data_7HCW
# 
_entry.id   7HCW 
# 
_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   7HCW         pdb_00007hcw 10.2210/pdb7hcw/pdb 
WWPDB D_1001407314 ?            ?                   
# 
_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                        7HCW 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                      18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 
'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn '(3R,4S)-4-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]oxolan-3-ol' 220.228   1   ?                      ? ? ? 
3 water       nat water                                                           18.015    420 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3R,4S)-4-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]oxolan-3-ol' A1A6Q 
3 water                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A6Q non-polymer         . '(3R,4S)-4-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]oxolan-3-ol' ? 'C10 H12 N4 O2'  220.228 
ALA   'L-peptide linking' y ALANINE                                                         ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                        ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                      ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                 ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                        ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                       ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                 ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                         ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                       ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                           ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                      ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                         ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                          ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                      ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                   ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                         ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                          ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                       ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                        ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1A6Q 1   201 201  A1A6Q LA1 A . 
D 3 HOH   1   301 93   HOH   HOH A . 
D 3 HOH   2   302 196  HOH   HOH A . 
D 3 HOH   3   303 493  HOH   HOH A . 
D 3 HOH   4   304 1310 HOH   HOH A . 
D 3 HOH   5   305 625  HOH   HOH A . 
D 3 HOH   6   306 292  HOH   HOH A . 
D 3 HOH   7   307 409  HOH   HOH A . 
D 3 HOH   8   308 247  HOH   HOH A . 
D 3 HOH   9   309 229  HOH   HOH A . 
D 3 HOH   10  310 209  HOH   HOH A . 
D 3 HOH   11  311 630  HOH   HOH A . 
D 3 HOH   12  312 1289 HOH   HOH A . 
D 3 HOH   13  313 12   HOH   HOH A . 
D 3 HOH   14  314 105  HOH   HOH A . 
D 3 HOH   15  315 296  HOH   HOH A . 
D 3 HOH   16  316 40   HOH   HOH A . 
D 3 HOH   17  317 236  HOH   HOH A . 
D 3 HOH   18  318 1301 HOH   HOH A . 
D 3 HOH   19  319 76   HOH   HOH A . 
D 3 HOH   20  320 136  HOH   HOH A . 
D 3 HOH   21  321 109  HOH   HOH A . 
D 3 HOH   22  322 124  HOH   HOH A . 
D 3 HOH   23  323 151  HOH   HOH A . 
D 3 HOH   24  324 1290 HOH   HOH A . 
D 3 HOH   25  325 281  HOH   HOH A . 
D 3 HOH   26  326 86   HOH   HOH A . 
D 3 HOH   27  327 225  HOH   HOH A . 
D 3 HOH   28  328 393  HOH   HOH A . 
D 3 HOH   29  329 661  HOH   HOH A . 
D 3 HOH   30  330 15   HOH   HOH A . 
D 3 HOH   31  331 1308 HOH   HOH A . 
D 3 HOH   32  332 153  HOH   HOH A . 
D 3 HOH   33  333 662  HOH   HOH A . 
D 3 HOH   34  334 333  HOH   HOH A . 
D 3 HOH   35  335 1300 HOH   HOH A . 
D 3 HOH   36  336 164  HOH   HOH A . 
D 3 HOH   37  337 140  HOH   HOH A . 
D 3 HOH   38  338 78   HOH   HOH A . 
D 3 HOH   39  339 320  HOH   HOH A . 
D 3 HOH   40  340 1295 HOH   HOH A . 
D 3 HOH   41  341 192  HOH   HOH A . 
D 3 HOH   42  342 241  HOH   HOH A . 
D 3 HOH   43  343 337  HOH   HOH A . 
D 3 HOH   44  344 964  HOH   HOH A . 
D 3 HOH   45  345 165  HOH   HOH A . 
D 3 HOH   46  346 7    HOH   HOH A . 
D 3 HOH   47  347 18   HOH   HOH A . 
D 3 HOH   48  348 36   HOH   HOH A . 
D 3 HOH   49  349 469  HOH   HOH A . 
D 3 HOH   50  350 1283 HOH   HOH A . 
D 3 HOH   51  351 139  HOH   HOH A . 
D 3 HOH   52  352 57   HOH   HOH A . 
D 3 HOH   53  353 42   HOH   HOH A . 
D 3 HOH   54  354 92   HOH   HOH A . 
D 3 HOH   55  355 396  HOH   HOH A . 
D 3 HOH   56  356 39   HOH   HOH A . 
D 3 HOH   57  357 66   HOH   HOH A . 
D 3 HOH   58  358 354  HOH   HOH A . 
D 3 HOH   59  359 2    HOH   HOH A . 
D 3 HOH   60  360 74   HOH   HOH A . 
D 3 HOH   61  361 155  HOH   HOH A . 
D 3 HOH   62  362 102  HOH   HOH A . 
D 3 HOH   63  363 33   HOH   HOH A . 
D 3 HOH   64  364 138  HOH   HOH A . 
D 3 HOH   65  365 19   HOH   HOH A . 
D 3 HOH   66  366 939  HOH   HOH A . 
D 3 HOH   67  367 21   HOH   HOH A . 
D 3 HOH   68  368 17   HOH   HOH A . 
D 3 HOH   69  369 5    HOH   HOH A . 
D 3 HOH   70  370 186  HOH   HOH A . 
D 3 HOH   71  371 45   HOH   HOH A . 
D 3 HOH   72  372 1    HOH   HOH A . 
D 3 HOH   73  373 162  HOH   HOH A . 
D 3 HOH   74  374 169  HOH   HOH A . 
D 3 HOH   75  375 49   HOH   HOH A . 
D 3 HOH   76  376 27   HOH   HOH A . 
D 3 HOH   77  377 81   HOH   HOH A . 
D 3 HOH   78  378 154  HOH   HOH A . 
D 3 HOH   79  379 46   HOH   HOH A . 
D 3 HOH   80  380 10   HOH   HOH A . 
D 3 HOH   81  381 56   HOH   HOH A . 
D 3 HOH   82  382 159  HOH   HOH A . 
D 3 HOH   83  383 218  HOH   HOH A . 
D 3 HOH   84  384 405  HOH   HOH A . 
D 3 HOH   85  385 8    HOH   HOH A . 
D 3 HOH   86  386 148  HOH   HOH A . 
D 3 HOH   87  387 1275 HOH   HOH A . 
D 3 HOH   88  388 134  HOH   HOH A . 
D 3 HOH   89  389 461  HOH   HOH A . 
D 3 HOH   90  390 6    HOH   HOH A . 
D 3 HOH   91  391 35   HOH   HOH A . 
D 3 HOH   92  392 85   HOH   HOH A . 
D 3 HOH   93  393 26   HOH   HOH A . 
D 3 HOH   94  394 199  HOH   HOH A . 
D 3 HOH   95  395 366  HOH   HOH A . 
D 3 HOH   96  396 132  HOH   HOH A . 
D 3 HOH   97  397 7    HOH   HOH A . 
D 3 HOH   98  398 24   HOH   HOH A . 
D 3 HOH   99  399 4    HOH   HOH A . 
D 3 HOH   100 400 116  HOH   HOH A . 
D 3 HOH   101 401 83   HOH   HOH A . 
D 3 HOH   102 402 58   HOH   HOH A . 
D 3 HOH   103 403 67   HOH   HOH A . 
D 3 HOH   104 404 34   HOH   HOH A . 
D 3 HOH   105 405 278  HOH   HOH A . 
D 3 HOH   106 406 3    HOH   HOH A . 
D 3 HOH   107 407 12   HOH   HOH A . 
D 3 HOH   108 408 3    HOH   HOH A . 
D 3 HOH   109 409 303  HOH   HOH A . 
D 3 HOH   110 410 121  HOH   HOH A . 
D 3 HOH   111 411 1315 HOH   HOH A . 
D 3 HOH   112 412 68   HOH   HOH A . 
D 3 HOH   113 413 1309 HOH   HOH A . 
D 3 HOH   114 414 1313 HOH   HOH A . 
D 3 HOH   115 415 1068 HOH   HOH A . 
D 3 HOH   116 416 381  HOH   HOH A . 
D 3 HOH   117 417 122  HOH   HOH A . 
D 3 HOH   118 418 96   HOH   HOH A . 
D 3 HOH   119 419 195  HOH   HOH A . 
D 3 HOH   120 420 397  HOH   HOH A . 
D 3 HOH   121 421 25   HOH   HOH A . 
D 3 HOH   122 422 351  HOH   HOH A . 
D 3 HOH   123 423 8    HOH   HOH A . 
D 3 HOH   124 424 123  HOH   HOH A . 
D 3 HOH   125 425 53   HOH   HOH A . 
D 3 HOH   126 426 125  HOH   HOH A . 
D 3 HOH   127 427 582  HOH   HOH A . 
D 3 HOH   128 428 95   HOH   HOH A . 
D 3 HOH   129 429 51   HOH   HOH A . 
D 3 HOH   130 430 1279 HOH   HOH A . 
D 3 HOH   131 431 212  HOH   HOH A . 
D 3 HOH   132 432 156  HOH   HOH A . 
D 3 HOH   133 433 1222 HOH   HOH A . 
D 3 HOH   134 434 1286 HOH   HOH A . 
D 3 HOH   135 435 70   HOH   HOH A . 
D 3 HOH   136 436 115  HOH   HOH A . 
D 3 HOH   137 437 16   HOH   HOH A . 
D 3 HOH   138 438 71   HOH   HOH A . 
D 3 HOH   139 439 80   HOH   HOH A . 
D 3 HOH   140 440 73   HOH   HOH A . 
D 3 HOH   141 441 1189 HOH   HOH A . 
D 3 HOH   142 442 1296 HOH   HOH A . 
D 3 HOH   143 443 1238 HOH   HOH A . 
D 3 HOH   144 444 952  HOH   HOH A . 
D 3 HOH   145 445 1094 HOH   HOH A . 
D 3 HOH   146 446 94   HOH   HOH A . 
D 3 HOH   147 447 2    HOH   HOH A . 
D 3 HOH   148 448 188  HOH   HOH A . 
D 3 HOH   149 449 13   HOH   HOH A . 
D 3 HOH   150 450 97   HOH   HOH A . 
D 3 HOH   151 451 944  HOH   HOH A . 
D 3 HOH   152 452 576  HOH   HOH A . 
D 3 HOH   153 453 104  HOH   HOH A . 
D 3 HOH   154 454 4    HOH   HOH A . 
D 3 HOH   155 455 79   HOH   HOH A . 
D 3 HOH   156 456 330  HOH   HOH A . 
D 3 HOH   157 457 1119 HOH   HOH A . 
D 3 HOH   158 458 9    HOH   HOH A . 
D 3 HOH   159 459 509  HOH   HOH A . 
D 3 HOH   160 460 107  HOH   HOH A . 
D 3 HOH   161 461 1134 HOH   HOH A . 
D 3 HOH   162 462 163  HOH   HOH A . 
D 3 HOH   163 463 726  HOH   HOH A . 
D 3 HOH   164 464 1276 HOH   HOH A . 
D 3 HOH   165 465 408  HOH   HOH A . 
D 3 HOH   166 466 756  HOH   HOH A . 
D 3 HOH   167 467 361  HOH   HOH A . 
D 3 HOH   168 468 63   HOH   HOH A . 
D 3 HOH   169 469 801  HOH   HOH A . 
D 3 HOH   170 470 280  HOH   HOH A . 
D 3 HOH   171 471 126  HOH   HOH A . 
D 3 HOH   172 472 319  HOH   HOH A . 
D 3 HOH   173 473 1307 HOH   HOH A . 
D 3 HOH   174 474 556  HOH   HOH A . 
D 3 HOH   175 475 342  HOH   HOH A . 
D 3 HOH   176 476 250  HOH   HOH A . 
D 3 HOH   177 477 1306 HOH   HOH A . 
D 3 HOH   178 478 1287 HOH   HOH A . 
D 3 HOH   179 479 370  HOH   HOH A . 
D 3 HOH   180 480 267  HOH   HOH A . 
D 3 HOH   181 481 135  HOH   HOH A . 
D 3 HOH   182 482 695  HOH   HOH A . 
D 3 HOH   183 483 919  HOH   HOH A . 
D 3 HOH   184 484 674  HOH   HOH A . 
D 3 HOH   185 485 224  HOH   HOH A . 
D 3 HOH   186 486 202  HOH   HOH A . 
D 3 HOH   187 487 521  HOH   HOH A . 
D 3 HOH   188 488 6    HOH   HOH A . 
D 3 HOH   189 489 309  HOH   HOH A . 
D 3 HOH   190 490 318  HOH   HOH A . 
D 3 HOH   191 491 1299 HOH   HOH A . 
D 3 HOH   192 492 1284 HOH   HOH A . 
D 3 HOH   193 493 1314 HOH   HOH A . 
D 3 HOH   194 494 315  HOH   HOH A . 
D 3 HOH   195 495 805  HOH   HOH A . 
D 3 HOH   196 496 5    HOH   HOH A . 
D 3 HOH   197 497 711  HOH   HOH A . 
D 3 HOH   198 498 331  HOH   HOH A . 
D 3 HOH   199 499 263  HOH   HOH A . 
D 3 HOH   200 500 152  HOH   HOH A . 
D 3 HOH   201 501 356  HOH   HOH A . 
D 3 HOH   202 502 941  HOH   HOH A . 
D 3 HOH   203 503 208  HOH   HOH A . 
D 3 HOH   204 504 1071 HOH   HOH A . 
D 3 HOH   205 505 180  HOH   HOH A . 
D 3 HOH   206 506 11   HOH   HOH A . 
D 3 HOH   207 507 350  HOH   HOH A . 
D 3 HOH   208 508 363  HOH   HOH A . 
D 3 HOH   209 509 371  HOH   HOH A . 
D 3 HOH   210 510 313  HOH   HOH A . 
D 3 HOH   211 511 326  HOH   HOH A . 
D 3 HOH   212 512 429  HOH   HOH A . 
D 3 HOH   213 513 185  HOH   HOH A . 
D 3 HOH   214 514 772  HOH   HOH A . 
D 3 HOH   215 515 376  HOH   HOH A . 
D 3 HOH   216 516 1074 HOH   HOH A . 
D 3 HOH   217 517 346  HOH   HOH A . 
D 3 HOH   218 518 1292 HOH   HOH A . 
D 3 HOH   219 519 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 358  HOH   HOH B . 
E 3 HOH   3   203 549  HOH   HOH B . 
E 3 HOH   4   204 398  HOH   HOH B . 
E 3 HOH   5   205 364  HOH   HOH B . 
E 3 HOH   6   206 1249 HOH   HOH B . 
E 3 HOH   7   207 900  HOH   HOH B . 
E 3 HOH   8   208 758  HOH   HOH B . 
E 3 HOH   9   209 240  HOH   HOH B . 
E 3 HOH   10  210 654  HOH   HOH B . 
E 3 HOH   11  211 264  HOH   HOH B . 
E 3 HOH   12  212 232  HOH   HOH B . 
E 3 HOH   13  213 743  HOH   HOH B . 
E 3 HOH   14  214 353  HOH   HOH B . 
E 3 HOH   15  215 531  HOH   HOH B . 
E 3 HOH   16  216 50   HOH   HOH B . 
E 3 HOH   17  217 276  HOH   HOH B . 
E 3 HOH   18  218 120  HOH   HOH B . 
E 3 HOH   19  219 444  HOH   HOH B . 
E 3 HOH   20  220 452  HOH   HOH B . 
E 3 HOH   21  221 332  HOH   HOH B . 
E 3 HOH   22  222 343  HOH   HOH B . 
E 3 HOH   23  223 131  HOH   HOH B . 
E 3 HOH   24  224 723  HOH   HOH B . 
E 3 HOH   25  225 54   HOH   HOH B . 
E 3 HOH   26  226 272  HOH   HOH B . 
E 3 HOH   27  227 1140 HOH   HOH B . 
E 3 HOH   28  228 1278 HOH   HOH B . 
E 3 HOH   29  229 75   HOH   HOH B . 
E 3 HOH   30  230 127  HOH   HOH B . 
E 3 HOH   31  231 1312 HOH   HOH B . 
E 3 HOH   32  232 282  HOH   HOH B . 
E 3 HOH   33  233 82   HOH   HOH B . 
E 3 HOH   34  234 166  HOH   HOH B . 
E 3 HOH   35  235 128  HOH   HOH B . 
E 3 HOH   36  236 325  HOH   HOH B . 
E 3 HOH   37  237 110  HOH   HOH B . 
E 3 HOH   38  238 69   HOH   HOH B . 
E 3 HOH   39  239 30   HOH   HOH B . 
E 3 HOH   40  240 1    HOH   HOH B . 
E 3 HOH   41  241 300  HOH   HOH B . 
E 3 HOH   42  242 9    HOH   HOH B . 
E 3 HOH   43  243 60   HOH   HOH B . 
E 3 HOH   44  244 129  HOH   HOH B . 
E 3 HOH   45  245 181  HOH   HOH B . 
E 3 HOH   46  246 143  HOH   HOH B . 
E 3 HOH   47  247 205  HOH   HOH B . 
E 3 HOH   48  248 133  HOH   HOH B . 
E 3 HOH   49  249 14   HOH   HOH B . 
E 3 HOH   50  250 144  HOH   HOH B . 
E 3 HOH   51  251 47   HOH   HOH B . 
E 3 HOH   52  252 252  HOH   HOH B . 
E 3 HOH   53  253 31   HOH   HOH B . 
E 3 HOH   54  254 72   HOH   HOH B . 
E 3 HOH   55  255 52   HOH   HOH B . 
E 3 HOH   56  256 231  HOH   HOH B . 
E 3 HOH   57  257 172  HOH   HOH B . 
E 3 HOH   58  258 10   HOH   HOH B . 
E 3 HOH   59  259 347  HOH   HOH B . 
E 3 HOH   60  260 150  HOH   HOH B . 
E 3 HOH   61  261 20   HOH   HOH B . 
E 3 HOH   62  262 41   HOH   HOH B . 
E 3 HOH   63  263 391  HOH   HOH B . 
E 3 HOH   64  264 62   HOH   HOH B . 
E 3 HOH   65  265 61   HOH   HOH B . 
E 3 HOH   66  266 271  HOH   HOH B . 
E 3 HOH   67  267 59   HOH   HOH B . 
E 3 HOH   68  268 221  HOH   HOH B . 
E 3 HOH   69  269 302  HOH   HOH B . 
E 3 HOH   70  270 1277 HOH   HOH B . 
E 3 HOH   71  271 243  HOH   HOH B . 
E 3 HOH   72  272 117  HOH   HOH B . 
E 3 HOH   73  273 114  HOH   HOH B . 
E 3 HOH   74  274 103  HOH   HOH B . 
E 3 HOH   75  275 1106 HOH   HOH B . 
E 3 HOH   76  276 11   HOH   HOH B . 
E 3 HOH   77  277 147  HOH   HOH B . 
E 3 HOH   78  278 287  HOH   HOH B . 
E 3 HOH   79  279 77   HOH   HOH B . 
E 3 HOH   80  280 84   HOH   HOH B . 
E 3 HOH   81  281 43   HOH   HOH B . 
E 3 HOH   82  282 242  HOH   HOH B . 
E 3 HOH   83  283 22   HOH   HOH B . 
E 3 HOH   84  284 175  HOH   HOH B . 
E 3 HOH   85  285 106  HOH   HOH B . 
E 3 HOH   86  286 235  HOH   HOH B . 
E 3 HOH   87  287 13   HOH   HOH B . 
E 3 HOH   88  288 137  HOH   HOH B . 
E 3 HOH   89  289 297  HOH   HOH B . 
E 3 HOH   90  290 1066 HOH   HOH B . 
E 3 HOH   91  291 1305 HOH   HOH B . 
E 3 HOH   92  292 99   HOH   HOH B . 
E 3 HOH   93  293 216  HOH   HOH B . 
E 3 HOH   94  294 299  HOH   HOH B . 
E 3 HOH   95  295 89   HOH   HOH B . 
E 3 HOH   96  296 32   HOH   HOH B . 
E 3 HOH   97  297 416  HOH   HOH B . 
E 3 HOH   98  298 160  HOH   HOH B . 
E 3 HOH   99  299 112  HOH   HOH B . 
E 3 HOH   100 300 704  HOH   HOH B . 
E 3 HOH   101 301 316  HOH   HOH B . 
E 3 HOH   102 302 88   HOH   HOH B . 
E 3 HOH   103 303 387  HOH   HOH B . 
E 3 HOH   104 304 635  HOH   HOH B . 
E 3 HOH   105 305 220  HOH   HOH B . 
E 3 HOH   106 306 311  HOH   HOH B . 
E 3 HOH   107 307 48   HOH   HOH B . 
E 3 HOH   108 308 341  HOH   HOH B . 
E 3 HOH   109 309 142  HOH   HOH B . 
E 3 HOH   110 310 38   HOH   HOH B . 
E 3 HOH   111 311 1291 HOH   HOH B . 
E 3 HOH   112 312 170  HOH   HOH B . 
E 3 HOH   113 313 215  HOH   HOH B . 
E 3 HOH   114 314 101  HOH   HOH B . 
E 3 HOH   115 315 37   HOH   HOH B . 
E 3 HOH   116 316 118  HOH   HOH B . 
E 3 HOH   117 317 1285 HOH   HOH B . 
E 3 HOH   118 318 91   HOH   HOH B . 
E 3 HOH   119 319 23   HOH   HOH B . 
E 3 HOH   120 320 55   HOH   HOH B . 
E 3 HOH   121 321 100  HOH   HOH B . 
E 3 HOH   122 322 177  HOH   HOH B . 
E 3 HOH   123 323 44   HOH   HOH B . 
E 3 HOH   124 324 28   HOH   HOH B . 
E 3 HOH   125 325 182  HOH   HOH B . 
E 3 HOH   126 326 1126 HOH   HOH B . 
E 3 HOH   127 327 161  HOH   HOH B . 
E 3 HOH   128 328 1274 HOH   HOH B . 
E 3 HOH   129 329 197  HOH   HOH B . 
E 3 HOH   130 330 29   HOH   HOH B . 
E 3 HOH   131 331 334  HOH   HOH B . 
E 3 HOH   132 332 717  HOH   HOH B . 
E 3 HOH   133 333 141  HOH   HOH B . 
E 3 HOH   134 334 98   HOH   HOH B . 
E 3 HOH   135 335 1294 HOH   HOH B . 
E 3 HOH   136 336 445  HOH   HOH B . 
E 3 HOH   137 337 339  HOH   HOH B . 
E 3 HOH   138 338 65   HOH   HOH B . 
E 3 HOH   139 339 234  HOH   HOH B . 
E 3 HOH   140 340 207  HOH   HOH B . 
E 3 HOH   141 341 619  HOH   HOH B . 
E 3 HOH   142 342 1293 HOH   HOH B . 
E 3 HOH   143 343 178  HOH   HOH B . 
E 3 HOH   144 344 362  HOH   HOH B . 
E 3 HOH   145 345 960  HOH   HOH B . 
E 3 HOH   146 346 90   HOH   HOH B . 
E 3 HOH   147 347 463  HOH   HOH B . 
E 3 HOH   148 348 623  HOH   HOH B . 
E 3 HOH   149 349 191  HOH   HOH B . 
E 3 HOH   150 350 335  HOH   HOH B . 
E 3 HOH   151 351 1304 HOH   HOH B . 
E 3 HOH   152 352 304  HOH   HOH B . 
E 3 HOH   153 353 1046 HOH   HOH B . 
E 3 HOH   154 354 87   HOH   HOH B . 
E 3 HOH   155 355 1280 HOH   HOH B . 
E 3 HOH   156 356 290  HOH   HOH B . 
E 3 HOH   157 357 203  HOH   HOH B . 
E 3 HOH   158 358 541  HOH   HOH B . 
E 3 HOH   159 359 1077 HOH   HOH B . 
E 3 HOH   160 360 389  HOH   HOH B . 
E 3 HOH   161 361 479  HOH   HOH B . 
E 3 HOH   162 362 718  HOH   HOH B . 
E 3 HOH   163 363 283  HOH   HOH B . 
E 3 HOH   164 364 1072 HOH   HOH B . 
E 3 HOH   165 365 291  HOH   HOH B . 
E 3 HOH   166 366 1316 HOH   HOH B . 
E 3 HOH   167 367 898  HOH   HOH B . 
E 3 HOH   168 368 373  HOH   HOH B . 
E 3 HOH   169 369 340  HOH   HOH B . 
E 3 HOH   170 370 667  HOH   HOH B . 
E 3 HOH   171 371 190  HOH   HOH B . 
E 3 HOH   172 372 1303 HOH   HOH B . 
E 3 HOH   173 373 310  HOH   HOH B . 
E 3 HOH   174 374 615  HOH   HOH B . 
E 3 HOH   175 375 1173 HOH   HOH B . 
E 3 HOH   176 376 431  HOH   HOH B . 
E 3 HOH   177 377 149  HOH   HOH B . 
E 3 HOH   178 378 183  HOH   HOH B . 
E 3 HOH   179 379 1163 HOH   HOH B . 
E 3 HOH   180 380 1000 HOH   HOH B . 
E 3 HOH   181 381 418  HOH   HOH B . 
E 3 HOH   182 382 176  HOH   HOH B . 
E 3 HOH   183 383 424  HOH   HOH B . 
E 3 HOH   184 384 1311 HOH   HOH B . 
E 3 HOH   185 385 981  HOH   HOH B . 
E 3 HOH   186 386 491  HOH   HOH B . 
E 3 HOH   187 387 1298 HOH   HOH B . 
E 3 HOH   188 388 248  HOH   HOH B . 
E 3 HOH   189 389 265  HOH   HOH B . 
E 3 HOH   190 390 470  HOH   HOH B . 
E 3 HOH   191 391 184  HOH   HOH B . 
E 3 HOH   192 392 360  HOH   HOH B . 
E 3 HOH   193 393 410  HOH   HOH B . 
E 3 HOH   194 394 355  HOH   HOH B . 
E 3 HOH   195 395 274  HOH   HOH B . 
E 3 HOH   196 396 566  HOH   HOH B . 
E 3 HOH   197 397 314  HOH   HOH B . 
E 3 HOH   198 398 157  HOH   HOH B . 
E 3 HOH   199 399 792  HOH   HOH B . 
E 3 HOH   200 400 321  HOH   HOH B . 
E 3 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           7HCW 
_cell.length_a           88.807 
_cell.length_b           88.807 
_cell.length_c           39.576 
_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                         7HCW 
_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          7HCW 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.8 
_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   2023-04-29 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HCW 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.400 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165407 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.044 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.600 
_reflns.B_iso_Wilson_estimate        11.660 
_reflns.pdbx_redundancy              5.900 
_reflns.pdbx_Rrim_I_all              0.048 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     968818 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.000 1.020  ? 30406 7432 ? 1.186 ? ? ? 4.100 ? 0.800  ? ? ? ? ? ? 90.400 1.357 0.644 0.594 ? 
1 2 5.480 44.400 ? 6937  1094 ? 0.029 ? ? ? 6.300 ? 51.400 ? ? ? ? ? ? 99.700 0.031 0.012 0.999 ? 
# 
_refine.entry_id                                 7HCW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             39.7200 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.3100 
_refine.ls_number_reflns_obs                     165326 
_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                          0.1463 
_refine.ls_R_factor_R_work                       0.1457 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1589 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7963 
_refine.ls_number_reflns_R_work                  157363 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.1966 
_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                                62.710 
_refine.B_iso_min                                8.100 
_refine.pdbx_overall_phase_error                 17.9600 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        39.7200 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             420 
_refine_hist.number_atoms_total               2990 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.29 
_refine_hist.pdbx_B_iso_mean_solvent          29.45 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.R_factor_obs 
1.0000 1.0100  30 88.0000  4623 . 0.4087 0.3468 . 237 0.0000 4860 . 'X-RAY DIFFRACTION' . 
1.0100 1.0200  30 96.0000  5071 . 0.3329 0.3255 . 237 0.0000 5308 . 'X-RAY DIFFRACTION' . 
1.0200 1.0400  30 100.0000 5240 . 0.2976 0.3124 . 236 0.0000 5476 . 'X-RAY DIFFRACTION' . 
1.0400 1.0500  30 100.0000 5199 . 0.2613 0.2703 . 286 0.0000 5485 . 'X-RAY DIFFRACTION' . 
1.0500 1.0600  30 100.0000 5185 . 0.2519 0.2740 . 316 0.0000 5501 . 'X-RAY DIFFRACTION' . 
1.0600 1.0800  30 100.0000 5270 . 0.2272 0.2420 . 255 0.0000 5525 . 'X-RAY DIFFRACTION' . 
1.0800 1.0900  30 100.0000 5318 . 0.2017 0.2129 . 268 0.0000 5586 . 'X-RAY DIFFRACTION' . 
1.0900 1.1100  30 100.0000 5212 . 0.1791 0.2042 . 252 0.0000 5464 . 'X-RAY DIFFRACTION' . 
1.1100 1.1300  30 100.0000 5264 . 0.1677 0.1727 . 280 0.0000 5544 . 'X-RAY DIFFRACTION' . 
1.1300 1.1400  30 100.0000 5259 . 0.1528 0.1669 . 243 0.0000 5502 . 'X-RAY DIFFRACTION' . 
1.1400 1.1600  30 100.0000 5286 . 0.1438 0.1679 . 253 0.0000 5539 . 'X-RAY DIFFRACTION' . 
1.1600 1.1900  30 100.0000 5275 . 0.1351 0.1588 . 264 0.0000 5539 . 'X-RAY DIFFRACTION' . 
1.1900 1.2100  30 100.0000 5199 . 0.1268 0.1650 . 294 0.0000 5493 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 5291 . 0.1240 0.1373 . 240 0.0000 5531 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 5241 . 0.1261 0.1547 . 266 0.0000 5507 . 'X-RAY DIFFRACTION' . 
1.2600 1.2900  30 100.0000 5283 . 0.1288 0.1524 . 273 0.0000 5556 . 'X-RAY DIFFRACTION' . 
1.2900 1.3200  30 100.0000 5266 . 0.1293 0.1485 . 280 0.0000 5546 . 'X-RAY DIFFRACTION' . 
1.3200 1.3600  30 100.0000 5241 . 0.1338 0.1494 . 278 0.0000 5519 . 'X-RAY DIFFRACTION' . 
1.3600 1.4000  30 100.0000 5270 . 0.1271 0.1591 . 251 0.0000 5521 . 'X-RAY DIFFRACTION' . 
1.4000 1.4400  30 100.0000 5252 . 0.1235 0.1493 . 262 0.0000 5514 . 'X-RAY DIFFRACTION' . 
1.4400 1.4900  30 100.0000 5334 . 0.1204 0.1265 . 257 0.0000 5591 . 'X-RAY DIFFRACTION' . 
1.4900 1.5500  30 100.0000 5227 . 0.1176 0.1240 . 274 0.0000 5501 . 'X-RAY DIFFRACTION' . 
1.5500 1.6200  30 100.0000 5285 . 0.1184 0.1338 . 264 0.0000 5549 . 'X-RAY DIFFRACTION' . 
1.6200 1.7100  30 100.0000 5328 . 0.1248 0.1465 . 270 0.0000 5598 . 'X-RAY DIFFRACTION' . 
1.7100 1.8200  30 100.0000 5279 . 0.1342 0.1461 . 249 0.0000 5528 . 'X-RAY DIFFRACTION' . 
1.8200 1.9600  30 100.0000 5263 . 0.1347 0.1312 . 282 0.0000 5545 . 'X-RAY DIFFRACTION' . 
1.9600 2.1500  30 100.0000 5299 . 0.1387 0.1420 . 281 0.0000 5580 . 'X-RAY DIFFRACTION' . 
2.1500 2.4700  30 99.0000  5286 . 0.1376 0.1423 . 290 0.0000 5576 . 'X-RAY DIFFRACTION' . 
2.4700 3.1100  30 100.0000 5338 . 0.1517 0.1651 . 259 0.0000 5597 . 'X-RAY DIFFRACTION' . 
3.1100 39.7200 30 100.0000 5479 . 0.1511 0.1726 . 266 0.0000 5745 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCW 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0001444' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCW 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HCW A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCW 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 7HCW SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCW MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCW SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCW MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D 
2 1 B,E   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HCW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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  ? ? 55.89 -133.45 
2 1 SER A 128 ? B 74.70 -7.26   
3 1 HIS B 86  ? ? 57.44 -127.58 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 517 ? 5.98 . 
2 1 O ? A HOH 518 ? 6.06 . 
3 1 O ? A HOH 519 ? 7.54 . 
4 1 O ? B HOH 401 ? 6.37 . 
# 
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 
A1A6Q N2   N Y N 1   
A1A6Q C3   C N N 2   
A1A6Q C6   C Y N 3   
A1A6Q C9   C Y N 4   
A1A6Q C1   C N R 5   
A1A6Q C10  C Y N 6   
A1A6Q C2   C N N 7   
A1A6Q C4   C N S 8   
A1A6Q C5   C Y N 9   
A1A6Q C7   C Y N 10  
A1A6Q C8   C Y N 11  
A1A6Q N1   N N N 12  
A1A6Q N3   N Y N 13  
A1A6Q N4   N Y N 14  
A1A6Q O1   O N N 15  
A1A6Q O2   O N N 16  
A1A6Q H6   H N N 17  
A1A6Q H7   H N N 18  
A1A6Q H9   H N N 19  
A1A6Q H10  H N N 20  
A1A6Q H1   H N N 21  
A1A6Q H11  H N N 22  
A1A6Q H5   H N N 23  
A1A6Q H4   H N N 24  
A1A6Q H2   H N N 25  
A1A6Q H8   H N N 26  
A1A6Q H12  H N N 27  
A1A6Q H3   H N N 28  
ALA   N    N N N 29  
ALA   CA   C N S 30  
ALA   C    C N N 31  
ALA   O    O N N 32  
ALA   CB   C N N 33  
ALA   OXT  O N N 34  
ALA   H    H N N 35  
ALA   H2   H N N 36  
ALA   HA   H N N 37  
ALA   HB1  H N N 38  
ALA   HB2  H N N 39  
ALA   HB3  H N N 40  
ALA   HXT  H N N 41  
ARG   N    N N N 42  
ARG   CA   C N S 43  
ARG   C    C N N 44  
ARG   O    O N N 45  
ARG   CB   C N N 46  
ARG   CG   C N N 47  
ARG   CD   C N N 48  
ARG   NE   N N N 49  
ARG   CZ   C N N 50  
ARG   NH1  N N N 51  
ARG   NH2  N N N 52  
ARG   OXT  O N N 53  
ARG   H    H N N 54  
ARG   H2   H N N 55  
ARG   HA   H N N 56  
ARG   HB2  H N N 57  
ARG   HB3  H N N 58  
ARG   HG2  H N N 59  
ARG   HG3  H N N 60  
ARG   HD2  H N N 61  
ARG   HD3  H N N 62  
ARG   HE   H N N 63  
ARG   HH11 H N N 64  
ARG   HH12 H N N 65  
ARG   HH21 H N N 66  
ARG   HH22 H N N 67  
ARG   HXT  H N N 68  
ASN   N    N N N 69  
ASN   CA   C N S 70  
ASN   C    C N N 71  
ASN   O    O N N 72  
ASN   CB   C N N 73  
ASN   CG   C N N 74  
ASN   OD1  O N N 75  
ASN   ND2  N N N 76  
ASN   OXT  O N N 77  
ASN   H    H N N 78  
ASN   H2   H N N 79  
ASN   HA   H N N 80  
ASN   HB2  H N N 81  
ASN   HB3  H N N 82  
ASN   HD21 H N N 83  
ASN   HD22 H N N 84  
ASN   HXT  H N N 85  
ASP   N    N N N 86  
ASP   CA   C N S 87  
ASP   C    C N N 88  
ASP   O    O N N 89  
ASP   CB   C N N 90  
ASP   CG   C N N 91  
ASP   OD1  O N N 92  
ASP   OD2  O N N 93  
ASP   OXT  O N N 94  
ASP   H    H N N 95  
ASP   H2   H N N 96  
ASP   HA   H N N 97  
ASP   HB2  H N N 98  
ASP   HB3  H N N 99  
ASP   HD2  H N N 100 
ASP   HXT  H N N 101 
CYS   N    N N N 102 
CYS   CA   C N R 103 
CYS   C    C N N 104 
CYS   O    O N N 105 
CYS   CB   C N N 106 
CYS   SG   S N N 107 
CYS   OXT  O N N 108 
CYS   H    H N N 109 
CYS   H2   H N N 110 
CYS   HA   H N N 111 
CYS   HB2  H N N 112 
CYS   HB3  H N N 113 
CYS   HG   H N N 114 
CYS   HXT  H N N 115 
GLN   N    N N N 116 
GLN   CA   C N S 117 
GLN   C    C N N 118 
GLN   O    O N N 119 
GLN   CB   C N N 120 
GLN   CG   C N N 121 
GLN   CD   C N N 122 
GLN   OE1  O N N 123 
GLN   NE2  N N N 124 
GLN   OXT  O N N 125 
GLN   H    H N N 126 
GLN   H2   H N N 127 
GLN   HA   H N N 128 
GLN   HB2  H N N 129 
GLN   HB3  H N N 130 
GLN   HG2  H N N 131 
GLN   HG3  H N N 132 
GLN   HE21 H N N 133 
GLN   HE22 H N N 134 
GLN   HXT  H N N 135 
GLU   N    N N N 136 
GLU   CA   C N S 137 
GLU   C    C N N 138 
GLU   O    O N N 139 
GLU   CB   C N N 140 
GLU   CG   C N N 141 
GLU   CD   C N N 142 
GLU   OE1  O N N 143 
GLU   OE2  O N N 144 
GLU   OXT  O N N 145 
GLU   H    H N N 146 
GLU   H2   H N N 147 
GLU   HA   H N N 148 
GLU   HB2  H N N 149 
GLU   HB3  H N N 150 
GLU   HG2  H N N 151 
GLU   HG3  H N N 152 
GLU   HE2  H N N 153 
GLU   HXT  H N N 154 
GLY   N    N N N 155 
GLY   CA   C N N 156 
GLY   C    C N N 157 
GLY   O    O N N 158 
GLY   OXT  O N N 159 
GLY   H    H N N 160 
GLY   H2   H N N 161 
GLY   HA2  H N N 162 
GLY   HA3  H N N 163 
GLY   HXT  H N N 164 
HIS   N    N N N 165 
HIS   CA   C N S 166 
HIS   C    C N N 167 
HIS   O    O N N 168 
HIS   CB   C N N 169 
HIS   CG   C Y N 170 
HIS   ND1  N Y N 171 
HIS   CD2  C Y N 172 
HIS   CE1  C Y N 173 
HIS   NE2  N Y N 174 
HIS   OXT  O N N 175 
HIS   H    H N N 176 
HIS   H2   H N N 177 
HIS   HA   H N N 178 
HIS   HB2  H N N 179 
HIS   HB3  H N N 180 
HIS   HD1  H N N 181 
HIS   HD2  H N N 182 
HIS   HE1  H N N 183 
HIS   HE2  H N N 184 
HIS   HXT  H N N 185 
HOH   O    O N N 186 
HOH   H1   H N N 187 
HOH   H2   H N N 188 
ILE   N    N N N 189 
ILE   CA   C N S 190 
ILE   C    C N N 191 
ILE   O    O N N 192 
ILE   CB   C N S 193 
ILE   CG1  C N N 194 
ILE   CG2  C N N 195 
ILE   CD1  C N N 196 
ILE   OXT  O N N 197 
ILE   H    H N N 198 
ILE   H2   H N N 199 
ILE   HA   H N N 200 
ILE   HB   H N N 201 
ILE   HG12 H N N 202 
ILE   HG13 H N N 203 
ILE   HG21 H N N 204 
ILE   HG22 H N N 205 
ILE   HG23 H N N 206 
ILE   HD11 H N N 207 
ILE   HD12 H N N 208 
ILE   HD13 H N N 209 
ILE   HXT  H N N 210 
LEU   N    N N N 211 
LEU   CA   C N S 212 
LEU   C    C N N 213 
LEU   O    O N N 214 
LEU   CB   C N N 215 
LEU   CG   C N N 216 
LEU   CD1  C N N 217 
LEU   CD2  C N N 218 
LEU   OXT  O N N 219 
LEU   H    H N N 220 
LEU   H2   H N N 221 
LEU   HA   H N N 222 
LEU   HB2  H N N 223 
LEU   HB3  H N N 224 
LEU   HG   H N N 225 
LEU   HD11 H N N 226 
LEU   HD12 H N N 227 
LEU   HD13 H N N 228 
LEU   HD21 H N N 229 
LEU   HD22 H N N 230 
LEU   HD23 H N N 231 
LEU   HXT  H N N 232 
LYS   N    N N N 233 
LYS   CA   C N S 234 
LYS   C    C N N 235 
LYS   O    O N N 236 
LYS   CB   C N N 237 
LYS   CG   C N N 238 
LYS   CD   C N N 239 
LYS   CE   C N N 240 
LYS   NZ   N N N 241 
LYS   OXT  O N N 242 
LYS   H    H N N 243 
LYS   H2   H N N 244 
LYS   HA   H N N 245 
LYS   HB2  H N N 246 
LYS   HB3  H N N 247 
LYS   HG2  H N N 248 
LYS   HG3  H N N 249 
LYS   HD2  H N N 250 
LYS   HD3  H N N 251 
LYS   HE2  H N N 252 
LYS   HE3  H N N 253 
LYS   HZ1  H N N 254 
LYS   HZ2  H N N 255 
LYS   HZ3  H N N 256 
LYS   HXT  H N N 257 
MET   N    N N N 258 
MET   CA   C N S 259 
MET   C    C N N 260 
MET   O    O N N 261 
MET   CB   C N N 262 
MET   CG   C N N 263 
MET   SD   S N N 264 
MET   CE   C N N 265 
MET   OXT  O N N 266 
MET   H    H N N 267 
MET   H2   H N N 268 
MET   HA   H N N 269 
MET   HB2  H N N 270 
MET   HB3  H N N 271 
MET   HG2  H N N 272 
MET   HG3  H N N 273 
MET   HE1  H N N 274 
MET   HE2  H N N 275 
MET   HE3  H N N 276 
MET   HXT  H N N 277 
PHE   N    N N N 278 
PHE   CA   C N S 279 
PHE   C    C N N 280 
PHE   O    O N N 281 
PHE   CB   C N N 282 
PHE   CG   C Y N 283 
PHE   CD1  C Y N 284 
PHE   CD2  C Y N 285 
PHE   CE1  C Y N 286 
PHE   CE2  C Y N 287 
PHE   CZ   C Y N 288 
PHE   OXT  O N N 289 
PHE   H    H N N 290 
PHE   H2   H N N 291 
PHE   HA   H N N 292 
PHE   HB2  H N N 293 
PHE   HB3  H N N 294 
PHE   HD1  H N N 295 
PHE   HD2  H N N 296 
PHE   HE1  H N N 297 
PHE   HE2  H N N 298 
PHE   HZ   H N N 299 
PHE   HXT  H N N 300 
PRO   N    N N N 301 
PRO   CA   C N S 302 
PRO   C    C N N 303 
PRO   O    O N N 304 
PRO   CB   C N N 305 
PRO   CG   C N N 306 
PRO   CD   C N N 307 
PRO   OXT  O N N 308 
PRO   H    H N N 309 
PRO   HA   H N N 310 
PRO   HB2  H N N 311 
PRO   HB3  H N N 312 
PRO   HG2  H N N 313 
PRO   HG3  H N N 314 
PRO   HD2  H N N 315 
PRO   HD3  H N N 316 
PRO   HXT  H N N 317 
SER   N    N N N 318 
SER   CA   C N S 319 
SER   C    C N N 320 
SER   O    O N N 321 
SER   CB   C N N 322 
SER   OG   O N N 323 
SER   OXT  O N N 324 
SER   H    H N N 325 
SER   H2   H N N 326 
SER   HA   H N N 327 
SER   HB2  H N N 328 
SER   HB3  H N N 329 
SER   HG   H N N 330 
SER   HXT  H N N 331 
THR   N    N N N 332 
THR   CA   C N S 333 
THR   C    C N N 334 
THR   O    O N N 335 
THR   CB   C N R 336 
THR   OG1  O N N 337 
THR   CG2  C N N 338 
THR   OXT  O N N 339 
THR   H    H N N 340 
THR   H2   H N N 341 
THR   HA   H N N 342 
THR   HB   H N N 343 
THR   HG1  H N N 344 
THR   HG21 H N N 345 
THR   HG22 H N N 346 
THR   HG23 H N N 347 
THR   HXT  H N N 348 
TYR   N    N N N 349 
TYR   CA   C N S 350 
TYR   C    C N N 351 
TYR   O    O N N 352 
TYR   CB   C N N 353 
TYR   CG   C Y N 354 
TYR   CD1  C Y N 355 
TYR   CD2  C Y N 356 
TYR   CE1  C Y N 357 
TYR   CE2  C Y N 358 
TYR   CZ   C Y N 359 
TYR   OH   O N N 360 
TYR   OXT  O N N 361 
TYR   H    H N N 362 
TYR   H2   H N N 363 
TYR   HA   H N N 364 
TYR   HB2  H N N 365 
TYR   HB3  H N N 366 
TYR   HD1  H N N 367 
TYR   HD2  H N N 368 
TYR   HE1  H N N 369 
TYR   HE2  H N N 370 
TYR   HH   H N N 371 
TYR   HXT  H N N 372 
VAL   N    N N N 373 
VAL   CA   C N S 374 
VAL   C    C N N 375 
VAL   O    O N N 376 
VAL   CB   C N N 377 
VAL   CG1  C N N 378 
VAL   CG2  C N N 379 
VAL   OXT  O N N 380 
VAL   H    H N N 381 
VAL   H2   H N N 382 
VAL   HA   H N N 383 
VAL   HB   H N N 384 
VAL   HG11 H N N 385 
VAL   HG12 H N N 386 
VAL   HG13 H N N 387 
VAL   HG21 H N N 388 
VAL   HG22 H N N 389 
VAL   HG23 H N N 390 
VAL   HXT  H N N 391 
# 
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 
A1A6Q O2  C2   sing N N 1   
A1A6Q O2  C3   sing N N 2   
A1A6Q C2  C1   sing N N 3   
A1A6Q C3  C4   sing N N 4   
A1A6Q O1  C1   sing N N 5   
A1A6Q C1  C4   sing N N 6   
A1A6Q C4  N1   sing N N 7   
A1A6Q N1  C5   sing N N 8   
A1A6Q C5  N2   doub Y N 9   
A1A6Q C5  C8   sing Y N 10  
A1A6Q C9  C8   sing Y N 11  
A1A6Q C9  C10  doub Y N 12  
A1A6Q N2  C6   sing Y N 13  
A1A6Q C8  C7   doub Y N 14  
A1A6Q C10 N4   sing Y N 15  
A1A6Q C6  N3   doub Y N 16  
A1A6Q C7  N4   sing Y N 17  
A1A6Q C7  N3   sing Y N 18  
A1A6Q C3  H6   sing N N 19  
A1A6Q C3  H7   sing N N 20  
A1A6Q C6  H9   sing N N 21  
A1A6Q C9  H10  sing N N 22  
A1A6Q C1  H1   sing N N 23  
A1A6Q C10 H11  sing N N 24  
A1A6Q C2  H5   sing N N 25  
A1A6Q C2  H4   sing N N 26  
A1A6Q C4  H2   sing N N 27  
A1A6Q N1  H8   sing N N 28  
A1A6Q N4  H12  sing N N 29  
A1A6Q O1  H3   sing N N 30  
ALA   N   CA   sing N N 31  
ALA   N   H    sing N N 32  
ALA   N   H2   sing N N 33  
ALA   CA  C    sing N N 34  
ALA   CA  CB   sing N N 35  
ALA   CA  HA   sing N N 36  
ALA   C   O    doub N N 37  
ALA   C   OXT  sing N N 38  
ALA   CB  HB1  sing N N 39  
ALA   CB  HB2  sing N N 40  
ALA   CB  HB3  sing N N 41  
ALA   OXT HXT  sing N N 42  
ARG   N   CA   sing N N 43  
ARG   N   H    sing N N 44  
ARG   N   H2   sing N N 45  
ARG   CA  C    sing N N 46  
ARG   CA  CB   sing N N 47  
ARG   CA  HA   sing N N 48  
ARG   C   O    doub N N 49  
ARG   C   OXT  sing N N 50  
ARG   CB  CG   sing N N 51  
ARG   CB  HB2  sing N N 52  
ARG   CB  HB3  sing N N 53  
ARG   CG  CD   sing N N 54  
ARG   CG  HG2  sing N N 55  
ARG   CG  HG3  sing N N 56  
ARG   CD  NE   sing N N 57  
ARG   CD  HD2  sing N N 58  
ARG   CD  HD3  sing N N 59  
ARG   NE  CZ   sing N N 60  
ARG   NE  HE   sing N N 61  
ARG   CZ  NH1  sing N N 62  
ARG   CZ  NH2  doub N N 63  
ARG   NH1 HH11 sing N N 64  
ARG   NH1 HH12 sing N N 65  
ARG   NH2 HH21 sing N N 66  
ARG   NH2 HH22 sing N N 67  
ARG   OXT HXT  sing N N 68  
ASN   N   CA   sing N N 69  
ASN   N   H    sing N N 70  
ASN   N   H2   sing N N 71  
ASN   CA  C    sing N N 72  
ASN   CA  CB   sing N N 73  
ASN   CA  HA   sing N N 74  
ASN   C   O    doub N N 75  
ASN   C   OXT  sing N N 76  
ASN   CB  CG   sing N N 77  
ASN   CB  HB2  sing N N 78  
ASN   CB  HB3  sing N N 79  
ASN   CG  OD1  doub N N 80  
ASN   CG  ND2  sing N N 81  
ASN   ND2 HD21 sing N N 82  
ASN   ND2 HD22 sing N N 83  
ASN   OXT HXT  sing N N 84  
ASP   N   CA   sing N N 85  
ASP   N   H    sing N N 86  
ASP   N   H2   sing N N 87  
ASP   CA  C    sing N N 88  
ASP   CA  CB   sing N N 89  
ASP   CA  HA   sing N N 90  
ASP   C   O    doub N N 91  
ASP   C   OXT  sing N N 92  
ASP   CB  CG   sing N N 93  
ASP   CB  HB2  sing N N 94  
ASP   CB  HB3  sing N N 95  
ASP   CG  OD1  doub N N 96  
ASP   CG  OD2  sing N N 97  
ASP   OD2 HD2  sing N N 98  
ASP   OXT HXT  sing N N 99  
CYS   N   CA   sing N N 100 
CYS   N   H    sing N N 101 
CYS   N   H2   sing N N 102 
CYS   CA  C    sing N N 103 
CYS   CA  CB   sing N N 104 
CYS   CA  HA   sing N N 105 
CYS   C   O    doub N N 106 
CYS   C   OXT  sing N N 107 
CYS   CB  SG   sing N N 108 
CYS   CB  HB2  sing N N 109 
CYS   CB  HB3  sing N N 110 
CYS   SG  HG   sing N N 111 
CYS   OXT HXT  sing N N 112 
GLN   N   CA   sing N N 113 
GLN   N   H    sing N N 114 
GLN   N   H2   sing N N 115 
GLN   CA  C    sing N N 116 
GLN   CA  CB   sing N N 117 
GLN   CA  HA   sing N N 118 
GLN   C   O    doub N N 119 
GLN   C   OXT  sing N N 120 
GLN   CB  CG   sing N N 121 
GLN   CB  HB2  sing N N 122 
GLN   CB  HB3  sing N N 123 
GLN   CG  CD   sing N N 124 
GLN   CG  HG2  sing N N 125 
GLN   CG  HG3  sing N N 126 
GLN   CD  OE1  doub N N 127 
GLN   CD  NE2  sing N N 128 
GLN   NE2 HE21 sing N N 129 
GLN   NE2 HE22 sing N N 130 
GLN   OXT HXT  sing N N 131 
GLU   N   CA   sing N N 132 
GLU   N   H    sing N N 133 
GLU   N   H2   sing N N 134 
GLU   CA  C    sing N N 135 
GLU   CA  CB   sing N N 136 
GLU   CA  HA   sing N N 137 
GLU   C   O    doub N N 138 
GLU   C   OXT  sing N N 139 
GLU   CB  CG   sing N N 140 
GLU   CB  HB2  sing N N 141 
GLU   CB  HB3  sing N N 142 
GLU   CG  CD   sing N N 143 
GLU   CG  HG2  sing N N 144 
GLU   CG  HG3  sing N N 145 
GLU   CD  OE1  doub N N 146 
GLU   CD  OE2  sing N N 147 
GLU   OE2 HE2  sing N N 148 
GLU   OXT HXT  sing N N 149 
GLY   N   CA   sing N N 150 
GLY   N   H    sing N N 151 
GLY   N   H2   sing N N 152 
GLY   CA  C    sing N N 153 
GLY   CA  HA2  sing N N 154 
GLY   CA  HA3  sing N N 155 
GLY   C   O    doub N N 156 
GLY   C   OXT  sing N N 157 
GLY   OXT HXT  sing N N 158 
HIS   N   CA   sing N N 159 
HIS   N   H    sing N N 160 
HIS   N   H2   sing N N 161 
HIS   CA  C    sing N N 162 
HIS   CA  CB   sing N N 163 
HIS   CA  HA   sing N N 164 
HIS   C   O    doub N N 165 
HIS   C   OXT  sing N N 166 
HIS   CB  CG   sing N N 167 
HIS   CB  HB2  sing N N 168 
HIS   CB  HB3  sing N N 169 
HIS   CG  ND1  sing Y N 170 
HIS   CG  CD2  doub Y N 171 
HIS   ND1 CE1  doub Y N 172 
HIS   ND1 HD1  sing N N 173 
HIS   CD2 NE2  sing Y N 174 
HIS   CD2 HD2  sing N N 175 
HIS   CE1 NE2  sing Y N 176 
HIS   CE1 HE1  sing N N 177 
HIS   NE2 HE2  sing N N 178 
HIS   OXT HXT  sing N N 179 
HOH   O   H1   sing N N 180 
HOH   O   H2   sing N N 181 
ILE   N   CA   sing N N 182 
ILE   N   H    sing N N 183 
ILE   N   H2   sing N N 184 
ILE   CA  C    sing N N 185 
ILE   CA  CB   sing N N 186 
ILE   CA  HA   sing N N 187 
ILE   C   O    doub N N 188 
ILE   C   OXT  sing N N 189 
ILE   CB  CG1  sing N N 190 
ILE   CB  CG2  sing N N 191 
ILE   CB  HB   sing N N 192 
ILE   CG1 CD1  sing N N 193 
ILE   CG1 HG12 sing N N 194 
ILE   CG1 HG13 sing N N 195 
ILE   CG2 HG21 sing N N 196 
ILE   CG2 HG22 sing N N 197 
ILE   CG2 HG23 sing N N 198 
ILE   CD1 HD11 sing N N 199 
ILE   CD1 HD12 sing N N 200 
ILE   CD1 HD13 sing N N 201 
ILE   OXT HXT  sing N N 202 
LEU   N   CA   sing N N 203 
LEU   N   H    sing N N 204 
LEU   N   H2   sing N N 205 
LEU   CA  C    sing N N 206 
LEU   CA  CB   sing N N 207 
LEU   CA  HA   sing N N 208 
LEU   C   O    doub N N 209 
LEU   C   OXT  sing N N 210 
LEU   CB  CG   sing N N 211 
LEU   CB  HB2  sing N N 212 
LEU   CB  HB3  sing N N 213 
LEU   CG  CD1  sing N N 214 
LEU   CG  CD2  sing N N 215 
LEU   CG  HG   sing N N 216 
LEU   CD1 HD11 sing N N 217 
LEU   CD1 HD12 sing N N 218 
LEU   CD1 HD13 sing N N 219 
LEU   CD2 HD21 sing N N 220 
LEU   CD2 HD22 sing N N 221 
LEU   CD2 HD23 sing N N 222 
LEU   OXT HXT  sing N N 223 
LYS   N   CA   sing N N 224 
LYS   N   H    sing N N 225 
LYS   N   H2   sing N N 226 
LYS   CA  C    sing N N 227 
LYS   CA  CB   sing N N 228 
LYS   CA  HA   sing N N 229 
LYS   C   O    doub N N 230 
LYS   C   OXT  sing N N 231 
LYS   CB  CG   sing N N 232 
LYS   CB  HB2  sing N N 233 
LYS   CB  HB3  sing N N 234 
LYS   CG  CD   sing N N 235 
LYS   CG  HG2  sing N N 236 
LYS   CG  HG3  sing N N 237 
LYS   CD  CE   sing N N 238 
LYS   CD  HD2  sing N N 239 
LYS   CD  HD3  sing N N 240 
LYS   CE  NZ   sing N N 241 
LYS   CE  HE2  sing N N 242 
LYS   CE  HE3  sing N N 243 
LYS   NZ  HZ1  sing N N 244 
LYS   NZ  HZ2  sing N N 245 
LYS   NZ  HZ3  sing N N 246 
LYS   OXT HXT  sing N N 247 
MET   N   CA   sing N N 248 
MET   N   H    sing N N 249 
MET   N   H2   sing N N 250 
MET   CA  C    sing N N 251 
MET   CA  CB   sing N N 252 
MET   CA  HA   sing N N 253 
MET   C   O    doub N N 254 
MET   C   OXT  sing N N 255 
MET   CB  CG   sing N N 256 
MET   CB  HB2  sing N N 257 
MET   CB  HB3  sing N N 258 
MET   CG  SD   sing N N 259 
MET   CG  HG2  sing N N 260 
MET   CG  HG3  sing N N 261 
MET   SD  CE   sing N N 262 
MET   CE  HE1  sing N N 263 
MET   CE  HE2  sing N N 264 
MET   CE  HE3  sing N N 265 
MET   OXT HXT  sing N N 266 
PHE   N   CA   sing N N 267 
PHE   N   H    sing N N 268 
PHE   N   H2   sing N N 269 
PHE   CA  C    sing N N 270 
PHE   CA  CB   sing N N 271 
PHE   CA  HA   sing N N 272 
PHE   C   O    doub N N 273 
PHE   C   OXT  sing N N 274 
PHE   CB  CG   sing N N 275 
PHE   CB  HB2  sing N N 276 
PHE   CB  HB3  sing N N 277 
PHE   CG  CD1  doub Y N 278 
PHE   CG  CD2  sing Y N 279 
PHE   CD1 CE1  sing Y N 280 
PHE   CD1 HD1  sing N N 281 
PHE   CD2 CE2  doub Y N 282 
PHE   CD2 HD2  sing N N 283 
PHE   CE1 CZ   doub Y N 284 
PHE   CE1 HE1  sing N N 285 
PHE   CE2 CZ   sing Y N 286 
PHE   CE2 HE2  sing N N 287 
PHE   CZ  HZ   sing N N 288 
PHE   OXT HXT  sing N N 289 
PRO   N   CA   sing N N 290 
PRO   N   CD   sing N N 291 
PRO   N   H    sing N N 292 
PRO   CA  C    sing N N 293 
PRO   CA  CB   sing N N 294 
PRO   CA  HA   sing N N 295 
PRO   C   O    doub N N 296 
PRO   C   OXT  sing N N 297 
PRO   CB  CG   sing N N 298 
PRO   CB  HB2  sing N N 299 
PRO   CB  HB3  sing N N 300 
PRO   CG  CD   sing N N 301 
PRO   CG  HG2  sing N N 302 
PRO   CG  HG3  sing N N 303 
PRO   CD  HD2  sing N N 304 
PRO   CD  HD3  sing N N 305 
PRO   OXT HXT  sing N N 306 
SER   N   CA   sing N N 307 
SER   N   H    sing N N 308 
SER   N   H2   sing N N 309 
SER   CA  C    sing N N 310 
SER   CA  CB   sing N N 311 
SER   CA  HA   sing N N 312 
SER   C   O    doub N N 313 
SER   C   OXT  sing N N 314 
SER   CB  OG   sing N N 315 
SER   CB  HB2  sing N N 316 
SER   CB  HB3  sing N N 317 
SER   OG  HG   sing N N 318 
SER   OXT HXT  sing N N 319 
THR   N   CA   sing N N 320 
THR   N   H    sing N N 321 
THR   N   H2   sing N N 322 
THR   CA  C    sing N N 323 
THR   CA  CB   sing N N 324 
THR   CA  HA   sing N N 325 
THR   C   O    doub N N 326 
THR   C   OXT  sing N N 327 
THR   CB  OG1  sing N N 328 
THR   CB  CG2  sing N N 329 
THR   CB  HB   sing N N 330 
THR   OG1 HG1  sing N N 331 
THR   CG2 HG21 sing N N 332 
THR   CG2 HG22 sing N N 333 
THR   CG2 HG23 sing N N 334 
THR   OXT HXT  sing N N 335 
TYR   N   CA   sing N N 336 
TYR   N   H    sing N N 337 
TYR   N   H2   sing N N 338 
TYR   CA  C    sing N N 339 
TYR   CA  CB   sing N N 340 
TYR   CA  HA   sing N N 341 
TYR   C   O    doub N N 342 
TYR   C   OXT  sing N N 343 
TYR   CB  CG   sing N N 344 
TYR   CB  HB2  sing N N 345 
TYR   CB  HB3  sing N N 346 
TYR   CG  CD1  doub Y N 347 
TYR   CG  CD2  sing Y N 348 
TYR   CD1 CE1  sing Y N 349 
TYR   CD1 HD1  sing N N 350 
TYR   CD2 CE2  doub Y N 351 
TYR   CD2 HD2  sing N N 352 
TYR   CE1 CZ   doub Y N 353 
TYR   CE1 HE1  sing N N 354 
TYR   CE2 CZ   sing Y N 355 
TYR   CE2 HE2  sing N N 356 
TYR   CZ  OH   sing N N 357 
TYR   OH  HH   sing N N 358 
TYR   OXT HXT  sing N N 359 
VAL   N   CA   sing N N 360 
VAL   N   H    sing N N 361 
VAL   N   H2   sing N N 362 
VAL   CA  C    sing N N 363 
VAL   CA  CB   sing N N 364 
VAL   CA  HA   sing N N 365 
VAL   C   O    doub N N 366 
VAL   C   OXT  sing N N 367 
VAL   CB  CG1  sing N N 368 
VAL   CB  CG2  sing N N 369 
VAL   CB  HB   sing N N 370 
VAL   CG1 HG11 sing N N 371 
VAL   CG1 HG12 sing N N 372 
VAL   CG1 HG13 sing N N 373 
VAL   CG2 HG21 sing N N 374 
VAL   CG2 HG22 sing N N 375 
VAL   CG2 HG23 sing N N 376 
VAL   OXT HXT  sing N N 377 
# 
_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                    7HCW 
_atom_sites.fract_transf_matrix[1][1]   0.011260 
_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]   0.011260 
_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]   0.025268 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.697 -16.329 22.274  0.84 48.12 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.640 -16.309 22.323  0.16 46.99 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.735 -15.246 22.441  0.84 47.70 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.707 -15.205 22.515  0.16 46.74 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.392 -13.903 22.139  0.84 46.11 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.376 -13.880 22.175  0.16 45.64 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.510 -13.636 22.580  0.84 46.31 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.487 -13.602 22.626  0.16 45.89 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.108 -15.267 23.851  0.84 48.45 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.146 -15.190 23.950  0.16 47.31 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.105 -14.130 24.011  0.84 48.77 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.169 -14.035 24.127  0.16 47.58 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.441 -16.610 24.115  0.84 48.69 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.474 -16.516 24.272  0.16 47.53 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.016 -15.366 21.805  0.84 57.23 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.958 -15.316 21.913  0.16 56.08 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.806 -15.146 24.513  0.84 58.13 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.876 -15.064 24.576  0.16 56.77 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.592 -14.274 24.822  0.84 58.52 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.694 -14.151 24.965  0.16 57.10 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.584 -13.289 24.069  0.84 58.52 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.662 -13.200 24.141  0.16 57.10 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.511 -14.123 23.244  0.84 58.52 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.540 -14.038 23.388  0.16 57.10 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.999 -16.579 24.978  0.84 58.42 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.065 -16.456 25.149  0.16 57.03 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.790 -16.782 23.416  0.84 58.42 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.796 -16.695 23.602  0.16 57.03 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.118 -17.304 24.114  0.84 58.42 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.142 -17.219 24.265  0.16 57.03 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.695 -13.067 21.371  1.00 43.94 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.152 -11.725 21.037  1.00 39.86 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.009 -10.742 21.272  1.00 36.52 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.882 -11.131 21.595  1.00 36.35 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.713 -11.645 19.609  1.00 38.95 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.693 -12.011 18.554  1.00 38.02 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.596 -11.456 18.516  1.00 37.41 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.053 -12.952 17.685  1.00 37.63 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.934 -13.265 21.019  0.84 52.73 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.943 -13.275 21.005  0.16 52.73 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.871 -11.485 21.635  1.00 47.83 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 20.007 -10.736 19.435  1.00 46.74 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.461 -12.256 19.529  1.00 46.74 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.512 -13.196 17.062  1.00 45.15 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.831 -13.318 17.745  1.00 45.15 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.306 -9.455  21.107  1.00 32.98 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.390 -8.394  21.504  1.00 29.75 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.469 -7.925  20.382  1.00 25.74 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.708 -6.974  20.586  1.00 26.45 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.172 -7.207  22.080  1.00 30.61 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.068 -6.676  21.122  1.00 31.28 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 19.038 -9.169  20.757  1.00 39.57 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.826 -8.727  22.214  1.00 35.70 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.549 -6.512  22.347  1.00 36.73 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.681 -7.506  22.853  1.00 36.73 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.491 -6.024  21.453  1.00 37.53 ?  5   SER   A HG   1 
ATOM   57   N N    A PHE   A 1 6   ? 16.511 -8.564  19.215  0.84 22.77 ?  6   PHE   A N    1 
ATOM   58   N N    B PHE   A 1 6   ? 16.505 -8.559  19.215  0.16 24.11 ?  6   PHE   A N    1 
ATOM   59   C CA   A PHE   A 1 6   ? 15.618 -8.188  18.124  0.84 20.51 ?  6   PHE   A CA   1 
ATOM   60   C CA   B PHE   A 1 6   ? 15.556 -8.209  18.168  0.16 22.36 ?  6   PHE   A CA   1 
ATOM   61   C C    A PHE   A 1 6   ? 14.181 -8.556  18.479  0.84 20.98 ?  6   PHE   A C    1 
ATOM   62   C C    B PHE   A 1 6   ? 14.149 -8.602  18.599  0.16 21.66 ?  6   PHE   A C    1 
ATOM   63   O O    A PHE   A 1 6   ? 13.909 -9.679  18.910  0.84 22.08 ?  6   PHE   A O    1 
ATOM   64   O O    B PHE   A 1 6   ? 13.937 -9.671  19.178  0.16 22.00 ?  6   PHE   A O    1 
ATOM   65   C CB   A PHE   A 1 6   ? 16.037 -8.898  16.839  0.84 18.71 ?  6   PHE   A CB   1 
ATOM   66   C CB   B PHE   A 1 6   ? 15.920 -8.914  16.864  0.16 21.28 ?  6   PHE   A CB   1 
ATOM   67   C CG   A PHE   A 1 6   ? 17.306 -8.355  16.230  0.84 17.68 ?  6   PHE   A CG   1 
ATOM   68   C CG   B PHE   A 1 6   ? 17.198 -8.422  16.245  0.16 20.34 ?  6   PHE   A CG   1 
ATOM   69   C CD1  A PHE   A 1 6   ? 17.300 -7.154  15.541  0.84 17.23 ?  6   PHE   A CD1  1 
ATOM   70   C CD1  B PHE   A 1 6   ? 17.237 -7.209  15.577  0.16 19.92 ?  6   PHE   A CD1  1 
ATOM   71   C CD2  A PHE   A 1 6   ? 18.497 -9.053  16.341  0.84 18.19 ?  6   PHE   A CD2  1 
ATOM   72   C CD2  B PHE   A 1 6   ? 18.357 -9.175  16.325  0.16 20.01 ?  6   PHE   A CD2  1 
ATOM   73   C CE1  A PHE   A 1 6   ? 18.463 -6.655  14.981  0.84 17.40 ?  6   PHE   A CE1  1 
ATOM   74   C CE1  B PHE   A 1 6   ? 18.411 -6.755  15.005  0.16 19.70 ?  6   PHE   A CE1  1 
ATOM   75   C CE2  A PHE   A 1 6   ? 19.659 -8.564  15.781  0.84 18.43 ?  6   PHE   A CE2  1 
