   A CG  
3084 O OD1 . ASP   A 145 ? 0.1728 0.2310 0.3024 -0.0530 -0.0204 0.0257  145 ASP   A OD1 
3085 O OD2 . ASP   A 145 ? 0.2043 0.2380 0.2953 -0.0548 -0.0516 0.0220  145 ASP   A OD2 
3090 N N   . THR   A 146 ? 0.1355 0.1363 0.2196 -0.0175 0.0038  0.0126  146 THR   A N   
3091 C CA  . THR   A 146 ? 0.1316 0.1304 0.2122 -0.0129 -0.0018 0.0068  146 THR   A CA  
3092 C C   . THR   A 146 ? 0.1223 0.1246 0.2199 -0.0054 0.0090  0.0180  146 THR   A C   
3093 O O   . THR   A 146 ? 0.1385 0.1431 0.2297 0.0027  -0.0044 0.0168  146 THR   A O   
3094 C CB  . THR   A 146 ? 0.1270 0.1304 0.2105 -0.0095 0.0003  0.0143  146 THR   A CB  
3095 O OG1 . THR   A 146 ? 0.1270 0.1523 0.2144 -0.0036 -0.0003 0.0106  146 THR   A OG1 
3096 C CG2 . THR   A 146 ? 0.1364 0.1329 0.2284 -0.0080 0.0081  0.0149  146 THR   A CG2 
3104 N N   . VAL   A 147 ? 0.1215 0.1340 0.2155 -0.0000 0.0094  0.0204  147 VAL   A N   
3105 C CA  . VAL   A 147 ? 0.1238 0.1378 0.2136 -0.0080 0.0199  0.0268  147 VAL   A CA  
3106 C C   . VAL   A 147 ? 0.1252 0.1331 0.2224 -0.0139 0.0150  0.0324  147 VAL   A C   
3107 O O   . VAL   A 147 ? 0.1294 0.1412 0.2349 -0.0157 0.0053  0.0358  147 VAL   A O   
3108 C CB  . VAL   A 147 ? 0.1370 0.1372 0.2012 -0.0148 0.0210  0.0248  147 VAL   A CB  
3109 C CG1 . VAL   A 147 ? 0.1640 0.1446 0.2027 -0.0095 0.0189  0.0360  147 VAL   A CG1 
3110 C CG2 . VAL   A 147 ? 0.1479 0.1372 0.2035 -0.0177 0.0131  0.0236  147 VAL   A CG2 
3120 N N   . ARG   A 148 ? 0.1285 0.1377 0.2289 -0.0153 0.0184  0.0439  148 ARG   A N   
3121 C CA  . ARG   A 148 ? 0.1359 0.1406 0.2240 -0.0167 0.0060  0.0428  148 ARG   A CA  
3122 C C   . ARG   A 148 ? 0.1445 0.1403 0.2229 -0.0196 0.0063  0.0580  148 ARG   A C   
3123 O O   . ARG   A 148 ? 0.1733 0.1523 0.2513 -0.0247 0.0141  0.0528  148 ARG   A O   
3124 C CB  . ARG   A 148 ? 0.1432 0.1383 0.2343 -0.0051 0.0250  0.0431  148 ARG   A CB  
3125 C CG  . ARG   A 148 ? 0.1598 0.1381 0.2732 -0.0116 0.0332  0.0330  148 ARG   A CG  
3126 C CD  . ARG   A 148 ? 0.1724 0.1390 0.2976 -0.0082 0.0403  0.0490  148 ARG   A CD  
3127 N NE  . ARG   A 148 ? 0.1653 0.1460 0.2942 0.0052  0.0434  0.0488  148 ARG   A NE  
3128 C CZ  . ARG   A 148 ? 0.1634 0.1298 0.2807 -0.0030 0.0345  0.0401  148 ARG   A CZ  
3129 N NH1 . ARG   A 148 ? 0.1718 0.1358 0.2900 -0.0127 0.0372  0.0209  148 ARG   A NH1 
3130 N NH2 . ARG   A 148 ? 0.1559 0.1494 0.2764 0.0074  0.0433  0.0398  148 ARG   A NH2 
3144 N N   . THR   A 149 ? 0.1440 0.1510 0.2123 -0.0182 -0.0082 0.0493  149 THR   A N   
3145 C CA  . THR   A 149 ? 0.1483 0.1571 0.2161 -0.0192 -0.0034 0.0506  149 THR   A CA  
3146 C C   . THR   A 149 ? 0.1432 0.1530 0.2060 -0.0234 -0.0026 0.0583  149 THR   A C   
3147 O O   . THR   A 149 ? 0.1437 0.1634 0.2164 -0.0225 0.0012  0.0494  149 THR   A O   
3148 C CB  . THR   A 149 ? 0.1450 0.1717 0.2212 -0.0221 -0.0026 0.0443  149 THR   A CB  
3149 O OG1 . THR   A 149 ? 0.1481 0.1574 0.2400 -0.0287 -0.0010 0.0425  149 THR   A OG1 
3150 C CG2 . THR   A 149 ? 0.1451 0.1865 0.2303 -0.0158 -0.0096 0.0416  149 THR   A CG2 
3158 N N   . ASN   A 150 ? 0.1445 0.1580 0.2113 -0.0176 -0.0067 0.0590  150 ASN   A N   
3159 C CA  . ASN   A 150 ? 0.1576 0.1667 0.2050 -0.0174 0.0042  0.0483  150 ASN   A CA  
3160 C C   . ASN   A 150 ? 0.1361 0.1581 0.2067 -0.0246 -0.0028 0.0442  150 ASN   A C   
3161 O O   . ASN   A 150 ? 0.1488 0.1714 0.2378 -0.0189 -0.0152 0.0407  150 ASN   A O   
3162 C CB  . ASN   A 150 ? 0.2003 0.1882 0.2265 -0.0233 0.0287  0.0682  150 ASN   A CB  
3163 C CG  . ASN   A 150 ? 0.2576 0.2203 0.2911 -0.0212 0.0109  0.0702  150 ASN   A CG  
3164 O OD1 . ASN   A 150 ? 0.2828 0.2277 0.3157 -0.0262 0.0100  0.0841  150 ASN   A OD1 
3165 N ND2 . ASN   A 150 ? 0.2875 0.2431 0.3272 -0.0117 0.0006  0.0677  150 ASN   A ND2 
3172 N N   . VAL   A 151 ? 0.1434 0.1463 0.2051 -0.0227 -0.0019 0.0439  151 VAL   A N   
3173 C CA  . VAL   A 151 ? 0.1475 0.1511 0.1954 -0.0244 0.0005  0.0428  151 VAL   A CA  
3174 C C   . VAL   A 151 ? 0.1361 0.1446 0.2088 -0.0316 0.0039  0.0454  151 VAL   A C   
3175 O O   . VAL   A 151 ? 0.1481 0.1517 0.2378 -0.0260 0.0050  0.0406  151 VAL   A O   
3176 C CB  . VAL   A 151 ? 0.1731 0.1658 0.1975 -0.0109 0.0072  0.0367  151 VAL   A CB  
3177 C CG1 . VAL   A 151 ? 0.1719 0.1841 0.2230 -0.0082 0.0041  0.0361  151 VAL   A CG1 
3178 C CG2 . VAL   A 151 ? 0.1840 0.1637 0.1929 -0.0085 0.0227  0.0380  151 VAL   A CG2 
3188 N N   . TYR   A 152 ? 0.1331 0.1462 0.2068 -0.0273 0.0041  0.0440  152 TYR   A N   
3189 C CA  . TYR   A 152 ? 0.1349 0.1525 0.1883 -0.0246 0.0072  0.0401  152 TYR   A CA  
3190 C C   . TYR   A 152 ? 0.1308 0.1455 0.1777 -0.0216 0.0140  0.0418  152 TYR   A C   
3191 O O   . TYR   A 152 ? 0.1448 0.1442 0.1823 -0.0272 0.0140  0.0342  152 TYR   A O   
3192 C CB  . TYR   A 152 ? 0.1549 0.1619 0.1925 -0.0227 0.0141  0.0462  152 TYR   A CB  
3193 C CG  . TYR   A 152 ? 0.1623 0.1848 0.1869 -0.0283 0.0211  0.0465  152 TYR   A CG  
3194 C CD1 . TYR   A 152 ? 0.1754 0.2062 0.2088 -0.0176 0.0227  0.0531  152 TYR   A CD1 
3195 C CD2 . TYR   A 152 ? 0.1683 0.1948 0.1813 -0.0398 0.0106  0.0379  152 TYR   A CD2 
3196 C CE1 . TYR   A 152 ? 0.2077 0.2178 0.2073 -0.0137 0.0066  0.0614  152 TYR   A CE1 
3197 C CE2 . TYR   A 152 ? 0.1942 0.2082 0.1908 -0.0427 0.0139  0.0479  152 TYR   A CE2 
3198 C CZ  . TYR   A 152 ? 0.2219 0.2129 0.1897 -0.0290 0.0072  0.0704  152 TYR   A CZ  
3199 O OH  . TYR   A 152 ? 0.2536 0.2313 0.2164 -0.0239 0.0116  0.0838  152 TYR   A OH  
3209 N N   A LEU   A 153 ? 0.1308 0.1421 0.1866 -0.0231 0.0158  0.0444  153 LEU   A N   
3210 N N   B LEU   A 153 ? 0.1356 0.1525 0.1615 -0.0188 0.0114  0.0400  153 LEU   A N   
3211 C CA  A LEU   A 153 ? 0.1232 0.1364 0.2002 -0.0127 0.0214  0.0375  153 LEU   A CA  
3212 C CA  B LEU   A 153 ? 0.1342 0.1544 0.1500 -0.0067 0.0136  0.0342  153 LEU   A CA  
3213 C C   A LEU   A 153 ? 0.1319 0.1380 0.2051 -0.0126 0.0326  0.0312  153 LEU   A C   
3214 C C   B LEU   A 153 ? 0.1382 0.1605 0.1437 0.0015  0.0195  0.0287  153 LEU   A C   
3215 O O   A LEU   A 153 ? 0.1375 0.1476 0.2250 -0.0180 0.0423  0.0335  153 LEU   A O   
3216 O O   B LEU   A 153 ? 0.1390 0.1666 0.1527 0.0044  0.0283  0.0274  153 LEU   A O   
3217 C CB  A LEU   A 153 ? 0.1192 0.1326 0.2090 -0.0142 0.0123  0.0319  153 LEU   A CB  
3218 C CB  B LEU   A 153 ? 0.1343 0.1539 0.1522 -0.0024 0.0063  0.0398  153 LEU   A CB  
3219 C CG  A LEU   A 153 ? 0.1193 0.1358 0.2068 -0.0153 0.0191  0.0238  153 LEU   A CG  
3220 C CG  B LEU   A 153 ? 0.1397 0.1577 0.1555 0.0025  0.0010  0.0367  153 LEU   A CG  
3221 C CD1 A LEU   A 153 ? 0.1304 0.1311 0.2084 -0.0086 0.0062  0.0326  153 LEU   A CD1 
3222 C CD1 B LEU   A 153 ? 0.1455 0.1572 0.1735 0.0051  -0.0008 0.0389  153 LEU   A CD1 
3223 C CD2 A LEU   A 153 ? 0.1290 0.1394 0.1910 -0.0190 0.0199  0.0058  153 LEU   A CD2 
3224 C CD2 B LEU   A 153 ? 0.1425 0.1640 0.1518 0.0029  -0.0021 0.0297  153 LEU   A CD2 
3247 N N   A ALA   A 154 ? 0.1280 0.1279 0.2025 -0.0144 0.0305  0.0375  154 ALA   A N   
3248 N N   B ALA   A 154 ? 0.1373 0.1601 0.1243 0.0024  0.0215  0.0241  154 ALA   A N   
3249 C CA  A ALA   A 154 ? 0.1433 0.1351 0.1971 -0.0087 0.0351  0.0325  154 ALA   A CA  
3250 C CA  B ALA   A 154 ? 0.1440 0.1633 0.1364 0.0056  0.0159  0.0168  154 ALA   A CA  
3251 C C   A ALA   A 154 ? 0.1331 0.1274 0.1846 -0.0050 0.0279  0.0322  154 ALA   A C   
3252 C C   B ALA   A 154 ? 0.1451 0.1664 0.1339 0.0067  0.0019  0.0247  154 ALA   A C   
3253 O O   A ALA   A 154 ? 0.1402 0.1446 0.1870 -0.0155 0.0243  0.0268  154 ALA   A O   
3254 O O   B ALA   A 154 ? 0.1485 0.1689 0.1203 -0.0027 -0.0074 0.0226  154 ALA   A O   
3255 C CB  A ALA   A 154 ? 0.1572 0.1408 0.1912 0.0054  0.0342  0.0260  154 ALA   A CB  
3256 C CB  B ALA   A 154 ? 0.1427 0.1633 0.1441 0.0081  0.0128  0.0103  154 ALA   A CB  
3267 N N   A VAL   A 155 ? 0.1008 0.0995 0.1513 0.0019  0.0403  0.0513  155 VAL   A N   
3268 N N   B VAL   A 155 ? 0.1395 0.1607 0.1380 0.0164  0.0035  0.0410  155 VAL   A N   
3269 C CA  A VAL   A 155 ? 0.1165 0.1253 0.1986 0.0013  0.0286  0.0490  155 VAL   A CA  
3270 C CA  B VAL   A 155 ? 0.1618 0.1867 0.1869 0.0186  -0.0033 0.0359  155 VAL   A CA  
3271 C CA  T VAL   A 155 ? 0.1642 0.1592 0.2217 -0.0150 0.0398  0.0537  155 VAL   A CA  
3272 C C   A VAL   A 155 ? 0.1303 0.1404 0.2218 0.0184  0.0287  0.0512  155 VAL   A C   
3273 C C   B VAL   A 155 ? 0.1819 0.2031 0.2249 0.0256  0.0013  0.0391  155 VAL   A C   
3274 C C   T VAL   A 155 ? 0.1715 0.1619 0.2007 0.0044  0.0482  0.0590  155 VAL   A C   
3275 O O   A VAL   A 155 ? 0.1310 0.1490 0.2481 0.0283  0.0359  0.0439  155 VAL   A O   
3276 O O   B VAL   A 155 ? 0.1823 0.2058 0.2470 0.0269  0.0134  0.0415  155 VAL   A O   
3277 O O   T VAL   A 155 ? 0.1699 0.1720 0.1931 0.0114  0.0505  0.0587  155 VAL   A O   
3278 C CB  A VAL   A 155 ? 0.1132 0.1343 0.2000 0.0039  0.0112  0.0478  155 VAL   A CB  
3279 C CB  B VAL   A 155 ? 0.1580 0.1942 0.1835 0.0206  -0.0120 0.0329  155 VAL   A CB  
3280 C CB  T VAL   A 155 ? 0.1560 0.1591 0.2201 -0.0153 0.0203  0.0574  155 VAL   A CB  
3281 C CG1 A VAL   A 155 ? 0.1132 0.1423 0.2026 0.0093  0.0097  0.0499  155 VAL   A CG1 
3282 C CG1 B VAL   A 155 ? 0.1587 0.1974 0.1884 0.0182  -0.0138 0.0341  155 VAL   A CG1 
3283 C CG1 T VAL   A 155 ? 0.1563 0.1656 0.2225 -0.0119 0.0179  0.0586  155 VAL   A CG1 
3284 C CG2 A VAL   A 155 ? 0.1155 0.1436 0.2060 0.0104  -0.0081 0.0362  155 VAL   A CG2 
3285 C CG2 B VAL   A 155 ? 0.1580 0.1971 0.1790 0.0210  -0.0148 0.0314  155 VAL   A CG2 
3286 C CG2 T VAL   A 155 ? 0.1566 0.1649 0.2284 -0.0074 0.0007  0.0476  155 VAL   A CG2 
3312 N N   A PHE   A 156 ? 0.1483 0.1494 0.2314 0.0242  0.0252  0.0599  156 PHE   A N   
3313 N N   B PHE   A 156 ? 0.2039 0.2183 0.2440 0.0293  -0.0034 0.0368  156 PHE   A N   
3314 N N   T PHE   A 156 ? 0.1860 0.1556 0.2004 0.0113  0.0516  0.0628  156 PHE   A N   
3315 C CA  A PHE   A 156 ? 0.1701 0.1615 0.2471 0.0335  0.0230  0.0601  156 PHE   A CA  
3316 C CA  B PHE   A 156 ? 0.2306 0.2363 0.2736 0.0320  -0.0021 0.0279  156 PHE   A CA  
3317 C CA  T PHE   A 156 ? 0.2055 0.1554 0.1931 0.0217  0.0563  0.0625  156 PHE   A CA  
3318 C C   A PHE   A 156 ? 0.1727 0.1643 0.2412 0.0449  0.0389  0.0757  156 PHE   A C   
3319 C C   B PHE   A 156 ? 0.2491 0.2479 0.2870 0.0317  -0.0019 0.0348  156 PHE   A C   
3320 C C   T PHE   A 156 ? 0.2018 0.1736 0.2043 0.0318  0.0669  0.0672  156 PHE   A C   
3321 O O   A PHE   A 156 ? 0.1808 0.1669 0.2443 0.0383  0.0454  0.0751  156 PHE   A O   
3322 O O   B PHE   A 156 ? 0.2560 0.2525 0.2937 0.0312  -0.0017 0.0365  156 PHE   A O   
3323 O O   T PHE   A 156 ? 0.2066 0.1770 0.2073 0.0323  0.0807  0.0540  156 PHE   A O   
3324 C CB  A PHE   A 156 ? 0.1848 0.1723 0.2505 0.0254  0.0136  0.0518  156 PHE   A CB  
3325 C CB  B PHE   A 156 ? 0.2404 0.2454 0.2879 0.0302  -0.0004 0.0132  156 PHE   A CB  
3326 C CB  T PHE   A 156 ? 0.2167 0.1402 0.1658 0.0181  0.0512  0.0590  156 PHE   A CB  
3327 C CG  A PHE   A 156 ? 0.1985 0.1816 0.2561 0.0237  0.0087  0.0379  156 PHE   A CG  
3328 C CG  B PHE   A 156 ? 0.2503 0.2529 0.3019 0.0289  -0.0035 -0.0043 156 PHE   A CG  
3329 C CG  T PHE   A 156 ? 0.2285 0.1404 0.1548 0.0205  0.0398  0.0549  156 PHE   A CG  
3330 C CD1 A PHE   A 156 ? 0.2022 0.1840 0.2610 0.0320  0.0185  0.0331  156 PHE   A CD1 
3331 C CD1 B PHE   A 156 ? 0.2546 0.2566 0.3126 0.0304  -0.0070 -0.0118 156 PHE   A CD1 
3332 C CD1 T PHE   A 156 ? 0.2383 0.1474 0.1840 0.0191  0.0194  0.0385  156 PHE   A CD1 
3333 C CD2 A PHE   A 156 ? 0.2069 0.1918 0.2570 0.0259  0.0063  0.0318  156 PHE   A CD2 
3334 C CD2 B PHE   A 156 ? 0.2526 0.2546 0.3082 0.0287  -0.0065 -0.0147 156 PHE   A CD2 
3335 C CD2 T PHE   A 156 ? 0.2328 0.1409 0.1638 0.0235  0.0424  0.0595  156 PHE   A CD2 
3336 C CE1 A PHE   A 156 ? 0.2088 0.1873 0.2630 0.0337  0.0257  0.0253  156 PHE   A CE1 
3337 C CE1 B PHE   A 156 ? 0.2557 0.2580 0.3131 0.0296  -0.0088 -0.0192 156 PHE   A CE1 
3338 C CE1 T PHE   A 156 ? 0.2435 0.1509 0.2008 0.0201  0.0168  0.0256  156 PHE   A CE1 
3339 C CE2 A PHE   A 156 ? 0.2150 0.1970 0.2585 0.0271  0.0119  0.0216  156 PHE   A CE2 
3340 C CE2 B PHE   A 156 ? 0.2558 0.2565 0.3132 0.0279  -0.0090 -0.0222 156 PHE   A CE2 
3341 C CE2 T PHE   A 156 ? 0.2419 0.1498 0.1826 0.0189  0.0340  0.0473  156 PHE   A CE2 
3342 C CZ  A PHE   A 156 ? 0.2149 0.1944 0.2607 0.0322  0.0240  0.0197  156 PHE   A CZ  
3343 C CZ  B PHE   A 156 ? 0.2571 0.2582 0.3114 0.0287  -0.0087 -0.0251 156 PHE   A CZ  
3344 C CZ  T PHE   A 156 ? 0.2430 0.1465 0.2011 0.0127  0.0253  0.0354  156 PHE   A CZ  
3372 N N   A ASP   A 157 ? 0.1708 0.1733 0.2297 0.0587  0.0421  0.0834  157 ASP   A N   
3373 N N   B ASP   A 157 ? 0.2593 0.2524 0.2938 0.0299  -0.0083 0.0396  157 ASP   A N   
3374 N N   T ASP   A 157 ? 0.1870 0.1927 0.2231 0.0345  0.0532  0.0850  157 ASP   A N   
3375 C CA  A ASP   A 157 ? 0.1831 0.1969 0.2330 0.0598  0.0486  0.0867  157 ASP   A CA  
3376 C CA  B ASP   A 157 ? 0.2681 0.2566 0.3020 0.0232  -0.0070 0.0492  157 ASP   A CA  
3377 C CA  T ASP   A 157 ? 0.1806 0.2168 0.2381 0.0349  0.0478  0.0964  157 ASP   A CA  
3378 C C   A ASP   A 157 ? 0.1708 0.2137 0.2474 0.0627  0.0521  0.0884  157 ASP   A C   
3379 C C   B ASP   A 157 ? 0.2649 0.2628 0.3216 0.0157  -0.0101 0.0443  157 ASP   A C   
3380 C C   T ASP   A 157 ? 0.1741 0.2337 0.2403 0.0426  0.0521  0.1051  157 ASP   A C   
3381 O O   A ASP   A 157 ? 0.1635 0.2101 0.2339 0.0617  0.0501  0.0997  157 ASP   A O   
3382 O O   B ASP   A 157 ? 0.2682 0.2678 0.3379 0.0163  -0.0101 0.0394  157 ASP   A O   
3383 O O   T ASP   A 157 ? 0.1652 0.2371 0.2384 0.0437  0.0483  0.1020  157 ASP   A O   
3384 C CB  A ASP   A 157 ? 0.2015 0.2023 0.2377 0.0641  0.0505  0.0810  157 ASP   A CB  
3385 C CB  B ASP   A 157 ? 0.2776 0.2522 0.2906 0.0226  -0.0013 0.0663  157 ASP   A CB  
3386 C CB  T ASP   A 157 ? 0.1793 0.2214 0.2528 0.0329  0.0415  0.0946  157 ASP   A CB  
3387 C CG  A ASP   A 157 ? 0.2175 0.2053 0.2500 0.0669  0.0477  0.0823  157 ASP   A CG  
3388 C CG  B ASP   A 157 ? 0.2852 0.2481 0.2816 0.0250  0.0069  0.0830  157 ASP   A CG  
3389 C CG  T ASP   A 157 ? 0.1739 0.2195 0.2682 0.0284  0.0327  0.0983  157 ASP   A CG  
3390 O OD1 A ASP   A 157 ? 0.2318 0.2075 0.2624 0.0652  0.0416  0.0733  157 ASP   A OD1 
3391 O OD1 B ASP   A 157 ? 0.2902 0.2452 0.2757 0.0209  0.0204  0.0879  157 ASP   A OD1 
3392 O OD1 T ASP   A 157 ? 0.1720 0.2151 0.2873 0.0274  0.0291  0.0903  157 ASP   A OD1 
3393 O OD2 A ASP   A 157 ? 0.2142 0.2038 0.2557 0.0657  0.0492  0.0969  157 ASP   A OD2 
3394 O OD2 B ASP   A 157 ? 0.2862 0.2460 0.2823 0.0267  0.0068  0.0963  157 ASP   A OD2 
3395 O OD2 T ASP   A 157 ? 0.1637 0.2199 0.2628 0.0277  0.0247  0.1081  157 ASP   A OD2 
3408 N N   A LYS   A 158 ? 0.1776 0.2366 0.2771 0.0641  0.0602  0.0735  158 LYS   A N   
3409 N N   B LYS   A 158 ? 0.2579 0.2632 0.3245 0.0063  -0.0118 0.0447  158 LYS   A N   
3410 N N   T LYS   A 158 ? 0.1874 0.2503 0.2585 0.0457  0.0631  0.0997  158 LYS   A N   
3411 C CA  A LYS   A 158 ? 0.1795 0.2574 0.2966 0.0644  0.0664  0.0655  158 LYS   A CA  
3412 C CA  B LYS   A 158 ? 0.2534 0.2660 0.3258 -0.0011 -0.0054 0.0446  158 LYS   A CA  
3413 C CA  T LYS   A 158 ? 0.1951 0.2682 0.2840 0.0489  0.0660  0.0904  158 LYS   A CA  
3414 C C   A LYS   A 158 ? 0.1683 0.2662 0.2933 0.0639  0.0539  0.0727  158 LYS   A C   
3415 C C   B LYS   A 158 ? 0.2291 0.2593 0.3056 -0.0041 -0.0155 0.0482  158 LYS   A C   
3416 C C   T LYS   A 158 ? 0.1787 0.2649 0.2791 0.0495  0.0554  0.0907  158 LYS   A C   
3417 O O   A LYS   A 158 ? 0.1644 0.2762 0.3017 0.0561  0.0597  0.0732  158 LYS   A O   
3418 O O   B LYS   A 158 ? 0.2277 0.2616 0.3054 -0.0116 -0.0163 0.0530  158 LYS   A O   
3419 O O   T LYS   A 158 ? 0.1704 0.2695 0.2913 0.0443  0.0562  0.0925  158 LYS   A O   
3420 C CB  A LYS   A 158 ? 0.1944 0.2669 0.3197 0.0637  0.0852  0.0568  158 LYS   A CB  
3421 C CB  B LYS   A 158 ? 0.2703 0.2760 0.3416 -0.0011 0.0116  0.0419  158 LYS   A CB  
3422 C CB  T LYS   A 158 ? 0.2199 0.2864 0.3231 0.0478  0.0834  0.0775  158 LYS   A CB  
3423 C CG  A LYS   A 158 ? 0.2138 0.2760 0.3424 0.0611  0.0942  0.0573  158 LYS   A CG  
3424 C CG  B LYS   A 158 ? 0.2832 0.2861 0.3575 -0.0013 0.0320  0.0401  158 LYS   A CG  
3425 C CG  T LYS   A 158 ? 0.2440 0.3011 0.3605 0.0477  0.0945  0.0744  158 LYS   A CG  
3426 C CD  A LYS   A 158 ? 0.2256 0.2847 0.3599 0.0589  0.1061  0.0622  158 LYS   A CD  
3427 C CD  B LYS   A 158 ? 0.2931 0.2939 0.3720 -0.0023 0.0507  0.0408  158 LYS   A CD  
3428 C CD  T LYS   A 158 ? 0.2621 0.3129 0.3981 0.0503  0.1003  0.0731  158 LYS   A CD  
3429 C CE  A LYS   A 158 ? 0.2320 0.2892 0.3699 0.0542  0.1180  0.0704  158 LYS   A CE  
3430 C CE  B LYS   A 158 ? 0.2988 0.2981 0.3818 -0.0003 0.0649  0.0437  158 LYS   A CE  
3431 C CE  T LYS   A 158 ? 0.2757 0.3201 0.4265 0.0508  0.1017  0.0737  158 LYS   A CE  
3432 N NZ  A LYS   A 158 ? 0.2344 0.2915 0.3775 0.0504  0.1239  0.0761  158 LYS   A NZ  
3433 N NZ  B LYS   A 158 ? 0.3009 0.3010 0.3890 -0.0003 0.0708  0.0456  158 LYS   A NZ  
3434 N NZ  T LYS   A 158 ? 0.2823 0.3239 0.4425 0.0506  0.1019  0.0742  158 LYS   A NZ  
3474 N N   A ASN   A 159 ? 0.1695 0.2640 0.2918 0.0588  0.0329  0.0765  159 ASN   A N   
3475 N N   B ASN   A 159 ? 0.2106 0.2532 0.2897 0.0044  -0.0177 0.0499  159 ASN   A N   
3476 N N   T ASN   A 159 ? 0.1825 0.2585 0.2853 0.0425  0.0359  0.0822  159 ASN   A N   
3477 C CA  A ASN   A 159 ? 0.1723 0.2593 0.2776 0.0527  0.0101  0.0865  159 ASN   A CA  
3478 C CA  B ASN   A 159 ? 0.1939 0.2502 0.2741 0.0146  -0.0149 0.0519  159 ASN   A CA  
3479 C CA  T ASN   A 159 ? 0.1937 0.2518 0.2810 0.0329  0.0159  0.0839  159 ASN   A CA  
3480 C C   A ASN   A 159 ? 0.1576 0.2552 0.2599 0.0483  0.0070  0.0934  159 ASN   A C   
3481 C C   B ASN   A 159 ? 0.1707 0.2474 0.2673 0.0237  -0.0134 0.0651  159 ASN   A C   
3482 C C   T ASN   A 159 ? 0.1958 0.2502 0.2779 0.0227  0.0178  0.0794  159 ASN   A C   
3483 O O   A ASN   A 159 ? 0.1486 0.2493 0.2641 0.0546  -0.0053 0.0869  159 ASN   A O   
3484 O O   B ASN   A 159 ? 0.1536 0.2464 0.2621 0.0331  -0.0177 0.0848  159 ASN   A O   
3485 O O   T ASN   A 159 ? 0.1936 0.2434 0.2814 0.0191  0.0080  0.0581  159 ASN   A O   
3486 C CB  A ASN   A 159 ? 0.1895 0.2608 0.2979 0.0476  -0.0005 0.0840  159 ASN   A CB  
3487 C CB  B ASN   A 159 ? 0.2019 0.2526 0.2724 0.0148  -0.0091 0.0346  159 ASN   A CB  
3488 C CB  T ASN   A 159 ? 0.2061 0.2516 0.3039 0.0314  0.0005  0.0864  159 ASN   A CB  
3489 C CG  A ASN   A 159 ? 0.2048 0.2665 0.3225 0.0386  -0.0015 0.0730  159 ASN   A CG  
3490 C CG  B ASN   A 159 ? 0.2087 0.2585 0.2744 0.0093  -0.0044 0.0152  159 ASN   A CG  
3491 C CG  T ASN   A 159 ? 0.2170 0.2563 0.3316 0.0270  -0.0038 0.0797  159 ASN   A CG  
3492 O OD1 A ASN   A 159 ? 0.2129 0.2735 0.3410 0.0322  0.0060  0.0630  159 ASN   A OD1 
3493 O OD1 B ASN   A 159 ? 0.2142 0.2645 0.2810 0.0072  0.0003  0.0011  159 ASN   A OD1 
3494 O OD1 T ASN   A 159 ? 0.2220 0.2637 0.3545 0.0211  0.0057  0.0658  159 ASN   A OD1 
3495 N ND2 A ASN   A 159 ? 0.2096 0.2685 0.3284 0.0369  -0.0063 0.0691  159 ASN   A ND2 
3496 N ND2 B ASN   A 159 ? 0.2082 0.2616 0.2735 0.0065  -0.0076 0.0165  159 ASN   A ND2 
3497 N ND2 T ASN   A 159 ? 0.2210 0.2591 0.3382 0.0272  -0.0113 0.0788  159 ASN   A ND2 
3516 N N   A LEU   A 160 ? 0.1475 0.2533 0.2324 0.0408  0.0080  0.1062  160 LEU   A N   
3517 N N   B LEU   A 160 ? 0.1674 0.2462 0.2655 0.0188  -0.0091 0.0649  160 LEU   A N   
3518 N N   T LEU   A 160 ? 0.1960 0.2531 0.2659 0.0186  0.0224  0.0948  160 LEU   A N   
3519 C CA  A LEU   A 160 ? 0.1374 0.2517 0.1984 0.0294  0.0203  0.1126  160 LEU   A CA  
3520 C CA  B LEU   A 160 ? 0.1684 0.2478 0.2506 0.0165  0.0046  0.0638  160 LEU   A CA  
3521 C CA  T LEU   A 160 ? 0.1984 0.2515 0.2410 0.0105  0.0304  0.1120  160 LEU   A CA  
3522 C C   A LEU   A 160 ? 0.1127 0.2393 0.1645 0.0187  0.0234  0.1125  160 LEU   A C   
3523 C C   B LEU   A 160 ? 0.1543 0.2445 0.2134 0.0188  0.0168  0.0715  160 LEU   A C   
3524 O O   A LEU   A 160 ? 0.0963 0.2364 0.1416 0.0108  0.0100  0.1025  160 LEU   A O   
3525 O O   B LEU   A 160 ? 0.1442 0.2435 0.2028 0.0217  0.0210  0.0820  160 LEU   A O   
3526 C CB  A LEU   A 160 ? 0.1444 0.2536 0.1905 0.0281  0.0207  0.1105  160 LEU   A CB  
3527 C CB  B LEU   A 160 ? 0.1887 0.2555 0.2710 0.0116  0.0067  0.0497  160 LEU   A CB  
3528 C CB  T LEU   A 160 ? 0.1940 0.2522 0.2159 -0.0004 0.0376  0.1178  160 LEU   A CB  
3529 C CG  A LEU   A 160 ? 0.1469 0.2598 0.2138 0.0260  0.0148  0.0863  160 LEU   A CG  
3530 C CG  B LEU   A 160 ? 0.2063 0.2645 0.2917 0.0068  0.0076  0.0294  160 LEU   A CG  
3531 C CG  T LEU   A 160 ? 0.1896 0.2560 0.2215 -0.0125 0.0377  0.0996  160 LEU   A CG  
3532 C CD1 A LEU   A 160 ? 0.1541 0.2646 0.2232 0.0227  0.0165  0.0754  160 LEU   A CD1 
3533 C CD1 B LEU   A 160 ? 0.2134 0.2654 0.2993 0.0029  0.0099  0.0279  160 LEU   A CD1 
3534 C CD1 T LEU   A 160 ? 0.1946 0.2629 0.2265 -0.0146 0.0401  0.0890  160 LEU   A CD1 
3535 C CD2 A LEU   A 160 ? 0.1466 0.2590 0.2211 0.0275  0.0182  0.0781  160 LEU   A CD2 
3536 C CD2 B LEU   A 160 ? 0.2086 0.2674 0.2974 0.0038  0.0086  0.0219  160 LEU   A CD2 
3537 C CD2 T LEU   A 160 ? 0.1881 0.2536 0.2228 -0.0168 0.0385  0.0918  160 LEU   A CD2 
3570 N N   A TYR   A 161 ? 0.1305 0.2434 0.2071 0.0132  0.0322  0.1103  161 TYR   A N   
3571 N N   B TYR   A 161 ? 0.1643 0.2422 0.2124 0.0194  0.0133  0.0661  161 TYR   A N   
3572 C CA  A TYR   A 161 ? 0.1335 0.2435 0.1966 0.0059  0.0217  0.1166  161 TYR   A CA  
3573 C CA  B TYR   A 161 ? 0.1698 0.2394 0.2063 0.0186  0.0162  0.0586  161 TYR   A CA  
3574 C C   A TYR   A 161 ? 0.1327 0.2721 0.2094 0.0005  0.0127  0.1094  161 TYR   A C   
3575 C C   B TYR   A 161 ? 0.1733 0.2431 0.2066 0.0188  0.0167  0.0657  161 TYR   A C   
3576 O O   A TYR   A 161 ? 0.1262 0.2723 0.1967 -0.0108 0.0131  0.1104  161 TYR   A O   
3577 O O   B TYR   A 161 ? 0.1686 0.2407 0.2017 0.0165  0.0147  0.0727  161 TYR   A O   
3578 C CB  A TYR   A 161 ? 0.1456 0.2328 0.1925 0.0040  0.0263  0.0951  161 TYR   A CB  
3579 C CB  B TYR   A 161 ? 0.1746 0.2348 0.2141 0.0153  0.0180  0.0401  161 TYR   A CB  
3580 C CG  A TYR   A 161 ? 0.1414 0.2195 0.1862 0.0041  0.0227  0.0607  161 TYR   A CG  
3581 C CG  B TYR   A 161 ? 0.1779 0.2303 0.2081 0.0147  0.0182  0.0238  161 TYR   A CG  
3582 C CD1 A TYR   A 161 ? 0.1361 0.2071 0.1756 0.0032  0.0172  0.0437  161 TYR   A CD1 
3583 C CD1 B TYR   A 161 ? 0.1813 0.2324 0.2108 0.0173  0.0167  0.0201  161 TYR   A CD1 
3584 C CD2 A TYR   A 161 ? 0.1441 0.2193 0.1915 0.0105  0.0138  0.0551  161 TYR   A CD2 
3585 C CD2 B TYR   A 161 ? 0.1772 0.2259 0.2011 0.0132  0.0209  0.0169  161 TYR   A CD2 
3586 C CE1 A TYR   A 161 ? 0.1346 0.2000 0.1731 0.0042  0.0075  0.0386  161 TYR   A CE1 
3587 C CE1 B TYR   A 161 ? 0.1853 0.2298 0.2105 0.0164  0.0187  0.0205  161 TYR   A CE1 
3588 C CE2 A TYR   A 161 ? 0.1440 0.2073 0.1910 0.0038  0.0140  0.0533  161 TYR   A CE2 
3589 C CE2 B TYR   A 161 ? 0.1808 0.2255 0.2038 0.0134  0.0225  0.0158  161 TYR   A CE2 
3590 C CZ  A TYR   A 161 ? 0.1466 0.1982 0.1734 -0.0038 0.0049  0.0504  161 TYR   A CZ  
3591 C CZ  B TYR   A 161 ? 0.1871 0.2272 0.2095 0.0152  0.0233  0.0185  161 TYR   A CZ  
3592 O OH  A TYR   A 161 ? 0.1670 0.1986 0.1752 -0.0144 -0.0016 0.0474  161 TYR   A OH  
3593 O OH  B TYR   A 161 ? 0.1978 0.2296 0.2163 0.0146  0.0183  0.0211  161 TYR   A OH  
3612 N N   A ASP   A 162 ? 0.1314 0.2981 0.2217 0.0054  0.0271  0.1181  162 ASP   A N   
3613 N N   B ASP   A 162 ? 0.1800 0.2489 0.2177 0.0200  0.0175  0.0615  162 ASP   A N   
3614 C CA  A ASP   A 162 ? 0.1304 0.3305 0.2282 0.0044  0.0291  0.1056  162 ASP   A CA  
3615 C CA  B ASP   A 162 ? 0.1846 0.2549 0.2295 0.0136  0.0166  0.0643  162 ASP   A CA  
3616 C C   A ASP   A 162 ? 0.1245 0.3431 0.2256 0.0003  0.0225  0.1021  162 ASP   A C   
3617 C C   B ASP   A 162 ? 0.1865 0.2673 0.2266 0.0071  0.0185  0.0602  162 ASP   A C   
3618 O O   A ASP   A 162 ? 0.1309 0.3467 0.2239 0.0040  0.0229  0.0852  162 ASP   A O   
3619 O O   B ASP   A 162 ? 0.1843 0.2671 0.2245 0.0049  0.0214  0.0638  162 ASP   A O   
3620 C CB  A ASP   A 162 ? 0.1432 0.3523 0.2565 0.0106  0.0421  0.0850  162 ASP   A CB  
3621 C CB  B ASP   A 162 ? 0.1896 0.2501 0.2441 0.0181  0.0130  0.0740  162 ASP   A CB  
3622 C CG  A ASP   A 162 ? 0.1590 0.3730 0.2785 0.0163  0.0503  0.0691  162 ASP   A CG  
3623 C CG  B ASP   A 162 ? 0.1936 0.2481 0.2606 0.0230  0.0108  0.0813  162 ASP   A CG  
3624 O OD1 A ASP   A 162 ? 0.1744 0.3828 0.2896 0.0074  0.0515  0.0704  162 ASP   A OD1 