ATOM   76   C CE2  B PHE   A 1 6   ? 19.532 -8.726  15.755  0.16 19.78 ?  6   PHE   A CE2  1 
ATOM   77   C CZ   A PHE   A 1 6   ? 19.643 -7.363  15.098  0.84 17.76 ?  6   PHE   A CZ   1 
ATOM   78   C CZ   B PHE   A 1 6   ? 19.559 -7.515  15.094  0.16 19.66 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 17.041 -9.216  19.036  0.84 27.32 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 17.056 -9.186  19.012  0.16 28.93 ?  6   PHE   A H    1 
ATOM   81   H HA   A PHE   A 1 6   ? 15.666 -7.235  17.982  0.84 24.61 ?  6   PHE   A HA   1 
ATOM   82   H HA   B PHE   A 1 6   ? 15.577 -7.252  18.020  0.16 26.83 ?  6   PHE   A HA   1 
ATOM   83   H HB2  A PHE   A 1 6   ? 16.179 -9.841  17.032  0.84 22.45 ?  6   PHE   A HB2  1 
ATOM   84   H HB2  B PHE   A 1 6   ? 16.020 -9.863  17.039  0.16 25.54 ?  6   PHE   A HB2  1 
ATOM   85   H HB3  A PHE   A 1 6   ? 15.329 -8.803  16.185  0.84 22.45 ?  6   PHE   A HB3  1 
ATOM   86   H HB3  B PHE   A 1 6   ? 15.205 -8.772  16.224  0.16 25.54 ?  6   PHE   A HB3  1 
ATOM   87   H HD1  A PHE   A 1 6   ? 16.506 -6.677  15.460  0.84 20.67 ?  6   PHE   A HD1  1 
ATOM   88   H HD1  B PHE   A 1 6   ? 16.466 -6.693  15.515  0.16 23.90 ?  6   PHE   A HD1  1 
ATOM   89   H HD2  A PHE   A 1 6   ? 18.512 -9.863  16.801  0.84 21.83 ?  6   PHE   A HD2  1 
ATOM   90   H HD2  B PHE   A 1 6   ? 18.344 -9.991  16.770  0.16 24.02 ?  6   PHE   A HD2  1 
ATOM   91   H HE1  A PHE   A 1 6   ? 18.449 -5.846  14.520  0.84 20.88 ?  6   PHE   A HE1  1 
ATOM   92   H HE1  B PHE   A 1 6   ? 18.426 -5.938  14.560  0.16 23.64 ?  6   PHE   A HE1  1 
ATOM   93   H HE2  A PHE   A 1 6   ? 20.455 -9.037  15.865  0.84 22.11 ?  6   PHE   A HE2  1 
ATOM   94   H HE2  B PHE   A 1 6   ? 20.305 -9.240  15.817  0.16 23.73 ?  6   PHE   A HE2  1 
ATOM   95   H HZ   A PHE   A 1 6   ? 20.425 -7.025  14.723  0.84 21.31 ?  6   PHE   A HZ   1 
ATOM   96   H HZ   B PHE   A 1 6   ? 20.350 -7.211  14.710  0.16 23.59 ?  6   PHE   A HZ   1 
ATOM   97   N N    A SER   A 1 7   ? 13.256 -7.614  18.284  0.84 20.41 ?  7   SER   A N    1 
ATOM   98   N N    B SER   A 1 7   ? 13.182 -7.730  18.320  0.16 20.69 ?  7   SER   A N    1 
ATOM   99   C CA   A SER   A 1 7   ? 11.885 -7.758  18.761  0.84 21.21 ?  7   SER   A CA   1 
ATOM   100  C CA   B SER   A 1 7   ? 11.819 -7.931  18.789  0.16 19.93 ?  7   SER   A CA   1 
ATOM   101  C C    A SER   A 1 7   ? 10.885 -7.498  17.641  0.84 19.83 ?  7   SER   A C    1 
ATOM   102  C C    B SER   A 1 7   ? 10.833 -7.469  17.726  0.16 18.81 ?  7   SER   A C    1 
ATOM   103  O O    A SER   A 1 7   ? 11.085 -6.609  16.809  0.84 19.98 ?  7   SER   A O    1 
ATOM   104  O O    B SER   A 1 7   ? 11.119 -6.559  16.943  0.16 18.78 ?  7   SER   A O    1 
ATOM   105  C CB   A SER   A 1 7   ? 11.625 -6.784  19.920  0.84 23.16 ?  7   SER   A CB   1 
ATOM   106  C CB   B SER   A 1 7   ? 11.568 -7.180  20.103  0.16 20.30 ?  7   SER   A CB   1 
ATOM   107  O OG   A SER   A 1 7   ? 10.277 -6.842  20.339  0.84 24.89 ?  7   SER   A OG   1 
ATOM   108  O OG   B SER   A 1 7   ? 10.423 -7.689  20.764  0.16 20.61 ?  7   SER   A OG   1 
ATOM   109  H H    A SER   A 1 7   ? 13.406 -6.875  17.867  0.84 24.49 ?  7   SER   A H    1 
ATOM   110  H H    B SER   A 1 7   ? 13.292 -7.013  17.853  0.16 24.83 ?  7   SER   A H    1 
ATOM   111  H HA   A SER   A 1 7   ? 11.749 -8.660  19.084  0.84 25.44 ?  7   SER   A HA   1 
ATOM   112  H HA   B SER   A 1 7   ? 11.668 -8.873  18.945  0.16 23.91 ?  7   SER   A HA   1 
ATOM   113  H HB2  A SER   A 1 7   ? 12.200 -7.021  20.667  0.84 27.79 ?  7   SER   A HB2  1 
ATOM   114  H HB2  B SER   A 1 7   ? 12.343 -7.286  20.680  0.16 24.36 ?  7   SER   A HB2  1 
ATOM   115  H HB3  A SER   A 1 7   ? 11.822 -5.881  19.627  0.84 27.79 ?  7   SER   A HB3  1 
ATOM   116  H HB3  B SER   A 1 7   ? 11.428 -6.239  19.911  0.16 24.36 ?  7   SER   A HB3  1 
ATOM   117  H HG   A SER   A 1 7   ? 10.148 -6.311  20.977  0.84 29.87 ?  7   SER   A HG   1 
ATOM   118  H HG   B SER   A 1 7   ? 10.535 -8.501  20.947  0.16 24.73 ?  7   SER   A HG   1 
ATOM   119  N N    A GLY   A 1 8   ? 9.804  -8.278  17.625  0.84 19.18 ?  8   GLY   A N    1 
ATOM   120  N N    B GLY   A 1 8   ? 9.665  -8.111  17.708  0.16 17.89 ?  8   GLY   A N    1 
ATOM   121  C CA   A GLY   A 1 8   ? 8.712  -8.025  16.707  0.84 18.52 ?  8   GLY   A CA   1 
ATOM   122  C CA   B GLY   A 1 8   ? 8.640  -7.805  16.732  0.16 17.13 ?  8   GLY   A CA   1 
ATOM   123  C C    A GLY   A 1 8   ? 8.896  -8.531  15.296  0.84 17.59 ?  8   GLY   A C    1 
ATOM   124  C C    B GLY   A 1 8   ? 8.888  -8.368  15.354  0.16 16.29 ?  8   GLY   A C    1 
ATOM   125  O O    A GLY   A 1 8   ? 8.148  -8.116  14.404  0.84 18.31 ?  8   GLY   A O    1 
ATOM   126  O O    B GLY   A 1 8   ? 8.173  -8.001  14.414  0.16 16.45 ?  8   GLY   A O    1 
ATOM   127  H H    A GLY   A 1 8   ? 9.689  -8.954  18.139  0.84 23.01 ?  8   GLY   A H    1 
ATOM   128  H H    B GLY   A 1 8   ? 9.447  -8.736  18.256  0.16 21.46 ?  8   GLY   A H    1 
ATOM   129  H HA2  A GLY   A 1 8   ? 7.909  -8.435  17.063  0.84 22.22 ?  8   GLY   A HA2  1 
ATOM   130  H HA2  B GLY   A 1 8   ? 7.790  -8.150  17.048  0.16 20.55 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  A GLY   A 1 8   ? 8.561  -7.068  16.659  0.84 22.22 ?  8   GLY   A HA3  1 
ATOM   132  H HA3  B GLY   A 1 8   ? 8.561  -6.843  16.647  0.16 20.55 ?  8   GLY   A HA3  1 
ATOM   133  N N    A TYR   A 1 9   ? 9.862  -9.413  15.055  0.84 16.10 ?  9   TYR   A N    1 
ATOM   134  N N    B TYR   A 1 9   ? 9.877  -9.244  15.200  0.16 15.38 ?  9   TYR   A N    1 
ATOM   135  C CA   A TYR   A 1 9   ? 10.100 -9.951  13.723  0.84 14.83 ?  9   TYR   A CA   1 
ATOM   136  C CA   B TYR   A 1 9   ? 10.235 -9.792  13.900  0.16 14.54 ?  9   TYR   A CA   1 
ATOM   137  C C    A TYR   A 1 9   ? 9.211  -11.160 13.454  0.84 14.66 ?  9   TYR   A C    1 
ATOM   138  C C    B TYR   A 1 9   ? 9.433  -11.053 13.612  0.16 14.13 ?  9   TYR   A C    1 
ATOM   139  O O    A TYR   A 1 9   ? 8.899  -11.949 14.351  0.84 16.05 ?  9   TYR   A O    1 
ATOM   140  O O    B TYR   A 1 9   ? 9.344  -11.950 14.458  0.16 14.36 ?  9   TYR   A O    1 
ATOM   141  C CB   A TYR   A 1 9   ? 11.572 -10.360 13.543  0.84 14.87 ?  9   TYR   A CB   1 
ATOM   142  C CB   B TYR   A 1 9   ? 11.730 -10.106 13.847  0.16 14.27 ?  9   TYR   A CB   1 
ATOM   143  C CG   A TYR   A 1 9   ? 12.500 -9.177  13.388  0.84 14.88 ?  9   TYR   A CG   1 
ATOM   144  C CG   B TYR   A 1 9   ? 12.590 -8.878  13.662  0.16 14.03 ?  9   TYR   A CG   1 
ATOM   145  C CD1  A TYR   A 1 9   ? 12.833 -8.394  14.481  0.84 15.15 ?  9   TYR   A CD1  1 
ATOM   146  C CD1  B TYR   A 1 9   ? 12.828 -8.009  14.718  0.16 14.04 ?  9   TYR   A CD1  1 
ATOM   147  C CD2  A TYR   A 1 9   ? 13.014 -8.833  12.148  0.84 14.69 ?  9   TYR   A CD2  1 
ATOM   148  C CD2  B TYR   A 1 9   ? 13.151 -8.581  12.428  0.16 13.68 ?  9   TYR   A CD2  1 
ATOM   149  C CE1  A TYR   A 1 9   ? 13.654 -7.294  14.349  0.84 15.82 ?  9   TYR   A CE1  1 
ATOM   150  C CE1  B TYR   A 1 9   ? 13.605 -6.881  14.552  0.16 13.88 ?  9   TYR   A CE1  1 
ATOM   151  C CE2  A TYR   A 1 9   ? 13.838 -7.736  12.002  0.84 15.09 ?  9   TYR   A CE2  1 
ATOM   152  C CE2  B TYR   A 1 9   ? 13.930 -7.454  12.251  0.16 13.60 ?  9   TYR   A CE2  1 
ATOM   153  C CZ   A TYR   A 1 9   ? 14.151 -6.965  13.105  0.84 15.79 ?  9   TYR   A CZ   1 
ATOM   154  C CZ   B TYR   A 1 9   ? 14.154 -6.607  13.318  0.16 13.73 ?  9   TYR   A CZ   1 
ATOM   155  O OH   A TYR   A 1 9   ? 14.968 -5.875  12.956  0.84 17.09 ?  9   TYR   A OH   1 
ATOM   156  O OH   B TYR   A 1 9   ? 14.928 -5.482  13.150  0.16 14.14 ?  9   TYR   A OH   1 
ATOM   157  H H    A TYR   A 1 9   ? 10.402 -9.717  15.651  0.84 19.32 ?  9   TYR   A H    1 
ATOM   158  H H    B TYR   A 1 9   ? 10.367 -9.533  15.843  0.16 18.45 ?  9   TYR   A H    1 
ATOM   159  H HA   A TYR   A 1 9   ? 9.898  -9.269  13.061  0.84 17.79 ?  9   TYR   A HA   1 
ATOM   160  H HA   B TYR   A 1 9   ? 10.034 -9.143  13.212  0.16 17.44 ?  9   TYR   A HA   1 
ATOM   161  H HB2  A TYR   A 1 9   ? 11.856 -10.871 14.316  0.84 17.84 ?  9   TYR   A HB2  1 
ATOM   162  H HB2  B TYR   A 1 9   ? 11.993 -10.540 14.674  0.16 17.12 ?  9   TYR   A HB2  1 
ATOM   163  H HB3  A TYR   A 1 9   ? 11.643 -10.904 12.742  0.84 17.84 ?  9   TYR   A HB3  1 
ATOM   164  H HB3  B TYR   A 1 9   ? 11.890 -10.701 13.099  0.16 17.12 ?  9   TYR   A HB3  1 
ATOM   165  H HD1  A TYR   A 1 9   ? 12.478 -8.611  15.318  0.84 18.18 ?  9   TYR   A HD1  1 
ATOM   166  H HD1  B TYR   A 1 9   ? 12.457 -8.193  15.551  0.16 16.85 ?  9   TYR   A HD1  1 
ATOM   167  H HD2  A TYR   A 1 9   ? 12.797 -9.348  11.402  0.84 17.62 ?  9   TYR   A HD2  1 
ATOM   168  H HD2  B TYR   A 1 9   ? 13.000 -9.152  11.707  0.16 16.41 ?  9   TYR   A HD2  1 
ATOM   169  H HE1  A TYR   A 1 9   ? 13.862 -6.779  15.093  0.84 18.99 ?  9   TYR   A HE1  1 
ATOM   170  H HE1  B TYR   A 1 9   ? 13.757 -6.310  15.269  0.16 16.66 ?  9   TYR   A HE1  1 
ATOM   171  H HE2  A TYR   A 1 9   ? 14.182 -7.517  11.167  0.84 18.11 ?  9   TYR   A HE2  1 
ATOM   172  H HE2  B TYR   A 1 9   ? 14.302 -7.269  11.419  0.16 16.32 ?  9   TYR   A HE2  1 
ATOM   173  H HH   A TYR   A 1 9   ? 15.090 -5.509  13.703  0.84 20.50 ?  9   TYR   A HH   1 
ATOM   174  H HH   B TYR   A 1 9   ? 14.984 -5.063  13.876  0.16 16.97 ?  9   TYR   A HH   1 
ATOM   175  N N    A LEU   A 1 10  ? 8.822  -11.302 12.192  0.84 14.28 ?  10  LEU   A N    1 
ATOM   176  N N    B LEU   A 1 10  ? 8.863  -11.118 12.413  0.16 13.56 ?  10  LEU   A N    1 
ATOM   177  C CA   A LEU   A 1 10  ? 8.222  -12.528 11.691  0.84 13.92 ?  10  LEU   A CA   1 
ATOM   178  C CA   B LEU   A 1 10  ? 8.199  -12.327 11.949  0.16 13.17 ?  10  LEU   A CA   1 
ATOM   179  C C    A LEU   A 1 10  ? 9.352  -13.451 11.244  0.84 13.53 ?  10  LEU   A C    1 
ATOM   180  C C    B LEU   A 1 10  ? 9.256  -13.297 11.439  0.16 12.42 ?  10  LEU   A C    1 
ATOM   181  O O    A LEU   A 1 10  ? 10.335 -12.998 10.647  0.84 13.65 ?  10  LEU   A O    1 
ATOM   182  O O    B LEU   A 1 10  ? 10.052 -12.953 10.558  0.16 12.31 ?  10  LEU   A O    1 
ATOM   183  C CB   A LEU   A 1 10  ? 7.315  -12.200 10.503  0.84 15.11 ?  10  LEU   A CB   1 
ATOM   184  C CB   B LEU   A 1 10  ? 7.215  -11.990 10.833  0.16 13.48 ?  10  LEU   A CB   1 
ATOM   185  C CG   A LEU   A 1 10  ? 6.601  -13.384 9.851   0.84 17.04 ?  10  LEU   A CG   1 
ATOM   186  C CG   B LEU   A 1 10  ? 6.339  -13.160 10.377  0.16 14.02 ?  10  LEU   A CG   1 
ATOM   187  C CD1  A LEU   A 1 10  ? 5.536  -13.946 10.780  0.84 18.43 ?  10  LEU   A CD1  1 
ATOM   188  C CD1  B LEU   A 1 10  ? 5.338  -13.528 11.463  0.16 14.28 ?  10  LEU   A CD1  1 
ATOM   189  C CD2  A LEU   A 1 10  ? 6.011  -13.006 8.499   0.84 18.90 ?  10  LEU   A CD2  1 
ATOM   190  C CD2  B LEU   A 1 10  ? 5.624  -12.831 9.079   0.16 14.65 ?  10  LEU   A CD2  1 
ATOM   191  H H    A LEU   A 1 10  ? 8.907  -10.690 11.586  0.84 17.13 ?  10  LEU   A H    1 
ATOM   192  H H    B LEU   A 1 10  ? 8.847  -10.469 11.846  0.16 16.27 ?  10  LEU   A H    1 
ATOM   193  H HA   A LEU   A 1 10  ? 7.698  -12.957 12.392  0.84 16.70 ?  10  LEU   A HA   1 
ATOM   194  H HA   B LEU   A 1 10  ? 7.719  -12.741 12.684  0.16 15.81 ?  10  LEU   A HA   1 
ATOM   195  H HB2  A LEU   A 1 10  ? 6.631  -11.579 10.801  0.84 18.13 ?  10  LEU   A HB2  1 
ATOM   196  H HB2  B LEU   A 1 10  ? 6.625  -11.285 11.142  0.16 16.18 ?  10  LEU   A HB2  1 
ATOM   197  H HB3  A LEU   A 1 10  ? 7.856  -11.777 9.818   0.84 18.13 ?  10  LEU   A HB3  1 
ATOM   198  H HB3  B LEU   A 1 10  ? 7.716  -11.681 10.063  0.16 16.18 ?  10  LEU   A HB3  1 
ATOM   199  H HG   A LEU   A 1 10  ? 7.251  -14.090 9.700   0.84 20.44 ?  10  LEU   A HG   1 
ATOM   200  H HG   B LEU   A 1 10  ? 6.903  -13.933 10.219  0.16 16.83 ?  10  LEU   A HG   1 
ATOM   201  H HD11 A LEU   A 1 10  ? 5.148  -14.736 10.373  0.84 22.12 ?  10  LEU   A HD11 1 
ATOM   202  H HD11 B LEU   A 1 10  ? 4.741  -14.210 11.120  0.16 17.14 ?  10  LEU   A HD11 1 
ATOM   203  H HD12 A LEU   A 1 10  ? 5.945  -14.181 11.630  0.84 22.12 ?  10  LEU   A HD12 1 
ATOM   204  H HD12 B LEU   A 1 10  ? 5.818  -13.866 12.235  0.16 17.14 ?  10  LEU   A HD12 1 
ATOM   205  H HD13 A LEU   A 1 10  ? 4.853  -13.273 10.919  0.84 22.12 ?  10  LEU   A HD13 1 
ATOM   206  H HD13 B LEU   A 1 10  ? 4.833  -12.737 11.706  0.16 17.14 ?  10  LEU   A HD13 1 
ATOM   207  H HD21 A LEU   A 1 10  ? 5.570  -13.785 8.125   0.84 22.68 ?  10  LEU   A HD21 1 
ATOM   208  H HD21 B LEU   A 1 10  ? 5.082  -13.591 8.819   0.16 17.57 ?  10  LEU   A HD21 1 
ATOM   209  H HD22 A LEU   A 1 10  ? 5.373  -12.290 8.627   0.84 22.68 ?  10  LEU   A HD22 1 
ATOM   210  H HD22 B LEU   A 1 10  ? 5.066  -12.053 9.217   0.16 17.57 ?  10  LEU   A HD22 1 
ATOM   211  H HD23 A LEU   A 1 10  ? 6.729  -12.718 7.917   0.84 22.68 ?  10  LEU   A HD23 1 
ATOM   212  H HD23 B LEU   A 1 10  ? 6.288  -12.648 8.395   0.16 17.57 ?  10  LEU   A HD23 1 
ATOM   213  N N    A LYS   A 1 11  ? 9.225  -14.738 11.558  0.84 12.99 ?  11  LYS   A N    1 
ATOM   214  N N    B LYS   A 1 11  ? 9.268  -14.502 11.996  0.16 11.88 ?  11  LYS   A N    1 
ATOM   215  C CA   A LYS   A 1 11  ? 10.236 -15.732 11.215  0.84 13.07 ?  11  LYS   A CA   1 
ATOM   216  C CA   B LYS   A 1 11  ? 10.218 -15.521 11.576  0.16 11.52 ?  11  LYS   A CA   1 
ATOM   217  C C    A LYS   A 1 11  ? 9.892  -16.320 9.854   0.84 13.32 ?  11  LYS   A C    1 
ATOM   218  C C    B LYS   A 1 11  ? 9.822  -16.037 10.199  0.16 11.00 ?  11  LYS   A C    1 
ATOM   219  O O    A LYS   A 1 11  ? 8.827  -16.919 9.695   0.84 15.66 ?  11  LYS   A O    1 
ATOM   220  O O    B LYS   A 1 11  ? 8.691  -16.497 10.004  0.16 10.63 ?  11  LYS   A O    1 
ATOM   221  C CB   A LYS   A 1 11  ? 10.273 -16.815 12.297  0.84 13.21 ?  11  LYS   A CB   1 
ATOM   222  C CB   B LYS   A 1 11  ? 10.231 -16.654 12.600  0.16 11.74 ?  11  LYS   A CB   1 
ATOM   223  C CG   A LYS   A 1 11  ? 11.314 -17.913 12.112  0.84 13.39 ?  11  LYS   A CG   1 
ATOM   224  C CG   B LYS   A 1 11  ? 11.293 -17.720 12.365  0.16 11.91 ?  11  LYS   A CG   1 
ATOM   225  C CD   A LYS   A 1 11  ? 11.392 -18.770 13.380  0.84 14.08 ?  11  LYS   A CD   1 
ATOM   226  C CD   B LYS   A 1 11  ? 11.324 -18.720 13.517  0.16 12.22 ?  11  LYS   A CD   1 
ATOM   227  C CE   A LYS   A 1 11  ? 12.381 -19.922 13.261  0.84 14.03 ?  11  LYS   A CE   1 
ATOM   228  C CE   B LYS   A 1 11  ? 12.386 -19.793 13.318  0.16 12.37 ?  11  LYS   A CE   1 
ATOM   229  N NZ   A LYS   A 1 11  ? 13.760 -19.453 12.973  0.84 14.04 ?  11  LYS   A NZ   1 
ATOM   230  N NZ   B LYS   A 1 11  ? 13.764 -19.228 13.296  0.16 12.32 ?  11  LYS   A NZ   1 
ATOM   231  H H    A LYS   A 1 11  ? 8.537  -15.069 11.961  0.84 15.59 ?  11  LYS   A H    1 
ATOM   232  H H    B LYS   A 1 11  ? 8.732  -14.749 12.615  0.16 14.25 ?  11  LYS   A H    1 
ATOM   233  H HA   A LYS   A 1 11  ? 11.103 -15.304 11.159  0.84 15.68 ?  11  LYS   A HA   1 
ATOM   234  H HA   B LYS   A 1 11  ? 11.104 -15.136 11.519  0.16 13.82 ?  11  LYS   A HA   1 
ATOM   235  H HB2  A LYS   A 1 11  ? 10.456 -16.378 13.145  0.84 15.85 ?  11  LYS   A HB2  1 
ATOM   236  H HB2  B LYS   A 1 11  ? 10.390 -16.270 13.478  0.16 14.08 ?  11  LYS   A HB2  1 
ATOM   237  H HB3  A LYS   A 1 11  ? 9.403  -17.235 12.332  0.84 15.85 ?  11  LYS   A HB3  1 
ATOM   238  H HB3  B LYS   A 1 11  ? 9.366  -17.090 12.588  0.16 14.08 ?  11  LYS   A HB3  1 
ATOM   239  H HG2  A LYS   A 1 11  ? 11.054 -18.478 11.368  0.84 16.07 ?  11  LYS   A HG2  1 
ATOM   240  H HG2  B LYS   A 1 11  ? 11.089 -18.201 11.547  0.16 14.29 ?  11  LYS   A HG2  1 
ATOM   241  H HG3  A LYS   A 1 11  ? 12.182 -17.513 11.952  0.84 16.07 ?  11  LYS   A HG3  1 
ATOM   242  H HG3  B LYS   A 1 11  ? 12.164 -17.299 12.299  0.16 14.29 ?  11  LYS   A HG3  1 
ATOM   243  H HD2  A LYS   A 1 11  ? 11.666 -18.209 14.120  0.84 16.89 ?  11  LYS   A HD2  1 
ATOM   244  H HD2  B LYS   A 1 11  ? 11.520 -18.249 14.342  0.16 14.66 ?  11  LYS   A HD2  1 
ATOM   245  H HD3  A LYS   A 1 11  ? 10.513 -19.145 13.557  0.84 16.89 ?  11  LYS   A HD3  1 
ATOM   246  H HD3  B LYS   A 1 11  ? 10.460 -19.158 13.580  0.16 14.66 ?  11  LYS   A HD3  1 
ATOM   247  H HE2  A LYS   A 1 11  ? 12.401 -20.411 14.099  0.84 16.84 ?  11  LYS   A HE2  1 
ATOM   248  H HE2  B LYS   A 1 11  ? 12.335 -20.431 14.049  0.16 14.84 ?  11  LYS   A HE2  1 
ATOM   249  H HE3  A LYS   A 1 11  ? 12.106 -20.507 12.540  0.84 16.84 ?  11  LYS   A HE3  1 
ATOM   250  H HE3  B LYS   A 1 11  ? 12.232 -20.243 12.473  0.16 14.84 ?  11  LYS   A HE3  1 
ATOM   251  H HZ1  A LYS   A 1 11  ? 14.298 -20.149 12.838  0.84 16.85 ?  11  LYS   A HZ1  1 
ATOM   252  H HZ1  B LYS   A 1 11  ? 14.342 -19.846 13.022  0.16 14.78 ?  11  LYS   A HZ1  1 
ATOM   253  H HZ2  A LYS   A 1 11  ? 13.763 -18.941 12.244  0.84 16.85 ?  11  LYS   A HZ2  1 
ATOM   254  H HZ2  B LYS   A 1 11  ? 13.799 -18.533 12.740  0.16 14.78 ?  11  LYS   A HZ2  1 
ATOM   255  H HZ3  A LYS   A 1 11  ? 14.072 -18.978 13.659  0.84 16.85 ?  11  LYS   A HZ3  1 
ATOM   256  H HZ3  B LYS   A 1 11  ? 13.995 -18.957 14.111  0.16 14.78 ?  11  LYS   A HZ3  1 
ATOM   257  N N    A LEU   A 1 12  ? 10.775 -16.153 8.872   0.84 12.13 ?  12  LEU   A N    1 
ATOM   258  N N    B LEU   A 1 12  ? 10.736 -15.928 9.234   0.16 11.01 ?  12  LEU   A N    1 
ATOM   259  C CA   A LEU   A 1 12  ? 10.515 -16.727 7.554   0.84 12.80 ?  12  LEU   A CA   1 
ATOM   260  C CA   B LEU   A 1 12  ? 10.492 -16.447 7.892   0.16 11.42 ?  12  LEU   A CA   1 
ATOM   261  C C    A LEU   A 1 12  ? 11.104 -18.122 7.406   0.84 12.69 ?  12  LEU   A C    1 
ATOM   262  C C    B LEU   A 1 12  ? 11.035 -17.862 7.724   0.16 11.45 ?  12  LEU   A C    1 
ATOM   263  O O    A LEU   A 1 12  ? 10.479 -18.991 6.790   0.84 12.87 ?  12  LEU   A O    1 
ATOM   264  O O    B LEU   A 1 12  ? 10.320 -18.755 7.260   0.16 11.63 ?  12  LEU   A O    1 
ATOM   265  C CB   A LEU   A 1 12  ? 11.069 -15.826 6.446   0.84 13.39 ?  12  LEU   A CB   1 
ATOM   266  C CB   B LEU   A 1 12  ? 11.106 -15.522 6.834   0.16 11.78 ?  12  LEU   A CB   1 
ATOM   267  C CG   A LEU   A 1 12  ? 10.423 -14.447 6.333   0.84 14.88 ?  12  LEU   A CG   1 
ATOM   268  C CG   B LEU   A 1 12  ? 10.298 -14.297 6.404   0.16 12.10 ?  12  LEU   A CG   1 
ATOM   269  C CD1  A LEU   A 1 12  ? 11.188 -13.600 5.332   0.84 16.03 ?  12  LEU   A CD1  1 
ATOM   270  C CD1  B LEU   A 1 12  ? 10.928 -13.651 5.176   0.16 12.22 ?  12  LEU   A CD1  1 
ATOM   271  C CD2  A LEU   A 1 12  ? 8.961  -14.571 5.926   0.84 15.80 ?  12  LEU   A CD2  1 
ATOM   272  C CD2  B LEU   A 1 12  ? 8.855  -14.679 6.126   0.16 12.30 ?  12  LEU   A CD2  1 
ATOM   273  H H    A LEU   A 1 12  ? 11.521 -15.714 8.931   0.84 14.56 ?  12  LEU   A H    1 
ATOM   274  H H    B LEU   A 1 12  ? 11.502 -15.543 9.331   0.16 13.22 ?  12  LEU   A H    1 
ATOM   275  H HA   A LEU   A 1 12  ? 9.556  -16.797 7.427   0.84 15.36 ?  12  LEU   A HA   1 
ATOM   276  H HA   B LEU   A 1 12  ? 9.537  -16.490 7.749   0.16 13.70 ?  12  LEU   A HA   1 
ATOM   277  H HB2  A LEU   A 1 12  ? 12.015 -15.693 6.604   0.84 16.07 ?  12  LEU   A HB2  1 
ATOM   278  H HB2  B LEU   A 1 12  ? 11.954 -15.195 7.173   0.16 14.14 ?  12  LEU   A HB2  1 
ATOM   279  H HB3  A LEU   A 1 12  ? 10.944 -16.277 5.594   0.84 16.07 ?  12  LEU   A HB3  1 
ATOM   280  H HB3  B LEU   A 1 12  ? 11.266 -16.047 6.034   0.16 14.14 ?  12  LEU   A HB3  1 
ATOM   281  H HG   A LEU   A 1 12  ? 10.461 -14.003 7.193   0.84 17.85 ?  12  LEU   A HG   1 
ATOM   282  H HG   B LEU   A 1 12  ? 10.305 -13.642 7.120   0.16 14.52 ?  12  LEU   A HG   1 
ATOM   283  H HD11 A LEU   A 1 12  ? 10.768 -12.729 5.266   0.84 19.24 ?  12  LEU   A HD11 1 
ATOM   284  H HD11 B LEU   A 1 12  ? 10.411 -12.869 4.926   0.16 14.66 ?  12  LEU   A HD11 1 
ATOM   285  H HD12 A LEU   A 1 12  ? 12.105 -13.503 5.637   0.84 19.24 ?  12  LEU   A HD12 1 
ATOM   286  H HD12 B LEU   A 1 12  ? 11.839 -13.392 5.386   0.16 14.66 ?  12  LEU   A HD12 1 
ATOM   287  H HD13 A LEU   A 1 12  ? 11.175 -14.041 4.467   0.84 19.24 ?  12  LEU   A HD13 1 
ATOM   288  H HD13 B LEU   A 1 12  ? 10.928 -14.293 4.447   0.16 14.66 ?  12  LEU   A HD13 1 
ATOM   289  H HD21 A LEU   A 1 12  ? 8.608  -13.691 5.730   0.84 18.96 ?  12  LEU   A HD21 1 
ATOM   290  H HD21 B LEU   A 1 12  ? 8.448  -13.999 5.571   0.16 14.76 ?  12  LEU   A HD21 1 
ATOM   291  H HD22 A LEU   A 1 12  ? 8.900  -15.136 5.137   0.84 18.96 ?  12  LEU   A HD22 1 
ATOM   292  H HD22 B LEU   A 1 12  ? 8.842  -15.535 5.668   0.16 14.76 ?  12  LEU   A HD22 1 
ATOM   293  H HD23 A LEU   A 1 12  ? 8.463  -14.974 6.655   0.84 18.96 ?  12  LEU   A HD23 1 
ATOM   294  H HD23 B LEU   A 1 12  ? 8.381  -14.750 6.969   0.16 14.76 ?  12  LEU   A HD23 1 
ATOM   295  N N    A THR   A 1 13  ? 12.308 -18.335 7.933   0.84 12.99 ?  13  THR   A N    1 
ATOM   296  N N    B THR   A 1 13  ? 12.300 -18.072 8.082   0.16 11.67 ?  13  THR   A N    1 
ATOM   297  C CA   A THR   A 1 13  ? 13.006 -19.612 7.835   0.84 12.98 ?  13  THR   A CA   1 
ATOM   298  C CA   B THR   A 1 13  ? 12.912 -19.392 8.036   0.16 11.96 ?  13  THR   A CA   1 
ATOM   299  C C    A THR   A 1 13  ? 13.782 -19.840 9.126   0.84 13.27 ?  13  THR   A C    1 
ATOM   300  C C    B THR   A 1 13  ? 13.688 -19.623 9.325   0.16 12.40 ?  13  THR   A C    1 
ATOM   301  O O    A THR   A 1 13  ? 13.700 -19.061 10.080  0.84 12.86 ?  13  THR   A O    1 
ATOM   302  O O    B THR   A 1 13  ? 13.560 -18.859 10.288  0.16 12.49 ?  13  THR   A O    1 
ATOM   303  C CB   A THR   A 1 13  ? 13.982 -19.639 6.653   0.84 14.26 ?  13  THR   A CB   1 
ATOM   304  C CB   B THR   A 1 13  ? 13.842 -19.534 6.821   0.16 12.21 ?  13  THR   A CB   1 
ATOM   305  O OG1  A THR   A 1 13  ? 15.046 -18.723 6.916   0.84 14.97 ?  13  THR   A OG1  1 
ATOM   306  O OG1  B THR   A 1 13  ? 14.954 -18.641 6.955   0.16 12.26 ?  13  THR   A OG1  1 
ATOM   307  C CG2  A THR   A 1 13  ? 13.304 -19.276 5.337   0.84 15.34 ?  13  THR   A CG2  1 
ATOM   308  C CG2  B THR   A 1 13  ? 13.103 -19.235 5.516   0.16 12.50 ?  13  THR   A CG2  1 
ATOM   309  H H    A THR   A 1 13  ? 12.756 -17.734 8.351   0.84 15.58 ?  13  THR   A H    1 
ATOM   310  H H    B THR   A 1 13  ? 12.824 -17.458 8.368   0.16 14.00 ?  13  THR   A H    1 
ATOM   311  H HA   A THR   A 1 13  ? 12.363 -20.330 7.721   0.84 15.57 ?  13  THR   A HA   1 
ATOM   312  H HA   B THR   A 1 13  ? 12.224 -20.069 7.964   0.16 14.35 ?  13  THR   A HA   1 
ATOM   313  H HB   A THR   A 1 13  ? 14.354 -20.526 6.562   0.84 17.11 ?  13  THR   A HB   1 
ATOM   314  H HB   B THR   A 1 13  ? 14.172 -20.445 6.768   0.16 14.65 ?  13  THR   A HB   1 
ATOM   315  H HG1  A THR   A 1 13  ? 15.589 -18.713 6.267   0.84 17.96 ?  13  THR   A HG1  1 
ATOM   316  H HG1  B THR   A 1 13  ? 15.462 -18.711 6.284   0.16 14.70 ?  13  THR   A HG1  1 
ATOM   317  H HG21 A THR   A 1 13  ? 13.909 -19.452 4.596   0.84 18.40 ?  13  THR   A HG21 1 
ATOM   318  H HG21 B THR   A 1 13  ? 13.696 -19.374 4.757   0.16 14.99 ?  13  THR   A HG21 1 
ATOM   319  H HG22 A THR   A 1 13  ? 12.506 -19.815 5.220   0.84 18.40 ?  13  THR   A HG22 1 
ATOM   320  H HG22 B THR   A 1 13  ? 12.338 -19.825 5.425   0.16 14.99 ?  13  THR   A HG22 1 
ATOM   321  H HG23 A THR   A 1 13  ? 13.060 -18.341 5.331   0.84 18.40 ?  13  THR   A HG23 1 
ATOM   322  H HG23 B THR   A 1 13  ? 12.797 -18.316 5.509   0.16 14.99 ?  13  THR   A HG23 1 
ATOM   323  N N    A ASP   A 1 14  ? 14.585 -20.904 9.134   0.84 13.76 ?  14  ASP   A N    1 
ATOM   324  N N    B ASP   A 1 14  ? 14.497 -20.680 9.347   0.16 12.70 ?  14  ASP   A N    1 
ATOM   325  C CA   A ASP   A 1 14  ? 15.433 -21.181 10.287  0.84 14.00 ?  14  ASP   A CA   1 
ATOM   326  C CA   B ASP   A 1 14  ? 15.324 -20.969 10.512  0.16 13.09 ?  14  ASP   A CA   1 
ATOM   327  C C    A ASP   A 1 14  ? 16.253 -19.961 10.695  0.84 13.67 ?  14  ASP   A C    1 
ATOM   328  C C    B ASP   A 1 14  ? 16.249 -19.806 10.853  0.16 12.60 ?  14  ASP   A C    1 
ATOM   329  O O    A ASP   A 1 14  ? 16.465 -19.726 11.890  0.84 15.17 ?  14  ASP   A O    1 
ATOM   330  O O    B ASP   A 1 14  ? 16.586 -19.609 12.026  0.16 12.87 ?  14  ASP   A O    1 
ATOM   331  C CB   A ASP   A 1 14  ? 16.369 -22.347 9.974   0.84 16.48 ?  14  ASP   A CB   1 
ATOM   332  C CB   B ASP   A 1 14  ? 16.151 -22.226 10.247  0.16 14.26 ?  14  ASP   A CB   1 
ATOM   333  C CG   A ASP   A 1 14  ? 17.235 -22.723 11.154  0.84 20.72 ?  14  ASP   A CG   1 
ATOM   334  C CG   B ASP   A 1 14  ? 17.279 -22.396 11.241  0.16 15.25 ?  14  ASP   A CG   1 
ATOM   335  O OD1  A ASP   A 1 14  ? 16.670 -23.164 12.177  0.84 21.88 ?  14  ASP   A OD1  1 
ATOM   336  O OD1  B ASP   A 1 14  ? 16.996 -22.676 12.424  0.16 15.66 ?  14  ASP   A OD1  1 
ATOM   337  O OD2  A ASP   A 1 14  ? 18.468 -22.576 11.056  0.84 23.89 -1 14  ASP   A OD2  1 
ATOM   338  O OD2  B ASP   A 1 14  ? 18.449 -22.231 10.839  0.16 15.80 -1 14  ASP   A OD2  1 
ATOM   339  H H    A ASP   A 1 14  ? 14.667 -21.463 8.483   0.84 16.51 ?  14  ASP   A H    1 
ATOM   340  H H    B ASP   A 1 14  ? 14.578 -21.232 8.704   0.16 15.24 ?  14  ASP   A H    1 
ATOM   341  H HA   A ASP   A 1 14  ? 14.872 -21.433 11.034  0.84 16.80 ?  14  ASP   A HA   1 
ATOM   342  H HA   B ASP   A 1 14  ? 14.752 -21.137 11.278  0.16 15.71 ?  14  ASP   A HA   1 
ATOM   343  H HB2  A ASP   A 1 14  ? 15.833 -23.125 9.739   0.84 19.78 ?  14  ASP   A HB2  1 
ATOM   344  H HB2  B ASP   A 1 14  ? 15.569 -23.002 10.298  0.16 17.11 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  A ASP   A 1 14  ? 16.944 -22.105 9.235   0.84 19.78 ?  14  ASP   A HB3  1 
ATOM   346  H HB3  B ASP   A 1 14  ? 16.541 -22.165 9.360   0.16 17.11 ?  14  ASP   A HB3  1 
ATOM   347  N N    A ASN   A 1 15  ? 16.727 -19.170 9.719   0.84 13.08 ?  15  ASN   A N    1 
ATOM   348  N N    B ASN   A 1 15  ? 16.665 -19.024 9.851   0.16 12.32 ?  15  ASN   A N    1 
ATOM   349  C CA   A ASN   A 1 15  ? 17.716 -18.131 9.997   0.84 13.74 ?  15  ASN   A CA   1 
ATOM   350  C CA   B ASN   A 1 15  ? 17.676 -17.992 10.048  0.16 12.24 ?  15  ASN   A CA   1 
ATOM   351  C C    A ASN   A 1 15  ? 17.339 -16.731 9.533   0.84 14.08 ?  15  ASN   A C    1 
ATOM   352  C C    B ASN   A 1 15  ? 17.324 -16.651 9.413   0.16 12.32 ?  15  ASN   A C    1 
ATOM   353  O O    A ASN   A 1 15  ? 18.088 -15.795 9.836   0.84 15.03 ?  15  ASN   A O    1 
ATOM   354  O O    B ASN   A 1 15  ? 18.179 -15.758 9.386   0.16 12.62 ?  15  ASN   A O    1 
ATOM   355  C CB   A ASN   A 1 15  ? 19.090 -18.506 9.403   0.84 13.46 ?  15  ASN   A CB   1 
ATOM   356  C CB   B ASN   A 1 15  ? 19.029 -18.454 9.493   0.16 12.08 ?  15  ASN   A CB   1 
ATOM   357  C CG   A ASN   A 1 15  ? 19.060 -18.622 7.895   0.84 14.15 ?  15  ASN   A CG   1 
ATOM   358  C CG   B ASN   A 1 15  ? 19.059 -18.478 7.977   0.16 12.08 ?  15  ASN   A CG   1 
ATOM   359  O OD1  A ASN   A 1 15  ? 18.300 -19.416 7.333   0.84 14.95 ?  15  ASN   A OD1  1 
ATOM   360  O OD1  B ASN   A 1 15  ? 18.523 -19.390 7.347   0.16 12.27 ?  15  ASN   A OD1  1 
ATOM   361  N ND2  A ASN   A 1 15  ? 19.875 -17.811 7.225   0.84 13.42 ?  15  ASN   A ND2  1 
ATOM   362  N ND2  B ASN   A 1 15  ? 19.689 -17.467 7.383   0.16 11.70 ?  15  ASN   A ND2  1 
ATOM   363  H H    A ASN   A 1 15  ? 16.485 -19.219 8.899   0.84 15.69 ?  15  ASN   A H    1 
ATOM   364  H H    B ASN   A 1 15  ? 16.373 -19.081 9.048   0.16 14.78 ?  15  ASN   A H    1 
ATOM   365  H HA   A ASN   A 1 15  ? 17.841 -18.083 10.957  0.84 16.49 ?  15  ASN   A HA   1 
ATOM   366  H HA   B ASN   A 1 15  ? 17.782 -17.852 11.005  0.16 14.68 ?  15  ASN   A HA   1 
ATOM   367  H HB2  A ASN   A 1 15  ? 19.740 -17.819 9.643   0.84 16.15 ?  15  ASN   A HB2  1 
ATOM   368  H HB2  B ASN   A 1 15  ? 19.715 -17.840 9.798   0.16 14.49 ?  15  ASN   A HB2  1 
ATOM   369  H HB3  A ASN   A 1 15  ? 19.376 -19.362 9.763   0.84 16.15 ?  15  ASN   A HB3  1 
ATOM   370  H HB3  B ASN   A 1 15  ? 19.212 -19.348 9.809   0.16 14.49 ?  15  ASN   A HB3  1 
ATOM   371  H HD21 A ASN   A 1 15  ? 19.897 -17.836 6.365   0.84 16.10 ?  15  ASN   A HD21 1 
ATOM   372  H HD21 B ASN   A 1 15  ? 19.732 -17.431 6.524   0.16 14.04 ?  15  ASN   A HD21 1 
ATOM   373  H HD22 A ASN   A 1 15  ? 20.394 -17.263 7.646   0.84 16.10 ?  15  ASN   A HD22 1 
ATOM   374  H HD22 B ASN   A 1 15  ? 20.053 -16.847 7.856   0.16 14.04 ?  15  ASN   A HD22 1 
ATOM   375  N N    A VAL   A 1 16  ? 16.219 -16.548 8.832   0.84 13.84 ?  16  VAL   A N    1 
ATOM   376  N N    B VAL   A 1 16  ? 16.114 -16.482 8.884   0.16 12.26 ?  16  VAL   A N    1 
ATOM   377  C CA   A VAL   A 1 16  ? 15.833 -15.255 8.277   0.84 13.60 ?  16  VAL   A CA   1 
ATOM   378  C CA   B VAL   A 1 16  ? 15.698 -15.236 8.250   0.16 12.28 ?  16  VAL   A CA   1 
ATOM   379  C C    A VAL   A 1 16  ? 14.548 -14.776 8.941   0.84 12.94 ?  16  VAL   A C    1 
ATOM   380  C C    B VAL   A 1 16  ? 14.477 -14.696 8.986   0.16 12.17 ?  16  VAL   A C    1 
ATOM   381  O O    A VAL   A 1 16  ? 13.543 -15.501 8.997   0.84 13.08 ?  16  VAL   A O    1 
ATOM   382  O O    B VAL   A 1 16  ? 13.485 -15.413 9.168   0.16 12.09 ?  16  VAL   A O    1 
ATOM   383  C CB   A VAL   A 1 16  ? 15.674 -15.300 6.748   0.84 13.66 ?  16  VAL   A CB   1 
ATOM   384  C CB   B VAL   A 1 16  ? 15.406 -15.433 6.751   0.16 12.39 ?  16  VAL   A CB   1 
ATOM   385  C CG1  A VAL   A 1 16  ? 15.238 -13.933 6.214   0.84 14.31 ?  16  VAL   A CG1  1 
ATOM   386  C CG1  B VAL   A 1 16  ? 14.931 -14.131 6.123   0.16 12.57 ?  16  VAL   A CG1  1 
ATOM   387  C CG2  A VAL   A 1 16  ? 16.963 -15.754 6.086   0.84 14.66 ?  16  VAL   A CG2  1 
ATOM   388  C CG2  B VAL   A 1 16  ? 16.647 -15.952 6.029   0.16 12.45 ?  16  VAL   A CG2  1 
ATOM   389  H H    A VAL   A 1 16  ? 15.657 -17.177 8.672   0.84 16.61 ?  16  VAL   A H    1 
ATOM   390  H H    B VAL   A 1 16  ? 15.508 -17.091 8.868   0.16 14.71 ?  16  VAL   A H    1 
ATOM   391  H HA   A VAL   A 1 16  ? 16.530 -14.611 8.480   0.84 16.31 ?  16  VAL   A HA   1 
ATOM   392  H HA   B VAL   A 1 16  ? 16.409 -14.581 8.332   0.16 14.74 ?  16  VAL   A HA   1 
ATOM   393  H HB   A VAL   A 1 16  ? 14.984 -15.943 6.526   0.84 16.39 ?  16  VAL   A HB   1 
ATOM   394  H HB   B VAL   A 1 16  ? 14.702 -16.092 6.648   0.16 14.87 ?  16  VAL   A HB   1 
ATOM   395  H HG11 A VAL   A 1 16  ? 15.339 -13.928 5.251   0.84 17.17 ?  16  VAL   A HG11 1 
ATOM   396  H HG11 B VAL   A 1 16  ? 14.944 -14.225 5.158   0.16 15.08 ?  16  VAL   A HG11 1 
ATOM   397  H HG12 A VAL   A 1 16  ? 14.306 -13.785 6.448   0.84 17.17 ?  16  VAL   A HG12 1 
ATOM   398  H HG12 B VAL   A 1 16  ? 14.029 -13.944 6.424   0.16 15.08 ?  16  VAL   A HG12 1 
ATOM   399  H HG13 A VAL   A 1 16  ? 15.793 -13.247 6.611   0.84 17.17 ?  16  VAL   A HG13 1 
ATOM   400  H HG13 B VAL   A 1 16  ? 15.529 -13.416 6.392   0.16 15.08 ?  16  VAL   A HG13 1 
ATOM   401  H HG21 A VAL   A 1 16  ? 16.880 -15.644 5.127   0.84 17.59 ?  16  VAL   A HG21 1 
ATOM   402  H HG21 B VAL   A 1 16  ? 16.468 -15.990 5.076   0.16 14.94 ?  16  VAL   A HG21 1 
ATOM   403  H HG22 A VAL   A 1 16  ? 17.696 -15.215 6.420   0.84 17.59 ?  16  VAL   A HG22 1 
ATOM   404  H HG22 B VAL   A 1 16  ? 17.387 -15.348 6.201   0.16 14.94 ?  16  VAL   A HG22 1 
ATOM   405  H HG23 A VAL   A 1 16  ? 17.116 -16.686 6.302   0.84 17.59 ?  16  VAL   A HG23 1 
ATOM   406  H HG23 B VAL   A 1 16  ? 16.860 -16.838 6.361   0.16 14.94 ?  16  VAL   A HG23 1 
ATOM   407  N N    A TYR   A 1 17  ? 14.580 -13.518 9.379   0.84 12.79 ?  17  TYR   A N    1 
ATOM   408  N N    B TYR   A 1 17  ? 14.555 -13.430 9.401   0.16 12.21 ?  17  TYR   A N    1 
ATOM   409  C CA   A TYR   A 1 17  ? 13.505 -12.840 10.081  0.84 12.73 ?  17  TYR   A CA   1 
ATOM   410  C CA   B TYR   A 1 17  ? 13.484 -12.749 10.115  0.16 12.28 ?  17  TYR   A CA   1 
ATOM   411  C C    A TYR   A 1 17  ? 13.232 -11.512 9.383   0.84 13.24 ?  17  TYR   A C    1 
ATOM   412  C C    B TYR   A 1 17  ? 13.231 -11.398 9.460   0.16 12.37 ?  17  TYR   A C    1 
ATOM   413  O O    A TYR   A 1 17  ? 14.127 -10.953 8.744   0.84 12.97 ?  17  TYR   A O    1 
ATOM   414  O O    B TYR   A 1 17  ? 14.160 -10.753 8.967   0.16 12.37 ?  17  TYR   A O    1 
ATOM   415  C CB   A TYR   A 1 17  ? 13.946 -12.583 11.521  0.84 13.14 ?  17  TYR   A CB   1 
ATOM   416  C CB   B TYR   A 1 17  ? 13.864 -12.514 11.582  0.16 12.52 ?  17  TYR   A CB   1 
ATOM   417  C CG   A TYR   A 1 17  ? 14.144 -13.852 12.324  0.84 13.99 ?  17  TYR   A CG   1 
ATOM   418  C CG   B TYR   A 1 17  ? 14.043 -13.775 12.400  0.16 12.86 ?  17  TYR   A CG   1 
ATOM   419  C CD1  A TYR   A 1 17  ? 15.316 -14.598 12.230  0.84 14.73 ?  17  TYR   A CD1  1 
ATOM   420  C CD1  B TYR   A 1 17  ? 15.195 -14.544 12.291  0.16 13.10 ?  17  TYR   A CD1  1 
ATOM   421  C CD2  A TYR   A 1 17  ? 13.145 -14.320 13.165  0.84 14.09 ?  17  TYR   A CD2  1 
ATOM   422  C CD2  B TYR   A 1 17  ? 13.065 -14.187 13.295  0.16 13.05 ?  17  TYR   A CD2  1 
ATOM   423  C CE1  A TYR   A 1 17  ? 15.481 -15.772 12.957  0.84 15.15 ?  17  TYR   A CE1  1 
ATOM   424  C CE1  B TYR   A 1 17  ? 15.360 -15.696 13.041  0.16 13.33 ?  17  TYR   A CE1  1 
ATOM   425  C CE2  A TYR   A 1 17  ? 13.304 -15.492 13.897  0.84 14.59 ?  17  TYR   A CE2  1 
ATOM   426  C CE2  B TYR   A 1 17  ? 13.221 -15.336 14.050  0.16 13.33 ?  17  TYR   A CE2  1 
ATOM   427  C CZ   A TYR   A 1 17  ? 14.477 -16.212 13.793  0.84 15.09 ?  17  TYR   A CZ   1 
ATOM   428  C CZ   B TYR   A 1 17  ? 14.371 -16.085 13.920  0.16 13.55 ?  17  TYR   A CZ   1 
ATOM   429  O OH   A TYR   A 1 17  ? 14.645 -17.374 14.518  0.84 15.76 ?  17  TYR   A OH   1 
ATOM   430  O OH   B TYR   A 1 17  ? 14.529 -17.228 14.671  0.16 13.98 ?  17  TYR   A OH   1 
ATOM   431  H H    A TYR   A 1 17  ? 15.263 -13.008 9.260   0.84 15.35 ?  17  TYR   A H    1 
ATOM   432  H H    B TYR   A 1 17  ? 15.244 -12.929 9.271   0.16 14.65 ?  17  TYR   A H    1 
ATOM   433  H HA   A TYR   A 1 17  ? 12.701 -13.388 10.073  0.84 15.27 ?  17  TYR   A HA   1 
ATOM   434  H HA   B TYR   A 1 17  ? 12.670 -13.274 10.077  0.16 14.73 ?  17  TYR   A HA   1 
ATOM   435  H HB2  A TYR   A 1 17  ? 14.789 -12.108 11.505  0.84 15.77 ?  17  TYR   A HB2  1 
ATOM   436  H HB2  B TYR   A 1 17  ? 14.698 -12.023 11.610  0.16 15.02 ?  17  TYR   A HB2  1 
ATOM   437  H HB3  A TYR   A 1 17  ? 13.271 -12.055 11.962  0.84 15.77 ?  17  TYR   A HB3  1 
ATOM   438  H HB3  B TYR   A 1 17  ? 13.163 -11.992 11.998  0.16 15.02 ?  17  TYR   A HB3  1 
ATOM   439  H HD1  A TYR   A 1 17  ? 16.001 -14.313 11.665  0.84 17.68 ?  17  TYR   A HD1  1 
ATOM   440  H HD1  B TYR   A 1 17  ? 15.863 -14.286 11.697  0.16 15.72 ?  17  TYR   A HD1  1 
ATOM   441  H HD2  A TYR   A 1 17  ? 12.352 -13.842 13.240  0.84 16.91 ?  17  TYR   A HD2  1 
ATOM   442  H HD2  B TYR   A 1 17  ? 12.287 -13.685 13.385  0.16 15.66 ?  17  TYR   A HD2  1 
ATOM   443  H HE1  A TYR   A 1 17  ? 16.274 -16.258 12.887  0.84 18.17 ?  17  TYR   A HE1  1 
ATOM   444  H HE1  B TYR   A 1 17  ? 16.136 -16.202 12.955  0.16 16.00 ?  17  TYR   A HE1  1 
ATOM   445  H HE2  A TYR   A 1 17  ? 12.622 -15.781 14.460  0.84 17.51 ?  17  TYR   A HE2  1 
ATOM   446  H HE2  B TYR   A 1 17  ? 12.556 -15.598 14.644  0.16 16.00 ?  17  TYR   A HE2  1 
ATOM   447  H HH   A TYR   A 1 17  ? 13.919 -17.572 14.896  0.84 18.91 ?  17  TYR   A HH   1 
ATOM   448  H HH   B TYR   A 1 17  ? 13.826 -17.381 15.106  0.16 16.78 ?  17  TYR   A HH   1 
ATOM   449  N N    A ILE   A 1 18  ? 12.004 -10.990 9.502   0.84 13.32 ?  18  ILE   A N    1 
ATOM   450  N N    B ILE   A 1 18  ? 11.969 -10.959 9.471   0.16 12.39 ?  18  ILE   A N    1 
ATOM   451  C CA   A ILE   A 1 18  ? 11.622 -9.782  8.769   0.84 13.50 ?  18  ILE   A CA   1 
ATOM   452  C CA   B ILE   A 1 18  ? 11.569 -9.741  8.773   0.16 12.53 ?  18  ILE   A CA   1 
ATOM   453  C C    A ILE   A 1 18  ? 10.663 -8.931  9.593   0.84 14.02 ?  18  ILE   A C    1 
ATOM   454  C C    B ILE   A 1 18  ? 10.677 -8.892  9.669   0.16 12.95 ?  18  ILE   A C    1 
ATOM   455  O O    A ILE   A 1 18  ? 9.812  -9.447  10.326  0.84 14.40 ?  18  ILE   A O    1 
ATOM   456  O O    B ILE   A 1 18  ? 9.971  -9.405  10.544  0.16 12.92 ?  18  ILE   A O    1 
ATOM   457  C CB   A ILE   A 1 18  ? 11.053 -10.152 7.377   0.84 13.54 ?  18  ILE   A CB   1 
ATOM   458  C CB   B ILE   A 1 18  ? 10.876 -10.068 7.429   0.16 12.47 ?  18  ILE   A CB   1 
ATOM   459  C CG1  A ILE   A 1 18  ? 10.986 -8.935  6.456   0.84 14.79 ?  18  ILE   A CG1  1 
ATOM   460  C CG1  B ILE   A 1 18  ? 10.813 -8.834  6.527   0.16 12.62 ?  18  ILE   A CG1  1 
ATOM   461  C CG2  A ILE   A 1 18  ? 9.710  -10.882 7.496   0.84 14.01 ?  18  ILE   A CG2  1 
ATOM   462  C CG2  B ILE   A 1 18  ? 9.485  -10.646 7.660   0.16 12.71 ?  18  ILE   A CG2  1 
ATOM   463  C CD1  A ILE   A 1 18  ? 10.750 -9.302  5.018   0.84 16.11 ?  18  ILE   A CD1  1 
ATOM   464  C CD1  B ILE   A 1 18  ? 10.331 -9.140  5.125   0.16 12.79 ?  18  ILE   A CD1  1 
ATOM   465  H H    A ILE   A 1 18  ? 11.378 -11.330 9.988   0.84 15.99 ?  18  ILE   A H    1 
ATOM   466  H H    B ILE   A 1 18  ? 11.321 -11.356 9.879   0.16 14.87 ?  18  ILE   A H    1 
ATOM   467  H HA   A ILE   A 1 18  ? 12.431 -9.259  8.622   0.84 16.19 ?  18  ILE   A HA   1 
ATOM   468  H HA   B ILE   A 1 18  ? 12.362 -9.223  8.576   0.16 15.04 ?  18  ILE   A HA   1 
ATOM   469  H HB   A ILE   A 1 18  ? 11.677 -10.770 6.974   0.84 16.25 ?  18  ILE   A HB   1 
ATOM   470  H HB   B ILE   A 1 18  ? 11.408 -10.737 6.978   0.16 14.96 ?  18  ILE   A HB   1 
ATOM   471  H HG12 A ILE   A 1 18  ? 10.264 -8.358  6.737   0.84 17.75 ?  18  ILE   A HG12 1 
ATOM   472  H HG12 B ILE   A 1 18  ? 10.204 -8.188  6.913   0.16 15.14 ?  18  ILE   A HG12 1 
ATOM   473  H HG13 A ILE   A 1 18  ? 11.831 -8.456  6.498   0.84 17.75 ?  18  ILE   A HG13 1 
ATOM   474  H HG13 B ILE   A 1 18  ? 11.702 -8.450  6.456   0.16 15.14 ?  18  ILE   A HG13 1 
ATOM   475  H HG21 A ILE   A 1 18  ? 9.456  -11.216 6.619   0.84 16.81 ?  18  ILE   A HG21 1 
ATOM   476  H HG21 B ILE   A 1 18  ? 9.167  -11.037 6.830   0.16 15.25 ?  18  ILE   A HG21 1 
ATOM   477  H HG22 A ILE   A 1 18  ? 9.807  -11.621 8.114   0.84 16.81 ?  18  ILE   A HG22 1 
ATOM   478  H HG22 B ILE   A 1 18  ? 9.540  -11.328 8.346   0.16 15.25 ?  18  ILE   A HG22 1 
ATOM   479  H HG23 A ILE   A 1 18  ? 9.037  -10.264 7.819   0.84 16.81 ?  18  ILE   A HG23 1 
ATOM   480  H HG23 B ILE   A 1 18  ? 8.887  -9.938  7.941   0.16 15.25 ?  18  ILE   A HG23 1 
ATOM   481  H HD11 A ILE   A 1 18  ? 10.790 -8.495  4.475   0.84 19.33 ?  18  ILE   A HD11 1 
ATOM   482  H HD11 B ILE   A 1 18  ? 10.445 -8.353  4.571   0.16 15.34 ?  18  ILE   A HD11 1 
ATOM   483  H HD12 A ILE   A 1 18  ? 11.431 -9.926  4.731   0.84 19.33 ?  18  ILE   A HD12 1 
ATOM   484  H HD12 B ILE   A 1 18  ? 10.855 -9.874  4.765   0.16 15.34 ?  18  ILE   A HD12 1 
ATOM   485  H HD13 A ILE   A 1 18  ? 9.871  -9.706  4.936   0.84 19.33 ?  18  ILE   A HD13 1 
ATOM   486  H HD13 B ILE   A 1 18  ? 9.395  -9.389  5.160   0.16 15.34 ?  18  ILE   A HD13 1 
ATOM   487  N N    A LYS   A 1 19  ? 10.793 -7.607  9.440   0.84 14.28 ?  19  LYS   A N    1 
ATOM   488  N N    B LYS   A 1 19  ? 10.710 -7.576  9.441   0.16 13.64 ?  19  LYS   A N    1 
ATOM   489  C CA   A LYS   A 1 19  ? 9.978  -6.641  10.172  0.84 15.53 ?  19  LYS   A CA   1 
ATOM   490  C CA   B LYS   A 1 19  ? 9.935  -6.636  10.244  0.16 14.54 ?  19  LYS   A CA   1 
ATOM   491  C C    A LYS   A 1 19  ? 9.754  -5.401  9.313   0.84 15.31 ?  19  LYS   A C    1 
ATOM   492  C C    B LYS   A 1 19  ? 9.796  -5.323  9.489   0.16 14.93 ?  19  LYS   A C    1 
ATOM   493  O O    A LYS   A 1 19  ? 10.627 -5.007  8.535   0.84 15.06 ?  19  LYS   A O    1 
ATOM   494  O O    B LYS   A 1 19  ? 10.782 -4.809  8.952   0.16 14.63 ?  19  LYS   A O    1 
ATOM   495  C CB   A LYS   A 1 19  ? 10.703 -6.243  11.466  0.84 16.45 ?  19  LYS   A CB   1 
ATOM   496  C CB   B LYS   A 1 19  ? 10.614 -6.386  11.596  0.16 15.16 ?  19  LYS   A CB   1 
ATOM   497  C CG   A LYS   A 1 19  ? 9.952  -5.347  12.443  0.84 18.15 ?  19  LYS   A CG   1 
ATOM   498  C CG   B LYS   A 1 19  ? 9.908  -5.356  12.463  0.16 15.81 ?  19  LYS   A CG   1 
ATOM   499  C CD   A LYS   A 1 19  ? 10.870 -5.062  13.633  0.84 19.40 ?  19  LYS   A CD   1 
ATOM   500  C CD   B LYS   A 1 19  ? 10.738 -5.013  13.683  0.16 16.43 ?  19  LYS   A CD   1 
ATOM   501  C CE   A LYS   A 1 19  ? 10.257 -4.135  14.667  0.84 20.11 ?  19  LYS   A CE   1 
ATOM   502  C CE   B LYS   A 1 19  ? 10.017 -4.029  14.586  0.16 16.76 ?  19  LYS   A CE   1 
ATOM   503  N NZ   A LYS   A 1 19  ? 11.173 -3.970  15.836  0.84 20.46 ?  19  LYS   A NZ   1 
ATOM   504  N NZ   B LYS   A 1 19  ? 10.846 -3.659  15.764  0.16 16.93 ?  19  LYS   A NZ   1 
ATOM   505  H H    A LYS   A 1 19  ? 11.373 -7.239  8.911   0.84 17.14 ?  19  LYS   A H    1 
ATOM   506  H H    B LYS   A 1 19  ? 11.173 -7.199  8.818   0.16 16.36 ?  19  LYS   A H    1 
ATOM   507  H HA   A LYS   A 1 19  ? 9.125  -7.042  10.392  0.84 18.64 ?  19  LYS   A HA   1 
ATOM   508  H HA   B LYS   A 1 19  ? 9.052  -6.992  10.404  0.16 17.45 ?  19  LYS   A HA   1 
ATOM   509  H HB2  A LYS   A 1 19  ? 10.927 -7.055  11.942  0.84 19.74 ?  19  LYS   A HB2  1 
ATOM   510  H HB2  B LYS   A 1 19  ? 10.637 -7.220  12.092  0.16 18.19 ?  19  LYS   A HB2  1 
ATOM   511  H HB3  A LYS   A 1 19  ? 11.518 -5.779  11.221  0.84 19.74 ?  19  LYS   A HB3  1 
ATOM   512  H HB3  B LYS   A 1 19  ? 11.518 -6.071  11.442  0.16 18.19 ?  19  LYS   A HB3  1 
ATOM   513  H HG2  A LYS   A 1 19  ? 9.723  -4.507  12.015  0.84 21.78 ?  19  LYS   A HG2  1 
ATOM   514  H HG2  B LYS   A 1 19  ? 9.768  -4.539  11.958  0.16 18.97 ?  19  LYS   A HG2  1 
ATOM   515  H HG3  A LYS   A 1 19  ? 9.155  -5.800  12.762  0.84 21.78 ?  19  LYS   A HG3  1 
ATOM   516  H HG3  B LYS   A 1 19  ? 9.058  -5.716  12.760  0.16 18.97 ?  19  LYS   A HG3  1 
ATOM   517  H HD2  A LYS   A 1 19  ? 11.078 -5.901  14.073  0.84 23.28 ?  19  LYS   A HD2  1 
ATOM   518  H HD2  B LYS   A 1 19  ? 10.911 -5.822  14.188  0.16 19.72 ?  19  LYS   A HD2  1 
ATOM   519  H HD3  A LYS   A 1 19  ? 11.684 -4.650  13.306  0.84 23.28 ?  19  LYS   A HD3  1 
ATOM   520  H HD3  B LYS   A 1 19  ? 11.573 -4.610  13.397  0.16 19.72 ?  19  LYS   A HD3  1 
ATOM   521  H HE2  A LYS   A 1 19  ? 10.110 -3.262  14.270  0.84 24.13 ?  19  LYS   A HE2  1 
ATOM   522  H HE2  B LYS   A 1 19  ? 9.822  -3.220  14.086  0.16 20.11 ?  19  LYS   A HE2  1 
ATOM   523  H HE3  A LYS   A 1 19  ? 9.422  -4.509  14.983  0.84 24.13 ?  19  LYS   A HE3  1 
ATOM   524  H HE3  B LYS   A 1 19  ? 9.196  -4.432  14.906  0.16 20.11 ?  19  LYS   A HE3  1 
ATOM   525  H HZ1  A LYS   A 1 19  ? 10.797 -3.440  16.443  0.84 24.55 ?  19  LYS   A HZ1  1 
ATOM   526  H HZ1  B LYS   A 1 19  ? 10.395 -3.104  16.291  0.16 20.31 ?  19  LYS   A HZ1  1 
ATOM   527  H HZ2  A LYS   A 1 19  ? 11.338 -4.762  16.205  0.84 24.55 ?  19  LYS   A HZ2  1 
ATOM   528  H HZ2  B LYS   A 1 19  ? 11.059 -4.390  16.226  0.16 20.31 ?  19  LYS   A HZ2  1 
ATOM   529  H HZ3  A LYS   A 1 19  ? 11.941 -3.608  15.572  0.84 24.55 ?  19  LYS   A HZ3  1 
ATOM   530  H HZ3  B LYS   A 1 19  ? 11.595 -3.260  15.495  0.16 20.31 ?  19  LYS   A HZ3  1 
ATOM   531  N N    . ASN   A 1 20  ? 8.578  -4.783  9.455   1.00 15.95 ?  20  ASN   A N    1 
ATOM   532  C CA   . ASN   A 1 20  ? 8.335  -3.459  8.885   1.00 17.37 ?  20  ASN   A CA   1 
ATOM   533  C C    . ASN   A 1 20  ? 8.946  -2.447  9.843   1.00 17.54 ?  20  ASN   A C    1 
ATOM   534  O O    . ASN   A 1 20  ? 8.411  -2.210  10.931  1.00 19.21 ?  20  ASN   A O    1 
ATOM   535  C CB   . ASN   A 1 20  ? 6.835  -3.228  8.697   1.00 18.86 ?  20  ASN   A CB   1 
ATOM   536  C CG   . ASN   A 1 20  ? 6.488  -1.790  8.291   1.00 20.49 ?  20  ASN   A CG   1 
ATOM   537  O OD1  . ASN   A 1 20  ? 5.500  -1.227  8.767   1.00 22.76 ?  20  ASN   A OD1  1 
ATOM   538  N ND2  . ASN   A 1 20  ? 7.286  -1.200  7.409   1.00 20.93 ?  20  ASN   A ND2  1 
ATOM   539  H H    A ASN   A 1 20  ? 7.914  -5.108  9.891   0.84 19.13 ?  20  ASN   A H    1 
ATOM   540  H H    B ASN   A 1 20  ? 7.873  -5.181  9.741   0.16 19.13 ?  20  ASN   A H    1 
ATOM   541  H HA   . ASN   A 1 20  ? 8.774  -3.387  8.023   1.00 20.84 ?  20  ASN   A HA   1 
ATOM   542  H HB2  . ASN   A 1 20  ? 6.511  -3.820  8.001   1.00 22.63 ?  20  ASN   A HB2  1 
ATOM   543  H HB3  . ASN   A 1 20  ? 6.383  -3.424  9.532   1.00 22.63 ?  20  ASN   A HB3  1 
ATOM   544  H HD21 . ASN   A 1 20  ? 7.123  -0.397  7.160   1.00 25.11 ?  20  ASN   A HD21 1 
ATOM   545  H HD22 . ASN   A 1 20  ? 7.967  -1.622  7.096   1.00 25.11 ?  20  ASN   A HD22 1 
ATOM   546  N N    A ALA   A 1 21  ? 10.088 -1.881  9.461   0.84 17.71 ?  21  ALA   A N    1 
ATOM   547  N N    B ALA   A 1 21  ? 10.069 -1.848  9.456   0.16 16.80 ?  21  ALA   A N    1 
ATOM   548  C CA   A ALA   A 1 21  ? 10.800 -0.987  10.361  0.84 17.74 ?  21  ALA   A CA   1 
ATOM   549  C CA   B ALA   A 1 21  ? 10.715 -0.866  10.317  0.16 16.24 ?  21  ALA   A CA   1 
ATOM   550  C C    A ALA   A 1 21  ? 11.754 -0.113  9.567   0.84 17.30 ?  21  ALA   A C    1 
ATOM   551  C C    B ALA   A 1 21  ? 11.802 -0.144  9.538   0.16 15.55 ?  21  ALA   A C    1 
ATOM   552  O O    A ALA   A 1 21  ? 12.192 -0.482  8.473   0.84 17.77 ?  21  ALA   A O    1 
ATOM   553  O O    B ALA   A 1 21  ? 12.322 -0.653  8.542   0.16 15.40 ?  21  ALA   A O    1 
ATOM   554  C CB   A ALA   A 1 21  ? 11.580 -1.775  11.417  0.84 18.77 ?  21  ALA   A CB   1 
ATOM   555  C CB   B ALA   A 1 21  ? 11.314 -1.519  11.567  0.16 16.50 ?  21  ALA   A CB   1 
ATOM   556  H H    A ALA   A 1 21  ? 10.464 -1.996  8.696   0.84 21.26 ?  21  ALA   A H    1 
ATOM   557  H H    B ALA   A 1 21  ? 10.471 -1.993  8.710   0.16 20.16 ?  21  ALA   A H    1 
ATOM   558  H HA   A ALA   A 1 21  ? 10.157 -0.414  10.814  0.84 21.28 ?  21  ALA   A HA   1 
ATOM   559  H HA   B ALA   A 1 21  ? 10.057 -0.213  10.603  0.16 19.48 ?  21  ALA   A HA   1 
ATOM   560  H HB1  A ALA   A 1 21  ? 11.992 -1.147  12.026  0.84 22.52 ?  21  ALA   A HB1  1 
ATOM   561  H HB1  B ALA   A 1 21  ? 11.738 -0.833  12.107  0.16 19.79 ?  21  ALA   A HB1  1 
ATOM   562  H HB2  A ALA   A 1 21  ? 10.959 -2.347  11.900  0.84 22.52 ?  21  ALA   A HB2  1 
ATOM   563  H HB2  B ALA   A 1 21  ? 10.606 -1.948  12.070  0.16 19.79 ?  21  ALA   A HB2  1 
ATOM   564  H HB3  A ALA   A 1 21  ? 12.250 -2.312  10.975  0.84 22.52 ?  21  ALA   A HB3  1 
ATOM   565  H HB3  B ALA   A 1 21  ? 11.973 -2.177  11.293  0.16 19.79 ?  21  ALA   A HB3  1 
ATOM   566  N N    A ASP   A 1 22  ? 12.052 1.054   10.142  0.84 17.28 ?  22  ASP   A N    1 
ATOM   567  N N    B ASP   A 1 22  ? 12.132 1.055   10.014  0.16 15.24 ?  22  ASP   A N    1 
ATOM   568  C CA   A ASP   A 1 22  ? 13.091 1.953   9.653   0.84 17.21 ?  22  ASP   A CA   1 
ATOM   569  C CA   B ASP   A 1 22  ? 13.272 1.803   9.505   0.16 15.11 ?  22  ASP   A CA   1 
ATOM   570  C C    A ASP   A 1 22  ? 14.425 1.465   10.209  0.84 16.24 ?  22  ASP   A C    1 
ATOM   571  C C    B ASP   A 1 22  ? 14.547 1.210   10.097  0.16 14.65 ?  22  ASP   A C    1 
ATOM   572  O O    A ASP   A 1 22  ? 14.628 1.460   11.428  0.84 16.84 ?  22  ASP   A O    1 
ATOM   573  O O    B ASP   A 1 22  ? 14.674 1.088   11.320  0.16 14.46 ?  22  ASP   A O    1 
ATOM   574  C CB   A ASP   A 1 22  ? 12.771 3.363   10.153  0.84 19.07 ?  22  ASP   A CB   1 
ATOM   575  C CB   B ASP   A 1 22  ? 13.141 3.272   9.913   0.16 15.49 ?  22  ASP   A CB   1 
ATOM   576  C CG   A ASP   A 1 22  ? 13.780 4.409   9.700   0.84 20.71 ?  22  ASP   A CG   1 
ATOM   577  C CG   B ASP   A 1 22  ? 14.141 4.170   9.210   0.16 15.76 ?  22  ASP   A CG   1 
ATOM   578  O OD1  A ASP   A 1 22  ? 14.866 4.055   9.203   0.84 20.76 ?  22  ASP   A OD1  1 
ATOM   579  O OD1  B ASP   A 1 22  ? 15.239 3.685   8.864   0.16 15.57 ?  22  ASP   A OD1  1 
ATOM   580  O OD2  A ASP   A 1 22  ? 13.480 5.611   9.857   0.84 22.49 -1 22  ASP   A OD2  1 
ATOM   581  O OD2  B ASP   A 1 22  ? 13.836 5.364   9.004   0.16 16.11 -1 22  ASP   A OD2  1 
ATOM   582  H H    A ASP   A 1 22  ? 11.637 1.355   10.840  0.84 20.73 ?  22  ASP   A H    1 
ATOM   583  H H    B ASP   A 1 22  ? 11.699 1.461   10.638  0.16 18.29 ?  22  ASP   A H    1 
ATOM   584  H HA   A ASP   A 1 22  ? 13.113 1.943   8.685   0.84 20.65 ?  22  ASP   A HA   1 
ATOM   585  H HA   B ASP   A 1 22  ? 13.304 1.746   8.534   0.16 18.13 ?  22  ASP   A HA   1 
ATOM   586  H HB2  A ASP   A 1 22  ? 11.890 3.617   9.831   0.84 22.88 ?  22  ASP   A HB2  1 
ATOM   587  H HB2  B ASP   A 1 22  ? 12.244 3.581   9.703   0.16 18.59 ?  22  ASP   A HB2  1 
ATOM   588  H HB3  A ASP   A 1 22  ? 12.772 3.354   11.125  0.84 22.88 ?  22  ASP   A HB3  1 
ATOM   589  H HB3  B ASP   A 1 22  ? 13.300 3.348   10.867  0.16 18.59 ?  22  ASP   A HB3  1 
ATOM   590  N N    A ILE   A 1 23  ? 15.321 1.026   9.320   0.84 15.41 ?  23  ILE   A N    1 
ATOM   591  N N    B ILE   A 1 23  ? 15.487 0.830   9.228   0.16 14.60 ?  23  ILE   A N    1 
ATOM   592  C CA   A ILE   A 1 23  ? 16.578 0.418   9.756   0.84 14.84 ?  23  ILE   A CA   1 
ATOM   593  C CA   B ILE   A 1 23  ? 16.731 0.224   9.693   0.16 14.66 ?  23  ILE   A CA   1 
ATOM   594  C C    A ILE   A 1 23  ? 17.378 1.365   10.638  0.84 14.92 ?  23  ILE   A C    1 
ATOM   595  C C    B ILE   A 1 23  ? 17.511 1.200   10.561  0.16 15.24 ?  23  ILE   A C    1 
ATOM   596  O O    A ILE   A 1 23  ? 18.097 0.919   11.541  0.84 15.45 ?  23  ILE   A O    1 
ATOM   597  O O    B ILE   A 1 23  ? 18.277 0.787   11.441  0.16 15.21 ?  23  ILE   A O    1 
ATOM   598  C CB   A ILE   A 1 23  ? 17.384 -0.088  8.539   0.84 14.41 ?  23  ILE   A CB   1 
ATOM   599  C CB   B ILE   A 1 23  ? 17.564 -0.300  8.502   0.16 14.03 ?  23  ILE   A CB   1 
ATOM   600  C CG1  A ILE   A 1 23  ? 18.538 -0.992  8.989   0.84 14.28 ?  23  ILE   A CG1  1 
ATOM   601  C CG1  B ILE   A 1 23  ? 18.628 -1.286  8.991   0.16 13.77 ?  23  ILE   A CG1  1 
ATOM   602  C CG2  A ILE   A 1 23  ? 17.871 1.075   7.681   0.84 14.72 ?  23  ILE   A CG2  1 
ATOM   603  C CG2  B ILE   A 1 23  ? 18.219 0.849   7.740   0.16 13.78 ?  23  ILE   A CG2  1 
ATOM   604  C CD1  A ILE   A 1 23  ? 19.254 -1.690  7.839   0.84 14.55 ?  23  ILE   A CD1  1 
ATOM   605  C CD1  B ILE   A 1 23  ? 19.473 -1.877  7.878   0.16 13.68 ?  23  ILE   A CD1  1 
ATOM   606  H H    A ILE   A 1 23  ? 15.214 1.055   8.475   0.84 18.49 ?  23  ILE   A H    1 
ATOM   607  H H    B ILE   A 1 23  ? 15.431 0.911   8.385   0.16 17.52 ?  23  ILE   A H    1 
ATOM   608  H HA   A ILE   A 1 23  ? 16.371 -0.356  10.300  0.84 17.81 ?  23  ILE   A HA   1 
ATOM   609  H HA   B ILE   A 1 23  ? 16.506 -0.541  10.241  0.16 17.60 ?  23  ILE   A HA   1 
ATOM   610  H HB   A ILE   A 1 23  ? 16.785 -0.624  7.998   0.84 17.29 ?  23  ILE   A HB   1 
ATOM   611  H HB   B ILE   A 1 23  ? 16.973 -0.770  7.895   0.16 16.84 ?  23  ILE   A HB   1 
ATOM   612  H HG12 A ILE   A 1 23  ? 19.193 -0.456  9.462   0.84 17.13 ?  23  ILE   A HG12 1 
ATOM   613  H HG12 B ILE   A 1 23  ? 19.225 -0.829  9.603   0.16 16.52 ?  23  ILE   A HG12 1 
ATOM   614  H HG13 A ILE   A 1 23  ? 18.188 -1.680  9.578   0.84 17.13 ?  23  ILE   A HG13 1 
ATOM   615  H HG13 B ILE   A 1 23  ? 18.188 -2.021  9.447   0.16 16.52 ?  23  ILE   A HG13 1 
ATOM   616  H HG21 A ILE   A 1 23  ? 18.230 0.726   6.850   0.84 17.66 ?  23  ILE   A HG21 1 
ATOM   617  H HG21 B ILE   A 1 23  ? 18.526 0.521   6.878   0.16 16.54 ?  23  ILE   A HG21 1 
ATOM   618  H HG22 A ILE   A 1 23  ? 17.118 1.662   7.491   0.84 17.66 ?  23  ILE   A HG22 1 
ATOM   619  H HG22 B ILE   A 1 23  ? 17.566 1.552   7.611   0.16 16.54 ?  23  ILE   A HG22 1 
ATOM   620  H HG23 A ILE   A 1 23  ? 18.555 1.563   8.161   0.84 17.66 ?  23  ILE   A HG23 1 
ATOM   621  H HG23 B ILE   A 1 23  ? 18.971 1.183   8.253   0.16 16.54 ?  23  ILE   A HG23 1 
ATOM   622  H HD11 A ILE   A 1 23  ? 19.920 -2.295  8.201   0.84 17.46 ?  23  ILE   A HD11 1 
ATOM   623  H HD11 B ILE   A 1 23  ? 20.023 -2.588  8.243   0.16 16.42 ?  23  ILE   A HD11 1 
ATOM   624  H HD12 A ILE   A 1 23  ? 18.604 -2.187  7.318   0.84 17.46 ?  23  ILE   A HD12 1 
ATOM   625  H HD12 B ILE   A 1 23  ? 18.886 -2.232  7.192   0.16 16.42 ?  23  ILE   A HD12 1 
ATOM   626  H HD13 A ILE   A 1 23  ? 19.682 -1.022  7.281   0.84 17.46 ?  23  ILE   A HD13 1 
ATOM   627  H HD13 B ILE   A 1 23  ? 20.036 -1.181  7.504   0.16 16.42 ?  23  ILE   A HD13 1 
ATOM   628  N N    A VAL   A 1 24  ? 17.256 2.676   10.413  0.84 15.73 ?  24  VAL   A N    1 
ATOM   629  N N    B VAL   A 1 24  ? 17.332 2.502   10.334  0.16 16.10 ?  24  VAL   A N    1 
ATOM   630  C CA   A VAL   A 1 24  ? 17.943 3.647   11.262  0.84 16.87 ?  24  VAL   A CA   1 
ATOM   631  C CA   B VAL   A 1 24  ? 17.972 3.501   11.183  0.16 16.97 ?  24  VAL   A CA   1 
ATOM   632  C C    A VAL   A 1 24  ? 17.433 3.554   12.693  0.84 17.56 ?  24  VAL   A C    1 
ATOM   633  C C    B VAL   A 1 24  ? 17.401 3.444   12.594  0.16 17.70 ?  24  VAL   A C    1 
ATOM   634  O O    A VAL   A 1 24  ? 18.214 3.478   13.651  0.84 17.98 ?  24  VAL   A O    1 
ATOM   635  O O    B VAL   A 1 24  ? 18.144 3.480   13.582  0.16 17.70 ?  24  VAL   A O    1 
ATOM   636  C CB   A VAL   A 1 24  ? 17.773 5.068   10.693  0.84 17.96 ?  24  VAL   A CB   1 
ATOM   637  C CB   B VAL   A 1 24  ? 17.825 4.902   10.561  0.16 17.37 ?  24  VAL   A CB   1 
ATOM   638  C CG1  A VAL   A 1 24  ? 18.293 6.112   11.679  0.84 18.94 ?  24  VAL   A CG1  1 
ATOM   639  C CG1  B VAL   A 1 24  ? 18.413 5.959   11.485  0.16 17.65 ?  24  VAL   A CG1  1 
ATOM   640  C CG2  A VAL   A 1 24  ? 18.477 5.190   9.350   0.84 18.75 ?  24  VAL   A CG2  1 
ATOM   641  C CG2  B VAL   A 1 24  ? 18.489 4.947   9.193   0.16 17.49 ?  24  VAL   A CG2  1 
ATOM   642  H H    A VAL   A 1 24  ? 16.790 3.025   9.780   0.84 18.88 ?  24  VAL   A H    1 
ATOM   643  H H    B VAL   A 1 24  ? 16.849 2.828   9.703   0.16 19.32 ?  24  VAL   A H    1 
ATOM   644  H HA   A VAL   A 1 24  ? 18.892 3.448   11.270  0.84 20.24 ?  24  VAL   A HA   1 
ATOM   645  H HA   B VAL   A 1 24  ? 18.918 3.302   11.239  0.16 20.36 ?  24  VAL   A HA   1 
ATOM   646  H HB   A VAL   A 1 24  ? 16.831 5.241   10.546  0.84 21.55 ?  24  VAL   A HB   1 
ATOM   647  H HB   B VAL   A 1 24  ? 16.882 5.099   10.443  0.16 20.84 ?  24  VAL   A HB   1 
ATOM   648  H HG11 A VAL   A 1 24  ? 18.430 6.948   11.206  0.84 22.72 ?  24  VAL   A HG11 1 
ATOM   649  H HG11 B VAL   A 1 24  ? 18.515 6.786   10.990  0.16 21.17 ?  24  VAL   A HG11 1 
ATOM   650  H HG12 A VAL   A 1 24  ? 17.639 6.234   12.383  0.84 22.72 ?  24  VAL   A HG12 1 
ATOM   651  H HG12 B VAL   A 1 24  ? 17.812 6.095   12.234  0.16 21.17 ?  24  VAL   A HG12 1 
ATOM   652  H HG13 A VAL   A 1 24  ? 19.133 5.801   12.050  0.84 22.72 ?  24  VAL   A HG13 1 
ATOM   653  H HG13 B VAL   A 1 24  ? 19.277 5.654   11.802  0.16 21.17 ?  24  VAL   A HG13 1 
ATOM   654  H HG21 A VAL   A 1 24  ? 18.306 6.070   8.978   0.84 22.50 ?  24  VAL   A HG21 1 
ATOM   655  H HG21 B VAL   A 1 24  ? 18.374 5.833   8.815   0.16 20.99 ?  24  VAL   A HG21 1 
ATOM   656  H HG22 A VAL   A 1 24  ? 19.433 5.070   9.481   0.84 22.50 ?  24  VAL   A HG22 1 
ATOM   657  H HG22 B VAL   A 1 24  ? 19.434 4.754   9.296   0.16 20.99 ?  24  VAL   A HG22 1 
ATOM   658  H HG23 A VAL   A 1 24  ? 18.140 4.507   8.750   0.84 22.50 ?  24  VAL   A HG23 1 
ATOM   659  H HG23 B VAL   A 1 24  ? 18.076 4.285   8.617   0.16 20.99 ?  24  VAL   A HG23 1 
ATOM   660  N N    A GLU   A 1 25  ? 16.109 3.561   12.858  0.84 18.74 ?  25  GLU   A N    1 
ATOM   661  N N    B GLU   A 1 25  ? 16.074 3.352   12.711  0.16 18.60 ?  25  GLU   A N    1 
ATOM   662  C CA   A GLU   A 1 25  ? 15.527 3.486   14.193  0.84 20.52 ?  25  GLU   A CA   1 
ATOM   663  C CA   B GLU   A 1 25  ? 15.455 3.271   14.030  0.16 19.55 ?  25  GLU   A CA   1 
ATOM   664  C C    A GLU   A 1 25  ? 15.776 2.123   14.829  0.84 19.64 ?  25  GLU   A C    1 
ATOM   665  C C    B GLU   A 1 25  ? 15.694 1.916   14.685  0.16 19.16 ?  25  GLU   A C    1 
ATOM   666  O O    A GLU   A 1 25  ? 16.035 2.033   16.034  0.84 20.58 ?  25  GLU   A O    1 
ATOM   667  O O    B GLU   A 1 25  ? 15.827 1.839   15.911  0.16 19.35 ?  25  GLU   A O    1 
ATOM   668  C CB   A GLU   A 1 25  ? 14.033 3.812   14.131  0.84 23.10 ?  25  GLU   A CB   1 
ATOM   669  C CB   B GLU   A 1 25  ? 13.959 3.575   13.931  0.16 20.95 ?  25  GLU   A CB   1 
ATOM   670  C CG   A GLU   A 1 25  ? 13.752 5.251   13.716  0.84 26.48 ?  25  GLU   A CG   1 
ATOM   671  C CG   B GLU   A 1 25  ? 13.652 4.998   13.491  0.16 22.40 ?  25  GLU   A CG   1 
ATOM   672  C CD   A GLU   A 1 25  ? 14.492 6.261   14.578  0.84 29.45 ?  25  GLU   A CD   1 
ATOM   673  C CD   B GLU   A 1 25  ? 14.274 6.037   14.399  0.16 23.59 ?  25  GLU   A CD   1 
ATOM   674  O OE1  A GLU   A 1 25  ? 14.546 6.068   15.812  0.84 30.30 ?  25  GLU   A OE1  1 
ATOM   675  O OE1  B GLU   A 1 25  ? 14.364 5.783   15.619  0.16 24.00 ?  25  GLU   A OE1  1 
ATOM   676  O OE2  A GLU   A 1 25  ? 15.040 7.234   14.018  0.84 31.02 -1 25  GLU   A OE2  1 
ATOM   677  O OE2  B GLU   A 1 25  ? 14.678 7.104   13.893  0.16 24.13 -1 25  GLU   A OE2  1 
ATOM   678  H H    A GLU   A 1 25  ? 15.536 3.613   12.220  0.84 22.48 ?  25  GLU   A H    1 
ATOM   679  H H    B GLU   A 1 25  ? 15.523 3.340   12.051  0.16 22.32 ?  25  GLU   A H    1 
ATOM   680  H HA   A GLU   A 1 25  ? 15.951 4.150   14.757  0.84 24.62 ?  25  GLU   A HA   1 
ATOM   681  H HA   B GLU   A 1 25  ? 15.858 3.942   14.599  0.16 23.45 ?  25  GLU   A HA   1 
ATOM   682  H HB2  A GLU   A 1 25  ? 13.605 3.231   13.481  0.84 27.71 ?  25  GLU   A HB2  1 
ATOM   683  H HB2  B GLU   A 1 25  ? 13.557 2.974   13.285  0.16 25.14 ?  25  GLU   A HB2  1 
ATOM   684  H HB3  A GLU   A 1 25  ? 13.638 3.676   15.006  0.84 27.71 ?  25  GLU   A HB3  1 
ATOM   685  H HB3  B GLU   A 1 25  ? 13.554 3.440   14.802  0.16 25.14 ?  25  GLU   A HB3  1 
ATOM   686  H HG2  A GLU   A 1 25  ? 14.042 5.379   12.800  0.84 31.77 ?  25  GLU   A HG2  1 
ATOM   687  H HG2  B GLU   A 1 25  ? 13.991 5.133   12.593  0.16 26.88 ?  25  GLU   A HG2  1 
ATOM   688  H HG3  A GLU   A 1 25  ? 12.797 5.421   13.788  0.84 31.77 ?  25  GLU   A HG3  1 
ATOM   689  H HG3  B GLU   A 1 25  ? 12.694 5.139   13.512  0.16 26.88 ?  25  GLU   A HG3  1 
ATOM   690  N N    A GLU   A 1 26  ? 15.726 1.053   14.031  0.84 18.87 ?  26  GLU   A N    1 
ATOM   691  N N    B GLU   A 1 26  ? 15.752 0.842   13.894  0.16 18.64 ?  26  GLU   A N    1 
ATOM   692  C CA   A GLU   A 1 26  ? 16.043 -0.275  14.551  0.84 18.81 ?  26  GLU   A CA   1 
ATOM   693  C CA   B GLU   A 1 26  ? 16.079 -0.464  14.456  0.16 18.20 ?  26  GLU   A CA   1 
ATOM   694  C C    A GLU   A 1 26  ? 17.472 -0.327  15.076  0.84 17.80 ?  26  GLU   A C    1 
ATOM   695  C C    B GLU   A 1 26  ? 17.507 -0.496  14.979  0.16 17.38 ?  26  GLU   A C    1 
ATOM   696  O O    A GLU   A 1 26  ? 17.727 -0.829  16.177  0.84 17.92 ?  26  GLU   A O    1 
ATOM   697  O O    B GLU   A 1 26  ? 17.788 -1.137  15.999  0.16 17.32 ?  26  GLU   A O    1 
ATOM   698  C CB   A GLU   A 1 26  ? 15.862 -1.325  13.453  0.84 20.24 ?  26  GLU   A CB   1 
ATOM   699  C CB   B GLU   A 1 26  ? 15.883 -1.554  13.404  0.16 18.72 ?  26  GLU   A CB   1 
ATOM   700  C CG   A GLU   A 1 26  ? 14.476 -1.909  13.322  0.84 22.72 ?  26  GLU   A CG   1 
ATOM   701  C CG   B GLU   A 1 26  ? 14.436 -1.892  13.132  0.16 19.21 ?  26  GLU   A CG   1 
ATOM   702  C CD   A GLU   A 1 26  ? 14.048 -2.702  14.546  0.84 23.96 ?  26  GLU   A CD   1 
ATOM   703  C CD   B GLU   A 1 26  ? 13.754 -2.522  14.325  0.16 19.44 ?  26  GLU   A CD   1 
ATOM   704  O OE1  A GLU   A 1 26  ? 14.497 -3.859  14.758  0.84 24.31 ?  26  GLU   A OE1  1 
ATOM   705  O OE1  B GLU   A 1 26  ? 14.387 -3.362  14.998  0.16 19.69 ?  26  GLU   A OE1  1 
ATOM   706  O OE2  A GLU   A 1 26  ? 13.238 -2.150  15.300  0.84 24.79 -1 26  GLU   A OE2  1 
ATOM   707  O OE2  B GLU   A 1 26  ? 12.590 -2.164  14.596  0.16 19.15 -1 26  GLU   A OE2  1 
ATOM   708  H H    A GLU   A 1 26  ? 15.523 1.078   13.198  0.84 22.65 ?  26  GLU   A H    1 
ATOM   709  H H    B GLU   A 1 26  ? 15.606 0.844   13.047  0.16 22.37 ?  26  GLU   A H    1 
ATOM   710  H HA   A GLU   A 1 26  ? 15.444 -0.482  15.281  0.84 22.57 ?  26  GLU   A HA   1 
ATOM   711  H HA   B GLU   A 1 26  ? 15.485 -0.647  15.199  0.16 21.84 ?  26  GLU   A HA   1 
ATOM   712  H HB2  A GLU   A 1 26  ? 16.090 -0.918  12.602  0.84 24.29 ?  26  GLU   A HB2  1 
ATOM   713  H HB2  B GLU   A 1 26  ? 16.279 -1.257  12.570  0.16 22.47 ?  26  GLU   A HB2  1 
ATOM   714  H HB3  A GLU   A 1 26  ? 16.471 -2.058  13.633  0.84 24.29 ?  26  GLU   A HB3  1 
ATOM   715  H HB3  B GLU   A 1 26  ? 16.326 -2.363  13.708  0.16 22.47 ?  26  GLU   A HB3  1 
ATOM   716  H HG2  A GLU   A 1 26  ? 13.845 -1.179  13.191  0.84 27.27 ?  26  GLU   A HG2  1 
ATOM   717  H HG2  B GLU   A 1 26  ? 13.957 -1.079  12.919  0.16 23.05 ?  26  GLU   A HG2  1 
ATOM   718  H HG3  A GLU   A 1 26  ? 14.452 -2.503  12.559  0.84 27.27 ?  26  GLU   A HG3  1 
ATOM   719  H HG3  B GLU   A 1 26  ? 14.392 -2.514  12.391  0.16 23.05 ?  26  GLU   A HG3  1 
ATOM   720  N N    . ALA   A 1 27  ? 18.426 0.184   14.293  1.00 16.67 ?  27  ALA   A N    1 
ATOM   721  C CA   . ALA   A 1 27  ? 19.820 0.159   14.722  1.00 16.51 ?  27  ALA   A CA   1 
ATOM   722  C C    . ALA   A 1 27  ? 20.013 0.962   16.002  1.00 17.65 ?  27  ALA   A C    1 
ATOM   723  O O    . ALA   A 1 27  ? 20.691 0.512   16.933  1.00 17.92 ?  27  ALA   A O    1 
ATOM   724  C CB   . ALA   A 1 27  ? 20.728 0.680   13.604  1.00 16.03 ?  27  ALA   A CB   1 
ATOM   725  H H    A ALA   A 1 27  ? 18.293 0.547   13.524  0.84 20.00 ?  27  ALA   A H    1 
ATOM   726  H H    B ALA   A 1 27  ? 18.272 0.658   13.591  0.16 20.00 ?  27  ALA   A H    1 
ATOM   727  H HA   . ALA   A 1 27  ? 20.073 -0.757  14.905  1.00 19.81 ?  27  ALA   A HA   1 
ATOM   728  H HB1  . ALA   A 1 27  ? 21.652 0.653   13.909  1.00 19.24 ?  27  ALA   A HB1  1 
ATOM   729  H HB2  . ALA   A 1 27  ? 20.626 0.113   12.822  1.00 19.24 ?  27  ALA   A HB2  1 
ATOM   730  H HB3  . ALA   A 1 27  ? 20.480 1.591   13.388  1.00 19.24 ?  27  ALA   A HB3  1 
ATOM   731  N N    . LYS   A 1 28  ? 19.411 2.150   16.076  1.00 19.35 ?  28  LYS   A N    1 
ATOM   732  C CA   . LYS   A 1 28  ? 19.557 2.971   17.274  1.00 22.79 ?  28  LYS   A CA   1 
ATOM   733  C C    . LYS   A 1 28  ? 19.027 2.260   18.513  1.00 24.07 ?  28  LYS   A C    1 
ATOM   734  O O    . LYS   A 1 28  ? 19.576 2.430   19.606  1.00 25.50 ?  28  LYS   A O    1 
ATOM   735  C CB   . LYS   A 1 28  ? 18.877 4.328   17.078  1.00 25.09 ?  28  LYS   A CB   1 
ATOM   736  C CG   . LYS   A 1 28  ? 19.673 5.270   16.186  1.00 27.52 ?  28  LYS   A CG   1 
ATOM   737  C CD   . LYS   A 1 28  ? 19.192 6.708   16.285  1.00 30.12 ?  28  LYS   A CD   1 
ATOM   738  C CE   . LYS   A 1 28  ? 17.865 6.897   15.582  1.00 32.03 ?  28  LYS   A CE   1 
ATOM   739  N NZ   . LYS   A 1 28  ? 17.460 8.329   15.554  1.00 33.14 ?  28  LYS   A NZ   1 
ATOM   740  H H    . LYS   A 1 28  ? 18.927 2.494   15.459  1.00 23.21 ?  28  LYS   A H    1 
ATOM   741  H HA   . LYS   A 1 28  ? 20.498 3.138   17.425  1.00 27.34 ?  28  LYS   A HA   1 
ATOM   742  H HB2  . LYS   A 1 28  ? 18.010 4.193   16.666  1.00 30.10 ?  28  LYS   A HB2  1 
ATOM   743  H HB3  . LYS   A 1 28  ? 18.770 4.758   17.941  1.00 30.10 ?  28  LYS   A HB3  1 
ATOM   744  H HG2  . LYS   A 1 28  ? 20.606 5.247   16.452  1.00 33.02 ?  28  LYS   A HG2  1 
ATOM   745  H HG3  . LYS   A 1 28  ? 19.582 4.986   15.263  1.00 33.02 ?  28  LYS   A HG3  1 
ATOM   746  H HD2  . LYS   A 1 28  ? 19.078 6.945   17.219  1.00 36.14 ?  28  LYS   A HD2  1 
ATOM   747  H HD3  . LYS   A 1 28  ? 19.843 7.293   15.867  1.00 36.14 ?  28  LYS   A HD3  1 
ATOM   748  H HE2  . LYS   A 1 28  ? 17.942 6.584   14.667  1.00 38.44 ?  28  LYS   A HE2  1 
ATOM   749  H HE3  . LYS   A 1 28  ? 17.181 6.396   16.052  1.00 38.44 ?  28  LYS   A HE3  1 
ATOM   750  H HZ1  . LYS   A 1 28  ? 16.680 8.416   15.137  1.00 39.76 ?  28  LYS   A HZ1  1 
ATOM   751  H HZ2  . LYS   A 1 28  ? 17.381 8.639   16.385  1.00 39.76 ?  28  LYS   A HZ2  1 
ATOM   752  H HZ3  . LYS   A 1 28  ? 18.074 8.810   15.124  1.00 39.76 ?  28  LYS   A HZ3  1 
ATOM   753  N N    . LYS   A 1 29  ? 17.982 1.445   18.360  1.00 24.61 ?  29  LYS   A N    1 
ATOM   754  C CA   . LYS   A 1 29  ? 17.395 0.747   19.501  1.00 26.54 ?  29  LYS   A CA   1 
ATOM   755  C C    . LYS   A 1 29  ? 18.208 -0.485  19.885  1.00 25.23 ?  29  LYS   A C    1 
ATOM   756  O O    . LYS   A 1 29  ? 18.500 -0.704  21.068  1.00 26.23 ?  29  LYS   A O    1 
ATOM   757  C CB   . LYS   A 1 29  ? 15.957 0.341   19.167  1.00 29.72 ?  29  LYS   A CB   1 
ATOM   758  C CG   . LYS   A 1 29  ? 15.201 -0.310  20.315  1.00 33.07 ?  29  LYS   A CG   1 
ATOM   759  C CD   . LYS   A 1 29  ? 14.828 0.712   21.375  1.00 36.13 ?  29  LYS   A CD   1 
ATOM   760  C CE   . LYS   A 1 29  ? 13.953 0.100   22.457  1.00 38.37 ?  29  LYS   A CE   1 
ATOM   761  N NZ   . LYS   A 1 29  ? 13.525 1.117   23.456  1.00 39.64 ?  29  LYS   A NZ   1 
ATOM   762  H H    . LYS   A 1 29  ? 17.596 1.282   17.609  1.00 29.53 ?  29  LYS   A H    1 
ATOM   763  H HA   . LYS   A 1 29  ? 17.371 1.343   20.264  1.00 31.85 ?  29  LYS   A HA   1 
ATOM   764  H HB2  . LYS   A 1 29  ? 15.462 1.133   18.906  1.00 35.67 ?  29  LYS   A HB2  1 
ATOM   765  H HB3  . LYS   A 1 29  ? 15.973 -0.291  18.432  1.00 35.67 ?  29  LYS   A HB3  1 
ATOM   766  H HG2  . LYS   A 1 29  ? 14.383 -0.708  19.976  1.00 39.68 ?  29  LYS   A HG2  1 
ATOM   767  H HG3  . LYS   A 1 29  ? 15.755 -0.991  20.730  1.00 39.68 ?  29  LYS   A HG3  1 
ATOM   768  H HD2  . LYS   A 1 29  ? 15.636 1.050   21.792  1.00 43.36 ?  29  LYS   A HD2  1 
ATOM   769  H HD3  . LYS   A 1 29  ? 14.335 1.437   20.959  1.00 43.36 ?  29  LYS   A HD3  1 
ATOM   770  H HE2  . LYS   A 1 29  ? 13.158 -0.278  22.048  1.00 46.05 ?  29  LYS   A HE2  1 
ATOM   771  H HE3  . LYS   A 1 29  ? 14.453 -0.590  22.920  1.00 46.05 ?  29  LYS   A HE3  1 
ATOM   772  H HZ1  . LYS   A 1 29  ? 13.015 0.736   24.078  1.00 47.57 ?  29  LYS   A HZ1  1 
ATOM   773  H HZ2  . LYS   A 1 29  ? 14.238 1.477   23.848  1.00 47.57 ?  29  LYS   A HZ2  1 
ATOM   774  H HZ3  . LYS   A 1 29  ? 13.059 1.761   23.055  1.00 47.57 ?  29  LYS   A HZ3  1 
ATOM   775  N N    . VAL   A 1 30  ? 18.558 -1.313  18.901  1.00 23.59 ?  30  VAL   A N    1 
ATOM   776  C CA   . VAL   A 1 30  ? 19.201 -2.592  19.182  1.00 22.40 ?  30  VAL   A CA   1 
ATOM   777  C C    . VAL   A 1 30  ? 20.707 -2.439  19.401  1.00 21.17 ?  30  VAL   A C    1 
ATOM   778  O O    . VAL   A 1 30  ? 21.297 -3.169  20.205  1.00 21.77 ?  30  VAL   A O    1 
ATOM   779  C CB   . VAL   A 1 30  ? 18.883 -3.576  18.041  1.00 23.33 ?  30  VAL   A CB   1 
ATOM   780  C CG1  . VAL   A 1 30  ? 19.644 -4.882  18.221  1.00 23.98 ?  30  VAL   A CG1  1 
ATOM   781  C CG2  . VAL   A 1 30  ? 17.382 -3.836  17.960  1.00 23.86 ?  30  VAL   A CG2  1 
ATOM   782  H H    . VAL   A 1 30  ? 18.421 -1.166  18.064  1.00 28.31 ?  30  VAL   A H    1 
ATOM   783  H HA   . VAL   A 1 30  ? 18.816 -2.960  19.991  1.00 26.88 ?  30  VAL   A HA   1 
ATOM   784  H HB   . VAL   A 1 30  ? 19.161 -3.188  17.197  1.00 28.00 ?  30  VAL   A HB   1 
ATOM   785  H HG11 . VAL   A 1 30  ? 19.262 -5.553  17.631  1.00 28.77 ?  30  VAL   A HG11 1 
ATOM   786  H HG12 . VAL   A 1 30  ? 20.575 -4.740  17.997  1.00 28.77 ?  30  VAL   A HG12 1 
ATOM   787  H HG13 . VAL   A 1 30  ? 19.560 -5.170  19.143  1.00 28.77 ?  30  VAL   A HG13 1 
ATOM   788  H HG21 . VAL   A 1 30  ? 17.211 -4.494  17.266  1.00 28.63 ?  30  VAL   A HG21 1 
ATOM   789  H HG22 . VAL   A 1 30  ? 17.073 -4.171  18.816  1.00 28.63 ?  30  VAL   A HG22 1 
ATOM   790  H HG23 . VAL   A 1 30  ? 16.930 -3.006  17.745  1.00 28.63 ?  30  VAL   A HG23 1 
ATOM   791  N N    . LYS   A 1 31  ? 21.347 -1.496  18.719  1.00 20.13 ?  31  LYS   A N    1 
ATOM   792  C CA   . LYS   A 1 31  ? 22.801 -1.401  18.669  1.00 21.01 ?  31  LYS   A CA   1 
ATOM   793  C C    . LYS   A 1 31  ? 23.396 -2.762  18.298  1.00 19.00 ?  31  LYS   A C    1 
ATOM   794  O O    . LYS   A 1 31  ? 24.179 -3.337  19.061  1.00 19.82 ?  31  LYS   A O    1 
ATOM   795  C CB   . LYS   A 1 31  ? 23.388 -0.881  19.973  1.00 26.03 ?  31  LYS   A CB   1 
ATOM   796  C CG   . LYS   A 1 31  ? 22.708 0.380   20.491  1.00 31.66 ?  31  LYS   A CG   1 
ATOM   797  C CD   . LYS   A 1 31  ? 23.714 1.465   20.854  1.00 36.02 ?  31  LYS   A CD   1 
ATOM   798  C CE   . LYS   A 1 31  ? 23.087 2.529   21.748  1.00 38.78 ?  31  LYS   A CE   1 
ATOM   799  N NZ   . LYS   A 1 31  ? 21.896 3.185   21.134  1.00 40.15 ?  31  LYS   A NZ   1 
ATOM   800  H H    . LYS   A 1 31  ? 20.947 -0.883  18.270  1.00 24.16 ?  31  LYS   A H    1 
ATOM   801  H HA   . LYS   A 1 31  ? 23.042 -0.776  17.974  1.00 25.21 ?  31  LYS   A HA   1 
ATOM   802  H HB2  . LYS   A 1 31  ? 23.302 -1.572  20.646  1.00 31.23 ?  31  LYS   A HB2  1 
ATOM   803  H HB3  . LYS   A 1 31  ? 24.329 -0.677  19.831  1.00 31.23 ?  31  LYS   A HB3  1 
ATOM   804  H HG2  . LYS   A 1 31  ? 22.120 0.732   19.804  1.00 37.99 ?  31  LYS   A HG2  1 
ATOM   805  H HG3  . LYS   A 1 31  ? 22.198 0.162   21.287  1.00 37.99 ?  31  LYS   A HG3  1 
ATOM   806  H HD2  . LYS   A 1 31  ? 24.459 1.066   21.332  1.00 43.22 ?  31  LYS   A HD2  1 
ATOM   807  H HD3  . LYS   A 1 31  ? 24.030 1.895   20.042  1.00 43.22 ?  31  LYS   A HD3  1 
ATOM   808  H HE2  . LYS   A 1 31  ? 22.804 2.116   22.579  1.00 46.54 ?  31  LYS   A HE2  1 
ATOM   809  H HE3  . LYS   A 1 31  ? 23.745 3.218   21.929  1.00 46.54 ?  31  LYS   A HE3  1 
ATOM   810  H HZ1  . LYS   A 1 31  ? 21.567 3.800   21.688  1.00 48.18 ?  31  LYS   A HZ1  1 
ATOM   811  H HZ2  . LYS   A 1 31  ? 22.125 3.578   20.369  1.00 48.18 ?  31  LYS   A HZ2  1 
ATOM   812  H HZ3  . LYS   A 1 31  ? 21.265 2.578   20.970  1.00 48.18 ?  31  LYS   A HZ3  1 
ATOM   813  N N    . PRO   A 1 32  ? 23.032 -3.302  17.141  1.00 16.99 ?  32  PRO   A N    1 
ATOM   814  C CA   . PRO   A 1 32  ? 23.505 -4.633  16.767  1.00 17.16 ?  32  PRO   A CA   1 
ATOM   815  C C    . PRO   A 1 32  ? 25.006 -4.639  16.548  1.00 17.28 ?  32  PRO   A C    1 
ATOM   816  O O    . PRO   A 1 32  ? 25.641 -3.604  16.337  1.00 17.00 ?  32  PRO   A O    1 
ATOM   817  C CB   . PRO   A 1 32  ? 22.764 -4.903  15.454  1.00 17.23 ?  32  PRO   A CB   1 
ATOM   818  C CG   . PRO   A 1 32  ? 22.577 -3.539  14.865  1.00 16.30 ?  32  PRO   A CG   1 
ATOM   819  C CD   . PRO   A 1 32  ? 22.288 -2.659  16.046  1.00 16.12 ?  32  PRO   A CD   1 
ATOM   820  H HA   . PRO   A 1 32  ? 23.264 -5.296  17.431  1.00 20.59 ?  32  PRO   A HA   1 
ATOM   821  H HB2  . PRO   A 1 32  ? 23.306 -5.464  14.873  1.00 20.67 ?  32  PRO   A HB2  1 
ATOM   822  H HB3  . PRO   A 1 32  ? 21.908 -5.326  15.638  1.00 20.67 ?  32  PRO   A HB3  1 
ATOM   823  H HG2  . PRO   A 1 32  ? 23.388 -3.267  14.414  1.00 19.56 ?  32  PRO   A HG2  1 
ATOM   824  H HG3  . PRO   A 1 32  ? 21.825 -3.554  14.250  1.00 19.56 ?  32  PRO   A HG3  1 
ATOM   825  H HD2  . PRO   A 1 32  ? 22.628 -1.766  15.878  1.00 19.34 ?  32  PRO   A HD2  1 
ATOM   826  H HD3  . PRO   A 1 32  ? 21.340 -2.653  16.234  1.00 19.34 ?  32  PRO   A HD3  1 
ATOM   827  N N    . THR   A 1 33  ? 25.570 -5.845  16.591  1.00 17.23 ?  33  THR   A N    1 
ATOM   828  C CA   . THR   A 1 33  ? 26.980 -6.005  16.265  1.00 17.06 ?  33  THR   A CA   1 
ATOM   829  C C    . THR   A 1 33  ? 27.266 -5.537  14.845  1.00 15.58 ?  33  THR   A C    1 
ATOM   830  O O    . THR   A 1 33  ? 28.297 -4.897  14.591  1.00 15.48 ?  33  THR   A O    1 
ATOM   831  C CB   . THR   A 1 33  ? 27.382 -7.468  16.453  1.00 18.65 ?  33  THR   A CB   1 
ATOM   832  O OG1  . THR   A 1 33  ? 27.060 -7.879  17.785  1.00 20.36 ?  33  THR   A OG1  1 
ATOM   833  C CG2  . THR   A 1 33  ? 28.875 -7.653  16.221  1.00 19.73 ?  33  THR   A CG2  1 
ATOM   834  H H    . THR   A 1 33  ? 25.167 -6.574  16.798  1.00 20.67 ?  33  THR   A H    1 
ATOM   835  H HA   . THR   A 1 33  ? 27.515 -5.471  16.872  1.00 20.47 ?  33  THR   A HA   1 
ATOM   836  H HB   . THR   A 1 33  ? 26.904 -8.026  15.818  1.00 22.37 ?  33  THR   A HB   1 
ATOM   837  H HG1  . THR   A 1 33  ? 27.475 -7.404  18.343  1.00 24.43 ?  33  THR   A HG1  1 
ATOM   838  H HG21 . THR   A 1 33  ? 29.143 -8.549  16.485  1.00 23.68 ?  33  THR   A HG21 1 
ATOM   839  H HG22 . THR   A 1 33  ? 29.086 -7.528  15.284  1.00 23.68 ?  33  THR   A HG22 1 
ATOM   840  H HG23 . THR   A 1 33  ? 29.373 -7.010  16.749  1.00 23.68 ?  33  THR   A HG23 1 
ATOM   841  N N    . VAL   A 1 34  ? 26.363 -5.836  13.910  1.00 14.04 ?  34  VAL   A N    1 
ATOM   842  C CA   . VAL   A 1 34  ? 26.543 -5.497  12.501  1.00 12.83 ?  34  VAL   A CA   1 
ATOM   843  C C    . VAL   A 1 34  ? 25.241 -4.932  11.944  1.00 12.24 ?  34  VAL   A C    1 
ATOM   844  O O    . VAL   A 1 34  ? 24.200 -5.599  11.990  1.00 12.77 ?  34  VAL   A O    1 
ATOM   845  C CB   . VAL   A 1 34  ? 26.984 -6.705  11.652  1.00 13.34 ?  34  VAL   A CB   1 
ATOM   846  C CG1  . VAL   A 1 34  ? 27.165 -6.288  10.201  1.00 13.41 ?  34  VAL   A CG1  1 
ATOM   847  C CG2  . VAL   A 1 34  ? 28.273 -7.330  12.205  1.00 14.55 ?  34  VAL   A CG2  1 
ATOM   848  H H    . VAL   A 1 34  ? 25.625 -6.246  14.072  1.00 16.84 ?  34  VAL   A H    1 
ATOM   849  H HA   . VAL   A 1 34  ? 27.225 -4.808  12.422  1.00 15.40 ?  34  VAL   A HA   1 
ATOM   850  H HB   . VAL   A 1 34  ? 26.289 -7.378  11.684  1.00 16.00 ?  34  VAL   A HB   1 
ATOM   851  H HG11 . VAL   A 1 34  ? 27.657 -6.982  9.735   1.00 16.10 ?  34  VAL   A HG11 1 
ATOM   852  H HG12 . VAL   A 1 34  ? 26.296 -6.167  9.792   1.00 16.10 ?  34  VAL   A HG12 1 
ATOM   853  H HG13 . VAL   A 1 34  ? 27.666 -5.456  10.171  1.00 16.10 ?  34  VAL   A HG13 1 
ATOM   854  H HG21 . VAL   A 1 34  ? 28.538 -8.067  11.631  1.00 17.45 ?  34  VAL   A HG21 1 
ATOM   855  H HG22 . VAL   A 1 34  ? 28.971 -6.657  12.222  1.00 17.45 ?  34  VAL   A HG22 1 
ATOM   856  H HG23 . VAL   A 1 34  ? 28.107 -7.656  13.104  1.00 17.45 ?  34  VAL   A HG23 1 
ATOM   857  N N    . VAL   A 1 35  ? 25.301 -3.719  11.391  1.00 11.54 ?  35  VAL   A N    1 
ATOM   858  C CA   . VAL   A 1 35  ? 24.264 -3.201  10.506  1.00 11.45 ?  35  VAL   A CA   1 
ATOM   859  C C    . VAL   A 1 35  ? 24.811 -3.198  9.087   1.00 10.78 ?  35  VAL   A C    1 
ATOM   860  O O    . VAL   A 1 35  ? 25.956 -2.795  8.852   1.00 11.24 ?  35  VAL   A O    1 
ATOM   861  C CB   . VAL   A 1 35  ? 23.731 -1.810  10.920  1.00 12.05 ?  35  VAL   A CB   1 
ATOM   862  C CG1  . VAL   A 1 35  ? 24.799 -0.722  10.796  1.00 12.52 ?  35  VAL   A CG1  1 
ATOM   863  C CG2  . VAL   A 1 35  ? 22.500 -1.453  10.092  1.00 12.74 ?  35  VAL   A CG2  1 
ATOM   864  H H    . VAL   A 1 35  ? 25.946 -3.162  11.513  1.00 13.85 ?  35  VAL   A H    1 
ATOM   865  H HA   . VAL   A 1 35  ? 23.508 -3.813  10.527  1.00 13.74 ?  35  VAL   A HA   1 
ATOM   866  H HB   . VAL   A 1 35  ? 23.450 -1.845  11.844  1.00 14.46 ?  35  VAL   A HB   1 
ATOM   867  H HG11 . VAL   A 1 35  ? 24.453 0.106   11.169  1.00 15.02 ?  35  VAL   A HG11 1 
ATOM   868  H HG12 . VAL   A 1 35  ? 25.588 -0.999  11.284  1.00 15.02 ?  35  VAL   A HG12 1 
ATOM   869  H HG13 . VAL   A 1 35  ? 25.018 -0.591  9.859   1.00 15.02 ?  35  VAL   A HG13 1 
ATOM   870  H HG21 . VAL   A 1 35  ? 22.134 -0.615  10.406  1.00 15.29 ?  35  VAL   A HG21 1 
ATOM   871  H HG22 . VAL   A 1 35  ? 22.759 -1.369  9.156   1.00 15.29 ?  35  VAL   A HG22 1 
ATOM   872  H HG23 . VAL   A 1 35  ? 21.840 -2.160  10.182  1.00 15.29 ?  35  VAL   A HG23 1 
ATOM   873  N N    . VAL   A 1 36  ? 23.990 -3.644  8.139   1.00 10.21 ?  36  VAL   A N    1 
ATOM   874  C CA   . VAL   A 1 36  ? 24.366 -3.657  6.733   1.00 9.82  ?  36  VAL   A CA   1 
ATOM   875  C C    . VAL   A 1 36  ? 23.905 -2.363  6.077   1.00 10.13 ?  36  VAL   A C    1 
ATOM   876  O O    . VAL   A 1 36  ? 22.745 -1.951  6.228   1.00 10.81 ?  36  VAL   A O    1 
ATOM   877  C CB   . VAL   A 1 36  ? 23.761 -4.868  6.010   1.00 10.01 ?  36  VAL   A CB   1 
ATOM   878  C CG1  . VAL   A 1 36  ? 24.004 -4.777  4.522   1.00 10.86 ?  36  VAL   A CG1  1 
ATOM   879  C CG2  . VAL   A 1 36  ? 24.312 -6.174  6.569   1.00 10.93 ?  36  VAL   A CG2  1 
ATOM   880  H H    . VAL   A 1 36  ? 23.198 -3.956  8.289   1.00 12.25 ?  36  VAL   A H    1 
ATOM   881  H HA   . VAL   A 1 36  ? 25.337 -3.718  6.662   1.00 11.78 ?  36  VAL   A HA   1 
ATOM   882  H HB   . VAL   A 1 36  ? 22.804 -4.866  6.150   1.00 12.01 ?  36  VAL   A HB   1 
ATOM   883  H HG11 . VAL   A 1 36  ? 23.880 -5.652  4.125   1.00 13.03 ?  36  VAL   A HG11 1 
ATOM   884  H HG12 . VAL   A 1 36  ? 23.375 -4.147  4.133   1.00 13.03 ?  36  VAL   A HG12 1 
ATOM   885  H HG13 . VAL   A 1 36  ? 24.914 -4.473  4.367   1.00 13.03 ?  36  VAL   A HG13 1 
ATOM   886  H HG21 . VAL   A 1 36  ? 23.908 -6.923  6.092   1.00 13.12 ?  36  VAL   A HG21 1 
ATOM   887  H HG22 . VAL   A 1 36  ? 25.275 -6.197  6.451   1.00 13.12 ?  36  VAL   A HG22 1 
ATOM   888  H HG23 . VAL   A 1 36  ? 24.094 -6.238  7.513   1.00 13.12 ?  36  VAL   A HG23 1 
ATOM   889  N N    . ASN   A 1 37  ? 24.814 -1.733  5.334   1.00 9.51  ?  37  ASN   A N    1 
ATOM   890  C CA   . ASN   A 1 37  ? 24.485 -0.606  4.477   1.00 9.46  ?  37  ASN   A CA   1 
ATOM   891  C C    . ASN   A 1 37  ? 24.349 -1.063  3.032   1.00 9.32  ?  37  ASN   A C    1 
ATOM   892  O O    . ASN   A 1 37  ? 25.126 -1.897  2.551   1.00 9.78  ?  37  ASN   A O    1 
ATOM   893  C CB   . ASN   A 1 37  ? 25.567 0.465   4.567   1.00 9.79  ?  37  ASN   A CB   1 
ATOM   894  C CG   . ASN   A 1 37  ? 25.245 1.681   3.725   1.00 9.98  ?  37  ASN   A CG   1 
ATOM   895  O OD1  . ASN   A 1 37  ? 24.072 2.022   3.545   1.00 10.39 ?  37  ASN   A OD1  1 
ATOM   896  N ND2  . ASN   A 1 37  ? 26.281 2.336   3.204   1.00 10.20 ?  37  ASN   A ND2  1 
ATOM   897  H H    . ASN   A 1 37  ? 25.654 -1.944  5.315   1.00 11.41 ?  37  ASN   A H    1 
ATOM   898  H HA   . ASN   A 1 37  ? 23.646 -0.218  4.764   1.00 11.35 ?  37  ASN   A HA   1 
ATOM   899  H HB2  . ASN   A 1 37  ? 25.650 0.760   5.491   1.00 11.75 ?  37  ASN   A HB2  1 
ATOM   900  H HB3  . ASN   A 1 37  ? 26.412 0.097   4.262   1.00 11.75 ?  37  ASN   A HB3  1 
ATOM   901  H HD21 . ASN   A 1 37  ? 26.142 3.030   2.713   1.00 12.24 ?  37  ASN   A HD21 1 
ATOM   902  H HD22 . ASN   A 1 37  ? 27.078 2.074   3.353   1.00 12.24 ?  37  ASN   A HD22 1 
ATOM   903  N N    A ALA   A 1 38  ? 23.341 -0.510  2.355   0.84 9.95  ?  38  ALA   A N    1 
ATOM   904  N N    B ALA   A 1 38  ? 23.356 -0.517  2.330   0.16 9.76  ?  38  ALA   A N    1 
ATOM   905  C CA   A ALA   A 1 38  ? 23.139 -0.644  0.913   0.84 10.19 ?  38  ALA   A CA   1 
ATOM   906  C CA   B ALA   A 1 38  ? 23.196 -0.779  0.899   0.16 10.06 ?  38  ALA   A CA   1 
ATOM   907  C C    A ALA   A 1 38  ? 24.072 0.338   0.199   0.84 9.93  ?  38  ALA   A C    1 
ATOM   908  C C    B ALA   A 1 38  ? 23.994 0.274   0.134   0.16 10.18 ?  38  ALA   A C    1 
ATOM   909  O O    A ALA   A 1 38  ? 23.679 1.432   -0.220  0.84 10.26 ?  38  ALA   A O    1 
ATOM   910  O O    B ALA   A 1 38  ? 23.465 1.270   -0.364  0.16 10.24 ?  38  ALA   A O    1 
ATOM   911  C CB   A ALA   A 1 38  ? 21.678 -0.377  0.570   0.84 11.68 ?  38  ALA   A CB   1 
ATOM   912  C CB   B ALA   A 1 38  ? 21.724 -0.775  0.510   0.16 10.36 ?  38  ALA   A CB   1 
ATOM   913  H H    A ALA   A 1 38  ? 22.739 -0.027  2.735   0.84 11.93 ?  38  ALA   A H    1 
ATOM   914  H H    B ALA   A 1 38  ? 22.760 0.010   2.663   0.16 11.70 ?  38  ALA   A H    1 
ATOM   915  H HA   A ALA   A 1 38  ? 23.363 -1.544  0.637   0.84 12.22 ?  38  ALA   A HA   1 
ATOM   916  H HA   B ALA   A 1 38  ? 23.563 -1.653  0.691   0.16 12.07 ?  38  ALA   A HA   1 
ATOM   917  H HB1  A ALA   A 1 38  ? 21.555 -0.473  -0.386  0.84 14.01 ?  38  ALA   A HB1  1 
ATOM   918  H HB1  B ALA   A 1 38  ? 21.652 -0.956  -0.441  0.16 12.43 ?  38  ALA   A HB1  1 
ATOM   919  H HB2  A ALA   A 1 38  ? 21.119 -1.019  1.041   0.84 14.01 ?  38  ALA   A HB2  1 
ATOM   920  H HB2  B ALA   A 1 38  ? 21.262 -1.462  1.013   0.16 12.43 ?  38  ALA   A HB2  1 
ATOM   921  H HB3  A ALA   A 1 38  ? 21.445 0.523   0.847   0.84 14.01 ?  38  ALA   A HB3  1 
ATOM   922  H HB3  B ALA   A 1 38  ? 21.348 0.095   0.711   0.16 12.43 ?  38  ALA   A HB3  1 
ATOM   923  N N    A ALA   A 1 39  ? 25.335 -0.064  0.064   0.84 10.14 ?  39  ALA   A N    1 
ATOM   924  N N    B ALA   A 1 39  ? 25.298 0.037   0.037   0.16 10.39 ?  39  ALA   A N    1 
ATOM   925  C CA   A ALA   A 1 39  ? 26.388 0.816   -0.416  0.84 9.84  ?  39  ALA   A CA   1 
ATOM   926  C CA   B ALA   A 1 39  ? 26.227 1.036   -0.467  0.16 10.86 ?  39  ALA   A CA   1 
ATOM   927  C C    A ALA   A 1 39  ? 26.498 0.776   -1.935  0.84 10.00 ?  39  ALA   A C    1 
ATOM   928  C C    B ALA   A 1 39  ? 26.517 0.829   -1.949  0.16 10.55 ?  39  ALA   A C    1 
ATOM   929  O O    A ALA   A 1 39  ? 25.992 -0.132  -2.600  0.84 10.24 ?  39  ALA   A O    1 
ATOM   930  O O    B ALA   A 1 39  ? 26.194 -0.203  -2.542  0.16 10.45 ?  39  ALA   A O    1 
ATOM   931  C CB   A ALA   A 1 39  ? 27.715 0.413   0.226   0.84 10.21 ?  39  ALA   A CB   1 
ATOM   932  C CB   B ALA   A 1 39  ? 27.533 0.991   0.328   0.16 11.54 ?  39  ALA   A CB   1 
ATOM   933  H H    A ALA   A 1 39  ? 25.605 -0.865  0.253   0.84 12.17 ?  39  ALA   A H    1 
ATOM   934  H H    B ALA   A 1 39  ? 25.670 -0.711  0.259   0.16 12.47 ?  39  ALA   A H    1 
ATOM   935  H HA   A ALA   A 1 39  ? 26.178 1.726   -0.148  0.84 11.80 ?  39  ALA   A HA   1 
ATOM   936  H HA   B ALA   A 1 39  ? 25.832 1.912   -0.348  0.16 13.03 ?  39  ALA   A HA   1 
ATOM   937  H HB1  A ALA   A 1 39  ? 28.407 1.011   -0.094  0.84 12.25 ?  39  ALA   A HB1  1 
ATOM   938  H HB1  B ALA   A 1 39  ? 28.115 1.695   0.005   0.16 13.85 ?  39  ALA   A HB1  1 
ATOM   939  H HB2  A ALA   A 1 39  ? 27.634 0.495   1.194   0.84 12.25 ?  39  ALA   A HB2  1 
ATOM   940  H HB2  B ALA   A 1 39  ? 27.334 1.127   1.266   0.16 13.85 ?  39  ALA   A HB2  1 
ATOM   941  H HB3  A ALA   A 1 39  ? 27.918 -0.498  -0.013  0.84 12.25 ?  39  ALA   A HB3  1 
ATOM   942  H HB3  B ALA   A 1 39  ? 27.948 0.126   0.199   0.16 13.85 ?  39  ALA   A HB3  1 
ATOM   943  N N    A ASN   A 1 40  ? 27.184 1.780   -2.481  0.84 10.60 ?  40  ASN   A N    1 
ATOM   944  N N    B ASN   A 1 40  ? 27.142 1.844   -2.546  0.16 10.45 ?  40  ASN   A N    1 
ATOM   945  C CA   A ASN   A 1 40  ? 27.703 1.739   -3.842  0.84 11.01 ?  40  ASN   A CA   1 
ATOM   946  C CA   B ASN   A 1 40  ? 27.698 1.749   -3.885  0.16 10.54 ?  40  ASN   A CA   1 
ATOM   947  C C    A ASN   A 1 40  ? 29.228 1.637   -3.798  0.84 10.64 ?  40  ASN   A C    1 
ATOM   948  C C    B ASN   A 1 40  ? 29.213 1.578   -3.799  0.16 10.45 ?  40  ASN   A C    1 
ATOM   949  O O    A ASN   A 1 40  ? 29.838 1.738   -2.734  0.84 10.59 ?  40  ASN   A O    1 
ATOM   950  O O    B ASN   A 1 40  ? 29.811 1.611   -2.721  0.16 10.24 ?  40  ASN   A O    1 
ATOM   951  C CB   A ASN   A 1 40  ? 27.195 2.921   -4.684  0.84 11.67 ?  40  ASN   A CB   1 
ATOM   952  C CB   B ASN   A 1 40  ? 27.319 2.965   -4.734  0.16 10.72 ?  40  ASN   A CB   1 
ATOM   953  C CG   A ASN   A 1 40  ? 27.595 4.270   -4.127  0.84 12.71 ?  40  ASN   A CG   1 
ATOM   954  C CG   B ASN   A 1 40  ? 27.603 4.280   -4.038  0.16 11.15 ?  40  ASN   A CG   1 
ATOM   955  O OD1  A ASN   A 1 40  ? 28.771 4.519   -3.849  0.84 13.78 ?  40  ASN   A OD1  1 
ATOM   956  O OD1  B ASN   A 1 40  ? 28.748 4.585   -3.702  0.16 11.65 ?  40  ASN   A OD1  1 
ATOM   957  N ND2  A ASN   A 1 40  ? 26.615 5.164   -3.982  0.84 13.69 ?  40  ASN   A ND2  1 
ATOM   958  N ND2  B ASN   A 1 40  ? 26.559 5.077   -3.834  0.16 11.42 ?  40  ASN   A ND2  1 
ATOM   959  H H    A ASN   A 1 40  ? 27.370 2.504   -2.066  0.84 12.71 ?  40  ASN   A H    1 
ATOM   960  H H    B ASN   A 1 40  ? 27.254 2.612   -2.178  0.16 12.53 ?  40  ASN   A H    1 
ATOM   961  H HA   A ASN   A 1 40  ? 27.375 0.928   -4.266  0.84 13.20 ?  40  ASN   A HA   1 
ATOM   962  H HA   B ASN   A 1 40  ? 27.340 0.958   -4.320  0.16 12.64 ?  40  ASN   A HA   1 
ATOM   963  H HB2  A ASN   A 1 40  ? 27.555 2.844   -5.582  0.84 14.00 ?  40  ASN   A HB2  1 
ATOM   964  H HB2  B ASN   A 1 40  ? 27.832 2.945   -5.559  0.16 12.86 ?  40  ASN   A HB2  1 
ATOM   965  H HB3  A ASN   A 1 40  ? 26.224 2.887   -4.718  0.84 14.00 ?  40  ASN   A HB3  1 
ATOM   966  H HB3  B ASN   A 1 40  ? 26.372 2.928   -4.933  0.16 12.86 ?  40  ASN   A HB3  1 
ATOM   967  H HD21 A ASN   A 1 40  ? 26.791 5.949   -3.676  0.84 16.42 ?  40  ASN   A HD21 1 
ATOM   968  H HD21 B ASN   A 1 40  ? 26.668 5.837   -3.448  0.16 13.71 ?  40  ASN   A HD21 1 
ATOM   969  H HD22 A ASN   A 1 40  ? 25.807 4.957   -4.190  0.84 16.42 ?  40  ASN   A HD22 1 
ATOM   970  H HD22 B ASN   A 1 40  ? 25.775 4.831   -4.089  0.16 13.71 ?  40  ASN   A HD22 1 
ATOM   971  N N    . VAL   A 1 41  ? 29.840 1.388   -4.962  1.00 10.74 ?  41  VAL   A N    1 
ATOM   972  C CA   . VAL   A 1 41  ? 31.271 1.077   -4.997  1.00 11.52 ?  41  VAL   A CA   1 
ATOM   973  C C    . VAL   A 1 41  ? 32.137 2.225   -4.519  1.00 11.47 ?  41  VAL   A C    1 
ATOM   974  O O    . VAL   A 1 41  ? 33.276 1.999   -4.098  1.00 11.93 ?  41  VAL   A O    1 
ATOM   975  C CB   . VAL   A 1 41  ? 31.756 0.603   -6.383  1.00 12.56 ?  41  VAL   A CB   1 
ATOM   976  C CG1  . VAL   A 1 41  ? 31.072 -0.693  -6.773  1.00 13.35 ?  41  VAL   A CG1  1 
ATOM   977  C CG2  . VAL   A 1 41  ? 31.578 1.673   -7.453  1.00 13.42 ?  41  VAL   A CG2  1 
ATOM   978  H H    A VAL   A 1 41  ? 29.450 1.382   -5.729  0.84 12.89 ?  41  VAL   A H    1 
ATOM   979  H H    B VAL   A 1 41  ? 29.458 1.415   -5.733  0.16 12.89 ?  41  VAL   A H    1 
ATOM   980  H HA   . VAL   A 1 41  ? 31.427 0.338   -4.384  1.00 13.82 ?  41  VAL   A HA   1 
ATOM   981  H HB   . VAL   A 1 41  ? 32.705 0.408   -6.323  1.00 15.07 ?  41  VAL   A HB   1 
ATOM   982  H HG11 . VAL   A 1 41  ? 31.407 -0.987  -7.635  1.00 16.01 ?  41  VAL   A HG11 1 
ATOM   983  H HG12 . VAL   A 1 41  ? 31.262 -1.370  -6.100  1.00 16.01 ?  41  VAL   A HG12 1 
ATOM   984  H HG13 . VAL   A 1 41  ? 30.114 -0.545  -6.824  1.00 16.01 ?  41  VAL   A HG13 1 
ATOM   985  H HG21 . VAL   A 1 41  ? 31.818 1.297   -8.316  1.00 16.10 ?  41  VAL   A HG21 1 
ATOM   986  H HG22 . VAL   A 1 41  ? 30.654 1.958   -7.462  1.00 16.10 ?  41  VAL   A HG22 1 
ATOM   987  H HG23 . VAL   A 1 41  ? 32.158 2.421   -7.246  1.00 16.10 ?  41  VAL   A HG23 1 
ATOM   988  N N    A TYR   A 1 42  ? 31.630 3.456   -4.582  0.84 11.43 ?  42  TYR   A N    1 
ATOM   989  N N    B TYR   A 1 42  ? 31.638 3.457   -4.597  0.16 11.23 ?  42  TYR   A N    1 
ATOM   990  C CA   A TYR   A 1 42  ? 32.370 4.639   -4.164  0.84 11.44 ?  42  TYR   A CA   1 
ATOM   991  C CA   B TYR   A 1 42  ? 32.379 4.635   -4.172  0.16 11.25 ?  42  TYR   A CA   1 
ATOM   992  C C    A TYR   A 1 42  ? 32.111 5.011   -2.715  0.84 11.36 ?  42  TYR   A C    1 
ATOM   993  C C    B TYR   A 1 42  ? 32.104 5.012   -2.723  0.16 10.97 ?  42  TYR   A C    1 
ATOM   994  O O    A TYR   A 1 42  ? 32.672 6.002   -2.228  0.84 12.09 ?  42  TYR   A O    1 
ATOM   995  O O    B TYR   A 1 42  ? 32.670 5.996   -2.233  0.16 11.05 ?  42  TYR   A O    1 
ATOM   996  C CB   A TYR   A 1 42  ? 32.024 5.831   -5.077  0.84 12.62 ?  42  TYR   A CB   1 
ATOM   997  C CB   B TYR   A 1 42  ? 32.036 5.825   -5.078  0.16 11.81 ?  42  TYR   A CB   1 
ATOM   998  C CG   A TYR   A 1 42  ? 32.227 5.525   -6.547  0.84 13.31 ?  42  TYR   A CG   1 
ATOM   999  C CG   B TYR   A 1 42  ? 32.099 5.519   -6.560  0.16 12.27 ?  42  TYR   A CG   1 
ATOM   1000 C CD1  A TYR   A 1 42  ? 33.494 5.321   -7.070  0.84 13.98 ?  42  TYR   A CD1  1 
ATOM   1001 C CD1  B TYR   A 1 42  ? 33.317 5.364   -7.206  0.16 12.39 ?  42  TYR   A CD1  1 
ATOM   1002 C CD2  A TYR   A 1 42  ? 31.142 5.401   -7.404  0.84 14.59 ?  42  TYR   A CD2  1 
ATOM   1003 C CD2  B TYR   A 1 42  ? 30.938 5.392   -7.314  0.16 12.72 ?  42  TYR   A CD2  1 
ATOM   1004 C CE1  A TYR   A 1 42  ? 33.678 5.013   -8.412  0.84 14.35 ?  42  TYR   A CE1  1 
ATOM   1005 C CE1  B TYR   A 1 42  ? 33.381 5.085   -8.560  0.16 12.65 ?  42  TYR   A CE1  1 
ATOM   1006 C CE2  A TYR   A 1 42  ? 31.316 5.105   -8.744  0.84 15.33 ?  42  TYR   A CE2  1 
ATOM   1007 C CE2  B TYR   A 1 42  ? 30.992 5.116   -8.670  0.16 13.01 ?  42  TYR   A CE2  1 
ATOM   1008 C CZ   A TYR   A 1 42  ? 32.585 4.909   -9.243  0.84 15.01 ?  42  TYR   A CZ   1 
ATOM   1009 C CZ   B TYR   A 1 42  ? 32.216 4.962   -9.286  0.16 13.00 ?  42  TYR   A CZ   1 
ATOM   1010 O OH   A TYR   A 1 42  ? 32.749 4.608   -10.576 0.84 16.80 ?  42  TYR   A OH   1 
ATOM   1011 O OH   B TYR   A 1 42  ? 32.282 4.688   -10.633 0.16 13.52 ?  42  TYR   A OH   1 
ATOM   1012 H H    A TYR   A 1 42  ? 30.841 3.635   -4.880  0.84 13.72 ?  42  TYR   A H    1 
ATOM   1013 H H    B TYR   A 1 42  ? 30.854 3.636   -4.903  0.16 13.47 ?  42  TYR   A H    1 
ATOM   1014 H HA   A TYR   A 1 42  ? 33.316 4.472   -4.260  0.84 13.73 ?  42  TYR   A HA   1 
ATOM   1015 H HA   B TYR   A 1 42  ? 33.327 4.459   -4.262  0.16 13.50 ?  42  TYR   A HA   1 
ATOM   1016 H HB2  A TYR   A 1 42  ? 31.091 6.075   -4.948  0.84 15.14 ?  42  TYR   A HB2  1 
ATOM   1017 H HB2  B TYR   A 1 42  ? 31.135 6.121   -4.877  0.16 14.17 ?  42  TYR   A HB2  1 
ATOM   1018 H HB3  A TYR   A 1 42  ? 32.593 6.586   -4.850  0.84 15.14 ?  42  TYR   A HB3  1 
ATOM   1019 H HB3  B TYR   A 1 42  ? 32.664 6.542   -4.900  0.16 14.17 ?  42  TYR   A HB3  1 
ATOM   1020 H HD1  A TYR   A 1 42  ? 34.234 5.388   -6.511  0.84 16.77 ?  42  TYR   A HD1  1 
ATOM   1021 H HD1  B TYR   A 1 42  ? 34.104 5.444   -6.720  0.16 14.87 ?  42  TYR   A HD1  1 
ATOM   1022 H HD2  A TYR   A 1 42  ? 30.281 5.536   -7.072  0.84 17.50 ?  42  TYR   A HD2  1 
ATOM   1023 H HD2  B TYR   A 1 42  ? 30.110 5.495   -6.903  0.16 15.26 ?  42  TYR   A HD2  1 
ATOM   1024 H HE1  A TYR   A 1 42  ? 34.535 4.882   -8.752  0.84 17.21 ?  42  TYR   A HE1  1 
ATOM   1025 H HE1  B TYR   A 1 42  ? 34.205 4.981   -8.978  0.16 15.18 ?  42  TYR   A HE1  1 
ATOM   1026 H HE2  A TYR   A 1 42  ? 30.577 5.033   -9.305  0.84 18.40 ?  42  TYR   A HE2  1 
ATOM   1027 H HE2  B TYR   A 1 42  ? 30.207 5.032   -9.164  0.16 15.61 ?  42  TYR   A HE2  1 
ATOM   1028 H HH   A TYR   A 1 42  ? 33.564 4.500   -10.750 0.84 20.16 ?  42  TYR   A HH   1 
ATOM   1029 H HH   B TYR   A 1 42  ? 31.509 4.640   -10.957 0.16 16.22 ?  42  TYR   A HH   1 
ATOM   1030 N N    . LEU   A 1 43  ? 31.250 4.256   -2.033  1.00 10.71 ?  43  LEU   A N    1 
ATOM   1031 C CA   . LEU   A 1 43  ? 30.812 4.589   -0.681  1.00 10.55 ?  43  LEU   A CA   1 
ATOM   1032 C C    . LEU   A 1 43  ? 30.326 6.034   -0.577  1.00 10.83 ?  43  LEU   A C    1 
ATOM   1033 O O    . LEU   A 1 43  ? 30.588 6.729   0.405   1.00 11.78 ?  43  LEU   A O    1 
ATOM   1034 C CB   . LEU   A 1 43  ? 31.863 4.276   0.380   1.00 10.59 ?  43  LEU   A CB   1 
ATOM   1035 C CG   . LEU   A 1 43  ? 32.355 2.826   0.474   1.00 11.06 ?  43  LEU   A CG   1 
ATOM   1036 C CD1  . LEU   A 1 43  ? 33.409 2.706   1.562   1.00 12.09 ?  43  LEU   A CD1  1 
ATOM   1037 C CD2  . LEU   A 1 43  ? 31.210 1.845   0.723   1.00 11.69 ?  43  LEU   A CD2  1 
ATOM   1038 H H    A LEU   A 1 43  ? 30.895 3.530   -2.338  0.84 12.85 ?  43  LEU   A H    1 
ATOM   1039 H H    B LEU   A 1 43  ? 30.894 3.529   -2.337  0.16 12.85 ?  43  LEU   A H    1 
ATOM   1040 H HA   . LEU   A 1 43  ? 30.045 4.024   -0.477  1.00 12.66 ?  43  LEU   A HA   1 
ATOM   1041 H HB2  . LEU   A 1 43  ? 32.637 4.833   0.213   1.00 12.70 ?  43  LEU   A HB2  1 
ATOM   1042 H HB3  . LEU   A 1 43  ? 31.488 4.502   1.248   1.00 12.70 ?  43  LEU   A HB3  1 
ATOM   1043 H HG   . LEU   A 1 43  ? 32.775 2.587   -0.365  1.00 13.28 ?  43  LEU   A HG   1 
ATOM   1044 H HD11 . LEU   A 1 43  ? 33.714 1.785   1.609   1.00 14.51 ?  43  LEU   A HD11 1 
ATOM   1045 H HD12 . LEU   A 1 43  ? 34.156 3.289   1.348   1.00 14.51 ?  43  LEU   A HD12 1 
ATOM   1046 H HD13 . LEU   A 1 43  ? 33.022 2.968   2.412   1.00 14.51 ?  43  LEU   A HD13 1 
ATOM   1047 H HD21 . LEU   A 1 43  ? 31.581 0.959   0.863   1.00 14.03 ?  43  LEU   A HD21 1 
ATOM   1048 H HD22 . LEU   A 1 43  ? 30.720 2.126   1.511   1.00 14.03 ?  43  LEU   A HD22 1 
ATOM   1049 H HD23 . LEU   A 1 43  ? 30.626 1.842   -0.049  1.00 14.03 ?  43  LEU   A HD23 1 
ATOM   1050 N N    A LYS   A 1 44  ? 29.602 6.481   -1.603  0.84 10.84 ?  44  LYS   A N    1 
ATOM   1051 N N    B LYS   A 1 44  ? 29.579 6.474   -1.588  0.16 11.70 ?  44  LYS   A N    1 
ATOM   1052 C CA   A LYS   A 1 44  ? 28.963 7.796   -1.602  0.84 11.13 ?  44  LYS   A CA   1 
ATOM   1053 C CA   B LYS   A 1 44  ? 28.928 7.780   -1.570  0.16 12.87 ?  44  LYS   A CA   1 
ATOM   1054 C C    A LYS   A 1 44  ? 27.538 7.610   -1.103  0.84 10.41 ?  44  LYS   A C    1 
ATOM   1055 C C    B LYS   A 1 44  ? 27.502 7.593   -1.068  0.16 12.18 ?  44  LYS   A C    1 
ATOM   1056 O O    A LYS   A 1 44  ? 26.673 7.089   -1.815  0.84 11.49 ?  44  LYS   A O    1 
ATOM   1057 O O    B LYS   A 1 44  ? 26.636 7.094   -1.795  0.16 12.12 ?  44  LYS   A O    1 
ATOM   1058 C CB   A LYS   A 1 44  ? 28.998 8.415   -2.992  0.84 13.18 ?  44  LYS   A CB   1 
ATOM   1059 C CB   B LYS   A 1 44  ? 28.961 8.421   -2.957  0.16 14.85 ?  44  LYS   A CB   1 
ATOM   1060 C CG   A LYS   A 1 44  ? 30.370 8.905   -3.420  0.84 16.56 ?  44  LYS   A CG   1 
ATOM   1061 C CG   B LYS   A 1 44  ? 30.347 8.897   -3.381  0.16 16.90 ?  44  LYS   A CG   1 
ATOM   1062 C CD   A LYS   A 1 44  ? 31.027 9.814   -2.380  0.84 21.93 ?  44  LYS   A CD   1 
ATOM   1063 C CD   B LYS   A 1 44  ? 30.968 9.816   -2.331  0.16 19.06 ?  44  LYS   A CD   1 
ATOM   1064 C CE   A LYS   A 1 44  ? 32.343 10.376  -2.891  0.84 25.17 ?  44  LYS   A CE   1 
ATOM   1065 C CE   B LYS   A 1 44  ? 32.372 10.234  -2.709  0.16 20.62 ?  44  LYS   A CE   1 
ATOM   1066 N NZ   A LYS   A 1 44  ? 33.193 10.918  -1.795  0.84 26.99 ?  44  LYS   A NZ   1 
ATOM   1067 N NZ   B LYS   A 1 44  ? 33.028 11.016  -1.625  0.16 21.53 ?  44  LYS   A NZ   1 
ATOM   1068 H H    A LYS   A 1 44  ? 29.463 6.031   -2.323  0.84 13.01 ?  44  LYS   A H    1 
ATOM   1069 H H    B LYS   A 1 44  ? 29.430 6.027   -2.305  0.16 14.04 ?  44  LYS   A H    1 
ATOM   1070 H HA   A LYS   A 1 44  ? 29.418 8.378   -0.973  0.84 13.35 ?  44  LYS   A HA   1 
ATOM   1071 H HA   B LYS   A 1 44  ? 29.373 8.358   -0.935  0.16 15.44 ?  44  LYS   A HA   1 
ATOM   1072 H HB2  A LYS   A 1 44  ? 28.705 7.754   -3.637  0.84 15.81 ?  44  LYS   A HB2  1 
ATOM   1073 H HB2  B LYS   A 1 44  ? 28.661 7.771   -3.615  0.16 17.81 ?  44  LYS   A HB2  1 
ATOM   1074 H HB3  A LYS   A 1 44  ? 28.395 9.178   -3.009  0.84 15.81 ?  44  LYS   A HB3  1 
ATOM   1075 H HB3  B LYS   A 1 44  ? 28.371 9.192   -2.968  0.16 17.81 ?  44  LYS   A HB3  1 
ATOM   1076 H HG2  A LYS   A 1 44  ? 30.948 8.141   -3.562  0.84 19.87 ?  44  LYS   A HG2  1 
ATOM   1077 H HG2  B LYS   A 1 44  ? 30.928 8.129   -3.497  0.16 20.28 ?  44  LYS   A HG2  1 
ATOM   1078 H HG3  A LYS   A 1 44  ? 30.282 9.412   -4.245  0.84 19.87 ?  44  LYS   A HG3  1 
ATOM   1079 H HG3  B LYS   A 1 44  ? 30.277 9.393   -4.215  0.16 20.28 ?  44  LYS   A HG3  1 
ATOM   1080 H HD2  A LYS   A 1 44  ? 30.427 10.548  -2.172  0.84 26.31 ?  44  LYS   A HD2  1 
ATOM   1081 H HD2  B LYS   A 1 44  ? 30.414 10.608  -2.236  0.16 22.87 ?  44  LYS   A HD2  1 
ATOM   1082 H HD3  A LYS   A 1 44  ? 31.216 9.297   -1.579  0.84 26.31 ?  44  LYS   A HD3  1 
ATOM   1083 H HD3  B LYS   A 1 44  ? 31.032 9.349   -1.484  0.16 22.87 ?  44  LYS   A HD3  1 
ATOM   1084 H HE2  A LYS   A 1 44  ? 32.837 9.667   -3.333  0.84 30.21 ?  44  LYS   A HE2  1 
ATOM   1085 H HE2  B LYS   A 1 44  ? 32.904 9.439   -2.874  0.16 24.74 ?  44  LYS   A HE2  1 
ATOM   1086 H HE3  A LYS   A 1 44  ? 32.157 11.092  -3.515  0.84 30.21 ?  44  LYS   A HE3  1 
ATOM   1087 H HE3  B LYS   A 1 44  ? 32.336 10.784  -3.504  0.16 24.74 ?  44  LYS   A HE3  1 
ATOM   1088 H HZ1  A LYS   A 1 44  ? 33.952 11.239  -2.131  0.84 32.38 ?  44  LYS   A HZ1  1 
ATOM   1089 H HZ1  B LYS   A 1 44  ? 33.850 11.247  -1.874  0.16 25.84 ?  44  LYS   A HZ1  1 
ATOM   1090 H HZ2  A LYS   A 1 44  ? 32.763 11.576  -1.375  0.84 32.38 ?  44  LYS   A HZ2  1 
ATOM   1091 H HZ2  B LYS   A 1 44  ? 32.558 11.753  -1.456  0.16 25.84 ?  44  LYS   A HZ2  1 
ATOM   1092 H HZ3  A LYS   A 1 44  ? 33.382 10.277  -1.209  0.84 32.38 ?  44  LYS   A HZ3  1 
ATOM   1093 H HZ3  B LYS   A 1 44  ? 33.076 10.528  -0.882  0.16 25.84 ?  44  LYS   A HZ3  1 
ATOM   1094 N N    A HIS   A 1 45  ? 27.301 7.995   0.145   0.84 10.11 ?  45  HIS   A N    1 
ATOM   1095 N N    B HIS   A 1 45  ? 27.263 7.990   0.180   0.16 11.80 ?  45  HIS   A N    1 
ATOM   1096 C CA   A HIS   A 1 45  ? 26.066 7.637   0.840   0.84 10.29 ?  45  HIS   A CA   1 
ATOM   1097 C CA   B HIS   A 1 45  ? 25.989 7.741   0.851   0.16 11.56 ?  45  HIS   A CA   1 
ATOM   1098 C C    A HIS   A 1 45  ? 25.033 8.757   0.681   0.84 11.16 ?  45  HIS   A C    1 
ATOM   1099 C C    B HIS   A 1 45  ? 25.088 8.947   0.629   0.16 11.67 ?  45  HIS   A C    1 
ATOM   1100 O O    A HIS   A 1 45  ? 24.690 9.482   1.618   0.84 11.85 ?  45  HIS   A O    1 
ATOM   1101 O O    B HIS   A 1 45  ? 25.131 9.930   1.370   0.16 12.16 ?  45  HIS   A O    1 
ATOM   1102 C CB   A HIS   A 1 45  ? 26.361 7.368   2.303   0.84 10.26 ?  45  HIS   A CB   1 
ATOM   1103 C CB   B HIS   A 1 45  ? 26.221 7.476   2.332   0.16 11.06 ?  45  HIS   A CB   1 
ATOM   1104 C CG   A HIS   A 1 45  ? 27.471 6.392   2.520   0.84 9.96  ?  45  HIS   A CG   1 
ATOM   1105 C CG   B HIS   A 1 45  ? 27.366 6.552   2.604   0.16 10.36 ?  45  HIS   A CG   1 
ATOM   1106 N ND1  A HIS   A 1 45  ? 27.450 5.104   2.023   0.84 10.38 ?  45  HIS   A ND1  1 
ATOM   1107 N ND1  B HIS   A 1 45  ? 27.399 5.252   2.148   0.16 10.30 ?  45  HIS   A ND1  1 
ATOM   1108 C CD2  A HIS   A 1 45  ? 28.641 6.532   3.187   0.84 10.44 ?  45  HIS   A CD2  1 
ATOM   1109 C CD2  B HIS   A 1 45  ? 28.521 6.744   3.284   0.16 9.62  ?  45  HIS   A CD2  1 
ATOM   1110 C CE1  A HIS   A 1 45  ? 28.572 4.499   2.378   0.84 10.23 ?  45  HIS   A CE1  1 
ATOM   1111 C CE1  B HIS   A 1 45  ? 28.527 4.683   2.535   0.16 9.43  ?  45  HIS   A CE1  1 
ATOM   1112 N NE2  A HIS   A 1 45  ? 29.310 5.339   3.085   0.84 10.23 ?  45  HIS   A NE2  1 
ATOM   1113 N NE2  B HIS   A 1 45  ? 29.225 5.566   3.227   0.16 9.11  ?  45  HIS   A NE2  1 
ATOM   1114 H H    A HIS   A 1 45  ? 27.839 8.473   0.621   0.84 12.13 ?  45  HIS   A H    1 
ATOM   1115 H H    B HIS   A 1 45  ? 27.832 8.418   0.665   0.16 14.16 ?  45  HIS   A H    1 
ATOM   1116 H HA   A HIS   A 1 45  ? 25.698 6.827   0.450   0.84 12.35 ?  45  HIS   A HA   1 
ATOM   1117 H HA   B HIS   A 1 45  ? 25.566 6.963   0.461   0.16 13.87 ?  45  HIS   A HA   1 
ATOM   1118 H HB2  A HIS   A 1 45  ? 26.604 8.202   2.735   0.84 12.31 ?  45  HIS   A HB2  1 
ATOM   1119 H HB2  B HIS   A 1 45  ? 26.405 8.316   2.778   0.16 13.27 ?  45  HIS   A HB2  1 
ATOM   1120 H HB3  A HIS   A 1 45  ? 25.561 7.006   2.725   0.84 12.31 ?  45  HIS   A HB3  1 
ATOM   1121 H HB3  B HIS   A 1 45  ? 25.421 7.074   2.705   0.16 13.27 ?  45  HIS   A HB3  1 
ATOM   1122 H HD2  A HIS   A 1 45  ? 28.944 7.299   3.627   0.84 12.53 ?  45  HIS   A HD2  1 
ATOM   1123 H HD2  B HIS   A 1 45  ? 28.788 7.528   3.710   0.16 11.54 ?  45  HIS   A HD2  1 
ATOM   1124 H HE1  A HIS   A 1 45  ? 28.801 3.618   2.182   0.84 12.28 ?  45  HIS   A HE1  1 
ATOM   1125 H HE1  B HIS   A 1 45  ? 28.784 3.809   2.355   0.16 11.31 ?  45  HIS   A HE1  1 
ATOM   1126 H HE2  A HIS   A 1 45  ? 30.085 5.167   3.426   0.84 12.27 ?  45  HIS   A HE2  1 
ATOM   1127 H HE2  B HIS   A 1 45  ? 29.995 5.427   3.584   0.16 10.94 ?  45  HIS   A HE2  1 
ATOM   1128 N N    A GLY   A 1 46  ? 24.525 8.885   -0.538  0.84 12.45 ?  46  GLY   A N    1 
ATOM   1129 N N    B GLY   A 1 46  ? 24.260 8.870   -0.409  0.16 11.48 ?  46  GLY   A N    1 
ATOM   1130 C CA   A GLY   A 1 46  ? 23.731 10.056  -0.869  0.84 13.34 ?  46  GLY   A CA   1 
ATOM   1131 C CA   B GLY   A 1 46  ? 23.391 9.973   -0.766  0.16 11.14 ?  46  GLY   A CA   1 
ATOM   1132 C C    A GLY   A 1 46  ? 22.242 9.934   -0.625  0.84 12.82 ?  46  GLY   A C    1 
ATOM   1133 C C    B GLY   A 1 46  ? 21.947 9.798   -0.341  0.16 10.42 ?  46  GLY   A C    1 
ATOM   1134 O O    A GLY   A 1 46  ? 21.572 10.935  -0.344  0.84 13.56 ?  46  GLY   A O    1 
ATOM   1135 O O    B GLY   A 1 46  ? 21.346 10.734  0.194   0.16 10.03 ?  46  GLY   A O    1 
ATOM   1136 H H    A GLY   A 1 46  ? 24.606 8.315   -1.171  0.84 14.93 ?  46  GLY   A H    1 
ATOM   1137 H H    B GLY   A 1 46  ? 24.193 8.190   -0.926  0.16 13.77 ?  46  GLY   A H    1 
ATOM   1138 H HA2  A GLY   A 1 46  ? 24.050 10.810  -0.347  0.84 16.00 ?  46  GLY   A HA2  1 
ATOM   1139 H HA2  B GLY   A 1 46  ? 23.722 10.788  -0.357  0.16 13.37 ?  46  GLY   A HA2  1 
ATOM   1140 H HA3  A GLY   A 1 46  ? 23.853 10.263  -1.803  0.84 16.00 ?  46  GLY   A HA3  1 
ATOM   1141 H HA3  B GLY   A 1 46  ? 23.416 10.092  -1.728  0.16 13.37 ?  46  GLY   A HA3  1 
ATOM   1142 N N    A GLY   A 1 47  ? 21.705 8.728   -0.756  0.84 12.75 ?  47  GLY   A N    1 
ATOM   1143 N N    B GLY   A 1 47  ? 21.376 8.614   -0.563  0.16 10.48 ?  47  GLY   A N    1 
ATOM   1144 C CA   A GLY   A 1 47  ? 20.269 8.534   -0.727  0.84 13.00 ?  47  GLY   A CA   1 
ATOM   1145 C CA   B GLY   A 1 47  ? 19.963 8.410   -0.323  0.16 10.13 ?  47  GLY   A CA   1 
ATOM   1146 C C    A GLY   A 1 47  ? 19.945 7.096   -0.384  0.84 12.04 ?  47  GLY   A C    1 
ATOM   1147 C C    B GLY   A 1 47  ? 19.639 6.970   0.013   0.16 9.35  ?  47  GLY   A C    1 
ATOM   1148 O O    A GLY   A 1 47  ? 20.830 6.268   -0.147  0.84 12.46 ?  47  GLY   A O    1 
ATOM   1149 O O    B GLY   A 1 47  ? 20.524 6.122   0.148   0.16 9.19  ?  47  GLY   A O    1 
ATOM   1150 H H    A GLY   A 1 47  ? 22.151 8.006   -0.840  0.84 15.30 ?  47  GLY   A H    1 
ATOM   1151 H H    B GLY   A 1 47  ? 21.792 7.914   -0.843  0.16 12.57 ?  47  GLY   A H    1 
ATOM   1152 H HA2  A GLY   A 1 47  ? 19.856 9.118   -0.066  0.84 15.60 ?  47  GLY   A HA2  1 
ATOM   1153 H HA2  B GLY   A 1 47  ? 19.673 8.959   0.419   0.16 12.16 ?  47  GLY   A HA2  1 
ATOM   1154 H HA3  A GLY   A 1 47  ? 19.890 8.738   -1.599  0.84 15.60 ?  47  GLY   A HA3  1 
ATOM   1155 H HA3  B GLY   A 1 47  ? 19.459 8.664   -1.112  0.16 12.16 ?  47  GLY   A HA3  1 
ATOM   1156 N N    A GLY   A 1 48  ? 18.652 6.794   -0.375  0.84 12.20 ?  48  GLY   A N    1 
ATOM   1157 N N    B GLY   A 1 48  ? 18.340 6.704   0.147   0.16 9.09  ?  48  GLY   A N    1 
ATOM   1158 C CA   A GLY   A 1 48  ? 18.241 5.461   0.008   0.84 12.05 ?  48  GLY   A CA   1 
ATOM   1159 C CA   B GLY   A 1 48  ? 17.902 5.379   0.546   0.16 8.30  ?  48  GLY   A CA   1 
ATOM   1160 C C    A GLY   A 1 48  ? 18.640 5.142   1.439   0.84 11.01 ?  48  GLY   A C    1 
ATOM   1161 C C    B GLY   A 1 48  ? 18.525 4.988   1.870   0.16 8.67  ?  48  GLY   A C    1 