3625 O OD1 B ASP   A 162 ? 0.1990 0.2520 0.2676 0.0209  0.0090  0.0816  162 ASP   A OD1 
3626 O OD2 A ASP   A 162 ? 0.1749 0.3828 0.2930 0.0277  0.0504  0.0568  162 ASP   A OD2 
3627 O OD2 B ASP   A 162 ? 0.1972 0.2433 0.2699 0.0249  0.0172  0.0909  162 ASP   A OD2 
3636 N N   A LYS   A 163 ? 0.1338 0.3570 0.2264 -0.0004 0.0005  0.0968  163 LYS   A N   
3637 N N   B LYS   A 163 ? 0.1962 0.2775 0.2337 0.0049  0.0086  0.0537  163 LYS   A N   
3638 C CA  A LYS   A 163 ? 0.1468 0.3680 0.2314 -0.0021 -0.0039 0.0892  163 LYS   A CA  
3639 C CA  B LYS   A 163 ? 0.2044 0.2874 0.2453 0.0006  0.0011  0.0466  163 LYS   A CA  
3640 C C   A LYS   A 163 ? 0.1394 0.3589 0.2270 -0.0134 0.0072  0.0890  163 LYS   A C   
3641 C C   B LYS   A 163 ? 0.1970 0.2879 0.2353 -0.0007 0.0047  0.0475  163 LYS   A C   
3642 O O   A LYS   A 163 ? 0.1321 0.3665 0.2331 -0.0236 0.0083  0.0810  163 LYS   A O   
3643 O O   B LYS   A 163 ? 0.1952 0.2960 0.2319 -0.0026 0.0089  0.0452  163 LYS   A O   
3644 C CB  A LYS   A 163 ? 0.1792 0.3861 0.2691 0.0165  -0.0135 0.0791  163 LYS   A CB  
3645 C CB  B LYS   A 163 ? 0.2228 0.2971 0.2785 0.0011  -0.0016 0.0340  163 LYS   A CB  
3646 C CG  A LYS   A 163 ? 0.2121 0.4006 0.3292 0.0240  -0.0063 0.0670  163 LYS   A CG  
3647 C CG  B LYS   A 163 ? 0.2401 0.3061 0.3103 0.0001  0.0013  0.0198  163 LYS   A CG  
3648 C CD  A LYS   A 163 ? 0.2460 0.4121 0.3954 0.0289  -0.0052 0.0567  163 LYS   A CD  
3649 C CD  B LYS   A 163 ? 0.2533 0.3150 0.3357 -0.0002 0.0035  0.0080  163 LYS   A CD  
3650 C CE  A LYS   A 163 ? 0.2729 0.4188 0.4469 0.0320  0.0026  0.0523  163 LYS   A CE  
3651 C CE  B LYS   A 163 ? 0.2622 0.3209 0.3594 0.0008  0.0044  -0.0020 163 LYS   A CE  
3652 N NZ  A LYS   A 163 ? 0.2847 0.4231 0.4778 0.0332  0.0053  0.0519  163 LYS   A NZ  
3653 N NZ  B LYS   A 163 ? 0.2663 0.3234 0.3702 0.0024  0.0065  -0.0067 163 LYS   A NZ  
3680 N N   A LEU   A 164 ? 0.1220 0.3324 0.2013 -0.0227 0.0066  0.0900  164 LEU   A N   
3681 N N   B LEU   A 164 ? 0.1883 0.2757 0.2314 -0.0036 0.0069  0.0453  164 LEU   A N   
3682 C CA  A LEU   A 164 ? 0.1305 0.3074 0.1934 -0.0324 0.0183  0.0862  164 LEU   A CA  
3683 C CA  B LEU   A 164 ? 0.1863 0.2636 0.2178 -0.0066 0.0131  0.0465  164 LEU   A CA  
3684 C C   A LEU   A 164 ? 0.1407 0.3042 0.1930 -0.0303 0.0097  0.0809  164 LEU   A C   
3685 C C   B LEU   A 164 ? 0.1885 0.2658 0.2256 -0.0091 0.0152  0.0438  164 LEU   A C   
3686 O O   A LEU   A 164 ? 0.1465 0.3080 0.1995 -0.0410 0.0310  0.0632  164 LEU   A O   
3687 O O   B LEU   A 164 ? 0.1849 0.2688 0.2264 -0.0103 0.0164  0.0398  164 LEU   A O   
3688 C CB  A LEU   A 164 ? 0.1313 0.2899 0.1819 -0.0274 0.0215  0.0813  164 LEU   A CB  
3689 C CB  B LEU   A 164 ? 0.1853 0.2498 0.2003 -0.0079 0.0197  0.0462  164 LEU   A CB  
3690 C CG  A LEU   A 164 ? 0.1380 0.2784 0.1796 -0.0173 0.0103  0.0654  164 LEU   A CG  
3691 C CG  B LEU   A 164 ? 0.1867 0.2406 0.1934 -0.0061 0.0202  0.0397  164 LEU   A CG  
3692 C CD1 A LEU   A 164 ? 0.1254 0.2677 0.1699 -0.0105 0.0060  0.0731  164 LEU   A CD1 
3693 C CD1 B LEU   A 164 ? 0.1831 0.2380 0.1895 -0.0032 0.0238  0.0348  164 LEU   A CD1 
3694 C CD2 A LEU   A 164 ? 0.1555 0.2791 0.1819 -0.0185 0.0242  0.0513  164 LEU   A CD2 
3695 C CD2 B LEU   A 164 ? 0.1890 0.2371 0.1934 -0.0095 0.0200  0.0352  164 LEU   A CD2 
3718 N N   A VAL   A 165 ? 0.1247 0.2921 0.1883 -0.0320 0.0089  0.0911  165 VAL   A N   
3719 N N   B VAL   A 165 ? 0.1896 0.2639 0.2260 -0.0128 0.0140  0.0454  165 VAL   A N   
3720 C CA  A VAL   A 165 ? 0.1373 0.2886 0.1822 -0.0263 0.0131  0.0943  165 VAL   A CA  
3721 C CA  B VAL   A 165 ? 0.1933 0.2651 0.2285 -0.0162 0.0123  0.0454  165 VAL   A CA  
3722 C C   A VAL   A 165 ? 0.1330 0.3059 0.1803 -0.0213 0.0159  0.0916  165 VAL   A C   
3723 C C   B VAL   A 165 ? 0.1893 0.2692 0.2265 -0.0148 0.0118  0.0459  165 VAL   A C   
3724 O O   A VAL   A 165 ? 0.1306 0.3092 0.1871 -0.0251 0.0248  0.0844  165 VAL   A O   
3725 O O   B VAL   A 165 ? 0.1883 0.2667 0.2164 -0.0175 0.0154  0.0499  165 VAL   A O   
3726 C CB  A VAL   A 165 ? 0.1510 0.2732 0.1856 -0.0235 0.0149  0.0894  165 VAL   A CB  
3727 C CB  B VAL   A 165 ? 0.2004 0.2644 0.2384 -0.0179 0.0054  0.0393  165 VAL   A CB  
3728 C CG1 A VAL   A 165 ? 0.1573 0.2730 0.1898 -0.0221 0.0229  0.0797  165 VAL   A CG1 
3729 C CG1 B VAL   A 165 ? 0.2017 0.2633 0.2375 -0.0180 0.0033  0.0422  165 VAL   A CG1 
3730 C CG2 A VAL   A 165 ? 0.1582 0.2686 0.1913 -0.0203 0.0112  0.0910  165 VAL   A CG2 
3731 C CG2 B VAL   A 165 ? 0.2049 0.2659 0.2446 -0.0189 0.0040  0.0395  165 VAL   A CG2 
3750 N N   A SER   A 166 ? 0.1254 0.3195 0.1880 -0.0183 0.0178  0.0790  166 SER   A N   
3751 N N   B SER   A 166 ? 0.1851 0.2742 0.2321 -0.0144 0.0117  0.0428  166 SER   A N   
3752 C CA  A SER   A 166 ? 0.1305 0.3346 0.2057 -0.0206 0.0202  0.0627  166 SER   A CA  
3753 C CA  B SER   A 166 ? 0.1843 0.2804 0.2309 -0.0184 0.0138  0.0385  166 SER   A CA  
3754 C C   A SER   A 166 ? 0.1352 0.3510 0.2135 -0.0183 0.0072  0.0466  166 SER   A C   
3755 C C   B SER   A 166 ? 0.1962 0.2890 0.2287 -0.0324 0.0177  0.0391  166 SER   A C   
3756 O O   A SER   A 166 ? 0.1603 0.3670 0.2352 -0.0280 0.0239  0.0161  166 SER   A O   
3757 O O   B SER   A 166 ? 0.1986 0.2948 0.2342 -0.0442 0.0329  0.0374  166 SER   A O   
3758 C CB  A SER   A 166 ? 0.1414 0.3347 0.2252 -0.0166 0.0184  0.0535  166 SER   A CB  
3759 C CB  B SER   A 166 ? 0.1715 0.2774 0.2356 -0.0102 0.0082  0.0359  166 SER   A CB  
3760 O OG  A SER   A 166 ? 0.1583 0.3349 0.2601 -0.0169 0.0162  0.0549  166 SER   A OG  
3761 O OG  B SER   A 166 ? 0.1637 0.2751 0.2434 -0.0042 0.0004  0.0375  166 SER   A OG  
3772 N N   A SER   A 167 ? 0.1365 0.3480 0.1878 0.0017  0.0037  0.0618  167 SER   A N   
3773 N N   B SER   A 167 ? 0.2115 0.2919 0.2383 -0.0318 0.0073  0.0402  167 SER   A N   
3774 C CA  A SER   A 167 ? 0.1595 0.3518 0.2024 0.0124  -0.0064 0.0415  167 SER   A CA  
3775 C CA  B SER   A 167 ? 0.2269 0.2965 0.2475 -0.0281 -0.0006 0.0392  167 SER   A CA  
3776 C C   A SER   A 167 ? 0.1656 0.3511 0.2084 0.0176  0.0134  0.0330  167 SER   A C   
3777 C C   B SER   A 167 ? 0.2384 0.3010 0.2457 -0.0197 -0.0054 0.0331  167 SER   A C   
3778 O O   A SER   A 167 ? 0.1835 0.3560 0.2134 0.0203  -0.0020 0.0271  167 SER   A O   
3779 O O   B SER   A 167 ? 0.2420 0.3020 0.2475 -0.0164 -0.0128 0.0315  167 SER   A O   
3780 C CB  A SER   A 167 ? 0.1601 0.3552 0.2035 0.0107  -0.0004 0.0366  167 SER   A CB  
3781 C CB  B SER   A 167 ? 0.2346 0.2989 0.2708 -0.0288 -0.0071 0.0371  167 SER   A CB  
3782 O OG  A SER   A 167 ? 0.1518 0.3579 0.2134 0.0030  0.0213  0.0380  167 SER   A OG  
3783 O OG  B SER   A 167 ? 0.2413 0.3017 0.2899 -0.0274 -0.0121 0.0373  167 SER   A OG  
3794 N N   A PHE   A 168 ? 0.1516 0.3436 0.2079 0.0213  0.0223  0.0324  168 PHE   A N   
3795 N N   B PHE   A 168 ? 0.2470 0.3036 0.2408 -0.0147 -0.0082 0.0292  168 PHE   A N   
3796 C CA  A PHE   A 168 ? 0.1498 0.3393 0.2253 0.0115  0.0288  0.0297  168 PHE   A CA  
3797 C CA  B PHE   A 168 ? 0.2611 0.3053 0.2445 -0.0116 -0.0114 0.0221  168 PHE   A CA  
3798 C C   A PHE   A 168 ? 0.1570 0.3566 0.2532 -0.0093 0.0588  0.0129  168 PHE   A C   
3799 C C   B PHE   A 168 ? 0.2853 0.3284 0.2829 -0.0048 -0.0141 0.0232  168 PHE   A C   
3800 O O   A PHE   A 168 ? 0.1698 0.3620 0.3032 -0.0178 0.0581  0.0247  168 PHE   A O   
3801 O O   B PHE   A 168 ? 0.2833 0.3297 0.2715 -0.0058 -0.0174 0.0300  168 PHE   A O   
3802 C CB  A PHE   A 168 ? 0.1528 0.3185 0.2213 0.0078  0.0148  0.0424  168 PHE   A CB  
3803 C CB  B PHE   A 168 ? 0.2542 0.2845 0.2169 -0.0181 -0.0128 0.0110  168 PHE   A CB  
3804 C CG  A PHE   A 168 ? 0.1460 0.2974 0.2209 -0.0027 0.0112  0.0576  168 PHE   A CG  
3805 C CG  B PHE   A 168 ? 0.2476 0.2641 0.1964 -0.0233 -0.0141 0.0032  168 PHE   A CG  
3806 C CD1 A PHE   A 168 ? 0.1474 0.2884 0.2205 -0.0088 0.0057  0.0735  168 PHE   A CD1 
3807 C CD1 B PHE   A 168 ? 0.2452 0.2570 0.1937 -0.0255 -0.0146 0.0014  168 PHE   A CD1 
3808 C CD2 A PHE   A 168 ? 0.1448 0.2889 0.2227 -0.0074 0.0219  0.0566  168 PHE   A CD2 
3809 C CD2 B PHE   A 168 ? 0.2473 0.2540 0.1882 -0.0237 -0.0159 -0.0028 168 PHE   A CD2 
3810 C CE1 A PHE   A 168 ? 0.1349 0.2779 0.2131 -0.0163 0.0093  0.0822  168 PHE   A CE1 
3811 C CE1 B PHE   A 168 ? 0.2418 0.2538 0.1895 -0.0270 -0.0191 -0.0041 168 PHE   A CE1 
3812 C CE2 A PHE   A 168 ? 0.1493 0.2774 0.2237 -0.0105 0.0223  0.0702  168 PHE   A CE2 
3813 C CE2 B PHE   A 168 ? 0.2470 0.2520 0.1874 -0.0246 -0.0191 -0.0066 168 PHE   A CE2 
3814 C CZ  A PHE   A 168 ? 0.1423 0.2733 0.2157 -0.0149 0.0132  0.0797  168 PHE   A CZ  
3815 C CZ  B PHE   A 168 ? 0.2453 0.2529 0.1906 -0.0255 -0.0198 -0.0042 168 PHE   A CZ  
3834 N N   A LEU   A 169 ? 0.1808 0.3680 0.2786 -0.0303 0.0635  -0.0185 169 LEU   A N   
3835 N N   B LEU   A 169 ? 0.3134 0.3501 0.3329 0.0018  -0.0108 0.0176  169 LEU   A N   
3836 C CA  A LEU   A 169 ? 0.2324 0.3847 0.3561 -0.0334 0.0463  -0.0316 169 LEU   A CA  
3837 C CA  B LEU   A 169 ? 0.3345 0.3690 0.3771 0.0091  -0.0108 0.0102  169 LEU   A CA  
3838 C C   A LEU   A 169 ? 0.2360 0.3812 0.3893 -0.0373 0.0456  -0.0229 169 LEU   A C   
3839 C C   B LEU   A 169 ? 0.3456 0.3782 0.4061 0.0139  -0.0129 0.0114  169 LEU   A C   
3840 O O   A LEU   A 169 ? 0.2441 0.3823 0.4012 -0.0342 0.0391  -0.0285 169 LEU   A O   
3841 O O   B LEU   A 169 ? 0.3491 0.3803 0.4148 0.0167  -0.0135 0.0127  169 LEU   A O   
3842 C CB  A LEU   A 169 ? 0.2642 0.3996 0.3844 -0.0391 0.0311  -0.0495 169 LEU   A CB  
3843 C CB  B LEU   A 169 ? 0.3426 0.3772 0.3870 0.0110  -0.0090 0.0002  169 LEU   A CB  
3844 C CG  A LEU   A 169 ? 0.2922 0.4118 0.4102 -0.0460 0.0146  -0.0692 169 LEU   A CG  
3845 C CG  B LEU   A 169 ? 0.3490 0.3835 0.3945 0.0122  -0.0053 -0.0072 169 LEU   A CG  
3846 C CD1 A LEU   A 169 ? 0.3043 0.4148 0.4223 -0.0470 0.0068  -0.0765 169 LEU   A CD1 
3847 C CD1 B LEU   A 169 ? 0.3505 0.3854 0.3956 0.0124  -0.0043 -0.0096 169 LEU   A CD1 
3848 C CD2 A LEU   A 169 ? 0.3010 0.4167 0.4125 -0.0499 0.0129  -0.0745 169 LEU   A CD2 
3849 C CD2 B LEU   A 169 ? 0.3518 0.3858 0.3955 0.0127  -0.0044 -0.0103 169 LEU   A CD2 
3850 O OXT A LEU   A 169 ? 0.2209 0.3779 0.3871 -0.0406 0.0523  -0.0156 169 LEU   A OXT 
3851 O OXT B LEU   A 169 ? 0.3519 0.3838 0.4190 0.0142  -0.0128 0.0106  169 LEU   A OXT 
3874 N N   A SER   B 1   ? 0.3683 0.3402 0.3526 -0.1161 -0.0699 0.0327  1   SER   B N   
3875 N N   B SER   B 1   ? 0.3330 0.3250 0.3357 -0.0681 -0.0436 0.0183  1   SER   B N   
3876 C CA  A SER   B 1   ? 0.3576 0.3441 0.3573 -0.1218 -0.0749 0.0304  1   SER   B CA  
3877 C CA  B SER   B 1   ? 0.3275 0.3265 0.3354 -0.0694 -0.0443 0.0180  1   SER   B CA  
3878 C C   A SER   B 1   ? 0.3290 0.3457 0.3384 -0.1239 -0.0830 0.0493  1   SER   B C   
3879 C C   B SER   B 1   ? 0.3144 0.3267 0.3234 -0.0679 -0.0496 0.0291  1   SER   B C   
3880 O O   A SER   B 1   ? 0.3368 0.3478 0.3176 -0.1192 -0.0757 0.0521  1   SER   B O   
3881 O O   B SER   B 1   ? 0.3158 0.3264 0.3115 -0.0679 -0.0516 0.0281  1   SER   B O   
3882 C CB  A SER   B 1   ? 0.3719 0.3430 0.3760 -0.1216 -0.0661 0.0149  1   SER   B CB  
3883 C CB  B SER   B 1   ? 0.3329 0.3259 0.3440 -0.0701 -0.0375 0.0082  1   SER   B CB  
3884 O OG  A SER   B 1   ? 0.3861 0.3515 0.4185 -0.1179 -0.0578 0.0103  1   SER   B OG  
3885 O OG  B SER   B 1   ? 0.3384 0.3293 0.3632 -0.0704 -0.0332 0.0038  1   SER   B OG  
3900 N N   A MET   B 2   ? 0.3008 0.3433 0.3428 -0.1224 -0.0854 0.0845  2   MET   B N   
3901 N N   B MET   B 2   ? 0.3027 0.3263 0.3224 -0.0637 -0.0487 0.0483  2   MET   B N   
3902 C CA  A MET   B 2   ? 0.2818 0.3445 0.3603 -0.1018 -0.0880 0.1049  2   MET   B CA  
3903 C CA  B MET   B 2   ? 0.2917 0.3252 0.3236 -0.0542 -0.0466 0.0629  2   MET   B CA  
3904 C C   A MET   B 2   ? 0.2453 0.3221 0.3317 -0.0809 -0.0978 0.1325  2   MET   B C   
3905 C C   B MET   B 2   ? 0.2721 0.3090 0.2998 -0.0485 -0.0442 0.0709  2   MET   B C   
3906 O O   A MET   B 2   ? 0.2367 0.3353 0.3346 -0.0672 -0.1112 0.1348  2   MET   B O   
3907 O O   B MET   B 2   ? 0.2735 0.3156 0.3031 -0.0446 -0.0417 0.0688  2   MET   B O   
3908 C CB  A MET   B 2   ? 0.3122 0.3771 0.4414 -0.0810 -0.0652 0.0829  2   MET   B CB  
3909 C CB  B MET   B 2   ? 0.3032 0.3417 0.3591 -0.0448 -0.0437 0.0655  2   MET   B CB  
3910 C CG  A MET   B 2   ? 0.3401 0.4052 0.5150 -0.0596 -0.0445 0.0684  2   MET   B CG  
3911 C CG  B MET   B 2   ? 0.3126 0.3562 0.3875 -0.0357 -0.0406 0.0728  2   MET   B CG  
3912 S SD  A MET   B 2   ? 0.3667 0.4308 0.5866 -0.0414 -0.0316 0.0570  2   MET   B SD  
3913 S SD  B MET   B 2   ? 0.3215 0.3704 0.4120 -0.0276 -0.0408 0.0802  2   MET   B SD  
3914 C CE  A MET   B 2   ? 0.3703 0.4365 0.5898 -0.0396 -0.0233 0.0574  2   MET   B CE  
3915 C CE  B MET   B 2   ? 0.3216 0.3719 0.4192 -0.0279 -0.0376 0.0750  2   MET   B CE  
3934 N N   A VAL   B 3   ? 0.2192 0.2810 0.3098 -0.0818 -0.0903 0.1483  3   VAL   B N   
3935 N N   B VAL   B 3   ? 0.2509 0.2840 0.2765 -0.0489 -0.0440 0.0790  3   VAL   B N   
3936 C CA  A VAL   B 3   ? 0.2106 0.2457 0.3096 -0.0725 -0.0799 0.1313  3   VAL   B CA  
3937 C CA  B VAL   B 3   ? 0.2329 0.2601 0.2624 -0.0463 -0.0438 0.0758  3   VAL   B CA  
3938 C C   A VAL   B 3   ? 0.1936 0.2345 0.2787 -0.0632 -0.0741 0.1105  3   VAL   B C   
3939 C C   B VAL   B 3   ? 0.2099 0.2411 0.2441 -0.0479 -0.0503 0.0795  3   VAL   B C   
3940 O O   A VAL   B 3   ? 0.1856 0.2390 0.2868 -0.0674 -0.0719 0.1218  3   VAL   B O   
3941 O O   B VAL   B 3   ? 0.2083 0.2464 0.2333 -0.0388 -0.0505 0.0826  3   VAL   B O   
3942 C CB  A VAL   B 3   ? 0.2275 0.2407 0.3538 -0.0687 -0.0712 0.1130  3   VAL   B CB  
3943 C CB  B VAL   B 3   ? 0.2390 0.2567 0.2722 -0.0436 -0.0373 0.0686  3   VAL   B CB  
3944 C CG1 A VAL   B 3   ? 0.2369 0.2381 0.3717 -0.0680 -0.0704 0.1056  3   VAL   B CG1 
3945 C CG1 B VAL   B 3   ? 0.2424 0.2554 0.2772 -0.0431 -0.0357 0.0646  3   VAL   B CG1 
3946 C CG2 A VAL   B 3   ? 0.2292 0.2428 0.3674 -0.0666 -0.0595 0.1191  3   VAL   B CG2 
3947 C CG2 B VAL   B 3   ? 0.2403 0.2563 0.2740 -0.0428 -0.0345 0.0703  3   VAL   B CG2 
3966 N N   . ASN   B 4   ? 0.1901 0.2150 0.2459 -0.0607 -0.0569 0.0823  4   ASN   B N   
3967 C CA  . ASN   B 4   ? 0.1908 0.2100 0.2123 -0.0603 -0.0455 0.0470  4   ASN   B CA  
3968 C C   . ASN   B 4   ? 0.1974 0.2213 0.2059 -0.0624 -0.0331 0.0362  4   ASN   B C   
3969 O O   . ASN   B 4   ? 0.1978 0.2267 0.2233 -0.0594 -0.0259 0.0195  4   ASN   B O   
3970 C CB  . ASN   B 4   ? 0.1892 0.2050 0.1977 -0.0509 -0.0586 0.0332  4   ASN   B CB  
3971 C CG  . ASN   B 4   ? 0.1838 0.1823 0.1963 -0.0475 -0.0546 0.0333  4   ASN   B CG  
3972 O OD1 . ASN   B 4   ? 0.1878 0.1677 0.2025 -0.0444 -0.0545 0.0329  4   ASN   B OD1 
3973 N ND2 . ASN   B 4   ? 0.2022 0.1932 0.2034 -0.0289 -0.0365 0.0286  4   ASN   B ND2 
3981 N N   . SER   B 5   ? 0.2134 0.2409 0.2144 -0.0613 -0.0232 0.0297  5   SER   B N   
3982 C CA  . SER   B 5   ? 0.2425 0.2734 0.2471 -0.0520 -0.0022 0.0325  5   SER   B CA  
3983 C C   . SER   B 5   ? 0.2637 0.2817 0.2652 -0.0705 0.0241  0.0381  5   SER   B C   
3984 O O   . SER   B 5   ? 0.2804 0.2795 0.3256 -0.0647 0.0521  0.0331  5   SER   B O   
3985 C CB  . SER   B 5   ? 0.2532 0.2925 0.2750 -0.0408 0.0050  0.0428  5   SER   B CB  
3986 O OG  . SER   B 5   ? 0.2768 0.3202 0.3285 -0.0258 0.0116  0.0453  5   SER   B OG  
3992 N N   . PHE   B 6   ? 0.2841 0.3038 0.2395 -0.0755 0.0330  0.0445  6   PHE   B N   
3993 C CA  . PHE   B 6   ? 0.2931 0.3090 0.2014 -0.0907 0.0415  0.0289  6   PHE   B CA  
3994 C C   . PHE   B 6   ? 0.3441 0.3431 0.2443 -0.0965 0.0620  0.0016  6   PHE   B C   
3995 O O   . PHE   B 6   ? 0.3567 0.3714 0.2780 -0.0901 0.0498  -0.0152 6   PHE   B O   
3996 C CB  . PHE   B 6   ? 0.2623 0.2844 0.1801 -0.0818 0.0135  0.0219  6   PHE   B CB  
3997 C CG  . PHE   B 6   ? 0.2271 0.2512 0.1763 -0.0782 -0.0051 0.0145  6   PHE   B CG  
3998 C CD1 . PHE   B 6   ? 0.2266 0.2243 0.1676 -0.0756 -0.0191 0.0114  6   PHE   B CD1 
3999 C CD2 . PHE   B 6   ? 0.2024 0.2498 0.1837 -0.0664 0.0002  0.0309  6   PHE   B CD2 
4000 C CE1 . PHE   B 6   ? 0.2196 0.2048 0.1791 -0.0674 -0.0217 0.0117  6   PHE   B CE1 
4001 C CE2 . PHE   B 6   ? 0.2049 0.2351 0.2117 -0.0533 0.0053  0.0296  6   PHE   B CE2 
4002 C CZ  . PHE   B 6   ? 0.2092 0.2127 0.2027 -0.0584 -0.0059 0.0136  6   PHE   B CZ  
4012 N N   . SER   B 7   ? 0.3794 0.3352 0.2657 -0.1169 0.0871  -0.0194 7   SER   B N   
4013 C CA  . SER   B 7   ? 0.4102 0.3518 0.3079 -0.1196 0.1120  -0.0283 7   SER   B CA  
4014 C C   . SER   B 7   ? 0.4111 0.3272 0.2844 -0.1234 0.1212  -0.0452 7   SER   B C   
4015 O O   . SER   B 7   ? 0.4193 0.3252 0.3066 -0.1235 0.1185  -0.0479 7   SER   B O   
4016 C CB  . SER   B 7   ? 0.4295 0.3799 0.3755 -0.1171 0.1284  -0.0240 7   SER   B CB  
4017 O OG  . SER   B 7   ? 0.4411 0.3907 0.4300 -0.1157 0.1326  -0.0181 7   SER   B OG  
4023 N N   . GLY   B 8   ? 0.4084 0.3112 0.2843 -0.1105 0.1254  -0.0587 8   GLY   B N   
4024 C CA  . GLY   B 8   ? 0.3960 0.2930 0.2871 -0.1017 0.1254  -0.0664 8   GLY   B CA  
4025 C C   . GLY   B 8   ? 0.3752 0.2637 0.2803 -0.0986 0.1251  -0.0630 8   GLY   B C   
4026 O O   . GLY   B 8   ? 0.3868 0.2731 0.3135 -0.0894 0.1281  -0.0604 8   GLY   B O   
4030 N N   . TYR   B 9   ? 0.3568 0.2364 0.2600 -0.0862 0.0987  -0.0721 9   TYR   B N   
4031 C CA  . TYR   B 9   ? 0.3350 0.2083 0.2411 -0.0702 0.0768  -0.0524 9   TYR   B CA  
4032 C C   . TYR   B 9   ? 0.3291 0.2070 0.2319 -0.0617 0.0503  -0.0379 9   TYR   B C   
4033 O O   . TYR   B 9   ? 0.3413 0.2296 0.2675 -0.0640 0.0465  -0.0254 9   TYR   B O   
4034 C CB  . TYR   B 9   ? 0.3248 0.1844 0.2517 -0.0651 0.0722  -0.0470 9   TYR   B CB  
4035 C CG  . TYR   B 9   ? 0.3146 0.1652 0.2551 -0.0736 0.0632  -0.0475 9   TYR   B CG  
4036 C CD1 . TYR   B 9   ? 0.3180 0.1657 0.2649 -0.0859 0.0640  -0.0442 9   TYR   B CD1 
4037 C CD2 . TYR   B 9   ? 0.3011 0.1646 0.2513 -0.0662 0.0568  -0.0446 9   TYR   B CD2 
4038 C CE1 . TYR   B 9   ? 0.3139 0.1801 0.2685 -0.0867 0.0682  -0.0548 9   TYR   B CE1 
4039 C CE2 . TYR   B 9   ? 0.3010 0.1618 0.2581 -0.0668 0.0576  -0.0518 9   TYR   B CE2 
4040 C CZ  . TYR   B 9   ? 0.3043 0.1813 0.2701 -0.0803 0.0661  -0.0623 9   TYR   B CZ  
4041 O OH  . TYR   B 9   ? 0.2998 0.1943 0.2882 -0.0897 0.0685  -0.0747 9   TYR   B OH  
4051 N N   . LEU   B 10  ? 0.3105 0.1787 0.2079 -0.0580 0.0294  -0.0433 10  LEU   B N   
4052 C CA  . LEU   B 10  ? 0.3033 0.1793 0.2077 -0.0675 -0.0074 -0.0349 10  LEU   B CA  
4053 C C   . LEU   B 10  ? 0.2842 0.1828 0.2074 -0.0679 -0.0235 -0.0297 10  LEU   B C   
4054 O O   . LEU   B 10  ? 0.2674 0.1837 0.2143 -0.0555 -0.0125 -0.0221 10  LEU   B O   
4055 C CB  . LEU   B 10  ? 0.3137 0.1774 0.2293 -0.0678 -0.0286 -0.0145 10  LEU   B CB  
4056 C CG  . LEU   B 10  ? 0.3304 0.1890 0.2697 -0.0616 -0.0531 -0.0052 10  LEU   B CG  
4057 C CD1 . LEU   B 10  ? 0.3423 0.2035 0.2925 -0.0567 -0.0517 0.0020  10  LEU   B CD1 
4058 C CD2 . LEU   B 10  ? 0.3406 0.1934 0.2984 -0.0589 -0.0513 0.0065  10  LEU   B CD2 
4070 N N   . LYS   B 11  ? 0.2965 0.2115 0.2157 -0.0620 -0.0356 -0.0206 11  LYS   B N   
4071 C CA  . LYS   B 11  ? 0.3083 0.2387 0.2514 -0.0515 -0.0493 -0.0243 11  LYS   B CA  
4072 C C   . LYS   B 11  ? 0.2861 0.2176 0.2612 -0.0707 -0.0442 -0.0314 11  LYS   B C   
4073 O O   . LYS   B 11  ? 0.3005 0.2348 0.2985 -0.0850 -0.0390 -0.0687 11  LYS   B O   
4074 C CB  . LYS   B 11  ? 0.3412 0.2890 0.3117 -0.0275 -0.0560 -0.0248 11  LYS   B CB  
4075 C CG  . LYS   B 11  ? 0.3716 0.3209 0.3801 -0.0141 -0.0567 -0.0273 11  LYS   B CG  
4076 C CD  . LYS   B 11  ? 0.3948 0.3436 0.4397 -0.0059 -0.0557 -0.0310 11  LYS   B CD  
4077 C CE  . LYS   B 11  ? 0.4106 0.3582 0.4836 -0.0049 -0.0565 -0.0327 11  LYS   B CE  
4078 N NZ  . LYS   B 11  ? 0.4194 0.3670 0.5072 -0.0050 -0.0583 -0.0311 11  LYS   B NZ  
4092 N N   . LEU   B 12  ? 0.2512 0.1964 0.2615 -0.0644 -0.0435 -0.0277 12  LEU   B N   
4093 C CA  . LEU   B 12  ? 0.2356 0.1766 0.2699 -0.0538 -0.0315 -0.0281 12  LEU   B CA  
4094 C C   . LEU   B 12  ? 0.2222 0.1718 0.2756 -0.0543 -0.0424 -0.0223 12  LEU   B C   
4095 O O   . LEU   B 12  ? 0.2184 0.1715 0.2973 -0.0622 -0.0573 -0.0186 12  LEU   B O   
4096 C CB  . LEU   B 12  ? 0.2339 0.1557 0.2687 -0.0439 -0.0220 -0.0298 12  LEU   B CB  
4097 C CG  . LEU   B 12  ? 0.2319 0.1537 0.2663 -0.0420 -0.0144 -0.0235 12  LEU   B CG  
4098 C CD1 . LEU   B 12  ? 0.2412 0.1557 0.2624 -0.0255 -0.0085 -0.0033 12  LEU   B CD1 
4099 C CD2 . LEU   B 12  ? 0.2368 0.1599 0.2740 -0.0431 -0.0119 -0.0252 12  LEU   B CD2 
4111 N N   . THR   B 13  ? 0.2120 0.1749 0.2792 -0.0575 -0.0470 -0.0310 13  THR   B N   
4112 C CA  . THR   B 13  ? 0.2108 0.1856 0.2771 -0.0623 -0.0585 -0.0144 13  THR   B CA  
4113 C C   . THR   B 13  ? 0.2522 0.2078 0.2882 -0.0651 -0.0718 -0.0138 13  THR   B C   
4114 O O   . THR   B 13  ? 0.2703 0.2053 0.3002 -0.0638 -0.0407 -0.0184 13  THR   B O   
4115 C CB  . THR   B 13  ? 0.1957 0.1888 0.2825 -0.0554 -0.0549 -0.0122 13  THR   B CB  
4116 O OG1 . THR   B 13  ? 0.1862 0.1847 0.2961 -0.0443 -0.0447 -0.0167 13  THR   B OG1 
4117 C CG2 . THR   B 13  ? 0.2019 0.2008 0.2883 -0.0481 -0.0468 -0.0098 13  THR   B CG2 
4125 N N   A ASP   B 14  ? 0.2640 0.2216 0.2957 -0.0730 -0.1057 -0.0045 14  ASP   B N   
4126 N N   B ASP   B 14  ? 0.2608 0.2177 0.2952 -0.0653 -0.0784 -0.0068 14  ASP   B N   
4127 C CA  A ASP   B 14  ? 0.2767 0.2383 0.3223 -0.0741 -0.1119 0.0161  14  ASP   B CA  
4128 C CA  B ASP   B 14  ? 0.2684 0.2282 0.3087 -0.0640 -0.0768 0.0034  14  ASP   B CA  
4129 C C   A ASP   B 14  ? 0.2683 0.2184 0.2915 -0.0755 -0.0900 0.0199  14  ASP   B C   
4130 C C   B ASP   B 14  ? 0.2566 0.2110 0.2815 -0.0650 -0.0768 0.0084  14  ASP   B C   
4131 O O   A ASP   B 14  ? 0.2944 0.2317 0.3016 -0.0768 -0.0820 0.0317  14  ASP   B O   
4132 O O   B ASP   B 14  ? 0.2680 0.2142 0.2797 -0.0644 -0.0759 0.0103  14  ASP   B O   
4133 C CB  A ASP   B 14  ? 0.2963 0.2754 0.3903 -0.0705 -0.1294 0.0161  14  ASP   B CB  
4134 C CB  B ASP   B 14  ? 0.2861 0.2546 0.3526 -0.0601 -0.0725 0.0038  14  ASP   B CB  
4135 C CG  A ASP   B 14  ? 0.3236 0.3074 0.4638 -0.0638 -0.1231 0.0026  14  ASP   B CG  
4136 C CG  B ASP   B 14  ? 0.3043 0.2771 0.3943 -0.0548 -0.0641 -0.0006 14  ASP   B CG  
4137 O OD1 A ASP   B 14  ? 0.3406 0.3180 0.4838 -0.0668 -0.1181 -0.0113 14  ASP   B OD1 
4138 O OD1 B ASP   B 14  ? 0.3121 0.2868 0.4053 -0.0541 -0.0578 -0.0032 14  ASP   B OD1 
4139 O OD2 A ASP   B 14  ? 0.3284 0.3223 0.4993 -0.0596 -0.1160 0.0057  14  ASP   B OD2 
4140 O OD2 B ASP   B 14  ? 0.3091 0.2847 0.4107 -0.0547 -0.0632 -0.0012 14  ASP   B OD2 
4149 N N   . ASN   B 15  ? 0.2322 0.1908 0.2665 -0.0599 -0.0806 0.0127  15  ASN   B N   
4150 C CA  . ASN   B 15  ? 0.1837 0.1592 0.2524 -0.0389 -0.0623 0.0083  15  ASN   B CA  
4151 C C   . ASN   B 15  ? 0.1687 0.1456 0.2417 -0.0233 -0.0456 0.0015  15  ASN   B C   
4152 O O   . ASN   B 15  ? 0.1686 0.1396 0.2550 -0.0258 -0.0544 -0.0129 15  ASN   B O   
4153 C CB  . ASN   B 15  ? 0.1772 0.1593 0.2637 -0.0163 -0.0584 0.0164  15  ASN   B CB  
4154 C CG  . ASN   B 15  ? 0.1632 0.1546 0.2751 -0.0240 -0.0335 0.0145  15  ASN   B CG  
4155 O OD1 . ASN   B 15  ? 0.1682 0.1795 0.3025 -0.0433 -0.0363 0.0184  15  ASN   B OD1 
4156 N ND2 . ASN   B 15  ? 0.1637 0.1360 0.2705 -0.0152 -0.0124 -0.0050 15  ASN   B ND2 
4164 N N   . VAL   B 16  ? 0.1681 0.1394 0.2382 -0.0311 -0.0530 0.0018  16  VAL   B N   
4165 C CA  . VAL   B 16  ? 0.1704 0.1474 0.2177 -0.0285 -0.0438 -0.0192 16  VAL   B CA  
4166 C C   . VAL   B 16  ? 0.1700 0.1562 0.2161 -0.0372 -0.0389 -0.0123 16  VAL   B C   
4167 O O   . VAL   B 16  ? 0.1792 0.1672 0.2363 -0.0350 -0.0355 -0.0239 16  VAL   B O   
4168 C CB  . VAL   B 16  ? 0.1783 0.1458 0.2312 -0.0180 -0.0260 -0.0198 16  VAL   B CB  
4169 C CG1 . VAL   B 16  ? 0.1879 0.1410 0.2237 -0.0066 -0.0205 -0.0087 16  VAL   B CG1 
4170 C CG2 . VAL   B 16  ? 0.1759 0.1522 0.2519 -0.0129 -0.0212 -0.0181 16  VAL   B CG2 
4180 N N   . TYR   B 17  ? 0.1773 0.1638 0.2195 -0.0307 -0.0393 -0.0158 17  TYR   B N   
4181 C CA  . TYR   B 17  ? 0.1855 0.1743 0.2158 -0.0433 -0.0310 0.0051  17  TYR   B CA  
4182 C C   . TYR   B 17  ? 0.1790 0.1500 0.2137 -0.0416 -0.0158 -0.0061 17  TYR   B C   
4183 O O   . TYR   B 17  ? 0.1764 0.1562 0.2154 -0.0353 -0.0265 -0.0260 17  TYR   B O   
4184 C CB  . TYR   B 17  ? 0.2191 0.2156 0.2320 -0.0312 -0.0356 0.0347  17  TYR   B CB  
4185 C CG  . TYR   B 17  ? 0.2491 0.2623 0.2652 -0.0210 -0.0520 0.0412  17  TYR   B CG  
4186 C CD1 . TYR   B 17  ? 0.2667 0.2754 0.2813 -0.0173 -0.0603 0.0561  17  TYR   B CD1 
4187 C CD2 . TYR   B 17  ? 0.2711 0.2877 0.2893 -0.0097 -0.0580 0.0389  17  TYR   B CD2 