ATOM   1162 O O    A GLY   A 1 48  ? 18.782 6.028   2.294   0.84 11.16 ?  48  GLY   A O    1 
ATOM   1163 O O    B GLY   A 1 48  ? 18.606 5.788   2.811   0.16 8.74  ?  48  GLY   A O    1 
ATOM   1164 H H    A GLY   A 1 48  ? 18.013 7.329   -0.570  0.84 14.64 ?  48  GLY   A H    1 
ATOM   1165 H H    B GLY   A 1 48  ? 17.699 7.269   0.015   0.16 10.90 ?  48  GLY   A H    1 
ATOM   1166 H HA2  A GLY   A 1 48  ? 17.286 5.367   -0.077  0.84 14.46 ?  48  GLY   A HA2  1 
ATOM   1167 H HA2  B GLY   A 1 48  ? 16.931 5.360   0.628   0.16 9.96  ?  48  GLY   A HA2  1 
ATOM   1168 H HA3  A GLY   A 1 48  ? 18.672 4.806   -0.573  0.84 14.46 ?  48  GLY   A HA3  1 
ATOM   1169 H HA3  B GLY   A 1 48  ? 18.162 4.726   -0.127  0.16 9.96  ?  48  GLY   A HA3  1 
ATOM   1170 N N    A VAL   A 1 49  ? 18.819 3.844   1.704   0.84 11.46 ?  49  VAL   A N    1 
ATOM   1171 N N    B VAL   A 1 49  ? 18.996 3.743   1.940   0.16 9.25  ?  49  VAL   A N    1 
ATOM   1172 C CA   A VAL   A 1 49  ? 19.285 3.398   3.015   0.84 11.24 ?  49  VAL   A CA   1 
ATOM   1173 C CA   B VAL   A 1 49  ? 19.587 3.235   3.174   0.16 9.26  ?  49  VAL   A CA   1 
ATOM   1174 C C    A VAL   A 1 49  ? 20.604 4.072   3.383   0.84 10.30 ?  49  VAL   A C    1 
ATOM   1175 C C    B VAL   A 1 49  ? 20.869 3.990   3.507   0.16 9.07  ?  49  VAL   A C    1 
ATOM   1176 O O    A VAL   A 1 49  ? 20.800 4.487   4.530   0.84 10.55 ?  49  VAL   A O    1 
ATOM   1177 O O    B VAL   A 1 49  ? 21.093 4.392   4.654   0.16 9.06  ?  49  VAL   A O    1 
ATOM   1178 C CB   A VAL   A 1 49  ? 19.406 1.860   3.043   0.84 12.60 ?  49  VAL   A CB   1 
ATOM   1179 C CB   B VAL   A 1 49  ? 19.828 1.719   3.067   0.16 9.32  ?  49  VAL   A CB   1 
ATOM   1180 C CG1  A VAL   A 1 49  ? 20.172 1.393   4.290   0.84 13.00 ?  49  VAL   A CG1  1 
ATOM   1181 C CG1  B VAL   A 1 49  ? 20.649 1.233   4.250   0.16 8.59  ?  49  VAL   A CG1  1 
ATOM   1182 C CG2  A VAL   A 1 49  ? 18.028 1.215   2.985   0.84 14.59 ?  49  VAL   A CG2  1 
ATOM   1183 C CG2  B VAL   A 1 49  ? 18.505 0.968   2.983   0.16 9.86  ?  49  VAL   A CG2  1 
ATOM   1184 H H    A VAL   A 1 49  ? 18.686 3.202   1.146   0.84 13.75 ?  49  VAL   A H    1 
ATOM   1185 H H    B VAL   A 1 49  ? 18.997 3.184   1.287   0.16 11.09 ?  49  VAL   A H    1 
ATOM   1186 H HA   A VAL   A 1 49  ? 18.634 3.644   3.686   0.84 13.49 ?  49  VAL   A HA   1 
ATOM   1187 H HA   B VAL   A 1 49  ? 18.965 3.381   3.900   0.16 11.11 ?  49  VAL   A HA   1 
ATOM   1188 H HB   A VAL   A 1 49  ? 19.910 1.563   2.267   0.84 15.12 ?  49  VAL   A HB   1 
ATOM   1189 H HB   B VAL   A 1 49  ? 20.330 1.532   2.257   0.16 11.18 ?  49  VAL   A HB   1 
ATOM   1190 H HG11 A VAL   A 1 49  ? 19.994 0.450   4.436   0.84 15.60 ?  49  VAL   A HG11 1 
ATOM   1191 H HG11 B VAL   A 1 49  ? 20.544 0.273   4.335   0.16 10.31 ?  49  VAL   A HG11 1 
ATOM   1192 H HG12 A VAL   A 1 49  ? 21.120 1.534   4.159   0.84 15.60 ?  49  VAL   A HG12 1 
ATOM   1193 H HG12 B VAL   A 1 49  ? 21.585 1.448   4.099   0.16 10.31 ?  49  VAL   A HG12 1 
ATOM   1194 H HG13 A VAL   A 1 49  ? 19.861 1.904   5.057   0.84 15.60 ?  49  VAL   A HG13 1 
ATOM   1195 H HG13 B VAL   A 1 49  ? 20.334 1.671   5.055   0.16 10.31 ?  49  VAL   A HG13 1 
ATOM   1196 H HG21 A VAL   A 1 49  ? 18.130 0.250   3.002   0.84 17.50 ?  49  VAL   A HG21 1 
ATOM   1197 H HG21 B VAL   A 1 49  ? 18.684 0.017   2.918   0.16 11.83 ?  49  VAL   A HG21 1 
ATOM   1198 H HG22 A VAL   A 1 49  ? 17.515 1.508   3.753   0.84 17.50 ?  49  VAL   A HG22 1 
ATOM   1199 H HG22 B VAL   A 1 49  ? 17.988 1.153   3.783   0.16 11.83 ?  49  VAL   A HG22 1 
ATOM   1200 H HG23 A VAL   A 1 49  ? 17.593 1.489   2.166   0.84 17.50 ?  49  VAL   A HG23 1 
ATOM   1201 H HG23 B VAL   A 1 49  ? 18.021 1.269   2.199   0.16 11.83 ?  49  VAL   A HG23 1 
ATOM   1202 N N    A ALA   A 1 50  ? 21.541 4.146   2.436   0.84 9.88  ?  50  ALA   A N    1 
ATOM   1203 N N    B ALA   A 1 50  ? 21.733 4.188   2.509   0.16 9.08  ?  50  ALA   A N    1 
ATOM   1204 C CA   A ALA   A 1 50  ? 22.862 4.695   2.745   0.84 10.10 ?  50  ALA   A CA   1 
ATOM   1205 C CA   B ALA   A 1 50  ? 23.031 4.804   2.765   0.16 9.11  ?  50  ALA   A CA   1 
ATOM   1206 C C    A ALA   A 1 50  ? 22.774 6.149   3.183   0.84 10.02 ?  50  ALA   A C    1 
ATOM   1207 C C    B ALA   A 1 50  ? 22.873 6.256   3.196   0.16 9.13  ?  50  ALA   A C    1 
ATOM   1208 O O    A ALA   A 1 50  ? 23.415 6.559   4.160   0.84 10.43 ?  50  ALA   A O    1 
ATOM   1209 O O    B ALA   A 1 50  ? 23.486 6.693   4.178   0.16 8.92  ?  50  ALA   A O    1 
ATOM   1210 C CB   A ALA   A 1 50  ? 23.774 4.567   1.529   0.84 10.16 ?  50  ALA   A CB   1 
ATOM   1211 C CB   B ALA   A 1 50  ? 23.918 4.694   1.524   0.16 9.16  ?  50  ALA   A CB   1 
ATOM   1212 H H    A ALA   A 1 50  ? 21.442 3.888   1.621   0.84 11.85 ?  50  ALA   A H    1 
ATOM   1213 H H    B ALA   A 1 50  ? 21.587 3.988   1.686   0.16 10.89 ?  50  ALA   A H    1 
ATOM   1214 H HA   A ALA   A 1 50  ? 23.259 4.187   3.471   0.84 12.12 ?  50  ALA   A HA   1 
ATOM   1215 H HA   B ALA   A 1 50  ? 23.469 4.330   3.485   0.16 10.93 ?  50  ALA   A HA   1 
ATOM   1216 H HB1  A ALA   A 1 50  ? 24.644 4.936   1.745   0.84 12.19 ?  50  ALA   A HB1  1 
ATOM   1217 H HB1  B ALA   A 1 50  ? 24.780 5.097   1.712   0.16 10.99 ?  50  ALA   A HB1  1 
ATOM   1218 H HB2  A ALA   A 1 50  ? 23.859 3.631   1.291   0.84 12.19 ?  50  ALA   A HB2  1 
ATOM   1219 H HB2  B ALA   A 1 50  ? 24.035 3.756   1.301   0.16 10.99 ?  50  ALA   A HB2  1 
ATOM   1220 H HB3  A ALA   A 1 50  ? 23.380 5.061   0.789   0.84 12.19 ?  50  ALA   A HB3  1 
ATOM   1221 H HB3  B ALA   A 1 50  ? 23.491 5.156   0.785   0.16 10.99 ?  50  ALA   A HB3  1 
ATOM   1222 N N    A GLY   A 1 51  ? 21.994 6.955   2.461   0.84 10.62 ?  51  GLY   A N    1 
ATOM   1223 N N    B GLY   A 1 51  ? 22.051 7.019   2.475   0.16 9.65  ?  51  GLY   A N    1 
ATOM   1224 C CA   A GLY   A 1 51  ? 21.847 8.345   2.847   0.84 11.11 ?  51  GLY   A CA   1 
ATOM   1225 C CA   B GLY   A 1 51  ? 21.829 8.404   2.852   0.16 10.06 ?  51  GLY   A CA   1 
ATOM   1226 C C    A GLY   A 1 51  ? 21.252 8.486   4.232   0.84 10.77 ?  51  GLY   A C    1 
ATOM   1227 C C    B GLY   A 1 51  ? 21.200 8.535   4.225   0.16 10.28 ?  51  GLY   A C    1 
ATOM   1228 O O    A GLY   A 1 51  ? 21.656 9.359   5.004   0.84 11.45 ?  51  GLY   A O    1 
ATOM   1229 O O    B GLY   A 1 51  ? 21.534 9.446   4.987   0.16 10.20 ?  51  GLY   A O    1 
ATOM   1230 H H    A GLY   A 1 51  ? 21.559 6.720   1.755   0.84 12.74 ?  51  GLY   A H    1 
ATOM   1231 H H    B GLY   A 1 51  ? 21.621 6.761   1.776   0.16 11.58 ?  51  GLY   A H    1 
ATOM   1232 H HA2  A GLY   A 1 51  ? 22.713 8.777   2.839   0.84 13.33 ?  51  GLY   A HA2  1 
ATOM   1233 H HA2  B GLY   A 1 51  ? 22.674 8.879   2.855   0.16 12.08 ?  51  GLY   A HA2  1 
ATOM   1234 H HA3  A GLY   A 1 51  ? 21.267 8.795   2.213   0.84 13.33 ?  51  GLY   A HA3  1 
ATOM   1235 H HA3  B GLY   A 1 51  ? 21.242 8.824   2.205   0.16 12.08 ?  51  GLY   A HA3  1 
ATOM   1236 N N    . ALA   A 1 52  ? 20.282 7.626   4.561   1.00 10.68 ?  52  ALA   A N    1 
ATOM   1237 C CA   . ALA   A 1 52  ? 19.642 7.679   5.870   1.00 11.27 ?  52  ALA   A CA   1 
ATOM   1238 C C    . ALA   A 1 52  ? 20.602 7.262   6.984   1.00 10.73 ?  52  ALA   A C    1 
ATOM   1239 O O    . ALA   A 1 52  ? 20.677 7.920   8.025   1.00 11.67 ?  52  ALA   A O    1 
ATOM   1240 C CB   . ALA   A 1 52  ? 18.376 6.817   5.866   1.00 12.76 ?  52  ALA   A CB   1 
ATOM   1241 H H    A ALA   A 1 52  ? 19.988 6.998   4.046   0.84 12.81 ?  52  ALA   A H    1 
ATOM   1242 H H    B ALA   A 1 52  ? 20.025 6.972   4.058   0.16 12.81 ?  52  ALA   A H    1 
ATOM   1243 H HA   . ALA   A 1 52  ? 19.374 8.588   6.044   1.00 13.52 ?  52  ALA   A HA   1 
ATOM   1244 H HB1  . ALA   A 1 52  ? 17.957 6.868   6.743   1.00 15.31 ?  52  ALA   A HB1  1 
ATOM   1245 H HB2  . ALA   A 1 52  ? 17.765 7.156   5.192   1.00 15.31 ?  52  ALA   A HB2  1 
ATOM   1246 H HB3  . ALA   A 1 52  ? 18.612 5.899   5.667   1.00 15.31 ?  52  ALA   A HB3  1 
ATOM   1247 N N    A LEU   A 1 53  ? 21.323 6.153   6.795   0.84 10.52 ?  53  LEU   A N    1 
ATOM   1248 N N    B LEU   A 1 53  ? 21.358 6.179   6.775   0.16 10.37 ?  53  LEU   A N    1 
ATOM   1249 C CA   A LEU   A 1 53  ? 22.289 5.731   7.808   0.84 10.84 ?  53  LEU   A CA   1 
ATOM   1250 C CA   B LEU   A 1 53  ? 22.348 5.769   7.770   0.16 10.37 ?  53  LEU   A CA   1 
ATOM   1251 C C    A LEU   A 1 53  ? 23.354 6.799   8.004   0.84 10.41 ?  53  LEU   A C    1 
ATOM   1252 C C    B LEU   A 1 53  ? 23.361 6.882   8.017   0.16 10.29 ?  53  LEU   A C    1 
ATOM   1253 O O    A LEU   A 1 53  ? 23.696 7.148   9.137   0.84 11.63 ?  53  LEU   A O    1 
ATOM   1254 O O    B LEU   A 1 53  ? 23.623 7.256   9.166   0.16 10.40 ?  53  LEU   A O    1 
ATOM   1255 C CB   A LEU   A 1 53  ? 22.941 4.394   7.430   0.84 11.31 ?  53  LEU   A CB   1 
ATOM   1256 C CB   B LEU   A 1 53  ? 23.062 4.484   7.331   0.16 10.26 ?  53  LEU   A CB   1 
ATOM   1257 C CG   A LEU   A 1 53  ? 22.043 3.151   7.478   0.84 11.86 ?  53  LEU   A CG   1 
ATOM   1258 C CG   B LEU   A 1 53  ? 22.346 3.131   7.457   0.16 10.27 ?  53  LEU   A CG   1 
ATOM   1259 C CD1  A LEU   A 1 53  ? 22.758 1.959   6.854   0.84 11.65 ?  53  LEU   A CD1  1 
ATOM   1260 C CD1  B LEU   A 1 53  ? 23.239 2.002   6.941   0.16 9.73  ?  53  LEU   A CD1  1 
ATOM   1261 C CD2  A LEU   A 1 53  ? 21.624 2.820   8.897   0.84 13.85 ?  53  LEU   A CD2  1 
ATOM   1262 C CD2  B LEU   A 1 53  ? 21.921 2.845   8.889   0.16 10.87 ?  53  LEU   A CD2  1 
ATOM   1263 H H    A LEU   A 1 53  ? 21.280 5.639   6.102   0.84 12.63 ?  53  LEU   A H    1 
ATOM   1264 H H    B LEU   A 1 53  ? 21.322 5.674   6.078   0.16 12.44 ?  53  LEU   A H    1 
ATOM   1265 H HA   A LEU   A 1 53  ? 21.829 5.609   8.649   0.84 13.00 ?  53  LEU   A HA   1 
ATOM   1266 H HA   B LEU   A 1 53  ? 21.897 5.591   8.607   0.16 12.44 ?  53  LEU   A HA   1 
ATOM   1267 H HB2  A LEU   A 1 53  ? 23.285 4.466   6.523   0.84 13.57 ?  53  LEU   A HB2  1 
ATOM   1268 H HB2  B LEU   A 1 53  ? 23.294 4.581   6.396   0.16 12.31 ?  53  LEU   A HB2  1 
ATOM   1269 H HB3  A LEU   A 1 53  ? 23.683 4.233   8.036   0.84 13.57 ?  53  LEU   A HB3  1 
ATOM   1270 H HB3  B LEU   A 1 53  ? 23.877 4.409   7.850   0.16 12.31 ?  53  LEU   A HB3  1 
ATOM   1271 H HG   A LEU   A 1 53  ? 21.242 3.325   6.956   0.84 14.23 ?  53  LEU   A HG   1 
ATOM   1272 H HG   B LEU   A 1 53  ? 21.549 3.144   6.908   0.16 12.32 ?  53  LEU   A HG   1 
ATOM   1273 H HD11 A LEU   A 1 53  ? 22.169 1.188   6.893   0.84 13.98 ?  53  LEU   A HD11 1 
ATOM   1274 H HD11 B LEU   A 1 53  ? 22.767 1.157   7.031   0.16 11.67 ?  53  LEU   A HD11 1 
ATOM   1275 H HD12 A LEU   A 1 53  ? 22.969 2.166   5.930   0.84 13.98 ?  53  LEU   A HD12 1 
ATOM   1276 H HD12 B LEU   A 1 53  ? 23.449 2.164   6.008   0.16 11.67 ?  53  LEU   A HD12 1 
ATOM   1277 H HD13 A LEU   A 1 53  ? 23.569 1.784   7.351   0.84 13.98 ?  53  LEU   A HD13 1 
ATOM   1278 H HD13 B LEU   A 1 53  ? 24.056 1.978   7.464   0.16 11.67 ?  53  LEU   A HD13 1 
ATOM   1279 H HD21 A LEU   A 1 53  ? 21.096 2.006   8.889   0.84 16.62 ?  53  LEU   A HD21 1 
ATOM   1280 H HD21 B LEU   A 1 53  ? 21.495 1.972   8.925   0.16 13.04 ?  53  LEU   A HD21 1 
ATOM   1281 H HD22 A LEU   A 1 53  ? 22.419 2.693   9.439   0.84 16.62 ?  53  LEU   A HD22 1 
ATOM   1282 H HD22 B LEU   A 1 53  ? 22.703 2.853   9.460   0.16 13.04 ?  53  LEU   A HD22 1 
ATOM   1283 H HD23 A LEU   A 1 53  ? 21.097 3.552   9.252   0.84 16.62 ?  53  LEU   A HD23 1 
ATOM   1284 H HD23 B LEU   A 1 53  ? 21.294 3.527   9.176   0.16 13.04 ?  53  LEU   A HD23 1 
ATOM   1285 N N    A ASN   A 1 54  ? 23.870 7.347   6.909   0.84 9.97  ?  54  ASN   A N    1 
ATOM   1286 N N    B ASN   A 1 54  ? 23.930 7.435   6.944   0.16 10.40 ?  54  ASN   A N    1 
ATOM   1287 C CA   A ASN   A 1 54  ? 24.925 8.344   7.040   0.84 10.08 ?  54  ASN   A CA   1 
ATOM   1288 C CA   B ASN   A 1 54  ? 24.967 8.450   7.104   0.16 10.49 ?  54  ASN   A CA   1 
ATOM   1289 C C    A ASN   A 1 54  ? 24.418 9.589   7.766   0.84 10.73 ?  54  ASN   A C    1 
ATOM   1290 C C    B ASN   A 1 54  ? 24.421 9.698   7.785   0.16 10.65 ?  54  ASN   A C    1 
ATOM   1291 O O    A ASN   A 1 54  ? 25.104 10.130  8.643   0.84 11.00 ?  54  ASN   A O    1 
ATOM   1292 O O    B ASN   A 1 54  ? 25.103 10.306  8.619   0.16 10.57 ?  54  ASN   A O    1 
ATOM   1293 C CB   A ASN   A 1 54  ? 25.485 8.713   5.676   0.84 10.62 ?  54  ASN   A CB   1 
ATOM   1294 C CB   B ASN   A 1 54  ? 25.580 8.801   5.749   0.16 10.56 ?  54  ASN   A CB   1 
ATOM   1295 C CG   A ASN   A 1 54  ? 26.518 9.800   5.787   0.84 10.43 ?  54  ASN   A CG   1 
ATOM   1296 C CG   B ASN   A 1 54  ? 26.536 9.971   5.839   0.16 10.21 ?  54  ASN   A CG   1 
ATOM   1297 O OD1  A ASN   A 1 54  ? 27.505 9.656   6.521   0.84 10.47 ?  54  ASN   A OD1  1 
ATOM   1298 O OD1  B ASN   A 1 54  ? 27.642 9.843   6.365   0.16 10.38 ?  54  ASN   A OD1  1 
ATOM   1299 N ND2  A ASN   A 1 54  ? 26.292 10.913  5.105   0.84 11.05 ?  54  ASN   A ND2  1 
ATOM   1300 N ND2  B ASN   A 1 54  ? 26.112 11.124  5.337   0.16 10.11 ?  54  ASN   A ND2  1 
ATOM   1301 H H    A ASN   A 1 54  ? 23.623 7.173   6.104   0.84 11.96 ?  54  ASN   A H    1 
ATOM   1302 H H    B ASN   A 1 54  ? 23.730 7.250   6.131   0.16 12.48 ?  54  ASN   A H    1 
ATOM   1303 H HA   A ASN   A 1 54  ? 25.641 7.965   7.568   0.84 12.09 ?  54  ASN   A HA   1 
ATOM   1304 H HA   B ASN   A 1 54  ? 25.669 8.095   7.666   0.16 12.59 ?  54  ASN   A HA   1 
ATOM   1305 H HB2  A ASN   A 1 54  ? 25.903 7.924   5.284   0.84 12.74 ?  54  ASN   A HB2  1 
ATOM   1306 H HB2  B ASN   A 1 54  ? 26.074 8.033   5.420   0.16 12.67 ?  54  ASN   A HB2  1 
ATOM   1307 H HB3  A ASN   A 1 54  ? 24.766 9.025   5.107   0.84 12.74 ?  54  ASN   A HB3  1 
ATOM   1308 H HB3  B ASN   A 1 54  ? 24.872 9.034   5.130   0.16 12.67 ?  54  ASN   A HB3  1 
ATOM   1309 H HD21 A ASN   A 1 54  ? 26.857 11.556  5.145   0.84 13.26 ?  54  ASN   A HD21 1 
ATOM   1310 H HD21 B ASN   A 1 54  ? 26.617 11.818  5.369   0.16 12.13 ?  54  ASN   A HD21 1 
ATOM   1311 H HD22 A ASN   A 1 54  ? 25.590 10.978  4.615   0.84 13.26 ?  54  ASN   A HD22 1 
ATOM   1312 H HD22 B ASN   A 1 54  ? 25.332 11.175  4.977   0.16 12.13 ?  54  ASN   A HD22 1 
ATOM   1313 N N    A LYS   A 1 55  ? 23.211 10.052  7.424   0.84 10.85 ?  55  LYS   A N    1 
ATOM   1314 N N    B LYS   A 1 55  ? 23.195 10.098  7.444   0.16 10.88 ?  55  LYS   A N    1 
ATOM   1315 C CA   A LYS   A 1 55  ? 22.636 11.209  8.101   0.84 11.65 ?  55  LYS   A CA   1 
ATOM   1316 C CA   B LYS   A 1 55  ? 22.585 11.240  8.114   0.16 11.48 ?  55  LYS   A CA   1 
ATOM   1317 C C    A LYS   A 1 55  ? 22.547 10.971  9.602   0.84 11.80 ?  55  LYS   A C    1 
ATOM   1318 C C    B LYS   A 1 55  ? 22.479 10.994  9.612   0.16 11.77 ?  55  LYS   A C    1 
ATOM   1319 O O    A LYS   A 1 55  ? 22.832 11.871  10.402  0.84 12.59 ?  55  LYS   A O    1 
ATOM   1320 O O    B LYS   A 1 55  ? 22.699 11.906  10.419  0.16 11.75 ?  55  LYS   A O    1 
ATOM   1321 C CB   A LYS   A 1 55  ? 21.259 11.507  7.502   0.84 12.43 ?  55  LYS   A CB   1 
ATOM   1322 C CB   B LYS   A 1 55  ? 21.207 11.518  7.512   0.16 11.97 ?  55  LYS   A CB   1 
ATOM   1323 C CG   A LYS   A 1 55  ? 20.526 12.687  8.117   0.84 13.75 ?  55  LYS   A CG   1 
ATOM   1324 C CG   B LYS   A 1 55  ? 20.466 12.679  8.152   0.16 12.65 ?  55  LYS   A CG   1 
ATOM   1325 C CD   A LYS   A 1 55  ? 19.208 12.944  7.374   0.84 14.75 ?  55  LYS   A CD   1 
ATOM   1326 C CD   B LYS   A 1 55  ? 19.069 12.817  7.569   0.16 13.22 ?  55  LYS   A CD   1 
ATOM   1327 C CE   A LYS   A 1 55  ? 18.368 14.020  8.043   0.84 16.69 ?  55  LYS   A CE   1 
ATOM   1328 C CE   B LYS   A 1 55  ? 18.331 14.002  8.167   0.16 13.86 ?  55  LYS   A CE   1 
ATOM   1329 N NZ   A LYS   A 1 55  ? 17.057 14.209  7.360   0.84 17.73 ?  55  LYS   A NZ   1 
ATOM   1330 N NZ   B LYS   A 1 55  ? 16.946 14.113  7.636   0.16 14.17 ?  55  LYS   A NZ   1 
ATOM   1331 H H    A LYS   A 1 55  ? 22.704 9.707   6.817   0.84 13.02 ?  55  LYS   A H    1 
ATOM   1332 H H    B LYS   A 1 55  ? 22.701 9.729   6.844   0.16 13.05 ?  55  LYS   A H    1 
ATOM   1333 H HA   A LYS   A 1 55  ? 23.203 11.979  7.949   0.84 13.98 ?  55  LYS   A HA   1 
ATOM   1334 H HA   B LYS   A 1 55  ? 23.136 12.025  7.976   0.16 13.78 ?  55  LYS   A HA   1 
ATOM   1335 H HB2  A LYS   A 1 55  ? 21.370 11.695  6.556   0.84 14.92 ?  55  LYS   A HB2  1 
ATOM   1336 H HB2  B LYS   A 1 55  ? 21.315 11.724  6.569   0.16 14.36 ?  55  LYS   A HB2  1 
ATOM   1337 H HB3  A LYS   A 1 55  ? 20.698 10.723  7.612   0.84 14.92 ?  55  LYS   A HB3  1 
ATOM   1338 H HB3  B LYS   A 1 55  ? 20.656 10.726  7.612   0.16 14.36 ?  55  LYS   A HB3  1 
ATOM   1339 H HG2  A LYS   A 1 55  ? 20.320 12.489  9.045   0.84 16.50 ?  55  LYS   A HG2  1 
ATOM   1340 H HG2  B LYS   A 1 55  ? 20.380 12.525  9.106   0.16 15.18 ?  55  LYS   A HG2  1 
ATOM   1341 H HG3  A LYS   A 1 55  ? 21.077 13.479  8.051   0.84 16.50 ?  55  LYS   A HG3  1 
ATOM   1342 H HG3  B LYS   A 1 55  ? 20.950 13.502  7.984   0.16 15.18 ?  55  LYS   A HG3  1 
ATOM   1343 H HD2  A LYS   A 1 55  ? 19.409 13.233  6.469   0.84 17.70 ?  55  LYS   A HD2  1 
ATOM   1344 H HD2  B LYS   A 1 55  ? 19.134 12.948  6.610   0.16 15.86 ?  55  LYS   A HD2  1 
ATOM   1345 H HD3  A LYS   A 1 55  ? 18.692 12.122  7.353   0.84 17.70 ?  55  LYS   A HD3  1 
ATOM   1346 H HD3  B LYS   A 1 55  ? 18.561 12.012  7.763   0.16 15.86 ?  55  LYS   A HD3  1 
ATOM   1347 H HE2  A LYS   A 1 55  ? 18.197 13.760  8.962   0.84 20.03 ?  55  LYS   A HE2  1 
ATOM   1348 H HE2  B LYS   A 1 55  ? 18.280 13.894  9.130   0.16 16.64 ?  55  LYS   A HE2  1 
ATOM   1349 H HE3  A LYS   A 1 55  ? 18.849 14.859  8.016   0.84 20.03 ?  55  LYS   A HE3  1 
ATOM   1350 H HE3  B LYS   A 1 55  ? 18.808 14.818  7.946   0.16 16.64 ?  55  LYS   A HE3  1 
ATOM   1351 H HZ1  A LYS   A 1 55  ? 16.478 14.594  7.917   0.84 21.28 ?  55  LYS   A HZ1  1 
ATOM   1352 H HZ1  B LYS   A 1 55  ? 16.430 14.537  8.223   0.16 17.00 ?  55  LYS   A HZ1  1 
ATOM   1353 H HZ2  A LYS   A 1 55  ? 17.156 14.729  6.646   0.84 21.28 ?  55  LYS   A HZ2  1 
ATOM   1354 H HZ2  B LYS   A 1 55  ? 16.948 14.570  6.872   0.16 17.00 ?  55  LYS   A HZ2  1 
ATOM   1355 H HZ3  A LYS   A 1 55  ? 16.727 13.422  7.104   0.84 21.28 ?  55  LYS   A HZ3  1 
ATOM   1356 H HZ3  B LYS   A 1 55  ? 16.610 13.302  7.489   0.16 17.00 ?  55  LYS   A HZ3  1 
ATOM   1357 N N    . ALA   A 1 56  ? 22.148 9.762   10.005  1.00 12.10 ?  56  ALA   A N    1 
ATOM   1358 C CA   . ALA   A 1 56  ? 22.027 9.436   11.420  1.00 12.80 ?  56  ALA   A CA   1 
ATOM   1359 C C    . ALA   A 1 56  ? 23.371 9.465   12.147  1.00 12.81 ?  56  ALA   A C    1 
ATOM   1360 O O    . ALA   A 1 56  ? 23.395 9.651   13.367  1.00 14.15 ?  56  ALA   A O    1 
ATOM   1361 C CB   . ALA   A 1 56  ? 21.337 8.077   11.587  1.00 13.66 ?  56  ALA   A CB   1 
ATOM   1362 H H    A ALA   A 1 56  ? 21.941 9.119   9.474   0.84 14.52 ?  56  ALA   A H    1 
ATOM   1363 H H    B ALA   A 1 56  ? 21.987 9.109   9.471   0.16 14.52 ?  56  ALA   A H    1 
ATOM   1364 H HA   . ALA   A 1 56  ? 21.462 10.095  11.841  1.00 15.36 ?  56  ALA   A HA   1 
ATOM   1365 H HB1  . ALA   A 1 56  ? 21.263 7.873   12.535  1.00 16.39 ?  56  ALA   A HB1  1 
ATOM   1366 H HB2  . ALA   A 1 56  ? 20.449 8.123   11.194  1.00 16.39 ?  56  ALA   A HB2  1 
ATOM   1367 H HB3  . ALA   A 1 56  ? 21.859 7.393   11.143  1.00 16.39 ?  56  ALA   A HB3  1 
ATOM   1368 N N    . THR   A 1 57  ? 24.486 9.279   11.430  1.00 11.73 ?  57  THR   A N    1 
ATOM   1369 C CA   . THR   A 1 57  ? 25.830 9.402   12.004  1.00 11.74 ?  57  THR   A CA   1 
ATOM   1370 C C    . THR   A 1 57  ? 26.379 10.823  11.932  1.00 12.15 ?  57  THR   A C    1 
ATOM   1371 O O    . THR   A 1 57  ? 27.561 11.034  12.231  1.00 12.77 ?  57  THR   A O    1 
ATOM   1372 C CB   . THR   A 1 57  ? 26.840 8.456   11.327  1.00 11.72 ?  57  THR   A CB   1 
ATOM   1373 O OG1  . THR   A 1 57  ? 27.226 8.962   10.037  1.00 11.41 ?  57  THR   A OG1  1 
ATOM   1374 C CG2  . THR   A 1 57  ? 26.309 7.037   11.207  1.00 11.56 ?  57  THR   A CG2  1 
ATOM   1375 H H    . THR   A 1 57  ? 24.488 9.052   10.596  1.00 14.08 ?  57  THR   A H    1 
ATOM   1376 H HA   . THR   A 1 57  ? 25.786 9.138   12.941  1.00 14.09 ?  57  THR   A HA   1 
ATOM   1377 H HB   . THR   A 1 57  ? 27.638 8.407   11.887  1.00 14.06 ?  57  THR   A HB   1 
ATOM   1378 H HG1  . THR   A 1 57  ? 26.552 9.029   9.545   1.00 13.69 ?  57  THR   A HG1  1 
ATOM   1379 H HG21 . THR   A 1 57  ? 26.999 6.441   10.869  1.00 13.87 ?  57  THR   A HG21 1 
ATOM   1380 H HG22 . THR   A 1 57  ? 26.014 6.711   12.073  1.00 13.87 ?  57  THR   A HG22 1 
ATOM   1381 H HG23 . THR   A 1 57  ? 25.555 7.013   10.594  1.00 13.87 ?  57  THR   A HG23 1 
ATOM   1382 N N    . ASN   A 1 58  ? 25.562 11.796  11.530  1.00 12.75 ?  58  ASN   A N    1 
ATOM   1383 C CA   . ASN   A 1 58  ? 26.024 13.180  11.434  1.00 13.57 ?  58  ASN   A CA   1 
ATOM   1384 C C    . ASN   A 1 58  ? 27.175 13.311  10.429  1.00 12.48 ?  58  ASN   A C    1 
ATOM   1385 O O    . ASN   A 1 58  ? 28.077 14.140  10.594  1.00 13.02 ?  58  ASN   A O    1 
ATOM   1386 C CB   . ASN   A 1 58  ? 26.402 13.715  12.831  1.00 16.27 ?  58  ASN   A CB   1 
ATOM   1387 C CG   . ASN   A 1 58  ? 26.823 15.173  12.829  1.00 19.52 ?  58  ASN   A CG   1 
ATOM   1388 O OD1  . ASN   A 1 58  ? 26.190 16.005  12.191  1.00 21.25 ?  58  ASN   A OD1  1 
ATOM   1389 N ND2  . ASN   A 1 58  ? 27.887 15.491  13.571  1.00 20.80 ?  58  ASN   A ND2  1 
ATOM   1390 H H    . ASN   A 1 58  ? 24.739 11.669  11.304  1.00 15.29 ?  58  ASN   A H    1 
ATOM   1391 H HA   . ASN   A 1 58  ? 25.286 13.712  11.108  1.00 16.28 ?  58  ASN   A HA   1 
ATOM   1392 H HB2  . ASN   A 1 58  ? 25.629 13.623  13.420  1.00 19.52 ?  58  ASN   A HB2  1 
ATOM   1393 H HB3  . ASN   A 1 58  ? 27.138 13.198  13.184  1.00 19.52 ?  58  ASN   A HB3  1 
ATOM   1394 H HD21 . ASN   A 1 58  ? 28.158 16.306  13.606  1.00 24.96 ?  58  ASN   A HD21 1 
ATOM   1395 H HD22 . ASN   A 1 58  ? 28.299 14.878  14.007  1.00 24.96 ?  58  ASN   A HD22 1 
ATOM   1396 N N    . ASN   A 1 59  ? 27.154 12.496  9.371   1.00 11.32 ?  59  ASN   A N    1 
ATOM   1397 C CA   . ASN   A 1 59  ? 28.132 12.475  8.275   1.00 11.27 ?  59  ASN   A CA   1 
ATOM   1398 C C    . ASN   A 1 59  ? 29.446 11.795  8.663   1.00 11.03 ?  59  ASN   A C    1 
ATOM   1399 O O    . ASN   A 1 59  ? 30.364 11.753  7.837   1.00 11.10 ?  59  ASN   A O    1 
ATOM   1400 C CB   . ASN   A 1 59  ? 28.420 13.860  7.670   1.00 11.51 ?  59  ASN   A CB   1 
ATOM   1401 C CG   . ASN   A 1 59  ? 28.770 13.796  6.200   1.00 11.88 ?  59  ASN   A CG   1 
ATOM   1402 O OD1  . ASN   A 1 59  ? 28.061 13.174  5.406   1.00 11.89 ?  59  ASN   A OD1  1 
ATOM   1403 N ND2  . ASN   A 1 59  ? 29.861 14.457  5.821   1.00 12.53 ?  59  ASN   A ND2  1 
ATOM   1404 H H    . ASN   A 1 59  ? 26.535 11.906  9.254   1.00 13.59 ?  59  ASN   A H    1 
ATOM   1405 H HA   . ASN   A 1 59  ? 27.751 11.945  7.562   1.00 13.53 ?  59  ASN   A HA   1 
ATOM   1406 H HB2  . ASN   A 1 59  ? 27.634 14.420  7.760   1.00 13.81 ?  59  ASN   A HB2  1 
ATOM   1407 H HB3  . ASN   A 1 59  ? 29.170 14.265  8.134   1.00 13.81 ?  59  ASN   A HB3  1 
ATOM   1408 H HD21 . ASN   A 1 59  ? 30.102 14.454  4.994   1.00 15.04 ?  59  ASN   A HD21 1 
ATOM   1409 H HD22 . ASN   A 1 59  ? 30.334 14.884  6.401   1.00 15.04 ?  59  ASN   A HD22 1 
ATOM   1410 N N    . ALA   A 1 60  ? 29.571 11.250  9.873   1.00 10.93 ?  60  ALA   A N    1 
ATOM   1411 C CA   . ALA   A 1 60  ? 30.810 10.565  10.232  1.00 11.41 ?  60  ALA   A CA   1 
ATOM   1412 C C    . ALA   A 1 60  ? 31.040 9.327   9.371   1.00 11.22 ?  60  ALA   A C    1 
ATOM   1413 O O    . ALA   A 1 60  ? 32.186 9.010   9.035   1.00 11.63 ?  60  ALA   A O    1 
ATOM   1414 C CB   . ALA   A 1 60  ? 30.803 10.198  11.713  1.00 12.12 ?  60  ALA   A CB   1 
ATOM   1415 H H    . ALA   A 1 60  ? 28.975 11.259  10.488  1.00 13.12 ?  60  ALA   A H    1 
ATOM   1416 H HA   . ALA   A 1 60  ? 31.557 11.168  10.081  1.00 13.69 ?  60  ALA   A HA   1 
ATOM   1417 H HB1  . ALA   A 1 60  ? 31.632 9.748   11.933  1.00 14.54 ?  60  ALA   A HB1  1 
ATOM   1418 H HB2  . ALA   A 1 60  ? 30.721 11.014  12.237  1.00 14.54 ?  60  ALA   A HB2  1 
ATOM   1419 H HB3  . ALA   A 1 60  ? 30.050 9.616   11.890  1.00 14.54 ?  60  ALA   A HB3  1 
ATOM   1420 N N    . MET   A 1 61  ? 29.969 8.628   8.990   1.00 10.57 ?  61  MET   A N    1 
ATOM   1421 C CA   . MET   A 1 61  ? 30.112 7.495   8.079   1.00 10.54 ?  61  MET   A CA   1 
ATOM   1422 C C    . MET   A 1 61  ? 30.745 7.924   6.755   1.00 10.41 ?  61  MET   A C    1 
ATOM   1423 O O    . MET   A 1 61  ? 31.638 7.246   6.234   1.00 10.56 ?  61  MET   A O    1 
ATOM   1424 C CB   . MET   A 1 61  ? 28.745 6.833   7.865   1.00 10.31 ?  61  MET   A CB   1 
ATOM   1425 C CG   . MET   A 1 61  ? 28.746 5.677   6.878   1.00 11.20 ?  61  MET   A CG   1 
ATOM   1426 S SD   . MET   A 1 61  ? 27.130 4.933   6.654   1.00 12.36 ?  61  MET   A SD   1 
ATOM   1427 C CE   . MET   A 1 61  ? 26.968 4.041   8.204   1.00 13.49 ?  61  MET   A CE   1 
ATOM   1428 H H    . MET   A 1 61  ? 29.162 8.787   9.239   1.00 12.68 ?  61  MET   A H    1 
ATOM   1429 H HA   . MET   A 1 61  ? 30.689 6.836   8.495   1.00 12.65 ?  61  MET   A HA   1 
ATOM   1430 H HB2  . MET   A 1 61  ? 28.431 6.488   8.715   1.00 12.37 ?  61  MET   A HB2  1 
ATOM   1431 H HB3  . MET   A 1 61  ? 28.125 7.497   7.533   1.00 12.37 ?  61  MET   A HB3  1 
ATOM   1432 H HG2  . MET   A 1 61  ? 29.037 5.991   6.010   1.00 13.44 ?  61  MET   A HG2  1 
ATOM   1433 H HG3  . MET   A 1 61  ? 29.342 4.981   7.198   1.00 13.44 ?  61  MET   A HG3  1 
ATOM   1434 H HE1  . MET   A 1 61  ? 26.125 3.560   8.208   1.00 16.19 ?  61  MET   A HE1  1 
ATOM   1435 H HE2  . MET   A 1 61  ? 27.705 3.415   8.284   1.00 16.19 ?  61  MET   A HE2  1 
ATOM   1436 H HE3  . MET   A 1 61  ? 26.991 4.673   8.939   1.00 16.19 ?  61  MET   A HE3  1 
ATOM   1437 N N    . GLN   A 1 62  ? 30.300 9.055   6.198   1.00 10.52 ?  62  GLN   A N    1 
ATOM   1438 C CA   . GLN   A 1 62  ? 30.859 9.535   4.937   1.00 10.80 ?  62  GLN   A CA   1 
ATOM   1439 C C    . GLN   A 1 62  ? 32.328 9.910   5.084   1.00 10.78 ?  62  GLN   A C    1 
ATOM   1440 O O    . GLN   A 1 62  ? 33.139 9.600   4.206   1.00 10.74 ?  62  GLN   A O    1 
ATOM   1441 C CB   . GLN   A 1 62  ? 30.050 10.719  4.410   1.00 10.79 ?  62  GLN   A CB   1 
ATOM   1442 C CG   . GLN   A 1 62  ? 30.420 11.089  2.985   1.00 10.90 ?  62  GLN   A CG   1 
ATOM   1443 C CD   . GLN   A 1 62  ? 30.102 9.962   2.033   1.00 10.96 ?  62  GLN   A CD   1 
ATOM   1444 O OE1  . GLN   A 1 62  ? 28.925 9.654   1.820   1.00 11.38 ?  62  GLN   A OE1  1 
ATOM   1445 N NE2  . GLN   A 1 62  ? 31.125 9.297   1.508   1.00 11.39 ?  62  GLN   A NE2  1 
ATOM   1446 H H    . GLN   A 1 62  ? 29.681 9.552   6.531   1.00 12.63 ?  62  GLN   A H    1 
ATOM   1447 H HA   . GLN   A 1 62  ? 30.804 8.816   4.289   1.00 12.95 ?  62  GLN   A HA   1 
ATOM   1448 H HB2  . GLN   A 1 62  ? 29.108 10.493  4.430   1.00 12.94 ?  62  GLN   A HB2  1 
ATOM   1449 H HB3  . GLN   A 1 62  ? 30.219 11.491  4.973   1.00 12.94 ?  62  GLN   A HB3  1 
ATOM   1450 H HG2  . GLN   A 1 62  ? 29.902 11.864  2.715   1.00 13.08 ?  62  GLN   A HG2  1 
ATOM   1451 H HG3  . GLN   A 1 62  ? 31.366 11.277  2.934   1.00 13.08 ?  62  GLN   A HG3  1 
ATOM   1452 H HE21 . GLN   A 1 62  ? 31.930 9.528   1.695   1.00 13.67 ?  62  GLN   A HE21 1 
ATOM   1453 H HE22 . GLN   A 1 62  ? 30.978 8.642   0.970   1.00 13.67 ?  62  GLN   A HE22 1 
ATOM   1454 N N    . VAL   A 1 63  ? 32.688 10.596  6.174   1.00 11.29 ?  63  VAL   A N    1 
ATOM   1455 C CA   . VAL   A 1 63  ? 34.081 10.984  6.392   1.00 12.04 ?  63  VAL   A CA   1 
ATOM   1456 C C    . VAL   A 1 63  ? 34.975 9.746   6.448   1.00 11.17 ?  63  VAL   A C    1 
ATOM   1457 O O    . VAL   A 1 63  ? 36.025 9.681   5.796   1.00 11.76 ?  63  VAL   A O    1 
ATOM   1458 C CB   . VAL   A 1 63  ? 34.193 11.852  7.659   1.00 13.46 ?  63  VAL   A CB   1 
ATOM   1459 C CG1  . VAL   A 1 63  ? 35.641 12.103  8.020   1.00 15.20 ?  63  VAL   A CG1  1 
ATOM   1460 C CG2  . VAL   A 1 63  ? 33.467 13.181  7.452   1.00 14.16 ?  63  VAL   A CG2  1 
ATOM   1461 H H    . VAL   A 1 63  ? 32.144 10.842  6.799   1.00 13.55 ?  63  VAL   A H    1 
ATOM   1462 H HA   . VAL   A 1 63  ? 34.367 11.523  5.643   1.00 14.45 ?  63  VAL   A HA   1 
ATOM   1463 H HB   . VAL   A 1 63  ? 33.772 11.391  8.404   1.00 16.15 ?  63  VAL   A HB   1 
ATOM   1464 H HG11 . VAL   A 1 63  ? 35.683 12.826  8.664   1.00 18.24 ?  63  VAL   A HG11 1 
ATOM   1465 H HG12 . VAL   A 1 63  ? 36.018 11.296  8.401   1.00 18.24 ?  63  VAL   A HG12 1 
ATOM   1466 H HG13 . VAL   A 1 63  ? 36.125 12.349  7.215   1.00 18.24 ?  63  VAL   A HG13 1 
ATOM   1467 H HG21 . VAL   A 1 63  ? 33.557 13.722  8.255   1.00 16.99 ?  63  VAL   A HG21 1 
ATOM   1468 H HG22 . VAL   A 1 63  ? 33.867 13.646  6.698   1.00 16.99 ?  63  VAL   A HG22 1 
ATOM   1469 H HG23 . VAL   A 1 63  ? 32.530 13.010  7.274   1.00 16.99 ?  63  VAL   A HG23 1 
ATOM   1470 N N    . GLU   A 1 64  ? 34.562 8.739   7.221   1.00 11.29 ?  64  GLU   A N    1 
ATOM   1471 C CA   . GLU   A 1 64  ? 35.325 7.500   7.308   1.00 11.31 ?  64  GLU   A CA   1 
ATOM   1472 C C    . GLU   A 1 64  ? 35.408 6.812   5.950   1.00 11.01 ?  64  GLU   A C    1 
ATOM   1473 O O    . GLU   A 1 64  ? 36.459 6.270   5.571   1.00 11.46 ?  64  GLU   A O    1 
ATOM   1474 C CB   . GLU   A 1 64  ? 34.637 6.587   8.321   1.00 12.13 ?  64  GLU   A CB   1 
ATOM   1475 C CG   . GLU   A 1 64  ? 35.292 5.233   8.471   1.00 12.49 ?  64  GLU   A CG   1 
ATOM   1476 C CD   . GLU   A 1 64  ? 34.412 4.239   9.203   1.00 13.23 ?  64  GLU   A CD   1 
ATOM   1477 O OE1  . GLU   A 1 64  ? 33.172 4.333   9.071   1.00 14.09 ?  64  GLU   A OE1  1 
ATOM   1478 O OE2  . GLU   A 1 64  ? 34.965 3.348   9.893   1.00 13.64 -1 64  GLU   A OE2  1 
ATOM   1479 H H    . GLU   A 1 64  ? 33.844 8.746   7.693   1.00 13.55 ?  64  GLU   A H    1 
ATOM   1480 H HA   . GLU   A 1 64  ? 36.227 7.694   7.621   1.00 13.57 ?  64  GLU   A HA   1 
ATOM   1481 H HB2  . GLU   A 1 64  ? 34.653 7.023   9.192   1.00 14.55 ?  64  GLU   A HB2  1 
ATOM   1482 H HB3  . GLU   A 1 64  ? 33.720 6.454   8.041   1.00 14.55 ?  64  GLU   A HB3  1 
ATOM   1483 H HG2  . GLU   A 1 64  ? 35.486 4.863   7.594   1.00 14.98 ?  64  GLU   A HG2  1 
ATOM   1484 H HG3  . GLU   A 1 64  ? 36.112 5.332   8.975   1.00 14.98 ?  64  GLU   A HG3  1 
ATOM   1485 N N    . SER   A 1 65  ? 34.293 6.808   5.213   1.00 10.79 ?  65  SER   A N    1 
ATOM   1486 C CA   . SER   A 1 65  ? 34.242 6.153   3.910   1.00 10.73 ?  65  SER   A CA   1 
ATOM   1487 C C    . SER   A 1 65  ? 35.164 6.825   2.902   1.00 11.14 ?  65  SER   A C    1 
ATOM   1488 O O    . SER   A 1 65  ? 35.811 6.149   2.094   1.00 11.54 ?  65  SER   A O    1 
ATOM   1489 C CB   . SER   A 1 65  ? 32.810 6.161   3.381   1.00 10.80 ?  65  SER   A CB   1 
ATOM   1490 O OG   . SER   A 1 65  ? 31.948 5.349   4.173   1.00 11.13 ?  65  SER   A OG   1 
ATOM   1491 H H    . SER   A 1 65  ? 33.557 7.180   5.450   1.00 12.95 ?  65  SER   A H    1 
ATOM   1492 H HA   . SER   A 1 65  ? 34.528 5.233   4.006   1.00 12.88 ?  65  SER   A HA   1 
ATOM   1493 H HB2  . SER   A 1 65  ? 32.478 7.070   3.392   1.00 12.96 ?  65  SER   A HB2  1 
ATOM   1494 H HB3  . SER   A 1 65  ? 32.816 5.821   2.474   1.00 12.96 ?  65  SER   A HB3  1 
ATOM   1495 H HG   . SER   A 1 65  ? 31.941 5.630   4.968   1.00 13.35 ?  65  SER   A HG   1 
ATOM   1496 N N    . ASP   A 1 66  ? 35.232 8.157   2.920   1.00 11.14 ?  66  ASP   A N    1 
ATOM   1497 C CA   . ASP   A 1 66  ? 36.096 8.857   1.973   1.00 12.24 ?  66  ASP   A CA   1 
ATOM   1498 C C    . ASP   A 1 66  ? 37.561 8.506   2.209   1.00 11.94 ?  66  ASP   A C    1 
ATOM   1499 O O    . ASP   A 1 66  ? 38.329 8.336   1.256   1.00 13.05 ?  66  ASP   A O    1 
ATOM   1500 C CB   . ASP   A 1 66  ? 35.880 10.365  2.075   1.00 13.38 ?  66  ASP   A CB   1 
ATOM   1501 C CG   . ASP   A 1 66  ? 34.541 10.823  1.487   1.00 15.06 ?  66  ASP   A CG   1 
ATOM   1502 O OD1  . ASP   A 1 66  ? 33.826 10.036  0.833   1.00 15.20 ?  66  ASP   A OD1  1 
ATOM   1503 O OD2  . ASP   A 1 66  ? 34.221 12.013  1.666   1.00 18.39 -1 66  ASP   A OD2  1 
ATOM   1504 H H    . ASP   A 1 66  ? 34.789 8.673   3.452   1.00 13.36 ?  66  ASP   A H    1 
ATOM   1505 H HA   . ASP   A 1 66  ? 35.863 8.583   1.072   1.00 14.68 ?  66  ASP   A HA   1 
ATOM   1506 H HB2  . ASP   A 1 66  ? 35.895 10.625  3.008   1.00 16.05 ?  66  ASP   A HB2  1 
ATOM   1507 H HB3  . ASP   A 1 66  ? 36.591 10.818  1.593   1.00 16.05 ?  66  ASP   A HB3  1 
ATOM   1508 N N    . ASP   A 1 67  ? 37.961 8.377   3.474   1.00 12.17 ?  67  ASP   A N    1 
ATOM   1509 C CA   . ASP   A 1 67  ? 39.318 7.930   3.774   1.00 12.84 ?  67  ASP   A CA   1 
ATOM   1510 C C    . ASP   A 1 67  ? 39.543 6.496   3.304   1.00 12.92 ?  67  ASP   A C    1 
ATOM   1511 O O    . ASP   A 1 67  ? 40.601 6.177   2.751   1.00 13.51 ?  67  ASP   A O    1 
ATOM   1512 C CB   . ASP   A 1 67  ? 39.584 8.061   5.271   1.00 14.22 ?  67  ASP   A CB   1 
ATOM   1513 C CG   . ASP   A 1 67  ? 40.884 7.405   5.697   1.00 15.39 ?  67  ASP   A CG   1 
ATOM   1514 O OD1  . ASP   A 1 67  ? 41.959 8.040   5.579   1.00 18.00 ?  67  ASP   A OD1  1 
ATOM   1515 O OD2  . ASP   A 1 67  ? 40.828 6.241   6.155   1.00 15.21 -1 67  ASP   A OD2  1 
ATOM   1516 H H    . ASP   A 1 67  ? 37.475 8.541   4.162   1.00 14.61 ?  67  ASP   A H    1 
ATOM   1517 H HA   . ASP   A 1 67  ? 39.946 8.497   3.301   1.00 15.41 ?  67  ASP   A HA   1 
ATOM   1518 H HB2  . ASP   A 1 67  ? 39.635 8.994   5.496   1.00 17.06 ?  67  ASP   A HB2  1 
ATOM   1519 H HB3  . ASP   A 1 67  ? 38.860 7.631   5.754   1.00 17.06 ?  67  ASP   A HB3  1 
ATOM   1520 N N    . TYR   A 1 68  ? 38.552 5.616   3.500   1.00 12.19 ?  68  TYR   A N    1 
ATOM   1521 C CA   . TYR   A 1 68  ? 38.671 4.236   3.025   1.00 12.42 ?  68  TYR   A CA   1 
ATOM   1522 C C    . TYR   A 1 68  ? 38.906 4.188   1.516   1.00 12.49 ?  68  TYR   A C    1 
ATOM   1523 O O    . TYR   A 1 68  ? 39.787 3.461   1.037   1.00 12.80 ?  68  TYR   A O    1 
ATOM   1524 C CB   . TYR   A 1 68  ? 37.423 3.413   3.408   1.00 13.09 ?  68  TYR   A CB   1 
ATOM   1525 C CG   . TYR   A 1 68  ? 37.448 2.023   2.776   1.00 14.32 ?  68  TYR   A CG   1 
ATOM   1526 C CD1  . TYR   A 1 68  ? 36.996 1.832   1.472   1.00 15.66 ?  68  TYR   A CD1  1 
ATOM   1527 C CD2  . TYR   A 1 68  ? 37.983 0.930   3.444   1.00 15.94 ?  68  TYR   A CD2  1 
ATOM   1528 C CE1  . TYR   A 1 68  ? 37.059 0.613   0.854   1.00 17.04 ?  68  TYR   A CE1  1 
ATOM   1529 C CE2  . TYR   A 1 68  ? 38.038 -0.334  2.824   1.00 16.47 ?  68  TYR   A CE2  1 
ATOM   1530 C CZ   . TYR   A 1 68  ? 37.583 -0.462  1.529   1.00 17.19 ?  68  TYR   A CZ   1 
ATOM   1531 O OH   . TYR   A 1 68  ? 37.662 -1.670  0.891   1.00 18.34 ?  68  TYR   A OH   1 
ATOM   1532 H H    . TYR   A 1 68  ? 37.807 5.788   3.902   1.00 14.62 ?  68  TYR   A H    1 
ATOM   1533 H HA   . TYR   A 1 68  ? 39.432 3.825   3.455   1.00 14.90 ?  68  TYR   A HA   1 
ATOM   1534 H HB2  . TYR   A 1 68  ? 37.392 3.302   4.371   1.00 15.70 ?  68  TYR   A HB2  1 
ATOM   1535 H HB3  . TYR   A 1 68  ? 36.624 3.869   3.097   1.00 15.70 ?  68  TYR   A HB3  1 
ATOM   1536 H HD1  . TYR   A 1 68  ? 36.651 2.561   1.004   1.00 18.79 ?  68  TYR   A HD1  1 
ATOM   1537 H HD2  . TYR   A 1 68  ? 38.307 1.030   4.307   1.00 19.12 ?  68  TYR   A HD2  1 
ATOM   1538 H HE1  . TYR   A 1 68  ? 36.744 0.516   -0.017  1.00 20.44 ?  68  TYR   A HE1  1 
ATOM   1539 H HE2  . TYR   A 1 68  ? 38.402 -1.065  3.265   1.00 19.76 ?  68  TYR   A HE2  1 
ATOM   1540 H HH   . TYR   A 1 68  ? 37.984 -2.247  1.410   1.00 22.01 ?  68  TYR   A HH   1 
ATOM   1541 N N    . ILE   A 1 69  ? 38.120 4.951   0.747   1.00 11.61 ?  69  ILE   A N    1 
ATOM   1542 C CA   . ILE   A 1 69  ? 38.251 4.939   -0.709  1.00 11.98 ?  69  ILE   A CA   1 
ATOM   1543 C C    . ILE   A 1 69  ? 39.581 5.551   -1.142  1.00 11.75 ?  69  ILE   A C    1 
ATOM   1544 O O    . ILE   A 1 69  ? 40.223 5.070   -2.083  1.00 12.13 ?  69  ILE   A O    1 
ATOM   1545 C CB   . ILE   A 1 69  ? 37.051 5.648   -1.370  1.00 12.91 ?  69  ILE   A CB   1 
ATOM   1546 C CG1  . ILE   A 1 69  ? 35.736 4.910   -1.096  1.00 13.56 ?  69  ILE   A CG1  1 
ATOM   1547 C CG2  . ILE   A 1 69  ? 37.285 5.838   -2.876  1.00 14.52 ?  69  ILE   A CG2  1 
ATOM   1548 C CD1  . ILE   A 1 69  ? 35.581 3.615   -1.863  1.00 14.23 ?  69  ILE   A CD1  1 
ATOM   1549 H H    . ILE   A 1 69  ? 37.515 5.481   1.046   1.00 13.93 ?  69  ILE   A H    1 
ATOM   1550 H HA   . ILE   A 1 69  ? 38.249 4.017   -1.007  1.00 14.37 ?  69  ILE   A HA   1 
ATOM   1551 H HB   . ILE   A 1 69  ? 36.979 6.528   -0.976  1.00 15.49 ?  69  ILE   A HB   1 
ATOM   1552 H HG12 . ILE   A 1 69  ? 35.691 4.701   -0.148  1.00 16.26 ?  69  ILE   A HG12 1 
ATOM   1553 H HG13 . ILE   A 1 69  ? 34.999 5.491   -1.338  1.00 16.26 ?  69  ILE   A HG13 1 
ATOM   1554 H HG21 . ILE   A 1 69  ? 36.438 6.052   -3.303  1.00 17.42 ?  69  ILE   A HG21 1 
ATOM   1555 H HG22 . ILE   A 1 69  ? 37.909 6.574   -3.012  1.00 17.42 ?  69  ILE   A HG22 1 
ATOM   1556 H HG23 . ILE   A 1 69  ? 37.647 5.024   -3.252  1.00 17.42 ?  69  ILE   A HG23 1 
ATOM   1557 H HD11 . ILE   A 1 69  ? 34.782 3.162   -1.551  1.00 17.07 ?  69  ILE   A HD11 1 
ATOM   1558 H HD12 . ILE   A 1 69  ? 35.498 3.815   -2.809  1.00 17.07 ?  69  ILE   A HD12 1 
ATOM   1559 H HD13 . ILE   A 1 69  ? 36.358 3.058   -1.708  1.00 17.07 ?  69  ILE   A HD13 1 
ATOM   1560 N N    . ALA   A 1 70  ? 39.999 6.634   -0.489  1.00 12.56 ?  70  ALA   A N    1 
ATOM   1561 C CA   . ALA   A 1 70  ? 41.276 7.244   -0.844  1.00 13.31 ?  70  ALA   A CA   1 
ATOM   1562 C C    . ALA   A 1 70  ? 42.426 6.261   -0.678  1.00 13.30 ?  70  ALA   A C    1 
ATOM   1563 O O    . ALA   A 1 70  ? 43.395 6.303   -1.441  1.00 15.41 ?  70  ALA   A O    1 
ATOM   1564 C CB   . ALA   A 1 70  ? 41.515 8.494   0.001   1.00 14.00 ?  70  ALA   A CB   1 
ATOM   1565 H H    . ALA   A 1 70  ? 39.572 7.028   0.140   1.00 15.07 ?  70  ALA   A H    1 
ATOM   1566 H HA   . ALA   A 1 70  ? 41.249 7.522   -1.774  1.00 15.97 ?  70  ALA   A HA   1 
ATOM   1567 H HB1  . ALA   A 1 70  ? 42.374 8.884   -0.248  1.00 16.79 ?  70  ALA   A HB1  1 
ATOM   1568 H HB2  . ALA   A 1 70  ? 40.806 9.131   -0.160  1.00 16.79 ?  70  ALA   A HB2  1 
ATOM   1569 H HB3  . ALA   A 1 70  ? 41.534 8.243   0.938   1.00 16.79 ?  70  ALA   A HB3  1 
ATOM   1570 N N    . THR   A 1 71  ? 42.331 5.361   0.299   1.00 12.91 ?  71  THR   A N    1 
ATOM   1571 C CA   . THR   A 1 71  ? 43.388 4.385   0.544   1.00 14.65 ?  71  THR   A CA   1 
ATOM   1572 C C    . THR   A 1 71  ? 43.269 3.163   -0.358  1.00 14.49 ?  71  THR   A C    1 
ATOM   1573 O O    . THR   A 1 71  ? 44.279 2.657   -0.864  1.00 16.56 ?  71  THR   A O    1 
ATOM   1574 C CB   . THR   A 1 71  ? 43.320 3.933   2.000   1.00 16.59 ?  71  THR   A CB   1 
ATOM   1575 O OG1  . THR   A 1 71  ? 43.571 5.058   2.848   1.00 18.05 ?  71  THR   A OG1  1 
ATOM   1576 C CG2  . THR   A 1 71  ? 44.327 2.818   2.286   1.00 17.87 ?  71  THR   A CG2  1 
ATOM   1577 H H    . THR   A 1 71  ? 41.659 5.284   0.825   1.00 15.49 ?  71  THR   A H    1 
ATOM   1578 H HA   . THR   A 1 71  ? 44.254 4.791   0.389   1.00 17.58 ?  71  THR   A HA   1 
ATOM   1579 H HB   . THR   A 1 71  ? 42.432 3.575   2.178   1.00 19.91 ?  71  THR   A HB   1 
ATOM   1580 H HG1  . THR   A 1 71  ? 42.979 5.638   2.723   1.00 21.66 ?  71  THR   A HG1  1 
ATOM   1581 H HG21 . THR   A 1 71  ? 44.467 2.735   3.243   1.00 21.44 ?  71  THR   A HG21 1 
ATOM   1582 H HG22 . THR   A 1 71  ? 44.006 1.969   1.943   1.00 21.44 ?  71  THR   A HG22 1 
ATOM   1583 H HG23 . THR   A 1 71  ? 45.180 3.025   1.866   1.00 21.44 ?  71  THR   A HG23 1 
ATOM   1584 N N    . ASN   A 1 72  ? 42.049 2.656   -0.542  1.00 13.58 ?  72  ASN   A N    1 
ATOM   1585 C CA   . ASN   A 1 72  ? 41.830 1.329   -1.101  1.00 14.03 ?  72  ASN   A CA   1 
ATOM   1586 C C    . ASN   A 1 72  ? 41.208 1.319   -2.484  1.00 14.22 ?  72  ASN   A C    1 
ATOM   1587 O O    . ASN   A 1 72  ? 41.212 0.263   -3.131  1.00 15.41 ?  72  ASN   A O    1 
ATOM   1588 C CB   . ASN   A 1 72  ? 40.939 0.508   -0.158  1.00 14.69 ?  72  ASN   A CB   1 
ATOM   1589 C CG   . ASN   A 1 72  ? 41.554 0.351   1.207   1.00 15.60 ?  72  ASN   A CG   1 
ATOM   1590 O OD1  . ASN   A 1 72  ? 41.106 0.953   2.181   1.00 17.35 ?  72  ASN   A OD1  1 
ATOM   1591 N ND2  . ASN   A 1 72  ? 42.597 -0.445  1.285   1.00 16.28 ?  72  ASN   A ND2  1 
ATOM   1592 H H    . ASN   A 1 72  ? 41.318 3.075   -0.350  1.00 16.29 ?  72  ASN   A H    1 
ATOM   1593 H HA   . ASN   A 1 72  ? 42.682 0.880   -1.168  1.00 16.83 ?  72  ASN   A HA   1 
ATOM   1594 H HB2  . ASN   A 1 72  ? 40.085 0.956   -0.059  1.00 17.63 ?  72  ASN   A HB2  1 
ATOM   1595 H HB3  . ASN   A 1 72  ? 40.812 -0.375  -0.536  1.00 17.63 ?  72  ASN   A HB3  1 
ATOM   1596 H HD21 . ASN   A 1 72  ? 42.990 -0.560  2.043   1.00 19.53 ?  72  ASN   A HD21 1 
ATOM   1597 H HD22 . ASN   A 1 72  ? 42.889 -0.843  0.584   1.00 19.53 ?  72  ASN   A HD22 1 
ATOM   1598 N N    . GLY   A 1 73  ? 40.657 2.435   -2.947  1.00 13.66 ?  73  GLY   A N    1 
ATOM   1599 C CA   . GLY   A 1 73  ? 39.919 2.447   -4.184  1.00 13.36 ?  73  GLY   A CA   1 
ATOM   1600 C C    . GLY   A 1 73  ? 38.528 1.865   -4.014  1.00 12.76 ?  73  GLY   A C    1 
ATOM   1601 O O    . GLY   A 1 73  ? 38.144 1.407   -2.934  1.00 13.24 ?  73  GLY   A O    1 
ATOM   1602 H H    . GLY   A 1 73  ? 40.703 3.211   -2.563  1.00 16.39 ?  73  GLY   A H    1 
ATOM   1603 H HA2  . GLY   A 1 73  ? 39.839 3.364   -4.507  1.00 16.03 ?  73  GLY   A HA2  1 
ATOM   1604 H HA3  . GLY   A 1 73  ? 40.395 1.931   -4.854  1.00 16.03 ?  73  GLY   A HA3  1 
ATOM   1605 N N    . PRO   A 1 74  ? 37.748 1.885   -5.094  1.00 12.97 ?  74  PRO   A N    1 
ATOM   1606 C CA   . PRO   A 1 74  ? 36.352 1.451   -5.009  1.00 13.20 ?  74  PRO   A CA   1 
ATOM   1607 C C    . PRO   A 1 74  ? 36.208 -0.033  -4.699  1.00 12.70 ?  74  PRO   A C    1 
ATOM   1608 O O    . PRO   A 1 74  ? 37.076 -0.863  -4.991  1.00 13.72 ?  74  PRO   A O    1 
ATOM   1609 C CB   . PRO   A 1 74  ? 35.799 1.762   -6.406  1.00 15.08 ?  74  PRO   A CB   1 
ATOM   1610 C CG   . PRO   A 1 74  ? 36.748 2.754   -7.002  1.00 17.52 ?  74  PRO   A CG   1 
ATOM   1611 C CD   . PRO   A 1 74  ? 38.087 2.401   -6.431  1.00 15.05 ?  74  PRO   A CD   1 
ATOM   1612 H HA   . PRO   A 1 74  ? 35.871 1.974   -4.345  1.00 15.84 ?  74  PRO   A HA   1 
ATOM   1613 H HB2  . PRO   A 1 74  ? 35.770 0.949   -6.932  1.00 18.09 ?  74  PRO   A HB2  1 
ATOM   1614 H HB3  . PRO   A 1 74  ? 34.908 2.146   -6.325  1.00 18.09 ?  74  PRO   A HB3  1 
ATOM   1615 H HG2  . PRO   A 1 74  ? 36.754 2.664   -7.968  1.00 21.02 ?  74  PRO   A HG2  1 
ATOM   1616 H HG3  . PRO   A 1 74  ? 36.493 3.652   -6.742  1.00 21.02 ?  74  PRO   A HG3  1 
ATOM   1617 H HD2  . PRO   A 1 74  ? 38.515 1.710   -6.966  1.00 18.05 ?  74  PRO   A HD2  1 
ATOM   1618 H HD3  . PRO   A 1 74  ? 38.644 3.195   -6.371  1.00 18.05 ?  74  PRO   A HD3  1 
ATOM   1619 N N    . LEU   A 1 75  ? 35.065 -0.362  -4.112  1.00 11.86 ?  75  LEU   A N    1 
ATOM   1620 C CA   . LEU   A 1 75  ? 34.662 -1.748  -3.970  1.00 11.31 ?  75  LEU   A CA   1 
ATOM   1621 C C    . LEU   A 1 75  ? 34.272 -2.323  -5.329  1.00 12.20 ?  75  LEU   A C    1 
ATOM   1622 O O    . LEU   A 1 75  ? 34.160 -1.611  -6.332  1.00 13.63 ?  75  LEU   A O    1 
ATOM   1623 C CB   . LEU   A 1 75  ? 33.478 -1.869  -3.013  1.00 11.96 ?  75  LEU   A CB   1 
ATOM   1624 C CG   . LEU   A 1 75  ? 33.695 -1.466  -1.558  1.00 13.64 ?  75  LEU   A CG   1 
ATOM   1625 C CD1  . LEU   A 1 75  ? 32.412 -1.670  -0.752  1.00 15.47 ?  75  LEU   A CD1  1 
ATOM   1626 C CD2  . LEU   A 1 75  ? 34.847 -2.194  -0.920  1.00 17.12 ?  75  LEU   A CD2  1 
ATOM   1627 H H    . LEU   A 1 75  ? 34.504 0.208   -3.787  1.00 14.24 ?  75  LEU   A H    1 
ATOM   1628 H HA   . LEU   A 1 75  ? 35.400 -2.260  -3.621  1.00 13.57 ?  75  LEU   A HA   1 
ATOM   1629 H HB2  . LEU   A 1 75  ? 32.756 -1.323  -3.355  1.00 14.35 ?  75  LEU   A HB2  1 
ATOM   1630 H HB3  . LEU   A 1 75  ? 33.197 -2.800  -3.010  1.00 14.35 ?  75  LEU   A HB3  1 
ATOM   1631 H HG   . LEU   A 1 75  ? 33.911 -0.519  -1.537  1.00 16.37 ?  75  LEU   A HG   1 
ATOM   1632 H HD11 . LEU   A 1 75  ? 32.575 -1.403  0.166   1.00 18.56 ?  75  LEU   A HD11 1 
ATOM   1633 H HD12 . LEU   A 1 75  ? 31.713 -1.119  -1.139  1.00 18.56 ?  75  LEU   A HD12 1 
ATOM   1634 H HD13 . LEU   A 1 75  ? 32.163 -2.603  -0.791  1.00 18.56 ?  75  LEU   A HD13 1 
ATOM   1635 H HD21 . LEU   A 1 75  ? 34.901 -1.944  0.015   1.00 20.54 ?  75  LEU   A HD21 1 
ATOM   1636 H HD22 . LEU   A 1 75  ? 34.701 -3.149  -1.002  1.00 20.54 ?  75  LEU   A HD22 1 
ATOM   1637 H HD23 . LEU   A 1 75  ? 35.673 -1.948  -1.373  1.00 20.54 ?  75  LEU   A HD23 1 
ATOM   1638 N N    . LYS   A 1 76  ? 34.091 -3.643  -5.349  1.00 12.48 ?  76  LYS   A N    1 
ATOM   1639 C CA   . LYS   A 1 76  ? 33.485 -4.360  -6.465  1.00 12.92 ?  76  LYS   A CA   1 
ATOM   1640 C C    . LYS   A 1 76  ? 31.974 -4.444  -6.265  1.00 11.83 ?  76  LYS   A C    1 
ATOM   1641 O O    . LYS   A 1 76  ? 31.498 -4.570  -5.141  1.00 11.57 ?  76  LYS   A O    1 
ATOM   1642 C CB   . LYS   A 1 76  ? 34.030 -5.798  -6.527  1.00 14.67 ?  76  LYS   A CB   1 
ATOM   1643 C CG   . LYS   A 1 76  ? 35.540 -5.910  -6.727  1.00 16.14 ?  76  LYS   A CG   1 
ATOM   1644 C CD   . LYS   A 1 76  ? 36.057 -7.316  -6.517  1.00 17.48 ?  76  LYS   A CD   1 
ATOM   1645 C CE   . LYS   A 1 76  ? 37.555 -7.387  -6.739  1.00 19.58 ?  76  LYS   A CE   1 
ATOM   1646 N NZ   . LYS   A 1 76  ? 38.077 -8.751  -6.536  1.00 20.66 ?  76  LYS   A NZ   1 
ATOM   1647 H H    . LYS   A 1 76  ? 34.322 -4.159  -4.701  1.00 14.98 ?  76  LYS   A H    1 
ATOM   1648 H HA   . LYS   A 1 76  ? 33.680 -3.908  -7.304  1.00 15.50 ?  76  LYS   A HA   1 
ATOM   1649 H HB2  . LYS   A 1 76  ? 33.811 -6.243  -5.695  1.00 17.60 ?  76  LYS   A HB2  1 
ATOM   1650 H HB3  . LYS   A 1 76  ? 33.602 -6.256  -7.266  1.00 17.60 ?  76  LYS   A HB3  1 
ATOM   1651 H HG2  . LYS   A 1 76  ? 35.760 -5.639  -7.633  1.00 19.37 ?  76  LYS   A HG2  1 
ATOM   1652 H HG3  . LYS   A 1 76  ? 35.988 -5.326  -6.092  1.00 19.37 ?  76  LYS   A HG3  1 
ATOM   1653 H HD2  . LYS   A 1 76  ? 35.869 -7.595  -5.607  1.00 20.97 ?  76  LYS   A HD2  1 
ATOM   1654 H HD3  . LYS   A 1 76  ? 35.627 -7.914  -7.149  1.00 20.97 ?  76  LYS   A HD3  1 
ATOM   1655 H HE2  . LYS   A 1 76  ? 37.754 -7.115  -7.648  1.00 23.50 ?  76  LYS   A HE2  1 
ATOM   1656 H HE3  . LYS   A 1 76  ? 37.996 -6.796  -6.108  1.00 23.50 ?  76  LYS   A HE3  1 
ATOM   1657 H HZ1  . LYS   A 1 76  ? 38.955 -8.769  -6.672  1.00 24.79 ?  76  LYS   A HZ1  1 
ATOM   1658 H HZ2  . LYS   A 1 76  ? 37.906 -9.026  -5.705  1.00 24.79 ?  76  LYS   A HZ2  1 
ATOM   1659 H HZ3  . LYS   A 1 76  ? 37.686 -9.317  -7.107  1.00 24.79 ?  76  LYS   A HZ3  1 
ATOM   1660 N N    . VAL   A 1 77  ? 31.218 -4.406  -7.367  1.00 12.05 ?  77  VAL   A N    1 
ATOM   1661 C CA   . VAL   A 1 77  ? 29.810 -4.789  -7.281  1.00 12.20 ?  77  VAL   A CA   1 
ATOM   1662 C C    . VAL   A 1 77  ? 29.743 -6.244  -6.844  1.00 11.81 ?  77  VAL   A C    1 
ATOM   1663 O O    . VAL   A 1 77  ? 30.405 -7.113  -7.426  1.00 12.12 ?  77  VAL   A O    1 
ATOM   1664 C CB   . VAL   A 1 77  ? 29.088 -4.565  -8.617  1.00 13.15 ?  77  VAL   A CB   1 
ATOM   1665 C CG1  . VAL   A 1 77  ? 27.627 -4.998  -8.512  1.00 14.05 ?  77  VAL   A CG1  1 
ATOM   1666 C CG2  . VAL   A 1 77  ? 29.172 -3.104  -9.030  1.00 14.90 ?  77  VAL   A CG2  1 
ATOM   1667 H H    . VAL   A 1 77  ? 31.494 -4.168  -8.148  1.00 14.46 ?  77  VAL   A H    1 
ATOM   1668 H HA   . VAL   A 1 77  ? 29.377 -4.244  -6.607  1.00 14.64 ?  77  VAL   A HA   1 
ATOM   1669 H HB   . VAL   A 1 77  ? 29.518 -5.094  -9.307  1.00 15.78 ?  77  VAL   A HB   1 
ATOM   1670 H HG11 . VAL   A 1 77  ? 27.156 -4.697  -9.303  1.00 16.86 ?  77  VAL   A HG11 1 
ATOM   1671 H HG12 . VAL   A 1 77  ? 27.590 -5.964  -8.450  1.00 16.86 ?  77  VAL   A HG12 1 
ATOM   1672 H HG13 . VAL   A 1 77  ? 27.239 -4.596  -7.720  1.00 16.86 ?  77  VAL   A HG13 1 
ATOM   1673 H HG21 . VAL   A 1 77  ? 28.665 -2.980  -9.848  1.00 17.87 ?  77  VAL   A HG21 1 
ATOM   1674 H HG22 . VAL   A 1 77  ? 28.794 -2.556  -8.322  1.00 17.87 ?  77  VAL   A HG22 1 
ATOM   1675 H HG23 . VAL   A 1 77  ? 30.099 -2.866  -9.174  1.00 17.87 ?  77  VAL   A HG23 1 
ATOM   1676 N N    . GLY   A 1 78  ? 28.959 -6.513  -5.798  1.00 11.46 ?  78  GLY   A N    1 
ATOM   1677 C CA   . GLY   A 1 78  ? 28.933 -7.804  -5.145  1.00 11.81 ?  78  GLY   A CA   1 
ATOM   1678 C C    . GLY   A 1 78  ? 29.858 -7.906  -3.953  1.00 11.18 ?  78  GLY   A C    1 
ATOM   1679 O O    . GLY   A 1 78  ? 29.802 -8.915  -3.236  1.00 11.73 ?  78  GLY   A O    1 
ATOM   1680 H H    . GLY   A 1 78  ? 28.415 -5.938  -5.450  1.00 13.75 ?  78  GLY   A H    1 
ATOM   1681 H HA2  . GLY   A 1 78  ? 28.030 -7.988  -4.845  1.00 14.17 ?  78  GLY   A HA2  1 
ATOM   1682 H HA3  . GLY   A 1 78  ? 29.185 -8.486  -5.786  1.00 14.17 ?  78  GLY   A HA3  1 
ATOM   1683 N N    . GLY   A 1 79  ? 30.708 -6.901  -3.722  1.00 11.03 ?  79  GLY   A N    1 
ATOM   1684 C CA   . GLY   A 1 79  ? 31.673 -6.927  -2.646  1.00 11.13 ?  79  GLY   A CA   1 
ATOM   1685 C C    . GLY   A 1 79  ? 31.226 -6.128  -1.431  1.00 10.83 ?  79  GLY   A C    1 
ATOM   1686 O O    . GLY   A 1 79  ? 30.109 -5.616  -1.353  1.00 11.31 ?  79  GLY   A O    1 
ATOM   1687 H H    . GLY   A 1 79  ? 30.740 -6.181  -4.192  1.00 13.24 ?  79  GLY   A H    1 
ATOM   1688 H HA2  . GLY   A 1 79  ? 31.818 -7.852  -2.372  1.00 13.35 ?  79  GLY   A HA2  1 
ATOM   1689 H HA3  . GLY   A 1 79  ? 32.514 -6.570  -2.960  1.00 13.35 ?  79  GLY   A HA3  1 
ATOM   1690 N N    . SER   A 1 80  ? 32.132 -6.040  -0.458  1.00 11.53 ?  80  SER   A N    1 
ATOM   1691 C CA   . SER   A 1 80  ? 31.813 -5.409  0.813   1.00 11.24 ?  80  SER   A CA   1 
ATOM   1692 C C    . SER   A 1 80  ? 33.087 -4.963  1.513   1.00 11.17 ?  80  SER   A C    1 
ATOM   1693 O O    . SER   A 1 80  ? 34.199 -5.390  1.184   1.00 12.23 ?  80  SER   A O    1 
ATOM   1694 C CB   . SER   A 1 80  ? 31.052 -6.368  1.738   1.00 12.23 ?  80  SER   A CB   1 
ATOM   1695 O OG   . SER   A 1 80  ? 31.887 -7.415  2.218   1.00 13.64 ?  80  SER   A OG   1 
ATOM   1696 H H    . SER   A 1 80  ? 32.942 -6.317  -0.520  1.00 13.83 ?  80  SER   A H    1 
ATOM   1697 H HA   . SER   A 1 80  ? 31.259 -4.629  0.643   1.00 13.48 ?  80  SER   A HA   1 
ATOM   1698 H HB2  . SER   A 1 80  ? 30.713 -5.868  2.497   1.00 14.68 ?  80  SER   A HB2  1 
ATOM   1699 H HB3  . SER   A 1 80  ? 30.312 -6.757  1.244   1.00 14.68 ?  80  SER   A HB3  1 
ATOM   1700 H HG   . SER   A 1 80  ? 32.186 -7.859  1.567   1.00 16.37 ?  80  SER   A HG   1 
ATOM   1701 N N    . CYS   A 1 81  ? 32.900 -4.114  2.520   1.00 10.85 ?  81  CYS   A N    1 
ATOM   1702 C CA   . CYS   A 1 81  ? 33.953 -3.824  3.483   1.00 10.94 ?  81  CYS   A CA   1 
ATOM   1703 C C    . CYS   A 1 81  ? 33.310 -3.587  4.841   1.00 11.25 ?  81  CYS   A C    1 
ATOM   1704 O O    . CYS   A 1 81  ? 32.146 -3.184  4.931   1.00 12.15 ?  81  CYS   A O    1 
ATOM   1705 C CB   . CYS   A 1 81  ? 34.823 -2.635  3.059   1.00 11.68 ?  81  CYS   A CB   1 
ATOM   1706 S SG   . CYS   A 1 81  ? 33.930 -1.057  3.081   1.00 12.21 ?  81  CYS   A SG   1 
ATOM   1707 H H    . CYS   A 1 81  ? 32.162 -3.692  2.673   1.00 13.02 ?  81  CYS   A H    1 
ATOM   1708 H HA   . CYS   A 1 81  ? 34.530 -4.599  3.557   1.00 13.12 ?  81  CYS   A HA   1 
ATOM   1709 H HB2  . CYS   A 1 81  ? 35.578 -2.567  3.666   1.00 14.02 ?  81  CYS   A HB2  1 
ATOM   1710 H HB3  . CYS   A 1 81  ? 35.146 -2.792  2.154   1.00 14.02 ?  81  CYS   A HB3  1 
ATOM   1711 H HG   . CYS   A 1 81  ? 34.675 -0.180  2.735   1.00 14.65 ?  81  CYS   A HG   1 
ATOM   1712 N N    . VAL   A 1 82  ? 34.078 -3.858  5.895   1.00 11.29 ?  82  VAL   A N    1 
ATOM   1713 C CA   . VAL   A 1 82  ? 33.652 -3.617  7.266   1.00 11.93 ?  82  VAL   A CA   1 
ATOM   1714 C C    . VAL   A 1 82  ? 34.256 -2.304  7.735   1.00 12.08 ?  82  VAL   A C    1 
ATOM   1715 O O    . VAL   A 1 82  ? 35.481 -2.132  7.711   1.00 12.73 ?  82  VAL   A O    1 
ATOM   1716 C CB   . VAL   A 1 82  ? 34.073 -4.762  8.199   1.00 13.36 ?  82  VAL   A CB   1 
ATOM   1717 C CG1  . VAL   A 1 82  ? 33.619 -4.466  9.618   1.00 14.78 ?  82  VAL   A CG1  1 
ATOM   1718 C CG2  . VAL   A 1 82  ? 33.521 -6.091  7.720   1.00 14.26 ?  82  VAL   A CG2  1 
ATOM   1719 H H    . VAL   A 1 82  ? 34.874 -4.197  5.838   1.00 13.54 ?  82  VAL   A H    1 
ATOM   1720 H HA   . VAL   A 1 82  ? 32.684 -3.540  7.291   1.00 14.31 ?  82  VAL   A HA   1 
ATOM   1721 H HB   . VAL   A 1 82  ? 35.040 -4.821  8.203   1.00 16.02 ?  82  VAL   A HB   1 
ATOM   1722 H HG11 . VAL   A 1 82  ? 33.695 -5.275  10.147  1.00 17.73 ?  82  VAL   A HG11 1 
ATOM   1723 H HG12 . VAL   A 1 82  ? 34.180 -3.771  9.996   1.00 17.73 ?  82  VAL   A HG12 1 
ATOM   1724 H HG13 . VAL   A 1 82  ? 32.694 -4.171  9.600   1.00 17.73 ?  82  VAL   A HG13 1 
ATOM   1725 H HG21 . VAL   A 1 82  ? 33.771 -6.781  8.353   1.00 17.11 ?  82  VAL   A HG21 1 
ATOM   1726 H HG22 . VAL   A 1 82  ? 32.555 -6.028  7.661   1.00 17.11 ?  82  VAL   A HG22 1 
ATOM   1727 H HG23 . VAL   A 1 82  ? 33.894 -6.290  6.847   1.00 17.11 ?  82  VAL   A HG23 1 
ATOM   1728 N N    . LEU   A 1 83  ? 33.403 -1.382  8.166   1.00 11.49 ?  83  LEU   A N    1 
ATOM   1729 C CA   . LEU   A 1 83  ? 33.824 -0.116  8.746   1.00 11.55 ?  83  LEU   A CA   1 
ATOM   1730 C C    . LEU   A 1 83  ? 33.107 0.061   10.080  1.00 11.61 ?  83  LEU   A C    1 
ATOM   1731 O O    . LEU   A 1 83  ? 32.383 -0.826  10.544  1.00 12.17 ?  83  LEU   A O    1 
ATOM   1732 C CB   . LEU   A 1 83  ? 33.568 1.045   7.771   1.00 12.11 ?  83  LEU   A CB   1 
ATOM   1733 C CG   . LEU   A 1 83  ? 34.469 1.047   6.529   1.00 12.66 ?  83  LEU   A CG   1 
ATOM   1734 C CD1  . LEU   A 1 83  ? 34.033 2.103   5.530   1.00 13.22 ?  83  LEU   A CD1  1 
ATOM   1735 C CD2  . LEU   A 1 83  ? 35.942 1.250   6.901   1.00 13.42 ?  83  LEU   A CD2  1 
ATOM   1736 H H    . LEU   A 1 83  ? 32.546 -1.468  8.125   1.00 13.79 ?  83  LEU   A H    1 
ATOM   1737 H HA   . LEU   A 1 83  ? 34.775 -0.147  8.923   1.00 13.86 ?  83  LEU   A HA   1 
ATOM   1738 H HB2  . LEU   A 1 83  ? 32.648 0.998   7.462   1.00 14.53 ?  83  LEU   A HB2  1 
ATOM   1739 H HB3  . LEU   A 1 83  ? 33.709 1.884   8.235   1.00 14.53 ?  83  LEU   A HB3  1 
ATOM   1740 H HG   . LEU   A 1 83  ? 34.396 0.184   6.093   1.00 15.19 ?  83  LEU   A HG   1 
ATOM   1741 H HD11 . LEU   A 1 83  ? 34.621 2.069   4.757   1.00 15.86 ?  83  LEU   A HD11 1 
ATOM   1742 H HD12 . LEU   A 1 83  ? 33.120 1.919   5.256   1.00 15.86 ?  83  LEU   A HD12 1 
ATOM   1743 H HD13 . LEU   A 1 83  ? 34.085 2.975   5.947   1.00 15.86 ?  83  LEU   A HD13 1 
ATOM   1744 H HD21 . LEU   A 1 83  ? 36.458 1.399   6.089   1.00 16.10 ?  83  LEU   A HD21 1 
ATOM   1745 H HD22 . LEU   A 1 83  ? 36.020 2.022   7.484   1.00 16.10 ?  83  LEU   A HD22 1 
ATOM   1746 H HD23 . LEU   A 1 83  ? 36.270 0.459   7.356   1.00 16.10 ?  83  LEU   A HD23 1 
ATOM   1747 N N    . SER   A 1 84  ? 33.326 1.210   10.712  1.00 12.01 ?  84  SER   A N    1 
ATOM   1748 C CA   . SER   A 1 84  ? 32.680 1.469   11.989  1.00 12.28 ?  84  SER   A CA   1 
ATOM   1749 C C    . SER   A 1 84  ? 31.163 1.542   11.838  1.00 12.08 ?  84  SER   A C    1 
ATOM   1750 O O    . SER   A 1 84  ? 30.638 2.000   10.824  1.00 12.10 ?  84  SER   A O    1 
ATOM   1751 C CB   . SER   A 1 84  ? 33.168 2.794   12.558  1.00 13.29 ?  84  SER   A CB   1 
ATOM   1752 O OG   . SER   A 1 84  ? 32.527 3.069   13.789  1.00 14.29 ?  84  SER   A OG   1 
ATOM   1753 H H    . SER   A 1 84  ? 33.834 1.848   10.419  1.00 14.41 ?  84  SER   A H    1 
ATOM   1754 H HA   . SER   A 1 84  ? 32.905 0.760   12.609  1.00 14.73 ?  84  SER   A HA   1 
ATOM   1755 H HB2  . SER   A 1 84  ? 34.130 2.750   12.687  1.00 15.95 ?  84  SER   A HB2  1 
ATOM   1756 H HB3  . SER   A 1 84  ? 32.952 3.506   11.933  1.00 15.95 ?  84  SER   A HB3  1 
ATOM   1757 H HG   . SER   A 1 84  ? 32.815 3.790   14.108  1.00 17.15 ?  84  SER   A HG   1 
ATOM   1758 N N    . GLY   A 1 85  ? 30.455 1.123   12.886  1.00 12.93 ?  85  GLY   A N    1 
ATOM   1759 C CA   . GLY   A 1 85  ? 29.032 1.358   12.976  1.00 13.85 ?  85  GLY   A CA   1 
ATOM   1760 C C    . GLY   A 1 85  ? 28.657 2.668   13.631  1.00 13.13 ?  85  GLY   A C    1 
ATOM   1761 O O    . GLY   A 1 85  ? 27.466 2.975   13.750  1.00 13.83 ?  85  GLY   A O    1 
ATOM   1762 H H    . GLY   A 1 85  ? 30.790 0.699   13.557  1.00 15.51 ?  85  GLY   A H    1 
ATOM   1763 H HA2  . GLY   A 1 85  ? 28.656 1.342   12.082  1.00 16.62 ?  85  GLY   A HA2  1 
ATOM   1764 H HA3  . GLY   A 1 85  ? 28.629 0.643   13.486  1.00 16.62 ?  85  GLY   A HA3  1 
ATOM   1765 N N    . HIS   A 1 86  ? 29.640 3.446   14.071  1.00 12.83 ?  86  HIS   A N    1 
ATOM   1766 C CA   . HIS   A 1 86  ? 29.408 4.780   14.636  1.00 13.13 ?  86  HIS   A CA   1 
ATOM   1767 C C    . HIS   A 1 86  ? 28.427 4.652   15.795  1.00 14.34 ?  86  HIS   A C    1 
ATOM   1768 O O    . HIS   A 1 86  ? 28.619 3.774   16.653  1.00 15.26 ?  86  HIS   A O    1 
ATOM   1769 C CB   . HIS   A 1 86  ? 29.024 5.757   13.532  1.00 13.21 ?  86  HIS   A CB   1 
ATOM   1770 C CG   . HIS   A 1 86  ? 30.081 5.868   12.496  1.00 13.46 ?  86  HIS   A CG   1 
ATOM   1771 N ND1  . HIS   A 1 86  ? 31.162 6.711   12.635  1.00 14.51 ?  86  HIS   A ND1  1 
ATOM   1772 C CD2  . HIS   A 1 86  ? 30.278 5.180   11.349  1.00 13.42 ?  86  HIS   A CD2  1 
ATOM   1773 C CE1  . HIS   A 1 86  ? 31.962 6.559   11.595  1.00 14.07 ?  86  HIS   A CE1  1 
ATOM   1774 N NE2  . HIS   A 1 86  ? 31.454 5.631   10.806  1.00 13.48 ?  86  HIS   A NE2  1 
ATOM   1775 H H    . HIS   A 1 86  ? 30.466 3.228   14.062  1.00 15.40 ?  86  HIS   A H    1 
ATOM   1776 H HA   . HIS   A 1 86  ? 30.241 5.099   15.011  1.00 15.76 ?  86  HIS   A HA   1 
ATOM   1777 H HB2  . HIS   A 1 86  ? 28.207 5.457   13.101  1.00 15.85 ?  86  HIS   A HB2  1 
ATOM   1778 H HB3  . HIS   A 1 86  ? 28.886 6.643   13.914  1.00 15.85 ?  86  HIS   A HB3  1 
ATOM   1779 H HD2  . HIS   A 1 86  ? 29.727 4.518   10.995  1.00 16.10 ?  86  HIS   A HD2  1 
ATOM   1780 H HE1  . HIS   A 1 86  ? 32.752 7.027   11.437  1.00 16.88 ?  86  HIS   A HE1  1 
ATOM   1781 H HE2  . HIS   A 1 86  ? 31.801 5.359   10.061  1.00 16.17 ?  86  HIS   A HE2  1 
ATOM   1782 N N    . ASN   A 1 87  ? 27.410 5.500   15.871  1.00 15.25 ?  87  ASN   A N    1 
ATOM   1783 C CA   . ASN   A 1 87  ? 26.422 5.481   16.931  1.00 16.32 ?  87  ASN   A CA   1 
ATOM   1784 C C    . ASN   A 1 87  ? 25.297 4.491   16.674  1.00 17.40 ?  87  ASN   A C    1 
ATOM   1785 O O    . ASN   A 1 87  ? 24.359 4.434   17.472  1.00 19.68 ?  87  ASN   A O    1 
ATOM   1786 C CB   . ASN   A 1 87  ? 25.826 6.885   17.102  1.00 17.25 ?  87  ASN   A CB   1 
ATOM   1787 C CG   . ASN   A 1 87  ? 25.327 7.477   15.790  1.00 18.13 ?  87  ASN   A CG   1 
ATOM   1788 O OD1  . ASN   A 1 87  ? 25.968 7.355   14.751  1.00 18.83 ?  87  ASN   A OD1  1 
ATOM   1789 N ND2  . ASN   A 1 87  ? 24.177 8.123   15.839  1.00 19.38 ?  87  ASN   A ND2  1 
ATOM   1790 H H    . ASN   A 1 87  ? 27.270 6.120   15.300  1.00 18.29 ?  87  ASN   A H    1 
ATOM   1791 H HA   . ASN   A 1 87  ? 26.846 5.233   17.771  1.00 19.58 ?  87  ASN   A HA   1 
ATOM   1792 H HB2  . ASN   A 1 87  ? 25.073 6.837   17.721  1.00 20.70 ?  87  ASN   A HB2  1 
ATOM   1793 H HB3  . ASN   A 1 87  ? 26.507 7.473   17.462  1.00 20.70 ?  87  ASN   A HB3  1 
ATOM   1794 H HD21 . ASN   A 1 87  ? 23.856 8.475   15.126  1.00 23.25 ?  87  ASN   A HD21 1 
ATOM   1795 H HD22 . ASN   A 1 87  ? 23.757 8.198   16.586  1.00 23.25 ?  87  ASN   A HD22 1 
ATOM   1796 N N    . LEU   A 1 88  ? 25.364 3.708   15.601  1.00 16.34 ?  88  LEU   A N    1 
ATOM   1797 C CA   . LEU   A 1 88  ? 24.258 2.841   15.206  1.00 16.28 ?  88  LEU   A CA   1 
ATOM   1798 C C    . LEU   A 1 88  ? 24.478 1.366   15.511  1.00 15.94 ?  88  LEU   A C    1 
ATOM   1799 O O    . LEU   A 1 88  ? 23.500 0.633   15.685  1.00 16.95 ?  88  LEU   A O    1 
ATOM   1800 C CB   . LEU   A 1 88  ? 24.005 2.986   13.705  1.00 17.00 ?  88  LEU   A CB   1 
ATOM   1801 C CG   . LEU   A 1 88  ? 23.728 4.409   13.216  1.00 18.75 ?  88  LEU   A CG   1 
ATOM   1802 C CD1  . LEU   A 1 88  ? 23.565 4.421   11.707  1.00 19.09 ?  88  LEU   A CD1  1 
ATOM   1803 C CD2  . LEU   A 1 88  ? 22.497 5.000   13.898  1.00 20.46 ?  88  LEU   A CD2  1 
ATOM   1804 H H    . LEU   A 1 88  ? 26.049 3.665   15.084  1.00 19.60 ?  88  LEU   A H    1 
ATOM   1805 H HA   . LEU   A 1 88  ? 23.460 3.122   15.673  1.00 19.54 ?  88  LEU   A HA   1 
ATOM   1806 H HB2  . LEU   A 1 88  ? 24.782 2.664   13.225  1.00 20.40 ?  88  LEU   A HB2  1 
ATOM   1807 H HB3  . LEU   A 1 88  ? 23.232 2.448   13.472  1.00 20.40 ?  88  LEU   A HB3  1 
ATOM   1808 H HG   . LEU   A 1 88  ? 24.487 4.971   13.433  1.00 22.50 ?  88  LEU   A HG   1 
ATOM   1809 H HD11 . LEU   A 1 88  ? 23.458 5.339   11.405  1.00 22.90 ?  88  LEU   A HD11 1 
ATOM   1810 H HD12 . LEU   A 1 88  ? 24.355 4.031   11.299  1.00 22.90 ?  88  LEU   A HD12 1 
ATOM   1811 H HD13 . LEU   A 1 88  ? 22.780 3.903   11.469  1.00 22.90 ?  88  LEU   A HD13 1 
ATOM   1812 H HD21 . LEU   A 1 88  ? 22.290 5.855   13.488  1.00 24.56 ?  88  LEU   A HD21 1 
ATOM   1813 H HD22 . LEU   A 1 88  ? 21.753 4.390   13.787  1.00 24.56 ?  88  LEU   A HD22 1 
ATOM   1814 H HD23 . LEU   A 1 88  ? 22.690 5.122   14.840  1.00 24.56 ?  88  LEU   A HD23 1 
ATOM   1815 N N    . ALA   A 1 89  ? 25.729 0.920   15.558  1.00 14.75 ?  89  ALA   A N    1 
ATOM   1816 C CA   . ALA   A 1 89  ? 26.078 -0.491  15.654  1.00 14.43 ?  89  ALA   A CA   1 
ATOM   1817 C C    . ALA   A 1 89  ? 27.562 -0.553  15.976  1.00 15.03 ?  89  ALA   A C    1 
ATOM   1818 O O    . ALA   A 1 89  ? 28.275 0.446   15.862  1.00 15.73 ?  89  ALA   A O    1 
ATOM   1819 C CB   . ALA   A 1 89  ? 25.814 -1.204  14.329  1.00 13.79 ?  89  ALA   A CB   1 
ATOM   1820 H H    . ALA   A 1 89  ? 26.417 1.435   15.528  1.00 17.69 ?  89  ALA   A H    1 
ATOM   1821 H HA   . ALA   A 1 89  ? 25.570 -0.919  16.364  1.00 17.31 ?  89  ALA   A HA   1 
ATOM   1822 H HB1  . ALA   A 1 89  ? 26.072 -2.137  14.414  1.00 16.55 ?  89  ALA   A HB1  1 
ATOM   1823 H HB2  . ALA   A 1 89  ? 24.868 -1.143  14.117  1.00 16.55 ?  89  ALA   A HB2  1 
ATOM   1824 H HB3  . ALA   A 1 89  ? 26.337 -0.780  13.632  1.00 16.55 ?  89  ALA   A HB3  1 
ATOM   1825 N N    . LYS   A 1 90  ? 28.042 -1.734  16.356  1.00 15.76 ?  90  LYS   A N    1 
ATOM   1826 C CA   . LYS   A 1 90  ? 29.486 -1.883  16.505  1.00 16.39 ?  90  LYS   A CA   1 
ATOM   1827 C C    . LYS   A 1 90  ? 30.188 -1.693  15.163  1.00 14.92 ?  90  LYS   A C    1 
ATOM   1828 O O    . LYS   A 1 90  ? 31.132 -0.895  15.039  1.00 16.30 ?  90  LYS   A O    1 
ATOM   1829 C CB   . LYS   A 1 90  ? 29.823 -3.242  17.119  1.00 19.11 ?  90  LYS   A CB   1 
ATOM   1830 C CG   . LYS   A 1 90  ? 31.303 -3.400  17.438  1.00 23.32 ?  90  LYS   A CG   1 
ATOM   1831 C CD   . LYS   A 1 90  ? 31.553 -4.610  18.324  1.00 27.22 ?  90  LYS   A CD   1 
ATOM   1832 C CE   . LYS   A 1 90  ? 32.967 -4.616  18.883  1.00 30.60 ?  90  LYS   A CE   1 
ATOM   1833 N NZ   . LYS   A 1 90  ? 33.983 -4.993  17.864  1.00 32.94 ?  90  LYS   A NZ   1 
ATOM   1834 H H    . LYS   A 1 90  ? 27.573 -2.432  16.529  1.00 18.91 ?  90  LYS   A H    1 
ATOM   1835 H HA   . LYS   A 1 90  ? 29.811 -1.199  17.107  1.00 19.67 ?  90  LYS   A HA   1 
ATOM   1836 H HB2  . LYS   A 1 90  ? 29.324 -3.346  17.949  1.00 22.94 ?  90  LYS   A HB2  1 
ATOM   1837 H HB3  . LYS   A 1 90  ? 29.572 -3.944  16.498  1.00 22.94 ?  90  LYS   A HB3  1 
ATOM   1838 H HG2  . LYS   A 1 90  ? 31.796 -3.519  16.613  1.00 27.98 ?  90  LYS   A HG2  1 
ATOM   1839 H HG3  . LYS   A 1 90  ? 31.614 -2.610  17.907  1.00 27.98 ?  90  LYS   A HG3  1 
ATOM   1840 H HD2  . LYS   A 1 90  ? 30.932 -4.595  19.070  1.00 32.66 ?  90  LYS   A HD2  1 
ATOM   1841 H HD3  . LYS   A 1 90  ? 31.429 -5.418  17.802  1.00 32.66 ?  90  LYS   A HD3  1 
ATOM   1842 H HE2  . LYS   A 1 90  ? 33.183 -3.728  19.208  1.00 36.72 ?  90  LYS   A HE2  1 
ATOM   1843 H HE3  . LYS   A 1 90  ? 33.017 -5.257  19.609  1.00 36.72 ?  90  LYS   A HE3  1 
ATOM   1844 H HZ1  . LYS   A 1 90  ? 34.795 -4.996  18.230  1.00 39.52 ?  90  LYS   A HZ1  1 
ATOM   1845 H HZ2  . LYS   A 1 90  ? 33.808 -5.806  17.546  1.00 39.52 ?  90  LYS   A HZ2  1 
ATOM   1846 H HZ3  . LYS   A 1 90  ? 33.972 -4.411  17.192  1.00 39.52 ?  90  LYS   A HZ3  1 
ATOM   1847 N N    . HIS   A 1 91  ? 29.714 -2.398  14.138  1.00 13.11 ?  91  HIS   A N    1 
ATOM   1848 C CA   . HIS   A 1 91  ? 30.290 -2.377  12.808  1.00 12.58 ?  91  HIS   A CA   1 
ATOM   1849 C C    . HIS   A 1 91  ? 29.203 -2.100  11.786  1.00 11.83 ?  91  HIS   A C    1 
ATOM   1850 O O    . HIS   A 1 91  ? 28.037 -2.462  11.982  1.00 12.52 ?  91  HIS   A O    1 
ATOM   1851 C CB   . HIS   A 1 91  ? 30.883 -3.746  12.439  1.00 15.27 ?  91  HIS   A CB   1 
ATOM   1852 C CG   . HIS   A 1 91  ? 31.879 -4.265  13.426  1.00 19.83 ?  91  HIS   A CG   1 
ATOM   1853 N ND1  . HIS   A 1 91  ? 33.146 -3.739  13.550  1.00 22.03 ?  91  HIS   A ND1  1 
ATOM   1854 C CD2  . HIS   A 1 91  ? 31.801 -5.272  14.328  1.00 21.55 ?  91  HIS   A CD2  1 
ATOM   1855 C CE1  . HIS   A 1 91  ? 33.805 -4.395  14.489  1.00 22.98 ?  91  HIS   A CE1  1 
ATOM   1856 N NE2  . HIS   A 1 91  ? 33.011 -5.333  14.975  1.00 22.84 ?  91  HIS   A NE2  1 
ATOM   1857 H H    . HIS   A 1 91  ? 29.029 -2.932  14.200  1.00 15.73 ?  91  HIS   A H    1 
ATOM   1858 H HA   . HIS   A 1 91  ? 30.980 -1.706  12.747  1.00 15.09 ?  91  HIS   A HA   1 
ATOM   1859 H HB2  . HIS   A 1 91  ? 30.165 -4.400  12.383  1.00 18.32 ?  91  HIS   A HB2  1 
ATOM   1860 H HB3  . HIS   A 1 91  ? 31.329 -3.678  11.582  1.00 18.32 ?  91  HIS   A HB3  1 
ATOM   1861 H HD1  . HIS   A 1 91  ? 33.460 -3.085  13.086  1.00 26.43 ?  91  HIS   A HD1  1 
ATOM   1862 H HD2  . HIS   A 1 91  ? 31.072 -5.824  14.485  1.00 25.86 ?  91  HIS   A HD2  1 
ATOM   1863 H HE1  . HIS   A 1 91  ? 34.682 -4.222  14.759  1.00 27.58 ?  91  HIS   A HE1  1 
ATOM   1864 N N    . CYS   A 1 92  ? 29.606 -1.492  10.675  1.00 11.45 ?  92  CYS   A N    1 
ATOM   1865 C CA   . CYS   A 1 92  ? 28.775 -1.414  9.481   1.00 11.39 ?  92  CYS   A CA   1 
ATOM   1866 C C    . CYS   A 1 92  ? 29.422 -2.237  8.374   1.00 10.91 ?  92  CYS   A C    1 
ATOM   1867 O O    . CYS   A 1 92  ? 30.580 -1.989  8.003   1.00 11.38 ?  92  CYS   A O    1 
ATOM   1868 C CB   . CYS   A 1 92  ? 28.561 0.032   9.022   1.00 11.52 ?  92  CYS   A CB   1 
ATOM   1869 S SG   . CYS   A 1 92  ? 27.538 0.144   7.519   1.00 10.97 ?  92  CYS   A SG   1 
ATOM   1870 H H    . CYS   A 1 92  ? 30.373 -1.104  10.591  1.00 13.74 ?  92  CYS   A H    1 
ATOM   1871 H HA   . CYS   A 1 92  ? 27.909 -1.794  9.675   1.00 13.66 ?  92  CYS   A HA   1 
ATOM   1872 H HB2  . CYS   A 1 92  ? 28.111 0.530   9.725   1.00 13.82 ?  92  CYS   A HB2  1 
ATOM   1873 H HB3  . CYS   A 1 92  ? 29.419 0.440   8.827   1.00 13.82 ?  92  CYS   A HB3  1 
ATOM   1874 H HG   . CYS   A 1 92  ? 27.396 1.293   7.224   1.00 13.16 ?  92  CYS   A HG   1 
ATOM   1875 N N    . LEU   A 1 93  ? 28.678 -3.219  7.867   1.00 10.62 ?  93  LEU   A N    1 
ATOM   1876 C CA   . LEU   A 1 93  ? 29.074 -3.978  6.687   1.00 10.48 ?  93  LEU   A CA   1 
ATOM   1877 C C    . LEU   A 1 93  ? 28.477 -3.280  5.469   1.00 9.95  ?  93  LEU   A C    1 
ATOM   1878 O O    . LEU   A 1 93  ? 27.261 -3.329  5.245   1.00 9.85  ?  93  LEU   A O    1 
ATOM   1879 C CB   . LEU   A 1 93  ? 28.588 -5.422  6.793   1.00 10.95 ?  93  LEU   A CB   1 
ATOM   1880 C CG   . LEU   A 1 93  ? 28.976 -6.323  5.623   1.00 11.06 ?  93  LEU   A CG   1 
ATOM   1881 C CD1  . LEU   A 1 93  ? 30.480 -6.572  5.619   1.00 12.17 ?  93  LEU   A CD1  1 
ATOM   1882 C CD2  . LEU   A 1 93  ? 28.204 -7.646  5.649   1.00 11.87 ?  93  LEU   A CD2  1 
ATOM   1883 H H    . LEU   A 1 93  ? 27.924 -3.463  8.206   1.00 12.74 ?  93  LEU   A H    1 
ATOM   1884 H HA   . LEU   A 1 93  ? 30.039 -3.971  6.615   1.00 12.57 ?  93  LEU   A HA   1 
ATOM   1885 H HB2  . LEU   A 1 93  ? 28.960 -5.808  7.605   1.00 13.14 ?  93  LEU   A HB2  1 
ATOM   1886 H HB3  . LEU   A 1 93  ? 27.622 -5.416  6.854   1.00 13.14 ?  93  LEU   A HB3  1 
ATOM   1887 H HG   . LEU   A 1 93  ? 28.758 -5.872  4.801   1.00 13.27 ?  93  LEU   A HG   1 
ATOM   1888 H HD11 . LEU   A 1 93  ? 30.702 -7.197  4.910   1.00 14.61 ?  93  LEU   A HD11 1 
ATOM   1889 H HD12 . LEU   A 1 93  ? 30.949 -5.734  5.478   1.00 14.61 ?  93  LEU   A HD12 1 
ATOM   1890 H HD13 . LEU   A 1 93  ? 30.749 -6.952  6.479   1.00 14.61 ?  93  LEU   A HD13 1 
ATOM   1891 H HD21 . LEU   A 1 93  ? 28.484 -8.189  4.891   1.00 14.25 ?  93  LEU   A HD21 1 
ATOM   1892 H HD22 . LEU   A 1 93  ? 28.397 -8.117  6.476   1.00 14.25 ?  93  LEU   A HD22 1 
ATOM   1893 H HD23 . LEU   A 1 93  ? 27.255 -7.461  5.587   1.00 14.25 ?  93  LEU   A HD23 1 
ATOM   1894 N N    . HIS   A 1 94  ? 29.330 -2.583  4.716   1.00 9.45  ?  94  HIS   A N    1 
ATOM   1895 C CA   . HIS   A 1 94  ? 28.910 -1.904  3.494   1.00 9.79  ?  94  HIS   A CA   1 
ATOM   1896 C C    . HIS   A 1 94  ? 28.910 -2.935  2.381   1.00 9.71  ?  94  HIS   A C    1 
ATOM   1897 O O    . HIS   A 1 94  ? 29.974 -3.443  2.025   1.00 11.14 ?  94  HIS   A O    1 
ATOM   1898 C CB   . HIS   A 1 94  ? 29.872 -0.763  3.163   1.00 9.90  ?  94  HIS   A CB   1 
ATOM   1899 C CG   . HIS   A 1 94  ? 29.858 0.334   4.174   1.00 9.95  ?  94  HIS   A CG   1 
ATOM   1900 N ND1  . HIS   A 1 94  ? 28.974 1.391   4.121   1.00 10.20 ?  94  HIS   A ND1  1 
ATOM   1901 C CD2  . HIS   A 1 94  ? 30.596 0.502   5.296   1.00 10.65 ?  94  HIS   A CD2  1 
ATOM   1902 C CE1  . HIS   A 1 94  ? 29.188 2.171   5.165   1.00 10.28 ?  94  HIS   A CE1  1 
ATOM   1903 N NE2  . HIS   A 1 94  ? 30.163 1.654   5.893   1.00 10.39 ?  94  HIS   A NE2  1 
ATOM   1904 H H    . HIS   A 1 94  ? 30.169 -2.486  4.898   1.00 11.34 ?  94  HIS   A H    1 
ATOM   1905 H HA   . HIS   A 1 94  ? 28.013 -1.552  3.600   1.00 11.74 ?  94  HIS   A HA   1 
ATOM   1906 H HB2  . HIS   A 1 94  ? 30.770 -1.116  3.114   1.00 11.88 ?  94  HIS   A HB2  1 
ATOM   1907 H HB3  . HIS   A 1 94  ? 29.616 -0.382  2.307   1.00 11.88 ?  94  HIS   A HB3  1 
ATOM   1908 H HD2  . HIS   A 1 94  ? 31.273 -0.053  5.601   1.00 12.78 ?  94  HIS   A HD2  1 
ATOM   1909 H HE1  . HIS   A 1 94  ? 28.717 2.954   5.355   1.00 12.33 ?  94  HIS   A HE1  1 
ATOM   1910 H HE2  . HIS   A 1 94  ? 30.475 1.998   6.615   1.00 12.46 ?  94  HIS   A HE2  1 
ATOM   1911 N N    . VAL   A 1 95  ? 27.737 -3.261  1.833   1.00 9.12  ?  95  VAL   A N    1 
ATOM   1912 C CA   . VAL   A 1 95  ? 27.596 -4.294  0.810   1.00 9.42  ?  95  VAL   A CA   1 
ATOM   1913 C C    . VAL   A 1 95  ? 27.053 -3.652  -0.456  1.00 9.44  ?  95  VAL   A C    1 
ATOM   1914 O O    . VAL   A 1 95  ? 26.051 -2.928  -0.406  1.00 9.95  ?  95  VAL   A O    1 
ATOM   1915 C CB   . VAL   A 1 95  ? 26.663 -5.435  1.259   1.00 10.27 ?  95  VAL   A CB   1 
ATOM   1916 C CG1  . VAL   A 1 95  ? 26.566 -6.473  0.162   1.00 11.23 ?  95  VAL   A CG1  1 
ATOM   1917 C CG2  . VAL   A 1 95  ? 27.164 -6.056  2.546   1.00 10.55 ?  95  VAL   A CG2  1 
ATOM   1918 H H    . VAL   A 1 95  ? 26.988 -2.890  2.048   1.00 10.94 ?  95  VAL   A H    1 
ATOM   1919 H HA   . VAL   A 1 95  ? 28.465 -4.673  0.613   1.00 11.31 ?  95  VAL   A HA   1 
ATOM   1920 H HB   . VAL   A 1 95  ? 25.777 -5.082  1.422   1.00 12.33 ?  95  VAL   A HB   1 
ATOM   1921 H HG11 . VAL   A 1 95  ? 26.178 -7.288  0.524   1.00 13.47 ?  95  VAL   A HG11 1 
ATOM   1922 H HG12 . VAL   A 1 95  ? 26.004 -6.136  -0.554  1.00 13.47 ?  95  VAL   A HG12 1 
ATOM   1923 H HG13 . VAL   A 1 95  ? 27.457 -6.663  -0.181  1.00 13.47 ?  95  VAL   A HG13 1 
ATOM   1924 H HG21 . VAL   A 1 95  ? 26.601 -6.813  2.772   1.00 12.66 ?  95  VAL   A HG21 1 
ATOM   1925 H HG22 . VAL   A 1 95  ? 28.079 -6.348  2.422   1.00 12.66 ?  95  VAL   A HG22 1 
ATOM   1926 H HG23 . VAL   A 1 95  ? 27.121 -5.391  3.253   1.00 12.66 ?  95  VAL   A HG23 1 
ATOM   1927 N N    . VAL   A 1 96  ? 27.689 -3.940  -1.591  1.00 9.42  ?  96  VAL   A N    1 
ATOM   1928 C CA   . VAL   A 1 96  ? 27.287 -3.384  -2.877  1.00 10.54 ?  96  VAL   A CA   1 
ATOM   1929 C C    . VAL   A 1 96  ? 26.472 -4.423  -3.636  1.00 10.34 ?  96  VAL   A C    1 
ATOM   1930 O O    . VAL   A 1 96  ? 27.023 -5.365  -4.211  1.00 11.20 ?  96  VAL   A O    1 
ATOM   1931 C CB   . VAL   A 1 96  ? 28.486 -2.908  -3.699  1.00 10.58 ?  96  VAL   A CB   1 
ATOM   1932 C CG1  . VAL   A 1 96  ? 27.983 -2.268  -4.976  1.00 10.90 ?  96  VAL   A CG1  1 
ATOM   1933 C CG2  . VAL   A 1 96  ? 29.348 -1.940  -2.899  1.00 11.31 ?  96  VAL   A CG2  1 
ATOM   1934 H H    . VAL   A 1 96  ? 28.380 -4.459  -1.636  1.00 11.31 ?  96  VAL   A H    1 
ATOM   1935 H HA   . VAL   A 1 96  ? 26.718 -2.617  -2.718  1.00 12.65 ?  96  VAL   A HA   1 
ATOM   1936 H HB   . VAL   A 1 96  ? 29.033 -3.670  -3.938  1.00 12.70 ?  96  VAL   A HB   1 
ATOM   1937 H HG11 . VAL   A 1 96  ? 28.722 -1.796  -5.396  1.00 13.07 ?  96  VAL   A HG11 1 
ATOM   1938 H HG12 . VAL   A 1 96  ? 27.654 -2.958  -5.568  1.00 13.07 ?  96  VAL   A HG12 1 
ATOM   1939 H HG13 . VAL   A 1 96  ? 27.277 -1.643  -4.758  1.00 13.07 ?  96  VAL   A HG13 1 
ATOM   1940 H HG21 . VAL   A 1 96  ? 30.053 -1.595  -3.465  1.00 13.58 ?  96  VAL   A HG21 1 
ATOM   1941 H HG22 . VAL   A 1 96  ? 28.790 -1.205  -2.583  1.00 13.58 ?  96  VAL   A HG22 1 
ATOM   1942 H HG23 . VAL   A 1 96  ? 29.730 -2.406  -2.138  1.00 13.58 ?  96  VAL   A HG23 1 
ATOM   1943 N N    . GLY   A 1 97  ? 25.154 -4.259  -3.657  1.00 10.34 ?  97  GLY   A N    1 
ATOM   1944 C CA   . GLY   A 1 97  ? 24.338 -5.021  -4.563  1.00 11.39 ?  97  GLY   A CA   1 
ATOM   1945 C C    . GLY   A 1 97  ? 24.340 -4.369  -5.931  1.00 11.22 ?  97  GLY   A C    1 
ATOM   1946 O O    . GLY   A 1 97  ? 24.617 -3.170  -6.071  1.00 12.01 ?  97  GLY   A O    1 
ATOM   1947 H H    . GLY   A 1 97  ? 24.715 -3.708  -3.154  1.00 12.41 ?  97  GLY   A H    1 
ATOM   1948 H HA2  . GLY   A 1 97  ? 24.696 -5.920  -4.624  1.00 13.66 ?  97  GLY   A HA2  1 
ATOM   1949 H HA3  . GLY   A 1 97  ? 23.427 -5.066  -4.232  1.00 13.66 ?  97  GLY   A HA3  1 
ATOM   1950 N N    A PRO   A 1 98  ? 23.997 -5.121  -6.975  0.84 11.41 ?  98  PRO   A N    1 
ATOM   1951 N N    B PRO   A 1 98  ? 24.068 -5.165  -6.964  0.16 11.68 ?  98  PRO   A N    1 
ATOM   1952 C CA   A PRO   A 1 98  ? 23.880 -4.503  -8.302  0.84 12.50 ?  98  PRO   A CA   1 
ATOM   1953 C CA   B PRO   A 1 98  ? 24.039 -4.624  -8.325  0.16 12.29 ?  98  PRO   A CA   1 
ATOM   1954 C C    A PRO   A 1 98  ? 22.769 -3.457  -8.336  0.84 12.29 ?  98  PRO   A C    1 
ATOM   1955 C C    B PRO   A 1 98  ? 22.907 -3.626  -8.495  0.16 12.83 ?  98  PRO   A C    1 
ATOM   1956 O O    A PRO   A 1 98  ? 21.701 -3.632  -7.747  0.84 12.06 ?  98  PRO   A O    1 
ATOM   1957 O O    B PRO   A 1 98  ? 21.781 -3.847  -8.045  0.16 12.94 ?  98  PRO   A O    1 
ATOM   1958 C CB   A PRO   A 1 98  ? 23.563 -5.690  -9.218  0.84 12.80 ?  98  PRO   A CB   1 
ATOM   1959 C CB   B PRO   A 1 98  ? 23.812 -5.867  -9.194  0.16 12.20 ?  98  PRO   A CB   1 
ATOM   1960 C CG   A PRO   A 1 98  ? 22.909 -6.691  -8.314  0.84 12.87 ?  98  PRO   A CG   1 
ATOM   1961 C CG   B PRO   A 1 98  ? 23.166 -6.858  -8.275  0.16 12.17 ?  98  PRO   A CG   1 
ATOM   1962 C CD   A PRO   A 1 98  ? 23.665 -6.557  -7.008  0.84 11.90 ?  98  PRO   A CD   1 
ATOM   1963 C CD   B PRO   A 1 98  ? 23.801 -6.614  -6.940  0.16 11.76 ?  98  PRO   A CD   1 
ATOM   1964 H HA   A PRO   A 1 98  ? 24.723 -4.099  -8.563  0.84 15.00 ?  98  PRO   A HA   1 
ATOM   1965 H HA   B PRO   A 1 98  ? 24.887 -4.210  -8.551  0.16 14.75 ?  98  PRO   A HA   1 
ATOM   1966 H HB2  A PRO   A 1 98  ? 22.956 -5.406  -9.921  0.84 15.36 ?  98  PRO   A HB2  1 
ATOM   1967 H HB2  B PRO   A 1 98  ? 23.222 -5.644  -9.931  0.16 14.64 ?  98  PRO   A HB2  1 
ATOM   1968 H HB3  A PRO   A 1 98  ? 24.385 -6.044  -9.593  0.84 15.36 ?  98  PRO   A HB3  1 
ATOM   1969 H HB3  B PRO   A 1 98  ? 24.661 -6.200  -9.518  0.16 14.64 ?  98  PRO   A HB3  1 
ATOM   1970 H HG2  A PRO   A 1 98  ? 21.973 -6.465  -8.200  0.84 15.44 ?  98  PRO   A HG2  1 
ATOM   1971 H HG2  B PRO   A 1 98  ? 22.209 -6.693  -8.234  0.16 14.60 ?  98  PRO   A HG2  1 
ATOM   1972 H HG3  A PRO   A 1 98  ? 23.010 -7.580  -8.685  0.84 15.44 ?  98  PRO   A HG3  1 
ATOM   1973 H HG3  B PRO   A 1 98  ? 23.346 -7.758  -8.583  0.16 14.60 ?  98  PRO   A HG3  1 
ATOM   1974 H HD2  A PRO   A 1 98  ? 23.091 -6.794  -6.260  0.84 14.28 ?  98  PRO   A HD2  1 
ATOM   1975 H HD2  B PRO   A 1 98  ? 23.185 -6.837  -6.224  0.16 14.11 ?  98  PRO   A HD2  1 
ATOM   1976 H HD3  A PRO   A 1 98  ? 24.471 -7.095  -7.023  0.84 14.28 ?  98  PRO   A HD3  1 
ATOM   1977 H HD3  B PRO   A 1 98  ? 24.632 -7.111  -6.862  0.16 14.11 ?  98  PRO   A HD3  1 
ATOM   1978 N N    A ASN   A 1 99  ? 23.038 -2.351  -9.028  0.84 13.51 ?  99  ASN   A N    1 
ATOM   1979 N N    B ASN   A 1 99  ? 23.219 -2.519  -9.156  0.16 13.41 ?  99  ASN   A N    1 
ATOM   1980 C CA   A ASN   A 1 99  ? 22.063 -1.279  -9.231  0.84 14.89 ?  99  ASN   A CA   1 
ATOM   1981 C CA   B ASN   A 1 99  ? 22.228 -1.497  -9.463  0.16 14.22 ?  99  ASN   A CA   1 
ATOM   1982 C C    A ASN   A 1 99  ? 21.489 -1.424  -10.639 0.84 16.00 ?  99  ASN   A C    1 
ATOM   1983 C C    B ASN   A 1 99  ? 21.695 -1.782  -10.863 0.16 14.66 ?  99  ASN   A C    1 
ATOM   1984 O O    A ASN   A 1 99  ? 22.172 -1.139  -11.631 0.84 17.49 ?  99  ASN   A O    1 
ATOM   1985 O O    B ASN   A 1 99  ? 22.430 -1.679  -11.852 0.16 13.98 ?  99  ASN   A O    1 
ATOM   1986 C CB   A ASN   A 1 99  ? 22.707 0.095   -9.031  0.84 15.41 ?  99  ASN   A CB   1 
ATOM   1987 C CB   B ASN   A 1 99  ? 22.852 -0.107  -9.364  0.16 14.99 ?  99  ASN   A CB   1 
ATOM   1988 C CG   A ASN   A 1 99  ? 21.686 1.246   -9.034  0.84 15.91 ?  99  ASN   A CG   1 
ATOM   1989 C CG   B ASN   A 1 99  ? 21.815 0.998   -9.363  0.16 15.79 ?  99  ASN   A CG   1 
ATOM   1990 O OD1  A ASN   A 1 99  ? 20.674 1.200   -9.737  0.84 16.53 ?  99  ASN   A OD1  1 
ATOM   1991 O OD1  B ASN   A 1 99  ? 20.899 1.005   -10.186 0.16 15.87 ?  99  ASN   A OD1  1 
ATOM   1992 N ND2  A ASN   A 1 99  ? 21.966 2.288   -8.247  0.84 16.58 ?  99  ASN   A ND2  1 
ATOM   1993 N ND2  B ASN   A 1 99  ? 21.945 1.935   -8.427  0.16 16.12 ?  99  ASN   A ND2  1 
ATOM   1994 H H    A ASN   A 1 99  ? 23.804 -2.187  -9.379  0.84 16.21 ?  99  ASN   A H    1 
ATOM   1995 H H    B ASN   A 1 99  ? 24.007 -2.336  -9.445  0.16 16.09 ?  99  ASN   A H    1 
ATOM   1996 H HA   A ASN   A 1 99  ? 21.341 -1.373  -8.578  0.84 17.86 ?  99  ASN   A HA   1 
ATOM   1997 H HA   B ASN   A 1 99  ? 21.493 -1.553  -8.828  0.16 17.07 ?  99  ASN   A HA   1 
ATOM   1998 H HB2  A ASN   A 1 99  ? 23.175 0.112   -8.179  0.84 18.49 ?  99  ASN   A HB2  1 
ATOM   1999 H HB2  B ASN   A 1 99  ? 23.360 -0.045  -8.538  0.16 17.99 ?  99  ASN   A HB2  1 
ATOM   2000 H HB3  A ASN   A 1 99  ? 23.334 0.253   -9.753  0.84 18.49 ?  99  ASN   A HB3  1 
ATOM   2001 H HB3  B ASN   A 1 99  ? 23.436 0.031   -10.122 0.16 17.99 ?  99  ASN   A HB3  1 
ATOM   2002 H HD21 A ASN   A 1 99  ? 21.431 2.959   -8.211  0.84 19.89 ?  99  ASN   A HD21 1 
ATOM   2003 H HD21 B ASN   A 1 99  ? 21.379 2.580   -8.380  0.16 19.34 ?  99  ASN   A HD21 1 
ATOM   2004 H HD22 A ASN   A 1 99  ? 22.686 2.289   -7.770  0.84 19.89 ?  99  ASN   A HD22 1 
ATOM   2005 H HD22 B ASN   A 1 99  ? 22.598 1.896   -7.865  0.16 19.34 ?  99  ASN   A HD22 1 
ATOM   2006 N N    A VAL   A 1 100 ? 20.232 -1.873  -10.713 0.84 16.34 ?  100 VAL   A N    1 
ATOM   2007 N N    B VAL   A 1 100 ? 20.424 -2.180  -10.940 0.16 16.16 ?  100 VAL   A N    1 
ATOM   2008 C CA   A VAL   A 1 100 ? 19.587 -2.099  -12.002 0.84 18.50 ?  100 VAL   A CA   1 
ATOM   2009 C CA   B VAL   A 1 100 ? 19.820 -2.500  -12.229 0.16 18.04 ?  100 VAL   A CA   1 
ATOM   2010 C C    A VAL   A 1 100 ? 19.471 -0.802  -12.786 0.84 19.14 ?  100 VAL   A C    1 
ATOM   2011 C C    B VAL   A 1 100 ? 19.783 -1.275  -13.128 0.16 19.24 ?  100 VAL   A C    1 
ATOM   2012 O O    A VAL   A 1 100 ? 19.530 -0.807  -14.021 0.84 20.70 ?  100 VAL   A O    1 
ATOM   2013 O O    B VAL   A 1 100 ? 19.866 -1.395  -14.357 0.16 19.56 ?  100 VAL   A O    1 
ATOM   2014 C CB   A VAL   A 1 100 ? 18.223 -2.791  -11.798 0.84 20.58 ?  100 VAL   A CB   1 
ATOM   2015 C CB   B VAL   A 1 100 ? 18.414 -3.094  -12.024 0.16 18.71 ?  100 VAL   A CB   1 
ATOM   2016 C CG1  A VAL   A 1 100 ? 17.485 -2.943  -13.123 0.84 21.27 ?  100 VAL   A CG1  1 
ATOM   2017 C CG1  B VAL   A 1 100 ? 17.845 -3.583  -13.349 0.16 18.82 ?  100 VAL   A CG1  1 
ATOM   2018 C CG2  A VAL   A 1 100 ? 18.425 -4.146  -11.143 0.84 21.62 ?  100 VAL   A CG2  1 
ATOM   2019 C CG2  B VAL   A 1 100 ? 18.460 -4.216  -11.003 0.16 19.05 ?  100 VAL   A CG2  1 
ATOM   2020 H H    A VAL   A 1 100 ? 19.731 -2.053  -10.026 0.84 19.60 ?  100 VAL   A H    1 
ATOM   2021 H H    B VAL   A 1 100 ? 19.905 -2.280  -10.264 0.16 19.39 ?  100 VAL   A H    1 
ATOM   2022 H HA   A VAL   A 1 100 ? 20.142 -2.698  -12.516 0.84 22.19 ?  100 VAL   A HA   1 
ATOM   2023 H HA   B VAL   A 1 100 ? 20.364 -3.170  -12.669 0.16 21.65 ?  100 VAL   A HA   1 
ATOM   2024 H HB   A VAL   A 1 100 ? 17.674 -2.249  -11.209 0.84 24.70 ?  100 VAL   A HB   1 
ATOM   2025 H HB   B VAL   A 1 100 ? 17.827 -2.400  -11.685 0.16 22.45 ?  100 VAL   A HB   1 
ATOM   2026 H HG11 A VAL   A 1 100 ? 16.734 -3.544  -12.998 0.84 25.52 ?  100 VAL   A HG11 1 
ATOM   2027 H HG11 B VAL   A 1 100 ? 17.002 -4.031  -13.181 0.16 22.58 ?  100 VAL   A HG11 1 
ATOM   2028 H HG12 A VAL   A 1 100 ? 17.167 -2.074  -13.413 0.84 25.52 ?  100 VAL   A HG12 1 
ATOM   2029 H HG12 B VAL   A 1 100 ? 17.703 -2.822  -13.935 0.16 22.58 ?  100 VAL   A HG12 1 
ATOM   2030 H HG13 A VAL   A 1 100 ? 18.094 -3.311  -13.783 0.84 25.52 ?  100 VAL   A HG13 1 
ATOM   2031 H HG13 B VAL   A 1 100 ? 18.474 -4.200  -13.753 0.16 22.58 ?  100 VAL   A HG13 1 
ATOM   2032 H HG21 A VAL   A 1 100 ? 17.569 -4.596  -11.077 0.84 25.94 ?  100 VAL   A HG21 1 
ATOM   2033 H HG21 B VAL   A 1 100 ? 17.637 -4.723  -11.058 0.16 22.86 ?  100 VAL   A HG21 1 
ATOM   2034 H HG22 A VAL   A 1 100 ? 19.034 -4.671  -11.686 0.84 25.94 ?  100 VAL   A HG22 1 
ATOM   2035 H HG22 B VAL   A 1 100 ? 19.218 -4.788  -11.201 0.16 22.86 ?  100 VAL   A HG22 1 
ATOM   2036 H HG23 A VAL   A 1 100 ? 18.801 -4.017  -10.258 0.84 25.94 ?  100 VAL   A HG23 1 
ATOM   2037 H HG23 B VAL   A 1 100 ? 18.556 -3.834  -10.117 0.16 22.86 ?  100 VAL   A HG23 1 
ATOM   2038 N N    A ASN   A 1 101 ? 19.304 0.325   -12.099 0.84 20.55 ?  101 ASN   A N    1 
ATOM   2039 N N    B ASN   A 1 101 ? 19.651 -0.084  -12.541 0.16 20.22 ?  101 ASN   A N    1 
ATOM   2040 C CA   A ASN   A 1 101 ? 19.255 1.604   -12.797 0.84 22.53 ?  101 ASN   A CA   1 
ATOM   2041 C CA   B ASN   A 1 101 ? 19.605 1.134   -13.342 0.16 21.11 ?  101 ASN   A CA   1 
ATOM   2042 C C    A ASN   A 1 101 ? 20.619 2.032   -13.349 0.84 24.70 ?  101 ASN   A C    1 
ATOM   2043 C C    B ASN   A 1 101 ? 20.967 1.465   -13.937 0.16 22.44 ?  101 ASN   A C    1 
ATOM   2044 O O    A ASN   A 1 101 ? 20.701 3.090   -13.987 0.84 26.45 ?  101 ASN   A O    1 
ATOM   2045 O O    B ASN   A 1 101 ? 21.040 2.075   -15.009 0.16 22.39 ?  101 ASN   A O    1 
ATOM   2046 C CB   A ASN   A 1 101 ? 18.615 2.652   -11.883 0.84 22.28 ?  101 ASN   A CB   1 
ATOM   2047 C CB   B ASN   A 1 101 ? 19.073 2.290   -12.493 0.16 20.66 ?  101 ASN   A CB   1 
ATOM   2048 C CG   A ASN   A 1 101 ? 17.239 2.214   -11.382 0.84 21.96 ?  101 ASN   A CG   1 
ATOM   2049 C CG   B ASN   A 1 101 ? 17.796 1.927   -11.756 0.16 20.36 ?  101 ASN   A CG   1 
ATOM   2050 O OD1  A ASN   A 1 101 ? 16.431 1.672   -12.143 0.84 22.43 ?  101 ASN   A OD1  1 
ATOM   2051 O OD1  B ASN   A 1 101 ? 16.906 1.283   -12.313 0.16 20.53 ?  101 ASN   A OD1  1 
ATOM   2052 N ND2  A ASN   A 1 101 ? 16.978 2.420   -10.096 0.84 21.78 ?  101 ASN   A ND2  1 
ATOM   2053 N ND2  B ASN   A 1 101 ? 17.708 2.326   -10.494 0.16 20.09 ?  101 ASN   A ND2  1 
ATOM   2054 H H    A ASN   A 1 101 ? 19.205 0.378   -11.248 0.84 24.66 ?  101 ASN   A H    1 
ATOM   2055 H H    B ASN   A 1 101 ? 19.587 0.045   -11.693 0.16 24.26 ?  101 ASN   A H    1 
ATOM   2056 H HA   A ASN   A 1 101 ? 18.670 1.509   -13.560 0.84 27.03 ?  101 ASN   A HA   1 
ATOM   2057 H HA   B ASN   A 1 101 ? 18.992 1.006   -14.078 0.16 25.33 ?  101 ASN   A HA   1 
ATOM   2058 H HB2  A ASN   A 1 101 ? 19.185 2.804   -11.114 0.84 26.74 ?  101 ASN   A HB2  1 
ATOM   2059 H HB2  B ASN   A 1 101 ? 19.737 2.538   -11.831 0.16 24.79 ?  101 ASN   A HB2  1 
ATOM   2060 H HB3  A ASN   A 1 101 ? 18.506 3.486   -12.380 0.84 26.74 ?  101 ASN   A HB3  1 
ATOM   2061 H HB3  B ASN   A 1 101 ? 18.880 3.049   -13.068 0.16 24.79 ?  101 ASN   A HB3  1 
ATOM   2062 H HD21 A ASN   A 1 101 ? 16.214 2.190   -9.775  0.84 26.13 ?  101 ASN   A HD21 1 
ATOM   2063 H HD21 B ASN   A 1 101 ? 17.004 2.142   -10.034 0.16 24.11 ?  101 ASN   A HD21 1 
ATOM   2064 H HD22 A ASN   A 1 101 ? 17.561 2.799   -9.594  0.84 26.13 ?  101 ASN   A HD22 1 
ATOM   2065 H HD22 B ASN   A 1 101 ? 18.351 2.770   -10.137 0.16 24.11 ?  101 ASN   A HD22 1 
ATOM   2066 N N    A LYS   A 1 102 ? 21.667 1.225   -13.145 0.84 26.80 ?  102 LYS   A N    1 
ATOM   2067 N N    B LYS   A 1 102 ? 22.050 1.065   -13.269 0.16 23.86 ?  102 LYS   A N    1 
ATOM   2068 C CA   A LYS   A 1 102 ? 22.957 1.390   -13.807 0.84 28.41 ?  102 LYS   A CA   1 
ATOM   2069 C CA   B LYS   A 1 102 ? 23.392 1.230   -13.811 0.16 25.19 ?  102 LYS   A CA   1 
ATOM   2070 C C    A LYS   A 1 102 ? 23.262 0.273   -14.800 0.84 28.47 ?  102 LYS   A C    1 
ATOM   2071 C C    B LYS   A 1 102 ? 23.757 0.140   -14.811 0.16 25.48 ?  102 LYS   A C    1 
ATOM   2072 O O    A LYS   A 1 102 ? 24.345 0.276   -15.395 0.84 29.03 ?  102 LYS   A O    1 
ATOM   2073 O O    B LYS   A 1 102 ? 24.876 0.152   -15.334 0.16 25.67 ?  102 LYS   A O    1 
ATOM   2074 C CB   A LYS   A 1 102 ? 24.093 1.444   -12.776 0.84 30.04 ?  102 LYS   A CB   1 
ATOM   2075 C CB   B LYS   A 1 102 ? 24.427 1.250   -12.681 0.16 26.15 ?  102 LYS   A CB   1 
ATOM   2076 C CG   A LYS   A 1 102 ? 23.996 2.574   -11.770 0.84 31.42 ?  102 LYS   A CG   1 
ATOM   2077 C CG   B LYS   A 1 102 ? 24.467 2.550   -11.890 0.16 26.96 ?  102 LYS   A CG   1 
ATOM   2078 C CD   A LYS   A 1 102 ? 25.177 2.544   -10.806 0.84 32.96 ?  102 LYS   A CD   1 
ATOM   2079 C CD   B LYS   A 1 102 ? 25.359 2.430   -10.661 0.16 27.64 ?  102 LYS   A CD   1 
ATOM   2080 C CE   A LYS   A 1 102 ? 25.087 3.661   -9.781  0.84 34.15 ?  102 LYS   A CE   1 
ATOM   2081 C CE   B LYS   A 1 102 ? 25.510 3.768   -9.950  0.16 28.13 ?  102 LYS   A CE   1 
ATOM   2082 N NZ   A LYS   A 1 102 ? 26.206 3.613   -8.797  0.84 34.92 ?  102 LYS   A NZ   1 
ATOM   2083 N NZ   B LYS   A 1 102 ? 26.218 3.636   -8.645  0.16 28.42 ?  102 LYS   A NZ   1 
ATOM   2084 H H    A LYS   A 1 102 ? 21.652 0.552   -12.608 0.84 32.16 ?  102 LYS   A H    1 
ATOM   2085 H H    B LYS   A 1 102 ? 22.030 0.685   -12.499 0.16 28.63 ?  102 LYS   A H    1 
ATOM   2086 H HA   A LYS   A 1 102 ? 22.957 2.226   -14.293 0.84 34.09 ?  102 LYS   A HA   1 
ATOM   2087 H HA   B LYS   A 1 102 ? 23.440 2.084   -14.266 0.16 30.23 ?  102 LYS   A HA   1 
ATOM   2088 H HB2  A LYS   A 1 102 ? 24.100 0.610   -12.279 0.84 36.05 ?  102 LYS   A HB2  1 
ATOM   2089 H HB2  B LYS   A 1 102 ? 24.229 0.532   -12.062 0.16 31.37 ?  102 LYS   A HB2  1 
ATOM   2090 H HB3  A LYS   A 1 102 ? 24.935 1.545   -13.249 0.84 36.05 ?  102 LYS   A HB3  1 
ATOM   2091 H HB3  B LYS   A 1 102 ? 25.308 1.115   -13.063 0.16 31.37 ?  102 LYS   A HB3  1 
ATOM   2092 H HG2  A LYS   A 1 102 ? 24.004 3.424   -12.237 0.84 37.71 ?  102 LYS   A HG2  1 
ATOM   2093 H HG2  B LYS   A 1 102 ? 24.822 3.257   -12.454 0.16 32.34 ?  102 LYS   A HG2  1 
ATOM   2094 H HG3  A LYS   A 1 102 ? 23.179 2.478   -11.255 0.84 37.71 ?  102 LYS   A HG3  1 
ATOM   2095 H HG3  B LYS   A 1 102 ? 23.571 2.774   -11.595 0.16 32.34 ?  102 LYS   A HG3  1 
ATOM   2096 H HD2  A LYS   A 1 102 ? 25.183 1.696   -10.334 0.84 39.55 ?  102 LYS   A HD2  1 
ATOM   2097 H HD2  B LYS   A 1 102 ? 24.964 1.799   -10.038 0.16 33.17 ?  102 LYS   A HD2  1 
ATOM   2098 H HD3  A LYS   A 1 102 ? 26.001 2.654   -11.307 0.84 39.55 ?  102 LYS   A HD3  1 
ATOM   2099 H HD3  B LYS   A 1 102 ? 26.240 2.128   -10.931 0.16 33.17 ?  102 LYS   A HD3  1 
ATOM   2100 H HE2  A LYS   A 1 102 ? 25.124 4.515   -10.241 0.84 40.98 ?  102 LYS   A HE2  1 
ATOM   2101 H HE2  B LYS   A 1 102 ? 26.023 4.370   -10.513 0.16 33.75 ?  102 LYS   A HE2  1 
ATOM   2102 H HE3  A LYS   A 1 102 ? 24.251 3.579   -9.296  0.84 40.98 ?  102 LYS   A HE3  1 
ATOM   2103 H HE3  B LYS   A 1 102 ? 24.630 4.139   -9.781  0.16 33.75 ?  102 LYS   A HE3  1 
ATOM   2104 H HZ1  A LYS   A 1 102 ? 26.125 4.278   -8.212  0.84 41.91 ?  102 LYS   A HZ1  1 
ATOM   2105 H HZ1  B LYS   A 1 102 ? 26.290 4.433   -8.256  0.16 34.10 ?  102 LYS   A HZ1  1 
ATOM   2106 H HZ2  A LYS   A 1 102 ? 26.191 2.838   -8.358  0.84 41.91 ?  102 LYS   A HZ2  1 
ATOM   2107 H HZ2  B LYS   A 1 102 ? 25.764 3.092   -8.107  0.16 34.10 ?  102 LYS   A HZ2  1 
ATOM   2108 H HZ3  A LYS   A 1 102 ? 26.986 3.691   -9.219  0.84 41.91 ?  102 LYS   A HZ3  1 
ATOM   2109 H HZ3  B LYS   A 1 102 ? 27.033 3.302   -8.773  0.16 34.10 ?  102 LYS   A HZ3  1 
ATOM   2110 N N    A GLY   A 1 103 ? 22.357 -0.689  -14.981 0.84 28.56 ?  103 GLY   A N    1 
ATOM   2111 N N    B GLY   A 1 103 ? 22.852 -0.795  -15.081 0.16 25.55 ?  103 GLY   A N    1 
ATOM   2112 C CA   A GLY   A 1 103 ? 22.590 -1.787  -15.902 0.84 28.33 ?  103 GLY   A CA   1 
ATOM   2113 C CA   B GLY   A 1 103 ? 23.131 -1.854  -16.030 0.16 25.38 ?  103 GLY   A CA   1 
ATOM   2114 C C    A GLY   A 1 103 ? 23.407 -2.937  -15.353 0.84 28.08 ?  103 GLY   A C    1 
ATOM   2115 C C    B GLY   A 1 103 ? 24.037 -2.935  -15.488 0.16 25.13 ?  103 GLY   A C    1 
ATOM   2116 O O    A GLY   A 1 103 ? 23.885 -3.768  -16.131 0.84 28.92 ?  103 GLY   A O    1 
ATOM   2117 O O    B GLY   A 1 103 ? 24.918 -3.421  -16.209 0.16 25.30 ?  103 GLY   A O    1 
ATOM   2118 H H    A GLY   A 1 103 ? 21.598 -0.725  -14.585 0.84 34.27 ?  103 GLY   A H    1 
ATOM   2119 H H    B GLY   A 1 103 ? 22.074 -0.841  -14.720 0.16 30.66 ?  103 GLY   A H    1 
ATOM   2120 H HA2  A GLY   A 1 103 ? 21.732 -2.138  -16.193 0.84 34.00 ?  103 GLY   A HA2  1 
ATOM   2121 H HA2  B GLY   A 1 103 ? 22.297 -2.261  -16.312 0.16 30.46 ?  103 GLY   A HA2  1 
ATOM   2122 H HA3  A GLY   A 1 103 ? 23.050 -1.446  -16.686 0.84 34.00 ?  103 GLY   A HA3  1 
ATOM   2123 H HA3  B GLY   A 1 103 ? 23.564 -1.472  -16.806 0.16 30.46 ?  103 GLY   A HA3  1 
ATOM   2124 N N    A GLU   A 1 104 ? 23.575 -3.024  -14.038 0.84 26.22 ?  104 GLU   A N    1 
ATOM   2125 N N    B GLU   A 1 104 ? 23.843 -3.332  -14.235 0.16 24.50 ?  104 GLU   A N    1 
ATOM   2126 C CA   A GLU   A 1 104 ? 24.447 -4.030  -13.448 0.84 24.55 ?  104 GLU   A CA   1 
ATOM   2127 C CA   B GLU   A 1 104 ? 24.732 -4.264  -13.559 0.16 23.88 ?  104 GLU   A CA   1 
ATOM   2128 C C    A GLU   A 1 104 ? 23.754 -5.389  -13.354 0.84 24.80 ?  104 GLU   A C    1 
ATOM   2129 C C    B GLU   A 1 104 ? 24.071 -5.630  -13.420 0.16 24.02 ?  104 GLU   A C    1 
ATOM   2130 O O    A GLU   A 1 104 ? 22.532 -5.485  -13.205 0.84 25.29 ?  104 GLU   A O    1 
ATOM   2131 O O    B GLU   A 1 104 ? 22.856 -5.733  -13.226 0.16 23.83 ?  104 GLU   A O    1 
ATOM   2132 C CB   A GLU   A 1 104 ? 24.953 -3.548  -12.085 0.84 22.37 ?  104 GLU   A CB   1 
ATOM   2133 C CB   B GLU   A 1 104 ? 25.145 -3.708  -12.194 0.16 23.32 ?  104 GLU   A CB   1 
ATOM   2134 C CG   A GLU   A 1 104 ? 25.942 -2.387  -12.241 0.84 21.70 ?  104 GLU   A CG   1 
ATOM   2135 C CG   B GLU   A 1 104 ? 25.812 -2.341  -12.300 0.16 22.97 ?  104 GLU   A CG   1 
ATOM   2136 C CD   A GLU   A 1 104 ? 26.241 -1.598  -10.974 0.84 20.88 ?  104 GLU   A CD   1 
ATOM   2137 C CD   B GLU   A 1 104 ? 26.283 -1.804  -10.962 0.16 22.73 ?  104 GLU   A CD   1 
ATOM   2138 O OE1  A GLU   A 1 104 ? 25.648 -1.867  -9.911  0.84 19.12 ?  104 GLU   A OE1  1 
ATOM   2139 O OE1  B GLU   A 1 104 ? 25.806 -2.293  -9.917  0.16 22.61 ?  104 GLU   A OE1  1 
ATOM   2140 O OE2  A GLU   A 1 104 ? 27.090 -0.680  -11.063 0.84 21.91 -1 104 GLU   A OE2  1 
ATOM   2141 O OE2  B GLU   A 1 104 ? 27.136 -0.890  -10.957 0.16 22.77 -1 104 GLU   A OE2  1 
ATOM   2142 H H    A GLU   A 1 104 ? 23.198 -2.508  -13.467 0.84 31.47 ?  104 GLU   A H    1 
ATOM   2143 H H    B GLU   A 1 104 ? 23.192 -3.060  -13.743 0.16 29.40 ?  104 GLU   A H    1 
ATOM   2144 H HA   A GLU   A 1 104 ? 25.218 -4.139  -14.023 0.84 29.46 ?  104 GLU   A HA   1 
ATOM   2145 H HA   B GLU   A 1 104 ? 25.535 -4.374  -14.088 0.16 28.66 ?  104 GLU   A HA   1 
ATOM   2146 H HB2  A GLU   A 1 104 ? 24.201 -3.245  -11.553 0.84 26.84 ?  104 GLU   A HB2  1 
ATOM   2147 H HB2  B GLU   A 1 104 ? 24.359 -3.613  -11.634 0.16 27.98 ?  104 GLU   A HB2  1 
ATOM   2148 H HB3  A GLU   A 1 104 ? 25.408 -4.281  -11.638 0.84 26.84 ?  104 GLU   A HB3  1 
ATOM   2149 H HB3  B GLU   A 1 104 ? 25.778 -4.316  -11.781 0.16 27.98 ?  104 GLU   A HB3  1 
ATOM   2150 H HG2  A GLU   A 1 104 ? 26.783 -2.741  -12.562 0.84 26.04 ?  104 GLU   A HG2  1 
ATOM   2151 H HG2  B GLU   A 1 104 ? 26.583 -2.410  -12.887 0.16 27.56 ?  104 GLU   A HG2  1 
ATOM   2152 H HG3  A GLU   A 1 104 ? 25.580 -1.762  -12.887 0.84 26.04 ?  104 GLU   A HG3  1 
ATOM   2153 H HG3  B GLU   A 1 104 ? 25.176 -1.707  -12.671 0.16 27.56 ?  104 GLU   A HG3  1 
ATOM   2154 N N    A ASP   A 1 105 ? 24.563 -6.444  -13.438 0.84 25.29 ?  105 ASP   A N    1 
ATOM   2155 N N    B ASP   A 1 105 ? 24.892 -6.672  -13.526 0.16 24.66 ?  105 ASP   A N    1 
ATOM   2156 C CA   A ASP   A 1 105 ? 24.062 -7.807  -13.583 0.84 26.38 ?  105 ASP   A CA   1 
ATOM   2157 C CA   B ASP   A 1 105 ? 24.417 -8.049  -13.554 0.16 25.33 ?  105 ASP   A CA   1 
ATOM   2158 C C    A ASP   A 1 105 ? 23.385 -8.269  -12.297 0.84 24.18 ?  105 ASP   A C    1 
ATOM   2159 C C    B ASP   A 1 105 ? 23.607 -8.364  -12.304 0.16 25.03 ?  105 ASP   A C    1 
ATOM   2160 O O    A ASP   A 1 105 ? 24.027 -8.356  -11.247 0.84 22.00 ?  105 ASP   A O    1 
ATOM   2161 O O    B ASP   A 1 105 ? 24.120 -8.288  -11.184 0.16 24.92 ?  105 ASP   A O    1 
ATOM   2162 C CB   A ASP   A 1 105 ? 25.232 -8.727  -13.924 0.84 29.83 ?  105 ASP   A CB   1 
ATOM   2163 C CB   B ASP   A 1 105 ? 25.632 -8.972  -13.643 0.16 26.28 ?  105 ASP   A CB   1 
ATOM   2164 C CG   A ASP   A 1 105 ? 24.808 -10.163 -14.120 0.84 32.79 ?  105 ASP   A CG   1 
ATOM   2165 C CG   B ASP   A 1 105 ? 25.263 -10.394 -14.007 0.16 27.05 ?  105 ASP   A CG   1 
ATOM   2166 O OD1  A ASP   A 1 105 ? 23.589 -10.413 -14.225 0.84 33.14 ?  105 ASP   A OD1  1 
ATOM   2167 O OD1  B ASP   A 1 105 ? 24.076 -10.648 -14.295 0.16 27.36 ?  105 ASP   A OD1  1 
ATOM   2168 O OD2  A ASP   A 1 105 ? 25.698 -11.042 -14.165 0.84 34.86 -1 105 ASP   A OD2  1 
ATOM   2169 O OD2  B ASP   A 1 105 ? 26.166 -11.260 -14.004 0.16 27.34 -1 105 ASP   A OD2  1 
ATOM   2170 H H    A ASP   A 1 105 ? 25.422 -6.396  -13.410 0.84 30.35 ?  105 ASP   A H    1 
ATOM   2171 H H    B ASP   A 1 105 ? 25.742 -6.604  -13.585 0.16 29.59 ?  105 ASP   A H    1 
ATOM   2172 H HA   A ASP   A 1 105 ? 23.416 -7.847  -14.303 0.84 31.65 ?  105 ASP   A HA   1 
ATOM   2173 H HA   B ASP   A 1 105 ? 23.856 -8.193  -14.330 0.16 30.39 ?  105 ASP   A HA   1 
ATOM   2174 H HB2  A ASP   A 1 105 ? 25.649 -8.417  -14.746 0.84 35.80 ?  105 ASP   A HB2  1 
ATOM   2175 H HB2  B ASP   A 1 105 ? 26.237 -8.628  -14.318 0.16 31.53 ?  105 ASP   A HB2  1 
ATOM   2176 H HB3  A ASP   A 1 105 ? 25.877 -8.705  -13.200 0.84 35.80 ?  105 ASP   A HB3  1 
ATOM   2177 H HB3  B ASP   A 1 105 ? 26.079 -8.986  -12.786 0.16 31.53 ?  105 ASP   A HB3  1 
ATOM   2178 N N    A ILE   A 1 106 ? 22.094 -8.600  -12.387 0.84 23.90 ?  106 ILE   A N    1 
ATOM   2179 N N    B ILE   A 1 106 ? 22.335 -8.724  -12.498 0.16 24.84 ?  106 ILE   A N    1 
ATOM   2180 C CA   A ILE   A 1 106 ? 21.341 -9.016  -11.210 0.84 23.26 ?  106 ILE   A CA   1 
ATOM   2181 C CA   B ILE   A 1 106 ? 21.478 -9.034  -11.360 0.16 24.76 ?  106 ILE   A CA   1 
ATOM   2182 C C    A ILE   A 1 106 ? 21.881 -10.308 -10.622 0.84 22.64 ?  106 ILE   A C    1 
ATOM   2183 C C    B ILE   A 1 106 ? 21.889 -10.331 -10.678 0.16 24.43 ?  106 ILE   A C    1 
ATOM   2184 O O    A ILE   A 1 106 ? 21.681 -10.568 -9.432  0.84 22.16 ?  106 ILE   A O    1 
ATOM   2185 O O    B ILE   A 1 106 ? 21.568 -10.535 -9.501  0.16 24.31 ?  106 ILE   A O    1 
ATOM   2186 C CB   A ILE   A 1 106 ? 19.831 -9.111  -11.529 0.84 24.76 ?  106 ILE   A CB   1 
ATOM   2187 C CB   B ILE   A 1 106 ? 19.989 -9.040  -11.763 0.16 25.12 ?  106 ILE   A CB   1 
ATOM   2188 C CG1  A ILE   A 1 106 ? 19.005 -9.230  -10.243 0.84 25.07 ?  106 ILE   A CG1  1 
ATOM   2189 C CG1  B ILE   A 1 106 ? 19.095 -8.908  -10.526 0.16 25.28 ?  106 ILE   A CG1  1 
ATOM   2190 C CG2  A ILE   A 1 106 ? 19.543 -10.292 -12.445 0.84 25.65 ?  106 ILE   A CG2  1 
ATOM   2191 C CG2  B ILE   A 1 106 ? 19.638 -10.316 -12.505 0.16 25.24 ?  106 ILE   A CG2  1 
ATOM   2192 C CD1  A ILE   A 1 106 ? 19.102 -8.021  -9.336  0.84 25.10 ?  106 ILE   A CD1  1 
ATOM   2193 C CD1  B ILE   A 1 106 ? 19.427 -7.718  -9.652  0.16 25.36 ?  106 ILE   A CD1  1 
ATOM   2194 H H    A ILE   A 1 106 ? 21.641 -8.591  -13.113 0.84 28.67 ?  106 ILE   A H    1 
ATOM   2195 H H    B ILE   A 1 106 ? 21.950 -8.782  -13.264 0.16 29.80 ?  106 ILE   A H    1 
ATOM   2196 H HA   A ILE   A 1 106 ? 21.451 -8.344  -10.532 0.84 27.92 ?  106 ILE   A HA   1 
ATOM   2197 H HA   B ILE   A 1 106 ? 21.607 -8.330  -10.715 0.16 29.71 ?  106 ILE   A HA   1 
ATOM   2198 H HB   A ILE   A 1 106 ? 19.566 -8.299  -11.987 0.84 29.71 ?  106 ILE   A HB   1 
ATOM   2199 H HB   B ILE   A 1 106 ? 19.819 -8.285  -12.348 0.16 30.14 ?  106 ILE   A HB   1 
ATOM   2200 H HG12 A ILE   A 1 106 ? 18.071 -9.343  -10.480 0.84 30.08 ?  106 ILE   A HG12 1 
ATOM   2201 H HG12 B ILE   A 1 106 ? 18.173 -8.813  -10.815 0.16 30.33 ?  106 ILE   A HG12 1 
ATOM   2202 H HG13 A ILE   A 1 106 ? 19.309 -10.002 -9.741  0.84 30.08 ?  106 ILE   A HG13 1 
ATOM   2203 H HG13 B ILE   A 1 106 ? 19.188 -9.708  -9.987  0.16 30.33 ?  106 ILE   A HG13 1 
ATOM   2204 H HG21 A ILE   A 1 106 ? 18.634 -10.218 -12.776 0.84 30.78 ?  106 ILE   A HG21 1 
ATOM   2205 H HG21 B ILE   A 1 106 ? 18.786 -10.195 -12.954 0.16 30.29 ?  106 ILE   A HG21 1 
ATOM   2206 H HG22 A ILE   A 1 106 ? 20.168 -10.271 -13.187 0.84 30.78 ?  106 ILE   A HG22 1 
ATOM   2207 H HG22 B ILE   A 1 106 ? 20.332 -10.501 -13.155 0.16 30.29 ?  106 ILE   A HG22 1 
ATOM   2208 H HG23 A ILE   A 1 106 ? 19.648 -11.115 -11.945 0.84 30.78 ?  106 ILE   A HG23 1 
ATOM   2209 H HG23 B ILE   A 1 106 ? 19.575 -11.046 -11.869 0.16 30.29 ?  106 ILE   A HG23 1 
ATOM   2210 H HD11 A ILE   A 1 106 ? 18.395 -8.065  -8.675  0.84 30.12 ?  106 ILE   A HD11 1 
ATOM   2211 H HD11 B ILE   A 1 106 ? 18.650 -7.487  -9.127  0.16 30.43 ?  106 ILE   A HD11 1 
ATOM   2212 H HD12 A ILE   A 1 106 ? 19.967 -8.025  -8.894  0.84 30.12 ?  106 ILE   A HD12 1 
ATOM   2213 H HD12 B ILE   A 1 106 ? 20.166 -7.953  -9.067  0.16 30.43 ?  106 ILE   A HD12 1 
ATOM   2214 H HD13 A ILE   A 1 106 ? 19.007 -7.217  -9.870  0.84 30.12 ?  106 ILE   A HD13 1 
ATOM   2215 H HD13 B ILE   A 1 106 ? 19.678 -6.972  -10.220 0.16 30.43 ?  106 ILE   A HD13 1 
ATOM   2216 N N    A GLN   A 1 107 ? 22.571 -11.126 -11.428 0.84 23.21 ?  107 GLN   A N    1 
ATOM   2217 N N    B GLN   A 1 107 ? 22.599 -11.215 -11.382 0.16 24.31 ?  107 GLN   A N    1 
ATOM   2218 C CA   A GLN   A 1 107 ? 23.214 -12.328 -10.910 0.84 25.33 ?  107 GLN   A CA   1 
ATOM   2219 C CA   B GLN   A 1 107 ? 23.101 -12.430 -10.751 0.16 24.37 ?  107 GLN   A CA   1 
ATOM   2220 C C    A GLN   A 1 107 ? 24.198 -12.003 -9.797  0.84 22.55 ?  107 GLN   A C    1 
ATOM   2221 C C    B GLN   A 1 107 ? 24.100 -12.111 -9.649  0.16 21.87 ?  107 GLN   A C    1 
ATOM   2222 O O    A GLN   A 1 107 ? 24.459 -12.856 -8.943  0.84 24.01 ?  107 GLN   A O    1 
ATOM   2223 O O    B GLN   A 1 107 ? 24.270 -12.913 -8.724  0.16 21.90 ?  107 GLN   A O    1 
ATOM   2224 C CB   A GLN   A 1 107 ? 23.928 -13.073 -12.047 0.84 29.62 ?  107 GLN   A CB   1 
ATOM   2225 C CB   B GLN   A 1 107 ? 23.754 -13.340 -11.794 0.16 26.87 ?  107 GLN   A CB   1 
ATOM   2226 C CG   A GLN   A 1 107 ? 23.046 -13.346 -13.262 0.84 34.19 ?  107 GLN   A CG   1 
ATOM   2227 C CG   B GLN   A 1 107 ? 23.004 -13.416 -13.119 0.16 29.27 ?  107 GLN   A CG   1 
ATOM   2228 C CD   A GLN   A 1 107 ? 21.803 -14.138 -12.915 0.84 38.10 ?  107 GLN   A CD   1 
ATOM   2229 C CD   B GLN   A 1 107 ? 21.590 -13.939 -12.970 0.16 31.23 ?  107 GLN   A CD   1 
ATOM   2230 O OE1  A GLN   A 1 107 ? 21.880 -15.190 -12.279 0.84 39.66 ?  107 GLN   A OE1  1 
ATOM   2231 O OE1  B GLN   A 1 107 ? 21.330 -14.851 -12.185 0.16 31.93 ?  107 GLN   A OE1  1 
ATOM   2232 N NE2  A GLN   A 1 107 ? 20.646 -13.632 -13.326 0.84 39.61 ?  107 GLN   A NE2  1 
ATOM   2233 N NE2  B GLN   A 1 107 ? 20.664 -13.361 -13.727 0.16 31.99 ?  107 GLN   A NE2  1 
ATOM   2234 H H    A GLN   A 1 107 ? 22.681 -11.005 -12.270 0.84 27.84 ?  107 GLN   A H    1 
ATOM   2235 H H    B GLN   A 1 107 ? 22.807 -11.124 -12.209 0.16 29.17 ?  107 GLN   A H    1 
ATOM   2236 H HA   A GLN   A 1 107 ? 22.547 -12.925 -10.545 0.84 30.39 ?  107 GLN   A HA   1 
ATOM   2237 H HA   B GLN   A 1 107 ? 22.360 -12.914 -10.356 0.16 29.24 ?  107 GLN   A HA   1 
ATOM   2238 H HB2  A GLN   A 1 107 ? 24.684 -12.544 -12.348 0.84 35.55 ?  107 GLN   A HB2  1 
ATOM   2239 H HB2  B GLN   A 1 107 ? 24.648 -13.014 -11.978 0.16 32.24 ?  107 GLN   A HB2  1 
ATOM   2240 H HB3  A GLN   A 1 107 ? 24.242 -13.932 -11.719 0.84 35.55 ?  107 GLN   A HB3  1 
ATOM   2241 H HB3  B GLN   A 1 107 ? 23.803 -14.242 -11.435 0.16 32.24 ?  107 GLN   A HB3  1 
ATOM   2242 H HG2  A GLN   A 1 107 ? 22.764 -12.503 -13.650 0.84 41.03 ?  107 GLN   A HG2  1 
ATOM   2243 H HG2  B GLN   A 1 107 ? 22.959 -12.535 -13.521 0.16 35.12 ?  107 GLN   A HG2  1 
ATOM   2244 H HG3  A GLN   A 1 107 ? 23.555 -13.853 -13.914 0.84 41.03 ?  107 GLN   A HG3  1 
ATOM   2245 H HG3  B GLN   A 1 107 ? 23.481 -14.016 -13.708 0.16 35.12 ?  107 GLN   A HG3  1 
ATOM   2246 H HE21 A GLN   A 1 107 ? 20.630 -12.894 -13.768 0.84 47.53 ?  107 GLN   A HE21 1 
ATOM   2247 H HE21 B GLN   A 1 107 ? 20.883 -12.725 -14.263 0.16 38.39 ?  107 GLN   A HE21 1 
ATOM   2248 H HE22 A GLN   A 1 107 ? 19.912 -14.045 -13.153 0.84 47.53 ?  107 GLN   A HE22 1 