4188 C CE1 . TYR   B 17  ? 0.2857 0.2968 0.2976 -0.0080 -0.0708 0.0497  17  TYR   B CE1 
4189 C CE2 . TYR   B 17  ? 0.2872 0.3046 0.3103 -0.0001 -0.0704 0.0445  17  TYR   B CE2 
4190 C CZ  . TYR   B 17  ? 0.2981 0.3113 0.3125 0.0010  -0.0800 0.0486  17  TYR   B CZ  
4191 O OH  . TYR   B 17  ? 0.3148 0.3303 0.3302 0.0087  -0.0889 0.0469  17  TYR   B OH  
4201 N N   . ILE   B 18  ? 0.1881 0.1476 0.2103 -0.0367 -0.0133 -0.0153 18  ILE   B N   
4202 C CA  . ILE   B 18  ? 0.1910 0.1453 0.2071 -0.0363 -0.0114 -0.0192 18  ILE   B CA  
4203 C C   . ILE   B 18  ? 0.2039 0.1504 0.2045 -0.0477 -0.0070 -0.0319 18  ILE   B C   
4204 O O   . ILE   B 18  ? 0.2207 0.1697 0.2172 -0.0405 0.0038  -0.0371 18  ILE   B O   
4205 C CB  . ILE   B 18  ? 0.1975 0.1478 0.2131 -0.0426 -0.0149 -0.0183 18  ILE   B CB  
4206 C CG1 . ILE   B 18  ? 0.1942 0.1515 0.2179 -0.0459 -0.0087 -0.0073 18  ILE   B CG1 
4207 C CG2 . ILE   B 18  ? 0.2026 0.1546 0.2155 -0.0420 -0.0186 -0.0105 18  ILE   B CG2 
4208 C CD1 . ILE   B 18  ? 0.2034 0.1821 0.2341 -0.0429 -0.0245 0.0117  18  ILE   B CD1 
4220 N N   . LYS   B 19  ? 0.2042 0.1473 0.2188 -0.0249 0.0259  -0.0376 19  LYS   B N   
4221 C CA  . LYS   B 19  ? 0.2105 0.1495 0.2276 -0.0293 0.0227  -0.0416 19  LYS   B CA  
4222 C C   . LYS   B 19  ? 0.1955 0.1522 0.2417 -0.0270 0.0261  -0.0438 19  LYS   B C   
4223 O O   . LYS   B 19  ? 0.1874 0.1573 0.2264 -0.0229 0.0187  -0.0401 19  LYS   B O   
4224 C CB  . LYS   B 19  ? 0.2360 0.1749 0.2323 -0.0330 0.0327  -0.0296 19  LYS   B CB  
4225 C CG  . LYS   B 19  ? 0.2641 0.2003 0.2526 -0.0411 0.0420  -0.0283 19  LYS   B CG  
4226 C CD  . LYS   B 19  ? 0.2882 0.2310 0.2635 -0.0483 0.0548  -0.0232 19  LYS   B CD  
4227 C CE  . LYS   B 19  ? 0.3110 0.2552 0.2858 -0.0500 0.0531  -0.0229 19  LYS   B CE  
4228 N NZ  . LYS   B 19  ? 0.3265 0.2697 0.2974 -0.0522 0.0569  -0.0202 19  LYS   B NZ  
4242 N N   . ASN   B 20  ? 0.1958 0.1604 0.2714 -0.0189 0.0318  -0.0577 20  ASN   B N   
4243 C CA  . ASN   B 20  ? 0.1953 0.1769 0.2986 -0.0121 0.0372  -0.0738 20  ASN   B CA  
4244 C C   . ASN   B 20  ? 0.1908 0.1924 0.2996 -0.0194 0.0467  -0.0820 20  ASN   B C   
4245 O O   . ASN   B 20  ? 0.2099 0.2325 0.3148 -0.0345 0.0468  -0.0795 20  ASN   B O   
4246 C CB  . ASN   B 20  ? 0.2176 0.1839 0.3297 0.0055  0.0312  -0.0742 20  ASN   B CB  
4247 C CG  . ASN   B 20  ? 0.2425 0.1956 0.3483 0.0327  0.0299  -0.0843 20  ASN   B CG  
4248 O OD1 . ASN   B 20  ? 0.2697 0.2275 0.3719 0.0461  0.0294  -0.0785 20  ASN   B OD1 
4249 N ND2 . ASN   B 20  ? 0.2311 0.1922 0.3453 0.0302  0.0170  -0.0862 20  ASN   B ND2 
4256 N N   . ALA   B 21  ? 0.1943 0.1767 0.2988 -0.0263 0.0499  -0.0644 21  ALA   B N   
4257 C CA  . ALA   B 21  ? 0.2044 0.1833 0.3059 -0.0295 0.0392  -0.0496 21  ALA   B CA  
4258 C C   . ALA   B 21  ? 0.2038 0.1614 0.2934 -0.0208 0.0369  -0.0340 21  ALA   B C   
4259 O O   . ALA   B 21  ? 0.2053 0.1518 0.2943 -0.0288 0.0295  -0.0275 21  ALA   B O   
4260 C CB  . ALA   B 21  ? 0.2191 0.2114 0.3099 -0.0350 0.0418  -0.0391 21  ALA   B CB  
4266 N N   . ASP   B 22  ? 0.1964 0.1502 0.2832 -0.0209 0.0322  -0.0273 22  ASP   B N   
4267 C CA  . ASP   B 22  ? 0.1887 0.1455 0.2729 -0.0101 0.0238  -0.0217 22  ASP   B CA  
4268 C C   . ASP   B 22  ? 0.1788 0.1432 0.2330 -0.0180 0.0129  -0.0147 22  ASP   B C   
4269 O O   . ASP   B 22  ? 0.1805 0.1472 0.2342 -0.0079 0.0052  -0.0094 22  ASP   B O   
4270 C CB  . ASP   B 22  ? 0.1956 0.1572 0.3052 -0.0054 0.0220  -0.0124 22  ASP   B CB  
4271 C CG  . ASP   B 22  ? 0.1973 0.1747 0.3405 -0.0027 0.0008  -0.0072 22  ASP   B CG  
4272 O OD1 . ASP   B 22  ? 0.2060 0.1678 0.3372 -0.0019 -0.0121 -0.0059 22  ASP   B OD1 
4273 O OD2 . ASP   B 22  ? 0.2060 0.2069 0.3895 0.0075  -0.0167 -0.0155 22  ASP   B OD2 
4278 N N   . ILE   B 23  ? 0.1833 0.1391 0.2070 -0.0115 0.0027  0.0076  23  ILE   B N   
4279 C CA  . ILE   B 23  ? 0.1699 0.1380 0.1907 -0.0123 -0.0027 0.0030  23  ILE   B CA  
4280 C C   . ILE   B 23  ? 0.1591 0.1371 0.1931 -0.0095 -0.0082 0.0042  23  ILE   B C   
4281 O O   . ILE   B 23  ? 0.1510 0.1388 0.1871 -0.0125 -0.0070 0.0092  23  ILE   B O   
4282 C CB  . ILE   B 23  ? 0.1641 0.1449 0.2080 -0.0197 -0.0033 0.0137  23  ILE   B CB  
4283 C CG1 . ILE   B 23  ? 0.1690 0.1575 0.2237 -0.0134 0.0050  0.0240  23  ILE   B CG1 
4284 C CG2 . ILE   B 23  ? 0.1740 0.1698 0.2150 -0.0190 -0.0047 0.0068  23  ILE   B CG2 
4285 C CD1 . ILE   B 23  ? 0.1730 0.1663 0.2362 -0.0135 0.0090  0.0188  23  ILE   B CD1 
4297 N N   . VAL   B 24  ? 0.1634 0.1394 0.2030 -0.0121 -0.0045 -0.0001 24  VAL   B N   
4298 C CA  . VAL   B 24  ? 0.1578 0.1472 0.2230 -0.0055 -0.0148 -0.0014 24  VAL   B CA  
4299 C C   . VAL   B 24  ? 0.1560 0.1505 0.2323 -0.0126 -0.0116 0.0055  24  VAL   B C   
4300 O O   . VAL   B 24  ? 0.1534 0.1574 0.2408 -0.0194 -0.0060 0.0144  24  VAL   B O   
4301 C CB  . VAL   B 24  ? 0.1664 0.1650 0.2295 0.0034  -0.0240 0.0004  24  VAL   B CB  
4302 C CG1 . VAL   B 24  ? 0.1657 0.1713 0.2538 -0.0044 -0.0290 0.0026  24  VAL   B CG1 
4303 C CG2 . VAL   B 24  ? 0.1771 0.1892 0.2307 0.0084  -0.0294 -0.0092 24  VAL   B CG2 
4313 N N   . GLU   B 25  ? 0.1747 0.1625 0.2328 -0.0108 -0.0040 0.0032  25  GLU   B N   
4314 C CA  . GLU   B 25  ? 0.1890 0.1862 0.2512 -0.0004 0.0096  -0.0038 25  GLU   B CA  
4315 C C   . GLU   B 25  ? 0.1824 0.1818 0.2234 -0.0096 0.0113  0.0005  25  GLU   B C   
4316 O O   . GLU   B 25  ? 0.1829 0.1966 0.2344 -0.0114 0.0118  0.0024  25  GLU   B O   
4317 C CB  . GLU   B 25  ? 0.2252 0.2275 0.3123 0.0248  0.0226  -0.0093 25  GLU   B CB  
4318 C CG  . GLU   B 25  ? 0.2682 0.2859 0.4141 0.0317  0.0180  -0.0090 25  GLU   B CG  
4319 C CD  . GLU   B 25  ? 0.3184 0.3437 0.4999 0.0260  0.0133  -0.0112 25  GLU   B CD  
4320 O OE1 . GLU   B 25  ? 0.3329 0.3666 0.5293 0.0308  0.0166  -0.0103 25  GLU   B OE1 
4321 O OE2 . GLU   B 25  ? 0.3284 0.3633 0.5256 0.0236  0.0079  -0.0173 25  GLU   B OE2 
4328 N N   . GLU   B 26  ? 0.1784 0.1708 0.1997 -0.0245 0.0054  -0.0001 26  GLU   B N   
4329 C CA  . GLU   B 26  ? 0.1812 0.1831 0.2038 -0.0385 -0.0116 0.0032  26  GLU   B CA  
4330 C C   . GLU   B 26  ? 0.1634 0.1823 0.1933 -0.0272 -0.0018 0.0199  26  GLU   B C   
4331 O O   . GLU   B 26  ? 0.1801 0.2022 0.2041 -0.0200 -0.0017 0.0243  26  GLU   B O   
4332 C CB  . GLU   B 26  ? 0.2164 0.2033 0.2135 -0.0462 -0.0022 0.0186  26  GLU   B CB  
4333 C CG  . GLU   B 26  ? 0.2575 0.2393 0.2662 -0.0541 0.0113  -0.0035 26  GLU   B CG  
4334 C CD  . GLU   B 26  ? 0.2838 0.2629 0.2855 -0.0744 0.0253  -0.0395 26  GLU   B CD  
4335 O OE1 . GLU   B 26  ? 0.3039 0.2469 0.2929 -0.0839 0.0663  -0.0443 26  GLU   B OE1 
4336 O OE2 . GLU   B 26  ? 0.2885 0.3013 0.3224 -0.0689 0.0237  -0.0325 26  GLU   B OE2 
4343 N N   . ALA   B 27  ? 0.1545 0.1659 0.1923 -0.0225 0.0071  0.0229  27  ALA   B N   
4344 C CA  . ALA   B 27  ? 0.1490 0.1647 0.2121 -0.0157 -0.0030 0.0339  27  ALA   B CA  
4345 C C   . ALA   B 27  ? 0.1526 0.1745 0.2397 -0.0146 0.0078  0.0464  27  ALA   B C   
4346 O O   . ALA   B 27  ? 0.1635 0.1813 0.2503 -0.0027 0.0134  0.0509  27  ALA   B O   
4347 C CB  . ALA   B 27  ? 0.1648 0.1469 0.2174 -0.0200 0.0000  0.0295  27  ALA   B CB  
4353 N N   . LYS   B 28  ? 0.1497 0.1906 0.2744 -0.0199 0.0151  0.0595  28  LYS   B N   
4354 C CA  . LYS   B 28  ? 0.1680 0.2298 0.2921 -0.0071 0.0448  0.0823  28  LYS   B CA  
4355 C C   . LYS   B 28  ? 0.1982 0.2470 0.2774 0.0007  0.0612  0.0761  28  LYS   B C   
4356 O O   . LYS   B 28  ? 0.2242 0.2491 0.2913 -0.0022 0.0669  0.0761  28  LYS   B O   
4357 C CB  . LYS   B 28  ? 0.1859 0.2632 0.3375 0.0047  0.0703  0.1024  28  LYS   B CB  
4358 C CG  . LYS   B 28  ? 0.2152 0.3113 0.3783 0.0135  0.0808  0.1119  28  LYS   B CG  
4359 C CD  . LYS   B 28  ? 0.2622 0.3670 0.4361 0.0194  0.0949  0.1120  28  LYS   B CD  
4360 C CE  . LYS   B 28  ? 0.3031 0.4096 0.4801 0.0270  0.1003  0.1153  28  LYS   B CE  
4361 N NZ  . LYS   B 28  ? 0.3198 0.4256 0.5007 0.0334  0.1000  0.1204  28  LYS   B NZ  
4375 N N   . LYS   B 29  ? 0.2154 0.2744 0.2715 0.0185  0.0644  0.0662  29  LYS   B N   
4376 C CA  . LYS   B 29  ? 0.2564 0.3089 0.3023 0.0180  0.0626  0.0633  29  LYS   B CA  
4377 C C   . LYS   B 29  ? 0.2470 0.3077 0.2700 0.0147  0.0483  0.0733  29  LYS   B C   
4378 O O   . LYS   B 29  ? 0.2638 0.3269 0.2821 0.0193  0.0460  0.0796  29  LYS   B O   
4379 C CB  . LYS   B 29  ? 0.3141 0.3464 0.3816 0.0170  0.0653  0.0503  29  LYS   B CB  
4380 C CG  . LYS   B 29  ? 0.3653 0.3781 0.4688 0.0128  0.0680  0.0452  29  LYS   B CG  
4381 C CD  . LYS   B 29  ? 0.4107 0.4022 0.5381 0.0084  0.0758  0.0379  29  LYS   B CD  
4382 C CE  . LYS   B 29  ? 0.4433 0.4182 0.5855 0.0038  0.0844  0.0337  29  LYS   B CE  
4383 N NZ  . LYS   B 29  ? 0.4577 0.4265 0.6136 0.0013  0.0875  0.0311  29  LYS   B NZ  
4397 N N   . VAL   B 30  ? 0.2172 0.2865 0.2522 0.0024  0.0332  0.0717  30  VAL   B N   
4398 C CA  . VAL   B 30  ? 0.2058 0.2743 0.2712 -0.0126 0.0000  0.0747  30  VAL   B CA  
4399 C C   . VAL   B 30  ? 0.1840 0.2593 0.2654 -0.0123 0.0001  0.0898  30  VAL   B C   
4400 O O   . VAL   B 30  ? 0.1981 0.2774 0.2704 -0.0002 0.0041  0.1065  30  VAL   B O   
4401 C CB  . VAL   B 30  ? 0.2124 0.2751 0.3061 -0.0275 -0.0203 0.0720  30  VAL   B CB  
4402 C CG1 . VAL   B 30  ? 0.2198 0.2824 0.3080 -0.0308 -0.0121 0.0676  30  VAL   B CG1 
4403 C CG2 . VAL   B 30  ? 0.2234 0.2768 0.3226 -0.0353 -0.0300 0.0598  30  VAL   B CG2 
4413 N N   A LYS   B 31  ? 0.1663 0.2291 0.2952 -0.0259 0.0017  0.0979  31  LYS   B N   
4414 N N   B LYS   B 31  ? 0.1873 0.2420 0.2709 -0.0195 -0.0079 0.0816  31  LYS   B N   
4415 C CA  A LYS   B 31  ? 0.1512 0.2254 0.3305 -0.0368 0.0002  0.1016  31  LYS   B CA  
4416 C CA  B LYS   B 31  ? 0.1913 0.2326 0.2849 -0.0249 -0.0158 0.0720  31  LYS   B CA  
4417 C C   A LYS   B 31  ? 0.1500 0.1897 0.2913 -0.0291 -0.0242 0.0896  31  LYS   B C   
4418 C C   B LYS   B 31  ? 0.1784 0.1970 0.2568 -0.0284 -0.0319 0.0646  31  LYS   B C   
4419 O O   A LYS   B 31  ? 0.1573 0.1963 0.3060 -0.0222 -0.0213 0.1038  31  LYS   B O   
4420 O O   B LYS   B 31  ? 0.1818 0.2011 0.2544 -0.0282 -0.0373 0.0669  31  LYS   B O   
4421 C CB  A LYS   B 31  ? 0.1682 0.2686 0.3821 -0.0318 0.0251  0.1106  31  LYS   B CB  
4422 C CB  B LYS   B 31  ? 0.2135 0.2597 0.3216 -0.0216 -0.0080 0.0659  31  LYS   B CB  
4423 C CG  A LYS   B 31  ? 0.1914 0.3095 0.4239 -0.0285 0.0339  0.1034  31  LYS   B CG  
4424 C CG  B LYS   B 31  ? 0.2348 0.2831 0.3530 -0.0205 -0.0041 0.0532  31  LYS   B CG  
4425 C CD  A LYS   B 31  ? 0.2160 0.3490 0.4592 -0.0235 0.0281  0.0911  31  LYS   B CD  
4426 C CD  B LYS   B 31  ? 0.2527 0.3034 0.3818 -0.0193 -0.0034 0.0421  31  LYS   B CD  
4427 C CE  A LYS   B 31  ? 0.2316 0.3757 0.4894 -0.0200 0.0164  0.0807  31  LYS   B CE  
4428 C CE  B LYS   B 31  ? 0.2643 0.3171 0.4058 -0.0181 -0.0042 0.0348  31  LYS   B CE  
4429 N NZ  A LYS   B 31  ? 0.2498 0.3915 0.5030 -0.0108 0.0028  0.0708  31  LYS   B NZ  
4430 N NZ  B LYS   B 31  ? 0.2723 0.3257 0.4165 -0.0148 -0.0082 0.0290  31  LYS   B NZ  
4457 N N   . PRO   B 32  ? 0.1682 0.1593 0.2328 -0.0341 -0.0400 0.0545  32  PRO   B N   
4458 C CA  . PRO   B 32  ? 0.1793 0.1481 0.1919 -0.0350 -0.0378 0.0278  32  PRO   B CA  
4459 C C   . PRO   B 32  ? 0.1886 0.1387 0.1994 -0.0384 -0.0510 0.0314  32  PRO   B C   
4460 O O   . PRO   B 32  ? 0.2006 0.1402 0.2327 -0.0416 -0.0715 0.0331  32  PRO   B O   
4461 C CB  . PRO   B 32  ? 0.1925 0.1455 0.1937 -0.0375 -0.0299 0.0141  32  PRO   B CB  
4462 C CG  . PRO   B 32  ? 0.2046 0.1349 0.2003 -0.0331 -0.0479 0.0212  32  PRO   B CG  
4463 C CD  . PRO   B 32  ? 0.1906 0.1412 0.2156 -0.0262 -0.0621 0.0312  32  PRO   B CD  
4471 N N   . THR   B 33  ? 0.1917 0.1304 0.1878 -0.0307 -0.0526 0.0225  33  THR   B N   
4472 C CA  . THR   B 33  ? 0.1961 0.1372 0.1830 -0.0367 -0.0450 0.0305  33  THR   B CA  
4473 C C   . THR   B 33  ? 0.1972 0.1285 0.1771 -0.0352 -0.0496 0.0206  33  THR   B C   
4474 O O   . THR   B 33  ? 0.2181 0.1299 0.1871 -0.0440 -0.0576 0.0176  33  THR   B O   
4475 C CB  . THR   B 33  ? 0.2070 0.1470 0.1873 -0.0204 -0.0503 0.0287  33  THR   B CB  
4476 O OG1 . THR   B 33  ? 0.1932 0.1549 0.1943 -0.0230 -0.0490 0.0340  33  THR   B OG1 
4477 C CG2 . THR   B 33  ? 0.2316 0.1551 0.1996 -0.0112 -0.0481 0.0247  33  THR   B CG2 
4485 N N   . VAL   B 34  ? 0.1831 0.1296 0.1700 -0.0344 -0.0433 0.0169  34  VAL   B N   
4486 C CA  . VAL   B 34  ? 0.1698 0.1243 0.1697 -0.0277 -0.0343 0.0075  34  VAL   B CA  
4487 C C   . VAL   B 34  ? 0.1527 0.1199 0.1526 -0.0235 -0.0220 0.0070  34  VAL   B C   
4488 O O   . VAL   B 34  ? 0.1723 0.1211 0.1570 -0.0222 -0.0354 0.0034  34  VAL   B O   
4489 C CB  . VAL   B 34  ? 0.1714 0.1332 0.1954 -0.0092 -0.0382 0.0020  34  VAL   B CB  
4490 C CG1 . VAL   B 34  ? 0.1693 0.1478 0.1986 -0.0060 -0.0159 -0.0012 34  VAL   B CG1 
4491 C CG2 . VAL   B 34  ? 0.1779 0.1408 0.2247 -0.0087 -0.0362 0.0099  34  VAL   B CG2 
4501 N N   . VAL   B 35  ? 0.1407 0.1209 0.1427 -0.0238 -0.0178 0.0098  35  VAL   B N   
4502 C CA  . VAL   B 35  ? 0.1353 0.1178 0.1483 -0.0220 -0.0137 0.0069  35  VAL   B CA  
4503 C C   . VAL   B 35  ? 0.1276 0.1139 0.1482 -0.0163 -0.0189 0.0105  35  VAL   B C   
4504 O O   . VAL   B 35  ? 0.1345 0.1192 0.1603 -0.0222 -0.0045 -0.0048 35  VAL   B O   
4505 C CB  . VAL   B 35  ? 0.1364 0.1358 0.1580 -0.0189 0.0001  0.0061  35  VAL   B CB  
4506 C CG1 . VAL   B 35  ? 0.1311 0.1433 0.1724 -0.0225 -0.0013 -0.0001 35  VAL   B CG1 
4507 C CG2 . VAL   B 35  ? 0.1397 0.1410 0.1774 -0.0087 -0.0019 0.0015  35  VAL   B CG2 
4517 N N   . VAL   B 36  ? 0.1304 0.1152 0.1466 -0.0161 -0.0159 0.0092  36  VAL   B N   
4518 C CA  . VAL   B 36  ? 0.1264 0.1149 0.1482 -0.0166 -0.0071 0.0089  36  VAL   B CA  
4519 C C   . VAL   B 36  ? 0.1247 0.1120 0.1408 -0.0137 -0.0025 0.0002  36  VAL   B C   
4520 O O   . VAL   B 36  ? 0.1324 0.1241 0.1605 -0.0104 -0.0009 -0.0035 36  VAL   B O   
4521 C CB  . VAL   B 36  ? 0.1278 0.1249 0.1513 -0.0168 -0.0061 0.0055  36  VAL   B CB  
4522 C CG1 . VAL   B 36  ? 0.1275 0.1383 0.1645 -0.0186 -0.0079 0.0039  36  VAL   B CG1 
4523 C CG2 . VAL   B 36  ? 0.1293 0.1259 0.1659 -0.0117 -0.0088 0.0066  36  VAL   B CG2 
4533 N N   . ASN   B 37  ? 0.1276 0.1197 0.1440 -0.0036 -0.0061 0.0055  37  ASN   B N   
4534 C CA  . ASN   B 37  ? 0.1260 0.1192 0.1557 -0.0017 -0.0160 0.0085  37  ASN   B CA  
4535 C C   . ASN   B 37  ? 0.1250 0.1192 0.1518 -0.0034 -0.0121 0.0056  37  ASN   B C   
4536 O O   . ASN   B 37  ? 0.1331 0.1294 0.1559 0.0024  -0.0003 0.0055  37  ASN   B O   
4537 C CB  . ASN   B 37  ? 0.1272 0.1264 0.1411 -0.0034 -0.0171 0.0044  37  ASN   B CB  
4538 C CG  . ASN   B 37  ? 0.1343 0.1227 0.1546 -0.0063 -0.0147 0.0025  37  ASN   B CG  
4539 O OD1 . ASN   B 37  ? 0.1421 0.1311 0.1694 0.0026  -0.0177 0.0032  37  ASN   B OD1 
4540 N ND2 . ASN   B 37  ? 0.1404 0.1237 0.1488 -0.0021 -0.0179 0.0086  37  ASN   B ND2 
4547 N N   . ALA   B 38  ? 0.1383 0.1184 0.1511 0.0045  0.0015  0.0087  38  ALA   B N   
4548 C CA  . ALA   B 38  ? 0.1458 0.1248 0.1592 0.0015  -0.0019 0.0109  38  ALA   B CA  
4549 C C   . ALA   B 38  ? 0.1372 0.1202 0.1569 -0.0040 0.0009  0.0095  38  ALA   B C   
4550 O O   . ALA   B 38  ? 0.1516 0.1311 0.1660 0.0041  -0.0020 0.0081  38  ALA   B O   
4551 C CB  . ALA   B 38  ? 0.1688 0.1331 0.1638 -0.0111 0.0026  0.0104  38  ALA   B CB  
4557 N N   . ALA   B 39  ? 0.1429 0.1221 0.1491 0.0034  -0.0013 0.0048  39  ALA   B N   
4558 C CA  . ALA   B 39  ? 0.1526 0.1294 0.1437 -0.0001 -0.0096 0.0122  39  ALA   B CA  
4559 C C   . ALA   B 39  ? 0.1538 0.1328 0.1394 0.0072  -0.0082 0.0062  39  ALA   B C   
4560 O O   . ALA   B 39  ? 0.1578 0.1432 0.1667 -0.0031 -0.0034 0.0117  39  ALA   B O   
4561 C CB  . ALA   B 39  ? 0.1520 0.1362 0.1624 -0.0073 -0.0054 -0.0019 39  ALA   B CB  
4567 N N   . ASN   B 40  ? 0.1551 0.1515 0.1370 -0.0046 -0.0010 -0.0063 40  ASN   B N   
4568 C CA  . ASN   B 40  ? 0.1650 0.1593 0.1534 0.0001  -0.0097 -0.0070 40  ASN   B CA  
4569 C C   . ASN   B 40  ? 0.1672 0.1622 0.1398 0.0013  -0.0074 0.0039  40  ASN   B C   
4570 O O   . ASN   B 40  ? 0.1601 0.1562 0.1440 0.0039  -0.0076 0.0009  40  ASN   B O   
4571 C CB  . ASN   B 40  ? 0.1783 0.1596 0.1753 0.0093  -0.0163 0.0174  40  ASN   B CB  
4572 C CG  . ASN   B 40  ? 0.1796 0.1678 0.2038 0.0058  -0.0286 0.0198  40  ASN   B CG  
4573 O OD1 . ASN   B 40  ? 0.1785 0.1668 0.2819 0.0053  -0.0368 0.0205  40  ASN   B OD1 
4574 N ND2 . ASN   B 40  ? 0.1836 0.1698 0.2050 0.0031  -0.0202 0.0204  40  ASN   B ND2 
4581 N N   . VAL   B 41  ? 0.1781 0.1648 0.1455 0.0103  0.0020  -0.0015 41  VAL   B N   
4582 C CA  . VAL   B 41  ? 0.1809 0.1763 0.1516 0.0054  0.0013  -0.0067 41  VAL   B CA  
4583 C C   . VAL   B 41  ? 0.1804 0.1753 0.1468 0.0168  -0.0039 -0.0118 41  VAL   B C   
4584 O O   . VAL   B 41  ? 0.1794 0.1720 0.1595 0.0098  -0.0124 -0.0133 41  VAL   B O   
4585 C CB  . VAL   B 41  ? 0.1951 0.1996 0.1805 -0.0060 0.0157  -0.0190 41  VAL   B CB  
4586 C CG1 . VAL   B 41  ? 0.1922 0.1995 0.1853 -0.0103 0.0260  -0.0241 41  VAL   B CG1 
4587 C CG2 . VAL   B 41  ? 0.2089 0.2213 0.1938 -0.0172 0.0114  -0.0164 41  VAL   B CG2 
4597 N N   . TYR   B 42  ? 0.1863 0.1778 0.1471 0.0151  -0.0182 0.0022  42  TYR   B N   
4598 C CA  . TYR   B 42  ? 0.1884 0.1839 0.1583 0.0152  -0.0248 -0.0119 42  TYR   B CA  
4599 C C   . TYR   B 42  ? 0.1723 0.1622 0.1709 0.0193  -0.0226 -0.0108 42  TYR   B C   
4600 O O   . TYR   B 42  ? 0.1790 0.1688 0.2025 0.0126  -0.0270 -0.0122 42  TYR   B O   
4601 C CB  . TYR   B 42  ? 0.2152 0.2146 0.1767 0.0128  -0.0287 0.0054  42  TYR   B CB  
4602 C CG  . TYR   B 42  ? 0.2204 0.2315 0.1658 0.0013  -0.0275 0.0180  42  TYR   B CG  
4603 C CD1 . TYR   B 42  ? 0.2194 0.2334 0.1417 -0.0011 -0.0137 0.0120  42  TYR   B CD1 
4604 C CD2 . TYR   B 42  ? 0.2335 0.2461 0.2019 -0.0003 -0.0109 0.0230  42  TYR   B CD2 
4605 C CE1 . TYR   B 42  ? 0.2299 0.2470 0.1596 0.0048  -0.0055 0.0135  42  TYR   B CE1 
4606 C CE2 . TYR   B 42  ? 0.2382 0.2523 0.2007 0.0073  0.0114  0.0360  42  TYR   B CE2 
4607 C CZ  . TYR   B 42  ? 0.2488 0.2638 0.1905 0.0196  0.0165  0.0209  42  TYR   B CZ  
4608 O OH  . TYR   B 42  ? 0.2828 0.2936 0.2355 0.0317  0.0251  0.0274  42  TYR   B OH  
4618 N N   . LEU   B 43  ? 0.1608 0.1487 0.1606 0.0099  -0.0139 -0.0108 43  LEU   B N   
4619 C CA  . LEU   B 43  ? 0.1600 0.1489 0.1506 0.0002  -0.0164 -0.0053 43  LEU   B CA  
4620 C C   . LEU   B 43  ? 0.1644 0.1507 0.1553 -0.0029 -0.0184 -0.0003 43  LEU   B C   
4621 O O   . LEU   B 43  ? 0.1580 0.1548 0.1851 0.0037  -0.0223 0.0058  43  LEU   B O   
4622 C CB  . LEU   B 43  ? 0.1599 0.1450 0.1616 -0.0020 -0.0243 -0.0024 43  LEU   B CB  
4623 C CG  . LEU   B 43  ? 0.1655 0.1417 0.1697 0.0014  -0.0285 -0.0041 43  LEU   B CG  
4624 C CD1 . LEU   B 43  ? 0.1756 0.1425 0.1999 0.0007  -0.0431 -0.0066 43  LEU   B CD1 
4625 C CD2 . LEU   B 43  ? 0.1620 0.1424 0.1904 -0.0040 -0.0287 -0.0072 43  LEU   B CD2 
4637 N N   . LYS   B 44  ? 0.1632 0.1500 0.1638 0.0058  -0.0157 -0.0051 44  LYS   B N   
4638 C CA  . LYS   B 44  ? 0.1781 0.1590 0.1713 0.0067  -0.0143 0.0063  44  LYS   B CA  
4639 C C   . LYS   B 44  ? 0.1676 0.1544 0.1624 0.0106  -0.0155 0.0055  44  LYS   B C   
4640 O O   . LYS   B 44  ? 0.1855 0.1539 0.1930 -0.0008 -0.0102 0.0033  44  LYS   B O   
4641 C CB  . LYS   B 44  ? 0.2043 0.1795 0.1881 0.0137  -0.0262 0.0010  44  LYS   B CB  
4642 C CG  . LYS   B 44  ? 0.2431 0.2051 0.2167 0.0097  -0.0505 0.0052  44  LYS   B CG  
4643 C CD  . LYS   B 44  ? 0.2784 0.2260 0.2759 -0.0007 -0.0624 0.0070  44  LYS   B CD  
4644 C CE  . LYS   B 44  ? 0.3083 0.2517 0.3194 -0.0059 -0.0698 0.0156  44  LYS   B CE  
4645 N NZ  . LYS   B 44  ? 0.3197 0.2609 0.3462 -0.0040 -0.0776 0.0280  44  LYS   B NZ  
4659 N N   . HIS   B 45  ? 0.1552 0.1546 0.1636 0.0017  -0.0160 0.0105  45  HIS   B N   
4660 C CA  . HIS   B 45  ? 0.1610 0.1469 0.1656 0.0071  -0.0108 0.0066  45  HIS   B CA  
4661 C C   . HIS   B 45  ? 0.1864 0.1695 0.1994 0.0152  -0.0164 -0.0033 45  HIS   B C   
4662 O O   . HIS   B 45  ? 0.1967 0.2002 0.2440 0.0428  0.0021  -0.0023 45  HIS   B O   
4663 C CB  . HIS   B 45  ? 0.1536 0.1536 0.1622 -0.0062 -0.0154 -0.0022 45  HIS   B CB  
4664 C CG  . HIS   B 45  ? 0.1537 0.1499 0.1577 -0.0066 -0.0114 0.0024  45  HIS   B CG  
4665 N ND1 . HIS   B 45  ? 0.1602 0.1448 0.1651 -0.0021 -0.0166 -0.0057 45  HIS   B ND1 
4666 C CD2 . HIS   B 45  ? 0.1668 0.1513 0.1830 -0.0098 -0.0168 -0.0006 45  HIS   B CD2 
4667 C CE1 . HIS   B 45  ? 0.1719 0.1306 0.1594 -0.0024 -0.0271 -0.0032 45  HIS   B CE1 
4668 N NE2 . HIS   B 45  ? 0.1724 0.1414 0.1657 -0.0034 -0.0208 -0.0027 45  HIS   B NE2 
4676 N N   A GLY   B 46  ? 0.2012 0.1616 0.2281 0.0212  -0.0409 0.0051  46  GLY   B N   
4677 N N   B GLY   B 46  ? 0.1962 0.1749 0.2132 0.0169  -0.0278 0.0035  46  GLY   B N   
4678 C CA  A GLY   B 46  ? 0.2158 0.1785 0.2666 0.0166  -0.0500 0.0046  46  GLY   B CA  
4679 C CA  B GLY   B 46  ? 0.2054 0.1875 0.2334 0.0147  -0.0343 0.0079  46  GLY   B CA  
4680 C C   A GLY   B 46  ? 0.2116 0.1934 0.3127 0.0238  -0.0440 0.0014  46  GLY   B C   
4681 C C   B GLY   B 46  ? 0.2073 0.1993 0.2614 0.0169  -0.0328 0.0121  46  GLY   B C   
4682 O O   A GLY   B 46  ? 0.2204 0.2044 0.3918 0.0318  -0.0232 -0.0239 46  GLY   B O   
4683 O O   B GLY   B 46  ? 0.2124 0.2072 0.2683 0.0195  -0.0273 0.0209  46  GLY   B O   
4690 N N   . GLY   B 47  ? 0.2053 0.2062 0.2858 0.0101  -0.0256 0.0003  47  GLY   B N   
4691 C CA  . GLY   B 47  ? 0.1932 0.1790 0.2540 0.0042  -0.0191 0.0038  47  GLY   B CA  
4692 C C   . GLY   B 47  ? 0.1712 0.1554 0.2175 0.0036  -0.0001 0.0054  47  GLY   B C   
4693 O O   . GLY   B 47  ? 0.1842 0.1414 0.2217 0.0025  -0.0074 0.0137  47  GLY   B O   
4698 N N   . GLY   B 48  ? 0.1544 0.1474 0.2115 0.0017  -0.0112 0.0168  48  GLY   B N   
4699 C CA  . GLY   B 48  ? 0.1511 0.1444 0.2082 -0.0040 -0.0055 0.0107  48  GLY   B CA  
4700 C C   . GLY   B 48  ? 0.1457 0.1379 0.1935 0.0022  0.0044  0.0081  48  GLY   B C   
4701 O O   . GLY   B 48  ? 0.1429 0.1444 0.2167 0.0049  -0.0078 0.0037  48  GLY   B O   
4705 N N   . VAL   B 49  ? 0.1473 0.1419 0.1817 0.0135  0.0028  0.0074  49  VAL   B N   
4706 C CA  . VAL   B 49  ? 0.1506 0.1493 0.1771 0.0148  -0.0132 -0.0008 49  VAL   B CA  
4707 C C   . VAL   B 49  ? 0.1403 0.1429 0.1593 0.0136  -0.0086 0.0023  49  VAL   B C   
4708 O O   . VAL   B 49  ? 0.1486 0.1463 0.1803 0.0042  -0.0001 0.0054  49  VAL   B O   
4709 C CB  . VAL   B 49  ? 0.1521 0.1642 0.2035 0.0042  -0.0247 -0.0029 49  VAL   B CB  
4710 C CG1 . VAL   B 49  ? 0.1541 0.1724 0.1989 0.0092  -0.0314 0.0023  49  VAL   B CG1 
4711 C CG2 . VAL   B 49  ? 0.1727 0.1781 0.2181 -0.0045 -0.0397 -0.0011 49  VAL   B CG2 
4721 N N   . ALA   B 50  ? 0.1341 0.1380 0.1619 0.0026  -0.0019 0.0044  50  ALA   B N   
4722 C CA  . ALA   B 50  ? 0.1361 0.1313 0.1647 0.0046  -0.0036 0.0061  50  ALA   B CA  
4723 C C   . ALA   B 50  ? 0.1498 0.1337 0.1660 0.0053  -0.0005 0.0084  50  ALA   B C   
4724 O O   . ALA   B 50  ? 0.1463 0.1359 0.1625 0.0082  -0.0051 0.0036  50  ALA   B O   
4725 C CB  . ALA   B 50  ? 0.1448 0.1317 0.1681 0.0054  0.0002  0.0068  50  ALA   B CB  
4731 N N   . GLY   B 51  ? 0.1422 0.1497 0.1754 0.0127  -0.0123 0.0052  51  GLY   B N   
4732 C CA  . GLY   B 51  ? 0.1505 0.1536 0.1882 0.0162  -0.0196 0.0080  51  GLY   B CA  
4733 C C   . GLY   B 51  ? 0.1484 0.1493 0.1897 0.0214  -0.0118 0.0069  51  GLY   B C   
4734 O O   . GLY   B 51  ? 0.1486 0.1616 0.2058 0.0094  -0.0149 -0.0049 51  GLY   B O   
4738 N N   . ALA   B 52  ? 0.1506 0.1432 0.1833 0.0206  -0.0082 0.0090  52  ALA   B N   
4739 C CA  . ALA   B 52  ? 0.1512 0.1528 0.1834 0.0159  -0.0045 -0.0011 52  ALA   B CA  
4740 C C   . ALA   B 52  ? 0.1375 0.1532 0.1799 0.0085  -0.0001 0.0042  52  ALA   B C   
4741 O O   . ALA   B 52  ? 0.1397 0.1623 0.1962 0.0049  0.0005  0.0035  52  ALA   B O   
4742 C CB  . ALA   B 52  ? 0.1681 0.1541 0.1931 0.0109  0.0010  0.0064  52  ALA   B CB  
4748 N N   . LEU   B 53  ? 0.1329 0.1450 0.1722 0.0155  0.0030  0.0093  53  LEU   B N   
4749 C CA  . LEU   B 53  ? 0.1337 0.1517 0.1716 0.0116  -0.0046 0.0042  53  LEU   B CA  
4750 C C   . LEU   B 53  ? 0.1423 0.1457 0.1601 0.0107  0.0051  0.0141  53  LEU   B C   
4751 O O   . LEU   B 53  ? 0.1534 0.1518 0.1748 -0.0005 0.0038  0.0193  53  LEU   B O   
4752 C CB  . LEU   B 53  ? 0.1358 0.1600 0.1818 0.0084  -0.0051 0.0129  53  LEU   B CB  
4753 C CG  . LEU   B 53  ? 0.1323 0.1698 0.1793 0.0042  -0.0033 0.0223  53  LEU   B CG  
4754 C CD1 . LEU   B 53  ? 0.1399 0.1853 0.2132 0.0105  -0.0061 0.0056  53  LEU   B CD1 
4755 C CD2 . LEU   B 53  ? 0.1464 0.1976 0.2043 -0.0082 -0.0050 -0.0088 53  LEU   B CD2 
4767 N N   . ASN   B 54  ? 0.1392 0.1372 0.1582 0.0053  -0.0041 0.0114  54  ASN   B N   
4768 C CA  . ASN   B 54  ? 0.1470 0.1452 0.1756 0.0046  -0.0086 -0.0028 54  ASN   B CA  
4769 C C   . ASN   B 54  ? 0.1461 0.1473 0.1959 0.0036  0.0001  0.0027  54  ASN   B C   
4770 O O   . ASN   B 54  ? 0.1409 0.1556 0.2087 -0.0049 0.0017  0.0040  54  ASN   B O   
4771 C CB  . ASN   B 54  ? 0.1511 0.1582 0.1878 0.0067  -0.0041 0.0018  54  ASN   B CB  
4772 C CG  . ASN   B 54  ? 0.1457 0.1691 0.1873 0.0047  -0.0087 -0.0009 54  ASN   B CG  
4773 O OD1 . ASN   B 54  ? 0.1457 0.1679 0.1892 -0.0009 -0.0143 -0.0122 54  ASN   B OD1 
4774 N ND2 . ASN   B 54  ? 0.1599 0.1883 0.2105 -0.0048 -0.0316 0.0076  54  ASN   B ND2 
4781 N N   . LYS   B 55  ? 0.1422 0.1557 0.2095 0.0124  0.0004  0.0041  55  LYS   B N   
4782 C CA  . LYS   B 55  ? 0.1479 0.1686 0.2238 0.0197  -0.0027 0.0066  55  LYS   B CA  
4783 C C   . LYS   B 55  ? 0.1415 0.1662 0.2209 0.0118  0.0081  -0.0052 55  LYS   B C   
4784 O O   . LYS   B 55  ? 0.1364 0.1812 0.2423 0.0081  0.0065  -0.0051 55  LYS   B O   
4785 C CB  . LYS   B 55  ? 0.1623 0.1830 0.2636 0.0285  0.0055  0.0108  55  LYS   B CB  
4786 C CG  . LYS   B 55  ? 0.2017 0.2092 0.3416 0.0361  0.0191  0.0243  55  LYS   B CG  
4787 C CD  . LYS   B 55  ? 0.2371 0.2353 0.4054 0.0417  0.0348  0.0339  55  LYS   B CD  
4788 C CE  . LYS   B 55  ? 0.2626 0.2590 0.4660 0.0435  0.0498  0.0370  55  LYS   B CE  
4789 N NZ  . LYS   B 55  ? 0.2690 0.2748 0.4944 0.0420  0.0404  0.0455  55  LYS   B NZ  
4803 N N   . ALA   B 56  ? 0.1415 0.1743 0.2022 0.0074  0.0008  -0.0137 56  ALA   B N   
4804 C CA  . ALA   B 56  ? 0.1539 0.1916 0.2013 0.0037  0.0007  -0.0100 56  ALA   B CA  
4805 C C   . ALA   B 56  ? 0.1536 0.1824 0.1944 0.0046  0.0096  -0.0000 56  ALA   B C   
4806 O O   . ALA   B 56  ? 0.1675 0.1952 0.2149 0.0071  0.0288  -0.0014 56  ALA   B O   
4807 C CB  . ALA   B 56  ? 0.1655 0.2124 0.2049 -0.0080 -0.0061 -0.0158 56  ALA   B CB  
4813 N N   . THR   B 57  ? 0.1452 0.1716 0.2039 -0.0018 0.0182  0.0060  57  THR   B N   
4814 C CA  . THR   B 57  ? 0.1533 0.1762 0.2012 -0.0008 0.0204  0.0109  57  THR   B CA  
4815 C C   . THR   B 57  ? 0.1505 0.1860 0.2128 -0.0007 0.0176  0.0092  57  THR   B C   
4816 O O   . THR   B 57  ? 0.1576 0.1907 0.2165 -0.0212 0.0123  0.0083  57  THR   B O   
4817 C CB  . THR   B 57  ? 0.1574 0.1590 0.1835 0.0002  0.0169  0.0144  57  THR   B CB  
4818 O OG1 . THR   B 57  ? 0.1556 0.1562 0.2073 -0.0066 0.0155  0.0073  57  THR   B OG1 
4819 C CG2 . THR   B 57  ? 0.1537 0.1676 0.1738 -0.0021 0.0180  0.0103  57  THR   B CG2 
4827 N N   . ASN   B 58  ? 0.1370 0.2083 0.2413 -0.0081 0.0009  -0.0068 58  ASN   B N   
4828 C CA  . ASN   B 58  ? 0.1673 0.2548 0.2840 -0.0205 0.0253  0.0033  58  ASN   B CA  
4829 C C   . ASN   B 58  ? 0.1446 0.2274 0.2399 -0.0169 -0.0020 0.0050  58  ASN   B C   
4830 O O   . ASN   B 58  ? 0.1503 0.2350 0.2451 -0.0206 -0.0051 -0.0029 58  ASN   B O   
4831 C CB  . ASN   B 58  ? 0.2630 0.3321 0.4085 -0.0332 0.0614  0.0168  58  ASN   B CB  
4832 C CG  . ASN   B 58  ? 0.3671 0.4001 0.5493 -0.0367 0.0771  0.0369  58  ASN   B CG  
4833 O OD1 . ASN   B 58  ? 0.3948 0.4238 0.6006 -0.0381 0.0812  0.0420  58  ASN   B OD1 
4834 N ND2 . ASN   B 58  ? 0.4490 0.4490 0.5968 -0.0391 0.0837  0.0434  58  ASN   B ND2 
4841 N N   . ASN   B 59  ? 0.1446 0.2117 0.2245 -0.0116 -0.0061 0.0067  59  ASN   B N   
4842 C CA  . ASN   B 59  ? 0.1492 0.2080 0.2120 -0.0135 -0.0172 0.0151  59  ASN   B CA  
4843 C C   . ASN   B 59  ? 0.1460 0.1947 0.2041 -0.0169 -0.0159 0.0017  59  ASN   B C   
4844 O O   . ASN   B 59  ? 0.1479 0.1960 0.2026 -0.0183 -0.0105 0.0017  59  ASN   B O   
4845 C CB  . ASN   B 59  ? 0.1601 0.2221 0.2221 -0.0061 -0.0277 0.0162  59  ASN   B CB  
4846 C CG  . ASN   B 59  ? 0.1727 0.2383 0.2396 -0.0037 -0.0379 0.0100  59  ASN   B CG  
4847 O OD1 . ASN   B 59  ? 0.1736 0.2436 0.2410 -0.0027 -0.0216 0.0210  59  ASN   B OD1 
4848 N ND2 . ASN   B 59  ? 0.1798 0.2510 0.2489 -0.0090 -0.0430 0.0012  59  ASN   B ND2 
4855 N N   . ALA   B 60  ? 0.1495 0.1805 0.2106 -0.0167 -0.0027 0.0034  60  ALA   B N   
4856 C CA  . ALA   B 60  ? 0.1518 0.1693 0.2162 -0.0229 -0.0039 0.0115  60  ALA   B CA  
4857 C C   . ALA   B 60  ? 0.1530 0.1562 0.1892 -0.0158 -0.0105 0.0074  60  ALA   B C   
4858 O O   . ALA   B 60  ? 0.1510 0.1605 0.2007 -0.0209 -0.0047 -0.0057 60  ALA   B O   
4859 C CB  . ALA   B 60  ? 0.1652 0.1704 0.2422 -0.0179 0.0050  0.0110  60  ALA   B CB  
4865 N N   . MET   B 61  ? 0.1483 0.1487 0.1827 -0.0082 -0.0032 0.0081  61  MET   B N   
4866 C CA  . MET   B 61  ? 0.1434 0.1460 0.1810 -0.0062 -0.0104 0.0075  61  MET   B CA  
4867 C C   . MET   B 61  ? 0.1484 0.1449 0.1826 -0.0124 -0.0127 0.0087  61  MET   B C   
4868 O O   . MET   B 61  ? 0.1522 0.1449 0.1664 -0.0004 -0.0034 -0.0097 61  MET   B O   
4869 C CB  . MET   B 61  ? 0.1397 0.1506 0.1833 -0.0014 -0.0094 0.0018  61  MET   B CB  
4870 C CG  . MET   B 61  ? 0.1369 0.1493 0.1788 -0.0028 -0.0069 0.0040  61  MET   B CG  
4871 S SD  . MET   B 61  ? 0.1406 0.1491 0.1886 -0.0029 -0.0066 -0.0069 61  MET   B SD  
4872 C CE  . MET   B 61  ? 0.1493 0.1685 0.2204 0.0009  0.0028  -0.0172 61  MET   B CE  
4882 N N   . GLN   B 62  ? 0.1491 0.1534 0.1714 -0.0068 -0.0164 0.0070  62  GLN   B N   
4883 C CA  . GLN   B 62  ? 0.1493 0.1601 0.1786 -0.0060 -0.0226 0.0005  62  GLN   B CA  
4884 C C   . GLN   B 62  ? 0.1468 0.1638 0.1892 -0.0059 -0.0262 -0.0018 62  GLN   B C   
4885 O O   . GLN   B 62  ? 0.1597 0.1625 0.1966 -0.0034 -0.0351 -0.0078 62  GLN   B O   
4886 C CB  . GLN   B 62  ? 0.1476 0.1642 0.1801 0.0019  -0.0166 0.0072  62  GLN   B CB  
4887 C CG  . GLN   B 62  ? 0.1533 0.1646 0.1847 -0.0012 -0.0250 -0.0006 62  GLN   B CG  
4888 C CD  . GLN   B 62  ? 0.1539 0.1623 0.1780 0.0045  -0.0285 0.0066  62  GLN   B CD  
4889 O OE1 . GLN   B 62  ? 0.1516 0.1606 0.1950 0.0002  -0.0304 -0.0055 62  GLN   B OE1 
4890 N NE2 . GLN   B 62  ? 0.1513 0.1683 0.1893 0.0026  -0.0210 -0.0019 62  GLN   B NE2 
4899 N N   . VAL   B 63  ? 0.1460 0.1638 0.2078 -0.0101 -0.0221 -0.0032 63  VAL   B N   
4900 C CA  . VAL   B 63  ? 0.1623 0.1661 0.2244 -0.0175 -0.0290 -0.0039 63  VAL   B CA  
4901 C C   . VAL   B 63  ? 0.1651 0.1550 0.2057 -0.0216 -0.0350 -0.0162 63  VAL   B C   
4902 O O   . VAL   B 63  ? 0.1767 0.1551 0.2212 -0.0183 -0.0508 -0.0131 63  VAL   B O   
4903 C CB  . VAL   B 63  ? 0.1631 0.1853 0.2509 -0.0226 -0.0275 -0.0097 63  VAL   B CB  
4904 C CG1 . VAL   B 63  ? 0.1713 0.1887 0.2677 -0.0306 -0.0209 -0.0129 63  VAL   B CG1 
4905 C CG2 . VAL   B 63  ? 0.1594 0.2011 0.2610 -0.0108 -0.0304 -0.0119 63  VAL   B CG2 
4915 N N   . GLU   B 64  ? 0.1565 0.1477 0.1968 -0.0155 -0.0253 -0.0086 64  GLU   B N   
4916 C CA  . GLU   B 64  ? 0.1602 0.1443 0.1911 -0.0144 -0.0263 -0.0002 64  GLU   B CA  
4917 C C   . GLU   B 64  ? 0.1535 0.1427 0.1824 -0.0104 -0.0270 -0.0116 64  GLU   B C   
4918 O O   . GLU   B 64  ? 0.1661 0.1539 0.1795 -0.0099 -0.0271 -0.0141 64  GLU   B O   
4919 C CB  . GLU   B 64  ? 0.1563 0.1525 0.1892 -0.0247 -0.0249 0.0007  64  GLU   B CB  
4920 C CG  . GLU   B 64  ? 0.1657 0.1579 0.1905 -0.0305 -0.0279 -0.0084 64  GLU   B CG  
4921 C CD  . GLU   B 64  ? 0.1749 0.1666 0.1995 -0.0385 -0.0255 -0.0048 64  GLU   B CD  
4922 O OE1 . GLU   B 64  ? 0.1769 0.1829 0.2083 -0.0355 -0.0247 -0.0222 64  GLU   B OE1 
4923 O OE2 . GLU   B 64  ? 0.1835 0.1788 0.2068 -0.0425 -0.0383 -0.0054 64  GLU   B OE2 
4930 N N   . SER   B 65  ? 0.1536 0.1361 0.1773 -0.0101 -0.0166 -0.0132 65  SER   B N   
4931 C CA  . SER   B 65  ? 0.1579 0.1362 0.1824 -0.0000 -0.0176 -0.0164 65  SER   B CA  
4932 C C   . SER   B 65  ? 0.1578 0.1354 0.1828 -0.0016 -0.0262 -0.0211 65  SER   B C   
4933 O O   . SER   B 65  ? 0.1591 0.1520 0.1813 -0.0053 -0.0249 -0.0226 65  SER   B O   
4934 C CB  . SER   B 65  ? 0.1552 0.1468 0.1775 -0.0083 -0.0224 -0.0141 65  SER   B CB  
4935 O OG  . SER   B 65  ? 0.1574 0.1463 0.1803 -0.0084 -0.0187 -0.0197 65  SER   B OG  
4941 N N   . ASP   B 66  ? 0.1698 0.1456 0.1805 -0.0035 -0.0290 -0.0157 66  ASP   B N   
4942 C CA  . ASP   B 66  ? 0.1759 0.1586 0.1754 -0.0006 -0.0349 -0.0149 66  ASP   B CA  
4943 C C   . ASP   B 66  ? 0.1777 0.1585 0.1815 -0.0051 -0.0271 -0.0184 66  ASP   B C   
4944 O O   . ASP   B 66  ? 0.1813 0.1628 0.1816 0.0022  -0.0278 -0.0166 66  ASP   B O   
4945 C CB  . ASP   B 66  ? 0.1866 0.1731 0.1911 0.0116  -0.0432 -0.0187 66  ASP   B CB  
4946 C CG  . ASP   B 66  ? 0.2162 0.1905 0.2237 0.0202  -0.0533 -0.0020 66  ASP   B CG  
4947 O OD1 . ASP   B 66  ? 0.2409 0.1890 0.2312 0.0124  -0.0584 0.0072  66  ASP   B OD1 
4948 O OD2 . ASP   B 66  ? 0.2326 0.2129 0.2769 0.0336  -0.0486 -0.0013 66  ASP   B OD2 
4953 N N   . ASP   B 67  ? 0.1699 0.1538 0.1766 -0.0112 -0.0222 -0.0231 67  ASP   B N   
4954 C CA  . ASP   B 67  ? 0.1843 0.1477 0.1871 -0.0104 -0.0286 -0.0115 67  ASP   B CA  
4955 C C   . ASP   B 67  ? 0.1798 0.1504 0.1927 -0.0005 -0.0239 -0.0197 67  ASP   B C   
4956 O O   . ASP   B 67  ? 0.1874 0.1565 0.2055 -0.0027 -0.0139 -0.0239 67  ASP   B O   
4957 C CB  . ASP   B 67  ? 0.2071 0.1589 0.2086 -0.0230 -0.0387 -0.0054 67  ASP   B CB  
4958 C CG  . ASP   B 67  ? 0.2454 0.1672 0.2107 -0.0178 -0.0624 -0.0080 67  ASP   B CG  
4959 O OD1 . ASP   B 67  ? 0.2681 0.1752 0.2217 -0.0175 -0.0603 -0.0100 67  ASP   B OD1 
4960 O OD2 . ASP   B 67  ? 0.2601 0.1742 0.2318 -0.0001 -0.0735 -0.0020 67  ASP   B OD2 
4965 N N   . TYR   B 68  ? 0.1754 0.1496 0.1855 0.0002  -0.0355 -0.0251 68  TYR   B N   
4966 C CA  . TYR   B 68  ? 0.1736 0.1668 0.2000 0.0040  -0.0435 -0.0317 68  TYR   B CA  
4967 C C   . TYR   B 68  ? 0.1633 0.1638 0.1988 0.0023  -0.0362 -0.0340 68  TYR   B C   
4968 O O   . TYR   B 68  ? 0.1690 0.1761 0.2086 0.0053  -0.0287 -0.0519 68  TYR   B O   
4969 C CB  . TYR   B 68  ? 0.1784 0.1867 0.2052 0.0087  -0.0460 -0.0450 68  TYR   B CB  
4970 C CG  . TYR   B 68  ? 0.1922 0.2069 0.2143 0.0135  -0.0377 -0.0666 68  TYR   B CG  
4971 C CD1 . TYR   B 68  ? 0.1952 0.2121 0.2326 -0.0068 -0.0379 -0.0801 68  TYR   B CD1 
4972 C CD2 . TYR   B 68  ? 0.1919 0.2280 0.2329 0.0163  -0.0567 -0.0620 68  TYR   B CD2 
4973 C CE1 . TYR   B 68  ? 0.1983 0.2288 0.2593 -0.0034 -0.0355 -0.0746 68  TYR   B CE1 
4974 C CE2 . TYR   B 68  ? 0.1920 0.2318 0.2523 0.0168  -0.0365 -0.0743 68  TYR   B CE2 
4975 C CZ  . TYR   B 68  ? 0.1915 0.2380 0.2605 0.0048  -0.0370 -0.0769 68  TYR   B CZ  
4976 O OH  . TYR   B 68  ? 0.1869 0.2568 0.2854 0.0007  -0.0346 -0.0641 68  TYR   B OH  
4986 N N   . ILE   B 69  ? 0.1669 0.1551 0.1979 0.0032  -0.0301 -0.0387 69  ILE   B N   
4987 C CA  . ILE   B 69  ? 0.1743 0.1627 0.2089 -0.0045 -0.0248 -0.0334 69  ILE   B CA  
4988 C C   . ILE   B 69  ? 0.1743 0.1600 0.2015 0.0041  -0.0337 -0.0313 69  ILE   B C   
4989 O O   . ILE   B 69  ? 0.1796 0.1702 0.1921 0.0061  -0.0275 -0.0312 69  ILE   B O   
4990 C CB  . ILE   B 69  ? 0.1840 0.1672 0.2208 -0.0025 -0.0013 -0.0279 69  ILE   B CB  
4991 C CG1 . ILE   B 69  ? 0.1815 0.1686 0.2290 -0.0057 0.0057  -0.0295 69  ILE   B CG1 
4992 C CG2 . ILE   B 69  ? 0.1972 0.1758 0.2368 -0.0038 -0.0009 -0.0214 69  ILE   B CG2 
4993 C CD1 . ILE   B 69  ? 0.1732 0.1723 0.2360 -0.0157 0.0057  -0.0292 69  ILE   B CD1 
5005 N N   . ALA   B 70  ? 0.1717 0.1568 0.2069 0.0028  -0.0371 -0.0255 70  ALA   B N   
5006 C CA  . ALA   B 70  ? 0.1747 0.1638 0.1852 0.0004  -0.0415 -0.0250 70  ALA   B CA  
5007 C C   . ALA   B 70  ? 0.1803 0.1622 0.1892 -0.0029 -0.0431 -0.0367 70  ALA   B C   
5008 O O   . ALA   B 70  ? 0.1860 0.1661 0.1920 0.0015  -0.0442 -0.0359 70  ALA   B O   
5009 C CB  . ALA   B 70  ? 0.1792 0.1779 0.1910 -0.0017 -0.0434 -0.0210 70  ALA   B CB  
5015 N N   . THR   B 71  ? 0.1852 0.1659 0.1984 -0.0003 -0.0509 -0.0366 71  THR   B N   
5016 C CA  . THR   B 71  ? 0.1992 0.1662 0.2231 0.0071  -0.0599 -0.0344 71  THR   B CA  
5017 C C   . THR   B 71  ? 0.1942 0.1729 0.2401 0.0240  -0.0591 -0.0481 71  THR   B C   
5018 O O   . THR   B 71  ? 0.2053 0.1772 0.2777 0.0251  -0.0545 -0.0606 71  THR   B O   
5019 C CB  . THR   B 71  ? 0.2245 0.1870 0.2480 -0.0014 -0.0714 -0.0108 71  THR   B CB  
5020 O OG1 . THR   B 71  ? 0.2391 0.2104 0.2859 -0.0203 -0.0748 0.0155  71  THR   B OG1 
5021 C CG2 . THR   B 71  ? 0.2430 0.1864 0.2682 0.0037  -0.0615 -0.0015 71  THR   B CG2 
5029 N N   . ASN   B 72  ? 0.1824 0.1817 0.2322 0.0147  -0.0630 -0.0636 72  ASN   B N   
5030 C CA  . ASN   B 72  ? 0.1814 0.1890 0.2352 0.0171  -0.0480 -0.0689 72  ASN   B CA  
5031 C C   . ASN   B 72  ? 0.1832 0.2018 0.2431 0.0049  -0.0233 -0.0606 72  ASN   B C   
5032 O O   . ASN   B 72  ? 0.1853 0.2181 0.2662 0.0074  -0.0112 -0.0665 72  ASN   B O   
5033 C CB  . ASN   B 72  ? 0.1873 0.2015 0.2501 0.0151  -0.0600 -0.0589 72  ASN   B CB  
5034 C CG  . ASN   B 72  ? 0.2035 0.2167 0.2613 0.0254  -0.0589 -0.0391 72  ASN   B CG  
5035 O OD1 . ASN   B 72  ? 0.2223 0.2329 0.2615 0.0133  -0.0403 -0.0423 72  ASN   B OD1 
5036 N ND2 . ASN   B 72  ? 0.2137 0.2214 0.3004 0.0418  -0.0489 -0.0081 72  ASN   B ND2 
5043 N N   . GLY   B 73  ? 0.1853 0.1987 0.2229 -0.0007 -0.0269 -0.0576 73  GLY   B N   
5044 C CA  . GLY   B 73  ? 0.1811 0.2048 0.1986 -0.0039 -0.0252 -0.0447 73  GLY   B CA  
5045 C C   . GLY   B 73  ? 0.1767 0.2039 0.1664 0.0015  -0.0286 -0.0411 73  GLY   B C   
5046 O O   . GLY   B 73  ? 0.1719 0.1905 0.1779 0.0046  -0.0193 -0.0281 73  GLY   B O   
5050 N N   . PRO   B 74  ? 0.1790 0.2139 0.1628 0.0023  -0.0249 -0.0361 74  PRO   B N   
5051 C CA  . PRO   B 74  ? 0.1693 0.2121 0.1551 0.0078  -0.0183 -0.0186 74  PRO   B CA  
5052 C C   . PRO   B 74  ? 0.1588 0.1942 0.1610 0.0064  -0.0124 -0.0137 74  PRO   B C   
5053 O O   . PRO   B 74  ? 0.1636 0.1919 0.2003 0.0050  -0.0109 -0.0288 74  PRO   B O   
5054 C CB  . PRO   B 74  ? 0.1825 0.2309 0.1579 0.0025  -0.0169 -0.0191 74  PRO   B CB  
5055 C CG  . PRO   B 74  ? 0.2015 0.2416 0.1855 0.0029  -0.0203 -0.0167 74  PRO   B CG  
5056 C CD  . PRO   B 74  ? 0.2002 0.2311 0.1870 0.0027  -0.0147 -0.0236 74  PRO   B CD  
5064 N N   . LEU   B 75  ? 0.1553 0.1808 0.1462 0.0072  -0.0185 -0.0154 75  LEU   B N   
5065 C CA  . LEU   B 75  ? 0.1589 0.1856 0.1529 0.0096  -0.0117 -0.0049 75  LEU   B CA  
5066 C C   . LEU   B 75  ? 0.1659 0.1977 0.1575 0.0072  -0.0010 -0.0046 75  LEU   B C   
5067 O O   . LEU   B 75  ? 0.1814 0.2081 0.1692 0.0003  -0.0059 0.0026  75  LEU   B O   
5068 C CB  . LEU   B 75  ? 0.1706 0.1867 0.1362 -0.0029 -0.0159 0.0078  75  LEU   B CB  
5069 C CG  . LEU   B 75  ? 0.2057 0.2003 0.1597 -0.0261 -0.0076 0.0049  75  LEU   B CG  
5070 C CD1 . LEU   B 75  ? 0.2357 0.2143 0.1715 -0.0349 0.0178  0.0008  75  LEU   B CD1 
5071 C CD2 . LEU   B 75  ? 0.2402 0.2205 0.2272 -0.0187 0.0028  0.0130  75  LEU   B CD2 
5083 N N   . LYS   B 76  ? 0.1665 0.2180 0.1837 0.0006  -0.0004 0.0008  76  LYS   B N   
5084 C CA  . LYS   B 76  ? 0.1762 0.2258 0.2134 -0.0087 0.0182  0.0003  76  LYS   B CA  
5085 C C   . LYS   B 76  ? 0.1653 0.2075 0.1788 -0.0016 0.0019  0.0252  76  LYS   B C   
5086 O O   . LYS   B 76  ? 0.1671 0.1940 0.1817 -0.0011 -0.0003 0.0214  76  LYS   B O   
5087 C CB  . LYS   B 76  ? 0.1931 0.2340 0.2668 -0.0168 0.0416  -0.0309 76  LYS   B CB  
5088 C CG  . LYS   B 76  ? 0.2061 0.2557 0.3054 -0.0069 0.0306  -0.0396 76  LYS   B CG  
5089 C CD  . LYS   B 76  ? 0.2104 0.2695 0.3369 0.0029  0.0240  -0.0516 76  LYS   B CD  
5090 C CE  . LYS   B 76  ? 0.2159 0.2875 0.3795 0.0050  0.0081  -0.0575 76  LYS   B CE  
5091 N NZ  . LYS   B 76  ? 0.2181 0.2936 0.3964 0.0014  -0.0167 -0.0746 76  LYS   B NZ  
5105 N N   . VAL   B 77  ? 0.1733 0.2143 0.1788 0.0072  0.0055  0.0265  77  VAL   B N   
5106 C CA  . VAL   B 77  ? 0.1789 0.2072 0.1866 0.0119  0.0161  0.0453  77  VAL   B CA  
5107 C C   . VAL   B 77  ? 0.1656 0.1870 0.1808 0.0137  0.0212  0.0329  77  VAL   B C   
5108 O O   . VAL   B 77  ? 0.1697 0.1843 0.1813 0.0257  0.0299  0.0283  77  VAL   B O   
5109 C CB  . VAL   B 77  ? 0.1892 0.2162 0.2219 0.0110  0.0265  0.0616  77  VAL   B CB  
5110 C CG1 . VAL   B 77  ? 0.1898 0.2064 0.2549 0.0048  0.0281  0.0736  77  VAL   B CG1 
5111 C CG2 . VAL   B 77  ? 0.2044 0.2373 0.2432 0.0070  0.0100  0.0643  77  VAL   B CG2 
5121 N N   . GLY   B 78  ? 0.1606 0.1699 0.1787 0.0084  0.0162  0.0263  78  GLY   B N   
5122 C CA  . GLY   B 78  ? 0.1564 0.1680 0.1712 0.0089  0.0207  0.0157  78  GLY   B CA  
5123 C C   . GLY   B 78  ? 0.1504 0.1599 0.1711 0.0090  0.0141  0.0177  78  GLY   B C   
5124 O O   . GLY   B 78  ? 0.1538 0.1548 0.1846 0.0155  0.0169  0.0182  78  GLY   B O   
5128 N N   . GLY   B 79  ? 0.1501 0.1618 0.1767 0.0042  0.0099  0.0126  79  GLY   B N   
5129 C CA  . GLY   B 79  ? 0.1487 0.1516 0.1790 0.0111  0.0075  0.0107  79  GLY   B CA  
5130 C C   . GLY   B 79  ? 0.1383 0.1404 0.1787 0.0111  0.0040  0.0062  79  GLY   B C   
5131 O O   . GLY   B 79  ? 0.1455 0.1404 0.1838 0.0066  0.0102  0.0198  79  GLY   B O   
5135 N N   . SER   B 80  ? 0.1401 0.1352 0.1912 0.0049  0.0158  0.0037  80  SER   B N   
5136 C CA  . SER   B 80  ? 0.1331 0.1361 0.1729 0.0014  0.0050  0.0002  80  SER   B CA  
5137 C C   . SER   B 80  ? 0.1395 0.1360 0.1722 0.0091  -0.0028 0.0040  80  SER   B C   
5138 O O   . SER   B 80  ? 0.1535 0.1382 0.2047 0.0095  0.0031  -0.0028 80  SER   B O   
5139 C CB  . SER   B 80  ? 0.1403 0.1426 0.1813 -0.0071 -0.0032 0.0067  80  SER   B CB  
5140 O OG  . SER   B 80  ? 0.1461 0.1563 0.1976 -0.0016 -0.0086 0.0120  80  SER   B OG  
5146 N N   . CYS   B 81  ? 0.1362 0.1231 0.1763 0.0021  -0.0094 -0.0034 81  CYS   B N   
5147 C CA  . CYS   B 81  ? 0.1420 0.1199 0.1759 0.0026  -0.0141 -0.0024 81  CYS   B CA  
5148 C C   . CYS   B 81  ? 0.1375 0.1196 0.1582 -0.0013 -0.0153 -0.0029 81  CYS   B C   
5149 O O   . CYS   B 81  ? 0.1574 0.1243 0.1709 0.0033  -0.0028 -0.0080 81  CYS   B O   
5150 C CB  . CYS   B 81  ? 0.1607 0.1319 0.1844 -0.0048 -0.0153 -0.0040 81  CYS   B CB  
5151 S SG  . CYS   B 81  ? 0.1591 0.1546 0.1687 -0.0058 -0.0245 -0.0111 81  CYS   B SG  
5157 N N   . VAL   B 82  ? 0.1385 0.1224 0.1653 -0.0043 -0.0148 -0.0041 82  VAL   B N   
5158 C CA  . VAL   B 82  ? 0.1486 0.1256 0.1672 -0.0094 -0.0110 0.0040  82  VAL   B CA  
5159 C C   . VAL   B 82  ? 0.1582 0.1183 0.1767 -0.0070 -0.0060 0.0033  82  VAL   B C   
5160 O O   . VAL   B 82  ? 0.1648 0.1201 0.2022 -0.0086 -0.0116 -0.0135 82  VAL   B O   
5161 C CB  . VAL   B 82  ? 0.1592 0.1446 0.1843 -0.0036 -0.0107 0.0111  82  VAL   B CB  
5162 C CG1 . VAL   B 82  ? 0.1789 0.1631 0.1913 0.0017  -0.0069 0.0168  82  VAL   B CG1 
5163 C CG2 . VAL   B 82  ? 0.1644 0.1570 0.1963 -0.0070 -0.0261 0.0100  82  VAL   B CG2 
5173 N N   . LEU   B 83  ? 0.1415 0.1172 0.1808 -0.0165 -0.0192 -0.0086 83  LEU   B N   
5174 C CA  . LEU   B 83  ? 0.1455 0.1227 0.1648 -0.0113 -0.0199 -0.0035 83  LEU   B CA  
5175 C C   . LEU   B 83  ? 0.1491 0.1225 0.1612 -0.0175 -0.0177 -0.0012 83  LEU   B C   
5176 O O   . LEU   B 83  ? 0.1493 0.1351 0.1485 -0.0228 -0.0171 0.0048  83  LEU   B O   
5177 C CB  . LEU   B 83  ? 0.1536 0.1375 0.1663 -0.0158 -0.0239 -0.0094 83  LEU   B CB  
5178 C CG  . LEU   B 83  ? 0.1727 0.1604 0.1716 -0.0167 -0.0175 -0.0048 83  LEU   B CG  
5179 C CD1 . LEU   B 83  ? 0.1834 0.1653 0.1778 -0.0148 -0.0202 -0.0037 83  LEU   B CD1 
5180 C CD2 . LEU   B 83  ? 0.1927 0.1620 0.1795 -0.0110 -0.0193 -0.0167 83  LEU   B CD2 
5192 N N   . SER   B 84  ? 0.1545 0.1329 0.1857 -0.0264 -0.0175 -0.0008 84  SER   B N   
5193 C CA  . SER   B 84  ? 0.1488 0.1543 0.1765 -0.0284 -0.0117 0.0158  84  SER   B CA  
5194 C C   . SER   B 84  ? 0.1410 0.1687 0.1317 -0.0238 -0.0165 0.0216  84  SER   B C   
5195 O O   . SER   B 84  ? 0.1532 0.1568 0.1389 -0.0206 -0.0148 0.0045  84  SER   B O   
5196 C CB  . SER   B 84  ? 0.1671 0.1595 0.2300 -0.0297 0.0070  0.0143  84  SER   B CB  
5197 O OG  . SER   B 84  ? 0.1667 0.1762 0.2666 -0.0348 0.0111  0.0247  84  SER   B OG  
5203 N N   . GLY   B 85  ? 0.1464 0.1899 0.1484 -0.0264 -0.0201 0.0290  85  GLY   B N   
5204 C CA  . GLY   B 85  ? 0.1481 0.1971 0.1691 -0.0336 -0.0042 -0.0012 85  GLY   B CA  
5205 C C   . GLY   B 85  ? 0.1470 0.1760 0.1673 -0.0430 -0.0034 0.0076  85  GLY   B C   
5206 O O   . GLY   B 85  ? 0.1570 0.1720 0.1754 -0.0524 0.0134  -0.0066 85  GLY   B O   
5210 N N   . HIS   B 86  ? 0.1461 0.1620 0.1766 -0.0341 -0.0166 0.0168  86  HIS   B N   
5211 C CA  . HIS   B 86  ? 0.1478 0.1616 0.1702 -0.0338 -0.0116 0.0204  86  HIS   B CA  
5212 C C   . HIS   B 86  ? 0.1505 0.1764 0.1618 -0.0418 -0.0080 0.0329  86  HIS   B C   
5213 O O   . HIS   B 86  ? 0.1656 0.1899 0.1727 -0.0330 0.0017  0.0264  86  HIS   B O   
5214 C CB  . HIS   B 86  ? 0.1570 0.1651 0.1759 -0.0236 -0.0236 0.0096  86  HIS   B CB  
5215 C CG  . HIS   B 86  ? 0.1603 0.1674 0.1741 -0.0176 -0.0213 0.0133  86  HIS   B CG  
5216 N ND1 . HIS   B 86  ? 0.1728 0.1890 0.1973 -0.0246 -0.0245 -0.0053 86  HIS   B ND1 
5217 C CD2 . HIS   B 86  ? 0.1589 0.1712 0.1842 -0.0114 -0.0192 0.0109  86  HIS   B CD2 
5218 C CE1 . HIS   B 86  ? 0.1759 0.1886 0.1840 -0.0152 -0.0069 -0.0160 86  HIS   B CE1 
5219 N NE2 . HIS   B 86  ? 0.1706 0.1785 0.1735 -0.0047 -0.0113 -0.0017 86  HIS   B NE2 
5227 N N   . ASN   B 87  ? 0.1527 0.1775 0.1668 -0.0373 -0.0054 0.0294  87  ASN   B N   
5228 C CA  . ASN   B 87  ? 0.1590 0.1932 0.1781 -0.0347 0.0202  0.0247  87  ASN   B CA  
5229 C C   . ASN   B 87  ? 0.1728 0.1817 0.1709 -0.0339 0.0314  0.0189  87  ASN   B C   
5230 O O   . ASN   B 87  ? 0.1982 0.1978 0.1999 -0.0294 0.0450  0.0119  87  ASN   B O   
5231 C CB  . ASN   B 87  ? 0.1614 0.2289 0.2132 -0.0323 0.0204  0.0130  87  ASN   B CB  
5232 C CG  . ASN   B 87  ? 0.1670 0.2461 0.2199 0.0037  0.0220  0.0300  87  ASN   B CG  
5233 O OD1 . ASN   B 87  ? 0.1585 0.2367 0.2124 0.0065  0.0405  0.0477  87  ASN   B OD1 
5234 N ND2 . ASN   B 87  ? 0.2012 0.2570 0.2538 0.0047  0.0272  0.0282  87  ASN   B ND2 
5241 N N   . LEU   B 88  ? 0.1613 0.1666 0.1589 -0.0367 0.0171  0.0135  88  LEU   B N   
5242 C CA  . LEU   B 88  ? 0.1725 0.1604 0.1682 -0.0356 0.0121  0.0003  88  LEU   B CA  
5243 C C   . LEU   B 88  ? 0.1727 0.1498 0.1665 -0.0397 0.0024  -0.0010 88  LEU   B C   
5244 O O   . LEU   B 88  ? 0.1977 0.1633 0.1944 -0.0269 -0.0270 -0.0095 88  LEU   B O   
5245 C CB  . LEU   B 88  ? 0.1811 0.1627 0.1929 -0.0425 -0.0011 0.0124  88  LEU   B CB  
5246 C CG  . LEU   B 88  ? 0.2178 0.1903 0.2150 -0.0338 -0.0184 0.0333  88  LEU   B CG  
5247 C CD1 . LEU   B 88  ? 0.2298 0.2229 0.2269 -0.0431 -0.0116 0.0438  88  LEU   B CD1 
5248 C CD2 . LEU   B 88  ? 0.2529 0.2175 0.2635 0.0058  -0.0418 0.0173  88  LEU   B CD2 
5260 N N   . ALA   B 89  ? 0.1591 0.1491 0.1535 -0.0416 0.0177  0.0046  89  ALA   B N   
5261 C CA  . ALA   B 89  ? 0.1561 0.1454 0.1427 -0.0391 0.0028  0.0106  89  ALA   B CA  
5262 C C   . ALA   B 89  ? 0.1672 0.1510 0.1474 -0.0428 0.0107  0.0064  89  ALA   B C   
5263 O O   . ALA   B 89  ? 0.1505 0.1578 0.1782 -0.0417 0.0126  -0.0215 89  ALA   B O   
5264 C CB  . ALA   B 89  ? 0.1496 0.1484 0.1646 -0.0345 0.0116  0.0214  89  ALA   B CB  
5270 N N   . LYS   B 90  ? 0.2016 0.1413 0.1552 -0.0461 -0.0112 0.0099  90  LYS   B N   
5271 C CA  . LYS   B 90  ? 0.2130 0.1394 0.1508 -0.0460 -0.0078 0.0057  90  LYS   B CA  
5272 C C   . LYS   B 90  ? 0.1970 0.1298 0.1699 -0.0462 -0.0099 0.0001  90  LYS   B C   
5273 O O   . LYS   B 90  ? 0.2069 0.1473 0.1871 -0.0598 0.0016  -0.0002 90  LYS   B O   
5274 C CB  . LYS   B 90  ? 0.2318 0.1471 0.1741 -0.0363 -0.0024 0.0151  90  LYS   B CB  
5275 C CG  . LYS   B 90  ? 0.2363 0.1550 0.1732 -0.0215 0.0233  0.0138  90  LYS   B CG  
5276 C CD  . LYS   B 90  ? 0.2688 0.1783 0.2216 -0.0158 0.0454  -0.0043 90  LYS   B CD  
5277 C CE  . LYS   B 90  ? 0.2851 0.1923 0.2665 -0.0233 0.0588  -0.0123 90  LYS   B CE  
5278 N NZ  . LYS   B 90  ? 0.2932 0.1829 0.2698 -0.0325 0.0780  -0.0149 90  LYS   B NZ  
5292 N N   . HIS   B 91  ? 0.1708 0.1211 0.1507 -0.0341 -0.0183 0.0100  91  HIS   B N   
5293 C CA  . HIS   B 91  ? 0.1599 0.1261 0.1544 -0.0285 -0.0182 0.0024  91  HIS   B CA  
5294 C C   . HIS   B 91  ? 0.1502 0.1252 0.1429 -0.0292 -0.0007 0.0092  91  HIS   B C   
5295 O O   . HIS   B 91  ? 0.1630 0.1248 0.1508 -0.0276 -0.0227 0.0052  91  HIS   B O   
5296 C CB  . HIS   B 91  ? 0.1817 0.1291 0.1921 -0.0115 -0.0134 0.0141  91  HIS   B CB  
5297 C CG  . HIS   B 91  ? 0.2212 0.1450 0.2630 0.0026  0.0180  0.0232  91  HIS   B CG  
5298 N ND1 . HIS   B 91  ? 0.2481 0.1509 0.3173 -0.0006 0.0269  0.0116  91  HIS   B ND1 
5299 C CD2 . HIS   B 91  ? 0.2316 0.1787 0.3094 0.0171  0.0121  0.0489  91  HIS   B CD2 
5300 C CE1 . HIS   B 91  ? 0.2506 0.1661 0.3352 0.0161  0.0273  0.0176  91  HIS   B CE1 