ATOM   2249 H HE22 B GLN   A 1 107 ? 19.847 -13.624 -13.681 0.16 38.39 ?  107 GLN   A HE22 1 
ATOM   2250 N N    A LEU   A 1 108 ? 24.723 -10.776 -9.764  0.84 18.33 ?  108 LEU   A N    1 
ATOM   2251 N N    B LEU   A 1 108 ? 24.756 -10.950 -9.725  0.16 19.46 ?  108 LEU   A N    1 
ATOM   2252 C CA   A LEU   A 1 108 ? 25.649 -10.385 -8.710  0.84 15.60 ?  108 LEU   A CA   1 
ATOM   2253 C CA   B LEU   A 1 108 ? 25.670 -10.523 -8.674  0.16 17.06 ?  108 LEU   A CA   1 
ATOM   2254 C C    A LEU   A 1 108 ? 24.963 -10.237 -7.361  0.84 13.59 ?  108 LEU   A C    1 
ATOM   2255 C C    B LEU   A 1 108 ? 24.967 -10.281 -7.346  0.16 15.06 ?  108 LEU   A C    1 
ATOM   2256 O O    A LEU   A 1 108 ? 25.649 -10.086 -6.348  0.84 14.15 ?  108 LEU   A O    1 
ATOM   2257 O O    B LEU   A 1 108 ? 25.648 -10.078 -6.335  0.16 15.04 ?  108 LEU   A O    1 
ATOM   2258 C CB   A LEU   A 1 108 ? 26.366 -9.086  -9.096  0.84 15.50 ?  108 LEU   A CB   1 
ATOM   2259 C CB   B LEU   A 1 108 ? 26.421 -9.258  -9.104  0.16 16.89 ?  108 LEU   A CB   1 
ATOM   2260 C CG   A LEU   A 1 108 ? 27.398 -9.282  -10.208 0.84 16.81 ?  108 LEU   A CG   1 
ATOM   2261 C CG   B LEU   A 1 108 ? 27.357 -9.406  -10.305 0.16 16.91 ?  108 LEU   A CG   1 
ATOM   2262 C CD1  A LEU   A 1 108 ? 27.858 -7.952  -10.780 0.84 17.71 ?  108 LEU   A CD1  1 
ATOM   2263 C CD1  B LEU   A 1 108 ? 28.048 -8.082  -10.614 0.16 17.05 ?  108 LEU   A CD1  1 
ATOM   2264 C CD2  A LEU   A 1 108 ? 28.592 -10.075 -9.693  0.84 18.38 ?  108 LEU   A CD2  1 
ATOM   2265 C CD2  B LEU   A 1 108 ? 28.381 -10.503 -10.071 0.16 16.91 ?  108 LEU   A CD2  1 
ATOM   2266 H H    A LEU   A 1 108 ? 24.550 -10.161 -10.332 0.84 22.00 ?  108 LEU   A H    1 
ATOM   2267 H H    B LEU   A 1 108 ? 24.689 -10.399 -10.380 0.16 23.35 ?  108 LEU   A H    1 
ATOM   2268 H HA   A LEU   A 1 108 ? 26.320 -11.077 -8.614  0.84 18.72 ?  108 LEU   A HA   1 
ATOM   2269 H HA   B LEU   A 1 108 ? 26.322 -11.222 -8.528  0.16 20.47 ?  108 LEU   A HA   1 
ATOM   2270 H HB2  A LEU   A 1 108 ? 25.707 -8.446  -9.410  0.84 18.60 ?  108 LEU   A HB2  1 
ATOM   2271 H HB2  B LEU   A 1 108 ? 25.769 -8.576  -9.328  0.16 20.26 ?  108 LEU   A HB2  1 
ATOM   2272 H HB3  A LEU   A 1 108 ? 26.823 -8.736  -8.318  0.84 18.60 ?  108 LEU   A HB3  1 
ATOM   2273 H HB3  B LEU   A 1 108 ? 26.961 -8.956  -8.359  0.16 20.26 ?  108 LEU   A HB3  1 
ATOM   2274 H HG   A LEU   A 1 108 ? 26.993 -9.793  -10.927 0.84 20.18 ?  108 LEU   A HG   1 
ATOM   2275 H HG   B LEU   A 1 108 ? 26.832 -9.663  -11.075 0.16 20.28 ?  108 LEU   A HG   1 
ATOM   2276 H HD11 A LEU   A 1 108 ? 28.479 -8.118  -11.510 0.84 21.26 ?  108 LEU   A HD11 1 
ATOM   2277 H HD11 B LEU   A 1 108 ? 28.630 -8.199  -11.382 0.16 20.46 ?  108 LEU   A HD11 1 
ATOM   2278 H HD12 A LEU   A 1 108 ? 27.088 -7.464  -11.107 0.84 21.26 ?  108 LEU   A HD12 1 
ATOM   2279 H HD12 B LEU   A 1 108 ? 27.376 -7.409  -10.809 0.16 20.46 ?  108 LEU   A HD12 1 
ATOM   2280 H HD13 A LEU   A 1 108 ? 28.302 -7.443  -10.082 0.84 21.26 ?  108 LEU   A HD13 1 
ATOM   2281 H HD13 B LEU   A 1 108 ? 28.571 -7.812  -9.843  0.16 20.46 ?  108 LEU   A HD13 1 
ATOM   2282 H HD21 A LEU   A 1 108 ? 29.309 -10.021 -10.341 0.84 22.05 ?  108 LEU   A HD21 1 
ATOM   2283 H HD21 B LEU   A 1 108 ? 29.062 -10.452 -10.758 0.16 20.29 ?  108 LEU   A HD21 1 
ATOM   2284 H HD22 A LEU   A 1 108 ? 28.878 -9.699  -8.846  0.84 22.05 ?  108 LEU   A HD22 1 
ATOM   2285 H HD22 B LEU   A 1 108 ? 28.780 -10.375 -9.197  0.16 20.29 ?  108 LEU   A HD22 1 
ATOM   2286 H HD23 A LEU   A 1 108 ? 28.327 -11.002 -9.569  0.84 22.05 ?  108 LEU   A HD23 1 
ATOM   2287 H HD23 B LEU   A 1 108 ? 27.933 -11.362 -10.109 0.16 20.29 ?  108 LEU   A HD23 1 
ATOM   2288 N N    . LEU   A 1 109 ? 23.632 -10.300 -7.315  1.00 13.56 ?  109 LEU   A N    1 
ATOM   2289 C CA   . LEU   A 1 109 ? 22.938 -10.169 -6.043  1.00 12.49 ?  109 LEU   A CA   1 
ATOM   2290 C C    . LEU   A 1 109 ? 23.288 -11.320 -5.106  1.00 12.20 ?  109 LEU   A C    1 
ATOM   2291 O O    . LEU   A 1 109 ? 23.430 -11.121 -3.897  1.00 12.65 ?  109 LEU   A O    1 
ATOM   2292 C CB   . LEU   A 1 109 ? 21.435 -10.094 -6.292  1.00 13.54 ?  109 LEU   A CB   1 
ATOM   2293 C CG   . LEU   A 1 109 ? 20.552 -9.800  -5.085  1.00 13.72 ?  109 LEU   A CG   1 
ATOM   2294 C CD1  . LEU   A 1 109 ? 20.998 -8.527  -4.388  1.00 14.28 ?  109 LEU   A CD1  1 
ATOM   2295 C CD2  . LEU   A 1 109 ? 19.097 -9.690  -5.510  1.00 15.02 ?  109 LEU   A CD2  1 
ATOM   2296 H H    A LEU   A 1 109 ? 23.118 -10.425 -7.992  0.84 16.27 ?  109 LEU   A H    1 
ATOM   2297 H H    B LEU   A 1 109 ? 23.119 -10.395 -7.998  0.16 16.27 ?  109 LEU   A H    1 
ATOM   2298 H HA   . LEU   A 1 109 ? 23.220 -9.345  -5.619  1.00 14.99 ?  109 LEU   A HA   1 
ATOM   2299 H HB2  . LEU   A 1 109 ? 21.275 -9.391  -6.941  1.00 16.25 ?  109 LEU   A HB2  1 
ATOM   2300 H HB3  . LEU   A 1 109 ? 21.146 -10.942 -6.658  1.00 16.25 ?  109 LEU   A HB3  1 
ATOM   2301 H HG   . LEU   A 1 109 ? 20.625 -10.530 -4.453  1.00 16.46 ?  109 LEU   A HG   1 
ATOM   2302 H HD11 . LEU   A 1 109 ? 20.312 -8.242  -3.770  1.00 17.14 ?  109 LEU   A HD11 1 
ATOM   2303 H HD12 . LEU   A 1 109 ? 21.826 -8.702  -3.910  1.00 17.14 ?  109 LEU   A HD12 1 
ATOM   2304 H HD13 . LEU   A 1 109 ? 21.148 -7.839  -5.058  1.00 17.14 ?  109 LEU   A HD13 1 
ATOM   2305 H HD21 . LEU   A 1 109 ? 18.565 -9.399  -4.751  1.00 18.02 ?  109 LEU   A HD21 1 
ATOM   2306 H HD22 . LEU   A 1 109 ? 19.022 -9.044  -6.230  1.00 18.02 ?  109 LEU   A HD22 1 
ATOM   2307 H HD23 . LEU   A 1 109 ? 18.787 -10.559 -5.814  1.00 18.02 ?  109 LEU   A HD23 1 
ATOM   2308 N N    . LYS   A 1 110 ? 23.435 -12.535 -5.640  1.00 11.96 ?  110 LYS   A N    1 
ATOM   2309 C CA   . LYS   A 1 110 ? 23.818 -13.660 -4.788  1.00 11.75 ?  110 LYS   A CA   1 
ATOM   2310 C C    . LYS   A 1 110 ? 25.200 -13.439 -4.183  1.00 11.64 ?  110 LYS   A C    1 
ATOM   2311 O O    . LYS   A 1 110 ? 25.398 -13.638 -2.982  1.00 11.73 ?  110 LYS   A O    1 
ATOM   2312 C CB   . LYS   A 1 110 ? 23.738 -14.983 -5.552  1.00 12.65 ?  110 LYS   A CB   1 
ATOM   2313 C CG   . LYS   A 1 110 ? 23.933 -16.199 -4.642  1.00 13.11 ?  110 LYS   A CG   1 
ATOM   2314 C CD   . LYS   A 1 110 ? 23.711 -17.513 -5.362  1.00 13.45 ?  110 LYS   A CD   1 
ATOM   2315 C CE   . LYS   A 1 110 ? 23.821 -18.693 -4.413  1.00 14.56 ?  110 LYS   A CE   1 
ATOM   2316 N NZ   . LYS   A 1 110 ? 22.632 -18.832 -3.526  1.00 15.29 ?  110 LYS   A NZ   1 
ATOM   2317 H H    . LYS   A 1 110 ? 23.312 -12.736 -6.466  1.00 14.35 ?  110 LYS   A H    1 
ATOM   2318 H HA   . LYS   A 1 110 ? 23.184 -13.717 -4.050  1.00 14.09 ?  110 LYS   A HA   1 
ATOM   2319 H HB2  . LYS   A 1 110 ? 22.864 -15.058 -5.968  1.00 15.18 ?  110 LYS   A HB2  1 
ATOM   2320 H HB3  . LYS   A 1 110 ? 24.432 -15.001 -6.226  1.00 15.18 ?  110 LYS   A HB3  1 
ATOM   2321 H HG2  . LYS   A 1 110 ? 24.836 -16.195 -4.292  1.00 15.73 ?  110 LYS   A HG2  1 
ATOM   2322 H HG3  . LYS   A 1 110 ? 23.295 -16.149 -3.907  1.00 15.73 ?  110 LYS   A HG3  1 
ATOM   2323 H HD2  . LYS   A 1 110 ? 22.825 -17.517 -5.752  1.00 16.13 ?  110 LYS   A HD2  1 
ATOM   2324 H HD3  . LYS   A 1 110 ? 24.385 -17.612 -6.051  1.00 16.13 ?  110 LYS   A HD3  1 
ATOM   2325 H HE2  . LYS   A 1 110 ? 23.910 -19.508 -4.928  1.00 17.47 ?  110 LYS   A HE2  1 
ATOM   2326 H HE3  . LYS   A 1 110 ? 24.601 -18.572 -3.844  1.00 17.47 ?  110 LYS   A HE3  1 
ATOM   2327 H HZ1  . LYS   A 1 110 ? 22.728 -19.531 -2.988  1.00 18.34 ?  110 LYS   A HZ1  1 
ATOM   2328 H HZ2  . LYS   A 1 110 ? 22.526 -18.097 -3.035  1.00 18.34 ?  110 LYS   A HZ2  1 
ATOM   2329 H HZ3  . LYS   A 1 110 ? 21.897 -18.950 -4.022  1.00 18.34 ?  110 LYS   A HZ3  1 
ATOM   2330 N N    . SER   A 1 111 ? 26.162 -12.996 -4.999  1.00 11.44 ?  111 SER   A N    1 
ATOM   2331 C CA   . SER   A 1 111 ? 27.493 -12.694 -4.479  1.00 11.68 ?  111 SER   A CA   1 
ATOM   2332 C C    . SER   A 1 111 ? 27.424 -11.644 -3.371  1.00 11.23 ?  111 SER   A C    1 
ATOM   2333 O O    . SER   A 1 111 ? 28.124 -11.747 -2.357  1.00 11.86 ?  111 SER   A O    1 
ATOM   2334 C CB   . SER   A 1 111 ? 28.392 -12.204 -5.617  1.00 13.23 ?  111 SER   A CB   1 
ATOM   2335 O OG   . SER   A 1 111 ? 28.489 -13.188 -6.636  1.00 15.15 ?  111 SER   A OG   1 
ATOM   2336 H H    . SER   A 1 111 ? 26.064 -12.863 -5.841  1.00 13.72 ?  111 SER   A H    1 
ATOM   2337 H HA   . SER   A 1 111 ? 27.883 -13.501 -4.110  1.00 14.01 ?  111 SER   A HA   1 
ATOM   2338 H HB2  . SER   A 1 111 ? 28.007 -11.404 -6.002  1.00 15.88 ?  111 SER   A HB2  1 
ATOM   2339 H HB3  . SER   A 1 111 ? 29.274 -12.012 -5.259  1.00 15.88 ?  111 SER   A HB3  1 
ATOM   2340 H HG   . SER   A 1 111 ? 29.008 -12.914 -7.246  1.00 18.18 ?  111 SER   A HG   1 
ATOM   2341 N N    . ALA   A 1 112 ? 26.576 -10.628 -3.547  1.00 11.64 ?  112 ALA   A N    1 
ATOM   2342 C CA   . ALA   A 1 112 ? 26.432 -9.589  -2.530  1.00 11.39 ?  112 ALA   A CA   1 
ATOM   2343 C C    . ALA   A 1 112 ? 25.955 -10.187 -1.210  1.00 11.40 ?  112 ALA   A C    1 
ATOM   2344 O O    . ALA   A 1 112 ? 26.503 -9.891  -0.141  1.00 11.43 ?  112 ALA   A O    1 
ATOM   2345 C CB   . ALA   A 1 112 ? 25.475 -8.501  -3.024  1.00 11.89 ?  112 ALA   A CB   1 
ATOM   2346 H H    . ALA   A 1 112 ? 26.080 -10.514 -4.238  1.00 13.96 ?  112 ALA   A H    1 
ATOM   2347 H HA   . ALA   A 1 112 ? 27.294 -9.170  -2.373  1.00 13.67 ?  112 ALA   A HA   1 
ATOM   2348 H HB1  . ALA   A 1 112 ? 25.400 -7.808  -2.342  1.00 14.26 ?  112 ALA   A HB1  1 
ATOM   2349 H HB2  . ALA   A 1 112 ? 25.822 -8.117  -3.842  1.00 14.26 ?  112 ALA   A HB2  1 
ATOM   2350 H HB3  . ALA   A 1 112 ? 24.602 -8.894  -3.185  1.00 14.26 ?  112 ALA   A HB3  1 
ATOM   2351 N N    . TYR   A 1 113 ? 24.917 -11.030 -1.260  1.00 11.33 ?  113 TYR   A N    1 
ATOM   2352 C CA   . TYR   A 1 113 ? 24.412 -11.641 -0.034  1.00 11.36 ?  113 TYR   A CA   1 
ATOM   2353 C C    . TYR   A 1 113 ? 25.419 -12.595 0.609   1.00 10.87 ?  113 TYR   A C    1 
ATOM   2354 O O    . TYR   A 1 113 ? 25.380 -12.783 1.828   1.00 11.21 ?  113 TYR   A O    1 
ATOM   2355 C CB   . TYR   A 1 113 ? 23.098 -12.375 -0.305  1.00 11.55 ?  113 TYR   A CB   1 
ATOM   2356 C CG   . TYR   A 1 113 ? 21.881 -11.484 -0.214  1.00 11.60 ?  113 TYR   A CG   1 
ATOM   2357 C CD1  . TYR   A 1 113 ? 21.508 -10.908 0.996   1.00 11.73 ?  113 TYR   A CD1  1 
ATOM   2358 C CD2  . TYR   A 1 113 ? 21.075 -11.251 -1.322  1.00 11.81 ?  113 TYR   A CD2  1 
ATOM   2359 C CE1  . TYR   A 1 113 ? 20.381 -10.116 1.098   1.00 12.29 ?  113 TYR   A CE1  1 
ATOM   2360 C CE2  . TYR   A 1 113 ? 19.921 -10.456 -1.224  1.00 12.21 ?  113 TYR   A CE2  1 
ATOM   2361 C CZ   . TYR   A 1 113 ? 19.591 -9.894  -0.013  1.00 12.03 ?  113 TYR   A CZ   1 
ATOM   2362 O OH   . TYR   A 1 113 ? 18.467 -9.101  0.120   1.00 12.71 ?  113 TYR   A OH   1 
ATOM   2363 H H    . TYR   A 1 113 ? 24.504 -11.261 -1.978  1.00 13.60 ?  113 TYR   A H    1 
ATOM   2364 H HA   . TYR   A 1 113 ? 24.235 -10.938 0.607   1.00 13.63 ?  113 TYR   A HA   1 
ATOM   2365 H HB2  . TYR   A 1 113 ? 23.123 -12.744 -1.198  1.00 13.85 ?  113 TYR   A HB2  1 
ATOM   2366 H HB3  . TYR   A 1 113 ? 22.996 -13.083 0.347   1.00 13.85 ?  113 TYR   A HB3  1 
ATOM   2367 H HD1  . TYR   A 1 113 ? 22.034 -11.055 1.752   1.00 14.08 ?  113 TYR   A HD1  1 
ATOM   2368 H HD2  . TYR   A 1 113 ? 21.295 -11.640 -2.135  1.00 14.17 ?  113 TYR   A HD2  1 
ATOM   2369 H HE1  . TYR   A 1 113 ? 20.155 -9.734  1.914   1.00 14.74 ?  113 TYR   A HE1  1 
ATOM   2370 H HE2  . TYR   A 1 113 ? 19.388 -10.300 -1.971  1.00 14.65 ?  113 TYR   A HE2  1 
ATOM   2371 H HH   . TYR   A 1 113 ? 18.075 -9.046  -0.628  1.00 15.25 ?  113 TYR   A HH   1 
ATOM   2372 N N    . GLU   A 1 114 ? 26.318 -13.211 -0.174  1.00 11.09 ?  114 GLU   A N    1 
ATOM   2373 C CA   . GLU   A 1 114 ? 27.315 -14.107 0.424   1.00 11.31 ?  114 GLU   A CA   1 
ATOM   2374 C C    . GLU   A 1 114 ? 28.165 -13.391 1.474   1.00 11.03 ?  114 GLU   A C    1 
ATOM   2375 O O    . GLU   A 1 114 ? 28.640 -14.023 2.428   1.00 11.34 ?  114 GLU   A O    1 
ATOM   2376 C CB   . GLU   A 1 114 ? 28.187 -14.747 -0.667  1.00 11.24 ?  114 GLU   A CB   1 
ATOM   2377 C CG   . GLU   A 1 114 ? 27.428 -15.804 -1.450  1.00 11.71 ?  114 GLU   A CG   1 
ATOM   2378 C CD   . GLU   A 1 114 ? 28.130 -16.325 -2.694  1.00 12.26 ?  114 GLU   A CD   1 
ATOM   2379 O OE1  . GLU   A 1 114 ? 29.090 -15.696 -3.186  1.00 12.54 ?  114 GLU   A OE1  1 
ATOM   2380 O OE2  . GLU   A 1 114 ? 27.683 -17.386 -3.190  1.00 13.28 -1 114 GLU   A OE2  1 
ATOM   2381 H H    . GLU   A 1 114 ? 26.370 -13.125 -1.036  1.00 13.31 ?  114 GLU   A H    1 
ATOM   2382 H HA   . GLU   A 1 114 ? 26.846 -14.824 0.866   1.00 13.57 ?  114 GLU   A HA   1 
ATOM   2383 H HB2  . GLU   A 1 114 ? 28.479 -14.061 -1.294  1.00 13.49 ?  114 GLU   A HB2  1 
ATOM   2384 H HB3  . GLU   A 1 114 ? 28.957 -15.168 -0.256  1.00 13.49 ?  114 GLU   A HB3  1 
ATOM   2385 H HG2  . GLU   A 1 114 ? 27.274 -16.566 -0.870  1.00 14.05 ?  114 GLU   A HG2  1 
ATOM   2386 H HG3  . GLU   A 1 114 ? 26.577 -15.434 -1.731  1.00 14.05 ?  114 GLU   A HG3  1 
ATOM   2387 N N    . ASN   A 1 115 ? 28.346 -12.073 1.343   1.00 10.83 ?  115 ASN   A N    1 
ATOM   2388 C CA   . ASN   A 1 115 ? 29.107 -11.341 2.351   1.00 11.22 ?  115 ASN   A CA   1 
ATOM   2389 C C    . ASN   A 1 115 ? 28.490 -11.475 3.738   1.00 10.88 ?  115 ASN   A C    1 
ATOM   2390 O O    . ASN   A 1 115 ? 29.201 -11.410 4.745   1.00 11.42 ?  115 ASN   A O    1 
ATOM   2391 C CB   . ASN   A 1 115 ? 29.211 -9.862  1.976   1.00 11.19 ?  115 ASN   A CB   1 
ATOM   2392 C CG   . ASN   A 1 115 ? 30.005 -9.632  0.714   1.00 12.32 ?  115 ASN   A CG   1 
ATOM   2393 O OD1  . ASN   A 1 115 ? 31.225 -9.702  0.729   1.00 15.59 ?  115 ASN   A OD1  1 
ATOM   2394 N ND2  . ASN   A 1 115 ? 29.323 -9.342  -0.379  1.00 11.88 ?  115 ASN   A ND2  1 
ATOM   2395 H H    . ASN   A 1 115 ? 28.046 -11.590 0.695   1.00 12.99 ?  115 ASN   A H    1 
ATOM   2396 H HA   . ASN   A 1 115 ? 30.004 -11.699 2.390   1.00 13.46 ?  115 ASN   A HA   1 
ATOM   2397 H HB2  . ASN   A 1 115 ? 28.317 -9.507  1.847   1.00 13.43 ?  115 ASN   A HB2  1 
ATOM   2398 H HB3  . ASN   A 1 115 ? 29.651 -9.388  2.701   1.00 13.43 ?  115 ASN   A HB3  1 
ATOM   2399 H HD21 . ASN   A 1 115 ? 29.735 -9.198  -1.120  1.00 14.26 ?  115 ASN   A HD21 1 
ATOM   2400 H HD22 . ASN   A 1 115 ? 28.462 -9.312  -0.355  1.00 14.26 ?  115 ASN   A HD22 1 
ATOM   2401 N N    . PHE   A 1 116 ? 27.166 -11.647 3.816   1.00 11.13 ?  116 PHE   A N    1 
ATOM   2402 C CA   . PHE   A 1 116 ? 26.515 -11.749 5.118   1.00 11.12 ?  116 PHE   A CA   1 
ATOM   2403 C C    . PHE   A 1 116 ? 26.992 -12.983 5.887   1.00 11.44 ?  116 PHE   A C    1 
ATOM   2404 O O    . PHE   A 1 116 ? 26.920 -13.002 7.115   1.00 11.90 ?  116 PHE   A O    1 
ATOM   2405 C CB   . PHE   A 1 116 ? 24.985 -11.880 4.979   1.00 11.30 ?  116 PHE   A CB   1 
ATOM   2406 C CG   . PHE   A 1 116 ? 24.226 -10.631 4.523   1.00 11.12 ?  116 PHE   A CG   1 
ATOM   2407 C CD1  . PHE   A 1 116 ? 24.795 -9.602  3.781   1.00 10.90 ?  116 PHE   A CD1  1 
ATOM   2408 C CD2  . PHE   A 1 116 ? 22.872 -10.535 4.837   1.00 11.78 ?  116 PHE   A CD2  1 
ATOM   2409 C CE1  . PHE   A 1 116 ? 24.023 -8.525  3.370   1.00 11.30 ?  116 PHE   A CE1  1 
ATOM   2410 C CE2  . PHE   A 1 116 ? 22.109 -9.460  4.440   1.00 11.84 ?  116 PHE   A CE2  1 
ATOM   2411 C CZ   . PHE   A 1 116 ? 22.675 -8.454  3.706   1.00 11.28 ?  116 PHE   A CZ   1 
ATOM   2412 H H    . PHE   A 1 116 ? 26.633 -11.699 3.141   1.00 13.35 ?  116 PHE   A H    1 
ATOM   2413 H HA   . PHE   A 1 116 ? 26.708 -10.959 5.644   1.00 13.34 ?  116 PHE   A HA   1 
ATOM   2414 H HB2  . PHE   A 1 116 ? 24.801 -12.582 4.331   1.00 13.56 ?  116 PHE   A HB2  1 
ATOM   2415 H HB3  . PHE   A 1 116 ? 24.625 -12.141 5.841   1.00 13.56 ?  116 PHE   A HB3  1 
ATOM   2416 H HD1  . PHE   A 1 116 ? 25.691 -9.655  3.544   1.00 13.07 ?  116 PHE   A HD1  1 
ATOM   2417 H HD2  . PHE   A 1 116 ? 22.474 -11.224 5.329   1.00 14.14 ?  116 PHE   A HD2  1 
ATOM   2418 H HE1  . PHE   A 1 116 ? 24.414 -7.842  2.877   1.00 13.56 ?  116 PHE   A HE1  1 
ATOM   2419 H HE2  . PHE   A 1 116 ? 21.207 -9.428  4.670   1.00 14.20 ?  116 PHE   A HE2  1 
ATOM   2420 H HZ   . PHE   A 1 116 ? 22.164 -7.726  3.443   1.00 13.53 ?  116 PHE   A HZ   1 
ATOM   2421 N N    . ASN   A 1 117 ? 27.434 -14.034 5.183   1.00 11.35 ?  117 ASN   A N    1 
ATOM   2422 C CA   . ASN   A 1 117 ? 27.808 -15.281 5.847   1.00 11.82 ?  117 ASN   A CA   1 
ATOM   2423 C C    . ASN   A 1 117 ? 29.073 -15.160 6.681   1.00 12.26 ?  117 ASN   A C    1 
ATOM   2424 O O    . ASN   A 1 117 ? 29.377 -16.084 7.447   1.00 12.97 ?  117 ASN   A O    1 
ATOM   2425 C CB   . ASN   A 1 117 ? 27.922 -16.408 4.821   1.00 11.66 ?  117 ASN   A CB   1 
ATOM   2426 C CG   . ASN   A 1 117 ? 26.564 -16.789 4.278   1.00 11.61 ?  117 ASN   A CG   1 
ATOM   2427 O OD1  . ASN   A 1 117 ? 25.589 -16.820 5.026   1.00 12.51 ?  117 ASN   A OD1  1 
ATOM   2428 N ND2  . ASN   A 1 117 ? 26.483 -17.047 2.989   1.00 11.71 ?  117 ASN   A ND2  1 
ATOM   2429 H H    . ASN   A 1 117 ? 27.513 -14.049 4.324   1.00 13.62 ?  117 ASN   A H    1 
ATOM   2430 H HA   . ASN   A 1 117 ? 27.086 -15.517 6.451   1.00 14.18 ?  117 ASN   A HA   1 
ATOM   2431 H HB2  . ASN   A 1 117 ? 28.474 -16.113 4.080   1.00 13.99 ?  117 ASN   A HB2  1 
ATOM   2432 H HB3  . ASN   A 1 117 ? 28.309 -17.185 5.245   1.00 13.99 ?  117 ASN   A HB3  1 
ATOM   2433 H HD21 . ASN   A 1 117 ? 25.728 -17.265 2.643   1.00 14.04 ?  117 ASN   A HD21 1 
ATOM   2434 H HD22 . ASN   A 1 117 ? 27.188 -17.004 2.497   1.00 14.04 ?  117 ASN   A HD22 1 
ATOM   2435 N N    . GLN   A 1 118 ? 29.802 -14.053 6.559   1.00 12.15 ?  118 GLN   A N    1 
ATOM   2436 C CA   . GLN   A 1 118 ? 30.978 -13.814 7.383   1.00 12.53 ?  118 GLN   A CA   1 
ATOM   2437 C C    . GLN   A 1 118 ? 30.633 -13.248 8.754   1.00 12.68 ?  118 GLN   A C    1 
ATOM   2438 O O    . GLN   A 1 118 ? 31.548 -12.973 9.541   1.00 14.34 ?  118 GLN   A O    1 
ATOM   2439 C CB   . GLN   A 1 118 ? 31.962 -12.902 6.649   1.00 13.02 ?  118 GLN   A CB   1 
ATOM   2440 C CG   . GLN   A 1 118 ? 32.446 -13.481 5.329   1.00 12.90 ?  118 GLN   A CG   1 
ATOM   2441 C CD   . GLN   A 1 118 ? 33.273 -14.745 5.505   1.00 13.14 ?  118 GLN   A CD   1 
ATOM   2442 O OE1  . GLN   A 1 118 ? 34.137 -14.818 6.387   1.00 14.21 ?  118 GLN   A OE1  1 
ATOM   2443 N NE2  . GLN   A 1 118 ? 33.017 -15.745 4.661   1.00 13.50 ?  118 GLN   A NE2  1 
ATOM   2444 H H    . GLN   A 1 118 ? 29.626 -13.413 6.002   1.00 14.58 ?  118 GLN   A H    1 
ATOM   2445 H HA   . GLN   A 1 118 ? 31.415 -14.670 7.521   1.00 15.03 ?  118 GLN   A HA   1 
ATOM   2446 H HB2  . GLN   A 1 118 ? 31.528 -12.056 6.468   1.00 15.62 ?  118 GLN   A HB2  1 
ATOM   2447 H HB3  . GLN   A 1 118 ? 32.736 -12.766 7.215   1.00 15.62 ?  118 GLN   A HB3  1 
ATOM   2448 H HG2  . GLN   A 1 118 ? 31.674 -13.692 4.773   1.00 15.48 ?  118 GLN   A HG2  1 
ATOM   2449 H HG3  . GLN   A 1 118 ? 32.998 -12.821 4.880   1.00 15.48 ?  118 GLN   A HG3  1 
ATOM   2450 H HE21 . GLN   A 1 118 ? 32.400 -15.656 4.057   1.00 16.20 ?  118 GLN   A HE21 1 
ATOM   2451 H HE22 . GLN   A 1 118 ? 33.449 -16.481 4.718   1.00 16.20 ?  118 GLN   A HE22 1 
ATOM   2452 N N    . HIS   A 1 119 ? 29.344 -13.094 9.065   1.00 12.26 ?  119 HIS   A N    1 
ATOM   2453 C CA   . HIS   A 1 119 ? 28.896 -12.492 10.316  1.00 12.79 ?  119 HIS   A CA   1 
ATOM   2454 C C    . HIS   A 1 119 ? 27.761 -13.321 10.888  1.00 13.06 ?  119 HIS   A C    1 
ATOM   2455 O O    . HIS   A 1 119 ? 26.812 -13.651 10.172  1.00 13.54 ?  119 HIS   A O    1 
ATOM   2456 C CB   . HIS   A 1 119 ? 28.433 -11.057 10.052  1.00 13.14 ?  119 HIS   A CB   1 
ATOM   2457 C CG   . HIS   A 1 119 ? 29.514 -10.236 9.452   1.00 14.42 ?  119 HIS   A CG   1 
ATOM   2458 N ND1  . HIS   A 1 119 ? 30.480 -9.627  10.218  1.00 16.85 ?  119 HIS   A ND1  1 
ATOM   2459 C CD2  . HIS   A 1 119 ? 29.865 -10.036 8.162   1.00 15.54 ?  119 HIS   A CD2  1 
ATOM   2460 C CE1  . HIS   A 1 119 ? 31.351 -9.033  9.422   1.00 17.32 ?  119 HIS   A CE1  1 
ATOM   2461 N NE2  . HIS   A 1 119 ? 31.009 -9.276  8.170   1.00 16.94 ?  119 HIS   A NE2  1 
ATOM   2462 H H    . HIS   A 1 119 ? 28.691 -13.345 8.557   1.00 14.71 ?  119 HIS   A H    1 
ATOM   2463 H HA   . HIS   A 1 119 ? 29.631 -12.481 10.954  1.00 15.34 ?  119 HIS   A HA   1 
ATOM   2464 H HB2  . HIS   A 1 119 ? 27.684 -11.080 9.440   1.00 15.76 ?  119 HIS   A HB2  1 
ATOM   2465 H HB3  . HIS   A 1 119 ? 28.173 -10.656 10.894  1.00 15.76 ?  119 HIS   A HB3  1 
ATOM   2466 H HD2  . HIS   A 1 119 ? 29.414 -10.352 7.410   1.00 18.64 ?  119 HIS   A HD2  1 
ATOM   2467 H HE1  . HIS   A 1 119 ? 32.084 -8.531  9.695   1.00 20.78 ?  119 HIS   A HE1  1 
ATOM   2468 H HE2  . HIS   A 1 119 ? 31.418 -8.983  7.472   1.00 20.33 ?  119 HIS   A HE2  1 
ATOM   2469 N N    . GLU   A 1 120 ? 27.851 -13.642 12.179  1.00 13.86 ?  120 GLU   A N    1 
ATOM   2470 C CA   . GLU   A 1 120 ? 26.893 -14.574 12.773  1.00 15.57 ?  120 GLU   A CA   1 
ATOM   2471 C C    . GLU   A 1 120 ? 25.476 -14.008 12.834  1.00 14.31 ?  120 GLU   A C    1 
ATOM   2472 O O    . GLU   A 1 120 ? 24.501 -14.772 12.719  1.00 14.37 ?  120 GLU   A O    1 
ATOM   2473 C CB   . GLU   A 1 120 ? 27.363 -14.985 14.172  1.00 20.48 ?  120 GLU   A CB   1 
ATOM   2474 C CG   . GLU   A 1 120 ? 28.570 -15.913 14.176  1.00 28.28 ?  120 GLU   A CG   1 
ATOM   2475 C CD   . GLU   A 1 120 ? 28.742 -16.634 15.498  1.00 35.08 ?  120 GLU   A CD   1 
ATOM   2476 O OE1  . GLU   A 1 120 ? 28.339 -16.075 16.541  1.00 37.72 ?  120 GLU   A OE1  1 
ATOM   2477 O OE2  . GLU   A 1 120 ? 29.277 -17.763 15.495  1.00 41.54 -1 120 GLU   A OE2  1 
ATOM   2478 H H    . GLU   A 1 120 ? 28.449 -13.345 12.725  1.00 16.63 ?  120 GLU   A H    1 
ATOM   2479 H HA   . GLU   A 1 120 ? 26.869 -15.380 12.236  1.00 18.68 ?  120 GLU   A HA   1 
ATOM   2480 H HB2  . GLU   A 1 120 ? 27.609 -14.192 14.673  1.00 24.57 ?  120 GLU   A HB2  1 
ATOM   2481 H HB3  . GLU   A 1 120 ? 26.641 -15.448 14.628  1.00 24.57 ?  120 GLU   A HB3  1 
ATOM   2482 H HG2  . GLU   A 1 120 ? 28.467 -16.574 13.473  1.00 33.94 ?  120 GLU   A HG2  1 
ATOM   2483 H HG3  . GLU   A 1 120 ? 29.375 -15.394 14.032  1.00 33.94 ?  120 GLU   A HG3  1 
ATOM   2484 N N    . VAL   A 1 121 ? 25.342 -12.701 13.061  1.00 13.72 ?  121 VAL   A N    1 
ATOM   2485 C CA   . VAL   A 1 121 ? 24.051 -12.032 13.191  1.00 13.56 ?  121 VAL   A CA   1 
ATOM   2486 C C    . VAL   A 1 121 ? 24.162 -10.649 12.559  1.00 12.48 ?  121 VAL   A C    1 
ATOM   2487 O O    . VAL   A 1 121 ? 25.137 -9.929  12.799  1.00 13.38 ?  121 VAL   A O    1 
ATOM   2488 C CB   . VAL   A 1 121 ? 23.627 -11.890 14.670  1.00 16.33 ?  121 VAL   A CB   1 
ATOM   2489 C CG1  . VAL   A 1 121 ? 22.242 -11.261 14.775  1.00 17.16 ?  121 VAL   A CG1  1 
ATOM   2490 C CG2  . VAL   A 1 121 ? 23.656 -13.222 15.394  1.00 18.68 ?  121 VAL   A CG2  1 
ATOM   2491 H H    . VAL   A 1 121 ? 26.010 -12.164 13.147  1.00 16.46 ?  121 VAL   A H    1 
ATOM   2492 H HA   . VAL   A 1 121 ? 23.373 -12.541 12.722  1.00 16.27 ?  121 VAL   A HA   1 
ATOM   2493 H HB   . VAL   A 1 121 ? 24.248 -11.301 15.118  1.00 19.59 ?  121 VAL   A HB   1 
ATOM   2494 H HG11 . VAL   A 1 121 ? 21.936 -11.322 15.694  1.00 20.58 ?  121 VAL   A HG11 1 
ATOM   2495 H HG12 . VAL   A 1 121 ? 22.295 -10.330 14.507  1.00 20.58 ?  121 VAL   A HG12 1 
ATOM   2496 H HG13 . VAL   A 1 121 ? 21.631 -11.740 14.192  1.00 20.58 ?  121 VAL   A HG13 1 
ATOM   2497 H HG21 . VAL   A 1 121 ? 23.308 -13.103 16.297  1.00 22.41 ?  121 VAL   A HG21 1 
ATOM   2498 H HG22 . VAL   A 1 121 ? 23.099 -13.860 14.915  1.00 22.41 ?  121 VAL   A HG22 1 
ATOM   2499 H HG23 . VAL   A 1 121 ? 24.567 -13.545 15.435  1.00 22.41 ?  121 VAL   A HG23 1 
ATOM   2500 N N    . LEU   A 1 122 ? 23.145 -10.255 11.782  1.00 12.52 ?  122 LEU   A N    1 
ATOM   2501 C CA   . LEU   A 1 122 ? 23.143 -8.953  11.115  1.00 12.28 ?  122 LEU   A CA   1 
ATOM   2502 C C    . LEU   A 1 122 ? 21.743 -8.367  11.081  1.00 12.08 ?  122 LEU   A C    1 
ATOM   2503 O O    . LEU   A 1 122 ? 20.757 -9.091  10.938  1.00 13.11 ?  122 LEU   A O    1 
ATOM   2504 C CB   . LEU   A 1 122 ? 23.561 -9.039  9.642   1.00 13.69 ?  122 LEU   A CB   1 
ATOM   2505 C CG   . LEU   A 1 122 ? 24.760 -9.898  9.263   1.00 13.67 ?  122 LEU   A CG   1 
ATOM   2506 C CD1  . LEU   A 1 122 ? 24.353 -11.348 9.043   1.00 14.75 ?  122 LEU   A CD1  1 
ATOM   2507 C CD2  . LEU   A 1 122 ? 25.425 -9.322  8.020   1.00 13.18 ?  122 LEU   A CD2  1 
ATOM   2508 H H    . LEU   A 1 122 ? 22.437 -10.724 11.625  1.00 15.03 ?  122 LEU   A H    1 
ATOM   2509 H HA   . LEU   A 1 122 ? 23.739 -8.338  11.578  1.00 14.73 ?  122 LEU   A HA   1 
ATOM   2510 H HB2  . LEU   A 1 122 ? 22.812 -9.385  9.141   1.00 16.42 ?  122 LEU   A HB2  1 
ATOM   2511 H HB3  . LEU   A 1 122 ? 23.764 -8.143  9.336   1.00 16.42 ?  122 LEU   A HB3  1 
ATOM   2512 H HG   . LEU   A 1 122 ? 25.417 -9.880  9.980   1.00 16.40 ?  122 LEU   A HG   1 
ATOM   2513 H HD11 . LEU   A 1 122 ? 25.122 -11.859 8.748   1.00 17.69 ?  122 LEU   A HD11 1 
ATOM   2514 H HD12 . LEU   A 1 122 ? 24.018 -11.712 9.879   1.00 17.69 ?  122 LEU   A HD12 1 
ATOM   2515 H HD13 . LEU   A 1 122 ? 23.656 -11.382 8.368   1.00 17.69 ?  122 LEU   A HD13 1 
ATOM   2516 H HD21 . LEU   A 1 122 ? 26.160 -9.901  7.751   1.00 15.82 ?  122 LEU   A HD21 1 
ATOM   2517 H HD22 . LEU   A 1 122 ? 24.771 -9.272  7.307   1.00 15.82 ?  122 LEU   A HD22 1 
ATOM   2518 H HD23 . LEU   A 1 122 ? 25.764 -8.436  8.223   1.00 15.82 ?  122 LEU   A HD23 1 
ATOM   2519 N N    . LEU   A 1 123 ? 21.680 -7.039  11.173  1.00 11.53 ?  123 LEU   A N    1 
ATOM   2520 C CA   . LEU   A 1 123 ? 20.506 -6.243  10.819  1.00 11.43 ?  123 LEU   A CA   1 
ATOM   2521 C C    . LEU   A 1 123 ? 20.752 -5.704  9.416   1.00 11.27 ?  123 LEU   A C    1 
ATOM   2522 O O    . LEU   A 1 123 ? 21.798 -5.101  9.173   1.00 11.57 ?  123 LEU   A O    1 
ATOM   2523 C CB   . LEU   A 1 123 ? 20.384 -5.079  11.799  1.00 12.44 ?  123 LEU   A CB   1 
ATOM   2524 C CG   . LEU   A 1 123 ? 19.340 -4.010  11.471  1.00 13.07 ?  123 LEU   A CG   1 
ATOM   2525 C CD1  . LEU   A 1 123 ? 17.944 -4.604  11.476  1.00 13.98 ?  123 LEU   A CD1  1 
ATOM   2526 C CD2  . LEU   A 1 123 ? 19.428 -2.845  12.452  1.00 13.68 ?  123 LEU   A CD2  1 
ATOM   2527 H H    . LEU   A 1 123 ? 22.341 -6.554  11.442  1.00 13.83 ?  123 LEU   A H    1 
ATOM   2528 H HA   . LEU   A 1 123 ? 19.703 -6.786  10.834  1.00 13.71 ?  123 LEU   A HA   1 
ATOM   2529 H HB2  . LEU   A 1 123 ? 20.151 -5.441  12.671  1.00 14.93 ?  123 LEU   A HB2  1 
ATOM   2530 H HB3  . LEU   A 1 123 ? 21.238 -4.633  11.854  1.00 14.93 ?  123 LEU   A HB3  1 
ATOM   2531 H HG   . LEU   A 1 123 ? 19.506 -3.658  10.582  1.00 15.68 ?  123 LEU   A HG   1 
ATOM   2532 H HD11 . LEU   A 1 123 ? 17.298 -3.903  11.313  1.00 16.78 ?  123 LEU   A HD11 1 
ATOM   2533 H HD12 . LEU   A 1 123 ? 17.885 -5.279  10.780  1.00 16.78 ?  123 LEU   A HD12 1 
ATOM   2534 H HD13 . LEU   A 1 123 ? 17.779 -5.012  12.343  1.00 16.78 ?  123 LEU   A HD13 1 
ATOM   2535 H HD21 . LEU   A 1 123 ? 18.757 -2.184  12.224  1.00 16.41 ?  123 LEU   A HD21 1 
ATOM   2536 H HD22 . LEU   A 1 123 ? 19.268 -3.181  13.352  1.00 16.41 ?  123 LEU   A HD22 1 
ATOM   2537 H HD23 . LEU   A 1 123 ? 20.313 -2.456  12.399  1.00 16.41 ?  123 LEU   A HD23 1 
ATOM   2538 N N    A ALA   A 1 124 ? 19.786 -5.874  8.511   0.84 11.03 ?  124 ALA   A N    1 
ATOM   2539 N N    B ALA   A 1 124 ? 19.834 -5.961  8.489   0.16 11.02 ?  124 ALA   A N    1 
ATOM   2540 C CA   A ALA   A 1 124 ? 20.057 -5.572  7.112   0.84 10.92 ?  124 ALA   A CA   1 
ATOM   2541 C CA   B ALA   A 1 124 ? 20.131 -5.704  7.088   0.16 11.16 ?  124 ALA   A CA   1 
ATOM   2542 C C    A ALA   A 1 124 ? 18.812 -5.107  6.375   0.84 10.83 ?  124 ALA   A C    1 
ATOM   2543 C C    B ALA   A 1 124 ? 18.885 -5.230  6.362   0.16 11.16 ?  124 ALA   A C    1 
ATOM   2544 O O    A ALA   A 1 124 ? 17.685 -5.482  6.731   0.84 11.53 ?  124 ALA   A O    1 
ATOM   2545 O O    B ALA   A 1 124 ? 17.764 -5.549  6.777   0.16 11.15 ?  124 ALA   A O    1 
ATOM   2546 C CB   A ALA   A 1 124 ? 20.632 -6.791  6.388   0.84 11.57 ?  124 ALA   A CB   1 
ATOM   2547 C CB   B ALA   A 1 124 ? 20.676 -6.962  6.396   0.16 11.29 ?  124 ALA   A CB   1 
ATOM   2548 H H    A ALA   A 1 124 ? 18.999 -6.178  8.679   0.84 13.24 ?  124 ALA   A H    1 
ATOM   2549 H H    B ALA   A 1 124 ? 19.051 -6.272  8.642   0.16 13.22 ?  124 ALA   A H    1 
ATOM   2550 H HA   A ALA   A 1 124 ? 20.711 -4.858  7.080   0.84 13.11 ?  124 ALA   A HA   1 
ATOM   2551 H HA   B ALA   A 1 124 ? 20.810 -5.013  7.032   0.16 13.39 ?  124 ALA   A HA   1 
ATOM   2552 H HB1  A ALA   A 1 124 ? 20.802 -6.559  5.460   0.84 13.88 ?  124 ALA   A HB1  1 
ATOM   2553 H HB1  B ALA   A 1 124 ? 20.865 -6.755  5.466   0.16 13.55 ?  124 ALA   A HB1  1 
ATOM   2554 H HB2  A ALA   A 1 124 ? 21.470 -7.043  6.818   0.84 13.88 ?  124 ALA   A HB2  1 
ATOM   2555 H HB2  B ALA   A 1 124 ? 21.492 -7.242  6.842   0.16 13.55 ?  124 ALA   A HB2  1 
ATOM   2556 H HB3  A ALA   A 1 124 ? 20.002 -7.521  6.440   0.84 13.88 ?  124 ALA   A HB3  1 
ATOM   2557 H HB3  B ALA   A 1 124 ? 20.011 -7.665  6.451   0.16 13.55 ?  124 ALA   A HB3  1 
ATOM   2558 N N    A PRO   A 1 125 ? 18.994 -4.345  5.296   0.84 10.92 ?  125 PRO   A N    1 
ATOM   2559 N N    B PRO   A 1 125 ? 19.047 -4.471  5.275   0.16 11.11 ?  125 PRO   A N    1 
ATOM   2560 C CA   A PRO   A 1 125 ? 17.939 -4.116  4.311   0.84 11.50 ?  125 PRO   A CA   1 
ATOM   2561 C CA   B PRO   A 1 125 ? 17.903 -4.129  4.425   0.16 11.29 ?  125 PRO   A CA   1 
ATOM   2562 C C    A PRO   A 1 125 ? 18.000 -5.199  3.238   0.84 11.05 ?  125 PRO   A C    1 
ATOM   2563 C C    B PRO   A 1 125 ? 17.830 -5.076  3.239   0.16 11.23 ?  125 PRO   A C    1 
ATOM   2564 O O    A PRO   A 1 125 ? 18.975 -5.945  3.128   0.84 11.54 ?  125 PRO   A O    1 
ATOM   2565 O O    B PRO   A 1 125 ? 18.657 -5.987  3.127   0.16 11.53 ?  125 PRO   A O    1 
ATOM   2566 C CB   A PRO   A 1 125 ? 18.374 -2.777  3.703   0.84 11.36 ?  125 PRO   A CB   1 
ATOM   2567 C CB   B PRO   A 1 125 ? 18.248 -2.710  3.972   0.16 11.32 ?  125 PRO   A CB   1 
ATOM   2568 C CG   A PRO   A 1 125 ? 19.888 -2.933  3.618   0.84 11.70 ?  125 PRO   A CG   1 
ATOM   2569 C CG   B PRO   A 1 125 ? 19.749 -2.764  3.813   0.16 11.47 ?  125 PRO   A CG   1 
ATOM   2570 C CD   A PRO   A 1 125 ? 20.266 -3.709  4.880   0.84 11.36 ?  125 PRO   A CD   1 
ATOM   2571 C CD   B PRO   A 1 125 ? 20.267 -3.769  4.837   0.16 11.28 ?  125 PRO   A CD   1 
ATOM   2572 H HA   A PRO   A 1 125 ? 17.056 -4.060  4.716   0.84 13.79 ?  125 PRO   A HA   1 
ATOM   2573 H HA   B PRO   A 1 125 ? 17.068 -4.136  4.923   0.16 13.54 ?  125 PRO   A HA   1 
ATOM   2574 H HB2  A PRO   A 1 125 ? 17.973 -2.668  2.822   0.84 13.62 ?  125 PRO   A HB2  1 
ATOM   2575 H HB2  B PRO   A 1 125 ? 17.813 -2.513  3.127   0.16 13.59 ?  125 PRO   A HB2  1 
ATOM   2576 H HB3  A PRO   A 1 125 ? 18.119 -2.049  4.292   0.84 13.62 ?  125 PRO   A HB3  1 
ATOM   2577 H HB3  B PRO   A 1 125 ? 17.991 -2.069  4.655   0.16 13.59 ?  125 PRO   A HB3  1 
ATOM   2578 H HG2  A PRO   A 1 125 ? 20.123 -3.435  2.819   0.84 14.03 ?  125 PRO   A HG2  1 
ATOM   2579 H HG2  B PRO   A 1 125 ? 19.965 -3.056  2.914   0.16 13.76 ?  125 PRO   A HG2  1 
ATOM   2580 H HG3  A PRO   A 1 125 ? 20.306 -2.058  3.607   0.84 14.03 ?  125 PRO   A HG3  1 
ATOM   2581 H HG3  B PRO   A 1 125 ? 20.123 -1.887  3.983   0.16 13.76 ?  125 PRO   A HG3  1 
ATOM   2582 H HD2  A PRO   A 1 125 ? 20.940 -4.374  4.672   0.84 13.63 ?  125 PRO   A HD2  1 
ATOM   2583 H HD2  B PRO   A 1 125 ? 20.887 -4.390  4.420   0.16 13.53 ?  125 PRO   A HD2  1 
ATOM   2584 H HD3  A PRO   A 1 125 ? 20.573 -3.094  5.566   0.84 13.63 ?  125 PRO   A HD3  1 
ATOM   2585 H HD3  B PRO   A 1 125 ? 20.676 -3.308  5.585   0.16 13.53 ?  125 PRO   A HD3  1 
ATOM   2586 N N    A LEU   A 1 126 ? 16.947 -5.254  2.424   0.84 11.37 ?  126 LEU   A N    1 
ATOM   2587 N N    B LEU   A 1 126 ? 16.868 -4.872  2.343   0.16 11.21 ?  126 LEU   A N    1 
ATOM   2588 C CA   A LEU   A 1 126 ? 16.983 -6.075  1.222   0.84 11.55 ?  126 LEU   A CA   1 
ATOM   2589 C CA   B LEU   A 1 126 ? 16.763 -5.687  1.135   0.16 10.93 ?  126 LEU   A CA   1 
ATOM   2590 C C    A LEU   A 1 126 ? 17.925 -5.457  0.193   0.84 11.80 ?  126 LEU   A C    1 
ATOM   2591 C C    B LEU   A 1 126 ? 17.692 -5.105  0.078   0.16 10.37 ?  126 LEU   A C    1 
ATOM   2592 O O    A LEU   A 1 126 ? 17.721 -4.326  -0.254  0.84 12.46 ?  126 LEU   A O    1 
ATOM   2593 O O    B LEU   A 1 126 ? 17.387 -4.083  -0.541  0.16 10.40 ?  126 LEU   A O    1 
ATOM   2594 C CB   A LEU   A 1 126 ? 15.585 -6.228  0.637   0.84 12.16 ?  126 LEU   A CB   1 
ATOM   2595 C CB   B LEU   A 1 126 ? 15.325 -5.714  0.637   0.16 11.20 ?  126 LEU   A CB   1 
ATOM   2596 C CG   A LEU   A 1 126 ? 14.654 -7.172  1.397   0.84 13.32 ?  126 LEU   A CG   1 
ATOM   2597 C CG   B LEU   A 1 126 ? 14.340 -6.580  1.418   0.16 11.24 ?  126 LEU   A CG   1 
ATOM   2598 C CD1  A LEU   A 1 126 ? 13.244 -7.043  0.873   0.84 15.03 ?  126 LEU   A CD1  1 
ATOM   2599 C CD1  B LEU   A 1 126 ? 12.993 -6.553  0.722   0.16 11.50 ?  126 LEU   A CD1  1 
ATOM   2600 C CD2  A LEU   A 1 126 ? 15.135 -8.621  1.278   0.84 13.66 ?  126 LEU   A CD2  1 
ATOM   2601 C CD2  B LEU   A 1 126 ? 14.848 -8.004  1.548   0.16 11.06 ?  126 LEU   A CD2  1 
ATOM   2602 H H    A LEU   A 1 126 ? 16.211 -4.822  2.539   0.84 13.64 ?  126 LEU   A H    1 
ATOM   2603 H H    B LEU   A 1 126 ? 16.259 -4.267  2.412   0.16 13.45 ?  126 LEU   A H    1 
ATOM   2604 H HA   A LEU   A 1 126 ? 17.317 -6.952  1.443   0.84 13.85 ?  126 LEU   A HA   1 
ATOM   2605 H HA   B LEU   A 1 126 ? 17.050 -6.595  1.328   0.16 13.11 ?  126 LEU   A HA   1 
ATOM   2606 H HB2  A LEU   A 1 126 ? 15.155 -5.356  0.624   0.84 14.59 ?  126 LEU   A HB2  1 
ATOM   2607 H HB2  B LEU   A 1 126 ? 14.982 -4.807  0.656   0.16 13.44 ?  126 LEU   A HB2  1 
ATOM   2608 H HB3  A LEU   A 1 126 ? 15.658 -6.564  -0.269  0.84 14.59 ?  126 LEU   A HB3  1 
ATOM   2609 H HB3  B LEU   A 1 126 ? 15.325 -6.039  -0.275  0.16 13.44 ?  126 LEU   A HB3  1 
ATOM   2610 H HG   A LEU   A 1 126 ? 14.649 -6.933  2.336   0.84 15.99 ?  126 LEU   A HG   1 
ATOM   2611 H HG   B LEU   A 1 126 ? 14.226 -6.213  2.310   0.16 13.49 ?  126 LEU   A HG   1 
ATOM   2612 H HD11 A LEU   A 1 126 ? 12.665 -7.652  1.358   0.84 18.04 ?  126 LEU   A HD11 1 
ATOM   2613 H HD11 B LEU   A 1 126 ? 12.368 -7.101  1.221   0.16 13.80 ?  126 LEU   A HD11 1 
ATOM   2614 H HD12 A LEU   A 1 126 ? 12.942 -6.129  0.999   0.84 18.04 ?  126 LEU   A HD12 1 
ATOM   2615 H HD12 B LEU   A 1 126 ? 12.675 -5.639  0.683   0.16 13.80 ?  126 LEU   A HD12 1 
ATOM   2616 H HD13 A LEU   A 1 126 ? 13.236 -7.265  -0.073  0.84 18.04 ?  126 LEU   A HD13 1 
ATOM   2617 H HD13 B LEU   A 1 126 ? 13.097 -6.906  -0.177  0.16 13.80 ?  126 LEU   A HD13 1 
ATOM   2618 H HD21 A LEU   A 1 126 ? 14.464 -9.214  1.647   0.84 16.39 ?  126 LEU   A HD21 1 
ATOM   2619 H HD21 B LEU   A 1 126 ? 14.119 -8.575  1.830   0.16 13.27 ?  126 LEU   A HD21 1 
ATOM   2620 H HD22 A LEU   A 1 126 ? 15.284 -8.831  0.342   0.84 16.39 ?  126 LEU   A HD22 1 
ATOM   2621 H HD22 B LEU   A 1 126 ? 15.184 -8.295  0.685   0.16 13.27 ?  126 LEU   A HD22 1 
ATOM   2622 H HD23 A LEU   A 1 126 ? 15.969 -8.720  1.771   0.84 16.39 ?  126 LEU   A HD23 1 
ATOM   2623 H HD23 B LEU   A 1 126 ? 15.562 -8.025  2.205   0.16 13.27 ?  126 LEU   A HD23 1 
ATOM   2624 N N    A LEU   A 1 127 ? 18.945 -6.213  -0.201  0.84 11.58 ?  127 LEU   A N    1 
ATOM   2625 N N    B LEU   A 1 127 ? 18.823 -5.767  -0.148  0.16 10.16 ?  127 LEU   A N    1 
ATOM   2626 C CA   A LEU   A 1 127 ? 19.933 -5.708  -1.141  0.84 11.44 ?  127 LEU   A CA   1 
ATOM   2627 C CA   B LEU   A 1 127 ? 19.817 -5.240  -1.071  0.16 10.22 ?  127 LEU   A CA   1 
ATOM   2628 C C    A LEU   A 1 127 ? 19.316 -5.496  -2.513  0.84 10.81 ?  127 LEU   A C    1 
ATOM   2629 C C    B LEU   A 1 127 ? 19.270 -5.200  -2.494  0.16 10.50 ?  127 LEU   A C    1 
ATOM   2630 O O    A LEU   A 1 127 ? 18.477 -6.275  -2.979  0.84 11.50 ?  127 LEU   A O    1 
ATOM   2631 O O    B LEU   A 1 127 ? 18.434 -6.018  -2.891  0.16 10.70 ?  127 LEU   A O    1 
ATOM   2632 C CB   A LEU   A 1 127 ? 21.104 -6.684  -1.252  0.84 12.00 ?  127 LEU   A CB   1 
ATOM   2633 C CB   B LEU   A 1 127 ? 21.084 -6.098  -1.037  0.16 10.34 ?  127 LEU   A CB   1 
ATOM   2634 C CG   A LEU   A 1 127 ? 21.912 -6.898  0.027   0.84 12.26 ?  127 LEU   A CG   1 
ATOM   2635 C CG   B LEU   A 1 127 ? 21.875 -6.092  0.276   0.16 10.24 ?  127 LEU   A CG   1 
ATOM   2636 C CD1  A LEU   A 1 127 ? 23.035 -7.882  -0.225  0.84 12.95 ?  127 LEU   A CD1  1 
ATOM   2637 C CD1  B LEU   A 1 127 ? 23.081 -7.024  0.207   0.16 10.30 ?  127 LEU   A CD1  1 
ATOM   2638 C CD2  A LEU   A 1 127 ? 22.483 -5.590  0.538   0.84 13.41 ?  127 LEU   A CD2  1 
ATOM   2639 C CD2  B LEU   A 1 127 ? 22.307 -4.675  0.639   0.16 10.04 ?  127 LEU   A CD2  1 
ATOM   2640 H H    A LEU   A 1 127 ? 19.086 -7.014  0.070   0.84 13.90 ?  127 LEU   A H    1 
ATOM   2641 H H    B LEU   A 1 127 ? 19.034 -6.517  0.218   0.16 12.19 ?  127 LEU   A H    1 
ATOM   2642 H HA   A LEU   A 1 127 ? 20.272 -4.856  -0.824  0.84 13.73 ?  127 LEU   A HA   1 
ATOM   2643 H HA   B LEU   A 1 127 ? 20.046 -4.337  -0.802  0.16 12.26 ?  127 LEU   A HA   1 
ATOM   2644 H HB2  A LEU   A 1 127 ? 20.754 -7.549  -1.520  0.84 14.40 ?  127 LEU   A HB2  1 
ATOM   2645 H HB2  B LEU   A 1 127 ? 20.831 -7.017  -1.223  0.16 12.40 ?  127 LEU   A HB2  1 
ATOM   2646 H HB3  A LEU   A 1 127 ? 21.712 -6.355  -1.930  0.84 14.40 ?  127 LEU   A HB3  1 
ATOM   2647 H HB3  B LEU   A 1 127 ? 21.678 -5.783  -1.737  0.16 12.40 ?  127 LEU   A HB3  1 
ATOM   2648 H HG   A LEU   A 1 127 ? 21.334 -7.261  0.715   0.84 14.71 ?  127 LEU   A HG   1 
ATOM   2649 H HG   B LEU   A 1 127 ? 21.297 -6.416  0.982   0.16 12.28 ?  127 LEU   A HG   1 
ATOM   2650 H HD11 A LEU   A 1 127 ? 23.529 -8.015  0.602   0.84 15.54 ?  127 LEU   A HD11 1 
ATOM   2651 H HD11 B LEU   A 1 127 ? 23.573 -6.963  1.041   0.16 12.36 ?  127 LEU   A HD11 1 
ATOM   2652 H HD12 A LEU   A 1 127 ? 22.658 -8.723  -0.522  0.84 15.54 ?  127 LEU   A HD12 1 
ATOM   2653 H HD12 B LEU   A 1 127 ? 22.771 -7.935  0.074   0.16 12.36 ?  127 LEU   A HD12 1 
ATOM   2654 H HD13 A LEU   A 1 127 ? 23.625 -7.523  -0.905  0.84 15.54 ?  127 LEU   A HD13 1 
ATOM   2655 H HD13 B LEU   A 1 127 ? 23.647 -6.757  -0.532  0.16 12.36 ?  127 LEU   A HD13 1 
ATOM   2656 H HD21 A LEU   A 1 127 ? 23.119 -5.773  1.246   0.84 16.10 ?  127 LEU   A HD21 1 
ATOM   2657 H HD21 B LEU   A 1 127 ? 22.935 -4.719  1.377   0.16 12.04 ?  127 LEU   A HD21 1 
ATOM   2658 H HD22 A LEU   A 1 127 ? 22.934 -5.132  -0.195  0.84 16.10 ?  127 LEU   A HD22 1 
ATOM   2659 H HD22 B LEU   A 1 127 ? 22.729 -4.267  -0.132  0.16 12.04 ?  127 LEU   A HD22 1 
ATOM   2660 H HD23 A LEU   A 1 127 ? 21.764 -5.033  0.874   0.84 16.10 ?  127 LEU   A HD23 1 
ATOM   2661 H HD23 B LEU   A 1 127 ? 21.525 -4.165  0.899   0.16 12.04 ?  127 LEU   A HD23 1 
ATOM   2662 N N    A SER   A 1 128 ? 19.752 -4.425  -3.160  0.84 10.81 ?  128 SER   A N    1 
ATOM   2663 N N    B SER   A 1 128 ? 19.747 -4.216  -3.257  0.16 10.59 ?  128 SER   A N    1 
ATOM   2664 C CA   A SER   A 1 128 ? 19.338 -4.008  -4.494  0.84 10.97 ?  128 SER   A CA   1 
ATOM   2665 C CA   B SER   A 1 128 ? 19.462 -4.084  -4.684  0.16 10.39 ?  128 SER   A CA   1 
ATOM   2666 C C    A SER   A 1 128 ? 17.882 -3.552  -4.570  0.84 11.47 ?  128 SER   A C    1 
ATOM   2667 C C    B SER   A 1 128 ? 18.050 -3.586  -4.981  0.16 10.35 ?  128 SER   A C    1 
ATOM   2668 O O    A SER   A 1 128 ? 17.412 -3.232  -5.662  0.84 12.52 ?  128 SER   A O    1 
ATOM   2669 O O    B SER   A 1 128 ? 17.729 -3.289  -6.136  0.16 10.39 ?  128 SER   A O    1 
ATOM   2670 C CB   A SER   A 1 128 ? 19.675 -5.033  -5.588  0.84 11.10 ?  128 SER   A CB   1 
ATOM   2671 C CB   B SER   A 1 128 ? 19.755 -5.384  -5.439  0.16 10.37 ?  128 SER   A CB   1 
ATOM   2672 O OG   A SER   A 1 128 ? 21.085 -5.229  -5.662  0.84 11.77 ?  128 SER   A OG   1 
ATOM   2673 O OG   B SER   A 1 128 ? 21.152 -5.534  -5.637  0.16 10.43 ?  128 SER   A OG   1 
ATOM   2674 H H    A SER   A 1 128 ? 20.336 -3.891  -2.825  0.84 12.97 ?  128 SER   A H    1 
ATOM   2675 H H    B SER   A 1 128 ? 20.256 -3.587  -2.955  0.16 12.70 ?  128 SER   A H    1 
ATOM   2676 H HA   A SER   A 1 128 ? 19.866 -3.226  -4.704  0.84 13.16 ?  128 SER   A HA   1 
ATOM   2677 H HA   B SER   A 1 128 ? 20.066 -3.419  -5.035  0.16 12.47 ?  128 SER   A HA   1 
ATOM   2678 H HB2  A SER   A 1 128 ? 19.240 -5.874  -5.385  0.84 13.31 ?  128 SER   A HB2  1 
ATOM   2679 H HB2  B SER   A 1 128 ? 19.420 -6.144  -4.941  0.16 12.44 ?  128 SER   A HB2  1 
ATOM   2680 H HB3  A SER   A 1 128 ? 19.354 -4.694  -6.445  0.84 13.31 ?  128 SER   A HB3  1 
ATOM   2681 H HB3  B SER   A 1 128 ? 19.319 -5.342  -6.306  0.16 12.44 ?  128 SER   A HB3  1 
ATOM   2682 H HG   A SER   A 1 128 ? 21.466 -4.504  -5.840  0.84 14.12 ?  128 SER   A HG   1 
ATOM   2683 H HG   B SER   A 1 128 ? 21.444 -4.877  -6.074  0.16 12.51 ?  128 SER   A HG   1 
ATOM   2684 N N    A ALA   A 1 129 ? 17.170 -3.474  -3.443  0.84 12.02 ?  129 ALA   A N    1 
ATOM   2685 N N    B ALA   A 1 129 ? 17.209 -3.475  -3.956  0.16 10.42 ?  129 ALA   A N    1 
ATOM   2686 C CA   A ALA   A 1 129 ? 15.807 -2.960  -3.430  0.84 12.31 ?  129 ALA   A CA   1 
ATOM   2687 C CA   B ALA   A 1 129 ? 15.866 -2.939  -4.125  0.16 10.84 ?  129 ALA   A CA   1 
ATOM   2688 C C    A ALA   A 1 129 ? 15.819 -1.431  -3.418  0.84 11.61 ?  129 ALA   A C    1 
ATOM   2689 C C    B ALA   A 1 129 ? 15.918 -1.411  -4.048  0.16 11.06 ?  129 ALA   A C    1 
ATOM   2690 O O    A ALA   A 1 129 ? 16.869 -0.786  -3.515  0.84 11.95 ?  129 ALA   A O    1 
ATOM   2691 O O    B ALA   A 1 129 ? 16.990 -0.802  -3.989  0.16 10.91 ?  129 ALA   A O    1 
ATOM   2692 C CB   A ALA   A 1 129 ? 15.035 -3.530  -2.239  0.84 13.70 ?  129 ALA   A CB   1 
ATOM   2693 C CB   B ALA   A 1 129 ? 14.913 -3.565  -3.109  0.16 11.01 ?  129 ALA   A CB   1 
ATOM   2694 H H    A ALA   A 1 129 ? 17.459 -3.710  -2.665  0.84 14.42 ?  129 ALA   A H    1 
ATOM   2695 H H    B ALA   A 1 129 ? 17.393 -3.704  -3.151  0.16 12.50 ?  129 ALA   A H    1 
ATOM   2696 H HA   A ALA   A 1 129 ? 15.360 -3.247  -4.237  0.84 14.77 ?  129 ALA   A HA   1 
ATOM   2697 H HA   B ALA   A 1 129 ? 15.549 -3.174  -5.007  0.16 13.00 ?  129 ALA   A HA   1 
ATOM   2698 H HB1  A ALA   A 1 129 ? 14.126 -3.186  -2.259  0.84 16.44 ?  129 ALA   A HB1  1 
ATOM   2699 H HB1  B ALA   A 1 129 ? 14.025 -3.197  -3.242  0.16 13.21 ?  129 ALA   A HB1  1 
ATOM   2700 H HB2  A ALA   A 1 129 ? 15.023 -4.496  -2.304  0.84 16.44 ?  129 ALA   A HB2  1 
ATOM   2701 H HB2  B ALA   A 1 129 ? 14.895 -4.526  -3.245  0.16 13.21 ?  129 ALA   A HB2  1 
ATOM   2702 H HB3  A ALA   A 1 129 ? 15.471 -3.257  -1.416  0.84 16.44 ?  129 ALA   A HB3  1 
ATOM   2703 H HB3  B ALA   A 1 129 ? 15.224 -3.364  -2.213  0.16 13.21 ?  129 ALA   A HB3  1 
ATOM   2704 N N    A GLY   A 1 130 ? 14.628 -0.843  -3.321  0.84 12.28 ?  130 GLY   A N    1 
ATOM   2705 N N    B GLY   A 1 130 ? 14.750 -0.774  -4.059  0.16 11.25 ?  130 GLY   A N    1 
ATOM   2706 C CA   A GLY   A 1 130 ? 14.536 0.606   -3.275  0.84 13.12 ?  130 GLY   A CA   1 
ATOM   2707 C CA   B GLY   A 1 130 ? 14.707 0.678   -4.010  0.16 11.62 ?  130 GLY   A CA   1 
ATOM   2708 C C    A GLY   A 1 130 ? 15.132 1.223   -4.522  0.84 12.47 ?  130 GLY   A C    1 
ATOM   2709 C C    B GLY   A 1 130 ? 15.381 1.293   -5.217  0.16 11.65 ?  130 GLY   A C    1 
ATOM   2710 O O    A GLY   A 1 130 ? 14.874 0.775   -5.646  0.84 12.62 ?  130 GLY   A O    1 
ATOM   2711 O O    B GLY   A 1 130 ? 15.237 0.822   -6.351  0.16 11.78 ?  130 GLY   A O    1 
ATOM   2712 H H    A GLY   A 1 130 ? 13.871 -1.255  -3.284  0.84 14.74 ?  130 GLY   A H    1 
ATOM   2713 H H    B GLY   A 1 130 ? 13.981 -1.152  -4.101  0.16 13.50 ?  130 GLY   A H    1 
ATOM   2714 H HA2  A GLY   A 1 130 ? 13.601 0.874   -3.206  0.84 15.74 ?  130 GLY   A HA2  1 
ATOM   2715 H HA2  B GLY   A 1 130 ? 13.781 0.978   -3.963  0.16 13.94 ?  130 GLY   A HA2  1 
ATOM   2716 H HA3  A GLY   A 1 130 ? 15.012 0.942   -2.505  0.84 15.74 ?  130 GLY   A HA3  1 
ATOM   2717 H HA3  B GLY   A 1 130 ? 15.171 0.998   -3.226  0.16 13.94 ?  130 GLY   A HA3  1 
ATOM   2718 N N    A ILE   A 1 131 ? 15.942 2.270   -4.327  0.84 12.39 ?  131 ILE   A N    1 
ATOM   2719 N N    B ILE   A 1 131 ? 16.153 2.355   -4.971  0.16 11.71 ?  131 ILE   A N    1 
ATOM   2720 C CA   A ILE   A 1 131 ? 16.499 3.022   -5.448  0.84 12.77 ?  131 ILE   A CA   1 
ATOM   2721 C CA   B ILE   A 1 131 ? 16.798 3.092   -6.049  0.16 11.76 ?  131 ILE   A CA   1 
ATOM   2722 C C    A ILE   A 1 131 ? 17.517 2.240   -6.265  0.84 12.18 ?  131 ILE   A C    1 
ATOM   2723 C C    B ILE   A 1 131 ? 17.781 2.242   -6.840  0.16 11.93 ?  131 ILE   A C    1 
ATOM   2724 O O    A ILE   A 1 131 ? 17.937 2.729   -7.322  0.84 13.04 ?  131 ILE   A O    1 
ATOM   2725 O O    B ILE   A 1 131 ? 18.228 2.668   -7.910  0.16 11.99 ?  131 ILE   A O    1 
ATOM   2726 C CB   A ILE   A 1 131 ? 17.063 4.394   -5.017  0.84 13.79 ?  131 ILE   A CB   1 
ATOM   2727 C CB   B ILE   A 1 131 ? 17.460 4.395   -5.534  0.16 11.95 ?  131 ILE   A CB   1 
ATOM   2728 C CG1  A ILE   A 1 131 ? 18.309 4.242   -4.135  0.84 15.31 ?  131 ILE   A CG1  1 
ATOM   2729 C CG1  B ILE   A 1 131 ? 18.655 4.097   -4.623  0.16 11.91 ?  131 ILE   A CG1  1 
ATOM   2730 C CG2  A ILE   A 1 131 ? 15.977 5.214   -4.322  0.84 14.83 ?  131 ILE   A CG2  1 
ATOM   2731 C CG2  B ILE   A 1 131 ? 16.436 5.257   -4.806  0.16 12.17 ?  131 ILE   A CG2  1 
ATOM   2732 C CD1  A ILE   A 1 131 ? 18.944 5.574   -3.736  0.84 17.02 ?  131 ILE   A CD1  1 
ATOM   2733 C CD1  B ILE   A 1 131 ? 19.385 5.346   -4.155  0.16 12.00 ?  131 ILE   A CD1  1 
ATOM   2734 H H    A ILE   A 1 131 ? 16.163 2.569   -3.554  0.84 14.87 ?  131 ILE   A H    1 
ATOM   2735 H H    B ILE   A 1 131 ? 16.318 2.660   -4.185  0.16 14.04 ?  131 ILE   A H    1 
ATOM   2736 H HA   A ILE   A 1 131 ? 15.771 3.213   -6.051  0.84 15.32 ?  131 ILE   A HA   1 
ATOM   2737 H HA   B ILE   A 1 131 ? 16.114 3.364   -6.673  0.16 14.10 ?  131 ILE   A HA   1 
ATOM   2738 H HB   A ILE   A 1 131 ? 17.322 4.870   -5.819  0.84 16.55 ?  131 ILE   A HB   1 
ATOM   2739 H HB   B ILE   A 1 131 ? 17.780 4.897   -6.298  0.16 14.34 ?  131 ILE   A HB   1 
ATOM   2740 H HG12 A ILE   A 1 131 ? 18.062 3.774   -3.323  0.84 18.37 ?  131 ILE   A HG12 1 
ATOM   2741 H HG12 B ILE   A 1 131 ? 18.342 3.627   -3.836  0.16 14.28 ?  131 ILE   A HG12 1 
ATOM   2742 H HG13 A ILE   A 1 131 ? 18.977 3.732   -4.619  0.84 18.37 ?  131 ILE   A HG13 1 
ATOM   2743 H HG13 B ILE   A 1 131 ? 19.293 3.553   -5.104  0.16 14.28 ?  131 ILE   A HG13 1 
ATOM   2744 H HG21 A ILE   A 1 131 ? 16.292 6.123   -4.206  0.84 17.79 ?  131 ILE   A HG21 1 
ATOM   2745 H HG21 B ILE   A 1 131 ? 16.802 6.147   -4.678  0.16 14.60 ?  131 ILE   A HG21 1 
ATOM   2746 H HG22 A ILE   A 1 131 ? 15.179 5.209   -4.874  0.84 17.79 ?  131 ILE   A HG22 1 
ATOM   2747 H HG22 B ILE   A 1 131 ? 15.630 5.307   -5.343  0.16 14.60 ?  131 ILE   A HG22 1 
ATOM   2748 H HG23 A ILE   A 1 131 ? 15.784 4.815   -3.460  0.84 17.79 ?  131 ILE   A HG23 1 
ATOM   2749 H HG23 B ILE   A 1 131 ? 16.236 4.854   -3.947  0.16 14.60 ?  131 ILE   A HG23 1 
ATOM   2750 H HD11 A ILE   A 1 131 ? 19.784 5.401   -3.281  0.84 20.42 ?  131 ILE   A HD11 1 
ATOM   2751 H HD11 B ILE   A 1 131 ? 20.198 5.083   -3.698  0.16 14.40 ?  131 ILE   A HD11 1 
ATOM   2752 H HD12 A ILE   A 1 131 ? 19.105 6.102   -4.534  0.84 20.42 ?  131 ILE   A HD12 1 
ATOM   2753 H HD12 B ILE   A 1 131 ? 19.600 5.893   -4.927  0.16 14.40 ?  131 ILE   A HD12 1 
ATOM   2754 H HD13 A ILE   A 1 131 ? 18.341 6.050   -3.143  0.84 20.42 ?  131 ILE   A HD13 1 
ATOM   2755 H HD13 B ILE   A 1 131 ? 18.810 5.842   -3.549  0.16 14.40 ?  131 ILE   A HD13 1 
ATOM   2756 N N    A PHE   A 1 132 ? 17.920 1.036   -5.822  0.84 11.77 ?  132 PHE   A N    1 
ATOM   2757 N N    B PHE   A 1 132 ? 18.131 1.051   -6.347  0.16 11.98 ?  132 PHE   A N    1 
ATOM   2758 C CA   A PHE   A 1 132 ? 18.773 0.182   -6.645  0.84 11.92 ?  132 PHE   A CA   1 
ATOM   2759 C CA   B PHE   A 1 132 ? 19.028 0.177   -7.093  0.16 12.15 ?  132 PHE   A CA   1 
ATOM   2760 C C    A PHE   A 1 132 ? 17.990 -0.577  -7.720  0.84 12.59 ?  132 PHE   A C    1 
ATOM   2761 C C    B PHE   A 1 132 ? 18.322 -0.587  -8.211  0.16 12.51 ?  132 PHE   A C    1 
ATOM   2762 O O    A PHE   A 1 132 ? 18.604 -1.229  -8.572  0.84 13.36 ?  132 PHE   A O    1 
ATOM   2763 O O    B PHE   A 1 132 ? 18.998 -1.108  -9.105  0.16 12.86 ?  132 PHE   A O    1 
ATOM   2764 C CB   A PHE   A 1 132 ? 19.584 -0.796  -5.778  0.84 11.69 ?  132 PHE   A CB   1 
ATOM   2765 C CB   B PHE   A 1 132 ? 19.757 -0.782  -6.148  0.16 11.84 ?  132 PHE   A CB   1 
ATOM   2766 C CG   A PHE   A 1 132 ? 20.817 -0.192  -5.120  0.84 11.46 ?  132 PHE   A CG   1 
ATOM   2767 C CG   B PHE   A 1 132 ? 20.939 -0.162  -5.448  0.16 12.09 ?  132 PHE   A CG   1 
ATOM   2768 C CD1  A PHE   A 1 132 ? 20.706 0.830   -4.194  0.84 12.35 ?  132 PHE   A CD1  1 
ATOM   2769 C CD1  B PHE   A 1 132 ? 20.773 0.922   -4.599  0.16 12.30 ?  132 PHE   A CD1  1 
ATOM   2770 C CD2  A PHE   A 1 132 ? 22.076 -0.707  -5.387  0.84 12.52 ?  132 PHE   A CD2  1 
ATOM   2771 C CD2  B PHE   A 1 132 ? 22.214 -0.668  -5.635  0.16 12.52 ?  132 PHE   A CD2  1 
ATOM   2772 C CE1  A PHE   A 1 132 ? 21.836 1.361   -3.580  0.84 12.97 ?  132 PHE   A CE1  1 
ATOM   2773 C CE1  B PHE   A 1 132 ? 21.858 1.491   -3.955  0.16 12.67 ?  132 PHE   A CE1  1 
ATOM   2774 C CE2  A PHE   A 1 132 ? 23.206 -0.185  -4.773  0.84 12.81 ?  132 PHE   A CE2  1 
ATOM   2775 C CE2  B PHE   A 1 132 ? 23.301 -0.104  -4.993  0.16 12.81 ?  132 PHE   A CE2  1 
ATOM   2776 C CZ   A PHE   A 1 132 ? 23.081 0.850   -3.864  0.84 12.79 ?  132 PHE   A CZ   1 
ATOM   2777 C CZ   B PHE   A 1 132 ? 23.123 0.976   -4.152  0.16 12.88 ?  132 PHE   A CZ   1 
ATOM   2778 H H    A PHE   A 1 132 ? 17.713 0.696   -5.054  0.84 14.12 ?  132 PHE   A H    1 
ATOM   2779 H H    B PHE   A 1 132 ? 17.870 0.737   -5.585  0.16 14.38 ?  132 PHE   A H    1 
ATOM   2780 H HA   A PHE   A 1 132 ? 19.413 0.749   -7.097  0.84 14.30 ?  132 PHE   A HA   1 
ATOM   2781 H HA   B PHE   A 1 132 ? 19.706 0.735   -7.501  0.16 14.57 ?  132 PHE   A HA   1 
ATOM   2782 H HB2  A PHE   A 1 132 ? 19.012 -1.131  -5.070  0.84 14.03 ?  132 PHE   A HB2  1 
ATOM   2783 H HB2  B PHE   A 1 132 ? 19.138 -1.087  -5.468  0.16 14.21 ?  132 PHE   A HB2  1 
ATOM   2784 H HB3  A PHE   A 1 132 ? 19.879 -1.536  -6.336  0.84 14.03 ?  132 PHE   A HB3  1 
ATOM   2785 H HB3  B PHE   A 1 132 ? 20.082 -1.538  -6.662  0.16 14.21 ?  132 PHE   A HB3  1 
ATOM   2786 H HD1  A PHE   A 1 132 ? 19.869 1.180   -3.995  0.84 14.82 ?  132 PHE   A HD1  1 
ATOM   2787 H HD1  B PHE   A 1 132 ? 19.924 1.275   -4.462  0.16 14.76 ?  132 PHE   A HD1  1 
ATOM   2788 H HD2  A PHE   A 1 132 ? 22.169 -1.405  -6.002  0.84 15.03 ?  132 PHE   A HD2  1 
ATOM   2789 H HD2  B PHE   A 1 132 ? 22.341 -1.396  -6.200  0.16 15.02 ?  132 PHE   A HD2  1 
ATOM   2790 H HE1  A PHE   A 1 132 ? 21.749 2.056   -2.971  0.84 15.57 ?  132 PHE   A HE1  1 
ATOM   2791 H HE1  B PHE   A 1 132 ? 21.736 2.220   -3.388  0.16 15.20 ?  132 PHE   A HE1  1 