5301 N NE2 . HIS   B 91  ? 0.2417 0.1819 0.3348 0.0313  0.0236  0.0537  91  HIS   B NE2 
5309 N N   . CYS   B 92  ? 0.1426 0.1260 0.1482 -0.0273 -0.0076 0.0067  92  CYS   B N   
5310 C CA  . CYS   B 92  ? 0.1371 0.1215 0.1427 -0.0239 -0.0073 0.0011  92  CYS   B CA  
5311 C C   . CYS   B 92  ? 0.1313 0.1190 0.1343 -0.0139 -0.0057 0.0036  92  CYS   B C   
5312 O O   . CYS   B 92  ? 0.1391 0.1260 0.1631 -0.0165 -0.0022 -0.0043 92  CYS   B O   
5313 C CB  . CYS   B 92  ? 0.1397 0.1310 0.1510 -0.0154 -0.0046 0.0036  92  CYS   B CB  
5314 S SG  . CYS   B 92  ? 0.1394 0.1317 0.1561 -0.0120 -0.0127 0.0062  92  CYS   B SG  
5320 N N   . LEU   B 93  ? 0.1247 0.1181 0.1446 -0.0132 -0.0109 -0.0048 93  LEU   B N   
5321 C CA  . LEU   B 93  ? 0.1257 0.1182 0.1506 -0.0058 -0.0095 0.0031  93  LEU   B CA  
5322 C C   . LEU   B 93  ? 0.1224 0.1159 0.1438 -0.0073 -0.0061 0.0089  93  LEU   B C   
5323 O O   . LEU   B 93  ? 0.1328 0.1177 0.1584 -0.0078 -0.0087 0.0049  93  LEU   B O   
5324 C CB  . LEU   B 93  ? 0.1270 0.1168 0.1680 -0.0010 -0.0074 0.0043  93  LEU   B CB  
5325 C CG  . LEU   B 93  ? 0.1241 0.1287 0.1807 -0.0029 -0.0064 0.0084  93  LEU   B CG  
5326 C CD1 . LEU   B 93  ? 0.1303 0.1412 0.1816 0.0006  -0.0035 -0.0032 93  LEU   B CD1 
5327 C CD2 . LEU   B 93  ? 0.1290 0.1366 0.1797 -0.0067 -0.0120 0.0082  93  LEU   B CD2 
5339 N N   . HIS   B 94  ? 0.1293 0.1140 0.1404 -0.0067 -0.0151 0.0069  94  HIS   B N   
5340 C CA  . HIS   B 94  ? 0.1296 0.1158 0.1407 0.0013  -0.0058 0.0061  94  HIS   B CA  
5341 C C   . HIS   B 94  ? 0.1246 0.1183 0.1574 -0.0018 -0.0038 0.0114  94  HIS   B C   
5342 O O   . HIS   B 94  ? 0.1297 0.1295 0.1953 -0.0094 0.0102  -0.0071 94  HIS   B O   
5343 C CB  . HIS   B 94  ? 0.1293 0.1214 0.1518 -0.0001 -0.0046 0.0025  94  HIS   B CB  
5344 C CG  . HIS   B 94  ? 0.1349 0.1202 0.1564 -0.0093 -0.0221 0.0029  94  HIS   B CG  
5345 N ND1 . HIS   B 94  ? 0.1356 0.1278 0.1596 -0.0111 -0.0227 0.0016  94  HIS   B ND1 
5346 C CD2 . HIS   B 94  ? 0.1397 0.1220 0.1578 -0.0024 -0.0179 0.0025  94  HIS   B CD2 
5347 C CE1 . HIS   B 94  ? 0.1427 0.1256 0.1494 -0.0136 -0.0228 0.0065  94  HIS   B CE1 
5348 N NE2 . HIS   B 94  ? 0.1350 0.1255 0.1579 -0.0149 -0.0155 0.0048  94  HIS   B NE2 
5356 N N   . VAL   B 95  ? 0.1196 0.1164 0.1599 -0.0034 -0.0035 0.0052  95  VAL   B N   
5357 C CA  . VAL   B 95  ? 0.1231 0.1231 0.1604 -0.0011 0.0019  0.0143  95  VAL   B CA  
5358 C C   . VAL   B 95  ? 0.1302 0.1249 0.1686 -0.0049 0.0068  0.0080  95  VAL   B C   
5359 O O   . VAL   B 95  ? 0.1361 0.1230 0.1822 0.0055  0.0077  0.0158  95  VAL   B O   
5360 C CB  . VAL   B 95  ? 0.1300 0.1238 0.1586 -0.0021 -0.0095 0.0063  95  VAL   B CB  
5361 C CG1 . VAL   B 95  ? 0.1392 0.1424 0.1856 -0.0099 -0.0015 0.0155  95  VAL   B CG1 
5362 C CG2 . VAL   B 95  ? 0.1385 0.1271 0.1508 0.0011  -0.0048 0.0019  95  VAL   B CG2 
5372 N N   . VAL   B 96  ? 0.1417 0.1285 0.1641 0.0043  0.0087  0.0185  96  VAL   B N   
5373 C CA  . VAL   B 96  ? 0.1477 0.1386 0.1642 0.0028  0.0021  0.0161  96  VAL   B CA  
5374 C C   . VAL   B 96  ? 0.1510 0.1443 0.1750 0.0049  0.0079  0.0181  96  VAL   B C   
5375 O O   . VAL   B 96  ? 0.1496 0.1487 0.1928 0.0034  0.0187  0.0078  96  VAL   B O   
5376 C CB  . VAL   B 96  ? 0.1557 0.1547 0.1590 0.0052  0.0012  0.0116  96  VAL   B CB  
5377 C CG1 . VAL   B 96  ? 0.1556 0.1750 0.1753 0.0136  0.0054  0.0033  96  VAL   B CG1 
5378 C CG2 . VAL   B 96  ? 0.1634 0.1592 0.1681 0.0053  0.0121  0.0070  96  VAL   B CG2 
5388 N N   . GLY   B 97  ? 0.1573 0.1415 0.1645 0.0032  0.0062  0.0219  97  GLY   B N   
5389 C CA  . GLY   B 97  ? 0.1731 0.1452 0.1681 0.0019  0.0086  0.0181  97  GLY   B CA  
5390 C C   . GLY   B 97  ? 0.1865 0.1571 0.1800 0.0054  -0.0001 0.0198  97  GLY   B C   
5391 O O   . GLY   B 97  ? 0.2009 0.1671 0.1733 0.0021  0.0018  0.0127  97  GLY   B O   
5395 N N   . PRO   B 98  ? 0.2004 0.1597 0.1934 0.0057  0.0270  0.0325  98  PRO   B N   
5396 C CA  . PRO   B 98  ? 0.2103 0.1762 0.1958 0.0123  0.0391  0.0249  98  PRO   B CA  
5397 C C   . PRO   B 98  ? 0.2222 0.1765 0.1677 0.0281  0.0381  0.0477  98  PRO   B C   
5398 O O   . PRO   B 98  ? 0.2162 0.1778 0.1884 0.0226  0.0369  0.0459  98  PRO   B O   
5399 C CB  . PRO   B 98  ? 0.2009 0.1814 0.2024 0.0080  0.0467  0.0264  98  PRO   B CB  
5400 C CG  . PRO   B 98  ? 0.1964 0.1769 0.2025 0.0072  0.0379  0.0354  98  PRO   B CG  
5401 C CD  . PRO   B 98  ? 0.1863 0.1639 0.1986 0.0052  0.0284  0.0386  98  PRO   B CD  
5409 N N   . ASN   B 99  ? 0.2339 0.1921 0.1835 0.0425  0.0411  0.0277  99  ASN   B N   
5410 C CA  . ASN   B 99  ? 0.2521 0.2022 0.1792 0.0457  0.0359  0.0449  99  ASN   B CA  
5411 C C   . ASN   B 99  ? 0.2797 0.2372 0.2135 0.0401  0.0482  0.0728  99  ASN   B C   
5412 O O   . ASN   B 99  ? 0.2865 0.2419 0.2226 0.0402  0.0347  0.0801  99  ASN   B O   
5413 C CB  . ASN   B 99  ? 0.2598 0.2008 0.1895 0.0452  0.0251  0.0382  99  ASN   B CB  
5414 C CG  . ASN   B 99  ? 0.2618 0.2094 0.2111 0.0392  0.0147  0.0316  99  ASN   B CG  
5415 O OD1 . ASN   B 99  ? 0.2627 0.2120 0.2340 0.0429  0.0147  0.0355  99  ASN   B OD1 
5416 N ND2 . ASN   B 99  ? 0.2595 0.2070 0.2258 0.0430  -0.0100 0.0284  99  ASN   B ND2 
5423 N N   A VAL   B 100 ? 0.2984 0.2510 0.2537 0.0287  0.0548  0.0913  100 VAL   B N   
5424 N N   B VAL   B 100 ? 0.3022 0.2534 0.2477 0.0324  0.0440  0.0839  100 VAL   B N   
5425 C CA  A VAL   B 100 ? 0.3264 0.2733 0.3058 0.0168  0.0557  0.1051  100 VAL   B CA  
5426 C CA  B VAL   B 100 ? 0.3282 0.2725 0.2857 0.0246  0.0379  0.0924  100 VAL   B CA  
5427 C C   A VAL   B 100 ? 0.3477 0.2796 0.2935 0.0240  0.0504  0.1202  100 VAL   B C   
5428 C C   B VAL   B 100 ? 0.3475 0.2799 0.2861 0.0284  0.0360  0.1115  100 VAL   B C   
5429 O O   A VAL   B 100 ? 0.3538 0.2892 0.2940 0.0213  0.0594  0.1140  100 VAL   B O   
5430 O O   B VAL   B 100 ? 0.3509 0.2852 0.2842 0.0265  0.0377  0.1082  100 VAL   B O   
5431 C CB  A VAL   B 100 ? 0.3354 0.2880 0.3696 -0.0023 0.0567  0.1150  100 VAL   B CB  
5432 C CB  B VAL   B 100 ? 0.3350 0.2827 0.3222 0.0135  0.0333  0.0871  100 VAL   B CB  
5433 C CG1 A VAL   B 100 ? 0.3409 0.2945 0.3962 -0.0052 0.0566  0.1128  100 VAL   B CG1 
5434 C CG1 B VAL   B 100 ? 0.3381 0.2866 0.3367 0.0111  0.0320  0.0838  100 VAL   B CG1 
5435 C CG2 A VAL   B 100 ? 0.3366 0.2928 0.3886 -0.0104 0.0603  0.1255  100 VAL   B CG2 
5436 C CG2 B VAL   B 100 ? 0.3368 0.2864 0.3345 0.0094  0.0326  0.0873  100 VAL   B CG2 
5455 N N   . ASN   B 101 ? 0.3619 0.2832 0.2905 0.0354  0.0335  0.1283  101 ASN   B N   
5456 C CA  . ASN   B 101 ? 0.3969 0.2977 0.3050 0.0470  0.0147  0.1411  101 ASN   B CA  
5457 C C   . ASN   B 101 ? 0.4364 0.3357 0.3136 0.0492  0.0010  0.1518  101 ASN   B C   
5458 O O   . ASN   B 101 ? 0.4416 0.3505 0.3381 0.0565  -0.0009 0.1273  101 ASN   B O   
5459 C CB  . ASN   B 101 ? 0.3956 0.2826 0.3195 0.0471  0.0191  0.1227  101 ASN   B CB  
5460 C CG  . ASN   B 101 ? 0.3936 0.2680 0.3235 0.0480  0.0244  0.1176  101 ASN   B CG  
5461 O OD1 . ASN   B 101 ? 0.3976 0.2681 0.3545 0.0417  0.0374  0.1073  101 ASN   B OD1 
5462 N ND2 . ASN   B 101 ? 0.3892 0.2624 0.3159 0.0512  0.0254  0.1048  101 ASN   B ND2 
5470 N N   . LYS   B 102 ? 0.4687 0.3680 0.3350 0.0364  0.0078  0.1498  102 LYS   B N   
5471 C CA  . LYS   B 102 ? 0.4989 0.4084 0.3635 0.0207  0.0198  0.1234  102 LYS   B CA  
5472 C C   . LYS   B 102 ? 0.4970 0.4115 0.3490 0.0213  0.0255  0.1276  102 LYS   B C   
5473 O O   . LYS   B 102 ? 0.5066 0.4178 0.3637 0.0221  0.0108  0.1222  102 LYS   B O   
5474 C CB  . LYS   B 102 ? 0.5271 0.4427 0.4209 0.0063  0.0334  0.0800  102 LYS   B CB  
5475 C CG  . LYS   B 102 ? 0.5506 0.4724 0.4829 -0.0046 0.0466  0.0358  102 LYS   B CG  
5476 C CD  . LYS   B 102 ? 0.5701 0.4963 0.5443 -0.0129 0.0595  0.0011  102 LYS   B CD  
5477 C CE  . LYS   B 102 ? 0.5834 0.5129 0.5917 -0.0193 0.0690  -0.0226 102 LYS   B CE  
5478 N NZ  . LYS   B 102 ? 0.5906 0.5229 0.6199 -0.0222 0.0730  -0.0351 102 LYS   B NZ  
5492 N N   . GLY   B 103 ? 0.4813 0.4045 0.3393 0.0199  0.0458  0.1285  103 GLY   B N   
5493 C CA  . GLY   B 103 ? 0.4633 0.3969 0.3464 0.0215  0.0627  0.1092  103 GLY   B CA  
5494 C C   . GLY   B 103 ? 0.4411 0.3848 0.3421 0.0209  0.0768  0.0866  103 GLY   B C   
5495 O O   . GLY   B 103 ? 0.4460 0.3914 0.3462 0.0188  0.0781  0.0894  103 GLY   B O   
5499 N N   A GLU   B 104 ? 0.4226 0.3706 0.3277 0.0251  0.0917  0.0709  104 GLU   B N   
5500 N N   B GLU   B 104 ? 0.4292 0.3771 0.3410 0.0162  0.0706  0.0693  104 GLU   B N   
5501 C CA  A GLU   B 104 ? 0.4028 0.3559 0.3109 0.0327  0.0992  0.0548  104 GLU   B CA  
5502 C CA  B GLU   B 104 ? 0.4160 0.3680 0.3344 0.0125  0.0639  0.0500  104 GLU   B CA  
5503 C C   A GLU   B 104 ? 0.4048 0.3604 0.3196 0.0164  0.1326  0.0576  104 GLU   B C   
5504 C C   B GLU   B 104 ? 0.4137 0.3662 0.3415 0.0042  0.0788  0.0442  104 GLU   B C   
5505 O O   A GLU   B 104 ? 0.4064 0.3641 0.3401 0.0117  0.1327  0.0547  104 GLU   B O   
5506 O O   B GLU   B 104 ? 0.4148 0.3683 0.3491 0.0029  0.0770  0.0412  104 GLU   B O   
5507 C CB  A GLU   B 104 ? 0.3854 0.3352 0.2977 0.0566  0.0629  0.0273  104 GLU   B CB  
5508 C CB  B GLU   B 104 ? 0.4061 0.3593 0.3222 0.0165  0.0421  0.0333  104 GLU   B CB  
5509 C CG  A GLU   B 104 ? 0.3698 0.3190 0.2786 0.0768  0.0250  -0.0046 104 GLU   B CG  
5510 C CG  B GLU   B 104 ? 0.3976 0.3521 0.3095 0.0196  0.0214  0.0152  104 GLU   B CG  
5511 C CD  A GLU   B 104 ? 0.3556 0.3031 0.2560 0.0941  -0.0081 -0.0227 104 GLU   B CD  
5512 C CD  B GLU   B 104 ? 0.3910 0.3455 0.2980 0.0215  0.0044  0.0021  104 GLU   B CD  
5513 O OE1 A GLU   B 104 ? 0.3385 0.2881 0.2214 0.1073  -0.0073 -0.0243 104 GLU   B OE1 
5514 O OE1 B GLU   B 104 ? 0.3865 0.3411 0.2871 0.0211  0.0030  -0.0001 104 GLU   B OE1 
5515 O OE2 A GLU   B 104 ? 0.3577 0.3074 0.2576 0.0928  -0.0317 -0.0355 104 GLU   B OE2 
5516 O OE2 B GLU   B 104 ? 0.3903 0.3457 0.2972 0.0227  -0.0067 -0.0054 104 GLU   B OE2 
5529 N N   A ASP   B 105 ? 0.4013 0.3610 0.3103 0.0042  0.1595  0.0632  105 ASP   B N   
5530 N N   B ASP   B 105 ? 0.4087 0.3614 0.3381 -0.0033 0.0955  0.0421  105 ASP   B N   
5531 C CA  A ASP   B 105 ? 0.4019 0.3636 0.3251 -0.0061 0.1767  0.0492  105 ASP   B CA  
5532 C CA  B ASP   B 105 ? 0.4043 0.3558 0.3411 -0.0106 0.1106  0.0351  105 ASP   B CA  
5533 C C   A ASP   B 105 ? 0.3895 0.3385 0.2972 -0.0165 0.1702  0.0474  105 ASP   B C   
5534 C C   B ASP   B 105 ? 0.3949 0.3389 0.3203 -0.0167 0.1294  0.0357  105 ASP   B C   
5535 O O   A ASP   B 105 ? 0.3819 0.3310 0.2814 -0.0179 0.1771  0.0548  105 ASP   B O   
5536 O O   B ASP   B 105 ? 0.3949 0.3391 0.3141 -0.0167 0.1310  0.0358  105 ASP   B O   
5537 C CB  A ASP   B 105 ? 0.4155 0.3886 0.3918 -0.0003 0.1848  0.0253  105 ASP   B CB  
5538 C CB  B ASP   B 105 ? 0.4078 0.3648 0.3682 -0.0098 0.1056  0.0258  105 ASP   B CB  
5539 C CG  A ASP   B 105 ? 0.4245 0.4076 0.4553 0.0022  0.1963  0.0076  105 ASP   B CG  
5540 C CG  B ASP   B 105 ? 0.4097 0.3705 0.3940 -0.0106 0.1034  0.0200  105 ASP   B CG  
5541 O OD1 A ASP   B 105 ? 0.4233 0.4125 0.4645 -0.0056 0.2090  0.0122  105 ASP   B OD1 
5542 O OD1 B ASP   B 105 ? 0.4095 0.3727 0.4006 -0.0135 0.1033  0.0197  105 ASP   B OD1 
5543 O OD2 A ASP   B 105 ? 0.4305 0.4171 0.4914 0.0084  0.1893  -0.0064 105 ASP   B OD2 
5544 O OD2 B ASP   B 105 ? 0.4093 0.3722 0.4007 -0.0107 0.1045  0.0187  105 ASP   B OD2 
5553 N N   . ILE   B 106 ? 0.3835 0.3192 0.3113 -0.0207 0.1428  0.0376  106 ILE   B N   
5554 C CA  . ILE   B 106 ? 0.3577 0.2792 0.3198 -0.0337 0.1432  0.0276  106 ILE   B CA  
5555 C C   . ILE   B 106 ? 0.3172 0.2730 0.3148 -0.0277 0.1330  0.0073  106 ILE   B C   
5556 O O   . ILE   B 106 ? 0.3024 0.2425 0.3110 -0.0374 0.1283  0.0020  106 ILE   B O   
5557 C CB  . ILE   B 106 ? 0.3791 0.2628 0.3426 -0.0460 0.1408  0.0331  106 ILE   B CB  
5558 C CG1 . ILE   B 106 ? 0.3900 0.2621 0.3491 -0.0333 0.1353  0.0262  106 ILE   B CG1 
5559 C CG2 . ILE   B 106 ? 0.3868 0.2644 0.3714 -0.0559 0.1412  0.0373  106 ILE   B CG2 
5560 C CD1 . ILE   B 106 ? 0.3957 0.2662 0.3448 -0.0222 0.1354  0.0252  106 ILE   B CD1 
5573 N N   A GLN   B 107 ? 0.3052 0.2878 0.3272 -0.0276 0.1322  0.0067  107 GLN   B N   
5574 N N   B GLN   B 107 ? 0.3107 0.2878 0.3234 -0.0221 0.1183  0.0048  107 GLN   B N   
5575 C CA  A GLN   B 107 ? 0.2940 0.3058 0.3466 -0.0258 0.1223  0.0099  107 GLN   B CA  
5576 C CA  B GLN   B 107 ? 0.3030 0.3012 0.3348 -0.0153 0.1000  0.0051  107 GLN   B CA  
5577 C C   A GLN   B 107 ? 0.2670 0.2841 0.3200 -0.0162 0.0994  0.0029  107 GLN   B C   
5578 C C   B GLN   B 107 ? 0.2753 0.2851 0.3069 -0.0069 0.0935  0.0026  107 GLN   B C   
5579 O O   A GLN   B 107 ? 0.2620 0.2856 0.3445 -0.0132 0.0744  -0.0111 107 GLN   B O   
5580 O O   B GLN   B 107 ? 0.2759 0.2890 0.3131 -0.0057 0.0839  -0.0036 107 GLN   B O   
5581 C CB  A GLN   B 107 ? 0.3253 0.3472 0.4132 -0.0244 0.1061  0.0144  107 GLN   B CB  
5582 C CB  B GLN   B 107 ? 0.3261 0.3291 0.3826 -0.0137 0.0806  0.0064  107 GLN   B CB  
5583 C CG  A GLN   B 107 ? 0.3576 0.3844 0.4817 -0.0191 0.0763  0.0172  107 GLN   B CG  
5584 C CG  B GLN   B 107 ? 0.3474 0.3530 0.4295 -0.0110 0.0581  0.0076  107 GLN   B CG  
5585 C CD  A GLN   B 107 ? 0.3814 0.4123 0.5366 -0.0179 0.0552  0.0216  107 GLN   B CD  
5586 C CD  B GLN   B 107 ? 0.3635 0.3707 0.4674 -0.0103 0.0410  0.0093  107 GLN   B CD  
5587 O OE1 A GLN   B 107 ? 0.3899 0.4229 0.5566 -0.0169 0.0517  0.0204  107 GLN   B OE1 
5588 O OE1 B GLN   B 107 ? 0.3691 0.3769 0.4803 -0.0103 0.0372  0.0093  107 GLN   B OE1 
5589 N NE2 A GLN   B 107 ? 0.3909 0.4212 0.5546 -0.0148 0.0467  0.0263  107 GLN   B NE2 
5590 N NE2 B GLN   B 107 ? 0.3698 0.3765 0.4805 -0.0086 0.0351  0.0109  107 GLN   B NE2 
5607 N N   . LEU   B 108 ? 0.2456 0.2634 0.2839 0.0054  0.0935  0.0037  108 LEU   B N   
5608 C CA  . LEU   B 108 ? 0.2219 0.2318 0.2499 0.0215  0.0696  0.0180  108 LEU   B CA  
5609 C C   . LEU   B 108 ? 0.1867 0.1889 0.2398 0.0225  0.0446  0.0304  108 LEU   B C   
5610 O O   . LEU   B 108 ? 0.1868 0.1767 0.2321 0.0191  0.0354  0.0227  108 LEU   B O   
5611 C CB  . LEU   B 108 ? 0.2391 0.2485 0.2364 0.0168  0.0675  0.0244  108 LEU   B CB  
5612 C CG  . LEU   B 108 ? 0.2572 0.2748 0.2457 0.0194  0.0566  0.0043  108 LEU   B CG  
5613 C CD1 . LEU   B 108 ? 0.2664 0.2869 0.2282 0.0095  0.0616  0.0074  108 LEU   B CD1 
5614 C CD2 . LEU   B 108 ? 0.2716 0.2866 0.2550 0.0316  0.0458  -0.0135 108 LEU   B CD2 
5627 N N   . LEU   B 109 ? 0.1700 0.1678 0.2466 0.0142  0.0419  0.0272  109 LEU   B N   
5628 C CA  . LEU   B 109 ? 0.1539 0.1440 0.2563 0.0087  0.0366  0.0310  109 LEU   B CA  
5629 C C   . LEU   B 109 ? 0.1457 0.1322 0.2525 0.0034  0.0355  0.0231  109 LEU   B C   
5630 O O   . LEU   B 109 ? 0.1407 0.1329 0.2396 0.0024  0.0339  0.0314  109 LEU   B O   
5631 C CB  . LEU   B 109 ? 0.1620 0.1365 0.2588 0.0071  0.0291  0.0396  109 LEU   B CB  
5632 C CG  . LEU   B 109 ? 0.1615 0.1369 0.2510 -0.0010 0.0220  0.0251  109 LEU   B CG  
5633 C CD1 . LEU   B 109 ? 0.1590 0.1495 0.2331 0.0111  0.0217  0.0294  109 LEU   B CD1 
5634 C CD2 . LEU   B 109 ? 0.1745 0.1418 0.2668 0.0047  0.0124  0.0241  109 LEU   B CD2 
5646 N N   . LYS   B 110 ? 0.1422 0.1351 0.2453 -0.0034 0.0326  0.0211  110 LYS   B N   
5647 C CA  . LYS   B 110 ? 0.1403 0.1335 0.2397 -0.0031 0.0235  0.0155  110 LYS   B CA  
5648 C C   . LYS   B 110 ? 0.1363 0.1319 0.2307 -0.0025 0.0270  0.0099  110 LYS   B C   
5649 O O   . LYS   B 110 ? 0.1298 0.1341 0.2226 -0.0061 0.0177  0.0052  110 LYS   B O   
5650 C CB  . LYS   B 110 ? 0.1418 0.1353 0.2587 -0.0071 0.0273  0.0167  110 LYS   B CB  
5651 C CG  . LYS   B 110 ? 0.1401 0.1310 0.2703 -0.0075 0.0104  0.0153  110 LYS   B CG  
5652 C CD  . LYS   B 110 ? 0.1459 0.1360 0.2798 -0.0102 0.0131  0.0153  110 LYS   B CD  
5653 C CE  . LYS   B 110 ? 0.1442 0.1481 0.2910 -0.0028 0.0106  0.0117  110 LYS   B CE  
5654 N NZ  . LYS   B 110 ? 0.1502 0.1702 0.2824 0.0009  0.0032  -0.0002 110 LYS   B NZ  
5668 N N   . SER   B 111 ? 0.1420 0.1323 0.2355 -0.0061 0.0298  0.0143  111 SER   B N   
5669 C CA  . SER   B 111 ? 0.1492 0.1362 0.2215 -0.0003 0.0188  0.0157  111 SER   B CA  
5670 C C   . SER   B 111 ? 0.1457 0.1314 0.2126 -0.0010 0.0117  0.0111  111 SER   B C   
5671 O O   . SER   B 111 ? 0.1383 0.1367 0.2185 -0.0018 0.0066  0.0120  111 SER   B O   
5672 C CB  . SER   B 111 ? 0.1574 0.1576 0.2271 0.0012  0.0336  0.0303  111 SER   B CB  
5673 O OG  . SER   B 111 ? 0.1770 0.1950 0.2417 0.0052  0.0385  0.0296  111 SER   B OG  
5679 N N   . ALA   B 112 ? 0.1325 0.1344 0.2224 0.0060  0.0182  0.0186  112 ALA   B N   
5680 C CA  . ALA   B 112 ? 0.1360 0.1385 0.2085 -0.0032 0.0069  0.0071  112 ALA   B CA  
5681 C C   . ALA   B 112 ? 0.1289 0.1323 0.2018 -0.0029 0.0069  0.0040  112 ALA   B C   
5682 O O   . ALA   B 112 ? 0.1291 0.1325 0.2099 -0.0064 0.0086  0.0041  112 ALA   B O   
5683 C CB  . ALA   B 112 ? 0.1382 0.1383 0.2271 0.0026  0.0100  0.0153  112 ALA   B CB  
5689 N N   . TYR   B 113 ? 0.1250 0.1209 0.2103 -0.0035 0.0137  0.0061  113 TYR   B N   
5690 C CA  . TYR   B 113 ? 0.1244 0.1170 0.2065 -0.0042 0.0118  0.0056  113 TYR   B CA  
5691 C C   . TYR   B 113 ? 0.1186 0.1127 0.2086 -0.0105 0.0066  0.0059  113 TYR   B C   
5692 O O   . TYR   B 113 ? 0.1246 0.1191 0.1964 -0.0074 0.0021  0.0045  113 TYR   B O   
5693 C CB  . TYR   B 113 ? 0.1318 0.1114 0.2125 -0.0043 0.0166  0.0132  113 TYR   B CB  
5694 C CG  . TYR   B 113 ? 0.1291 0.1140 0.2200 -0.0061 0.0105  0.0130  113 TYR   B CG  
5695 C CD1 . TYR   B 113 ? 0.1344 0.1183 0.2348 -0.0041 0.0106  0.0166  113 TYR   B CD1 
5696 C CD2 . TYR   B 113 ? 0.1338 0.1199 0.2264 -0.0067 0.0095  0.0143  113 TYR   B CD2 
5697 C CE1 . TYR   B 113 ? 0.1330 0.1193 0.2333 -0.0029 0.0167  0.0083  113 TYR   B CE1 
5698 C CE2 . TYR   B 113 ? 0.1417 0.1168 0.2437 -0.0023 0.0099  0.0132  113 TYR   B CE2 
5699 C CZ  . TYR   B 113 ? 0.1313 0.1187 0.2464 0.0031  0.0077  0.0082  113 TYR   B CZ  
5700 O OH  . TYR   B 113 ? 0.1365 0.1160 0.2723 0.0067  0.0209  0.0080  113 TYR   B OH  
5710 N N   . GLU   B 114 ? 0.1161 0.1074 0.2208 -0.0039 0.0096  0.0087  114 GLU   B N   
5711 C CA  . GLU   B 114 ? 0.1157 0.1111 0.2227 -0.0017 0.0042  0.0055  114 GLU   B CA  
5712 C C   . GLU   B 114 ? 0.1215 0.1123 0.2145 -0.0028 0.0058  -0.0006 114 GLU   B C   
5713 O O   . GLU   B 114 ? 0.1200 0.1139 0.2142 -0.0004 0.0035  0.0050  114 GLU   B O   
5714 C CB  . GLU   B 114 ? 0.1203 0.1178 0.2323 -0.0031 0.0074  0.0125  114 GLU   B CB  
5715 C CG  . GLU   B 114 ? 0.1251 0.1189 0.2305 -0.0037 0.0092  0.0086  114 GLU   B CG  
5716 C CD  . GLU   B 114 ? 0.1246 0.1273 0.2368 -0.0057 0.0043  0.0065  114 GLU   B CD  
5717 O OE1 . GLU   B 114 ? 0.1227 0.1417 0.2225 -0.0093 0.0172  0.0086  114 GLU   B OE1 
5718 O OE2 . GLU   B 114 ? 0.1247 0.1378 0.2506 -0.0168 0.0092  0.0115  114 GLU   B OE2 
5725 N N   . ASN   B 115 ? 0.1263 0.1087 0.2026 -0.0030 -0.0038 0.0080  115 ASN   B N   
5726 C CA  . ASN   B 115 ? 0.1270 0.1191 0.1856 -0.0085 -0.0007 0.0091  115 ASN   B CA  
5727 C C   . ASN   B 115 ? 0.1181 0.1109 0.1846 -0.0117 -0.0065 0.0021  115 ASN   B C   
5728 O O   . ASN   B 115 ? 0.1323 0.1172 0.2021 -0.0122 0.0010  0.0065  115 ASN   B O   
5729 C CB  . ASN   B 115 ? 0.1319 0.1329 0.1902 -0.0138 -0.0060 0.0103  115 ASN   B CB  
5730 C CG  . ASN   B 115 ? 0.1426 0.1345 0.1941 -0.0022 -0.0006 0.0013  115 ASN   B CG  
5731 O OD1 . ASN   B 115 ? 0.1830 0.1472 0.2089 -0.0037 0.0125  -0.0057 115 ASN   B OD1 
5732 N ND2 . ASN   B 115 ? 0.1357 0.1439 0.1910 -0.0067 0.0030  0.0055  115 ASN   B ND2 
5739 N N   . PHE   B 116 ? 0.1235 0.1115 0.1794 -0.0052 -0.0017 0.0021  116 PHE   B N   
5740 C CA  . PHE   B 116 ? 0.1254 0.1144 0.1858 -0.0103 -0.0034 0.0039  116 PHE   B CA  
5741 C C   . PHE   B 116 ? 0.1298 0.1075 0.1895 -0.0127 -0.0045 0.0088  116 PHE   B C   
5742 O O   . PHE   B 116 ? 0.1321 0.1181 0.1909 -0.0039 -0.0062 0.0041  116 PHE   B O   
5743 C CB  . PHE   B 116 ? 0.1253 0.1171 0.1804 -0.0065 -0.0149 0.0084  116 PHE   B CB  
5744 C CG  . PHE   B 116 ? 0.1183 0.1139 0.1875 -0.0086 -0.0042 0.0058  116 PHE   B CG  
5745 C CD1 . PHE   B 116 ? 0.1251 0.1179 0.2043 -0.0034 -0.0024 0.0001  116 PHE   B CD1 
5746 C CD2 . PHE   B 116 ? 0.1254 0.1224 0.1884 -0.0045 -0.0009 0.0000  116 PHE   B CD2 
5747 C CE1 . PHE   B 116 ? 0.1280 0.1234 0.2033 -0.0049 -0.0103 0.0028  116 PHE   B CE1 
5748 C CE2 . PHE   B 116 ? 0.1247 0.1205 0.1916 -0.0036 -0.0008 0.0031  116 PHE   B CE2 
5749 C CZ  . PHE   B 116 ? 0.1209 0.1237 0.2013 -0.0029 -0.0033 0.0020  116 PHE   B CZ  
5759 N N   . ASN   B 117 ? 0.1223 0.1124 0.2002 -0.0058 -0.0045 0.0089  117 ASN   B N   
5760 C CA  . ASN   B 117 ? 0.1282 0.1182 0.1980 -0.0028 -0.0049 -0.0013 117 ASN   B CA  
5761 C C   . ASN   B 117 ? 0.1320 0.1190 0.2200 0.0019  -0.0074 0.0034  117 ASN   B C   
5762 O O   . ASN   B 117 ? 0.1429 0.1234 0.2343 -0.0056 -0.0305 0.0066  117 ASN   B O   
5763 C CB  . ASN   B 117 ? 0.1263 0.1175 0.2039 -0.0034 -0.0054 -0.0043 117 ASN   B CB  
5764 C CG  . ASN   B 117 ? 0.1242 0.1223 0.2105 -0.0010 -0.0032 -0.0068 117 ASN   B CG  
5765 O OD1 . ASN   B 117 ? 0.1483 0.1175 0.2290 -0.0112 0.0047  -0.0073 117 ASN   B OD1 
5766 N ND2 . ASN   B 117 ? 0.1328 0.1229 0.2088 -0.0035 -0.0008 -0.0024 117 ASN   B ND2 
5773 N N   . GLN   B 118 ? 0.1282 0.1161 0.2084 -0.0100 -0.0143 -0.0023 118 GLN   B N   
5774 C CA  . GLN   B 118 ? 0.1344 0.1152 0.2218 0.0014  -0.0122 0.0003  118 GLN   B CA  
5775 C C   . GLN   B 118 ? 0.1427 0.1159 0.2234 -0.0020 -0.0097 -0.0011 118 GLN   B C   
5776 O O   . GLN   B 118 ? 0.1619 0.1115 0.2476 -0.0129 0.0013  0.0055  118 GLN   B O   
5777 C CB  . GLN   B 118 ? 0.1413 0.1189 0.2378 0.0001  -0.0180 0.0001  118 GLN   B CB  
5778 C CG  . GLN   B 118 ? 0.1510 0.1216 0.2289 0.0024  -0.0083 -0.0120 118 GLN   B CG  
5779 C CD  . GLN   B 118 ? 0.1550 0.1198 0.2215 0.0029  -0.0104 -0.0161 118 GLN   B CD  
5780 O OE1 . GLN   B 118 ? 0.1608 0.1173 0.2387 0.0031  0.0017  0.0041  118 GLN   B OE1 
5781 N NE2 . GLN   B 118 ? 0.1644 0.1213 0.2238 0.0037  -0.0086 -0.0026 118 GLN   B NE2 
5790 N N   . HIS   B 119 ? 0.1451 0.1144 0.1904 -0.0069 -0.0099 0.0072  119 HIS   B N   
5791 C CA  . HIS   B 119 ? 0.1513 0.1281 0.1816 -0.0046 -0.0160 0.0044  119 HIS   B CA  
5792 C C   . HIS   B 119 ? 0.1523 0.1255 0.1756 -0.0058 -0.0229 0.0059  119 HIS   B C   
5793 O O   . HIS   B 119 ? 0.1600 0.1259 0.2012 -0.0240 -0.0221 0.0082  119 HIS   B O   
5794 C CB  . HIS   B 119 ? 0.1566 0.1406 0.1911 -0.0024 -0.0182 -0.0001 119 HIS   B CB  
5795 C CG  . HIS   B 119 ? 0.1618 0.1630 0.2060 0.0072  -0.0353 -0.0198 119 HIS   B CG  
5796 N ND1 . HIS   B 119 ? 0.1708 0.1802 0.2335 0.0032  -0.0465 -0.0355 119 HIS   B ND1 
5797 C CD2 . HIS   B 119 ? 0.1810 0.1815 0.2105 0.0343  -0.0447 -0.0270 119 HIS   B CD2 
5798 C CE1 . HIS   B 119 ? 0.1920 0.1965 0.2395 0.0186  -0.0516 -0.0396 119 HIS   B CE1 
5799 N NE2 . HIS   B 119 ? 0.1929 0.2046 0.2251 0.0298  -0.0488 -0.0363 119 HIS   B NE2 
5807 N N   . GLU   B 120 ? 0.1721 0.1276 0.1779 -0.0096 -0.0292 0.0111  120 GLU   B N   
5808 C CA  . GLU   B 120 ? 0.1981 0.1440 0.1940 -0.0073 -0.0453 0.0248  120 GLU   B CA  
5809 C C   . GLU   B 120 ? 0.1765 0.1353 0.1901 -0.0166 -0.0368 0.0259  120 GLU   B C   
5810 O O   . GLU   B 120 ? 0.1706 0.1442 0.1863 -0.0169 -0.0358 0.0163  120 GLU   B O   
5811 C CB  . GLU   B 120 ? 0.2630 0.1789 0.2607 0.0154  -0.0735 0.0481  120 GLU   B CB  
5812 C CG  . GLU   B 120 ? 0.3228 0.2538 0.3501 0.0243  -0.0940 0.0603  120 GLU   B CG  
5813 C CD  . GLU   B 120 ? 0.3678 0.3222 0.4428 0.0251  -0.0995 0.0705  120 GLU   B CD  
5814 O OE1 . GLU   B 120 ? 0.3904 0.3465 0.4748 0.0210  -0.0938 0.0829  120 GLU   B OE1 
5815 O OE2 . GLU   B 120 ? 0.3880 0.3507 0.4928 0.0242  -0.0984 0.0624  120 GLU   B OE2 
5822 N N   . VAL   B 121 ? 0.1671 0.1313 0.1847 -0.0239 -0.0199 0.0226  121 VAL   B N   
5823 C CA  . VAL   B 121 ? 0.1655 0.1425 0.1689 -0.0192 -0.0227 0.0102  121 VAL   B CA  
5824 C C   . VAL   B 121 ? 0.1529 0.1348 0.1657 -0.0259 -0.0150 0.0103  121 VAL   B C   
5825 O O   . VAL   B 121 ? 0.1640 0.1348 0.1855 -0.0331 -0.0239 0.0075  121 VAL   B O   
5826 C CB  . VAL   B 121 ? 0.1869 0.1809 0.1702 -0.0086 -0.0257 0.0108  121 VAL   B CB  
5827 C CG1 . VAL   B 121 ? 0.1926 0.1919 0.1974 -0.0201 -0.0153 0.0108  121 VAL   B CG1 
5828 C CG2 . VAL   B 121 ? 0.2130 0.2032 0.1721 0.0037  -0.0204 0.0055  121 VAL   B CG2 
5838 N N   . LEU   B 122 ? 0.1470 0.1288 0.1600 -0.0164 -0.0237 0.0073  122 LEU   B N   
5839 C CA  . LEU   B 122 ? 0.1360 0.1396 0.1491 -0.0194 -0.0184 0.0119  122 LEU   B CA  
5840 C C   . LEU   B 122 ? 0.1379 0.1252 0.1621 -0.0261 -0.0185 0.0110  122 LEU   B C   
5841 O O   . LEU   B 122 ? 0.1492 0.1279 0.1953 -0.0319 -0.0229 0.0046  122 LEU   B O   
5842 C CB  . LEU   B 122 ? 0.1621 0.1476 0.1799 -0.0052 -0.0257 0.0134  122 LEU   B CB  
5843 C CG  . LEU   B 122 ? 0.1500 0.1528 0.1922 -0.0126 -0.0140 0.0153  122 LEU   B CG  
5844 C CD1 . LEU   B 122 ? 0.1524 0.1791 0.2006 -0.0176 -0.0130 0.0050  122 LEU   B CD1 
5845 C CD2 . LEU   B 122 ? 0.1542 0.1558 0.1728 -0.0109 -0.0092 0.0002  122 LEU   B CD2 
5857 N N   . LEU   B 123 ? 0.1383 0.1170 0.1603 -0.0229 -0.0146 0.0128  123 LEU   B N   
5858 C CA  . LEU   B 123 ? 0.1415 0.1204 0.1623 -0.0240 -0.0177 -0.0012 123 LEU   B CA  
5859 C C   . LEU   B 123 ? 0.1391 0.1152 0.1657 -0.0251 -0.0179 0.0015  123 LEU   B C   
5860 O O   . LEU   B 123 ? 0.1466 0.1192 0.1663 -0.0299 -0.0160 0.0019  123 LEU   B O   
5861 C CB  . LEU   B 123 ? 0.1447 0.1206 0.1732 -0.0232 -0.0094 -0.0010 123 LEU   B CB  
5862 C CG  . LEU   B 123 ? 0.1429 0.1288 0.1753 -0.0163 -0.0046 0.0085  123 LEU   B CG  
5863 C CD1 . LEU   B 123 ? 0.1537 0.1349 0.1925 -0.0157 -0.0027 -0.0089 123 LEU   B CD1 
5864 C CD2 . LEU   B 123 ? 0.1500 0.1394 0.1949 -0.0140 -0.0003 0.0167  123 LEU   B CD2 
5876 N N   . ALA   B 124 ? 0.1355 0.1170 0.1649 -0.0243 -0.0087 0.0025  124 ALA   B N   
5877 C CA  . ALA   B 124 ? 0.1324 0.1193 0.1684 -0.0180 -0.0112 -0.0022 124 ALA   B CA  
5878 C C   . ALA   B 124 ? 0.1254 0.1149 0.1662 -0.0165 -0.0119 0.0024  124 ALA   B C   
5879 O O   . ALA   B 124 ? 0.1359 0.1185 0.1731 -0.0131 -0.0110 0.0007  124 ALA   B O   
5880 C CB  . ALA   B 124 ? 0.1373 0.1231 0.1783 -0.0110 -0.0031 0.0002  124 ALA   B CB  
5886 N N   . PRO   B 125 ? 0.1366 0.1204 0.1620 -0.0137 -0.0143 0.0095  125 PRO   B N   
5887 C CA  . PRO   B 125 ? 0.1455 0.1211 0.1760 -0.0155 -0.0176 0.0193  125 PRO   B CA  
5888 C C   . PRO   B 125 ? 0.1375 0.1158 0.1877 -0.0129 -0.0112 0.0141  125 PRO   B C   
5889 O O   . PRO   B 125 ? 0.1408 0.1185 0.2035 -0.0119 -0.0058 0.0151  125 PRO   B O   
5890 C CB  . PRO   B 125 ? 0.1488 0.1468 0.1926 -0.0160 -0.0180 0.0321  125 PRO   B CB  
5891 C CG  . PRO   B 125 ? 0.1500 0.1510 0.1839 -0.0284 -0.0203 0.0170  125 PRO   B CG  
5892 C CD  . PRO   B 125 ? 0.1449 0.1301 0.1673 -0.0254 -0.0116 0.0103  125 PRO   B CD  
5900 N N   . LEU   B 126 ? 0.1423 0.1150 0.2110 -0.0161 0.0079  0.0159  126 LEU   B N   
5901 C CA  . LEU   B 126 ? 0.1469 0.1224 0.2147 -0.0110 0.0142  0.0119  126 LEU   B CA  
5902 C C   . LEU   B 126 ? 0.1410 0.1302 0.2184 -0.0021 0.0182  0.0171  126 LEU   B C   
5903 O O   . LEU   B 126 ? 0.1632 0.1593 0.2281 0.0161  -0.0029 -0.0059 126 LEU   B O   
5904 C CB  . LEU   B 126 ? 0.1709 0.1298 0.2428 -0.0119 0.0239  0.0092  126 LEU   B CB  
5905 C CG  . LEU   B 126 ? 0.1859 0.1374 0.2565 -0.0217 0.0247  -0.0095 126 LEU   B CG  
5906 C CD1 . LEU   B 126 ? 0.2005 0.1475 0.2942 -0.0238 0.0185  -0.0230 126 LEU   B CD1 
5907 C CD2 . LEU   B 126 ? 0.1864 0.1426 0.2568 -0.0255 0.0236  -0.0098 126 LEU   B CD2 
5919 N N   . LEU   B 127 ? 0.1415 0.1171 0.2348 0.0013  0.0219  0.0160  127 LEU   B N   
5920 C CA  . LEU   B 127 ? 0.1410 0.1308 0.2422 -0.0052 0.0233  0.0196  127 LEU   B CA  
5921 C C   . LEU   B 127 ? 0.1365 0.1228 0.2365 -0.0043 0.0185  0.0225  127 LEU   B C   
5922 O O   . LEU   B 127 ? 0.1395 0.1286 0.2494 -0.0145 0.0130  0.0261  127 LEU   B O   
5923 C CB  . LEU   B 127 ? 0.1526 0.1280 0.2487 -0.0045 0.0201  0.0221  127 LEU   B CB  
5924 C CG  . LEU   B 127 ? 0.1650 0.1301 0.2474 0.0011  0.0225  0.0259  127 LEU   B CG  
5925 C CD1 . LEU   B 127 ? 0.1751 0.1290 0.2468 0.0062  0.0172  0.0138  127 LEU   B CD1 
5926 C CD2 . LEU   B 127 ? 0.1678 0.1412 0.2610 -0.0140 0.0271  0.0318  127 LEU   B CD2 
5938 N N   . SER   B 128 ? 0.1387 0.1270 0.2357 -0.0002 0.0068  0.0152  128 SER   B N   
5939 C CA  . SER   B 128 ? 0.1600 0.1346 0.2272 0.0068  -0.0017 0.0211  128 SER   B CA  
5940 C C   . SER   B 128 ? 0.1674 0.1401 0.2411 0.0029  -0.0252 0.0202  128 SER   B C   
5941 O O   . SER   B 128 ? 0.1850 0.1435 0.2694 0.0025  -0.0243 0.0308  128 SER   B O   
5942 C CB  . SER   B 128 ? 0.1705 0.1353 0.2190 0.0098  0.0066  0.0357  128 SER   B CB  
5943 O OG  . SER   B 128 ? 0.1731 0.1504 0.2330 0.0125  0.0145  0.0346  128 SER   B OG  
5949 N N   . ALA   B 129 ? 0.1837 0.1440 0.2725 0.0237  -0.0125 0.0064  129 ALA   B N   
5950 C CA  . ALA   B 129 ? 0.1956 0.1518 0.2878 0.0321  -0.0099 -0.0034 129 ALA   B CA  
5951 C C   . ALA   B 129 ? 0.1841 0.1429 0.2757 0.0186  0.0052  0.0053  129 ALA   B C   
5952 O O   . ALA   B 129 ? 0.1742 0.1485 0.2706 0.0150  0.0014  0.0047  129 ALA   B O   
5953 C CB  . ALA   B 129 ? 0.2160 0.1757 0.3134 0.0348  0.0025  -0.0103 129 ALA   B CB  
5959 N N   . GLY   B 130 ? 0.1814 0.1403 0.2746 0.0249  0.0062  -0.0026 130 GLY   B N   
5960 C CA  . GLY   B 130 ? 0.1880 0.1499 0.2754 0.0197  0.0243  -0.0079 130 GLY   B CA  
5961 C C   . GLY   B 130 ? 0.1946 0.1564 0.2681 0.0168  0.0136  0.0084  130 GLY   B C   
5962 O O   . GLY   B 130 ? 0.2087 0.1654 0.2712 0.0165  0.0088  0.0182  130 GLY   B O   
5966 N N   . ILE   B 131 ? 0.1844 0.1731 0.2760 0.0316  0.0116  0.0059  131 ILE   B N   
5967 C CA  . ILE   B 131 ? 0.2025 0.1864 0.2753 0.0255  -0.0059 0.0217  131 ILE   B CA  
5968 C C   . ILE   B 131 ? 0.2151 0.1740 0.2368 0.0167  -0.0095 0.0258  131 ILE   B C   
5969 O O   . ILE   B 131 ? 0.2417 0.1920 0.2484 0.0165  -0.0225 0.0212  131 ILE   B O   
5970 C CB  . ILE   B 131 ? 0.2018 0.2175 0.3173 0.0269  -0.0125 0.0254  131 ILE   B CB  
5971 C CG1 . ILE   B 131 ? 0.2035 0.2343 0.3355 0.0026  -0.0066 0.0280  131 ILE   B CG1 
5972 C CG2 . ILE   B 131 ? 0.1972 0.2344 0.3375 0.0390  -0.0100 0.0223  131 ILE   B CG2 
5973 C CD1 . ILE   B 131 ? 0.2088 0.2538 0.3503 -0.0142 -0.0131 0.0323  131 ILE   B CD1 
5985 N N   . PHE   B 132 ? 0.1972 0.1565 0.2276 0.0130  0.0036  0.0284  132 PHE   B N   
5986 C CA  . PHE   B 132 ? 0.2066 0.1590 0.2321 0.0073  0.0281  0.0124  132 PHE   B CA  
5987 C C   . PHE   B 132 ? 0.2250 0.1721 0.2529 0.0085  0.0365  0.0127  132 PHE   B C   
5988 O O   . PHE   B 132 ? 0.2437 0.1924 0.2756 0.0064  0.0503  0.0224  132 PHE   B O   
5989 C CB  . PHE   B 132 ? 0.1905 0.1570 0.2126 0.0118  0.0287  0.0183  132 PHE   B CB  
5990 C CG  . PHE   B 132 ? 0.1875 0.1635 0.2207 0.0148  0.0274  0.0204  132 PHE   B CG  
5991 C CD1 . PHE   B 132 ? 0.1930 0.1637 0.2440 0.0154  0.0242  0.0214  132 PHE   B CD1 
5992 C CD2 . PHE   B 132 ? 0.1891 0.1636 0.2019 0.0241  0.0194  0.0320  132 PHE   B CD2 
5993 C CE1 . PHE   B 132 ? 0.2005 0.1679 0.2487 0.0103  0.0206  0.0234  132 PHE   B CE1 
5994 C CE2 . PHE   B 132 ? 0.1944 0.1666 0.2084 0.0200  0.0147  0.0251  132 PHE   B CE2 
5995 C CZ  . PHE   B 132 ? 0.1981 0.1685 0.2360 0.0120  0.0052  0.0309  132 PHE   B CZ  
6005 N N   . GLY   B 133 ? 0.2252 0.1634 0.2549 0.0036  0.0252  0.0363  133 GLY   B N   
6006 C CA  . GLY   B 133 ? 0.2336 0.1777 0.2596 -0.0175 0.0221  0.0376  133 GLY   B CA  
6007 C C   . GLY   B 133 ? 0.2381 0.1842 0.2544 -0.0315 0.0256  0.0484  133 GLY   B C   
6008 O O   . GLY   B 133 ? 0.2576 0.1994 0.2855 -0.0423 0.0283  0.0571  133 GLY   B O   
6012 N N   . ALA   B 134 ? 0.2190 0.1836 0.2443 -0.0324 0.0246  0.0334  134 ALA   B N   
6013 C CA  . ALA   B 134 ? 0.2112 0.1810 0.2525 -0.0247 0.0336  0.0156  134 ALA   B CA  
6014 C C   . ALA   B 134 ? 0.2169 0.1703 0.2537 -0.0132 0.0350  0.0250  134 ALA   B C   
6015 O O   . ALA   B 134 ? 0.2241 0.1869 0.2762 0.0031  0.0320  0.0200  134 ALA   B O   
6016 C CB  . ALA   B 134 ? 0.2108 0.1803 0.2694 -0.0161 0.0278  0.0059  134 ALA   B CB  
6022 N N   . ASP   B 135 ? 0.2293 0.1627 0.2569 -0.0177 0.0194  0.0296  135 ASP   B N   
6023 C CA  . ASP   B 135 ? 0.2467 0.1553 0.2776 -0.0173 0.0026  0.0323  135 ASP   B CA  
6024 C C   . ASP   B 135 ? 0.2290 0.1457 0.2612 -0.0038 0.0011  0.0318  135 ASP   B C   
6025 O O   . ASP   B 135 ? 0.2203 0.1398 0.2766 -0.0019 0.0055  0.0317  135 ASP   B O   
6026 C CB  . ASP   B 135 ? 0.2763 0.1695 0.3140 -0.0399 -0.0005 0.0360  135 ASP   B CB  
6027 C CG  . ASP   B 135 ? 0.3050 0.1712 0.3559 -0.0589 -0.0004 0.0332  135 ASP   B CG  
6028 O OD1 . ASP   B 135 ? 0.3144 0.1587 0.3565 -0.0402 -0.0054 0.0378  135 ASP   B OD1 
6029 O OD2 . ASP   B 135 ? 0.3287 0.2023 0.4019 -0.0721 0.0010  0.0157  135 ASP   B OD2 
6034 N N   . PRO   B 136 ? 0.2205 0.1492 0.2731 0.0140  -0.0103 0.0242  136 PRO   B N   
6035 C CA  . PRO   B 136 ? 0.1957 0.1364 0.2786 0.0166  -0.0079 0.0155  136 PRO   B CA  
6036 C C   . PRO   B 136 ? 0.1797 0.1278 0.2882 0.0111  -0.0058 0.0172  136 PRO   B C   
6037 O O   . PRO   B 136 ? 0.1658 0.1268 0.2803 0.0082  0.0029  0.0183  136 PRO   B O   
6038 C CB  . PRO   B 136 ? 0.2034 0.1620 0.2902 0.0237  -0.0125 -0.0021 136 PRO   B CB  
6039 C CG  . PRO   B 136 ? 0.2228 0.1680 0.3022 0.0293  -0.0065 -0.0018 136 PRO   B CG  
6040 C CD  . PRO   B 136 ? 0.2250 0.1626 0.2877 0.0332  -0.0027 0.0082  136 PRO   B CD  
6048 N N   . ILE   B 137 ? 0.1925 0.1269 0.2992 0.0131  -0.0060 0.0095  137 ILE   B N   
6049 C CA  . ILE   B 137 ? 0.1966 0.1225 0.3101 -0.0029 -0.0021 0.0064  137 ILE   B CA  
6050 C C   . ILE   B 137 ? 0.1890 0.1307 0.3052 -0.0115 0.0092  0.0127  137 ILE   B C   
6051 O O   . ILE   B 137 ? 0.1792 0.1294 0.2996 -0.0138 0.0063  0.0114  137 ILE   B O   
6052 C CB  . ILE   B 137 ? 0.2187 0.1315 0.3531 -0.0059 0.0044  0.0068  137 ILE   B CB  
6053 C CG1 . ILE   B 137 ? 0.2439 0.1470 0.3996 0.0027  0.0131  -0.0054 137 ILE   B CG1 
6054 C CG2 . ILE   B 137 ? 0.2161 0.1350 0.3635 -0.0260 0.0048  0.0110  137 ILE   B CG2 
6055 C CD1 . ILE   B 137 ? 0.2648 0.1726 0.4334 0.0168  0.0127  0.0022  137 ILE   B CD1 
6067 N N   . HIS   B 138 ? 0.1941 0.1287 0.2964 -0.0089 0.0210  0.0131  138 HIS   B N   
6068 C CA  . HIS   B 138 ? 0.2027 0.1431 0.2908 -0.0104 0.0279  0.0132  138 HIS   B CA  
6069 C C   . HIS   B 138 ? 0.1855 0.1365 0.2803 -0.0100 0.0251  0.0223  138 HIS   B C   
6070 O O   . HIS   B 138 ? 0.1730 0.1413 0.3018 -0.0063 0.0395  0.0366  138 HIS   B O   
6071 C CB  . HIS   B 138 ? 0.2283 0.1572 0.3014 -0.0128 0.0378  0.0137  138 HIS   B CB  
6072 C CG  . HIS   B 138 ? 0.2453 0.1730 0.3039 -0.0163 0.0543  0.0309  138 HIS   B CG  
6073 N ND1 . HIS   B 138 ? 0.2514 0.1865 0.3217 -0.0105 0.0685  0.0230  138 HIS   B ND1 
6074 C CD2 . HIS   B 138 ? 0.2591 0.1849 0.2988 -0.0146 0.0569  0.0274  138 HIS   B CD2 
6075 C CE1 . HIS   B 138 ? 0.2561 0.1901 0.3179 -0.0100 0.0738  0.0252  138 HIS   B CE1 
6076 N NE2 . HIS   B 138 ? 0.2638 0.1821 0.3039 -0.0052 0.0687  0.0194  138 HIS   B NE2 
6084 N N   . SER   B 139 ? 0.1822 0.1256 0.2746 -0.0016 0.0265  0.0115  139 SER   B N   
6085 C CA  . SER   B 139 ? 0.1765 0.1178 0.2642 -0.0036 0.0245  0.0085  139 SER   B CA  
6086 C C   . SER   B 139 ? 0.1538 0.1112 0.2680 -0.0047 0.0163  0.0089  139 SER   B C   
6087 O O   . SER   B 139 ? 0.1576 0.1126 0.2606 0.0005  0.0080  0.0117  139 SER   B O   
6088 C CB  . SER   B 139 ? 0.1818 0.1231 0.2778 -0.0022 0.0134  0.0002  139 SER   B CB  
6089 O OG  . SER   B 139 ? 0.1803 0.1183 0.2784 -0.0011 0.0004  0.0145  139 SER   B OG  
6095 N N   . LEU   B 140 ? 0.1555 0.1077 0.2614 -0.0097 0.0194  0.0023  140 LEU   B N   
6096 C CA  . LEU   B 140 ? 0.1503 0.1131 0.2633 -0.0053 0.0122  0.0057  140 LEU   B CA  
6097 C C   . LEU   B 140 ? 0.1478 0.1116 0.2774 -0.0084 0.0022  -0.0007 140 LEU   B C   
6098 O O   . LEU   B 140 ? 0.1392 0.1197 0.2755 -0.0019 -0.0015 0.0056  140 LEU   B O   
6099 C CB  . LEU   B 140 ? 0.1457 0.1116 0.2696 -0.0106 0.0138  -0.0089 140 LEU   B CB  
6100 C CG  . LEU   B 140 ? 0.1559 0.1162 0.2682 -0.0143 0.0070  0.0005  140 LEU   B CG  
6101 C CD1 . LEU   B 140 ? 0.1657 0.1260 0.2844 -0.0148 0.0080  0.0003  140 LEU   B CD1 
6102 C CD2 . LEU   B 140 ? 0.1735 0.1259 0.2819 -0.0087 0.0041  -0.0084 140 LEU   B CD2 
6114 N N   . ARG   B 141 ? 0.1365 0.1123 0.2954 -0.0144 0.0083  -0.0030 141 ARG   B N   
6115 C CA  . ARG   B 141 ? 0.1407 0.1114 0.3219 -0.0161 0.0254  -0.0028 141 ARG   B CA  
6116 C C   . ARG   B 141 ? 0.1322 0.1199 0.3038 -0.0168 0.0164  -0.0031 141 ARG   B C   
6117 O O   . ARG   B 141 ? 0.1371 0.1228 0.3064 -0.0131 0.0056  -0.0100 141 ARG   B O   
6118 C CB  . ARG   B 141 ? 0.1579 0.1269 0.3380 -0.0200 0.0298  -0.0036 141 ARG   B CB  
6119 C CG  . ARG   B 141 ? 0.1865 0.1543 0.3515 -0.0204 0.0313  -0.0031 141 ARG   B CG  
6120 C CD  . ARG   B 141 ? 0.2264 0.1784 0.3474 -0.0166 0.0189  -0.0158 141 ARG   B CD  
6121 N NE  . ARG   B 141 ? 0.2498 0.1789 0.3397 -0.0342 0.0221  -0.0190 141 ARG   B NE  
6122 C CZ  . ARG   B 141 ? 0.2651 0.1643 0.3232 -0.0297 0.0343  -0.0264 141 ARG   B CZ  
6123 N NH1 . ARG   B 141 ? 0.2759 0.1574 0.3160 -0.0265 0.0322  -0.0256 141 ARG   B NH1 
6124 N NH2 . ARG   B 141 ? 0.2768 0.1761 0.3309 -0.0167 0.0209  -0.0156 141 ARG   B NH2 
6138 N N   . VAL   B 142 ? 0.1403 0.1121 0.2842 -0.0106 0.0161  -0.0052 142 VAL   B N   
6139 C CA  . VAL   B 142 ? 0.1388 0.1152 0.2812 -0.0110 0.0177  -0.0001 142 VAL   B CA  
6140 C C   . VAL   B 142 ? 0.1306 0.1114 0.2796 -0.0023 0.0085  -0.0077 142 VAL   B C   
6141 O O   . VAL   B 142 ? 0.1378 0.1132 0.2898 -0.0013 0.0108  -0.0041 142 VAL   B O   
6142 C CB  . VAL   B 142 ? 0.1516 0.1295 0.2792 -0.0036 0.0190  0.0119  142 VAL   B CB  
6143 C CG1 . VAL   B 142 ? 0.1473 0.1258 0.2743 0.0054  0.0195  0.0098  142 VAL   B CG1 
6144 C CG2 . VAL   B 142 ? 0.1702 0.1291 0.2828 -0.0011 0.0180  0.0098  142 VAL   B CG2 
6154 N N   . CYS   B 143 ? 0.1286 0.1169 0.2696 -0.0007 0.0026  0.0064  143 CYS   B N   
6155 C CA  . CYS   B 143 ? 0.1278 0.1148 0.2713 -0.0082 0.0028  0.0050  143 CYS   B CA  
6156 C C   . CYS   B 143 ? 0.1261 0.1127 0.2674 -0.0070 0.0054  -0.0006 143 CYS   B C   
6157 O O   . CYS   B 143 ? 0.1344 0.1184 0.2633 -0.0035 0.0029  0.0001  143 CYS   B O   
6158 C CB  . CYS   B 143 ? 0.1356 0.1280 0.2682 -0.0097 0.0020  0.0014  143 CYS   B CB  
6159 S SG  . CYS   B 143 ? 0.1381 0.1390 0.2570 -0.0060 0.0054  0.0069  143 CYS   B SG  
6165 N N   . VAL   B 144 ? 0.1329 0.1182 0.2765 -0.0121 -0.0016 -0.0078 144 VAL   B N   
6166 C CA  . VAL   B 144 ? 0.1386 0.1296 0.2925 -0.0131 -0.0068 -0.0162 144 VAL   B CA  
6167 C C   . VAL   B 144 ? 0.1379 0.1313 0.2948 -0.0121 -0.0112 -0.0031 144 VAL   B C   
6168 O O   . VAL   B 144 ? 0.1463 0.1482 0.3205 -0.0036 -0.0124 0.0149  144 VAL   B O   
6169 C CB  . VAL   B 144 ? 0.1611 0.1438 0.3416 -0.0143 -0.0188 -0.0347 144 VAL   B CB  
6170 C CG1 . VAL   B 144 ? 0.1862 0.1855 0.3747 -0.0084 -0.0299 -0.0214 144 VAL   B CG1 
6171 C CG2 . VAL   B 144 ? 0.1773 0.1473 0.3261 -0.0032 -0.0355 -0.0451 144 VAL   B CG2 
6181 N N   . ASP   B 145 ? 0.1406 0.1282 0.3033 -0.0113 -0.0082 -0.0113 145 ASP   B N   
6182 C CA  . ASP   B 145 ? 0.1372 0.1298 0.3247 -0.0084 0.0111  -0.0102 145 ASP   B CA  
6183 C C   . ASP   B 145 ? 0.1328 0.1366 0.3128 -0.0125 0.0135  -0.0121 145 ASP   B C   
6184 O O   . ASP   B 145 ? 0.1363 0.1482 0.3610 -0.0142 0.0199  -0.0254 145 ASP   B O   
6185 C CB  . ASP   B 145 ? 0.1499 0.1383 0.3627 -0.0142 0.0263  -0.0075 145 ASP   B CB  
6186 C CG  . ASP   B 145 ? 0.1663 0.1405 0.4037 -0.0294 0.0348  -0.0095 145 ASP   B CG  
6187 O OD1 . ASP   B 145 ? 0.1711 0.1425 0.4111 -0.0252 0.0012  -0.0197 145 ASP   B OD1 
6188 O OD2 . ASP   B 145 ? 0.1985 0.1522 0.4461 -0.0351 0.0549  -0.0004 145 ASP   B OD2 
6193 N N   . THR   B 146 ? 0.1264 0.1251 0.2713 -0.0123 0.0007  0.0021  146 THR   B N   
6194 C CA  . THR   B 146 ? 0.1306 0.1194 0.2468 -0.0123 0.0031  -0.0021 146 THR   B CA  
6195 C C   . THR   B 146 ? 0.1342 0.1209 0.2476 -0.0065 0.0004  0.0042  146 THR   B C   
6196 O O   . THR   B 146 ? 0.1399 0.1190 0.2526 -0.0046 -0.0021 0.0033  146 THR   B O   
6197 C CB  . THR   B 146 ? 0.1396 0.1191 0.2576 -0.0088 0.0178  0.0014  146 THR   B CB  
6198 O OG1 . THR   B 146 ? 0.1441 0.1194 0.2763 -0.0075 0.0209  0.0117  146 THR   B OG1 
6199 C CG2 . THR   B 146 ? 0.1482 0.1271 0.2630 -0.0083 0.0161  -0.0000 146 THR   B CG2 
6207 N N   . VAL   B 147 ? 0.1361 0.1210 0.2448 -0.0073 0.0109  0.0056  147 VAL   B N   
6208 C CA  . VAL   B 147 ? 0.1369 0.1210 0.2360 -0.0126 -0.0071 0.0017  147 VAL   B CA  
6209 C C   . VAL   B 147 ? 0.1336 0.1162 0.2436 -0.0174 -0.0085 -0.0021 147 VAL   B C   
6210 O O   . VAL   B 147 ? 0.1445 0.1267 0.2598 -0.0209 -0.0299 -0.0071 147 VAL   B O   
6211 C CB  . VAL   B 147 ? 0.1408 0.1322 0.2228 -0.0096 -0.0064 0.0010  147 VAL   B CB  
6212 C CG1 . VAL   B 147 ? 0.1423 0.1427 0.2088 -0.0119 -0.0013 -0.0002 147 VAL   B CG1 
6213 C CG2 . VAL   B 147 ? 0.1410 0.1293 0.2233 -0.0070 0.0055  -0.0037 147 VAL   B CG2 
6223 N N   . ARG   B 148 ? 0.1348 0.1200 0.2402 -0.0111 -0.0189 -0.0057 148 ARG   B N   
6224 C CA  . ARG   B 148 ? 0.1403 0.1325 0.2347 -0.0072 -0.0303 -0.0068 148 ARG   B CA  
6225 C C   . ARG   B 148 ? 0.1459 0.1420 0.2237 -0.0077 -0.0323 -0.0072 148 ARG   B C   
6226 O O   . ARG   B 148 ? 0.1645 0.1666 0.2258 -0.0232 -0.0397 0.0008  148 ARG   B O   
6227 C CB  . ARG   B 148 ? 0.1450 0.1435 0.2319 -0.0026 -0.0293 -0.0165 148 ARG   B CB  
6228 C CG  . ARG   B 148 ? 0.1405 0.1581 0.2473 -0.0119 -0.0276 -0.0254 148 ARG   B CG  
6229 C CD  . ARG   B 148 ? 0.1491 0.1733 0.2567 -0.0001 -0.0251 -0.0270 148 ARG   B CD  
6230 N NE  . ARG   B 148 ? 0.1537 0.1691 0.2511 0.0169  -0.0267 -0.0261 148 ARG   B NE  
6231 C CZ  . ARG   B 148 ? 0.1440 0.1599 0.2275 0.0133  -0.0166 -0.0169 148 ARG   B CZ  
6232 N NH1 . ARG   B 148 ? 0.1435 0.1630 0.2319 -0.0002 -0.0034 -0.0154 148 ARG   B NH1 
6233 N NH2 . ARG   B 148 ? 0.1689 0.1469 0.2123 0.0129  -0.0128 -0.0093 148 ARG   B NH2 
6247 N N   . THR   B 149 ? 0.1460 0.1317 0.2240 -0.0107 -0.0293 0.0002  149 THR   B N   
6248 C CA  . THR   B 149 ? 0.1495 0.1382 0.2122 -0.0127 -0.0240 0.0067  149 THR   B CA  
6249 C C   . THR   B 149 ? 0.1533 0.1356 0.2032 -0.0130 -0.0300 0.0004  149 THR   B C   
6250 O O   . THR   B 149 ? 0.1566 0.1336 0.2147 -0.0226 -0.0164 -0.0010 149 THR   B O   
6251 C CB  . THR   B 149 ? 0.1525 0.1312 0.2141 -0.0154 -0.0269 -0.0012 149 THR   B CB  
6252 O OG1 . THR   B 149 ? 0.1556 0.1398 0.2032 -0.0232 -0.0312 0.0034  149 THR   B OG1 
6253 C CG2 . THR   B 149 ? 0.1613 0.1396 0.2282 -0.0098 -0.0197 -0.0025 149 THR   B CG2 
6261 N N   . ASN   B 150 ? 0.1602 0.1338 0.1969 -0.0146 -0.0335 -0.0024 150 ASN   B N   
6262 C CA  . ASN   B 150 ? 0.1643 0.1495 0.1899 -0.0205 -0.0327 -0.0034 150 ASN   B CA  
6263 C C   . ASN   B 150 ? 0.1542 0.1431 0.1918 -0.0173 -0.0259 -0.0010 150 ASN   B C   
6264 O O   . ASN   B 150 ? 0.1634 0.1388 0.2058 -0.0271 -0.0381 -0.0016 150 ASN   B O   
6265 C CB  . ASN   B 150 ? 0.1860 0.1845 0.1975 -0.0262 -0.0391 0.0089  150 ASN   B CB  
6266 C CG  . ASN   B 150 ? 0.2123 0.2262 0.2322 -0.0220 -0.0459 0.0290  150 ASN   B CG  
6267 O OD1 . ASN   B 150 ? 0.2195 0.2429 0.2568 -0.0304 -0.0615 0.0223  150 ASN   B OD1 
6268 N ND2 . ASN   B 150 ? 0.2222 0.2437 0.2549 -0.0119 -0.0467 0.0660  150 ASN   B ND2 
6275 N N   . VAL   B 151 ? 0.1466 0.1394 0.1989 -0.0208 -0.0315 0.0045  151 VAL   B N   
6276 C CA  . VAL   B 151 ? 0.1436 0.1383 0.2013 -0.0250 -0.0221 0.0009  151 VAL   B CA  
6277 C C   . VAL   B 151 ? 0.1514 0.1311 0.1945 -0.0305 -0.0243 -0.0003 151 VAL   B C   
6278 O O   . VAL   B 151 ? 0.1555 0.1372 0.2172 -0.0285 -0.0203 -0.0100 151 VAL   B O   
6279 C CB  . VAL   B 151 ? 0.1688 0.1517 0.2126 -0.0079 -0.0177 -0.0024 151 VAL   B CB  
6280 C CG1 . VAL   B 151 ? 0.1750 0.1538 0.2356 -0.0169 -0.0096 -0.0012 151 VAL   B CG1 
6281 C CG2 . VAL   B 151 ? 0.1781 0.1657 0.2043 0.0098  -0.0228 0.0111  151 VAL   B CG2 
6291 N N   . TYR   B 152 ? 0.1477 0.1207 0.1836 -0.0241 -0.0254 -0.0003 152 TYR   B N   
6292 C CA  . TYR   B 152 ? 0.1511 0.1374 0.1716 -0.0284 -0.0129 -0.0092 152 TYR   B CA  
6293 C C   . TYR   B 152 ? 0.1469 0.1236 0.1676 -0.0192 -0.0114 -0.0101 152 TYR   B C   
6294 O O   . TYR   B 152 ? 0.1539 0.1280 0.1768 -0.0270 -0.0131 -0.0064 152 TYR   B O   
6295 C CB  . TYR   B 152 ? 0.1612 0.1510 0.1825 -0.0318 -0.0131 0.0076  152 TYR   B CB  
6296 C CG  . TYR   B 152 ? 0.1790 0.1627 0.1776 -0.0410 -0.0193 0.0022  152 TYR   B CG  
6297 C CD1 . TYR   B 152 ? 0.1923 0.1767 0.1652 -0.0333 -0.0262 -0.0007 152 TYR   B CD1 
6298 C CD2 . TYR   B 152 ? 0.2016 0.1792 0.1795 -0.0349 -0.0173 -0.0073 152 TYR   B CD2 
6299 C CE1 . TYR   B 152 ? 0.2054 0.1943 0.1815 -0.0299 -0.0307 0.0160  152 TYR   B CE1 
6300 C CE2 . TYR   B 152 ? 0.2119 0.2001 0.1788 -0.0364 -0.0204 -0.0126 152 TYR   B CE2 
6301 C CZ  . TYR   B 152 ? 0.2123 0.2116 0.1724 -0.0338 -0.0389 0.0137  152 TYR   B CZ  
6302 O OH  . TYR   B 152 ? 0.2337 0.2422 0.2086 -0.0230 -0.0331 0.0223  152 TYR   B OH  
6312 N N   . LEU   B 153 ? 0.1500 0.1221 0.1774 -0.0293 -0.0137 -0.0090 153 LEU   B N   
6313 C CA  . LEU   B 153 ? 0.1518 0.1237 0.1730 -0.0200 -0.0098 -0.0071 153 LEU   B CA  
6314 C C   . LEU   B 153 ? 0.1530 0.1237 0.1854 -0.0244 -0.0096 -0.0146 153 LEU   B C   
6315 O O   . LEU   B 153 ? 0.1658 0.1440 0.1938 -0.0138 -0.0097 -0.0309 153 LEU   B O   
6316 C CB  . LEU   B 153 ? 0.1501 0.1185 0.1891 -0.0283 -0.0072 -0.0051 153 LEU   B CB  
6317 C CG  . LEU   B 153 ? 0.1484 0.1302 0.2143 -0.0248 -0.0074 0.0008  153 LEU   B CG  
6318 C CD1 . LEU   B 153 ? 0.1564 0.1486 0.2186 -0.0263 0.0030  0.0046  153 LEU   B CD1 
6319 C CD2 . LEU   B 153 ? 0.1512 0.1448 0.2260 -0.0314 -0.0001 0.0050  153 LEU   B CD2 
6331 N N   . ALA   B 154 ? 0.1427 0.1202 0.1984 -0.0088 -0.0145 -0.0097 154 ALA   B N   
6332 C CA  . ALA   B 154 ? 0.1542 0.1326 0.2219 -0.0013 -0.0134 -0.0099 154 ALA   B CA  
6333 C C   . ALA   B 154 ? 0.1627 0.1353 0.2175 0.0022  -0.0241 -0.0188 154 ALA   B C   
6334 O O   . ALA   B 154 ? 0.1933 0.1408 0.2300 0.0054  -0.0101 -0.0057 154 ALA   B O   
6335 C CB  . ALA   B 154 ? 0.1481 0.1490 0.2360 -0.0019 -0.0097 -0.0232 154 ALA   B CB  
6341 N N   . VAL   B 155 ? 0.1391 0.1254 0.2292 -0.0056 -0.0010 -0.0131 155 VAL   B N   
6342 C CA  . VAL   B 155 ? 0.1343 0.1265 0.2417 -0.0036 -0.0095 -0.0027 155 VAL   B CA  
6343 C C   . VAL   B 155 ? 0.1358 0.1322 0.2354 -0.0047 -0.0131 -0.0105 155 VAL   B C   
6344 O O   . VAL   B 155 ? 0.1572 0.1473 0.2674 0.0028  -0.0112 -0.0311 155 VAL   B O   
6345 C CB  . VAL   B 155 ? 0.1424 0.1425 0.2749 -0.0047 -0.0169 0.0078  155 VAL   B CB  
6346 C CG1 . VAL   B 155 ? 0.1469 0.1392 0.2712 -0.0103 -0.0121 -0.0007 155 VAL   B CG1 
6347 C CG2 . VAL   B 155 ? 0.1360 0.1587 0.2959 -0.0096 -0.0121 0.0352  155 VAL   B CG2 
6357 N N   . PHE   B 156 ? 0.1255 0.1422 0.2554 0.0040  -0.0083 -0.0100 156 PHE   B N   
6358 C CA  . PHE   B 156 ? 0.1313 0.1439 0.2940 0.0054  -0.0105 -0.0120 156 PHE   B CA  
6359 C C   . PHE   B 156 ? 0.1302 0.1523 0.3175 0.0101  -0.0152 -0.0316 156 PHE   B C   
6360 O O   . PHE   B 156 ? 0.1590 0.1767 0.3403 0.0227  -0.0010 -0.0399 156 PHE   B O   
6361 C CB  . PHE   B 156 ? 0.1398 0.1419 0.2945 0.0023  -0.0117 -0.0083 156 PHE   B CB  
6362 C CG  . PHE   B 156 ? 0.1408 0.1576 0.3007 -0.0016 -0.0109 0.0117  156 PHE   B CG  
6363 C CD1 . PHE   B 156 ? 0.1469 0.1823 0.3293 0.0088  -0.0030 0.0412  156 PHE   B CD1 
6364 C CD2 . PHE   B 156 ? 0.1486 0.1724 0.3017 0.0096  -0.0169 0.0191  156 PHE   B CD2 
6365 C CE1 . PHE   B 156 ? 0.1493 0.1957 0.3439 0.0065  -0.0039 0.0379  156 PHE   B CE1 
6366 C CE2 . PHE   B 156 ? 0.1559 0.1949 0.3210 0.0133  -0.0176 0.0184  156 PHE   B CE2 
6367 C CZ  . PHE   B 156 ? 0.1455 0.2002 0.3413 0.0183  -0.0215 0.0279  156 PHE   B CZ  
6377 N N   . ASP   B 157 ? 0.1333 0.1425 0.3353 0.0080  -0.0273 -0.0150 157 ASP   B N   
6378 C CA  . ASP   B 157 ? 0.1450 0.1531 0.3660 0.0057  -0.0234 -0.0205 157 ASP   B CA  
6379 C C   . ASP   B 157 ? 0.1490 0.1484 0.3796 0.0055  -0.0206 -0.0337 157 ASP   B C   
6380 O O   . ASP   B 157 ? 0.1360 0.1445 0.3727 0.0033  -0.0207 -0.0330 157 ASP   B O   
6381 C CB  . ASP   B 157 ? 0.1686 0.1751 0.3762 -0.0001 -0.0405 -0.0049 157 ASP   B CB  
6382 C CG  . ASP   B 157 ? 0.2044 0.1886 0.3981 -0.0038 -0.0229 -0.0083 157 ASP   B CG  
6383 O OD1 . ASP   B 157 ? 0.2143 0.1817 0.4139 0.0005  -0.0149 -0.0026 157 ASP   B OD1 
6384 O OD2 . ASP   B 157 ? 0.2339 0.2124 0.4183 -0.0024 -0.0113 -0.0094 157 ASP   B OD2 
6389 N N   . LYS   B 158 ? 0.1502 0.1726 0.3859 0.0064  -0.0058 -0.0576 158 LYS   B N   
6390 C CA  . LYS   B 158 ? 0.1637 0.1879 0.3916 0.0036  -0.0001 -0.0808 158 LYS   B CA  
6391 C C   . LYS   B 158 ? 0.1652 0.1701 0.4007 0.0048  -0.0083 -0.0794 158 LYS   B C   
6392 O O   . LYS   B 158 ? 0.1698 0.1695 0.4082 -0.0077 -0.0072 -0.0837 158 LYS   B O   
6393 C CB  . LYS   B 158 ? 0.1911 0.2293 0.3896 0.0041  0.0151  -0.1019 158 LYS   B CB  
6394 C CG  . LYS   B 158 ? 0.2254 0.2733 0.3946 0.0099  0.0249  -0.1114 158 LYS   B CG  