ATOM   2792 H HE2  A PHE   A 1 132 ? 24.047 -0.531  -4.979  0.84 15.37 ?  132 PHE   A HE2  1 
ATOM   2793 H HE2  B PHE   A 1 132 ? 24.152 -0.454  -5.128  0.16 15.37 ?  132 PHE   A HE2  1 
ATOM   2794 H HZ   A PHE   A 1 132 ? 23.839 1.205   -3.462  0.84 15.35 ?  132 PHE   A HZ   1 
ATOM   2795 H HZ   B PHE   A 1 132 ? 23.854 1.356   -3.720  0.16 15.46 ?  132 PHE   A HZ   1 
ATOM   2796 N N    A GLY   A 1 133 ? 16.659 -0.522  -7.700  0.84 12.40 ?  133 GLY   A N    1 
ATOM   2797 N N    B GLY   A 1 133 ? 16.988 -0.679  -8.177  0.16 12.36 ?  133 GLY   A N    1 
ATOM   2798 C CA   A GLY   A 1 133 ? 15.859 -0.892  -8.851  0.84 13.59 ?  133 GLY   A CA   1 
ATOM   2799 C CA   B GLY   A 1 133 ? 16.192 -1.075  -9.324  0.16 12.45 ?  133 GLY   A CA   1 
ATOM   2800 C C    A GLY   A 1 133 ? 15.546 -2.361  -9.046  0.84 14.04 ?  133 GLY   A C    1 
ATOM   2801 C C    B GLY   A 1 133 ? 15.520 -2.434  -9.213  0.16 12.58 ?  133 GLY   A C    1 
ATOM   2802 O O    A GLY   A 1 133 ? 14.917 -2.695  -10.058 0.84 15.50 ?  133 GLY   A O    1 
ATOM   2803 O O    B GLY   A 1 133 ? 14.483 -2.650  -9.854  0.16 12.73 ?  133 GLY   A O    1 
ATOM   2804 H H    A GLY   A 1 133 ? 16.196 -0.266  -7.024  0.84 14.88 ?  133 GLY   A H    1 
ATOM   2805 H H    B GLY   A 1 133 ? 16.520 -0.507  -7.475  0.16 14.83 ?  133 GLY   A H    1 
ATOM   2806 H HA2  A GLY   A 1 133 ? 15.011 -0.431  -8.797  0.84 16.30 ?  133 GLY   A HA2  1 
ATOM   2807 H HA2  B GLY   A 1 133 ? 15.494 -0.419  -9.460  0.16 14.93 ?  133 GLY   A HA2  1 
ATOM   2808 H HA3  A GLY   A 1 133 ? 16.311 -0.588  -9.653  0.84 16.30 ?  133 GLY   A HA3  1 
ATOM   2809 H HA3  B GLY   A 1 133 ? 16.759 -1.075  -10.110 0.16 14.93 ?  133 GLY   A HA3  1 
ATOM   2810 N N    A ALA   A 1 134 ? 15.953 -3.252  -8.142  0.84 13.49 ?  134 ALA   A N    1 
ATOM   2811 N N    B ALA   A 1 134 ? 16.075 -3.350  -8.422  0.16 12.56 ?  134 ALA   A N    1 
ATOM   2812 C CA   A ALA   A 1 134 ? 15.612 -4.658  -8.305  0.84 14.28 ?  134 ALA   A CA   1 
ATOM   2813 C CA   B ALA   A 1 134 ? 15.608 -4.728  -8.454  0.16 12.68 ?  134 ALA   A CA   1 
ATOM   2814 C C    A ALA   A 1 134 ? 14.242 -4.960  -7.693  0.84 14.50 ?  134 ALA   A C    1 
ATOM   2815 C C    B ALA   A 1 134 ? 14.302 -4.890  -7.680  0.16 12.69 ?  134 ALA   A C    1 
ATOM   2816 O O    A ALA   A 1 134 ? 13.675 -4.174  -6.929  0.84 15.68 ?  134 ALA   A O    1 
ATOM   2817 O O    B ALA   A 1 134 ? 13.917 -4.052  -6.859  0.16 13.17 ?  134 ALA   A O    1 
ATOM   2818 C CB   A ALA   A 1 134 ? 16.686 -5.568  -7.702  0.84 15.28 ?  134 ALA   A CB   1 
ATOM   2819 C CB   B ALA   A 1 134 ? 16.667 -5.674  -7.888  0.16 12.77 ?  134 ALA   A CB   1 
ATOM   2820 H H    A ALA   A 1 134 ? 16.439 -3.072  -7.445  0.84 16.19 ?  134 ALA   A H    1 
ATOM   2821 H H    B ALA   A 1 134 ? 16.706 -3.204  -7.858  0.16 15.08 ?  134 ALA   A H    1 
ATOM   2822 H HA   A ALA   A 1 134 ? 15.571 -4.858  -9.256  0.84 17.13 ?  134 ALA   A HA   1 
ATOM   2823 H HA   B ALA   A 1 134 ? 15.443 -4.984  -9.376  0.16 15.21 ?  134 ALA   A HA   1 
ATOM   2824 H HB1  A ALA   A 1 134 ? 16.431 -6.493  -7.846  0.84 18.34 ?  134 ALA   A HB1  1 
ATOM   2825 H HB1  B ALA   A 1 134 ? 16.335 -6.585  -7.933  0.16 15.33 ?  134 ALA   A HB1  1 
ATOM   2826 H HB2  A ALA   A 1 134 ? 17.538 -5.392  -8.138  0.84 18.34 ?  134 ALA   A HB2  1 
ATOM   2827 H HB2  B ALA   A 1 134 ? 17.476 -5.592  -8.417  0.16 15.33 ?  134 ALA   A HB2  1 
ATOM   2828 H HB3  A ALA   A 1 134 ? 16.759 -5.387  -6.754  0.84 18.34 ?  134 ALA   A HB3  1 
ATOM   2829 H HB3  B ALA   A 1 134 ? 16.847 -5.433  -6.967  0.16 15.33 ?  134 ALA   A HB3  1 
ATOM   2830 N N    A ASP   A 1 135 ? 13.709 -6.119  -8.055  0.84 15.52 ?  135 ASP   A N    1 
ATOM   2831 N N    B ASP   A 1 135 ? 13.623 -6.000  -7.956  0.16 12.88 ?  135 ASP   A N    1 
ATOM   2832 C CA   A ASP   A 1 135 ? 12.449 -6.599  -7.496  0.84 16.39 ?  135 ASP   A CA   1 
ATOM   2833 C CA   B ASP   A 1 135 ? 12.351 -6.304  -7.317  0.16 13.04 ?  135 ASP   A CA   1 
ATOM   2834 C C    A ASP   A 1 135 ? 12.692 -7.057  -6.063  0.84 16.07 ?  135 ASP   A C    1 
ATOM   2835 C C    B ASP   A 1 135 ? 12.601 -6.798  -5.896  0.16 13.16 ?  135 ASP   A C    1 
ATOM   2836 O O    A ASP   A 1 135 ? 13.473 -7.994  -5.849  0.84 15.60 ?  135 ASP   A O    1 
ATOM   2837 O O    B ASP   A 1 135 ? 13.330 -7.781  -5.715  0.16 13.21 ?  135 ASP   A O    1 
ATOM   2838 C CB   A ASP   A 1 135 ? 11.972 -7.770  -8.351  0.84 19.02 ?  135 ASP   A CB   1 
ATOM   2839 C CB   B ASP   A 1 135 ? 11.644 -7.390  -8.118  0.16 13.16 ?  135 ASP   A CB   1 
ATOM   2840 C CG   A ASP   A 1 135 ? 10.695 -8.424  -7.827  0.84 21.50 ?  135 ASP   A CG   1 
ATOM   2841 C CG   B ASP   A 1 135 ? 10.223 -7.637  -7.645  0.16 13.36 ?  135 ASP   A CG   1 
ATOM   2842 O OD1  A ASP   A 1 135 ? 10.136 -7.962  -6.811  0.84 21.33 ?  135 ASP   A OD1  1 
ATOM   2843 O OD1  B ASP   A 1 135 ? 9.892  -7.245  -6.505  0.16 13.60 ?  135 ASP   A OD1  1 
ATOM   2844 O OD2  A ASP   A 1 135 ? 10.248 -9.412  -8.450  0.84 24.34 -1 135 ASP   A OD2  1 
ATOM   2845 O OD2  B ASP   A 1 135 ? 9.441  -8.237  -8.411  0.16 13.25 -1 135 ASP   A OD2  1 
ATOM   2846 H H    A ASP   A 1 135 ? 14.062 -6.653  -8.626  0.84 18.62 ?  135 ASP   A H    1 
ATOM   2847 H H    B ASP   A 1 135 ? 13.875 -6.600  -8.519  0.16 15.45 ?  135 ASP   A H    1 
ATOM   2848 H HA   A ASP   A 1 135 ? 11.782 -5.886  -7.525  0.84 19.67 ?  135 ASP   A HA   1 
ATOM   2849 H HA   B ASP   A 1 135 ? 11.788 -5.512  -7.306  0.16 15.64 ?  135 ASP   A HA   1 
ATOM   2850 H HB2  A ASP   A 1 135 ? 11.801 -7.450  -9.250  0.84 22.83 ?  135 ASP   A HB2  1 
ATOM   2851 H HB2  B ASP   A 1 135 ? 11.628 -7.126  -9.055  0.16 15.79 ?  135 ASP   A HB2  1 
ATOM   2852 H HB3  A ASP   A 1 135 ? 12.668 -8.442  -8.363  0.84 22.83 ?  135 ASP   A HB3  1 
ATOM   2853 H HB3  B ASP   A 1 135 ? 12.134 -8.222  -8.023  0.16 15.79 ?  135 ASP   A HB3  1 
ATOM   2854 N N    A PRO   A 1 136 ? 12.077 -6.428  -5.057  0.84 15.83 ?  136 PRO   A N    1 
ATOM   2855 N N    B PRO   A 1 136 ? 12.030 -6.160  -4.869  0.16 13.35 ?  136 PRO   A N    1 
ATOM   2856 C CA   A PRO   A 1 136 ? 12.338 -6.845  -3.666  0.84 15.86 ?  136 PRO   A CA   1 
ATOM   2857 C CA   B PRO   A 1 136 ? 12.252 -6.646  -3.495  0.16 13.62 ?  136 PRO   A CA   1 
ATOM   2858 C C    A PRO   A 1 136 ? 11.902 -8.267  -3.350  0.84 15.13 ?  136 PRO   A C    1 
ATOM   2859 C C    B PRO   A 1 136 ? 11.843 -8.094  -3.274  0.16 13.74 ?  136 PRO   A C    1 
ATOM   2860 O O    A PRO   A 1 136 ? 12.500 -8.903  -2.473  0.84 14.99 ?  136 PRO   A O    1 
ATOM   2861 O O    B PRO   A 1 136 ? 12.415 -8.758  -2.400  0.16 13.44 ?  136 PRO   A O    1 
ATOM   2862 C CB   A PRO   A 1 136 ? 11.568 -5.806  -2.838  0.84 17.30 ?  136 PRO   A CB   1 
ATOM   2863 C CB   B PRO   A 1 136 ? 11.428 -5.672  -2.636  0.16 13.92 ?  136 PRO   A CB   1 
ATOM   2864 C CG   A PRO   A 1 136 ? 10.505 -5.298  -3.764  0.84 18.75 ?  136 PRO   A CG   1 
ATOM   2865 C CG   B PRO   A 1 136 ? 10.461 -5.038  -3.592  0.16 14.21 ?  136 PRO   A CG   1 
ATOM   2866 C CD   A PRO   A 1 136 ? 11.125 -5.306  -5.129  0.84 17.12 ?  136 PRO   A CD   1 
ATOM   2867 C CD   B PRO   A 1 136 ? 11.203 -4.941  -4.882  0.16 13.73 ?  136 PRO   A CD   1 
ATOM   2868 H HA   A PRO   A 1 136 ? 13.287 -6.756  -3.469  0.84 19.03 ?  136 PRO   A HA   1 
ATOM   2869 H HA   B PRO   A 1 136 ? 13.186 -6.548  -3.258  0.16 16.35 ?  136 PRO   A HA   1 
ATOM   2870 H HB2  A PRO   A 1 136 ? 11.174 -6.233  -2.061  0.84 20.76 ?  136 PRO   A HB2  1 
ATOM   2871 H HB2  B PRO   A 1 136 ? 10.955 -6.158  -1.942  0.16 16.70 ?  136 PRO   A HB2  1 
ATOM   2872 H HB3  A PRO   A 1 136 ? 12.167 -5.089  -2.570  0.84 20.76 ?  136 PRO   A HB3  1 
ATOM   2873 H HB3  B PRO   A 1 136 ? 12.012 -5.001  -2.246  0.16 16.70 ?  136 PRO   A HB3  1 
ATOM   2874 H HG2  A PRO   A 1 136 ? 9.738  -5.888  -3.737  0.84 22.49 ?  136 PRO   A HG2  1 
ATOM   2875 H HG2  B PRO   A 1 136 ? 9.682  -5.608  -3.692  0.16 17.05 ?  136 PRO   A HG2  1 
ATOM   2876 H HG3  A PRO   A 1 136 ? 10.254 -4.396  -3.511  0.84 22.49 ?  136 PRO   A HG3  1 
ATOM   2877 H HG3  B PRO   A 1 136 ? 10.209 -4.160  -3.274  0.16 17.05 ?  136 PRO   A HG3  1 
ATOM   2878 H HD2  A PRO   A 1 136 ? 10.448 -5.482  -5.806  0.84 20.54 ?  136 PRO   A HD2  1 
ATOM   2879 H HD2  B PRO   A 1 136 ? 10.580 -4.950  -5.626  0.16 16.48 ?  136 PRO   A HD2  1 
ATOM   2880 H HD3  A PRO   A 1 136 ? 11.587 -4.469  -5.303  0.84 20.54 ?  136 PRO   A HD3  1 
ATOM   2881 H HD3  B PRO   A 1 136 ? 11.765 -4.148  -4.894  0.16 16.48 ?  136 PRO   A HD3  1 
ATOM   2882 N N    A ILE   A 1 137 ? 10.865 -8.778  -4.016  0.84 15.32 ?  137 ILE   A N    1 
ATOM   2883 N N    B ILE   A 1 137 ? 10.869 -8.606  -4.030  0.16 14.20 ?  137 ILE   A N    1 
ATOM   2884 C CA   A ILE   A 1 137 ? 10.480 -10.174 -3.821  0.84 15.98 ?  137 ILE   A CA   1 
ATOM   2885 C CA   B ILE   A 1 137 ? 10.478 -10.008 -3.889  0.16 14.72 ?  137 ILE   A CA   1 
ATOM   2886 C C    A ILE   A 1 137 ? 11.622 -11.091 -4.240  0.84 15.42 ?  137 ILE   A C    1 
ATOM   2887 C C    B ILE   A 1 137 ? 11.651 -10.913 -4.242  0.16 14.63 ?  137 ILE   A C    1 
ATOM   2888 O O    A ILE   A 1 137 ? 11.932 -12.081 -3.565  0.84 15.63 ?  137 ILE   A O    1 
ATOM   2889 O O    B ILE   A 1 137 ? 11.978 -11.858 -3.514  0.16 14.62 ?  137 ILE   A O    1 
ATOM   2890 C CB   A ILE   A 1 137 ? 9.177  -10.484 -4.583  0.84 17.48 ?  137 ILE   A CB   1 
ATOM   2891 C CB   B ILE   A 1 137 ? 9.248  -10.316 -4.764  0.16 15.42 ?  137 ILE   A CB   1 
ATOM   2892 C CG1  A ILE   A 1 137 ? 8.004  -9.668  -4.021  0.84 19.25 ?  137 ILE   A CG1  1 
ATOM   2893 C CG1  B ILE   A 1 137 ? 8.090  -9.369  -4.445  0.16 15.83 ?  137 ILE   A CG1  1 
ATOM   2894 C CG2  A ILE   A 1 137 ? 8.875  -11.979 -4.529  0.84 18.11 ?  137 ILE   A CG2  1 
ATOM   2895 C CG2  B ILE   A 1 137 ? 8.811  -11.766 -4.579  0.16 15.69 ?  137 ILE   A CG2  1 
ATOM   2896 C CD1  A ILE   A 1 137 ? 6.719  -9.817  -4.812  0.84 20.80 ?  137 ILE   A CD1  1 
ATOM   2897 C CD1  B ILE   A 1 137 ? 6.865  -9.621  -5.300  0.16 16.17 ?  137 ILE   A CD1  1 
ATOM   2898 H H    A ILE   A 1 137 ? 10.381 -8.341  -4.574  0.84 18.39 ?  137 ILE   A H    1 
ATOM   2899 H H    B ILE   A 1 137 ? 10.431 -8.167  -4.624  0.16 17.04 ?  137 ILE   A H    1 
ATOM   2900 H HA   A ILE   A 1 137 ? 10.316 -10.321 -2.880  0.84 19.17 ?  137 ILE   A HA   1 
ATOM   2901 H HA   B ILE   A 1 137 ? 10.236 -10.178 -2.966  0.16 17.67 ?  137 ILE   A HA   1 
ATOM   2902 H HB   A ILE   A 1 137 ? 9.299  -10.228 -5.510  0.84 20.97 ?  137 ILE   A HB   1 
ATOM   2903 H HB   B ILE   A 1 137 ? 9.493  -10.188 -5.692  0.16 18.50 ?  137 ILE   A HB   1 
ATOM   2904 H HG12 A ILE   A 1 137 ? 7.830  -9.953  -3.111  0.84 23.09 ?  137 ILE   A HG12 1 
ATOM   2905 H HG12 B ILE   A 1 137 ? 7.834  -9.482  -3.516  0.16 18.99 ?  137 ILE   A HG12 1 
ATOM   2906 H HG13 A ILE   A 1 137 ? 8.245  -8.724  -4.027  0.84 23.09 ?  137 ILE   A HG13 1 
ATOM   2907 H HG13 B ILE   A 1 137 ? 8.373  -8.454  -4.600  0.16 18.99 ?  137 ILE   A HG13 1 
ATOM   2908 H HG21 A ILE   A 1 137 ? 7.955  -12.138 -4.793  0.84 21.73 ?  137 ILE   A HG21 1 
ATOM   2909 H HG21 B ILE   A 1 137 ? 8.046  -11.946 -5.147  0.16 18.82 ?  137 ILE   A HG21 1 
ATOM   2910 H HG22 A ILE   A 1 137 ? 9.470  -12.436 -5.138  0.84 21.73 ?  137 ILE   A HG22 1 
ATOM   2911 H HG22 B ILE   A 1 137 ? 9.541  -12.352 -4.827  0.16 18.82 ?  137 ILE   A HG22 1 
ATOM   2912 H HG23 A ILE   A 1 137 ? 9.013  -12.289 -3.625  0.84 21.73 ?  137 ILE   A HG23 1 
ATOM   2913 H HG23 B ILE   A 1 137 ? 8.574  -11.906 -3.650  0.16 18.82 ?  137 ILE   A HG23 1 
ATOM   2914 H HD11 A ILE   A 1 137 ? 6.005  -10.073 -4.208  0.84 24.96 ?  137 ILE   A HD11 1 
ATOM   2915 H HD11 B ILE   A 1 137 ? 6.433  -8.778  -5.491  0.16 19.40 ?  137 ILE   A HD11 1 
ATOM   2916 H HD12 A ILE   A 1 137 ? 6.520  -8.968  -5.229  0.84 24.96 ?  137 ILE   A HD12 1 
ATOM   2917 H HD12 B ILE   A 1 137 ? 7.144  -10.044 -6.128  0.16 19.40 ?  137 ILE   A HD12 1 
ATOM   2918 H HD13 A ILE   A 1 137 ? 6.836  -10.494 -5.496  0.84 24.96 ?  137 ILE   A HD13 1 
ATOM   2919 H HD13 B ILE   A 1 137 ? 6.260  -10.209 -4.819  0.16 19.40 ?  137 ILE   A HD13 1 
ATOM   2920 N N    A HIS   A 1 138 ? 12.271 -10.765 -5.359  0.84 15.37 ?  138 HIS   A N    1 
ATOM   2921 N N    B HIS   A 1 138 ? 12.298 -10.635 -5.375  0.16 14.63 ?  138 HIS   A N    1 
ATOM   2922 C CA   A HIS   A 1 138 ? 13.445 -11.516 -5.783  0.84 15.05 ?  138 HIS   A CA   1 
ATOM   2923 C CA   B HIS   A 1 138 ? 13.427 -11.447 -5.816  0.16 14.45 ?  138 HIS   A CA   1 
ATOM   2924 C C    A HIS   A 1 138 ? 14.587 -11.370 -4.784  0.84 14.45 ?  138 HIS   A C    1 
ATOM   2925 C C    B HIS   A 1 138 ? 14.594 -11.346 -4.841  0.16 14.07 ?  138 HIS   A C    1 
ATOM   2926 O O    A HIS   A 1 138 ? 15.249 -12.359 -4.437  0.84 14.90 ?  138 HIS   A O    1 
ATOM   2927 O O    B HIS   A 1 138 ? 15.279 -12.340 -4.574  0.16 14.11 ?  138 HIS   A O    1 
ATOM   2928 C CB   A HIS   A 1 138 ? 13.862 -11.072 -7.183  0.84 15.74 ?  138 HIS   A CB   1 
ATOM   2929 C CB   B HIS   A 1 138 ? 13.845 -11.003 -7.217  0.16 14.82 ?  138 HIS   A CB   1 
ATOM   2930 C CG   A HIS   A 1 138 ? 15.123 -11.714 -7.659  0.84 16.81 ?  138 HIS   A CG   1 
ATOM   2931 C CG   B HIS   A 1 138 ? 15.150 -11.576 -7.669  0.16 15.33 ?  138 HIS   A CG   1 
ATOM   2932 N ND1  A HIS   A 1 138 ? 15.219 -13.065 -7.914  0.84 18.32 ?  138 HIS   A ND1  1 
ATOM   2933 N ND1  B HIS   A 1 138 ? 15.320 -12.915 -7.948  0.16 15.81 ?  138 HIS   A ND1  1 
ATOM   2934 C CD2  A HIS   A 1 138 ? 16.347 -11.194 -7.906  0.84 17.03 ?  138 HIS   A CD2  1 
ATOM   2935 C CD2  B HIS   A 1 138 ? 16.349 -10.989 -7.894  0.16 15.44 ?  138 HIS   A CD2  1 
ATOM   2936 C CE1  A HIS   A 1 138 ? 16.448 -13.348 -8.308  0.84 18.53 ?  138 HIS   A CE1  1 
ATOM   2937 C CE1  B HIS   A 1 138 ? 16.569 -13.128 -8.324  0.16 15.84 ?  138 HIS   A CE1  1 
ATOM   2938 N NE2  A HIS   A 1 138 ? 17.153 -12.231 -8.311  0.84 17.75 ?  138 HIS   A NE2  1 
ATOM   2939 N NE2  B HIS   A 1 138 ? 17.214 -11.976 -8.299  0.16 15.66 ?  138 HIS   A NE2  1 
ATOM   2940 H H    A HIS   A 1 138 ? 12.051 -10.117 -5.888  0.84 18.45 ?  138 HIS   A H    1 
ATOM   2941 H H    B HIS   A 1 138 ? 12.102 -9.984  -5.901  0.16 17.56 ?  138 HIS   A H    1 
ATOM   2942 H HA   A HIS   A 1 138 ? 13.208 -12.453 -5.834  0.84 18.06 ?  138 HIS   A HA   1 
ATOM   2943 H HA   B HIS   A 1 138 ? 13.152 -12.374 -5.862  0.16 17.34 ?  138 HIS   A HA   1 
ATOM   2944 H HB2  A HIS   A 1 138 ? 13.152 -11.304 -7.812  0.84 18.89 ?  138 HIS   A HB2  1 
ATOM   2945 H HB2  B HIS   A 1 138 ? 13.162 -11.284 -7.849  0.16 17.78 ?  138 HIS   A HB2  1 
ATOM   2946 H HB3  A HIS   A 1 138 ? 13.994 -10.112 -7.186  0.84 18.89 ?  138 HIS   A HB3  1 
ATOM   2947 H HB3  B HIS   A 1 138 ? 13.923 -10.036 -7.230  0.16 17.78 ?  138 HIS   A HB3  1 
ATOM   2948 H HD1  A HIS   A 1 138 ? 14.578 -13.633 -7.834  0.84 21.98 ?  138 HIS   A HD1  1 
ATOM   2949 H HD2  A HIS   A 1 138 ? 16.589 -10.299 -7.821  0.84 20.44 ?  138 HIS   A HD2  1 
ATOM   2950 H HD2  B HIS   A 1 138 ? 16.549 -10.086 -7.792  0.16 18.53 ?  138 HIS   A HD2  1 
ATOM   2951 H HE1  A HIS   A 1 138 ? 16.763 -14.188 -8.540  0.84 22.23 ?  138 HIS   A HE1  1 
ATOM   2952 H HE1  B HIS   A 1 138 ? 16.930 -13.950 -8.564  0.16 19.00 ?  138 HIS   A HE1  1 
ATOM   2953 H HE2  B HIS   A 1 138 ? 18.040 -11.861 -8.504  0.16 18.79 ?  138 HIS   A HE2  1 
ATOM   2954 N N    . SER   A 1 139 ? 14.832 -10.151 -4.299  1.00 13.90 ?  139 SER   A N    1 
ATOM   2955 C CA   . SER   A 1 139 ? 15.910 -9.973  -3.336  1.00 13.63 ?  139 SER   A CA   1 
ATOM   2956 C C    . SER   A 1 139 ? 15.695 -10.829 -2.093  1.00 13.41 ?  139 SER   A C    1 
ATOM   2957 O O    . SER   A 1 139 ? 16.646 -11.423 -1.570  1.00 13.25 ?  139 SER   A O    1 
ATOM   2958 C CB   . SER   A 1 139 ? 16.042 -8.498  -2.968  1.00 13.84 ?  139 SER   A CB   1 
ATOM   2959 O OG   . SER   A 1 139 ? 17.138 -8.336  -2.084  1.00 13.68 ?  139 SER   A OG   1 
ATOM   2960 H H    A SER   A 1 139 ? 14.396 -9.436  -4.499  0.84 16.67 ?  139 SER   A H    1 
ATOM   2961 H H    B SER   A 1 139 ? 14.382 -9.437  -4.469  0.16 16.67 ?  139 SER   A H    1 
ATOM   2962 H HA   . SER   A 1 139 ? 16.745 -10.248 -3.744  1.00 16.36 ?  139 SER   A HA   1 
ATOM   2963 H HB2  . SER   A 1 139 ? 16.201 -7.972  -3.771  1.00 16.60 ?  139 SER   A HB2  1 
ATOM   2964 H HB3  . SER   A 1 139 ? 15.230 -8.196  -2.528  1.00 16.60 ?  139 SER   A HB3  1 
ATOM   2965 H HG   . SER   A 1 139 ? 17.225 -7.528  -1.870  1.00 16.41 ?  139 SER   A HG   1 
ATOM   2966 N N    . LEU   A 1 140 ? 14.458 -10.891 -1.597  1.00 13.22 ?  140 LEU   A N    1 
ATOM   2967 C CA   . LEU   A 1 140 ? 14.181 -11.710 -0.422  1.00 13.20 ?  140 LEU   A CA   1 
ATOM   2968 C C    . LEU   A 1 140 ? 14.442 -13.186 -0.710  1.00 13.26 ?  140 LEU   A C    1 
ATOM   2969 O O    . LEU   A 1 140 ? 14.990 -13.909 0.132   1.00 13.86 ?  140 LEU   A O    1 
ATOM   2970 C CB   . LEU   A 1 140 ? 12.738 -11.488 0.031   1.00 13.72 ?  140 LEU   A CB   1 
ATOM   2971 C CG   . LEU   A 1 140 ? 12.272 -12.351 1.201   1.00 13.91 ?  140 LEU   A CG   1 
ATOM   2972 C CD1  . LEU   A 1 140 ? 13.167 -12.173 2.416   1.00 14.22 ?  140 LEU   A CD1  1 
ATOM   2973 C CD2  . LEU   A 1 140 ? 10.812 -12.044 1.551   1.00 15.07 ?  140 LEU   A CD2  1 
ATOM   2974 H H    . LEU   A 1 140 ? 13.776 -10.469 -1.911  1.00 15.86 ?  140 LEU   A H    1 
ATOM   2975 H HA   . LEU   A 1 140 ? 14.765 -11.440 0.302   1.00 15.84 ?  140 LEU   A HA   1 
ATOM   2976 H HB2  . LEU   A 1 140 ? 12.638 -10.567 0.301   1.00 16.46 ?  140 LEU   A HB2  1 
ATOM   2977 H HB3  . LEU   A 1 140 ? 12.150 -11.678 -0.716  1.00 16.46 ?  140 LEU   A HB3  1 
ATOM   2978 H HG   . LEU   A 1 140 ? 12.309 -13.288 0.939   1.00 16.69 ?  140 LEU   A HG   1 
ATOM   2979 H HD11 . LEU   A 1 140 ? 12.778 -12.651 3.167   1.00 17.06 ?  140 LEU   A HD11 1 
ATOM   2980 H HD12 . LEU   A 1 140 ? 14.043 -12.543 2.213   1.00 17.06 ?  140 LEU   A HD12 1 
ATOM   2981 H HD13 . LEU   A 1 140 ? 13.239 -11.233 2.618   1.00 17.06 ?  140 LEU   A HD13 1 
ATOM   2982 H HD21 . LEU   A 1 140 ? 10.538 -12.610 2.296   1.00 18.09 ?  140 LEU   A HD21 1 
ATOM   2983 H HD22 . LEU   A 1 140 ? 10.735 -11.113 1.801   1.00 18.09 ?  140 LEU   A HD22 1 
ATOM   2984 H HD23 . LEU   A 1 140 ? 10.253 -12.231 0.780   1.00 18.09 ?  140 LEU   A HD23 1 
ATOM   2985 N N    . ARG   A 1 141 ? 14.054 -13.648 -1.900  1.00 13.60 ?  141 ARG   A N    1 
ATOM   2986 C CA   . ARG   A 1 141 ? 14.289 -15.037 -2.282  1.00 14.86 ?  141 ARG   A CA   1 
ATOM   2987 C C    . ARG   A 1 141 ? 15.784 -15.350 -2.292  1.00 13.90 ?  141 ARG   A C    1 
ATOM   2988 O O    . ARG   A 1 141 ? 16.232 -16.364 -1.740  1.00 13.93 ?  141 ARG   A O    1 
ATOM   2989 C CB   . ARG   A 1 141 ? 13.673 -15.266 -3.664  1.00 16.76 ?  141 ARG   A CB   1 
ATOM   2990 C CG   . ARG   A 1 141 ? 13.650 -16.697 -4.138  1.00 19.60 ?  141 ARG   A CG   1 
ATOM   2991 C CD   . ARG   A 1 141 ? 12.614 -17.474 -3.387  1.00 21.03 ?  141 ARG   A CD   1 
ATOM   2992 N NE   . ARG   A 1 141 ? 13.222 -18.246 -2.317  1.00 21.13 ?  141 ARG   A NE   1 
ATOM   2993 C CZ   . ARG   A 1 141 ? 12.534 -18.840 -1.351  1.00 21.96 ?  141 ARG   A CZ   1 
ATOM   2994 N NH1  . ARG   A 1 141 ? 11.234 -18.647 -1.209  1.00 21.63 ?  141 ARG   A NH1  1 
ATOM   2995 N NH2  . ARG   A 1 141 ? 13.170 -19.638 -0.499  1.00 23.19 ?  141 ARG   A NH2  1 
ATOM   2996 H H    . ARG   A 1 141 ? 13.650 -13.180 -2.499  1.00 16.31 ?  141 ARG   A H    1 
ATOM   2997 H HA   . ARG   A 1 141 ? 13.857 -15.628 -1.650  1.00 17.83 ?  141 ARG   A HA   1 
ATOM   2998 H HB2  . ARG   A 1 141 ? 12.758 -14.941 -3.652  1.00 20.11 ?  141 ARG   A HB2  1 
ATOM   2999 H HB3  . ARG   A 1 141 ? 14.183 -14.754 -4.313  1.00 20.11 ?  141 ARG   A HB3  1 
ATOM   3000 H HG2  . ARG   A 1 141 ? 13.430 -16.721 -5.084  1.00 23.52 ?  141 ARG   A HG2  1 
ATOM   3001 H HG3  . ARG   A 1 141 ? 14.518 -17.104 -3.985  1.00 23.52 ?  141 ARG   A HG3  1 
ATOM   3002 H HD2  . ARG   A 1 141 ? 11.972 -16.864 -2.989  1.00 25.24 ?  141 ARG   A HD2  1 
ATOM   3003 H HD3  . ARG   A 1 141 ? 12.165 -18.083 -3.994  1.00 25.24 ?  141 ARG   A HD3  1 
ATOM   3004 H HE   . ARG   A 1 141 ? 14.062 -18.419 -2.372  1.00 25.35 ?  141 ARG   A HE   1 
ATOM   3005 H HH11 . ARG   A 1 141 ? 10.806 -18.145 -1.761  1.00 25.96 ?  141 ARG   A HH11 1 
ATOM   3006 H HH12 . ARG   A 1 141 ? 10.807 -19.042 -0.573  1.00 25.96 ?  141 ARG   A HH12 1 
ATOM   3007 H HH21 . ARG   A 1 141 ? 14.019 -19.761 -0.577  1.00 27.83 ?  141 ARG   A HH21 1 
ATOM   3008 H HH22 . ARG   A 1 141 ? 12.740 -20.016 0.142   1.00 27.83 ?  141 ARG   A HH22 1 
ATOM   3009 N N    . VAL   A 1 142 ? 16.580 -14.483 -2.923  1.00 13.29 ?  142 VAL   A N    1 
ATOM   3010 C CA   . VAL   A 1 142 ? 18.026 -14.698 -2.950  1.00 13.35 ?  142 VAL   A CA   1 
ATOM   3011 C C    . VAL   A 1 142 ? 18.597 -14.684 -1.538  1.00 12.72 ?  142 VAL   A C    1 
ATOM   3012 O O    . VAL   A 1 142 ? 19.464 -15.496 -1.195  1.00 13.01 ?  142 VAL   A O    1 
ATOM   3013 C CB   . VAL   A 1 142 ? 18.721 -13.676 -3.869  1.00 13.67 ?  142 VAL   A CB   1 
ATOM   3014 C CG1  . VAL   A 1 142 ? 20.236 -13.884 -3.829  1.00 13.20 ?  142 VAL   A CG1  1 
ATOM   3015 C CG2  . VAL   A 1 142 ? 18.231 -13.817 -5.297  1.00 14.67 ?  142 VAL   A CG2  1 
ATOM   3016 H H    . VAL   A 1 142 ? 16.314 -13.770 -3.337  1.00 15.94 ?  142 VAL   A H    1 
ATOM   3017 H HA   . VAL   A 1 142 ? 18.197 -15.570 -3.327  1.00 16.01 ?  142 VAL   A HA   1 
ATOM   3018 H HB   . VAL   A 1 142 ? 18.532 -12.769 -3.566  1.00 16.41 ?  142 VAL   A HB   1 
ATOM   3019 H HG11 . VAL   A 1 142 ? 20.646 -13.390 -4.559  1.00 15.84 ?  142 VAL   A HG11 1 
ATOM   3020 H HG12 . VAL   A 1 142 ? 20.583 -13.558 -2.981  1.00 15.84 ?  142 VAL   A HG12 1 
ATOM   3021 H HG13 . VAL   A 1 142 ? 20.427 -14.829 -3.923  1.00 15.84 ?  142 VAL   A HG13 1 
ATOM   3022 H HG21 . VAL   A 1 142 ? 18.701 -13.179 -5.858  1.00 17.60 ?  142 VAL   A HG21 1 
ATOM   3023 H HG22 . VAL   A 1 142 ? 18.419 -14.721 -5.599  1.00 17.60 ?  142 VAL   A HG22 1 
ATOM   3024 H HG23 . VAL   A 1 142 ? 17.282 -13.647 -5.320  1.00 17.60 ?  142 VAL   A HG23 1 
ATOM   3025 N N    . CYS   A 1 143 ? 18.132 -13.757 -0.700  1.00 12.44 ?  143 CYS   A N    1 
ATOM   3026 C CA   . CYS   A 1 143 ? 18.590 -13.710 0.684   1.00 12.41 ?  143 CYS   A CA   1 
ATOM   3027 C C    . CYS   A 1 143 ? 18.369 -15.054 1.372   1.00 12.37 ?  143 CYS   A C    1 
ATOM   3028 O O    . CYS   A 1 143 ? 19.294 -15.638 1.946   1.00 12.47 ?  143 CYS   A O    1 
ATOM   3029 C CB   . CYS   A 1 143 ? 17.850 -12.604 1.430   1.00 13.24 ?  143 CYS   A CB   1 
ATOM   3030 S SG   . CYS   A 1 143 ? 18.345 -12.424 3.154   1.00 13.07 ?  143 CYS   A SG   1 
ATOM   3031 H H    . CYS   A 1 143 ? 17.555 -13.154 -0.908  1.00 14.92 ?  143 CYS   A H    1 
ATOM   3032 H HA   . CYS   A 1 143 ? 19.538 -13.518 0.700   1.00 14.89 ?  143 CYS   A HA   1 
ATOM   3033 H HB2  . CYS   A 1 143 ? 18.015 -11.760 0.980   1.00 15.89 ?  143 CYS   A HB2  1 
ATOM   3034 H HB3  . CYS   A 1 143 ? 16.902 -12.798 1.415   1.00 15.89 ?  143 CYS   A HB3  1 
ATOM   3035 H HG   . CYS   A 1 143 ? 17.745 -11.503 3.631   1.00 15.68 ?  143 CYS   A HG   1 
ATOM   3036 N N    . VAL   A 1 144 ? 17.139 -15.561 1.315   1.00 13.25 ?  144 VAL   A N    1 
ATOM   3037 C CA   . VAL   A 1 144 ? 16.803 -16.794 2.014   1.00 14.44 ?  144 VAL   A CA   1 
ATOM   3038 C C    . VAL   A 1 144 ? 17.616 -17.964 1.482   1.00 14.15 ?  144 VAL   A C    1 
ATOM   3039 O O    . VAL   A 1 144 ? 17.989 -18.873 2.235   1.00 14.76 ?  144 VAL   A O    1 
ATOM   3040 C CB   . VAL   A 1 144 ? 15.286 -17.035 1.898   1.00 17.26 ?  144 VAL   A CB   1 
ATOM   3041 C CG1  . VAL   A 1 144 ? 14.923 -18.458 2.257   1.00 19.16 ?  144 VAL   A CG1  1 
ATOM   3042 C CG2  . VAL   A 1 144 ? 14.536 -16.020 2.765   1.00 17.07 ?  144 VAL   A CG2  1 
ATOM   3043 H H    . VAL   A 1 144 ? 16.483 -15.204 0.877   1.00 15.89 ?  144 VAL   A H    1 
ATOM   3044 H HA   . VAL   A 1 144 ? 17.008 -16.685 2.950   1.00 17.32 ?  144 VAL   A HA   1 
ATOM   3045 H HB   . VAL   A 1 144 ? 15.011 -16.885 0.977   1.00 20.71 ?  144 VAL   A HB   1 
ATOM   3046 H HG11 . VAL   A 1 144 ? 13.971 -18.501 2.448   1.00 22.99 ?  144 VAL   A HG11 1 
ATOM   3047 H HG12 . VAL   A 1 144 ? 15.135 -19.037 1.510   1.00 22.99 ?  144 VAL   A HG12 1 
ATOM   3048 H HG13 . VAL   A 1 144 ? 15.427 -18.720 3.041   1.00 22.99 ?  144 VAL   A HG13 1 
ATOM   3049 H HG21 . VAL   A 1 144 ? 13.582 -16.085 2.587   1.00 20.49 ?  144 VAL   A HG21 1 
ATOM   3050 H HG22 . VAL   A 1 144 ? 14.707 -16.205 3.700   1.00 20.49 ?  144 VAL   A HG22 1 
ATOM   3051 H HG23 . VAL   A 1 144 ? 14.842 -15.121 2.546   1.00 20.49 ?  144 VAL   A HG23 1 
ATOM   3052 N N    . ASP   A 1 145 ? 17.877 -17.979 0.179   1.00 14.38 ?  145 ASP   A N    1 
ATOM   3053 C CA   . ASP   A 1 145 ? 18.586 -19.082 -0.458  1.00 14.91 ?  145 ASP   A CA   1 
ATOM   3054 C C    . ASP   A 1 145 ? 20.105 -18.931 -0.419  1.00 14.63 ?  145 ASP   A C    1 
ATOM   3055 O O    . ASP   A 1 145 ? 20.808 -19.821 -0.913  1.00 16.42 ?  145 ASP   A O    1 
ATOM   3056 C CB   . ASP   A 1 145 ? 18.132 -19.220 -1.913  1.00 16.16 ?  145 ASP   A CB   1 
ATOM   3057 C CG   . ASP   A 1 145 ? 16.674 -19.647 -2.040  1.00 18.42 ?  145 ASP   A CG   1 
ATOM   3058 O OD1  . ASP   A 1 145 ? 16.117 -20.208 -1.074  1.00 19.10 ?  145 ASP   A OD1  1 
ATOM   3059 O OD2  . ASP   A 1 145 ? 16.079 -19.420 -3.112  1.00 19.67 -1 145 ASP   A OD2  1 
ATOM   3060 H H    . ASP   A 1 145 ? 17.640 -17.356 -0.367  1.00 17.26 ?  145 ASP   A H    1 
ATOM   3061 H HA   . ASP   A 1 145 ? 18.357 -19.902 0.005   1.00 17.90 ?  145 ASP   A HA   1 
ATOM   3062 H HB2  . ASP   A 1 145 ? 18.246 -18.367 -2.360  1.00 19.39 ?  145 ASP   A HB2  1 
ATOM   3063 H HB3  . ASP   A 1 145 ? 18.671 -19.899 -2.344  1.00 19.39 ?  145 ASP   A HB3  1 
ATOM   3064 N N    . THR   A 1 146 ? 20.633 -17.847 0.147   1.00 12.83 ?  146 THR   A N    1 
ATOM   3065 C CA   . THR   A 1 146 ? 22.072 -17.590 0.153   1.00 12.45 ?  146 THR   A CA   1 
ATOM   3066 C C    . THR   A 1 146 ? 22.631 -17.413 1.554   1.00 12.44 ?  146 THR   A C    1 
ATOM   3067 O O    . THR   A 1 146 ? 23.710 -17.942 1.862   1.00 13.20 ?  146 THR   A O    1 
ATOM   3068 C CB   . THR   A 1 146 ? 22.390 -16.335 -0.684  1.00 12.40 ?  146 THR   A CB   1 
ATOM   3069 O OG1  . THR   A 1 146 ? 21.865 -16.490 -2.002  1.00 12.91 ?  146 THR   A OG1  1 
ATOM   3070 C CG2  . THR   A 1 146 ? 23.893 -16.102 -0.776  1.00 12.92 ?  146 THR   A CG2  1 
ATOM   3071 H H    . THR   A 1 146 ? 20.171 -17.229 0.534   1.00 15.39 ?  146 THR   A H    1 
ATOM   3072 H HA   . THR   A 1 146 ? 22.530 -18.340 -0.252  1.00 14.94 ?  146 THR   A HA   1 
ATOM   3073 H HB   . THR   A 1 146 ? 21.991 -15.558 -0.267  1.00 14.88 ?  146 THR   A HB   1 
ATOM   3074 H HG1  . THR   A 1 146 ? 21.029 -16.575 -1.969  1.00 15.49 ?  146 THR   A HG1  1 
ATOM   3075 H HG21 . THR   A 1 146 ? 24.082 -15.430 -1.448  1.00 15.50 ?  146 THR   A HG21 1 
ATOM   3076 H HG22 . THR   A 1 146 ? 24.235 -15.798 0.079   1.00 15.50 ?  146 THR   A HG22 1 
ATOM   3077 H HG23 . THR   A 1 146 ? 24.341 -16.927 -1.020  1.00 15.50 ?  146 THR   A HG23 1 
ATOM   3078 N N    . VAL   A 1 147 ? 21.952 -16.633 2.392   1.00 12.35 ?  147 VAL   A N    1 
ATOM   3079 C CA   . VAL   A 1 147 ? 22.437 -16.337 3.731   1.00 12.25 ?  147 VAL   A CA   1 
ATOM   3080 C C    . VAL   A 1 147 ? 22.122 -17.511 4.647   1.00 12.53 ?  147 VAL   A C    1 
ATOM   3081 O O    . VAL   A 1 147 ? 20.978 -17.985 4.703   1.00 13.17 ?  147 VAL   A O    1 
ATOM   3082 C CB   . VAL   A 1 147 ? 21.816 -15.032 4.252   1.00 12.46 ?  147 VAL   A CB   1 
ATOM   3083 C CG1  . VAL   A 1 147 ? 22.361 -14.716 5.622   1.00 13.51 ?  147 VAL   A CG1  1 
ATOM   3084 C CG2  . VAL   A 1 147 ? 22.072 -13.880 3.284   1.00 12.55 ?  147 VAL   A CG2  1 
ATOM   3085 H H    . VAL   A 1 147 ? 21.199 -16.265 2.205   1.00 14.81 ?  147 VAL   A H    1 
ATOM   3086 H HA   . VAL   A 1 147 ? 23.400 -16.224 3.701   1.00 14.69 ?  147 VAL   A HA   1 
ATOM   3087 H HB   . VAL   A 1 147 ? 20.859 -15.146 4.334   1.00 14.96 ?  147 VAL   A HB   1 
ATOM   3088 H HG11 . VAL   A 1 147 ? 22.113 -13.814 5.862   1.00 16.21 ?  147 VAL   A HG11 1 
ATOM   3089 H HG12 . VAL   A 1 147 ? 21.984 -15.345 6.263   1.00 16.21 ?  147 VAL   A HG12 1 
ATOM   3090 H HG13 . VAL   A 1 147 ? 23.327 -14.805 5.606   1.00 16.21 ?  147 VAL   A HG13 1 
ATOM   3091 H HG21 . VAL   A 1 147 ? 21.737 -13.057 3.678   1.00 15.05 ?  147 VAL   A HG21 1 
ATOM   3092 H HG22 . VAL   A 1 147 ? 23.024 -13.806 3.123   1.00 15.05 ?  147 VAL   A HG22 1 
ATOM   3093 H HG23 . VAL   A 1 147 ? 21.606 -14.059 2.452   1.00 15.05 ?  147 VAL   A HG23 1 
ATOM   3094 N N    . ARG   A 1 148 ? 23.147 -17.985 5.355   1.00 12.83 ?  148 ARG   A N    1 
ATOM   3095 C CA   . ARG   A 1 148 ? 23.024 -19.068 6.318   1.00 13.02 ?  148 ARG   A CA   1 
ATOM   3096 C C    . ARG   A 1 148 ? 23.151 -18.595 7.755   1.00 13.08 ?  148 ARG   A C    1 
ATOM   3097 O O    . ARG   A 1 148 ? 22.736 -19.314 8.672   1.00 14.72 ?  148 ARG   A O    1 
ATOM   3098 C CB   . ARG   A 1 148 ? 24.065 -20.162 6.035   1.00 13.55 ?  148 ARG   A CB   1 
ATOM   3099 C CG   . ARG   A 1 148 ? 23.904 -20.795 4.665   1.00 15.00 ?  148 ARG   A CG   1 
ATOM   3100 C CD   . ARG   A 1 148 ? 24.979 -21.838 4.368   1.00 15.98 ?  148 ARG   A CD   1 
ATOM   3101 N NE   . ARG   A 1 148 ? 26.318 -21.258 4.388   1.00 15.83 ?  148 ARG   A NE   1 
ATOM   3102 C CZ   . ARG   A 1 148 ? 26.819 -20.504 3.418   1.00 15.06 ?  148 ARG   A CZ   1 
ATOM   3103 N NH1  . ARG   A 1 148 ? 26.139 -20.267 2.307   1.00 15.68 ?  148 ARG   A NH1  1 
ATOM   3104 N NH2  . ARG   A 1 148 ? 28.036 -19.978 3.564   1.00 15.50 ?  148 ARG   A NH2  1 
ATOM   3105 H H    . ARG   A 1 148 ? 23.953 -17.681 5.279   1.00 15.39 ?  148 ARG   A H    1 
ATOM   3106 H HA   . ARG   A 1 148 ? 22.152 -19.466 6.217   1.00 15.62 ?  148 ARG   A HA   1 
ATOM   3107 H HB2  . ARG   A 1 148 ? 24.954 -19.784 6.085   1.00 16.25 ?  148 ARG   A HB2  1 
ATOM   3108 H HB3  . ARG   A 1 148 ? 23.967 -20.868 6.696   1.00 16.25 ?  148 ARG   A HB3  1 
ATOM   3109 H HG2  . ARG   A 1 148 ? 23.037 -21.224 4.619   1.00 18.00 ?  148 ARG   A HG2  1 
ATOM   3110 H HG3  . ARG   A 1 148 ? 23.965 -20.096 3.994   1.00 18.00 ?  148 ARG   A HG3  1 
ATOM   3111 H HD2  . ARG   A 1 148 ? 24.939 -22.537 5.040   1.00 19.17 ?  148 ARG   A HD2  1 
ATOM   3112 H HD3  . ARG   A 1 148 ? 24.818 -22.216 3.486   1.00 19.17 ?  148 ARG   A HD3  1 
ATOM   3113 H HE   . ARG   A 1 148 ? 26.813 -21.418 5.067   1.00 19.00 ?  148 ARG   A HE   1 
ATOM   3114 H HH11 . ARG   A 1 148 ? 25.353 -20.597 2.199   1.00 18.81 ?  148 ARG   A HH11 1 
ATOM   3115 H HH12 . ARG   A 1 148 ? 26.483 -19.771 1.691   1.00 18.81 ?  148 ARG   A HH12 1 
ATOM   3116 H HH21 . ARG   A 1 148 ? 28.481 -20.124 4.282   1.00 18.59 ?  148 ARG   A HH21 1 
ATOM   3117 H HH22 . ARG   A 1 148 ? 28.368 -19.484 2.942   1.00 18.59 ?  148 ARG   A HH22 1 
ATOM   3118 N N    . THR   A 1 149 ? 23.691 -17.399 7.965   1.00 12.90 ?  149 THR   A N    1 
ATOM   3119 C CA   . THR   A 1 149 ? 23.770 -16.806 9.283   1.00 13.25 ?  149 THR   A CA   1 
ATOM   3120 C C    . THR   A 1 149 ? 22.447 -16.107 9.594   1.00 13.11 ?  149 THR   A C    1 
ATOM   3121 O O    . THR   A 1 149 ? 21.506 -16.107 8.791   1.00 13.43 ?  149 THR   A O    1 
ATOM   3122 C CB   . THR   A 1 149 ? 24.973 -15.870 9.345   1.00 13.68 ?  149 THR   A CB   1 
ATOM   3123 O OG1  . THR   A 1 149 ? 24.838 -14.923 8.284   1.00 13.69 ?  149 THR   A OG1  1 
ATOM   3124 C CG2  . THR   A 1 149 ? 26.283 -16.656 9.199   1.00 14.43 ?  149 THR   A CG2  1 
ATOM   3125 H H    . THR   A 1 149 ? 24.029 -16.903 7.343   1.00 15.47 ?  149 THR   A H    1 
ATOM   3126 H HA   . THR   A 1 149 ? 23.894 -17.512 9.937   1.00 15.89 ?  149 THR   A HA   1 
ATOM   3127 H HB   . THR   A 1 149 ? 24.972 -15.407 10.195  1.00 16.42 ?  149 THR   A HB   1 
ATOM   3128 H HG1  . THR   A 1 149 ? 25.493 -14.395 8.287   1.00 16.43 ?  149 THR   A HG1  1 
ATOM   3129 H HG21 . THR   A 1 149 ? 27.038 -16.055 9.260   1.00 17.32 ?  149 THR   A HG21 1 
ATOM   3130 H HG22 . THR   A 1 149 ? 26.351 -17.324 9.902   1.00 17.32 ?  149 THR   A HG22 1 
ATOM   3131 H HG23 . THR   A 1 149 ? 26.307 -17.108 8.338   1.00 17.32 ?  149 THR   A HG23 1 
ATOM   3132 N N    . ASN   A 1 150 ? 22.336 -15.563 10.797  1.00 13.22 ?  150 ASN   A N    1 
ATOM   3133 C CA   . ASN   A 1 150 ? 21.054 -15.058 11.294  1.00 13.76 ?  150 ASN   A CA   1 
ATOM   3134 C C    . ASN   A 1 150 ? 20.865 -13.615 10.841  1.00 13.09 ?  150 ASN   A C    1 
ATOM   3135 O O    . ASN   A 1 150 ? 21.598 -12.719 11.273  1.00 14.71 ?  150 ASN   A O    1 
ATOM   3136 C CB   . ASN   A 1 150 ? 21.009 -15.176 12.813  1.00 16.36 ?  150 ASN   A CB   1 
ATOM   3137 C CG   . ASN   A 1 150 ? 20.867 -16.607 13.269  1.00 20.36 ?  150 ASN   A CG   1 
ATOM   3138 O OD1  . ASN   A 1 150 ? 20.257 -17.423 12.580  1.00 21.76 ?  150 ASN   A OD1  1 
ATOM   3139 N ND2  . ASN   A 1 150 ? 21.443 -16.926 14.420  1.00 22.63 ?  150 ASN   A ND2  1 
ATOM   3140 H H    . ASN   A 1 150 ? 22.986 -15.476 11.351  1.00 15.86 ?  150 ASN   A H    1 
ATOM   3141 H HA   . ASN   A 1 150 ? 20.332 -15.594 10.927  1.00 16.51 ?  150 ASN   A HA   1 
ATOM   3142 H HB2  . ASN   A 1 150 ? 21.834 -14.822 13.184  1.00 19.63 ?  150 ASN   A HB2  1 
ATOM   3143 H HB3  . ASN   A 1 150 ? 20.250 -14.677 13.150  1.00 19.63 ?  150 ASN   A HB3  1 
ATOM   3144 H HD21 . ASN   A 1 150 ? 21.391 -17.734 14.721  1.00 27.15 ?  150 ASN   A HD21 1 
ATOM   3145 H HD22 . ASN   A 1 150 ? 21.864 -16.330 14.875  1.00 27.15 ?  150 ASN   A HD22 1 
ATOM   3146 N N    . VAL   A 1 151 ? 19.882 -13.385 9.975   1.00 12.71 ?  151 VAL   A N    1 
ATOM   3147 C CA   . VAL   A 1 151 ? 19.662 -12.074 9.381   1.00 12.85 ?  151 VAL   A CA   1 
ATOM   3148 C C    . VAL   A 1 151 ? 18.275 -11.563 9.753   1.00 12.89 ?  151 VAL   A C    1 
ATOM   3149 O O    . VAL   A 1 151 ? 17.265 -12.275 9.615   1.00 13.98 ?  151 VAL   A O    1 
ATOM   3150 C CB   . VAL   A 1 151 ? 19.943 -12.062 7.864   1.00 13.98 ?  151 VAL   A CB   1 
ATOM   3151 C CG1  . VAL   A 1 151 ? 19.119 -13.084 7.116   1.00 15.28 ?  151 VAL   A CG1  1 
ATOM   3152 C CG2  . VAL   A 1 151 ? 19.749 -10.658 7.289   1.00 14.41 ?  151 VAL   A CG2  1 
ATOM   3153 H H    . VAL   A 1 151 ? 19.325 -13.987 9.710   1.00 15.25 ?  151 VAL   A H    1 
ATOM   3154 H HA   . VAL   A 1 151 ? 20.299 -11.463 9.773   1.00 15.41 ?  151 VAL   A HA   1 
ATOM   3155 H HB   . VAL   A 1 151 ? 20.877 -12.298 7.724   1.00 16.78 ?  151 VAL   A HB   1 
ATOM   3156 H HG11 . VAL   A 1 151 ? 19.313 -13.024 6.165   1.00 18.34 ?  151 VAL   A HG11 1 
ATOM   3157 H HG12 . VAL   A 1 151 ? 19.348 -13.976 7.437   1.00 18.34 ?  151 VAL   A HG12 1 
ATOM   3158 H HG13 . VAL   A 1 151 ? 18.177 -12.914 7.271   1.00 18.34 ?  151 VAL   A HG13 1 
ATOM   3159 H HG21 . VAL   A 1 151 ? 20.064 -10.647 6.368   1.00 17.29 ?  151 VAL   A HG21 1 
ATOM   3160 H HG22 . VAL   A 1 151 ? 18.808 -10.431 7.316   1.00 17.29 ?  151 VAL   A HG22 1 
ATOM   3161 H HG23 . VAL   A 1 151 ? 20.261 -10.027 7.817   1.00 17.29 ?  151 VAL   A HG23 1 
ATOM   3162 N N    . TYR   A 1 152 ? 18.260 -10.321 10.238  1.00 12.73 ?  152 TYR   A N    1 
ATOM   3163 C CA   . TYR   A 1 152 ? 17.070 -9.584  10.630  1.00 12.39 ?  152 TYR   A CA   1 
ATOM   3164 C C    . TYR   A 1 152 ? 16.872 -8.475  9.607   1.00 12.26 ?  152 TYR   A C    1 
ATOM   3165 O O    . TYR   A 1 152 ? 17.643 -7.507  9.569   1.00 12.31 ?  152 TYR   A O    1 
ATOM   3166 C CB   . TYR   A 1 152 ? 17.250 -9.047  12.050  1.00 13.10 ?  152 TYR   A CB   1 
ATOM   3167 C CG   . TYR   A 1 152 ? 17.209 -10.178 13.044  1.00 13.68 ?  152 TYR   A CG   1 
ATOM   3168 C CD1  . TYR   A 1 152 ? 18.341 -10.933 13.320  1.00 14.91 ?  152 TYR   A CD1  1 
ATOM   3169 C CD2  . TYR   A 1 152 ? 16.027 -10.536 13.668  1.00 13.81 ?  152 TYR   A CD2  1 
ATOM   3170 C CE1  . TYR   A 1 152 ? 18.304 -12.000 14.196  1.00 16.18 ?  152 TYR   A CE1  1 
ATOM   3171 C CE2  . TYR   A 1 152 ? 15.974 -11.613 14.550  1.00 15.02 ?  152 TYR   A CE2  1 
ATOM   3172 C CZ   . TYR   A 1 152 ? 17.118 -12.338 14.809  1.00 15.67 ?  152 TYR   A CZ   1 
ATOM   3173 O OH   . TYR   A 1 152 ? 17.087 -13.413 15.680  1.00 17.75 ?  152 TYR   A OH   1 
ATOM   3174 H H    . TYR   A 1 152 ? 18.977 -9.851  10.334  1.00 15.27 ?  152 TYR   A H    1 
ATOM   3175 H HA   . TYR   A 1 152 ? 16.297 -10.173 10.611  1.00 14.87 ?  152 TYR   A HA   1 
ATOM   3176 H HB2  . TYR   A 1 152 ? 18.111 -8.614  12.121  1.00 15.71 ?  152 TYR   A HB2  1 
ATOM   3177 H HB3  . TYR   A 1 152 ? 16.535 -8.430  12.257  1.00 15.71 ?  152 TYR   A HB3  1 
ATOM   3178 H HD1  . TYR   A 1 152 ? 19.141 -10.712 12.899  1.00 17.89 ?  152 TYR   A HD1  1 
ATOM   3179 H HD2  . TYR   A 1 152 ? 15.246 -10.056 13.487  1.00 16.57 ?  152 TYR   A HD2  1 
ATOM   3180 H HE1  . TYR   A 1 152 ? 19.077 -12.482 14.372  1.00 19.42 ?  152 TYR   A HE1  1 
ATOM   3181 H HE2  . TYR   A 1 152 ? 15.173 -11.832 14.968  1.00 18.03 ?  152 TYR   A HE2  1 
ATOM   3182 H HH   . TYR   A 1 152 ? 16.309 -13.492 15.996  1.00 21.29 ?  152 TYR   A HH   1 
ATOM   3183 N N    . LEU   A 1 153 ? 15.855 -8.640  8.763   1.00 12.16 ?  153 LEU   A N    1 
ATOM   3184 C CA   . LEU   A 1 153 ? 15.586 -7.728  7.661   1.00 12.55 ?  153 LEU   A CA   1 
ATOM   3185 C C    . LEU   A 1 153 ? 14.590 -6.659  8.073   1.00 13.06 ?  153 LEU   A C    1 
ATOM   3186 O O    . LEU   A 1 153 ? 13.501 -6.971  8.574   1.00 14.04 ?  153 LEU   A O    1 
ATOM   3187 C CB   . LEU   A 1 153 ? 15.017 -8.493  6.465   1.00 12.88 ?  153 LEU   A CB   1 
ATOM   3188 C CG   . LEU   A 1 153 ? 15.944 -9.517  5.804   1.00 12.86 ?  153 LEU   A CG   1 
ATOM   3189 C CD1  . LEU   A 1 153 ? 15.154 -10.395 4.848   1.00 13.26 ?  153 LEU   A CD1  1 
ATOM   3190 C CD2  . LEU   A 1 153 ? 17.086 -8.820  5.068   1.00 13.31 ?  153 LEU   A CD2  1 
ATOM   3191 H H    . LEU   A 1 153 ? 15.295 -9.294  8.811   1.00 14.60 ?  153 LEU   A H    1 
ATOM   3192 H HA   . LEU   A 1 153 ? 16.411 -7.302  7.396   1.00 15.06 ?  153 LEU   A HA   1 
ATOM   3193 H HB2  . LEU   A 1 153 ? 14.223 -8.962  6.758   1.00 15.45 ?  153 LEU   A HB2  1 
ATOM   3194 H HB3  . LEU   A 1 153 ? 14.773 -7.840  5.786   1.00 15.45 ?  153 LEU   A HB3  1 
ATOM   3195 H HG   . LEU   A 1 153 ? 16.333 -10.079 6.495   1.00 15.43 ?  153 LEU   A HG   1 
ATOM   3196 H HD11 . LEU   A 1 153 ? 15.734 -11.093 4.514   1.00 15.91 ?  153 LEU   A HD11 1 
ATOM   3197 H HD12 . LEU   A 1 153 ? 14.406 -10.780 5.326   1.00 15.91 ?  153 LEU   A HD12 1 
ATOM   3198 H HD13 . LEU   A 1 153 ? 14.834 -9.846  4.115   1.00 15.91 ?  153 LEU   A HD13 1 
ATOM   3199 H HD21 . LEU   A 1 153 ? 17.655 -9.498  4.673   1.00 15.97 ?  153 LEU   A HD21 1 
ATOM   3200 H HD22 . LEU   A 1 153 ? 16.710 -8.256  4.378   1.00 15.97 ?  153 LEU   A HD22 1 
ATOM   3201 H HD23 . LEU   A 1 153 ? 17.591 -8.289  5.699   1.00 15.97 ?  153 LEU   A HD23 1 
ATOM   3202 N N    A ALA   A 1 154 ? 14.960 -5.405  7.838   0.84 12.96 ?  154 ALA   A N    1 
ATOM   3203 N N    B ALA   A 1 154 ? 14.952 -5.400  7.843   0.16 12.91 ?  154 ALA   A N    1 
ATOM   3204 C CA   A ALA   A 1 154 ? 14.094 -4.257  8.070   0.84 14.00 ?  154 ALA   A CA   1 
ATOM   3205 C CA   B ALA   A 1 154 ? 14.103 -4.256  8.157   0.16 13.21 ?  154 ALA   A CA   1 
ATOM   3206 C C    A ALA   A 1 154 ? 13.603 -3.747  6.724   0.84 13.97 ?  154 ALA   A C    1 
ATOM   3207 C C    B ALA   A 1 154 ? 13.564 -3.689  6.850   0.16 13.49 ?  154 ALA   A C    1 
ATOM   3208 O O    A ALA   A 1 154 ? 14.410 -3.400  5.852   0.84 14.53 ?  154 ALA   A O    1 
ATOM   3209 O O    B ALA   A 1 154 ? 14.330 -3.172  6.029   0.16 13.57 ?  154 ALA   A O    1 
ATOM   3210 C CB   A ALA   A 1 154 ? 14.849 -3.148  8.801   0.84 14.69 ?  154 ALA   A CB   1 
ATOM   3211 C CB   B ALA   A 1 154 ? 14.889 -3.192  8.919   0.16 13.23 ?  154 ALA   A CB   1 
ATOM   3212 H H    A ALA   A 1 154 ? 15.731 -5.190  7.526   0.84 15.55 ?  154 ALA   A H    1 
ATOM   3213 H H    B ALA   A 1 154 ? 15.704 -5.180  7.491   0.16 15.49 ?  154 ALA   A H    1 
ATOM   3214 H HA   A ALA   A 1 154 ? 13.331 -4.518  8.610   0.84 16.80 ?  154 ALA   A HA   1 
ATOM   3215 H HA   B ALA   A 1 154 ? 13.355 -4.543  8.704   0.16 15.85 ?  154 ALA   A HA   1 
ATOM   3216 H HB1  A ALA   A 1 154 ? 14.254 -2.395  8.942   0.84 17.62 ?  154 ALA   A HB1  1 
ATOM   3217 H HB1  B ALA   A 1 154 ? 14.301 -2.444  9.111   0.16 15.88 ?  154 ALA   A HB1  1 
ATOM   3218 H HB2  A ALA   A 1 154 ? 15.167 -3.483  9.654   0.84 17.62 ?  154 ALA   A HB2  1 
ATOM   3219 H HB2  B ALA   A 1 154 ? 15.221 -3.574  9.745   0.16 15.88 ?  154 ALA   A HB2  1 
ATOM   3220 H HB3  A ALA   A 1 154 ? 15.607 -2.869  8.257   0.84 17.62 ?  154 ALA   A HB3  1 
ATOM   3221 H HB3  B ALA   A 1 154 ? 15.632 -2.894  8.369   0.16 15.88 ?  154 ALA   A HB3  1 
ATOM   3222 N N    A VAL   A 1 155 ? 12.284 -3.668  6.576   0.84 14.29 ?  155 VAL   A N    1 
ATOM   3223 N N    B VAL   A 1 155 ? 12.249 -3.777  6.665   0.16 13.94 ?  155 VAL   A N    1 
ATOM   3224 C CA   A VAL   A 1 155 ? 11.634 -3.202  5.358   0.84 15.21 ?  155 VAL   A CA   1 
ATOM   3225 C CA   B VAL   A 1 155 ? 11.579 -3.264  5.476   0.16 14.37 ?  155 VAL   A CA   1 
ATOM   3226 C C    A VAL   A 1 155 ? 10.872 -1.932  5.718   0.84 16.82 ?  155 VAL   A C    1 
ATOM   3227 C C    B VAL   A 1 155 ? 10.960 -1.916  5.821   0.16 15.24 ?  155 VAL   A C    1 
ATOM   3228 O O    A VAL   A 1 155 ? 9.914  -1.985  6.499   0.84 16.78 ?  155 VAL   A O    1 
ATOM   3229 O O    B VAL   A 1 155 ? 10.198 -1.804  6.790   0.16 14.77 ?  155 VAL   A O    1 
ATOM   3230 C CB   A VAL   A 1 155 ? 10.708 -4.271  4.762   0.84 15.18 ?  155 VAL   A CB   1 
ATOM   3231 C CB   B VAL   A 1 155 ? 10.516 -4.254  4.967   0.16 14.33 ?  155 VAL   A CB   1 
ATOM   3232 C CG1  A VAL   A 1 155 ? 9.974  -3.723  3.548   0.84 16.24 ?  155 VAL   A CG1  1 
ATOM   3233 C CG1  B VAL   A 1 155 ? 9.840  -3.717  3.712   0.16 14.62 ?  155 VAL   A CG1  1 
ATOM   3234 C CG2  A VAL   A 1 155 ? 11.522 -5.511  4.379   0.84 15.97 ?  155 VAL   A CG2  1 
ATOM   3235 C CG2  B VAL   A 1 155 ? 11.147 -5.615  4.696   0.16 14.29 ?  155 VAL   A CG2  1 
ATOM   3236 H H    A VAL   A 1 155 ? 11.728 -3.899  7.194   0.84 17.15 ?  155 VAL   A H    1 
ATOM   3237 H H    B VAL   A 1 155 ? 11.712 -4.137  7.231   0.16 16.72 ?  155 VAL   A H    1 
ATOM   3238 H HA   A VAL   A 1 155 ? 12.309 -2.979  4.700   0.84 18.25 ?  155 VAL   A HA   1 
ATOM   3239 H HA   B VAL   A 1 155 ? 12.229 -3.131  4.771   0.16 17.24 ?  155 VAL   A HA   1 
ATOM   3240 H HB   A VAL   A 1 155 ? 10.051 -4.534  5.431   0.84 18.22 ?  155 VAL   A HB   1 
ATOM   3241 H HB   B VAL   A 1 155 ? 9.836  -4.371  5.649   0.16 17.19 ?  155 VAL   A HB   1 
ATOM   3242 H HG11 A VAL   A 1 155 ? 9.556  -4.461  3.077   0.84 19.49 ?  155 VAL   A HG11 1 
ATOM   3243 H HG11 B VAL   A 1 155 ? 9.285  -4.415  3.329   0.16 17.54 ?  155 VAL   A HG11 1 
ATOM   3244 H HG12 A VAL   A 1 155 ? 9.295  -3.095  3.843   0.84 19.49 ?  155 VAL   A HG12 1 
ATOM   3245 H HG12 B VAL   A 1 155 ? 9.291  -2.953  3.949   0.16 17.54 ?  155 VAL   A HG12 1 
ATOM   3246 H HG13 A VAL   A 1 155 ? 10.611 -3.279  2.970   0.84 19.49 ?  155 VAL   A HG13 1 
ATOM   3247 H HG13 B VAL   A 1 155 ? 10.522 -3.452  3.076   0.16 17.54 ?  155 VAL   A HG13 1 
ATOM   3248 H HG21 A VAL   A 1 155 ? 10.932 -6.166  3.977   0.84 19.16 ?  155 VAL   A HG21 1 
ATOM   3249 H HG21 B VAL   A 1 155 ? 10.511 -6.167  4.216   0.16 17.14 ?  155 VAL   A HG21 1 
ATOM   3250 H HG22 A VAL   A 1 155 ? 12.210 -5.252  3.744   0.84 19.16 ?  155 VAL   A HG22 1 
ATOM   3251 H HG22 B VAL   A 1 155 ? 11.947 -5.491  4.160   0.16 17.14 ?  155 VAL   A HG22 1 
ATOM   3252 H HG23 A VAL   A 1 155 ? 11.936 -5.883  5.176   0.84 19.16 ?  155 VAL   A HG23 1 
ATOM   3253 H HG23 B VAL   A 1 155 ? 11.378 -6.032  5.541   0.16 17.14 ?  155 VAL   A HG23 1 
ATOM   3254 N N    A PHE   A 1 156 ? 11.308 -0.794  5.161   0.84 18.01 ?  156 PHE   A N    1 
ATOM   3255 N N    B PHE   A 1 156 ? 11.285 -0.892  5.029   0.16 16.53 ?  156 PHE   A N    1 
ATOM   3256 C CA   A PHE   A 1 156 ? 10.762 0.512   5.538   0.84 19.70 ?  156 PHE   A CA   1 
ATOM   3257 C CA   B PHE   A 1 156 ? 10.847 0.466   5.342   0.16 17.63 ?  156 PHE   A CA   1 
ATOM   3258 C C    A PHE   A 1 156 ? 9.290  0.653   5.162   0.84 20.17 ?  156 PHE   A C    1 
ATOM   3259 C C    B PHE   A 1 156 ? 9.372  0.672   5.016   0.16 18.58 ?  156 PHE   A C    1 
ATOM   3260 O O    A PHE   A 1 156 ? 8.492  1.195   5.938   0.84 21.27 ?  156 PHE   A O    1 
ATOM   3261 O O    B PHE   A 1 156 ? 8.625  1.244   5.818   0.16 18.65 ?  156 PHE   A O    1 
ATOM   3262 C CB   A PHE   A 1 156 ? 11.592 1.607   4.861   0.84 20.67 ?  156 PHE   A CB   1 
ATOM   3263 C CB   B PHE   A 1 156 ? 11.707 1.472   4.575   0.16 17.77 ?  156 PHE   A CB   1 
ATOM   3264 C CG   A PHE   A 1 156 ? 11.136 3.007   5.174   0.84 22.61 ?  156 PHE   A CG   1 
ATOM   3265 C CG   B PHE   A 1 156 ? 11.402 2.909   4.897   0.16 18.02 ?  156 PHE   A CG   1 
ATOM   3266 C CD1  A PHE   A 1 156 ? 11.097 3.452   6.484   0.84 23.67 ?  156 PHE   A CD1  1 
ATOM   3267 C CD1  B PHE   A 1 156 ? 12.000 3.530   5.983   0.16 18.00 ?  156 PHE   A CD1  1 
ATOM   3268 C CD2  A PHE   A 1 156 ? 10.776 3.881   4.159   0.84 23.49 ?  156 PHE   A CD2  1 
ATOM   3269 C CD2  B PHE   A 1 156 ? 10.534 3.644   4.106   0.16 18.33 ?  156 PHE   A CD2  1 
ATOM   3270 C CE1  A PHE   A 1 156 ? 10.686 4.737   6.781   0.84 24.70 ?  156 PHE   A CE1  1 
ATOM   3271 C CE1  B PHE   A 1 156 ? 11.728 4.853   6.281   0.16 18.01 ?  156 PHE   A CE1  1 
ATOM   3272 C CE2  A PHE   A 1 156 ? 10.366 5.173   4.447   0.84 24.57 ?  156 PHE   A CE2  1 
ATOM   3273 C CE2  B PHE   A 1 156 ? 10.258 4.968   4.399   0.16 18.40 ?  156 PHE   A CE2  1 
ATOM   3274 C CZ   A PHE   A 1 156 ? 10.325 5.602   5.761   0.84 25.07 ?  156 PHE   A CZ   1 
ATOM   3275 C CZ   B PHE   A 1 156 ? 10.858 5.573   5.488   0.16 18.18 ?  156 PHE   A CZ   1 
ATOM   3276 H H    A PHE   A 1 156 ? 11.933 -0.756  4.573   0.84 21.61 ?  156 PHE   A H    1 
ATOM   3277 H H    B PHE   A 1 156 ? 11.758 -0.960  4.310   0.16 19.83 ?  156 PHE   A H    1 
ATOM   3278 H HA   A PHE   A 1 156 ? 10.844 0.625   6.497   0.84 23.64 ?  156 PHE   A HA   1 
ATOM   3279 H HA   B PHE   A 1 156 ? 10.975 0.624   6.290   0.16 21.16 ?  156 PHE   A HA   1 
ATOM   3280 H HB2  A PHE   A 1 156 ? 12.514 1.526   5.151   0.84 24.80 ?  156 PHE   A HB2  1 
ATOM   3281 H HB2  B PHE   A 1 156 ? 12.632 1.317   4.805   0.16 21.32 ?  156 PHE   A HB2  1 
ATOM   3282 H HB3  A PHE   A 1 156 ? 11.540 1.488   3.900   0.84 24.80 ?  156 PHE   A HB3  1 
ATOM   3283 H HB3  B PHE   A 1 156 ? 11.576 1.340   3.623   0.16 21.32 ?  156 PHE   A HB3  1 
ATOM   3284 H HD1  A PHE   A 1 156 ? 11.341 2.871   7.173   0.84 28.40 ?  156 PHE   A HD1  1 
ATOM   3285 H HD1  B PHE   A 1 156 ? 12.587 3.048   6.522   0.16 21.60 ?  156 PHE   A HD1  1 
ATOM   3286 H HD2  A PHE   A 1 156 ? 10.803 3.589   3.275   0.84 28.18 ?  156 PHE   A HD2  1 
ATOM   3287 H HD2  B PHE   A 1 156 ? 10.128 3.242   3.372   0.16 21.99 ?  156 PHE   A HD2  1 
ATOM   3288 H HE1  A PHE   A 1 156 ? 10.661 5.022   7.665   0.84 29.63 ?  156 PHE   A HE1  1 
ATOM   3289 H HE1  B PHE   A 1 156 ? 12.133 5.256   7.015   0.16 21.61 ?  156 PHE   A HE1  1 
ATOM   3290 H HE2  A PHE   A 1 156 ? 10.122 5.744   3.759   0.84 29.48 ?  156 PHE   A HE2  1 
ATOM   3291 H HE2  B PHE   A 1 156 ? 9.671  5.451   3.864   0.16 22.08 ?  156 PHE   A HE2  1 
ATOM   3292 H HZ   A PHE   A 1 156 ? 10.049 6.464   5.961   0.84 30.09 ?  156 PHE   A HZ   1 
ATOM   3293 H HZ   B PHE   A 1 156 ? 10.673 6.462   5.687   0.16 21.81 ?  156 PHE   A HZ   1 
ATOM   3294 N N    A ASP   A 1 157 ? 8.919  0.197   3.972   0.84 19.69 ?  157 ASP   A N    1 
ATOM   3295 N N    B ASP   A 1 157 ? 8.941  0.219   3.844   0.16 19.36 ?  157 ASP   A N    1 
ATOM   3296 C CA   A ASP   A 1 157 ? 7.596  0.438   3.410   0.84 20.84 ?  157 ASP   A CA   1 
ATOM   3297 C CA   B ASP   A 1 157 ? 7.583  0.461   3.378   0.16 20.33 ?  157 ASP   A CA   1 
ATOM   3298 C C    A ASP   A 1 157 ? 6.614  -0.629  3.892   0.84 20.85 ?  157 ASP   A C    1 
ATOM   3299 C C    B ASP   A 1 157 ? 6.632  -0.576  3.964   0.16 20.86 ?  157 ASP   A C    1 
ATOM   3300 O O    A ASP   A 1 157 ? 6.809  -1.821  3.629   0.84 19.91 ?  157 ASP   A O    1 
ATOM   3301 O O    B ASP   A 1 157 ? 6.850  -1.784  3.826   0.16 20.72 ?  157 ASP   A O    1 
ATOM   3302 C CB   A ASP   A 1 157 ? 7.701  0.404   1.889   0.84 22.38 ?  157 ASP   A CB   1 
ATOM   3303 C CB   B ASP   A 1 157 ? 7.547  0.405   1.851   0.16 20.87 ?  157 ASP   A CB   1 
ATOM   3304 C CG   A ASP   A 1 157 ? 6.455  0.926   1.221   0.84 24.24 ?  157 ASP   A CG   1 
ATOM   3305 C CG   B ASP   A 1 157 ? 6.199  0.802   1.284   0.16 21.35 ?  157 ASP   A CG   1 
ATOM   3306 O OD1  A ASP   A 1 157 ? 6.244  2.153   1.249   0.84 26.86 ?  157 ASP   A OD1  1 
ATOM   3307 O OD1  B ASP   A 1 157 ? 5.215  0.074   1.522   0.16 21.25 ?  157 ASP   A OD1  1 
ATOM   3308 O OD2  A ASP   A 1 157 ? 5.670  0.108   0.694   0.84 24.09 -1 157 ASP   A OD2  1 
ATOM   3309 O OD2  B ASP   A 1 157 ? 6.122  1.849   0.608   0.16 21.84 -1 157 ASP   A OD2  1 
ATOM   3310 H H    A ASP   A 1 157 ? 9.430  -0.268  3.460   0.84 23.63 ?  157 ASP   A H    1 
ATOM   3311 H H    B ASP   A 1 157 ? 9.421  -0.233  3.298   0.16 23.23 ?  157 ASP   A H    1 
ATOM   3312 H HA   A ASP   A 1 157 ? 7.272  1.308   3.684   0.84 25.00 ?  157 ASP   A HA   1 
ATOM   3313 H HA   B ASP   A 1 157 ? 7.294  1.342   3.660   0.16 24.40 ?  157 ASP   A HA   1 
ATOM   3314 H HB2  A ASP   A 1 157 ? 8.476  0.933   1.617   0.84 26.86 ?  157 ASP   A HB2  1 
ATOM   3315 H HB2  B ASP   A 1 157 ? 8.215  1.010   1.496   0.16 25.04 ?  157 ASP   A HB2  1 
ATOM   3316 H HB3  A ASP   A 1 157 ? 7.824  -0.513  1.598   0.84 26.86 ?  157 ASP   A HB3  1 
ATOM   3317 H HB3  B ASP   A 1 157 ? 7.737  -0.502  1.564   0.16 25.04 ?  157 ASP   A HB3  1 
ATOM   3318 N N    A LYS   A 1 158 ? 5.554  -0.202  4.590   0.84 22.43 ?  158 LYS   A N    1 
ATOM   3319 N N    B LYS   A 1 158 ? 5.572  -0.096  4.619   0.16 21.67 ?  158 LYS   A N    1 
ATOM   3320 C CA   A LYS   A 1 158 ? 4.589  -1.157  5.134   0.84 23.39 ?  158 LYS   A CA   1 
ATOM   3321 C CA   B LYS   A 1 158 ? 4.598  -1.001  5.222   0.16 22.40 ?  158 LYS   A CA   1 
ATOM   3322 C C    A LYS   A 1 158 ? 3.884  -1.923  4.020   0.84 22.59 ?  158 LYS   A C    1 
ATOM   3323 C C    B LYS   A 1 158 ? 3.858  -1.807  4.161   0.16 22.45 ?  158 LYS   A C    1 
ATOM   3324 O O    A LYS   A 1 158 ? 3.712  -3.147  4.106   0.84 22.50 ?  158 LYS   A O    1 
ATOM   3325 O O    B LYS   A 1 158 ? 3.652  -3.016  4.323   0.16 22.53 ?  158 LYS   A O    1 
ATOM   3326 C CB   A LYS   A 1 158 ? 3.581  -0.429  6.029   0.84 24.98 ?  158 LYS   A CB   1 
ATOM   3327 C CB   B LYS   A 1 158 ? 3.618  -0.199  6.079   0.16 23.10 ?  158 LYS   A CB   1 
ATOM   3328 C CG   A LYS   A 1 158 ? 2.375  -1.267  6.466   0.84 26.70 ?  158 LYS   A CG   1 
ATOM   3329 C CG   B LYS   A 1 158 ? 2.368  -0.949  6.508   0.16 23.77 ?  158 LYS   A CG   1 
ATOM   3330 C CD   A LYS   A 1 158 ? 2.770  -2.513  7.259   0.84 27.88 ?  158 LYS   A CD   1 
ATOM   3331 C CD   B LYS   A 1 158 ? 2.692  -2.195  7.315   0.16 24.25 ?  158 LYS   A CD   1 
ATOM   3332 C CE   A LYS   A 1 158 ? 1.528  -3.243  7.768   0.84 28.65 ?  158 LYS   A CE   1 
ATOM   3333 C CE   B LYS   A 1 158 ? 1.574  -2.508  8.285   0.16 24.53 ?  158 LYS   A CE   1 
ATOM   3334 N NZ   A LYS   A 1 158 ? 1.833  -4.571  8.374   0.84 28.82 ?  158 LYS   A NZ   1 