6395 C CD  . LYS   B 158 ? 0.2503 0.3178 0.4058 0.0064  0.0293  -0.1067 158 LYS   B CD  
6396 C CE  . LYS   B 158 ? 0.2701 0.3507 0.4177 0.0079  0.0274  -0.1039 158 LYS   B CE  
6397 N NZ  . LYS   B 158 ? 0.2696 0.3659 0.4173 0.0060  0.0256  -0.1027 158 LYS   B NZ  
6411 N N   . ASN   B 159 ? 0.1701 0.1646 0.4142 0.0023  -0.0175 -0.0629 159 ASN   B N   
6412 C CA  . ASN   B 159 ? 0.1844 0.1583 0.4326 0.0162  -0.0294 -0.0493 159 ASN   B CA  
6413 C C   . ASN   B 159 ? 0.1669 0.1486 0.4188 0.0079  -0.0434 -0.0385 159 ASN   B C   
6414 O O   . ASN   B 159 ? 0.1681 0.1415 0.4383 -0.0042 -0.0495 -0.0302 159 ASN   B O   
6415 C CB  . ASN   B 159 ? 0.2042 0.1718 0.4615 0.0253  -0.0359 -0.0420 159 ASN   B CB  
6416 C CG  . ASN   B 159 ? 0.2323 0.1961 0.4903 0.0292  -0.0473 -0.0566 159 ASN   B CG  
6417 O OD1 . ASN   B 159 ? 0.2463 0.2072 0.4944 0.0356  -0.0523 -0.0643 159 ASN   B OD1 
6418 N ND2 . ASN   B 159 ? 0.2360 0.2076 0.5053 0.0349  -0.0511 -0.0533 159 ASN   B ND2 
6425 N N   . LEU   B 160 ? 0.1526 0.1452 0.3913 0.0042  -0.0468 -0.0336 160 LEU   B N   
6426 C CA  . LEU   B 160 ? 0.1499 0.1464 0.3616 0.0093  -0.0366 -0.0161 160 LEU   B CA  
6427 C C   . LEU   B 160 ? 0.1492 0.1350 0.3538 -0.0004 -0.0282 -0.0230 160 LEU   B C   
6428 O O   . LEU   B 160 ? 0.1396 0.1404 0.3456 -0.0022 -0.0294 -0.0175 160 LEU   B O   
6429 C CB  . LEU   B 160 ? 0.1537 0.1545 0.3453 0.0084  -0.0329 -0.0136 160 LEU   B CB  
6430 C CG  . LEU   B 160 ? 0.1476 0.1726 0.3241 0.0049  -0.0333 -0.0016 160 LEU   B CG  
6431 C CD1 . LEU   B 160 ? 0.1631 0.1903 0.3176 -0.0022 -0.0142 -0.0020 160 LEU   B CD1 
6432 C CD2 . LEU   B 160 ? 0.1519 0.1833 0.3215 0.0183  -0.0294 -0.0132 160 LEU   B CD2 
6444 N N   . TYR   B 161 ? 0.1449 0.1438 0.3480 -0.0043 -0.0053 -0.0354 161 TYR   B N   
6445 C CA  . TYR   B 161 ? 0.1556 0.1416 0.3314 -0.0150 0.0100  -0.0430 161 TYR   B CA  
6446 C C   . TYR   B 161 ? 0.1615 0.1409 0.3289 -0.0105 0.0103  -0.0375 161 TYR   B C   
6447 O O   . TYR   B 161 ? 0.1656 0.1387 0.3229 -0.0146 -0.0025 -0.0363 161 TYR   B O   
6448 C CB  . TYR   B 161 ? 0.1714 0.1549 0.3236 -0.0224 0.0268  -0.0495 161 TYR   B CB  
6449 C CG  . TYR   B 161 ? 0.1948 0.1596 0.3175 -0.0330 0.0313  -0.0598 161 TYR   B CG  
6450 C CD1 . TYR   B 161 ? 0.2018 0.1600 0.3223 -0.0445 0.0343  -0.0565 161 TYR   B CD1 
6451 C CD2 . TYR   B 161 ? 0.2135 0.1657 0.3102 -0.0322 0.0264  -0.0623 161 TYR   B CD2 
6452 C CE1 . TYR   B 161 ? 0.2224 0.1771 0.3220 -0.0443 0.0390  -0.0562 161 TYR   B CE1 
6453 C CE2 . TYR   B 161 ? 0.2351 0.1844 0.3172 -0.0380 0.0293  -0.0626 161 TYR   B CE2 
6454 C CZ  . TYR   B 161 ? 0.2364 0.1898 0.3224 -0.0532 0.0286  -0.0526 161 TYR   B CZ  
6455 O OH  . TYR   B 161 ? 0.2650 0.2137 0.3402 -0.0543 0.0295  -0.0454 161 TYR   B OH  
6465 N N   . ASP   B 162 ? 0.1665 0.1389 0.3438 -0.0106 -0.0013 -0.0480 162 ASP   B N   
6466 C CA  . ASP   B 162 ? 0.1751 0.1463 0.3485 -0.0059 -0.0072 -0.0488 162 ASP   B CA  
6467 C C   . ASP   B 162 ? 0.1704 0.1414 0.3348 -0.0102 -0.0114 -0.0399 162 ASP   B C   
6468 O O   . ASP   B 162 ? 0.1759 0.1497 0.3366 -0.0213 -0.0233 -0.0313 162 ASP   B O   
6469 C CB  . ASP   B 162 ? 0.1912 0.1623 0.3691 -0.0015 -0.0106 -0.0691 162 ASP   B CB  
6470 C CG  . ASP   B 162 ? 0.1962 0.1943 0.3922 0.0100  -0.0078 -0.0801 162 ASP   B CG  
6471 O OD1 . ASP   B 162 ? 0.1962 0.2149 0.3825 0.0008  0.0047  -0.0750 162 ASP   B OD1 
6472 O OD2 . ASP   B 162 ? 0.2064 0.2152 0.4239 0.0226  -0.0016 -0.0812 162 ASP   B OD2 
6477 N N   A LYS   B 163 ? 0.1659 0.1226 0.3330 -0.0115 -0.0246 -0.0253 163 LYS   B N   
6478 N N   B LYS   B 163 ? 0.1750 0.1495 0.3268 -0.0110 -0.0169 -0.0251 163 LYS   B N   
6479 C CA  A LYS   B 163 ? 0.1723 0.1304 0.3308 -0.0219 -0.0279 -0.0067 163 LYS   B CA  
6480 C CA  B LYS   B 163 ? 0.1823 0.1649 0.3233 -0.0139 -0.0183 -0.0112 163 LYS   B CA  
6481 C C   A LYS   B 163 ? 0.1466 0.1305 0.3238 -0.0232 -0.0244 0.0006  163 LYS   B C   
6482 C C   B LYS   B 163 ? 0.1587 0.1482 0.3109 -0.0164 -0.0193 -0.0054 163 LYS   B C   
6483 O O   A LYS   B 163 ? 0.1429 0.1421 0.3479 -0.0242 -0.0211 -0.0003 163 LYS   B O   
6484 O O   B LYS   B 163 ? 0.1578 0.1532 0.3159 -0.0169 -0.0180 -0.0027 163 LYS   B O   
6485 C CB  A LYS   B 163 ? 0.2152 0.1542 0.3531 -0.0164 -0.0297 0.0060  163 LYS   B CB  
6486 C CB  B LYS   B 163 ? 0.2142 0.1992 0.3435 -0.0117 -0.0186 -0.0038 163 LYS   B CB  
6487 C CG  A LYS   B 163 ? 0.2818 0.2159 0.3912 -0.0198 -0.0157 0.0104  163 LYS   B CG  
6488 C CG  B LYS   B 163 ? 0.2506 0.2381 0.3714 -0.0122 -0.0140 0.0004  163 LYS   B CG  
6489 C CD  A LYS   B 163 ? 0.3387 0.2612 0.4324 -0.0297 -0.0090 -0.0019 163 LYS   B CD  
6490 C CD  B LYS   B 163 ? 0.2822 0.2721 0.4034 -0.0149 -0.0113 -0.0014 163 LYS   B CD  
6491 C CE  A LYS   B 163 ? 0.3800 0.2952 0.4578 -0.0359 -0.0019 -0.0068 163 LYS   B CE  
6492 C CE  B LYS   B 163 ? 0.3052 0.2961 0.4278 -0.0170 -0.0079 -0.0022 163 LYS   B CE  
6493 N NZ  A LYS   B 163 ? 0.4027 0.3135 0.4784 -0.0385 0.0006  -0.0128 163 LYS   B NZ  
6494 N NZ  B LYS   B 163 ? 0.3162 0.3058 0.4449 -0.0177 -0.0069 -0.0037 163 LYS   B NZ  
6521 N N   . LEU   B 164 ? 0.1398 0.1276 0.3037 -0.0177 -0.0220 -0.0085 164 LEU   B N   
6522 C CA  . LEU   B 164 ? 0.1420 0.1284 0.2905 -0.0071 -0.0251 -0.0002 164 LEU   B CA  
6523 C C   . LEU   B 164 ? 0.1482 0.1289 0.2874 -0.0123 -0.0331 -0.0000 164 LEU   B C   
6524 O O   . LEU   B 164 ? 0.1496 0.1526 0.3067 -0.0123 -0.0332 -0.0038 164 LEU   B O   
6525 C CB  . LEU   B 164 ? 0.1380 0.1255 0.2728 -0.0121 -0.0270 -0.0029 164 LEU   B CB  
6526 C CG  . LEU   B 164 ? 0.1492 0.1430 0.2869 -0.0102 -0.0147 0.0060  164 LEU   B CG  
6527 C CD1 . LEU   B 164 ? 0.1514 0.1399 0.2835 -0.0110 -0.0200 -0.0080 164 LEU   B CD1 
6528 C CD2 . LEU   B 164 ? 0.1622 0.1788 0.3093 -0.0116 0.0000  0.0008  164 LEU   B CD2 
6541 N N   . VAL   B 165 ? 0.1838 0.1426 0.3062 -0.0193 -0.0383 -0.0009 165 VAL   B N   
6542 C CA  . VAL   B 165 ? 0.2195 0.1536 0.3081 -0.0287 -0.0548 -0.0032 165 VAL   B CA  
6543 C C   . VAL   B 165 ? 0.2426 0.1605 0.3356 -0.0405 -0.0840 -0.0053 165 VAL   B C   
6544 O O   . VAL   B 165 ? 0.2617 0.1745 0.3486 -0.0408 -0.0878 -0.0005 165 VAL   B O   
6545 C CB  . VAL   B 165 ? 0.2395 0.1710 0.3052 -0.0127 -0.0296 -0.0157 165 VAL   B CB  
6546 C CG1 . VAL   B 165 ? 0.2527 0.1804 0.3263 -0.0211 -0.0156 -0.0109 165 VAL   B CG1 
6547 C CG2 . VAL   B 165 ? 0.2359 0.1747 0.2954 -0.0076 -0.0221 -0.0174 165 VAL   B CG2 
6557 N N   . SER   B 166 ? 0.2483 0.1512 0.3632 -0.0430 -0.0856 -0.0290 166 SER   B N   
6558 C CA  . SER   B 166 ? 0.2408 0.1508 0.4052 -0.0346 -0.0716 -0.0344 166 SER   B CA  
6559 C C   . SER   B 166 ? 0.2262 0.1584 0.4159 -0.0369 -0.0713 -0.0109 166 SER   B C   
6560 O O   . SER   B 166 ? 0.2303 0.1805 0.4335 -0.0481 -0.0817 -0.0347 166 SER   B O   
6561 C CB  . SER   B 166 ? 0.2433 0.1628 0.4291 -0.0265 -0.0620 -0.0433 166 SER   B CB  
6562 O OG  . SER   B 166 ? 0.2322 0.1642 0.4474 -0.0237 -0.0635 -0.0229 166 SER   B OG  
6568 N N   . SER   B 167 ? 0.2064 0.1517 0.3979 -0.0410 -0.0736 0.0244  167 SER   B N   
6569 C CA  . SER   B 167 ? 0.2002 0.1637 0.3841 -0.0335 -0.0529 0.0222  167 SER   B CA  
6570 C C   . SER   B 167 ? 0.1962 0.1701 0.3671 -0.0478 -0.0482 0.0386  167 SER   B C   
6571 O O   . SER   B 167 ? 0.1972 0.1842 0.3652 -0.0498 -0.0445 0.0336  167 SER   B O   
6572 C CB  . SER   B 167 ? 0.1901 0.1734 0.3810 -0.0300 -0.0286 0.0214  167 SER   B CB  
6573 O OG  . SER   B 167 ? 0.1839 0.1831 0.3673 -0.0248 -0.0174 0.0263  167 SER   B OG  
6579 N N   . PHE   B 168 ? 0.1990 0.1695 0.3541 -0.0405 -0.0352 0.0505  168 PHE   B N   
6580 C CA  . PHE   B 168 ? 0.2010 0.1670 0.3284 -0.0428 -0.0316 0.0295  168 PHE   B CA  
6581 C C   . PHE   B 168 ? 0.1723 0.1572 0.2888 -0.0258 -0.0182 0.0125  168 PHE   B C   
6582 O O   . PHE   B 168 ? 0.2055 0.1518 0.2982 0.0003  -0.0128 0.0011  168 PHE   B O   
6583 C CB  . PHE   B 168 ? 0.2166 0.1689 0.3294 -0.0539 -0.0434 0.0405  168 PHE   B CB  
6584 C CG  . PHE   B 168 ? 0.2415 0.1542 0.3213 -0.0590 -0.0475 0.0137  168 PHE   B CG  
6585 C CD1 . PHE   B 168 ? 0.2710 0.1600 0.3289 -0.0501 -0.0488 0.0105  168 PHE   B CD1 
6586 C CD2 . PHE   B 168 ? 0.2297 0.1500 0.3173 -0.0544 -0.0440 0.0221  168 PHE   B CD2 
6587 C CE1 . PHE   B 168 ? 0.2841 0.1723 0.3223 -0.0360 -0.0382 0.0197  168 PHE   B CE1 
6588 C CE2 . PHE   B 168 ? 0.2573 0.1619 0.3184 -0.0394 -0.0500 0.0146  168 PHE   B CE2 
6589 C CZ  . PHE   B 168 ? 0.2725 0.1586 0.3183 -0.0265 -0.0488 0.0256  168 PHE   B CZ  
6599 N N   . LEU   B 169 ? 0.1737 0.1677 0.2822 -0.0015 -0.0079 -0.0007 169 LEU   B N   
6600 C CA  . LEU   B 169 ? 0.1933 0.2012 0.3063 -0.0075 -0.0001 -0.0236 169 LEU   B CA  
6601 C C   . LEU   B 169 ? 0.2205 0.2248 0.3485 0.0058  0.0029  -0.0484 169 LEU   B C   
6602 O O   . LEU   B 169 ? 0.2429 0.2439 0.3956 0.0055  -0.0004 -0.0669 169 LEU   B O   
6603 C CB  . LEU   B 169 ? 0.2116 0.2411 0.3108 -0.0156 -0.0042 -0.0009 169 LEU   B CB  
6604 C CG  . LEU   B 169 ? 0.2497 0.2779 0.3378 -0.0026 0.0016  0.0083  169 LEU   B CG  
6605 C CD1 . LEU   B 169 ? 0.2655 0.2966 0.3403 -0.0028 -0.0007 0.0236  169 LEU   B CD1 
6606 C CD2 . LEU   B 169 ? 0.2406 0.2827 0.3326 0.0164  0.0218  -0.0063 169 LEU   B CD2 
6607 O OXT . LEU   B 169 ? 0.2427 0.2391 0.3456 0.0254  0.0116  -0.0551 169 LEU   B OXT 
6619 C C1  T TFA   C .   ? 0.1416 0.1711 0.1483 -0.0060 0.0158  0.0187  201 TFA   A C1  
6620 C C2  T TFA   C .   ? 0.1696 0.2054 0.1898 -0.0210 0.0103  0.0098  201 TFA   A C2  
6621 O O   T TFA   C .   ? 0.1135 0.1437 0.1428 -0.0062 0.0199  0.0336  201 TFA   A O   
6622 F F1  T TFA   C .   ? 0.1824 0.2149 0.2181 -0.0230 0.0001  0.0015  201 TFA   A F1  
6623 F F2  T TFA   C .   ? 0.1839 0.2159 0.1903 -0.0220 0.0136  0.0207  201 TFA   A F2  
6624 F F3  T TFA   C .   ? 0.1846 0.2194 0.2207 -0.0362 0.0212  -0.0020 201 TFA   A F3  
6625 O OXT T TFA   C .   ? 0.1451 0.1663 0.1636 0.0205  0.0152  0.0142  201 TFA   A OXT 
6626 N N2  B A1A9N D .   ? 0.2199 0.2657 0.2399 -0.0156 -0.0021 -0.0100 202 A1A9N A N2  
6627 C C3  B A1A9N D .   ? 0.2493 0.3009 0.2708 -0.0311 -0.0014 -0.0343 202 A1A9N A C3  
6628 C C6  B A1A9N D .   ? 0.1963 0.2510 0.2188 -0.0092 -0.0028 0.0097  202 A1A9N A C6  
6629 C C9  B A1A9N D .   ? 0.1806 0.2436 0.2060 -0.0164 0.0018  0.0187  202 A1A9N A C9  
6630 C C12 B A1A9N D .   ? 0.2593 0.3151 0.2994 -0.0321 0.0073  -0.0407 202 A1A9N A C12 
6631 C C1  B A1A9N D .   ? 0.2473 0.3054 0.2476 -0.0393 -0.0154 -0.0461 202 A1A9N A C1  
6632 C C10 B A1A9N D .   ? 0.2579 0.3125 0.2923 -0.0316 0.0076  -0.0394 202 A1A9N A C10 
6633 C C11 B A1A9N D .   ? 0.2613 0.3161 0.2978 -0.0308 0.0090  -0.0410 202 A1A9N A C11 
6634 C C2  B A1A9N D .   ? 0.2480 0.3035 0.2587 -0.0358 -0.0092 -0.0414 202 A1A9N A C2  
6635 C C4  B A1A9N D .   ? 0.2204 0.2705 0.2414 -0.0177 0.0003  -0.0092 202 A1A9N A C4  
6636 C C5  B A1A9N D .   ? 0.2147 0.2618 0.2351 -0.0134 -0.0027 0.0003  202 A1A9N A C5  
6637 C C7  B A1A9N D .   ? 0.2038 0.2580 0.2240 -0.0131 0.0033  0.0031  202 A1A9N A C7  
6638 C C8  B A1A9N D .   ? 0.1956 0.2526 0.2140 -0.0156 0.0095  0.0090  202 A1A9N A C8  
6639 N N1  B A1A9N D .   ? 0.2372 0.2857 0.2598 -0.0251 0.0005  -0.0198 202 A1A9N A N1  
6640 N N3  B A1A9N D .   ? 0.2070 0.2565 0.2272 -0.0101 -0.0054 0.0085  202 A1A9N A N3  
6641 N N4  B A1A9N D .   ? 0.1799 0.2399 0.1999 -0.0090 -0.0023 0.0213  202 A1A9N A N4  
6642 O O1  B A1A9N D .   ? 0.2593 0.3147 0.2948 -0.0321 0.0122  -0.0441 202 A1A9N A O1  
6661 O O   . HOH   E .   ? 0.4140 0.8104 0.4990 -0.1138 0.0683  0.1003  301 HOH   A O   
6662 O O   A HOH   E .   ? 0.2347 0.2369 0.3470 -0.0194 -0.0307 0.0439  302 HOH   A O   
6663 O O   . HOH   E .   ? 0.6068 0.4960 0.3343 0.2052  -0.1408 0.0601  303 HOH   A O   
6664 O O   . HOH   E .   ? 0.2877 0.6023 0.5769 -0.0463 -0.0761 0.1895  304 HOH   A O   
6665 O O   . HOH   E .   ? 0.6827 0.6255 0.4652 -0.1252 -0.0324 0.2571  305 HOH   A O   
6666 O O   . HOH   E .   ? 0.4771 0.2692 0.3032 -0.1267 0.0411  0.0206  306 HOH   A O   
6667 O O   B HOH   E .   ? 0.4769 0.4209 0.3574 0.1196  -0.0397 0.0126  307 HOH   A O   
6668 O O   . HOH   E .   ? 0.4563 0.3467 0.4463 -0.0403 0.1295  -0.0251 308 HOH   A O   
6669 O O   . HOH   E .   ? 0.3164 0.3273 0.2703 -0.1150 0.0107  0.0771  309 HOH   A O   
6670 O O   . HOH   E .   ? 0.2870 0.2619 0.4044 -0.0347 -0.1087 0.1046  310 HOH   A O   
6671 O O   . HOH   E .   ? 0.6008 0.3533 0.5091 -0.0869 0.1710  0.0570  311 HOH   A O   
6672 O O   . HOH   E .   ? 0.2537 0.5798 0.6076 0.0800  0.0670  0.0685  312 HOH   A O   
6673 O O   . HOH   E .   ? 0.2923 0.3131 0.1829 -0.0381 0.0491  0.0382  313 HOH   A O   
6674 O O   . HOH   E .   ? 0.3534 0.3200 0.3971 -0.0703 0.1509  0.0163  314 HOH   A O   
6675 O O   . HOH   E .   ? 0.2136 0.1757 0.3763 -0.0392 0.0090  -0.0157 315 HOH   A O   
6676 O O   . HOH   E .   ? 0.5333 0.6630 0.4959 -0.1246 -0.1188 -0.1067 316 HOH   A O   
6677 O O   . HOH   E .   ? 0.1792 0.2909 0.3074 0.0302  -0.0121 -0.0297 317 HOH   A O   
6678 O O   . HOH   E .   ? 0.4550 0.3932 0.5197 0.0924  0.1456  -0.1500 318 HOH   A O   
6679 O O   . HOH   E .   ? 0.5063 0.4854 0.4095 -0.0638 0.1009  0.1719  319 HOH   A O   
6680 O O   . HOH   E .   ? 0.5048 0.2063 0.4997 0.0659  -0.0030 0.0136  320 HOH   A O   
6681 O O   B HOH   E .   ? 0.1806 0.2699 0.2746 0.0105  -0.1228 -0.0459 321 HOH   A O   
6682 O O   . HOH   E .   ? 0.4549 0.4903 0.5888 0.1541  0.1583  -0.0772 322 HOH   A O   
6683 O O   . HOH   E .   ? 0.1910 0.3255 0.4282 -0.0234 0.0393  -0.1121 323 HOH   A O   
6684 O O   . HOH   E .   ? 0.6556 0.5294 0.3691 -0.0274 -0.0083 0.1223  324 HOH   A O   
6685 O O   A HOH   E .   ? 0.1337 0.1970 0.2016 0.0299  0.0347  0.0332  325 HOH   A O   
6686 O O   . HOH   E .   ? 0.5692 0.3388 0.3064 -0.0870 -0.0905 0.0120  326 HOH   A O   
6687 O O   . HOH   E .   ? 0.8156 0.3023 0.5505 -0.0471 -0.1401 0.1158  327 HOH   A O   
6688 O O   . HOH   E .   ? 0.1544 0.1454 0.2445 -0.0234 0.0051  0.0119  328 HOH   A O   
6689 O O   . HOH   E .   ? 0.3437 0.4539 0.2335 -0.0154 0.0566  0.0328  329 HOH   A O   
6690 O O   . HOH   E .   ? 0.2179 0.1669 0.2581 -0.0084 -0.0563 -0.0016 330 HOH   A O   
6691 O O   . HOH   E .   ? 0.1885 0.1626 0.1651 -0.0094 0.0122  0.0168  331 HOH   A O   
6692 O O   . HOH   E .   ? 0.6961 0.5128 0.4660 -0.1284 -0.0261 0.2387  332 HOH   A O   
6693 O O   . HOH   E .   ? 0.5591 0.4760 0.5128 0.0605  0.2616  -0.0603 333 HOH   A O   
6694 O O   . HOH   E .   ? 0.4814 0.1957 0.4721 0.0091  -0.1785 0.0632  334 HOH   A O   
6695 O O   . HOH   E .   ? 0.2462 0.2289 0.3041 0.0381  0.0290  0.0452  335 HOH   A O   
6696 O O   . HOH   E .   ? 0.2085 0.4812 0.3876 0.0045  -0.0501 0.1604  336 HOH   A O   
6697 O O   . HOH   E .   ? 0.1754 0.1670 0.2260 0.0123  -0.0296 0.0266  337 HOH   A O   
6698 O O   . HOH   E .   ? 0.1545 0.1868 0.2943 0.0138  -0.0436 -0.0729 338 HOH   A O   
6699 O O   . HOH   E .   ? 0.5793 0.4047 0.6423 0.0149  -0.0697 0.0066  339 HOH   A O   
6700 O O   . HOH   E .   ? 0.2249 0.3888 0.3691 0.0739  -0.0580 -0.0120 340 HOH   A O   
6701 O O   . HOH   E .   ? 0.4903 0.5322 0.2641 -0.1312 0.1093  0.0885  341 HOH   A O   
6702 O O   . HOH   E .   ? 0.1520 0.4208 0.2463 -0.0017 0.0263  0.0746  342 HOH   A O   
6703 O O   . HOH   E .   ? 0.2836 0.3841 0.3657 -0.1002 -0.0587 -0.0156 343 HOH   A O   
6704 O O   . HOH   E .   ? 0.2520 0.2124 0.2512 -0.0289 -0.0024 0.0002  344 HOH   A O   
6705 O O   . HOH   E .   ? 0.5294 0.5121 0.4188 -0.0694 -0.0734 -0.1066 345 HOH   A O   
6706 O O   . HOH   E .   ? 0.1707 0.2636 0.2922 -0.0182 0.0519  0.0597  346 HOH   A O   
6707 O O   . HOH   E .   ? 0.5339 0.4446 0.3959 -0.1980 -0.0875 0.2021  347 HOH   A O   
6708 O O   A HOH   E .   ? 0.2073 0.2896 0.3791 -0.0068 0.0844  0.1518  348 HOH   A O   
6709 O O   . HOH   E .   ? 0.3233 0.2855 0.3678 -0.0944 -0.0032 -0.0150 349 HOH   A O   
6710 O O   . HOH   E .   ? 0.2104 0.1658 0.2561 0.0261  -0.0353 -0.0067 350 HOH   A O   
6711 O O   . HOH   E .   ? 0.1963 0.2019 0.3748 0.0203  0.0989  -0.0074 351 HOH   A O   
6712 O O   . HOH   E .   ? 0.3674 0.4082 0.3864 0.1785  0.0796  0.0576  352 HOH   A O   
6713 O O   A HOH   E .   ? 0.2066 0.2331 0.2337 -0.0388 0.0318  0.0479  353 HOH   A O   
6714 O O   A HOH   E .   ? 0.1783 0.2147 0.2404 0.0222  0.0207  0.0160  354 HOH   A O   
6715 O O   . HOH   E .   ? 0.1460 0.2227 0.2286 -0.0022 -0.0143 0.0582  355 HOH   A O   
6716 O O   A HOH   E .   ? 0.2996 0.1493 0.2008 0.0249  0.0066  0.0058  356 HOH   A O   
6717 O O   . HOH   E .   ? 0.2758 0.5659 0.3892 0.0054  -0.0607 0.0810  357 HOH   A O   
6718 O O   . HOH   E .   ? 0.1311 0.1245 0.1490 -0.0015 0.0088  0.0085  358 HOH   A O   
6719 O O   . HOH   E .   ? 0.3242 0.3267 0.4773 -0.0858 -0.1032 -0.0895 359 HOH   A O   
6720 O O   . HOH   E .   ? 0.1744 0.2180 0.1808 -0.0142 0.0024  0.0535  360 HOH   A O   
6721 O O   . HOH   E .   ? 0.5604 0.3650 0.3405 -0.0190 -0.0278 0.1266  361 HOH   A O   
6722 O O   . HOH   E .   ? 0.1508 0.1901 0.2685 0.0029  -0.0127 0.0079  362 HOH   A O   
6723 O O   . HOH   E .   ? 0.1578 0.1334 0.2409 -0.0101 0.0171  -0.0134 363 HOH   A O   
6724 O O   . HOH   E .   ? 0.2592 0.4029 0.3343 -0.0430 0.0661  0.0103  364 HOH   A O   
6725 O O   . HOH   E .   ? 0.1676 0.1735 0.2389 -0.0257 0.0085  0.0370  365 HOH   A O   
6726 O O   . HOH   E .   ? 0.3571 0.6967 0.4674 -0.0446 -0.1466 0.0531  366 HOH   A O   
6727 O O   . HOH   E .   ? 0.4506 0.2554 0.4335 -0.1529 0.1672  -0.0560 367 HOH   A O   
6728 O O   . HOH   E .   ? 0.2699 0.4345 0.3000 0.0658  0.0840  0.1757  368 HOH   A O   
6729 O O   . HOH   E .   ? 0.1393 0.1510 0.1712 -0.0065 -0.0128 -0.0036 369 HOH   A O   
6730 O O   . HOH   E .   ? 0.2855 0.3491 0.2516 -0.0854 -0.0051 -0.0726 370 HOH   A O   
6731 O O   . HOH   E .   ? 0.1927 0.1850 0.2739 -0.0346 0.0060  0.0398  371 HOH   A O   
6732 O O   . HOH   E .   ? 0.3853 0.2397 0.4605 -0.1177 0.0695  0.0271  372 HOH   A O   
6733 O O   . HOH   E .   ? 0.2039 0.2270 0.2321 -0.0377 -0.0497 0.0463  373 HOH   A O   
6734 O O   . HOH   E .   ? 0.1980 0.2495 0.3580 0.0268  0.0817  -0.0565 374 HOH   A O   
6735 O O   . HOH   E .   ? 0.3804 0.2059 0.2541 0.1067  0.0520  0.0231  375 HOH   A O   
6736 O O   . HOH   E .   ? 0.3000 0.2865 0.2302 0.0262  0.0796  0.0177  376 HOH   A O   
6737 O O   . HOH   E .   ? 0.3272 0.2656 0.3214 -0.0298 -0.0508 0.0910  377 HOH   A O   
6738 O O   . HOH   E .   ? 0.3227 0.2370 0.4936 -0.0652 -0.0255 0.0097  378 HOH   A O   
6739 O O   . HOH   E .   ? 0.2432 0.1767 0.2662 -0.0085 0.0076  0.0222  379 HOH   A O   
6740 O O   . HOH   E .   ? 0.3062 0.3619 0.3423 -0.1412 0.0742  -0.0188 380 HOH   A O   
6741 O O   . HOH   E .   ? 0.2415 0.3992 0.3225 -0.0642 -0.0149 0.0883  381 HOH   A O   
6742 O O   B HOH   E .   ? 0.3007 0.2924 0.2453 0.0202  -0.0327 -0.0114 382 HOH   A O   
6743 O O   . HOH   E .   ? 0.3885 0.5129 0.5528 0.0806  -0.0424 0.1496  383 HOH   A O   
6744 O O   . HOH   E .   ? 0.1947 0.1882 0.1872 0.0050  0.0132  0.0154  384 HOH   A O   
6745 O O   T HOH   E .   ? 0.1125 0.1174 0.2511 -0.0118 0.0178  0.0456  385 HOH   A O   
6746 O O   . HOH   E .   ? 0.5665 0.5107 0.6287 -0.0863 0.0331  0.1255  386 HOH   A O   
6747 O O   . HOH   E .   ? 0.2603 0.2009 0.1901 -0.0611 0.0133  0.0295  387 HOH   A O   
6748 O O   A HOH   E .   ? 0.2633 0.2089 0.1889 0.0423  0.0499  0.0155  388 HOH   A O   
6749 O O   . HOH   E .   ? 0.2876 0.6447 0.3374 0.1177  0.0197  -0.0970 389 HOH   A O   
6750 O O   . HOH   E .   ? 0.1767 0.1871 0.4024 0.0312  0.0937  0.0924  390 HOH   A O   
6751 O O   . HOH   E .   ? 0.3794 0.6189 0.3966 -0.0968 -0.0177 0.1218  391 HOH   A O   
6752 O O   . HOH   E .   ? 0.2487 0.3889 0.3801 -0.0375 0.0943  -0.0849 392 HOH   A O   
6753 O O   . HOH   E .   ? 0.1408 0.1683 0.1912 0.0088  -0.0307 -0.0284 393 HOH   A O   
6754 O O   . HOH   E .   ? 0.3092 0.2698 0.2294 -0.0667 -0.0806 0.0315  394 HOH   A O   
6755 O O   . HOH   E .   ? 0.2752 0.3444 0.3105 -0.0427 0.0957  -0.0410 395 HOH   A O   
6756 O O   . HOH   E .   ? 0.2819 0.2651 0.3138 0.0025  -0.0422 -0.0727 396 HOH   A O   
6757 O O   . HOH   E .   ? 0.2082 0.2050 0.3393 -0.0017 -0.0521 0.0432  397 HOH   A O   
6758 O O   . HOH   E .   ? 0.1948 0.2169 0.2809 -0.0173 -0.0238 0.0797  398 HOH   A O   
6759 O O   . HOH   E .   ? 0.2998 0.3797 0.4217 -0.0559 0.1443  0.0199  399 HOH   A O   
6760 O O   . HOH   E .   ? 0.2167 0.1638 0.2971 -0.0023 -0.0330 0.0061  400 HOH   A O   
6761 O O   A HOH   E .   ? 0.1747 0.1729 0.2901 -0.0129 0.0377  0.0011  401 HOH   A O   
6762 O O   . HOH   E .   ? 0.1305 0.1418 0.2000 -0.0033 -0.0195 0.0108  402 HOH   A O   
6763 O O   . HOH   E .   ? 0.5588 0.2645 0.4958 0.0761  -0.0165 -0.0279 403 HOH   A O   
6764 O O   . HOH   E .   ? 0.4827 0.5063 0.2138 0.0129  0.0966  0.1122  404 HOH   A O   
6765 O O   B HOH   E .   ? 0.1386 0.0764 0.1110 -0.0367 -0.0145 0.0014  405 HOH   A O   
6766 O O   . HOH   E .   ? 0.3393 0.3203 0.2222 -0.0240 -0.0811 0.0352  406 HOH   A O   
6767 O O   . HOH   E .   ? 0.3111 0.3764 0.6681 -0.0076 0.0985  -0.0268 407 HOH   A O   
6768 O O   . HOH   E .   ? 0.1675 0.1330 0.1799 -0.0248 0.0110  -0.0003 408 HOH   A O   
6769 O O   . HOH   E .   ? 0.1529 0.1681 0.3146 -0.0101 0.0006  0.0186  409 HOH   A O   
6770 O O   . HOH   E .   ? 0.4420 0.2187 0.5192 -0.0904 -0.2166 0.0983  410 HOH   A O   
6771 O O   . HOH   E .   ? 0.2482 0.2132 0.2636 -0.0624 -0.0036 0.0555  411 HOH   A O   
6772 O O   . HOH   E .   ? 0.2036 0.2991 0.2587 -0.0138 -0.0524 0.0549  412 HOH   A O   
6773 O O   . HOH   E .   ? 0.1859 0.2532 0.3819 -0.0031 -0.0205 0.0268  413 HOH   A O   
6774 O O   . HOH   E .   ? 0.2626 0.6354 0.1904 -0.0452 0.0399  -0.0014 414 HOH   A O   
6775 O O   . HOH   E .   ? 0.3350 0.1312 0.2181 0.0059  -0.0494 0.0098  415 HOH   A O   
6776 O O   . HOH   E .   ? 0.3921 0.4408 0.3480 0.1645  -0.0699 -0.1620 416 HOH   A O   
6777 O O   . HOH   E .   ? 0.2100 0.2340 0.4270 0.0142  -0.0532 -0.0537 417 HOH   A O   
6778 O O   . HOH   E .   ? 0.4458 0.5827 0.3386 -0.0653 0.0065  0.1252  418 HOH   A O   
6779 O O   A HOH   E .   ? 0.1533 0.1417 0.1776 0.0041  -0.0147 0.0118  419 HOH   A O   
6780 O O   . HOH   E .   ? 0.2285 0.4142 0.2659 0.1522  -0.0122 0.0138  420 HOH   A O   
6781 O O   . HOH   E .   ? 0.4915 0.4659 0.3630 0.2196  0.0076  -0.0873 421 HOH   A O   
6782 O O   . HOH   E .   ? 0.6196 0.6166 0.6579 -0.1273 -0.0631 -0.0983 422 HOH   A O   
6783 O O   . HOH   E .   ? 0.6266 0.5975 0.4085 0.2142  -0.0507 -0.0213 423 HOH   A O   
6784 O O   . HOH   E .   ? 0.6571 0.3707 0.5286 0.1838  -0.0840 0.1471  424 HOH   A O   
6785 O O   . HOH   E .   ? 0.1644 0.2032 0.2825 -0.0167 0.0022  0.0362  425 HOH   A O   
6786 O O   . HOH   E .   ? 0.5879 0.5497 0.5484 0.0295  0.1122  0.0453  426 HOH   A O   
6787 O O   . HOH   E .   ? 0.3650 0.6655 0.5362 0.1569  0.0481  0.0645  427 HOH   A O   
6788 O O   . HOH   E .   ? 0.5637 0.5892 0.5611 -0.0461 0.0987  0.0520  428 HOH   A O   
6789 O O   . HOH   E .   ? 0.3210 0.3077 0.2496 -0.0347 -0.0555 0.0330  429 HOH   A O   
6790 O O   . HOH   E .   ? 0.5539 0.7193 0.4253 0.1215  0.2352  -0.0726 430 HOH   A O   
6791 O O   A HOH   E .   ? 0.2036 0.1962 0.2202 0.0054  0.0027  0.0611  431 HOH   A O   
6792 O O   . HOH   E .   ? 0.1884 0.1705 0.2791 0.0228  -0.0444 0.0150  432 HOH   A O   
6793 O O   . HOH   E .   ? 0.6715 0.6517 0.6132 0.0642  -0.1218 0.0073  433 HOH   A O   
6794 O O   . HOH   E .   ? 0.3632 0.2751 0.2003 -0.0949 0.0186  0.0603  434 HOH   A O   
6795 O O   B HOH   E .   ? 0.3696 0.3560 0.3214 -0.0735 0.0437  0.0996  435 HOH   A O   
6796 O O   . HOH   E .   ? 0.5958 0.4949 0.3656 -0.0579 -0.1532 0.0521  436 HOH   A O   
6797 O O   . HOH   E .   ? 0.2545 0.1543 0.2987 0.0057  0.0057  0.0204  437 HOH   A O   
6798 O O   B HOH   E .   ? 0.4862 0.2594 0.3570 -0.0281 0.0916  -0.0094 438 HOH   A O   
6799 O O   . HOH   E .   ? 0.1877 0.2107 0.5140 -0.0303 -0.0848 0.0567  439 HOH   A O   
6800 O O   A HOH   E .   ? 0.1916 0.1633 0.1707 0.0227  -0.0302 -0.0237 440 HOH   A O   
6801 O O   . HOH   E .   ? 0.5181 0.4226 0.5760 0.0994  0.0382  -0.1130 441 HOH   A O   
6802 O O   . HOH   E .   ? 0.5042 0.6339 0.6117 -0.1515 -0.0625 -0.1333 442 HOH   A O   
6803 O O   . HOH   E .   ? 0.4153 0.3396 0.3165 0.2178  -0.0712 -0.0429 443 HOH   A O   
6804 O O   . HOH   E .   ? 0.4665 0.4463 0.4831 -0.1484 -0.0904 -0.1177 444 HOH   A O   
6805 O O   . HOH   E .   ? 0.5889 0.7617 0.4101 0.1748  -0.1036 0.1853  445 HOH   A O   
6806 O O   . HOH   E .   ? 0.2276 0.1881 0.2833 0.0126  0.0202  0.0156  446 HOH   A O   
6807 O O   . HOH   E .   ? 0.2601 0.3797 0.5001 0.0015  0.0720  -0.1741 447 HOH   A O   
6808 O O   A HOH   E .   ? 0.4173 0.1712 0.2818 -0.0813 0.0305  0.0675  448 HOH   A O   
6809 O O   . HOH   E .   ? 0.8872 0.8674 0.6610 -0.0623 -0.0732 -0.0050 449 HOH   A O   
6810 O O   . HOH   E .   ? 0.2238 0.2760 0.2570 0.0036  -0.0179 -0.0454 450 HOH   A O   
6811 O O   . HOH   E .   ? 0.6677 0.5239 0.7660 0.1850  -0.1245 0.1541  451 HOH   A O   
6812 O O   A HOH   E .   ? 0.1813 0.2199 0.1934 0.0308  0.0054  -0.0182 452 HOH   A O   
6813 O O   . HOH   E .   ? 0.6192 0.5706 0.5009 -0.0892 0.1008  0.0726  453 HOH   A O   
6814 O O   . HOH   E .   ? 0.5599 0.3897 0.4241 -0.0186 0.0076  0.1022  454 HOH   A O   
6815 O O   . HOH   E .   ? 0.4040 0.4575 0.4321 0.0773  0.0037  0.0982  455 HOH   A O   
6816 O O   A HOH   E .   ? 0.5339 0.3930 0.4551 0.0139  0.1162  0.2014  456 HOH   A O   
6817 O O   . HOH   E .   ? 0.3853 0.3660 0.4500 0.0129  0.0025  0.0418  457 HOH   A O   
6818 O O   . HOH   E .   ? 0.2922 0.4346 0.3964 0.1307  -0.0216 0.1125  458 HOH   A O   
6819 O O   . HOH   E .   ? 0.2936 0.2719 0.3521 -0.0538 0.0231  -0.0645 459 HOH   A O   
6820 O O   . HOH   E .   ? 0.6631 0.7641 0.4863 0.1176  -0.1068 -0.0038 460 HOH   A O   
6821 O O   . HOH   E .   ? 0.3156 0.5109 0.5237 -0.1561 0.0936  -0.1363 461 HOH   A O   
6822 O O   B HOH   E .   ? 0.1815 0.2156 0.3528 -0.0494 0.0269  0.1188  462 HOH   A O   
6823 O O   . HOH   E .   ? 0.3954 0.4826 0.4982 0.0591  -0.0309 0.1357  463 HOH   A O   
6824 O O   . HOH   E .   ? 0.3332 0.4800 0.3831 -0.0615 0.0010  -0.0197 464 HOH   A O   
6825 O O   . HOH   E .   ? 0.2638 0.2784 0.3578 -0.1054 0.0491  -0.0320 465 HOH   A O   
6826 O O   . HOH   E .   ? 0.2759 0.4436 0.4961 0.0746  -0.0003 -0.1737 466 HOH   A O   
6827 O O   . HOH   E .   ? 0.2884 0.2388 0.6471 0.0519  -0.1514 -0.0627 467 HOH   A O   
6828 O O   . HOH   E .   ? 0.5627 0.3729 0.6872 0.0089  0.0504  0.1979  468 HOH   A O   
6829 O O   . HOH   E .   ? 0.4158 0.6230 0.3684 -0.0875 -0.0719 0.2292  469 HOH   A O   
6830 O O   . HOH   E .   ? 0.3427 0.2363 0.3614 0.0231  0.0600  -0.0089 470 HOH   A O   
6831 O O   . HOH   E .   ? 0.5496 0.4794 0.4540 0.0114  0.0967  0.0415  471 HOH   A O   
6832 O O   . HOH   E .   ? 0.2554 0.1769 0.2662 0.0258  -0.0856 -0.0311 472 HOH   A O   
6833 O O   . HOH   E .   ? 0.7221 0.6309 0.6403 0.1576  0.1755  0.2114  473 HOH   A O   
6834 O O   . HOH   E .   ? 0.4261 0.4814 0.3252 -0.0370 -0.0393 -0.0154 474 HOH   A O   
6835 O O   . HOH   E .   ? 0.4071 0.5331 0.3823 0.0422  -0.0500 -0.0779 475 HOH   A O   
6836 O O   . HOH   E .   ? 0.5146 0.5556 0.4564 0.0929  -0.0759 -0.0697 476 HOH   A O   
6837 O O   . HOH   E .   ? 0.2474 0.2153 0.2575 0.0223  -0.0078 -0.0042 477 HOH   A O   
6838 O O   . HOH   E .   ? 0.4127 0.4659 0.2691 -0.0087 -0.0130 0.0012  478 HOH   A O   
6839 O O   . HOH   E .   ? 0.4684 0.5459 0.5895 -0.1636 -0.1278 -0.0030 479 HOH   A O   
6840 O O   . HOH   E .   ? 0.5913 0.3706 0.4494 -0.0110 0.1410  -0.0321 480 HOH   A O   
6841 O O   . HOH   E .   ? 0.4447 0.4954 0.5633 -0.2032 -0.0527 -0.0391 481 HOH   A O   
6842 O O   . HOH   E .   ? 0.6501 0.5732 0.6678 -0.1037 0.0237  -0.0894 482 HOH   A O   
6843 O O   . HOH   E .   ? 0.2781 0.4545 0.3466 -0.0343 -0.0351 -0.0794 483 HOH   A O   
6844 O O   B HOH   E .   ? 0.3792 0.4418 0.3448 0.0084  0.0624  -0.0212 484 HOH   A O   
6845 O O   . HOH   E .   ? 0.7686 0.3748 0.3326 -0.0518 -0.1255 0.0385  485 HOH   A O   
6846 O O   . HOH   E .   ? 0.5511 0.3837 0.3898 0.0540  0.0204  -0.1147 486 HOH   A O   
6847 O O   . HOH   E .   ? 0.4379 0.2894 0.3417 -0.0902 -0.1459 0.0660  487 HOH   A O   
6848 O O   . HOH   E .   ? 0.5738 0.6190 0.6459 0.1338  0.1759  -0.1027 488 HOH   A O   
6849 O O   . HOH   E .   ? 0.2666 0.5147 0.3691 0.1168  0.1011  0.2387  489 HOH   A O   
6850 O O   . HOH   E .   ? 0.2749 0.3905 0.4907 0.0065  0.1088  0.1085  490 HOH   A O   
6851 O O   . HOH   E .   ? 0.4068 0.3753 0.2694 -0.0902 0.1196  -0.0583 491 HOH   A O   
6852 O O   . HOH   E .   ? 0.5930 0.6210 0.4323 -0.0834 0.1340  0.1278  492 HOH   A O   
6853 O O   . HOH   E .   ? 0.5184 0.5253 0.5413 0.0343  -0.1176 0.0580  493 HOH   A O   
6854 O O   . HOH   E .   ? 0.2460 0.2626 0.6971 -0.0158 -0.1452 0.0371  494 HOH   A O   
6855 O O   . HOH   E .   ? 0.6131 0.4940 0.4700 -0.0884 -0.1190 -0.0701 495 HOH   A O   
6856 O O   B HOH   E .   ? 0.4249 0.3354 0.3407 -0.0821 -0.0335 0.1340  496 HOH   A O   
6857 O O   . HOH   E .   ? 0.4053 0.3340 0.4492 -0.0948 0.0286  0.0924  497 HOH   A O   
6858 O O   . HOH   E .   ? 0.6174 0.2460 0.4375 -0.0638 0.0552  0.0549  498 HOH   A O   
6859 O O   . HOH   E .   ? 0.4480 0.3157 0.5086 -0.0249 0.2424  0.0133  499 HOH   A O   
6860 O O   . HOH   E .   ? 0.3107 0.2008 0.5147 0.0049  -0.0067 0.0777  500 HOH   A O   
6861 O O   . HOH   E .   ? 0.2502 0.3133 0.4640 -0.0076 0.0751  -0.0423 501 HOH   A O   
6862 O O   . HOH   E .   ? 0.4037 0.8369 0.5781 -0.1356 -0.0531 0.1973  502 HOH   A O   
6863 O O   . HOH   E .   ? 0.6291 0.6636 0.4225 0.1401  -0.1357 0.1298  503 HOH   A O   
6864 O O   . HOH   E .   ? 0.2479 0.4016 0.3322 0.0833  -0.0339 0.0700  504 HOH   A O   
6865 O O   . HOH   E .   ? 0.4838 0.2624 0.4221 -0.1438 -0.0166 0.0346  505 HOH   A O   
6866 O O   . HOH   E .   ? 0.2947 0.4091 0.4165 0.0767  -0.0315 -0.0030 506 HOH   A O   
6867 O O   . HOH   E .   ? 0.7215 0.4835 0.5958 0.1696  -0.0620 0.0983  507 HOH   A O   
6868 O O   . HOH   E .   ? 0.5868 0.6872 0.4979 0.1279  -0.0456 0.0212  508 HOH   A O   
6869 O O   B HOH   E .   ? 0.3218 0.3805 0.3870 0.0734  0.0720  -0.0435 509 HOH   A O   
6870 O O   B HOH   E .   ? 0.2867 0.1822 0.2725 0.0520  -0.0728 0.0192  510 HOH   A O   
6871 O O   . HOH   E .   ? 0.3145 0.2486 0.4438 -0.0029 0.0179  0.0939  511 HOH   A O   
6872 O O   . HOH   E .   ? 0.5631 0.6866 0.4371 0.3315  0.0120  0.1445  512 HOH   A O   
6873 O O   T HOH   E .   ? 0.1160 0.1451 0.2303 -0.0217 -0.0128 0.0745  513 HOH   A O   
6874 O O   A HOH   E .   ? 0.3750 0.8932 0.4528 0.1862  0.1210  -0.0425 514 HOH   A O   
6875 O O   . HOH   E .   ? 0.4800 0.5594 0.4296 -0.0791 -0.0272 -0.1394 515 HOH   A O   
6876 O O   . HOH   E .   ? 0.2553 0.7132 0.4226 0.0519  0.0252  -0.0673 516 HOH   A O   
6877 O O   B HOH   E .   ? 0.4502 0.4190 0.3810 0.1486  -0.0250 0.0077  517 HOH   A O   
6878 O O   . HOH   E .   ? 0.4802 0.4362 0.4223 0.1238  -0.0144 0.1317  518 HOH   A O   
6879 O O   . HOH   E .   ? 0.5040 0.6703 0.5210 -0.0584 -0.0692 0.0179  519 HOH   A O   
6880 O O   . HOH   E .   ? 0.2758 0.4566 0.5585 0.0052  -0.0705 0.2659  520 HOH   A O   
6881 O O   . HOH   F .   ? 0.2213 0.2140 0.3481 0.0120  0.0673  0.0364  201 HOH   B O   
6882 O O   . HOH   F .   ? 0.4518 0.3336 0.3959 -0.0305 -0.0046 -0.1377 202 HOH   B O   
6883 O O   . HOH   F .   ? 0.5422 0.5781 0.2581 0.0441  -0.0557 -0.1459 203 HOH   B O   
6884 O O   . HOH   F .   ? 0.6481 0.5842 0.6218 0.1715  0.0627  0.0099  204 HOH   B O   
6885 O O   . HOH   F .   ? 0.4574 0.3793 0.6418 0.0343  -0.0978 0.2509  205 HOH   B O   
6886 O O   . HOH   F .   ? 0.5192 0.5443 0.4176 0.2794  -0.1466 -0.0302 206 HOH   B O   
6887 O O   . HOH   F .   ? 0.3619 0.7046 0.3587 0.0540  0.0157  0.2407  207 HOH   B O   
6888 O O   . HOH   F .   ? 0.3146 0.5305 0.5165 -0.0032 0.1737  -0.1832 208 HOH   B O   
6889 O O   . HOH   F .   ? 0.3698 0.4787 0.5359 -0.1056 0.0186  -0.1250 209 HOH   B O   
6890 O O   . HOH   F .   ? 0.3516 0.3659 0.6832 -0.0771 0.0368  -0.0634 210 HOH   B O   
6891 O O   . HOH   F .   ? 0.7199 0.3499 0.4510 0.1291  0.1295  0.0433  211 HOH   B O   
6892 O O   . HOH   F .   ? 0.2880 0.3282 0.6270 0.0762  -0.1102 0.0484  212 HOH   B O   
6893 O O   . HOH   F .   ? 0.3139 0.1970 0.5421 0.0090  0.1979  0.0697  213 HOH   B O   
6894 O O   . HOH   F .   ? 0.1886 0.2249 0.3196 -0.0069 0.0116  -0.0304 214 HOH   B O   
6895 O O   . HOH   F .   ? 0.1588 0.1894 0.2865 -0.0150 -0.0022 0.0060  215 HOH   B O   
6896 O O   . HOH   F .   ? 0.3609 0.5585 0.4401 0.2377  0.0348  -0.0358 216 HOH   B O   
6897 O O   . HOH   F .   ? 0.4543 0.3873 0.3695 0.0145  -0.1022 0.0458  217 HOH   B O   
6898 O O   . HOH   F .   ? 0.4067 0.5264 0.3722 0.2287  -0.0310 0.0431  218 HOH   B O   
6899 O O   . HOH   F .   ? 0.3287 0.4121 0.5309 0.0531  -0.0182 0.0133  219 HOH   B O   
6900 O O   . HOH   F .   ? 0.5856 0.2962 0.4160 -0.1680 0.0298  0.0164  220 HOH   B O   
6901 O O   . HOH   F .   ? 0.4272 0.4503 0.3943 0.0133  0.0691  -0.1601 221 HOH   B O   
6902 O O   . HOH   F .   ? 0.4932 0.1893 0.3308 -0.0011 -0.0981 0.0039  222 HOH   B O   
6903 O O   . HOH   F .   ? 0.4542 0.4512 0.6410 -0.0454 -0.1575 -0.1012 223 HOH   B O   
6904 O O   . HOH   F .   ? 0.3204 0.3210 0.5592 0.0157  0.0336  0.0069  224 HOH   B O   
6905 O O   . HOH   F .   ? 0.4082 0.6662 0.3654 0.2014  0.0100  -0.0239 225 HOH   B O   
6906 O O   . HOH   F .   ? 0.1696 0.2107 0.3203 -0.0145 0.0053  -0.0050 226 HOH   B O   
6907 O O   . HOH   F .   ? 0.2432 0.1837 0.3054 -0.0333 0.1103  -0.0051 227 HOH   B O   
6908 O O   . HOH   F .   ? 0.4911 0.3120 0.4110 -0.2228 -0.0235 0.0199  228 HOH   B O   
6909 O O   . HOH   F .   ? 0.2012 0.1277 0.3551 0.0052  -0.0564 -0.0098 229 HOH   B O   
6910 O O   . HOH   F .   ? 0.3758 0.4344 0.5370 -0.1654 -0.0069 0.0726  230 HOH   B O   
6911 O O   . HOH   F .   ? 0.2827 0.4170 0.3273 -0.1183 0.0130  0.0202  231 HOH   B O   
6912 O O   . HOH   F .   ? 0.6866 0.4516 0.4734 0.1983  -0.0553 -0.1260 232 HOH   B O   
6913 O O   . HOH   F .   ? 0.2104 0.2262 0.4114 -0.0418 -0.0066 -0.0600 233 HOH   B O   
6914 O O   . HOH   F .   ? 0.3626 0.1722 0.2286 0.0126  -0.0818 -0.0070 234 HOH   B O   
6915 O O   . HOH   F .   ? 0.3146 0.2159 0.4892 0.0037  0.1634  0.0327  235 HOH   B O   
6916 O O   . HOH   F .   ? 0.6463 0.6222 0.3349 0.0285  -0.0249 0.0635  236 HOH   B O   
6917 O O   . HOH   F .   ? 0.1461 0.1409 0.1754 -0.0120 -0.0062 -0.0006 237 HOH   B O   
6918 O O   . HOH   F .   ? 0.3940 0.2762 0.4117 0.0944  -0.0447 -0.0740 238 HOH   B O   
6919 O O   . HOH   F .   ? 0.2958 0.2447 0.3107 0.0463  0.0155  -0.0777 239 HOH   B O   
6920 O O   . HOH   F .   ? 0.1621 0.1437 0.2888 -0.0059 0.0019  -0.0070 240 HOH   B O   
6921 O O   . HOH   F .   ? 0.3554 0.2677 0.4161 0.0312  -0.0935 -0.1280 241 HOH   B O   
6922 O O   . HOH   F .   ? 0.2258 0.3667 0.3495 -0.0590 -0.0649 -0.0585 242 HOH   B O   
6923 O O   . HOH   F .   ? 0.2126 0.2455 0.3117 -0.0601 0.0096  -0.0232 243 HOH   B O   
6924 O O   . HOH   F .   ? 0.3601 0.3171 0.2567 0.0306  0.0644  0.0487  244 HOH   B O   
6925 O O   . HOH   F .   ? 0.1486 0.1301 0.1807 -0.0024 -0.0137 0.0121  245 HOH   B O   
6926 O O   . HOH   F .   ? 0.2167 0.2023 0.2314 -0.0383 -0.0489 0.0277  246 HOH   B O   
6927 O O   . HOH   F .   ? 0.2866 0.2194 0.3131 0.0752  0.0786  0.0055  247 HOH   B O   
6928 O O   . HOH   F .   ? 0.2005 0.3864 0.2705 -0.0447 -0.0257 0.0639  248 HOH   B O   
6929 O O   . HOH   F .   ? 0.3198 0.3765 0.2312 0.0274  0.0626  0.0143  249 HOH   B O   
6930 O O   . HOH   F .   ? 0.4410 0.3475 0.3601 -0.0806 0.0505  -0.1004 250 HOH   B O   
6931 O O   . HOH   F .   ? 0.6456 0.3011 0.2668 0.0271  0.0874  0.0107  251 HOH   B O   
6932 O O   . HOH   F .   ? 0.3156 0.1745 0.6278 -0.0137 -0.1224 -0.0323 252 HOH   B O   
6933 O O   . HOH   F .   ? 0.2961 0.4760 0.3178 -0.1206 -0.0178 -0.0711 253 HOH   B O   
6934 O O   . HOH   F .   ? 0.2406 0.4113 0.5791 0.1195  -0.0653 -0.1266 254 HOH   B O   
6935 O O   . HOH   F .   ? 0.2113 0.1876 0.3739 -0.0009 -0.0420 -0.0300 255 HOH   B O   
6936 O O   . HOH   F .   ? 0.2092 0.1471 0.2388 -0.0280 -0.0382 0.0237  256 HOH   B O   
6937 O O   . HOH   F .   ? 0.3181 0.4783 0.3432 -0.0371 -0.0945 0.0856  257 HOH   B O   
6938 O O   . HOH   F .   ? 0.3263 0.2479 0.3249 -0.0295 0.0062  -0.0465 258 HOH   B O   
6939 O O   . HOH   F .   ? 0.1606 0.1569 0.3349 -0.0257 -0.0293 0.0161  259 HOH   B O   
6940 O O   . HOH   F .   ? 0.2466 0.2038 0.2682 0.0763  -0.0718 -0.0575 260 HOH   B O   
6941 O O   . HOH   F .   ? 0.1762 0.2835 0.2974 0.0381  0.0349  0.1044  261 HOH   B O   
6942 O O   . HOH   F .   ? 0.2230 0.3083 0.2317 -0.0489 0.0236  0.0335  262 HOH   B O   
6943 O O   . HOH   F .   ? 0.2328 0.2208 0.2079 0.0043  -0.0088 -0.0005 263 HOH   B O   
6944 O O   . HOH   F .   ? 0.2471 0.1991 0.3045 -0.0601 0.0093  -0.0079 264 HOH   B O   
6945 O O   . HOH   F .   ? 0.1411 0.1663 0.2296 -0.0094 0.0056  0.0096  265 HOH   B O   
6946 O O   . HOH   F .   ? 0.3118 0.4863 0.5392 -0.0300 -0.0095 -0.1200 266 HOH   B O   
6947 O O   . HOH   F .   ? 0.4226 0.3108 0.4431 -0.0064 -0.1312 -0.0813 267 HOH   B O   
6948 O O   . HOH   F .   ? 0.3286 0.3281 0.5432 -0.0237 0.0429  -0.0572 268 HOH   B O   
6949 O O   . HOH   F .   ? 0.2481 0.2797 0.2597 -0.0468 -0.0754 0.0247  269 HOH   B O   
6950 O O   . HOH   F .   ? 0.1817 0.1799 0.1936 -0.0416 -0.0436 0.0076  270 HOH   B O   
6951 O O   . HOH   F .   ? 0.2468 0.3924 0.3723 0.0177  0.0971  0.0163  271 HOH   B O   
6952 O O   . HOH   F .   ? 0.2334 0.2068 0.2437 0.0059  -0.0081 -0.0078 272 HOH   B O   
6953 O O   . HOH   F .   ? 0.1998 0.1463 0.2455 -0.0231 -0.0145 0.0218  273 HOH   B O   
6954 O O   . HOH   F .   ? 0.2891 0.2036 0.5037 0.0181  0.0603  0.0425  274 HOH   B O   
6955 O O   . HOH   F .   ? 0.3488 0.3940 0.4813 0.1391  -0.0810 -0.1193 275 HOH   B O   
6956 O O   . HOH   F .   ? 0.2314 0.2525 0.2463 -0.0403 -0.0618 -0.0297 276 HOH   B O   
6957 O O   . HOH   F .   ? 0.2105 0.4393 0.4946 -0.0319 -0.0485 -0.1372 277 HOH   B O   
6958 O O   . HOH   F .   ? 0.4736 0.3626 0.2989 0.0197  0.0116  -0.0971 278 HOH   B O   
6959 O O   . HOH   F .   ? 0.2503 0.3885 0.2486 0.1425  -0.0377 -0.0416 279 HOH   B O   
6960 O O   . HOH   F .   ? 0.1631 0.1543 0.3694 -0.0114 0.0006  0.0034  280 HOH   B O   
6961 O O   . HOH   F .   ? 0.1792 0.1379 0.4533 -0.0085 -0.0342 -0.0080 281 HOH   B O   
6962 O O   . HOH   F .   ? 0.4767 0.4753 0.4670 0.0394  -0.1525 0.0031  282 HOH   B O   
6963 O O   . HOH   F .   ? 0.2849 0.2910 0.4811 -0.0427 -0.0655 0.1174  283 HOH   B O   
6964 O O   . HOH   F .   ? 0.2249 0.3890 0.3484 -0.0697 0.0472  -0.1185 284 HOH   B O   
6965 O O   . HOH   F .   ? 0.2735 0.6866 0.7191 0.1392  -0.0352 -0.1094 285 HOH   B O   
6966 O O   . HOH   F .   ? 0.1652 0.1470 0.2070 0.0011  0.0050  0.0040  286 HOH   B O   
6967 O O   . HOH   F .   ? 0.2543 0.7166 0.2474 0.0964  -0.0326 -0.0337 287 HOH   B O   
6968 O O   . HOH   F .   ? 0.3420 0.6666 0.3486 0.1490  -0.0478 0.0988  288 HOH   B O   
6969 O O   . HOH   F .   ? 0.3627 0.2096 0.4184 -0.0877 -0.2044 0.0822  289 HOH   B O   
6970 O O   . HOH   F .   ? 0.1627 0.2009 0.1797 -0.0160 -0.0176 0.0058  290 HOH   B O   
6971 O O   . HOH   F .   ? 0.2484 0.2632 0.3006 0.0254  -0.0774 0.0080  291 HOH   B O   
6972 O O   . HOH   F .   ? 0.1693 0.2002 0.2936 0.0150  -0.0019 0.0144  292 HOH   B O   
6973 O O   . HOH   F .   ? 0.1663 0.3409 0.4986 0.0218  0.0015  -0.1469 293 HOH   B O   
6974 O O   . HOH   F .   ? 0.4613 0.4646 0.2435 0.0044  0.0670  0.0821  294 HOH   B O   
6975 O O   . HOH   F .   ? 0.2782 0.4787 0.4710 -0.1097 -0.1118 0.0731  295 HOH   B O   
6976 O O   . HOH   F .   ? 0.3308 0.2750 0.3035 -0.0393 0.0259  -0.1180 296 HOH   B O   
6977 O O   . HOH   F .   ? 0.3426 0.2536 0.2285 0.0050  -0.0798 -0.0095 297 HOH   B O   
6978 O O   . HOH   F .   ? 0.4510 0.6170 0.2456 -0.0247 -0.0348 0.0948  298 HOH   B O   
6979 O O   . HOH   F .   ? 0.5455 0.3870 0.3336 0.2541  0.1370  0.1089  299 HOH   B O   
6980 O O   . HOH   F .   ? 0.4493 0.3344 0.4779 -0.0721 0.0162  0.1370  300 HOH   B O   
6981 O O   . HOH   F .   ? 0.4870 0.3882 0.2613 0.1399  -0.0896 0.0394  301 HOH   B O   
6982 O O   . HOH   F .   ? 0.3381 0.1910 0.3582 0.0790  0.1241  0.0478  302 HOH   B O   
6983 O O   . HOH   F .   ? 0.1801 0.1597 0.2682 0.0034  0.0072  0.0244  303 HOH   B O   
6984 O O   . HOH   F .   ? 0.1939 0.2718 0.6207 0.0373  -0.0362 -0.1142 304 HOH   B O   
6985 O O   . HOH   F .   ? 0.3401 0.3885 0.4074 -0.1552 0.1256  -0.0582 305 HOH   B O   
6986 O O   . HOH   F .   ? 0.2886 0.3019 0.3673 -0.0558 0.1110  -0.0870 306 HOH   B O   
6987 O O   . HOH   F .   ? 0.2044 0.1590 0.3731 0.0328  -0.1005 -0.0014 307 HOH   B O   
6988 O O   . HOH   F .   ? 0.2152 0.1556 0.2845 -0.0277 -0.0236 -0.0080 308 HOH   B O   
6989 O O   . HOH   F .   ? 0.1605 0.1868 0.3174 -0.0261 -0.0096 0.0141  309 HOH   B O   
6990 O O   . HOH   F .   ? 0.5535 0.2906 0.2450 -0.1887 0.0909  -0.0255 310 HOH   B O   
6991 O O   . HOH   F .   ? 0.4370 0.4472 0.2449 0.1390  -0.0726 -0.0043 311 HOH   B O   
6992 O O   . HOH   F .   ? 0.2454 0.1471 0.2645 -0.0167 -0.0227 0.0298  312 HOH   B O   
6993 O O   . HOH   F .   ? 0.2243 0.3205 0.4794 -0.0248 -0.0493 -0.0039 313 HOH   B O   
6994 O O   . HOH   F .   ? 0.1625 0.1508 0.3284 0.0052  -0.0024 -0.0046 314 HOH   B O   
6995 O O   . HOH   F .   ? 0.3449 0.4022 0.7641 -0.0232 -0.1023 0.2278  315 HOH   B O   
6996 O O   . HOH   F .   ? 0.6375 0.6405 0.5034 0.3094  -0.0081 -0.0503 316 HOH   B O   
6997 O O   . HOH   F .   ? 0.2141 0.1943 0.2084 -0.0098 0.0169  0.0247  317 HOH   B O   
6998 O O   . HOH   F .   ? 0.6419 0.4134 0.5342 0.1299  0.0807  -0.0205 318 HOH   B O   
6999 O O   . HOH   F .   ? 0.4608 0.4423 0.2954 0.0504  -0.0515 -0.0688 319 HOH   B O   
7000 O O   . HOH   F .   ? 0.4202 0.2265 0.2939 0.1540  0.1082  0.0391  320 HOH   B O   
7001 O O   . HOH   F .   ? 0.4708 0.4018 0.5588 0.0583  0.0260  0.0775  321 HOH   B O   
7002 O O   . HOH   F .   ? 0.6247 0.4938 0.6523 0.1467  -0.1114 0.1869  322 HOH   B O   
7003 O O   . HOH   F .   ? 0.1594 0.1598 0.3177 -0.0188 -0.0144 -0.0132 323 HOH   B O   
7004 O O   . HOH   F .   ? 0.4431 0.3145 0.5105 0.0918  0.2097  0.1762  324 HOH   B O   
7005 O O   . HOH   F .   ? 0.1707 0.2870 0.2524 -0.0123 -0.0173 0.0670  325 HOH   B O   
7006 O O   . HOH   F .   ? 0.2133 0.5614 0.4892 -0.0698 -0.0284 -0.0286 326 HOH   B O   
7007 O O   . HOH   F .   ? 0.1853 0.2041 0.2978 0.0337  0.0368  0.0203  327 HOH   B O   
7008 O O   . HOH   F .   ? 0.3075 0.2198 0.2464 0.0198  -0.0186 0.0327  328 HOH   B O   
7009 O O   . HOH   F .   ? 0.2823 0.3206 0.5069 -0.0604 -0.1513 0.1331  329 HOH   B O   
7010 O O   . HOH   F .   ? 0.4665 0.2440 0.3234 0.0232  0.0113  0.0854  330 HOH   B O   
7011 O O   . HOH   F .   ? 0.8272 0.2166 0.2860 0.0191  -0.0685 0.0028  331 HOH   B O   
7012 O O   . HOH   F .   ? 0.5779 0.5669 0.5474 -0.1104 -0.0436 0.1634  332 HOH   B O   
7013 O O   . HOH   F .   ? 0.2200 0.2354 0.5613 -0.0541 -0.0021 0.1301  333 HOH   B O   
7014 O O   . HOH   F .   ? 0.1705 0.2747 0.3162 0.0203  -0.0158 -0.0582 334 HOH   B O   
7015 O O   . HOH   F .   ? 0.2648 0.2010 0.5257 -0.0091 0.0036  0.0428  335 HOH   B O   
7016 O O   . HOH   F .   ? 0.5842 0.3412 0.3510 0.0055  0.1197  0.1176  336 HOH   B O   
7017 O O   . HOH   F .   ? 0.5257 0.3717 0.4209 0.0209  0.0760  -0.1360 337 HOH   B O   
7018 O O   . HOH   F .   ? 0.4901 0.5064 0.3866 0.0254  -0.0835 0.0547  338 HOH   B O   
7019 O O   . HOH   F .   ? 0.6126 0.4443 0.6503 -0.0748 -0.0856 -0.1100 339 HOH   B O   
7020 O O   . HOH   F .   ? 0.1696 0.1449 0.2634 0.0071  -0.0230 0.0082  340 HOH   B O   
7021 O O   . HOH   F .   ? 0.4834 0.3185 0.3180 0.0533  -0.1122 -0.0813 341 HOH   B O   
7022 O O   . HOH   F .   ? 0.4564 0.7338 0.3932 -0.0261 -0.0459 0.2227  342 HOH   B O   
7023 O O   . HOH   F .   ? 0.2001 0.5806 0.6365 -0.0232 -0.0873 -0.0245 343 HOH   B O   
7024 O O   . HOH   F .   ? 0.4010 0.6199 0.3888 -0.1054 -0.0861 -0.0690 344 HOH   B O   
7025 O O   . HOH   F .   ? 0.2119 0.1985 0.3046 -0.0101 0.0469  -0.0083 345 HOH   B O   
7026 O O   . HOH   F .   ? 0.6970 0.5805 0.2939 -0.0751 -0.0759 0.0845  346 HOH   B O   
7027 O O   . HOH   F .   ? 0.2128 0.4398 0.4745 0.0166  0.0262  0.0103  347 HOH   B O   
7028 O O   . HOH   F .   ? 0.4815 0.5400 0.4551 -0.1104 0.0278  0.1139  348 HOH   B O   
7029 O O   . HOH   F .   ? 0.2577 0.6150 0.3466 0.1717  -0.0516 -0.1554 349 HOH   B O   
7030 O O   . HOH   F .   ? 0.4147 0.5092 0.5229 0.0140  -0.0861 0.0706  350 HOH   B O   
7031 O O   . HOH   F .   ? 0.2592 0.2223 0.5000 -0.0288 -0.0958 -0.0369 351 HOH   B O   
7032 O O   . HOH   F .   ? 0.4109 0.5737 0.6126 -0.0067 0.0062  -0.0447 352 HOH   B O   
7033 O O   . HOH   F .   ? 0.2977 0.1802 0.4246 0.0355  -0.1197 -0.0485 353 HOH   B O   
7034 O O   . HOH   F .   ? 0.3705 0.2066 0.3568 -0.0581 0.0309  -0.0641 354 HOH   B O   
7035 O O   . HOH   F .   ? 0.3451 0.4189 0.4732 -0.1451 0.0085  -0.0449 355 HOH   B O   
7036 O O   . HOH   F .   ? 0.4807 0.3669 0.5467 -0.1301 0.1606  0.0808  356 HOH   B O   
7037 O O   . HOH   F .   ? 0.4945 0.3854 0.4007 0.0467  0.1148  -0.0624 357 HOH   B O   
7038 O O   . HOH   F .   ? 0.3662 0.2725 0.3535 -0.0905 0.0028  -0.0453 358 HOH   B O   
7039 O O   . HOH   F .   ? 0.4923 0.4704 0.5539 -0.0487 -0.0023 0.0331  359 HOH   B O   
7040 O O   . HOH   F .   ? 0.5256 0.3443 0.5039 -0.0036 -0.1512 -0.0571 360 HOH   B O   
7041 O O   . HOH   F .   ? 0.4647 0.5383 0.5091 0.1551  -0.1261 0.1557  361 HOH   B O   
7042 O O   . HOH   F .   ? 0.4666 0.3892 0.6340 0.0480  0.0785  0.1190  362 HOH   B O   
7043 O O   . HOH   F .   ? 0.2235 0.3661 0.6918 -0.0715 -0.0686 -0.0688 363 HOH   B O   
7044 O O   . HOH   F .   ? 0.4532 0.6296 0.3363 0.2015  0.0361  0.0888  364 HOH   B O   
7045 O O   . HOH   F .   ? 0.5178 0.2957 0.5309 -0.1367 0.0030  -0.0001 365 HOH   B O   
7046 O O   . HOH   F .   ? 0.6709 0.2118 0.3821 -0.0126 0.0307  0.0551  366 HOH   B O   
7047 O O   . HOH   F .   ? 0.5968 0.4784 0.4214 0.1311  0.0543  0.0693  367 HOH   B O   
7048 O O   . HOH   F .   ? 0.5475 0.5352 0.3453 0.1177  -0.1300 0.0570  368 HOH   B O   
7049 O O   . HOH   F .   ? 0.5021 0.5250 0.4471 -0.0700 -0.0514 -0.0999 369 HOH   B O   
7050 O O   . HOH   F .   ? 0.5125 0.3645 0.5398 0.1394  -0.1474 0.0001  370 HOH   B O   
7051 O O   . HOH   F .   ? 0.6096 0.3733 0.2819 -0.1263 -0.0972 -0.0315 371 HOH   B O   
7052 O O   . HOH   F .   ? 0.3854 0.5536 0.5336 0.2335  0.1120  0.1457  372 HOH   B O   
7053 O O   . HOH   F .   ? 0.7221 0.7184 0.4554 0.2190  -0.1281 0.1026  373 HOH   B O   
7054 O O   . HOH   F .   ? 0.4284 0.3419 0.4142 0.1031  -0.1429 -0.0835 374 HOH   B O   
7055 O O   . HOH   F .   ? 0.4408 0.5194 0.4695 -0.1047 -0.0337 0.0558  375 HOH   B O   
7056 O O   . HOH   F .   ? 0.2411 0.4625 0.4371 0.0262  -0.0788 -0.0948 376 HOH   B O   
7057 O O   . HOH   F .   ? 0.4727 0.7011 0.5883 0.1489  0.0482  0.2880  377 HOH   B O   
7058 O O   . HOH   F .   ? 0.3396 0.4534 0.2355 0.0355  0.0213  -0.0098 378 HOH   B O   
7059 O O   . HOH   F .   ? 0.4936 0.6920 0.4227 -0.1355 0.0313  -0.1395 379 HOH   B O   
7060 O O   . HOH   F .   ? 0.7041 0.3661 0.5111 -0.0940 -0.0863 0.0144  380 HOH   B O   
7061 O O   . HOH   F .   ? 0.3877 0.4198 0.4683 0.0821  -0.0046 -0.0281 381 HOH   B O   
7062 O O   . HOH   F .   ? 0.5594 0.6344 0.6339 0.0001  0.2081  0.1567  382 HOH   B O   
7063 O O   . HOH   F .   ? 0.3276 0.2577 0.3263 0.0197  0.0123  0.0387  383 HOH   B O   
7064 O O   . HOH   F .   ? 0.4917 0.7953 0.5778 -0.0024 0.2361  0.0478  384 HOH   B O   
7065 O O   . HOH   F .   ? 0.5480 0.4647 0.4414 0.0183  -0.0459 -0.0429 385 HOH   B O   
7066 O O   . HOH   F .   ? 0.6883 0.3962 0.4159 0.0970  0.1448  -0.0370 386 HOH   B O   
7067 O O   . HOH   F .   ? 0.6152 0.4072 0.5442 -0.0788 0.0640  -0.0328 387 HOH   B O   
7068 O O   . HOH   F .   ? 0.2404 0.4212 0.4110 -0.0771 -0.1072 -0.0325 388 HOH   B O   
7069 O O   . HOH   F .   ? 0.7525 0.5228 0.4298 0.1669  -0.0331 0.0764  389 HOH   B O   
7070 O O   . HOH   F .   ? 0.4683 0.3682 0.3631 0.0335  0.0471  -0.0076 390 HOH   B O   
7071 O O   . HOH   F .   ? 0.3644 0.2296 0.3446 0.0644  -0.0336 0.0117  391 HOH   B O   
7072 O O   . HOH   F .   ? 0.4704 0.4237 0.4425 0.0188  0.0675  0.0497  392 HOH   B O   
7073 O O   . HOH   F .   ? 0.2697 0.4369 0.6415 -0.1382 -0.0677 -0.0039 393 HOH   B O   
7074 O O   . HOH   F .   ? 0.4079 0.2101 0.5470 -0.0478 0.0768  0.0563  394 HOH   B O   
7075 O O   . HOH   F .   ? 0.3951 0.6092 0.4222 0.0861  0.0198  -0.1029 395 HOH   B O   
7076 O O   . HOH   F .   ? 0.4225 0.4350 0.4345 0.0254  0.0724  0.0797  396 HOH   B O   
7077 O O   . HOH   F .   ? 0.3213 0.3806 0.4105 0.0211  0.0164  -0.0795 397 HOH   B O   
7078 O O   . HOH   F .   ? 0.2083 0.2836 0.6217 -0.0635 -0.0872 0.0383  398 HOH   B O   
7079 O O   . HOH   F .   ? 0.5851 0.4112 0.3079 -0.2402 -0.0538 0.1070  399 HOH   B O   
7080 O O   . HOH   F .   ? 0.5501 0.5848 0.7227 0.1378  -0.1167 0.1732  400 HOH   B O   
7081 O O   . HOH   F .   ? 0.5294 0.6612 0.3737 0.1867  0.0113  -0.0370 401 HOH   B O   
# 