ATOM   3335 N NZ   B LYS   A 1 158 ? 0.237  -2.093  7.771   0.16 24.66 ?  158 LYS   A NZ   1 
ATOM   3336 H H    A LYS   A 1 158 ? 5.387  0.618   4.763   0.84 26.92 ?  158 LYS   A H    1 
ATOM   3337 H H    B LYS   A 1 158 ? 5.399  0.739   4.728   0.16 26.00 ?  158 LYS   A H    1 
ATOM   3338 H HA   A LYS   A 1 158 ? 5.061  -1.799  5.691   0.84 28.06 ?  158 LYS   A HA   1 
ATOM   3339 H HA   B LYS   A 1 158 ? 5.063  -1.622  5.802   0.16 26.88 ?  158 LYS   A HA   1 
ATOM   3340 H HB2  A LYS   A 1 158 ? 4.037  -0.132  6.835   0.84 29.98 ?  158 LYS   A HB2  1 
ATOM   3341 H HB2  B LYS   A 1 158 ? 4.076  0.086   6.887   0.16 27.72 ?  158 LYS   A HB2  1 
ATOM   3342 H HB3  A LYS   A 1 158 ? 3.243  0.345   5.548   0.84 29.98 ?  158 LYS   A HB3  1 
ATOM   3343 H HB3  B LYS   A 1 158 ? 3.331  0.579   5.578   0.16 27.72 ?  158 LYS   A HB3  1 
ATOM   3344 H HG2  A LYS   A 1 158 ? 1.807  -0.721  7.032   0.84 32.03 ?  158 LYS   A HG2  1 
ATOM   3345 H HG2  B LYS   A 1 158 ? 1.836  -0.359  7.064   0.16 28.52 ?  158 LYS   A HG2  1 
ATOM   3346 H HG3  A LYS   A 1 158 ? 1.878  -1.548  5.681   0.84 32.03 ?  158 LYS   A HG3  1 
ATOM   3347 H HG3  B LYS   A 1 158 ? 1.855  -1.218  5.728   0.16 28.52 ?  158 LYS   A HG3  1 
ATOM   3348 H HD2  A LYS   A 1 158 ? 3.268  -3.114  6.685   0.84 33.45 ?  158 LYS   A HD2  1 
ATOM   3349 H HD2  B LYS   A 1 158 ? 2.797  -2.952  6.724   0.16 29.09 ?  158 LYS   A HD2  1 
ATOM   3350 H HD3  A LYS   A 1 158 ? 3.308  -2.249  8.022   0.84 33.45 ?  158 LYS   A HD3  1 
ATOM   3351 H HD3  B LYS   A 1 158 ? 3.504  -2.048  7.827   0.16 29.09 ?  158 LYS   A HD3  1 
ATOM   3352 H HE2  A LYS   A 1 158 ? 1.099  -2.696  8.446   0.84 34.38 ?  158 LYS   A HE2  1 
ATOM   3353 H HE2  B LYS   A 1 158 ? 1.551  -3.459  8.489   0.16 29.44 ?  158 LYS   A HE2  1 
ATOM   3354 H HE3  A LYS   A 1 158 ? 0.920  -3.383  7.026   0.84 34.38 ?  158 LYS   A HE3  1 
ATOM   3355 H HE3  B LYS   A 1 158 ? 1.751  -2.005  9.083   0.16 29.44 ?  158 LYS   A HE3  1 
ATOM   3356 H HZ1  A LYS   A 1 158 ? 1.082  -4.957  8.655   0.84 34.59 ?  158 LYS   A HZ1  1 
ATOM   3357 H HZ1  B LYS   A 1 158 ? -0.408 -2.491  8.234   0.16 29.60 ?  158 LYS   A HZ1  1 
ATOM   3358 H HZ2  A LYS   A 1 158 ? 2.220  -5.099  7.771   0.84 34.59 ?  158 LYS   A HZ2  1 
ATOM   3359 H HZ2  B LYS   A 1 158 ? 0.140  -1.209  7.848   0.16 29.60 ?  158 LYS   A HZ2  1 
ATOM   3360 H HZ3  A LYS   A 1 158 ? 2.383  -4.472  9.066   0.84 34.59 ?  158 LYS   A HZ3  1 
ATOM   3361 H HZ3  B LYS   A 1 158 ? 0.163  -2.319  6.915   0.16 29.60 ?  158 LYS   A HZ3  1 
ATOM   3362 N N    A ASN   A 1 159 ? 3.469  -1.224  2.964   0.84 23.39 ?  159 ASN   A N    1 
ATOM   3363 N N    B ASN   A 1 159 ? 3.446  -1.157  3.070   0.16 22.51 ?  159 ASN   A N    1 
ATOM   3364 C CA   A ASN   A 1 159 ? 2.829  -1.911  1.850   0.84 23.61 ?  159 ASN   A CA   1 
ATOM   3365 C CA   B ASN   A 1 159 ? 2.699  -1.864  2.034   0.16 22.46 ?  159 ASN   A CA   1 
ATOM   3366 C C    A ASN   A 1 159 ? 3.744  -2.986  1.269   0.84 22.30 ?  159 ASN   A C    1 
ATOM   3367 C C    B ASN   A 1 159 ? 3.558  -2.899  1.319   0.16 21.42 ?  159 ASN   A C    1 
ATOM   3368 O O    A ASN   A 1 159 ? 3.309  -4.115  1.014   0.84 21.88 ?  159 ASN   A O    1 
ATOM   3369 O O    B ASN   A 1 159 ? 3.041  -3.935  0.887   0.16 21.39 ?  159 ASN   A O    1 
ATOM   3370 C CB   A ASN   A 1 159 ? 2.384  -0.894  0.797   0.84 25.93 ?  159 ASN   A CB   1 
ATOM   3371 C CB   B ASN   A 1 159 ? 2.102  -0.865  1.043   0.16 23.38 ?  159 ASN   A CB   1 
ATOM   3372 C CG   A ASN   A 1 159 ? 1.157  -0.110  1.231   0.84 28.65 ?  159 ASN   A CG   1 
ATOM   3373 C CG   B ASN   A 1 159 ? 1.025  0.003   1.671   0.16 24.27 ?  159 ASN   A CG   1 
ATOM   3374 O OD1  A ASN   A 1 159 ? 0.261  -0.658  1.871   0.84 29.75 ?  159 ASN   A OD1  1 
ATOM   3375 O OD1  B ASN   A 1 159 ? 0.199  -0.478  2.446   0.16 24.55 ?  159 ASN   A OD1  1 
ATOM   3376 N ND2  A ASN   A 1 159 ? 1.112  1.174   0.889   0.84 30.14 ?  159 ASN   A ND2  1 
ATOM   3377 N ND2  B ASN   A 1 159 ? 1.034  1.289   1.346   0.16 24.76 ?  159 ASN   A ND2  1 
ATOM   3378 H H    A ASN   A 1 159 ? 3.551  -0.374  2.878   0.84 28.07 ?  159 ASN   A H    1 
ATOM   3379 H H    B ASN   A 1 159 ? 3.578  -0.323  2.913   0.16 27.01 ?  159 ASN   A H    1 
ATOM   3380 H HA   A ASN   A 1 159 ? 2.036  -2.355  2.183   0.84 28.32 ?  159 ASN   A HA   1 
ATOM   3381 H HA   B ASN   A 1 159 ? 1.964  -2.336  2.451   0.16 26.95 ?  159 ASN   A HA   1 
ATOM   3382 H HB2  A ASN   A 1 159 ? 3.101  -0.261  0.641   0.84 31.11 ?  159 ASN   A HB2  1 
ATOM   3383 H HB2  B ASN   A 1 159 ? 2.806  -0.286  0.711   0.16 28.06 ?  159 ASN   A HB2  1 
ATOM   3384 H HB3  A ASN   A 1 159 ? 2.165  -1.363  -0.021  0.84 31.11 ?  159 ASN   A HB3  1 
ATOM   3385 H HB3  B ASN   A 1 159 ? 1.700  -1.353  0.305   0.16 28.06 ?  159 ASN   A HB3  1 
ATOM   3386 H HD21 A ASN   A 1 159 ? 0.438  1.656   1.117   0.84 36.17 ?  159 ASN   A HD21 1 
ATOM   3387 H HD21 B ASN   A 1 159 ? 0.451  1.823   1.668   0.16 29.71 ?  159 ASN   A HD21 1 
ATOM   3388 H HD22 A ASN   A 1 159 ? 1.762  1.521   0.449   0.84 36.17 ?  159 ASN   A HD22 1 
ATOM   3389 H HD22 B ASN   A 1 159 ? 1.625  1.591   0.806   0.16 29.71 ?  159 ASN   A HD22 1 
ATOM   3390 N N    A LEU   A 1 160 ? 5.028  -2.673  1.100   0.84 21.14 ?  160 LEU   A N    1 
ATOM   3391 N N    B LEU   A 1 160 ? 4.862  -2.648  1.185   0.16 20.46 ?  160 LEU   A N    1 
ATOM   3392 C CA   A LEU   A 1 160 ? 5.956  -3.672  0.578   0.84 20.02 ?  160 LEU   A CA   1 
ATOM   3393 C CA   B LEU   A 1 160 ? 5.736  -3.637  0.562   0.16 19.41 ?  160 LEU   A CA   1 
ATOM   3394 C C    A LEU   A 1 160 ? 6.151  -4.816  1.564   0.84 19.00 ?  160 LEU   A C    1 
ATOM   3395 C C    B LEU   A 1 160 ? 6.000  -4.808  1.501   0.16 18.76 ?  160 LEU   A C    1 
ATOM   3396 O O    A LEU   A 1 160 ? 6.183  -5.987  1.166   0.84 19.66 ?  160 LEU   A O    1 
ATOM   3397 O O    B LEU   A 1 160 ? 6.119  -5.955  1.054   0.16 18.80 ?  160 LEU   A O    1 
ATOM   3398 C CB   A LEU   A 1 160 ? 7.295  -3.025  0.233   0.84 19.67 ?  160 LEU   A CB   1 
ATOM   3399 C CB   B LEU   A 1 160 ? 7.049  -2.981  0.133   0.16 19.04 ?  160 LEU   A CB   1 
ATOM   3400 C CG   A LEU   A 1 160 ? 8.367  -4.026  -0.200  0.84 20.05 ?  160 LEU   A CG   1 
ATOM   3401 C CG   B LEU   A 1 160 ? 8.113  -3.923  -0.428  0.16 18.76 ?  160 LEU   A CG   1 
ATOM   3402 C CD1  A LEU   A 1 160 ? 7.914  -4.788  -1.430  0.84 20.75 ?  160 LEU   A CD1  1 
ATOM   3403 C CD1  B LEU   A 1 160 ? 7.561  -4.717  -1.602  0.16 18.71 ?  160 LEU   A CD1  1 
ATOM   3404 C CD2  A LEU   A 1 160 ? 9.687  -3.329  -0.459  0.84 20.19 ?  160 LEU   A CD2  1 
ATOM   3405 C CD2  B LEU   A 1 160 ? 9.348  -3.136  -0.835  0.16 18.66 ?  160 LEU   A CD2  1 
ATOM   3406 H H    A LEU   A 1 160 ? 5.385  -1.910  1.293   0.84 25.37 ?  160 LEU   A H    1 
ATOM   3407 H H    B LEU   A 1 160 ? 5.257  -1.927  1.439   0.16 24.54 ?  160 LEU   A H    1 
ATOM   3408 H HA   A LEU   A 1 160 ? 5.585  -4.039  -0.232  0.84 24.02 ?  160 LEU   A HA   1 
ATOM   3409 H HA   B LEU   A 1 160 ? 5.303  -3.981  -0.232  0.16 23.29 ?  160 LEU   A HA   1 
ATOM   3410 H HB2  A LEU   A 1 160 ? 7.163  -2.392  -0.495  0.84 23.60 ?  160 LEU   A HB2  1 
ATOM   3411 H HB2  B LEU   A 1 160 ? 6.856  -2.320  -0.553  0.16 22.85 ?  160 LEU   A HB2  1 
ATOM   3412 H HB3  A LEU   A 1 160 ? 7.630  -2.560  1.014   0.84 23.60 ?  160 LEU   A HB3  1 
ATOM   3413 H HB3  B LEU   A 1 160 ? 7.437  -2.542  0.904   0.16 22.85 ?  160 LEU   A HB3  1 
ATOM   3414 H HG   A LEU   A 1 160 ? 8.513  -4.666  0.512   0.84 24.06 ?  160 LEU   A HG   1 
ATOM   3415 H HG   B LEU   A 1 160 ? 8.379  -4.552  0.261   0.16 22.51 ?  160 LEU   A HG   1 
ATOM   3416 H HD11 A LEU   A 1 160 ? 8.649  -5.329  -1.750  0.84 24.89 ?  160 LEU   A HD11 1 
ATOM   3417 H HD11 B LEU   A 1 160 ? 8.268  -5.266  -1.971  0.16 22.44 ?  160 LEU   A HD11 1 
ATOM   3418 H HD12 A LEU   A 1 160 ? 7.164  -5.357  -1.192  0.84 24.89 ?  160 LEU   A HD12 1 
ATOM   3419 H HD12 B LEU   A 1 160 ? 6.836  -5.282  -1.291  0.16 22.44 ?  160 LEU   A HD12 1 
ATOM   3420 H HD13 A LEU   A 1 160 ? 7.644  -4.154  -2.113  0.84 24.89 ?  160 LEU   A HD13 1 
ATOM   3421 H HD13 B LEU   A 1 160 ? 7.234  -4.100  -2.275  0.16 22.44 ?  160 LEU   A HD13 1 
ATOM   3422 H HD21 A LEU   A 1 160 ? 10.344 -3.991  -0.728  0.84 24.23 ?  160 LEU   A HD21 1 
ATOM   3423 H HD21 B LEU   A 1 160 ? 10.063 -3.757  -1.043  0.16 22.39 ?  160 LEU   A HD21 1 
ATOM   3424 H HD22 A LEU   A 1 160 ? 9.568  -2.675  -1.166  0.84 24.23 ?  160 LEU   A HD22 1 
ATOM   3425 H HD22 B LEU   A 1 160 ? 9.138  -2.599  -1.615  0.16 22.39 ?  160 LEU   A HD22 1 
ATOM   3426 H HD23 A LEU   A 1 160 ? 9.977  -2.888  0.355   0.84 24.23 ?  160 LEU   A HD23 1 
ATOM   3427 H HD23 B LEU   A 1 160 ? 9.613  -2.563  -0.098  0.16 22.39 ?  160 LEU   A HD23 1 
ATOM   3428 N N    A TYR   A 1 161 ? 6.302  -4.497  2.850   0.84 18.08 ?  161 TYR   A N    1 
ATOM   3429 N N    B TYR   A 1 161 ? 6.100  -4.536  2.803   0.16 18.17 ?  161 TYR   A N    1 
ATOM   3430 C CA   A TYR   A 1 161 ? 6.435  -5.541  3.860   0.84 17.67 ?  161 TYR   A CA   1 
ATOM   3431 C CA   B TYR   A 1 161 ? 6.291  -5.604  3.779   0.16 17.73 ?  161 TYR   A CA   1 
ATOM   3432 C C    A TYR   A 1 161 ? 5.286  -6.545  3.770   0.84 18.19 ?  161 TYR   A C    1 
ATOM   3433 C C    B TYR   A 1 161 ? 5.166  -6.631  3.694   0.16 18.00 ?  161 TYR   A C    1 
ATOM   3434 O O    A TYR   A 1 161 ? 5.502  -7.762  3.747   0.84 18.48 ?  161 TYR   A O    1 
ATOM   3435 O O    B TYR   A 1 161 ? 5.415  -7.842  3.673   0.16 17.84 ?  161 TYR   A O    1 
ATOM   3436 C CB   A TYR   A 1 161 ? 6.510  -4.912  5.254   0.84 17.70 ?  161 TYR   A CB   1 
ATOM   3437 C CB   B TYR   A 1 161 ? 6.372  -4.997  5.182   0.16 17.17 ?  161 TYR   A CB   1 
ATOM   3438 C CG   A TYR   A 1 161 ? 6.409  -5.940  6.346   0.84 17.55 ?  161 TYR   A CG   1 
ATOM   3439 C CG   B TYR   A 1 161 ? 6.329  -6.005  6.309   0.16 16.67 ?  161 TYR   A CG   1 
ATOM   3440 C CD1  A TYR   A 1 161 ? 7.527  -6.645  6.762   0.84 17.35 ?  161 TYR   A CD1  1 
ATOM   3441 C CD1  B TYR   A 1 161 ? 7.497  -6.560  6.817   0.16 16.41 ?  161 TYR   A CD1  1 
ATOM   3442 C CD2  A TYR   A 1 161 ? 5.190  -6.223  6.949   0.84 17.61 ?  161 TYR   A CD2  1 
ATOM   3443 C CD2  B TYR   A 1 161 ? 5.120  -6.391  6.875   0.16 16.51 ?  161 TYR   A CD2  1 
ATOM   3444 C CE1  A TYR   A 1 161 ? 7.436  -7.606  7.745   0.84 17.25 ?  161 TYR   A CE1  1 
ATOM   3445 C CE1  B TYR   A 1 161 ? 7.460  -7.479  7.849   0.16 16.28 ?  161 TYR   A CE1  1 
ATOM   3446 C CE2  A TYR   A 1 161 ? 5.090  -7.179  7.936   0.84 17.63 ?  161 TYR   A CE2  1 
ATOM   3447 C CE2  B TYR   A 1 161 ? 5.074  -7.307  7.906   0.16 16.40 ?  161 TYR   A CE2  1 
ATOM   3448 C CZ   A TYR   A 1 161 ? 6.216  -7.869  8.332   0.84 17.61 ?  161 TYR   A CZ   1 
ATOM   3449 C CZ   B TYR   A 1 161 ? 6.246  -7.848  8.389   0.16 16.37 ?  161 TYR   A CZ   1 
ATOM   3450 O OH   A TYR   A 1 161 ? 6.134  -8.830  9.316   0.84 18.65 ?  161 TYR   A OH   1 
ATOM   3451 O OH   B TYR   A 1 161 ? 6.203  -8.762  9.417   0.16 16.61 ?  161 TYR   A OH   1 
ATOM   3452 H H    A TYR   A 1 161 ? 6.323  -3.696  3.160   0.84 21.69 ?  161 TYR   A H    1 
ATOM   3453 H H    B TYR   A 1 161 ? 6.066  -3.749  3.140   0.16 21.80 ?  161 TYR   A H    1 
ATOM   3454 H HA   A TYR   A 1 161 ? 7.260  -6.021  3.713   0.84 21.21 ?  161 TYR   A HA   1 
ATOM   3455 H HA   B TYR   A 1 161 ? 7.129  -6.057  3.598   0.16 21.27 ?  161 TYR   A HA   1 
ATOM   3456 H HB2  A TYR   A 1 161 ? 7.360  -4.453  5.355   0.84 21.23 ?  161 TYR   A HB2  1 
ATOM   3457 H HB2  B TYR   A 1 161 ? 7.206  -4.507  5.259   0.16 20.60 ?  161 TYR   A HB2  1 
ATOM   3458 H HB3  A TYR   A 1 161 ? 5.778  -4.283  5.367   0.84 21.23 ?  161 TYR   A HB3  1 
ATOM   3459 H HB3  B TYR   A 1 161 ? 5.625  -4.392  5.301   0.16 20.60 ?  161 TYR   A HB3  1 
ATOM   3460 H HD1  A TYR   A 1 161 ? 8.350  -6.472  6.369   0.84 20.81 ?  161 TYR   A HD1  1 
ATOM   3461 H HD1  B TYR   A 1 161 ? 8.317  -6.313  6.454   0.16 19.69 ?  161 TYR   A HD1  1 
ATOM   3462 H HD2  A TYR   A 1 161 ? 4.425  -5.763  6.686   0.84 21.13 ?  161 TYR   A HD2  1 
ATOM   3463 H HD2  B TYR   A 1 161 ? 4.327  -6.029  6.552   0.16 19.80 ?  161 TYR   A HD2  1 
ATOM   3464 H HE1  A TYR   A 1 161 ? 8.196  -8.071  8.016   0.84 20.69 ?  161 TYR   A HE1  1 
ATOM   3465 H HE1  B TYR   A 1 161 ? 8.249  -7.844  8.179   0.16 19.54 ?  161 TYR   A HE1  1 
ATOM   3466 H HE2  A TYR   A 1 161 ? 4.262  -7.361  8.334   0.84 21.16 ?  161 TYR   A HE2  1 
ATOM   3467 H HE2  B TYR   A 1 161 ? 4.256  -7.557  8.273   0.16 19.68 ?  161 TYR   A HE2  1 
ATOM   3468 H HH   A TYR   A 1 161 ? 5.332  -8.900  9.589   0.84 22.38 ?  161 TYR   A HH   1 
ATOM   3469 H HH   B TYR   A 1 161 ? 6.979  -9.011  9.615   0.16 19.93 ?  161 TYR   A HH   1 
ATOM   3470 N N    A ASP   A 1 162 ? 4.049  -6.049  3.714   0.84 19.00 ?  162 ASP   A N    1 
ATOM   3471 N N    B ASP   A 1 162 ? 3.917  -6.163  3.642   0.16 18.64 ?  162 ASP   A N    1 
ATOM   3472 C CA   A ASP   A 1 162 ? 2.900  -6.950  3.649   0.84 19.88 ?  162 ASP   A CA   1 
ATOM   3473 C CA   B ASP   A 1 162 ? 2.784  -7.081  3.561   0.16 19.30 ?  162 ASP   A CA   1 
ATOM   3474 C C    A ASP   A 1 162 ? 2.941  -7.798  2.384   0.84 19.80 ?  162 ASP   A C    1 
ATOM   3475 C C    B ASP   A 1 162 ? 2.859  -7.939  2.305   0.16 19.72 ?  162 ASP   A C    1 
ATOM   3476 O O    A ASP   A 1 162 ? 2.593  -8.987  2.409   0.84 20.80 ?  162 ASP   A O    1 
ATOM   3477 O O    B ASP   A 1 162 ? 2.541  -9.134  2.337   0.16 19.62 ?  162 ASP   A O    1 
ATOM   3478 C CB   A ASP   A 1 162 ? 1.595  -6.151  3.710   0.84 21.06 ?  162 ASP   A CB   1 
ATOM   3479 C CB   B ASP   A 1 162 ? 1.472  -6.293  3.588   0.16 19.62 ?  162 ASP   A CB   1 
ATOM   3480 C CG   A ASP   A 1 162 ? 1.292  -5.604  5.088   0.84 22.64 ?  162 ASP   A CG   1 
ATOM   3481 C CG   B ASP   A 1 162 ? 1.264  -5.550  4.891   0.16 20.04 ?  162 ASP   A CG   1 
ATOM   3482 O OD1  A ASP   A 1 162 ? 1.969  -5.984  6.061   0.84 23.65 ?  162 ASP   A OD1  1 
ATOM   3483 O OD1  B ASP   A 1 162 ? 1.806  -5.993  5.925   0.16 20.26 ?  162 ASP   A OD1  1 
ATOM   3484 O OD2  A ASP   A 1 162 ? 0.348  -4.791  5.197   0.84 23.79 -1 162 ASP   A OD2  1 
ATOM   3485 O OD2  B ASP   A 1 162 ? 0.556  -4.522  4.880   0.16 20.24 -1 162 ASP   A OD2  1 
ATOM   3486 H H    A ASP   A 1 162 ? 3.851  -5.214  3.716   0.84 22.80 ?  162 ASP   A H    1 
ATOM   3487 H H    B ASP   A 1 162 ? 3.704  -5.331  3.651   0.16 22.37 ?  162 ASP   A H    1 
ATOM   3488 H HA   A ASP   A 1 162 ? 2.920  -7.551  4.410   0.84 23.85 ?  162 ASP   A HA   1 
ATOM   3489 H HA   B ASP   A 1 162 ? 2.795  -7.670  4.331   0.16 23.16 ?  162 ASP   A HA   1 
ATOM   3490 H HB2  A ASP   A 1 162 ? 1.653  -5.398  3.108   0.84 25.26 ?  162 ASP   A HB2  1 
ATOM   3491 H HB2  B ASP   A 1 162 ? 1.478  -5.636  2.875   0.16 23.54 ?  162 ASP   A HB2  1 
ATOM   3492 H HB3  A ASP   A 1 162 ? 0.857  -6.727  3.465   0.84 25.26 ?  162 ASP   A HB3  1 
ATOM   3493 H HB3  B ASP   A 1 162 ? 0.729  -6.905  3.468   0.16 23.54 ?  162 ASP   A HB3  1 
ATOM   3494 N N    A LYS   A 1 163 ? 3.365  -7.207  1.266   0.84 21.05 ?  163 LYS   A N    1 
ATOM   3495 N N    B LYS   A 1 163 ? 3.276  -7.344  1.186   0.16 20.45 ?  163 LYS   A N    1 
ATOM   3496 C CA   A LYS   A 1 163 ? 3.460  -7.973  0.028   0.84 21.41 ?  163 LYS   A CA   1 
ATOM   3497 C CA   B LYS   A 1 163 ? 3.363  -8.088  -0.065  0.16 20.97 ?  163 LYS   A CA   1 
ATOM   3498 C C    A LYS   A 1 163 ? 4.546  -9.038  0.119   0.84 20.77 ?  163 LYS   A C    1 
ATOM   3499 C C    B LYS   A 1 163 ? 4.485  -9.119  -0.021  0.16 20.01 ?  163 LYS   A C    1 
ATOM   3500 O O    A LYS   A 1 163 ? 4.378  -10.147 -0.399  0.84 21.66 ?  163 LYS   A O    1 
ATOM   3501 O O    B LYS   A 1 163 ? 4.353  -10.212 -0.583  0.16 20.16 ?  163 LYS   A O    1 
ATOM   3502 C CB   A LYS   A 1 163 ? 3.712  -7.038  -1.156  0.84 23.90 ?  163 LYS   A CB   1 
ATOM   3503 C CB   B LYS   A 1 163 ? 3.567  -7.110  -1.219  0.16 22.46 ?  163 LYS   A CB   1 
ATOM   3504 C CG   A LYS   A 1 163 ? 3.799  -7.754  -2.494  0.84 27.17 ?  163 LYS   A CG   1 
ATOM   3505 C CG   B LYS   A 1 163 ? 3.729  -7.743  -2.585  0.16 23.98 ?  163 LYS   A CG   1 
ATOM   3506 C CD   A LYS   A 1 163 ? 4.156  -6.794  -3.616  0.84 30.40 ?  163 LYS   A CD   1 
ATOM   3507 C CD   B LYS   A 1 163 ? 3.651  -6.671  -3.659  0.16 25.35 ?  163 LYS   A CD   1 
ATOM   3508 C CE   A LYS   A 1 163 ? 4.065  -7.472  -4.975  0.84 32.74 ?  163 LYS   A CE   1 
ATOM   3509 C CE   B LYS   A 1 163 ? 4.692  -6.881  -4.741  0.16 26.43 ?  163 LYS   A CE   1 
ATOM   3510 N NZ   A LYS   A 1 163 ? 4.680  -6.649  -6.055  0.84 34.41 ?  163 LYS   A NZ   1 
ATOM   3511 N NZ   B LYS   A 1 163 ? 4.748  -5.735  -5.689  0.16 27.07 ?  163 LYS   A NZ   1 
ATOM   3512 H H    A LYS   A 1 163 ? 3.591  -6.374  1.200   0.84 25.26 ?  163 LYS   A H    1 
ATOM   3513 H H    B LYS   A 1 163 ? 3.506  -6.517  1.128   0.16 24.54 ?  163 LYS   A H    1 
ATOM   3514 H HA   A LYS   A 1 163 ? 2.612  -8.418  -0.123  0.84 25.69 ?  163 LYS   A HA   1 
ATOM   3515 H HA   B LYS   A 1 163 ? 2.527  -8.557  -0.212  0.16 25.16 ?  163 LYS   A HA   1 
ATOM   3516 H HB2  A LYS   A 1 163 ? 2.982  -6.397  -1.213  0.84 28.67 ?  163 LYS   A HB2  1 
ATOM   3517 H HB2  B LYS   A 1 163 ? 2.798  -6.521  -1.262  0.16 26.95 ?  163 LYS   A HB2  1 
ATOM   3518 H HB3  A LYS   A 1 163 ? 4.547  -6.570  -1.015  0.84 28.67 ?  163 LYS   A HB3  1 
ATOM   3519 H HB3  B LYS   A 1 163 ? 4.366  -6.590  -1.044  0.16 26.95 ?  163 LYS   A HB3  1 
ATOM   3520 H HG2  A LYS   A 1 163 ? 4.488  -8.436  -2.452  0.84 32.60 ?  163 LYS   A HG2  1 
ATOM   3521 H HG2  B LYS   A 1 163 ? 4.595  -8.178  -2.643  0.16 28.78 ?  163 LYS   A HG2  1 
ATOM   3522 H HG3  A LYS   A 1 163 ? 2.941  -8.158  -2.699  0.84 32.60 ?  163 LYS   A HG3  1 
ATOM   3523 H HG3  B LYS   A 1 163 ? 3.015  -8.384  -2.734  0.16 28.78 ?  163 LYS   A HG3  1 
ATOM   3524 H HD2  A LYS   A 1 163 ? 3.537  -6.047  -3.608  0.84 36.48 ?  163 LYS   A HD2  1 
ATOM   3525 H HD2  B LYS   A 1 163 ? 2.773  -6.697  -4.072  0.16 30.42 ?  163 LYS   A HD2  1 
ATOM   3526 H HD3  A LYS   A 1 163 ? 5.065  -6.478  -3.491  0.84 36.48 ?  163 LYS   A HD3  1 
ATOM   3527 H HD3  B LYS   A 1 163 ? 3.804  -5.803  -3.254  0.16 30.42 ?  163 LYS   A HD3  1 
ATOM   3528 H HE2  A LYS   A 1 163 ? 4.520  -8.327  -4.938  0.84 39.29 ?  163 LYS   A HE2  1 
ATOM   3529 H HE2  B LYS   A 1 163 ? 5.565  -6.976  -4.329  0.16 31.72 ?  163 LYS   A HE2  1 
ATOM   3530 H HE3  A LYS   A 1 163 ? 3.133  -7.606  -5.198  0.84 39.29 ?  163 LYS   A HE3  1 
ATOM   3531 H HE3  B LYS   A 1 163 ? 4.469  -7.679  -5.244  0.16 31.72 ?  163 LYS   A HE3  1 
ATOM   3532 H HZ1  A LYS   A 1 163 ? 4.613  -7.072  -6.835  0.84 41.28 ?  163 LYS   A HZ1  1 
ATOM   3533 H HZ1  B LYS   A 1 163 ? 5.367  -5.886  -6.310  0.16 32.48 ?  163 LYS   A HZ1  1 
ATOM   3534 H HZ2  A LYS   A 1 163 ? 4.261  -5.866  -6.114  0.84 41.28 ?  163 LYS   A HZ2  1 
ATOM   3535 H HZ2  B LYS   A 1 163 ? 3.959  -5.629  -6.085  0.16 32.48 ?  163 LYS   A HZ2  1 
ATOM   3536 H HZ3  A LYS   A 1 163 ? 5.540  -6.505  -5.877  0.84 41.28 ?  163 LYS   A HZ3  1 
ATOM   3537 H HZ3  B LYS   A 1 163 ? 4.955  -4.988  -5.250  0.16 32.48 ?  163 LYS   A HZ3  1 
ATOM   3538 N N    A LEU   A 1 164 ? 5.671  -8.715  0.762   0.84 19.01 ?  164 LEU   A N    1 
ATOM   3539 N N    B LEU   A 1 164 ? 5.596  -8.788  0.639   0.16 18.92 ?  164 LEU   A N    1 
ATOM   3540 C CA   A LEU   A 1 164 ? 6.760  -9.683  0.891   0.84 18.26 ?  164 LEU   A CA   1 
ATOM   3541 C CA   B LEU   A 1 164 ? 6.700  -9.735  0.760   0.16 18.08 ?  164 LEU   A CA   1 
ATOM   3542 C C    A LEU   A 1 164 ? 6.342  -10.876 1.738   0.84 18.53 ?  164 LEU   A C    1 
ATOM   3543 C C    B LEU   A 1 164 ? 6.307  -10.933 1.615   0.16 17.72 ?  164 LEU   A C    1 
ATOM   3544 O O    A LEU   A 1 164 ? 6.650  -12.025 1.403   0.84 18.79 ?  164 LEU   A O    1 
ATOM   3545 O O    B LEU   A 1 164 ? 6.594  -12.081 1.257   0.16 17.71 ?  164 LEU   A O    1 
ATOM   3546 C CB   A LEU   A 1 164 ? 7.971  -9.005  1.519   0.84 17.65 ?  164 LEU   A CB   1 
ATOM   3547 C CB   B LEU   A 1 164 ? 7.919  -9.032  1.357   0.16 17.70 ?  164 LEU   A CB   1 
ATOM   3548 C CG   A LEU   A 1 164 ? 8.737  -8.040  0.616   0.84 17.75 ?  164 LEU   A CG   1 
ATOM   3549 C CG   B LEU   A 1 164 ? 8.584  -7.974  0.477   0.16 17.37 ?  164 LEU   A CG   1 
ATOM   3550 C CD1  A LEU   A 1 164 ? 9.663  -7.169  1.447   0.84 17.59 ?  164 LEU   A CD1  1 
ATOM   3551 C CD1  B LEU   A 1 164 ? 9.463  -7.059  1.314   0.16 17.09 ?  164 LEU   A CD1  1 
ATOM   3552 C CD2  A LEU   A 1 164 ? 9.527  -8.790  -0.448  0.84 18.00 ?  164 LEU   A CD2  1 
ATOM   3553 C CD2  B LEU   A 1 164 ? 9.397  -8.635  -0.623  0.16 17.39 ?  164 LEU   A CD2  1 
ATOM   3554 H H    A LEU   A 1 164 ? 5.827  -7.947  1.132   0.84 22.81 ?  164 LEU   A H    1 
ATOM   3555 H H    B LEU   A 1 164 ? 5.733  -8.031  1.021   0.16 22.71 ?  164 LEU   A H    1 
ATOM   3556 H HA   A LEU   A 1 164 ? 7.007  -10.000 0.011   0.84 21.91 ?  164 LEU   A HA   1 
ATOM   3557 H HA   B LEU   A 1 164 ? 6.940  -10.060 -0.121  0.16 21.69 ?  164 LEU   A HA   1 
ATOM   3558 H HB2  A LEU   A 1 164 ? 7.678  -8.499  2.292   0.84 21.17 ?  164 LEU   A HB2  1 
ATOM   3559 H HB2  B LEU   A 1 164 ? 7.647  -8.593  2.177   0.16 21.23 ?  164 LEU   A HB2  1 
ATOM   3560 H HB3  A LEU   A 1 164 ? 8.596  -9.690  1.798   0.84 21.17 ?  164 LEU   A HB3  1 
ATOM   3561 H HB3  B LEU   A 1 164 ? 8.591  -9.702  1.557   0.16 21.23 ?  164 LEU   A HB3  1 
ATOM   3562 H HG   A LEU   A 1 164 ? 8.109  -7.454  0.167   0.84 21.30 ?  164 LEU   A HG   1 
ATOM   3563 H HG   B LEU   A 1 164 ? 7.898  -7.431  0.058   0.16 20.84 ?  164 LEU   A HG   1 
ATOM   3564 H HD11 A LEU   A 1 164 ? 10.153 -6.569  0.861   0.84 21.11 ?  164 LEU   A HD11 1 
ATOM   3565 H HD11 B LEU   A 1 164 ? 9.892  -6.413  0.732   0.16 20.51 ?  164 LEU   A HD11 1 
ATOM   3566 H HD12 A LEU   A 1 164 ? 9.138  -6.656  2.081   0.84 21.11 ?  164 LEU   A HD12 1 
ATOM   3567 H HD12 B LEU   A 1 164 ? 8.910  -6.601  1.967   0.16 20.51 ?  164 LEU   A HD12 1 
ATOM   3568 H HD13 A LEU   A 1 164 ? 10.290 -7.739  1.927   0.84 21.11 ?  164 LEU   A HD13 1 
ATOM   3569 H HD13 B LEU   A 1 164 ? 10.134 -7.594  1.767   0.16 20.51 ?  164 LEU   A HD13 1 
ATOM   3570 H HD21 A LEU   A 1 164 ? 10.042 -8.151  -0.969  0.84 21.60 ?  164 LEU   A HD21 1 
ATOM   3571 H HD21 B LEU   A 1 164 ? 9.800  -7.947  -1.174  0.16 20.86 ?  164 LEU   A HD21 1 
ATOM   3572 H HD22 A LEU   A 1 164 ? 10.122 -9.419  -0.015  0.84 21.60 ?  164 LEU   A HD22 1 
ATOM   3573 H HD22 B LEU   A 1 164 ? 10.090 -9.181  -0.217  0.16 20.86 ?  164 LEU   A HD22 1 
ATOM   3574 H HD23 A LEU   A 1 164 ? 8.907  -9.261  -1.025  0.84 21.60 ?  164 LEU   A HD23 1 
ATOM   3575 H HD23 B LEU   A 1 164 ? 8.810  -9.189  -1.160  0.16 20.86 ?  164 LEU   A HD23 1 
ATOM   3576 N N    A VAL   A 1 165 ? 5.650  -10.616 2.844   0.84 17.85 ?  165 VAL   A N    1 
ATOM   3577 N N    B VAL   A 1 165 ? 5.652  -10.685 2.750   0.16 17.38 ?  165 VAL   A N    1 
ATOM   3578 C CA   A VAL   A 1 165 ? 5.175  -11.697 3.700   0.84 17.94 ?  165 VAL   A CA   1 
ATOM   3579 C CA   B VAL   A 1 165 ? 5.249  -11.776 3.631   0.16 17.15 ?  165 VAL   A CA   1 
ATOM   3580 C C    A VAL   A 1 165 ? 4.146  -12.544 2.964   0.84 18.16 ?  165 VAL   A C    1 
ATOM   3581 C C    B VAL   A 1 165 ? 4.159  -12.617 2.977   0.16 17.57 ?  165 VAL   A C    1 
ATOM   3582 O O    A VAL   A 1 165 ? 4.249  -13.776 2.913   0.84 18.21 ?  165 VAL   A O    1 
ATOM   3583 O O    B VAL   A 1 165 ? 4.216  -13.852 2.986   0.16 17.50 ?  165 VAL   A O    1 
ATOM   3584 C CB   A VAL   A 1 165 ? 4.606  -11.111 5.004   0.84 18.25 ?  165 VAL   A CB   1 
ATOM   3585 C CB   B VAL   A 1 165 ? 4.802  -11.225 4.997   0.16 16.72 ?  165 VAL   A CB   1 
ATOM   3586 C CG1  A VAL   A 1 165 ? 3.844  -12.171 5.785   0.84 18.72 ?  165 VAL   A CG1  1 
ATOM   3587 C CG1  B VAL   A 1 165 ? 4.180  -12.331 5.840   0.16 16.54 ?  165 VAL   A CG1  1 
ATOM   3588 C CG2  A VAL   A 1 165 ? 5.717  -10.495 5.844   0.84 18.77 ?  165 VAL   A CG2  1 
ATOM   3589 C CG2  B VAL   A 1 165 ? 5.979  -10.591 5.724   0.16 16.81 ?  165 VAL   A CG2  1 
ATOM   3590 H H    A VAL   A 1 165 ? 5.447  -9.829  3.123   0.84 21.41 ?  165 VAL   A H    1 
ATOM   3591 H H    B VAL   A 1 165 ? 5.435  -9.901  3.027   0.16 20.85 ?  165 VAL   A H    1 
ATOM   3592 H HA   A VAL   A 1 165 ? 5.919  -12.271 3.934   0.84 21.52 ?  165 VAL   A HA   1 
ATOM   3593 H HA   B VAL   A 1 165 ? 6.014  -12.351 3.785   0.16 20.58 ?  165 VAL   A HA   1 
ATOM   3594 H HB   A VAL   A 1 165 ? 3.978  -10.405 4.781   0.84 21.90 ?  165 VAL   A HB   1 
ATOM   3595 H HB   B VAL   A 1 165 ? 4.130  -10.539 4.860   0.16 20.06 ?  165 VAL   A HB   1 
ATOM   3596 H HG11 A VAL   A 1 165 ? 3.741  -11.871 6.703   0.84 22.46 ?  165 VAL   A HG11 1 
ATOM   3597 H HG11 B VAL   A 1 165 ? 4.157  -12.044 6.766   0.16 19.85 ?  165 VAL   A HG11 1 
ATOM   3598 H HG12 A VAL   A 1 165 ? 2.966  -12.293 5.383   0.84 22.46 ?  165 VAL   A HG12 1 
ATOM   3599 H HG12 B VAL   A 1 165 ? 3.278  -12.501 5.525   0.16 19.85 ?  165 VAL   A HG12 1 
ATOM   3600 H HG13 A VAL   A 1 165 ? 4.339  -13.000 5.761   0.84 22.46 ?  165 VAL   A HG13 1 
ATOM   3601 H HG13 B VAL   A 1 165 ? 4.720  -13.132 5.755   0.16 19.85 ?  165 VAL   A HG13 1 
ATOM   3602 H HG21 A VAL   A 1 165 ? 5.336  -10.135 6.661   0.84 22.52 ?  165 VAL   A HG21 1 
ATOM   3603 H HG21 B VAL   A 1 165 ? 5.676  -10.258 6.584   0.16 20.17 ?  165 VAL   A HG21 1 
ATOM   3604 H HG22 A VAL   A 1 165 ? 6.370  -11.180 6.058   0.84 22.52 ?  165 VAL   A HG22 1 
ATOM   3605 H HG22 B VAL   A 1 165 ? 6.668  -11.261 5.852   0.16 20.17 ?  165 VAL   A HG22 1 
ATOM   3606 H HG23 A VAL   A 1 165 ? 6.139  -9.783  5.336   0.84 22.52 ?  165 VAL   A HG23 1 
ATOM   3607 H HG23 B VAL   A 1 165 ? 6.322  -9.859  5.188   0.16 20.17 ?  165 VAL   A HG23 1 
ATOM   3608 N N    A SER   A 1 166 ? 3.135  -11.894 2.385   0.84 18.68 ?  166 SER   A N    1 
ATOM   3609 N N    B SER   A 1 166 ? 3.150  -11.961 2.403   0.16 18.17 ?  166 SER   A N    1 
ATOM   3610 C CA   A SER   A 1 166 ? 2.013  -12.624 1.808   0.84 19.84 ?  166 SER   A CA   1 
ATOM   3611 C CA   B SER   A 1 166 ? 2.008  -12.690 1.861   0.16 18.76 ?  166 SER   A CA   1 
ATOM   3612 C C    A SER   A 1 166 ? 2.409  -13.429 0.583   0.84 20.38 ?  166 SER   A C    1 
ATOM   3613 C C    B SER   A 1 166 ? 2.421  -13.597 0.710   0.16 18.96 ?  166 SER   A C    1 
ATOM   3614 O O    A SER   A 1 166 ? 1.721  -14.401 0.248   0.84 22.24 ?  166 SER   A O    1 
ATOM   3615 O O    B SER   A 1 166 ? 1.878  -14.699 0.554   0.16 19.17 ?  166 SER   A O    1 
ATOM   3616 C CB   A SER   A 1 166 ? 0.886  -11.658 1.426   0.84 21.72 ?  166 SER   A CB   1 
ATOM   3617 C CB   B SER   A 1 166 ? 0.920  -11.710 1.422   0.16 19.30 ?  166 SER   A CB   1 
ATOM   3618 O OG   A SER   A 1 166 ? 0.244  -11.118 2.569   0.84 24.00 ?  166 SER   A OG   1 
ATOM   3619 O OG   B SER   A 1 166 ? 0.490  -10.905 2.508   0.16 19.82 ?  166 SER   A OG   1 
ATOM   3620 H H    A SER   A 1 166 ? 3.071  -11.042 2.318   0.84 22.42 ?  166 SER   A H    1 
ATOM   3621 H H    B SER   A 1 166 ? 3.103  -11.108 2.320   0.16 21.81 ?  166 SER   A H    1 
ATOM   3622 H HA   A SER   A 1 166 ? 1.651  -13.240 2.466   0.84 23.81 ?  166 SER   A HA   1 
ATOM   3623 H HA   B SER   A 1 166 ? 1.638  -13.250 2.555   0.16 22.51 ?  166 SER   A HA   1 
ATOM   3624 H HB2  A SER   A 1 166 ? 1.252  -10.945 0.877   0.84 26.06 ?  166 SER   A HB2  1 
ATOM   3625 H HB2  B SER   A 1 166 ? 1.272  -11.132 0.729   0.16 23.16 ?  166 SER   A HB2  1 
ATOM   3626 H HB3  A SER   A 1 166 ? 0.203  -12.136 0.929   0.84 26.06 ?  166 SER   A HB3  1 
ATOM   3627 H HB3  B SER   A 1 166 ? 0.160  -12.211 1.084   0.16 23.16 ?  166 SER   A HB3  1 
ATOM   3628 H HG   A SER   A 1 166 ? -0.329 -10.548 2.341   0.84 28.80 ?  166 SER   A HG   1 
ATOM   3629 H HG   B SER   A 1 166 ? 1.136  -10.466 2.815   0.16 23.78 ?  166 SER   A HG   1 
ATOM   3630 N N    A SER   A 1 167 ? 3.490  -13.044 -0.094  0.84 19.80 ?  167 SER   A N    1 
ATOM   3631 N N    B SER   A 1 167 ? 3.384  -13.164 -0.100  0.16 19.04 ?  167 SER   A N    1 
ATOM   3632 C CA   A SER   A 1 167 ? 3.949  -13.741 -1.286  0.84 20.62 ?  167 SER   A CA   1 
ATOM   3633 C CA   B SER   A 1 167 ? 3.816  -13.924 -1.264  0.16 19.24 ?  167 SER   A CA   1 
ATOM   3634 C C    A SER   A 1 167 ? 5.099  -14.700 -1.007  0.84 20.60 ?  167 SER   A C    1 
ATOM   3635 C C    B SER   A 1 167 ? 5.038  -14.789 -0.991  0.16 19.56 ?  167 SER   A C    1 
ATOM   3636 O O    A SER   A 1 167 ? 5.598  -15.334 -1.942  0.84 21.69 ?  167 SER   A O    1 
ATOM   3637 O O    B SER   A 1 167 ? 5.541  -15.431 -1.918  0.16 19.82 ?  167 SER   A O    1 
ATOM   3638 C CB   A SER   A 1 167 ? 4.363  -12.732 -2.368  0.84 21.24 ?  167 SER   A CB   1 
ATOM   3639 C CB   B SER   A 1 167 ? 4.098  -12.984 -2.443  0.16 19.15 ?  167 SER   A CB   1 
ATOM   3640 O OG   A SER   A 1 167 ? 5.420  -11.900 -1.913  0.84 21.35 ?  167 SER   A OG   1 
ATOM   3641 O OG   B SER   A 1 167 ? 5.273  -12.224 -2.220  0.16 19.03 ?  167 SER   A OG   1 
ATOM   3642 H H    A SER   A 1 167 ? 3.973  -12.363 0.123   0.84 23.76 ?  167 SER   A H    1 
ATOM   3643 H H    B SER   A 1 167 ? 3.813  -12.425 0.009   0.16 22.85 ?  167 SER   A H    1 
ATOM   3644 H HA   A SER   A 1 167 ? 3.213  -14.256 -1.641  0.84 24.74 ?  167 SER   A HA   1 
ATOM   3645 H HA   B SER   A 1 167 ? 3.097  -14.513 -1.534  0.16 23.09 ?  167 SER   A HA   1 
ATOM   3646 H HB2  A SER   A 1 167 ? 4.665  -13.218 -3.151  0.84 25.48 ?  167 SER   A HB2  1 
ATOM   3647 H HB2  B SER   A 1 167 ? 4.215  -13.512 -3.249  0.16 22.98 ?  167 SER   A HB2  1 
ATOM   3648 H HB3  A SER   A 1 167 ? 3.590  -12.186 -2.603  0.84 25.48 ?  167 SER   A HB3  1 
ATOM   3649 H HB3  B SER   A 1 167 ? 3.346  -12.379 -2.553  0.16 22.98 ?  167 SER   A HB3  1 
ATOM   3650 H HG   A SER   A 1 167 ? 5.157  -11.449 -1.249  0.84 25.61 ?  167 SER   A HG   1 
ATOM   3651 H HG   B SER   A 1 167 ? 5.182  -11.753 -1.530  0.16 22.83 ?  167 SER   A HG   1 
ATOM   3652 N N    . PHE   A 1 168 ? 5.526  -14.830 0.248   1.00 19.73 ?  168 PHE   A N    1 
ATOM   3653 C CA   . PHE   A 1 168 ? 6.699  -15.641 0.554   1.00 20.45 ?  168 PHE   A CA   1 
ATOM   3654 C C    . PHE   A 1 168 ? 6.375  -17.123 0.448   1.00 23.03 ?  168 PHE   A C    1 
ATOM   3655 O O    . PHE   A 1 168 ? 5.402  -17.606 1.038   1.00 24.15 ?  168 PHE   A O    1 
ATOM   3656 C CB   . PHE   A 1 168 ? 7.224  -15.353 1.956   1.00 19.48 ?  168 PHE   A CB   1 
ATOM   3657 C CG   . PHE   A 1 168 ? 8.494  -16.095 2.272   1.00 18.50 ?  168 PHE   A CG   1 
ATOM   3658 C CD1  . PHE   A 1 168 ? 9.677  -15.722 1.671   1.00 18.87 ?  168 PHE   A CD1  1 
ATOM   3659 C CD2  . PHE   A 1 168 ? 8.505  -17.180 3.136   1.00 17.97 ?  168 PHE   A CD2  1 
ATOM   3660 C CE1  . PHE   A 1 168 ? 10.848 -16.398 1.934   1.00 18.41 ?  168 PHE   A CE1  1 
ATOM   3661 C CE2  . PHE   A 1 168 ? 9.682  -17.859 3.403   1.00 18.42 ?  168 PHE   A CE2  1 
ATOM   3662 C CZ   . PHE   A 1 168 ? 10.850 -17.464 2.799   1.00 18.34 ?  168 PHE   A CZ   1 
ATOM   3663 H H    A PHE   A 1 168 ? 5.164  -14.454 0.931   0.84 23.68 ?  168 PHE   A H    1 
ATOM   3664 H H    B PHE   A 1 168 ? 5.203  -14.398 0.918   0.16 23.68 ?  168 PHE   A H    1 
ATOM   3665 H HA   . PHE   A 1 168 ? 7.404  -15.435 -0.083  1.00 24.54 ?  168 PHE   A HA   1 
ATOM   3666 H HB2  . PHE   A 1 168 ? 7.408  -14.403 2.035   1.00 23.37 ?  168 PHE   A HB2  1 
ATOM   3667 H HB3  . PHE   A 1 168 ? 6.553  -15.616 2.603   1.00 23.37 ?  168 PHE   A HB3  1 
ATOM   3668 H HD1  . PHE   A 1 168 ? 9.691  -15.000 1.086   1.00 22.65 ?  168 PHE   A HD1  1 
ATOM   3669 H HD2  . PHE   A 1 168 ? 7.713  -17.451 3.544   1.00 21.57 ?  168 PHE   A HD2  1 
ATOM   3670 H HE1  . PHE   A 1 168 ? 11.648 -16.131 1.531   1.00 22.09 ?  168 PHE   A HE1  1 
ATOM   3671 H HE2  . PHE   A 1 168 ? 9.678  -18.585 3.988   1.00 22.10 ?  168 PHE   A HE2  1 
ATOM   3672 H HZ   . PHE   A 1 168 ? 11.647 -17.919 2.978   1.00 22.00 ?  168 PHE   A HZ   1 
ATOM   3673 N N    . LEU   A 1 169 ? 7.224  -17.851 -0.272  1.00 27.06 ?  169 LEU   A N    1 
ATOM   3674 C CA   . LEU   A 1 169 ? 7.038  -19.281 -0.433  1.00 32.67 ?  169 LEU   A CA   1 
ATOM   3675 C C    . LEU   A 1 169 ? 7.943  -20.025 0.537   1.00 34.70 ?  169 LEU   A C    1 
ATOM   3676 O O    . LEU   A 1 169 ? 7.490  -20.478 1.589   1.00 35.62 ?  169 LEU   A O    1 
ATOM   3677 C CB   . LEU   A 1 169 ? 7.328  -19.705 -1.874  1.00 35.49 ?  169 LEU   A CB   1 
ATOM   3678 C CG   . LEU   A 1 169 ? 7.033  -21.167 -2.218  1.00 37.84 ?  169 LEU   A CG   1 
ATOM   3679 C CD1  . LEU   A 1 169 ? 5.642  -21.565 -1.746  1.00 38.77 ?  169 LEU   A CD1  1 
ATOM   3680 C CD2  . LEU   A 1 169 ? 7.175  -21.401 -3.715  1.00 38.56 ?  169 LEU   A CD2  1 
ATOM   3681 O OXT  . LEU   A 1 169 ? 9.143  -20.173 0.300   1.00 34.93 -1 169 LEU   A OXT  1 
ATOM   3682 H H    . LEU   A 1 169 ? 7.923  -17.539 -0.672  1.00 32.47 ?  169 LEU   A H    1 
ATOM   3683 H HA   . LEU   A 1 169 ? 6.119  -19.501 -0.224  1.00 39.20 ?  169 LEU   A HA   1 
ATOM   3684 H HB2  . LEU   A 1 169 ? 6.792  -19.157 -2.466  1.00 42.58 ?  169 LEU   A HB2  1 
ATOM   3685 H HB3  . LEU   A 1 169 ? 8.268  -19.552 -2.055  1.00 42.58 ?  169 LEU   A HB3  1 
ATOM   3686 H HG   . LEU   A 1 169 ? 7.676  -21.735 -1.766  1.00 45.40 ?  169 LEU   A HG   1 
ATOM   3687 H HD11 . LEU   A 1 169 ? 5.399  -22.409 -2.155  1.00 46.52 ?  169 LEU   A HD11 1 
ATOM   3688 H HD12 . LEU   A 1 169 ? 5.650  -21.657 -0.780  1.00 46.52 ?  169 LEU   A HD12 1 
ATOM   3689 H HD13 . LEU   A 1 169 ? 5.011  -20.876 -2.009  1.00 46.52 ?  169 LEU   A HD13 1 
ATOM   3690 H HD21 . LEU   A 1 169 ? 6.990  -22.333 -3.908  1.00 46.27 ?  169 LEU   A HD21 1 
ATOM   3691 H HD22 . LEU   A 1 169 ? 6.543  -20.834 -4.184  1.00 46.27 ?  169 LEU   A HD22 1 
ATOM   3692 H HD23 . LEU   A 1 169 ? 8.080  -21.180 -3.984  1.00 46.27 ?  169 LEU   A HD23 1 
ATOM   3693 N N    A SER   B 1 1   ? 50.766 -9.231  -23.748 0.84 28.69 ?  1   SER   B N    1 
ATOM   3694 N N    B SER   B 1 1   ? 50.736 -9.239  -23.731 0.16 27.92 ?  1   SER   B N    1 
ATOM   3695 C CA   A SER   B 1 1   ? 51.254 -10.285 -22.837 0.84 28.07 ?  1   SER   B CA   1 
ATOM   3696 C CA   B SER   B 1 1   ? 51.251 -10.259 -22.793 0.16 27.74 ?  1   SER   B CA   1 
ATOM   3697 C C    A SER   B 1 1   ? 50.182 -11.336 -22.587 0.84 26.84 ?  1   SER   B C    1 
ATOM   3698 C C    B SER   B 1 1   ? 50.204 -11.339 -22.570 0.16 27.63 ?  1   SER   B C    1 
ATOM   3699 O O    A SER   B 1 1   ? 48.988 -11.139 -22.866 0.84 26.19 ?  1   SER   B O    1 
ATOM   3700 O O    B SER   B 1 1   ? 49.040 -11.183 -22.943 0.16 27.42 ?  1   SER   B O    1 
ATOM   3701 C CB   A SER   B 1 1   ? 51.711 -9.690  -21.508 0.84 29.07 ?  1   SER   B CB   1 
ATOM   3702 C CB   B SER   B 1 1   ? 51.629 -9.619  -21.461 0.16 28.01 ?  1   SER   B CB   1 
ATOM   3703 O OG   A SER   B 1 1   ? 50.605 -9.416  -20.671 0.84 30.82 ?  1   SER   B OG   1 
ATOM   3704 O OG   B SER   B 1 1   ? 50.490 -9.468  -20.635 0.16 28.28 ?  1   SER   B OG   1 
ATOM   3705 H H1   A SER   B 1 1   ? 50.665 -9.574  -24.560 0.84 34.43 ?  1   SER   B H1   1 
ATOM   3706 H H1   B SER   B 1 1   ? 50.632 -9.610  -24.531 0.16 33.50 ?  1   SER   B H1   1 
ATOM   3707 H H2   A SER   B 1 1   ? 49.991 -8.926  -23.447 0.84 34.43 ?  1   SER   B H2   1 
ATOM   3708 H H2   B SER   B 1 1   ? 49.958 -8.939  -23.432 0.16 33.50 ?  1   SER   B H2   1 
ATOM   3709 H H3   A SER   B 1 1   ? 51.364 -8.574  -23.770 0.84 34.43 ?  1   SER   B H3   1 
ATOM   3710 H H3   B SER   B 1 1   ? 51.321 -8.574  -23.780 0.16 33.50 ?  1   SER   B H3   1 
ATOM   3711 H HA   A SER   B 1 1   ? 52.014 -10.714 -23.255 0.84 33.68 ?  1   SER   B HA   1 
ATOM   3712 H HA   B SER   B 1 1   ? 52.038 -10.664 -23.180 0.16 33.29 ?  1   SER   B HA   1 
ATOM   3713 H HB2  A SER   B 1 1   ? 52.291 -10.329 -21.066 0.84 34.88 ?  1   SER   B HB2  1 
ATOM   3714 H HB2  B SER   B 1 1   ? 52.280 -10.187 -21.022 0.16 33.62 ?  1   SER   B HB2  1 
ATOM   3715 H HB3  A SER   B 1 1   ? 52.192 -8.865  -21.677 0.84 34.88 ?  1   SER   B HB3  1 
ATOM   3716 H HB3  B SER   B 1 1   ? 52.010 -8.743  -21.628 0.16 33.62 ?  1   SER   B HB3  1 
ATOM   3717 H HG   A SER   B 1 1   ? 50.853 -8.950  -20.017 0.84 36.99 ?  1   SER   B HG   1 
ATOM   3718 H HG   B SER   B 1 1   ? 50.671 -8.957  -19.995 0.16 33.94 ?  1   SER   B HG   1 
ATOM   3719 N N    A MET   B 1 2   ? 50.633 -12.456 -22.042 0.84 26.52 ?  2   MET   B N    1 
ATOM   3720 N N    B MET   B 1 2   ? 50.629 -12.435 -21.949 0.16 27.53 ?  2   MET   B N    1 
ATOM   3721 C CA   A MET   B 1 2   ? 49.821 -13.651 -21.869 0.84 26.54 ?  2   MET   B CA   1 
ATOM   3722 C CA   B MET   B 1 2   ? 49.804 -13.625 -21.780 0.16 27.28 ?  2   MET   B CA   1 
ATOM   3723 C C    A MET   B 1 2   ? 49.580 -13.843 -20.379 0.84 24.04 ?  2   MET   B C    1 
ATOM   3724 C C    B MET   B 1 2   ? 49.542 -13.829 -20.296 0.16 25.18 ?  2   MET   B C    1 
ATOM   3725 O O    A MET   B 1 2   ? 50.514 -14.133 -19.626 0.84 24.35 ?  2   MET   B O    1 
ATOM   3726 O O    B MET   B 1 2   ? 50.446 -14.214 -19.547 0.16 25.31 ?  2   MET   B O    1 
ATOM   3727 C CB   A MET   B 1 2   ? 50.563 -14.842 -22.461 0.84 30.48 ?  2   MET   B CB   1 
ATOM   3728 C CB   B MET   B 1 2   ? 50.524 -14.827 -22.373 0.16 29.11 ?  2   MET   B CB   1 
ATOM   3729 C CG   A MET   B 1 2   ? 49.723 -16.088 -22.669 0.84 34.05 ?  2   MET   B CG   1 
ATOM   3730 C CG   B MET   B 1 2   ? 49.623 -15.989 -22.754 0.16 30.71 ?  2   MET   B CG   1 
ATOM   3731 S SD   A MET   B 1 2   ? 50.580 -17.278 -23.716 0.84 37.35 ?  2   MET   B SD   1 
ATOM   3732 S SD   B MET   B 1 2   ? 50.498 -17.179 -23.778 0.16 32.07 ?  2   MET   B SD   1 
ATOM   3733 C CE   A MET   B 1 2   ? 51.124 -16.197 -25.029 0.84 37.62 ?  2   MET   B CE   1 
ATOM   3734 C CE   B MET   B 1 2   ? 51.396 -16.064 -24.851 0.16 32.37 ?  2   MET   B CE   1 
ATOM   3735 H H    A MET   B 1 2   ? 51.439 -12.556 -21.754 0.84 31.82 ?  2   MET   B H    1 
ATOM   3736 H H    B MET   B 1 2   ? 51.419 -12.519 -21.620 0.16 33.03 ?  2   MET   B H    1 
ATOM   3737 H HA   A MET   B 1 2   ? 48.977 -13.554 -22.333 0.84 31.84 ?  2   MET   B HA   1 
ATOM   3738 H HA   B MET   B 1 2   ? 48.966 -13.514 -22.256 0.16 32.74 ?  2   MET   B HA   1 
ATOM   3739 H HB2  A MET   B 1 2   ? 50.916 -14.548 -23.311 0.84 36.58 ?  2   MET   B HB2  1 
ATOM   3740 H HB2  B MET   B 1 2   ? 50.981 -14.493 -23.156 0.16 34.93 ?  2   MET   B HB2  1 
ATOM   3741 H HB3  A MET   B 1 2   ? 51.293 -15.091 -21.878 0.84 36.58 ?  2   MET   B HB3  1 
ATOM   3742 H HB3  B MET   B 1 2   ? 51.172 -15.168 -21.742 0.16 34.93 ?  2   MET   B HB3  1 
ATOM   3743 H HG2  A MET   B 1 2   ? 49.548 -16.502 -21.805 0.84 40.85 ?  2   MET   B HG2  1 
ATOM   3744 H HG2  B MET   B 1 2   ? 49.329 -16.441 -21.946 0.16 36.85 ?  2   MET   B HG2  1 
ATOM   3745 H HG3  A MET   B 1 2   ? 48.890 -15.854 -23.105 0.84 40.85 ?  2   MET   B HG3  1 
ATOM   3746 H HG3  B MET   B 1 2   ? 48.859 -15.666 -23.253 0.16 36.85 ?  2   MET   B HG3  1 
ATOM   3747 H HE1  A MET   B 1 2   ? 51.273 -16.725 -25.816 0.84 45.14 ?  2   MET   B HE1  1 
ATOM   3748 H HE1  B MET   B 1 2   ? 51.660 -16.547 -25.632 0.16 38.84 ?  2   MET   B HE1  1 
ATOM   3749 H HE2  A MET   B 1 2   ? 50.428 -15.538 -25.191 0.84 45.14 ?  2   MET   B HE2  1 
ATOM   3750 H HE2  B MET   B 1 2   ? 50.816 -15.320 -25.097 0.16 38.84 ?  2   MET   B HE2  1 
ATOM   3751 H HE3  A MET   B 1 2   ? 51.946 -15.748 -24.763 0.84 45.14 ?  2   MET   B HE3  1 
ATOM   3752 H HE3  B MET   B 1 2   ? 52.181 -15.730 -24.379 0.16 38.84 ?  2   MET   B HE3  1 
ATOM   3753 N N    A VAL   B 1 3   ? 48.331 -13.664 -19.956 0.84 21.60 ?  3   VAL   B N    1 
ATOM   3754 N N    B VAL   B 1 3   ? 48.309 -13.567 -19.874 0.16 23.02 ?  3   VAL   B N    1 
ATOM   3755 C CA   A VAL   B 1 3   ? 47.919 -13.911 -18.582 0.84 20.29 ?  3   VAL   B CA   1 
ATOM   3756 C CA   B VAL   B 1 3   ? 47.877 -13.823 -18.507 0.16 20.96 ?  3   VAL   B CA   1 
ATOM   3757 C C    A VAL   B 1 3   ? 46.684 -14.802 -18.605 0.84 18.49 ?  3   VAL   B C    1 
ATOM   3758 C C    B VAL   B 1 3   ? 46.630 -14.693 -18.541 0.16 18.81 ?  3   VAL   B C    1 
ATOM   3759 O O    A VAL   B 1 3   ? 45.952 -14.871 -19.594 0.84 19.43 ?  3   VAL   B O    1 
ATOM   3760 O O    B VAL   B 1 3   ? 45.828 -14.631 -19.478 0.16 18.82 ?  3   VAL   B O    1 
ATOM   3761 C CB   A VAL   B 1 3   ? 47.641 -12.606 -17.800 0.84 21.97 ?  3   VAL   B CB   1 
ATOM   3762 C CB   B VAL   B 1 3   ? 47.612 -12.524 -17.714 0.16 21.22 ?  3   VAL   B CB   1 
ATOM   3763 C CG1  A VAL   B 1 3   ? 48.912 -11.755 -17.700 0.84 22.45 ?  3   VAL   B CG1  1 
ATOM   3764 C CG1  B VAL   B 1 3   ? 48.878 -11.684 -17.622 0.16 21.35 ?  3   VAL   B CG1  1 
ATOM   3765 C CG2  A VAL   B 1 3   ? 46.510 -11.823 -18.447 0.84 22.93 ?  3   VAL   B CG2  1 
ATOM   3766 C CG2  B VAL   B 1 3   ? 46.477 -11.735 -18.346 0.16 21.34 ?  3   VAL   B CG2  1 
ATOM   3767 H H    A VAL   B 1 3   ? 47.689 -13.406 -20.465 0.84 25.92 ?  3   VAL   B H    1 
ATOM   3768 H H    B VAL   B 1 3   ? 47.699 -13.230 -20.378 0.16 27.62 ?  3   VAL   B H    1 
ATOM   3769 H HA   A VAL   B 1 3   ? 48.619 -14.394 -18.118 0.84 24.35 ?  3   VAL   B HA   1 
ATOM   3770 H HA   B VAL   B 1 3   ? 48.574 -14.315 -18.049 0.16 25.15 ?  3   VAL   B HA   1 
ATOM   3771 H HB   A VAL   B 1 3   ? 47.369 -12.834 -16.897 0.84 26.36 ?  3   VAL   B HB   1 
ATOM   3772 H HB   B VAL   B 1 3   ? 47.346 -12.763 -16.813 0.16 25.46 ?  3   VAL   B HB   1 
ATOM   3773 H HG11 A VAL   B 1 3   ? 48.712 -10.951 -17.197 0.84 26.93 ?  3   VAL   B HG11 1 
ATOM   3774 H HG11 B VAL   B 1 3   ? 48.689 -10.887 -17.102 0.16 25.62 ?  3   VAL   B HG11 1 
ATOM   3775 H HG12 A VAL   B 1 3   ? 49.598 -12.269 -17.245 0.84 26.93 ?  3   VAL   B HG12 1 
ATOM   3776 H HG12 B VAL   B 1 3   ? 49.572 -12.205 -17.189 0.16 25.62 ?  3   VAL   B HG12 1 
ATOM   3777 H HG13 A VAL   B 1 3   ? 49.207 -11.526 -18.593 0.84 26.93 ?  3   VAL   B HG13 1 
ATOM   3778 H HG13 B VAL   B 1 3   ? 49.159 -11.437 -18.517 0.16 25.62 ?  3   VAL   B HG13 1 
ATOM   3779 H HG21 A VAL   B 1 3   ? 46.463 -10.944 -18.043 0.84 27.52 ?  3   VAL   B HG21 1 
ATOM   3780 H HG21 B VAL   B 1 3   ? 46.432 -10.863 -17.926 0.16 25.60 ?  3   VAL   B HG21 1 
ATOM   3781 H HG22 A VAL   B 1 3   ? 46.684 -11.742 -19.397 0.84 27.52 ?  3   VAL   B HG22 1 
ATOM   3782 H HG22 B VAL   B 1 3   ? 46.650 -11.639 -19.295 0.16 25.60 ?  3   VAL   B HG22 1 
ATOM   3783 H HG23 A VAL   B 1 3   ? 45.674 -12.297 -18.304 0.84 27.52 ?  3   VAL   B HG23 1 
ATOM   3784 H HG23 B VAL   B 1 3   ? 45.644 -12.213 -18.207 0.16 25.60 ?  3   VAL   B HG23 1 
ATOM   3785 N N    . ASN   B 1 4   ? 46.467 -15.504 -17.498 1.00 16.95 ?  4   ASN   B N    1 
ATOM   3786 C CA   . ASN   B 1 4   ? 45.328 -16.416 -17.383 1.00 15.92 ?  4   ASN   B CA   1 
ATOM   3787 C C    . ASN   B 1 4   ? 45.269 -17.384 -18.564 1.00 16.26 ?  4   ASN   B C    1 
ATOM   3788 O O    . ASN   B 1 4   ? 44.206 -17.645 -19.124 1.00 17.22 ?  4   ASN   B O    1 
ATOM   3789 C CB   . ASN   B 1 4   ? 44.009 -15.655 -17.221 1.00 15.52 ?  4   ASN   B CB   1 
ATOM   3790 C CG   . ASN   B 1 4   ? 43.964 -14.846 -15.943 1.00 14.68 ?  4   ASN   B CG   1 
ATOM   3791 O OD1  . ASN   B 1 4   ? 44.259 -15.355 -14.867 1.00 14.35 ?  4   ASN   B OD1  1 
ATOM   3792 N ND2  . ASN   B 1 4   ? 43.620 -13.566 -16.060 1.00 15.33 ?  4   ASN   B ND2  1 
ATOM   3793 H H    A ASN   B 1 4   ? 46.972 -15.482 -16.804 0.84 20.34 ?  4   ASN   B H    1 
ATOM   3794 H H    B ASN   B 1 4   ? 47.006 -15.537 -16.830 0.16 20.34 ?  4   ASN   B H    1 
ATOM   3795 H HA   . ASN   B 1 4   ? 45.453 -16.948 -16.582 1.00 19.11 ?  4   ASN   B HA   1 
ATOM   3796 H HB2  . ASN   B 1 4   ? 43.896 -15.048 -17.966 1.00 18.62 ?  4   ASN   B HB2  1 
ATOM   3797 H HB3  . ASN   B 1 4   ? 43.277 -16.293 -17.197 1.00 18.62 ?  4   ASN   B HB3  1 
ATOM   3798 H HD21 . ASN   B 1 4   ? 43.584 -13.061 -15.361 1.00 18.39 ?  4   ASN   B HD21 1 
ATOM   3799 H HD22 . ASN   B 1 4   ? 43.427 -13.238 -16.832 1.00 18.39 ?  4   ASN   B HD22 1 
ATOM   3800 N N    . SER   B 1 5   ? 46.429 -17.914 -18.950 1.00 17.18 ?  5   SER   B N    1 
ATOM   3801 C CA   . SER   B 1 5   ? 46.526 -18.835 -20.083 1.00 19.54 ?  5   SER   B CA   1 
ATOM   3802 C C    . SER   B 1 5   ? 46.514 -20.268 -19.559 1.00 21.02 ?  5   SER   B C    1 
ATOM   3803 O O    . SER   B 1 5   ? 47.531 -20.957 -19.516 1.00 23.07 ?  5   SER   B O    1 
ATOM   3804 C CB   . SER   B 1 5   ? 47.783 -18.547 -20.901 1.00 20.97 ?  5   SER   B CB   1 
ATOM   3805 O OG   . SER   B 1 5   ? 48.958 -18.768 -20.136 1.00 24.00 ?  5   SER   B OG   1 
ATOM   3806 H H    . SER   B 1 5   ? 47.183 -17.758 -18.568 1.00 20.61 ?  5   SER   B H    1 
ATOM   3807 H HA   . SER   B 1 5   ? 45.760 -18.719 -20.663 1.00 23.45 ?  5   SER   B HA   1 
ATOM   3808 H HB2  . SER   B 1 5   ? 47.799 -19.128 -21.681 1.00 25.16 ?  5   SER   B HB2  1 
ATOM   3809 H HB3  . SER   B 1 5   ? 47.757 -17.620 -21.185 1.00 25.16 ?  5   SER   B HB3  1 
ATOM   3810 H HG   . SER   B 1 5   ? 49.008 -19.578 -19.916 1.00 28.80 ?  5   SER   B HG   1 
ATOM   3811 N N    . PHE   B 1 6   ? 45.328 -20.697 -19.140 1.00 21.76 ?  6   PHE   B N    1 
ATOM   3812 C CA   . PHE   B 1 6   ? 45.147 -22.039 -18.606 1.00 21.33 ?  6   PHE   B CA   1 
ATOM   3813 C C    . PHE   B 1 6   ? 45.079 -23.030 -19.758 1.00 24.52 ?  6   PHE   B C    1 
ATOM   3814 O O    . PHE   B 1 6   ? 44.402 -22.780 -20.759 1.00 26.26 ?  6   PHE   B O    1 
ATOM   3815 C CB   . PHE   B 1 6   ? 43.861 -22.102 -17.782 1.00 19.26 ?  6   PHE   B CB   1 
ATOM   3816 C CG   . PHE   B 1 6   ? 43.883 -21.234 -16.554 1.00 17.39 ?  6   PHE   B CG   1 
ATOM   3817 C CD1  . PHE   B 1 6   ? 44.401 -21.715 -15.363 1.00 16.13 ?  6   PHE   B CD1  1 
ATOM   3818 C CD2  . PHE   B 1 6   ? 43.396 -19.934 -16.593 1.00 16.77 ?  6   PHE   B CD2  1 
ATOM   3819 C CE1  . PHE   B 1 6   ? 44.419 -20.922 -14.227 1.00 15.42 ?  6   PHE   B CE1  1 
ATOM   3820 C CE2  . PHE   B 1 6   ? 43.420 -19.132 -15.465 1.00 16.98 ?  6   PHE   B CE2  1 
ATOM   3821 C CZ   . PHE   B 1 6   ? 43.939 -19.619 -14.282 1.00 15.93 ?  6   PHE   B CZ   1 
ATOM   3822 H H    . PHE   B 1 6   ? 44.607 -20.230 -19.160 1.00 26.11 ?  6   PHE   B H    1 
ATOM   3823 H HA   . PHE   B 1 6   ? 45.894 -22.273 -18.037 1.00 25.60 ?  6   PHE   B HA   1 
ATOM   3824 H HB2  . PHE   B 1 6   ? 43.119 -21.814 -18.335 1.00 23.11 ?  6   PHE   B HB2  1 
ATOM   3825 H HB3  . PHE   B 1 6   ? 43.719 -23.018 -17.493 1.00 23.11 ?  6   PHE   B HB3  1 
ATOM   3826 H HD1  . PHE   B 1 6   ? 44.736 -22.582 -15.322 1.00 19.35 ?  6   PHE   B HD1  1 
ATOM   3827 H HD2  . PHE   B 1 6   ? 43.047 -19.601 -17.387 1.00 20.12 ?  6   PHE   B HD2  1 
ATOM   3828 H HE1  . PHE   B 1 6   ? 44.779 -21.250 -13.432 1.00 18.50 ?  6   PHE   B HE1  1 
ATOM   3829 H HE2  . PHE   B 1 6   ? 43.087 -18.263 -15.504 1.00 20.37 ?  6   PHE   B HE2  1 
ATOM   3830 H HZ   . PHE   B 1 6   ? 43.952 -19.085 -13.521 1.00 19.11 ?  6   PHE   B HZ   1 
ATOM   3831 N N    . SER   B 1 7   ? 45.795 -24.147 -19.620 1.00 25.27 ?  7   SER   B N    1 
ATOM   3832 C CA   . SER   B 1 7   ? 45.895 -25.135 -20.684 1.00 27.57 ?  7   SER   B CA   1 
ATOM   3833 C C    . SER   B 1 7   ? 45.829 -26.539 -20.103 1.00 26.87 ?  7   SER   B C    1 
ATOM   3834 O O    . SER   B 1 7   ? 46.415 -26.817 -19.053 1.00 27.93 ?  7   SER   B O    1 
ATOM   3835 C CB   . SER   B 1 7   ? 47.205 -24.967 -21.467 1.00 30.29 ?  7   SER   B CB   1 
ATOM   3836 O OG   . SER   B 1 7   ? 47.230 -25.807 -22.607 1.00 32.58 ?  7   SER   B OG   1 
ATOM   3837 H H    . SER   B 1 7   ? 46.240 -24.351 -18.910 1.00 30.32 ?  7   SER   B H    1 
ATOM   3838 H HA   . SER   B 1 7   ? 45.156 -25.026 -21.297 1.00 33.08 ?  7   SER   B HA   1 
ATOM   3839 H HB2  . SER   B 1 7   ? 47.283 -24.043 -21.756 1.00 36.35 ?  7   SER   B HB2  1 
ATOM   3840 H HB3  . SER   B 1 7   ? 47.951 -25.195 -20.890 1.00 36.35 ?  7   SER   B HB3  1 
ATOM   3841 H HG   . SER   B 1 7   ? 47.951 -25.704 -23.025 1.00 39.09 ?  7   SER   B HG   1 
ATOM   3842 N N    . GLY   B 1 8   ? 45.113 -27.422 -20.798 1.00 26.51 ?  8   GLY   B N    1 
ATOM   3843 C CA   . GLY   B 1 8   ? 45.068 -28.817 -20.420 1.00 25.75 ?  8   GLY   B CA   1 
ATOM   3844 C C    . GLY   B 1 8   ? 44.126 -29.146 -19.291 1.00 24.53 ?  8   GLY   B C    1 
ATOM   3845 O O    . GLY   B 1 8   ? 44.270 -30.206 -18.670 1.00 26.14 ?  8   GLY   B O    1 
ATOM   3846 H H    . GLY   B 1 8   ? 44.648 -27.225 -21.492 1.00 31.81 ?  8   GLY   B H    1 
ATOM   3847 H HA2  . GLY   B 1 8   ? 44.800 -29.339 -21.191 1.00 30.90 ?  8   GLY   B HA2  1 
ATOM   3848 H HA3  . GLY   B 1 8   ? 45.954 -29.100 -20.156 1.00 30.90 ?  8   GLY   B HA3  1 
ATOM   3849 N N    . TYR   B 1 9   ? 43.144 -28.291 -19.017 1.00 22.55 ?  9   TYR   B N    1 
ATOM   3850 C CA   . TYR   B 1 9   ? 42.187 -28.563 -17.958 1.00 20.79 ?  9   TYR   B CA   1 
ATOM   3851 C C    . TYR   B 1 9   ? 41.000 -29.354 -18.482 1.00 20.21 ?  9   TYR   B C    1 
ATOM   3852 O O    . TYR   B 1 9   ? 40.586 -29.217 -19.637 1.00 21.80 ?  9   TYR   B O    1 
ATOM   3853 C CB   . TYR   B 1 9   ? 41.685 -27.272 -17.314 1.00 20.09 ?  9   TYR   B CB   1 
ATOM   3854 C CG   . TYR   B 1 9   ? 42.705 -26.649 -16.392 1.00 19.34 ?  9   TYR   B CG   1 
ATOM   3855 C CD1  . TYR   B 1 9   ? 43.807 -25.983 -16.906 1.00 19.83 ?  9   TYR   B CD1  1 
ATOM   3856 C CD2  . TYR   B 1 9   ? 42.581 -26.738 -15.014 1.00 18.56 ?  9   TYR   B CD2  1 
ATOM   3857 C CE1  . TYR   B 1 9   ? 44.758 -25.419 -16.075 1.00 20.09 ?  9   TYR   B CE1  1 
ATOM   3858 C CE2  . TYR   B 1 9   ? 43.528 -26.178 -14.173 1.00 18.76 ?  9   TYR   B CE2  1 
ATOM   3859 C CZ   . TYR   B 1 9   ? 44.615 -25.515 -14.711 1.00 19.50 ?  9   TYR   B CZ   1 
ATOM   3860 O OH   . TYR   B 1 9   ? 45.561 -24.965 -13.883 1.00 20.04 ?  9   TYR   B OH   1 
ATOM   3861 H H    . TYR   B 1 9   ? 42.994 -27.560 -19.445 1.00 27.05 ?  9   TYR   B H    1 
ATOM   3862 H HA   . TYR   B 1 9   ? 42.611 -29.091 -17.270 1.00 24.94 ?  9   TYR   B HA   1 
ATOM   3863 H HB2  . TYR   B 1 9   ? 41.468 -26.624 -18.005 1.00 24.11 ?  9   TYR   B HB2  1 
ATOM   3864 H HB3  . TYR   B 1 9   ? 40.900 -27.474 -16.788 1.00 24.11 ?  9   TYR   B HB3  1 
ATOM   3865 H HD1  . TYR   B 1 9   ? 43.911 -25.913 -17.828 1.00 23.80 ?  9   TYR   B HD1  1 
ATOM   3866 H HD2  . TYR   B 1 9   ? 41.848 -27.188 -14.648 1.00 22.27 ?  9   TYR   B HD2  1 
ATOM   3867 H HE1  . TYR   B 1 9   ? 45.486 -24.979 -16.436 1.00 24.10 ?  9   TYR   B HE1  1 
ATOM   3868 H HE2  . TYR   B 1 9   ? 43.423 -26.253 -13.250 1.00 22.51 ?  9   TYR   B HE2  1 
ATOM   3869 H HH   . TYR   B 1 9   ? 46.155 -24.603 -14.345 1.00 24.04 ?  9   TYR   B HH   1 
ATOM   3870 N N    . LEU   B 1 10  ? 40.467 -30.200 -17.609 1.00 18.35 ?  10  LEU   B N    1 
ATOM   3871 C CA   . LEU   B 1 10  ? 39.257 -30.955 -17.883 1.00 18.25 ?  10  LEU   B CA   1 
ATOM   3872 C C    . LEU   B 1 10  ? 38.069 -30.187 -17.316 1.00 17.73 ?  10  LEU   B C    1 
ATOM   3873 O O    . LEU   B 1 10  ? 38.087 -29.772 -16.155 1.00 17.21 ?  10  LEU   B O    1 
ATOM   3874 C CB   . LEU   B 1 10  ? 39.362 -32.329 -17.224 1.00 18.96 ?  10  LEU   B CB   1 
ATOM   3875 C CG   . LEU   B 1 10  ? 38.213 -33.282 -17.542 1.00 20.52 ?  10  LEU   B CG   1 
ATOM   3876 C CD1  . LEU   B 1 10  ? 38.322 -33.792 -18.973 1.00 21.77 ?  10  LEU   B CD1  1 
ATOM   3877 C CD2  . LEU   B 1 10  ? 38.148 -34.430 -16.547 1.00 21.43 ?  10  LEU   B CD2  1 
ATOM   3878 H H    . LEU   B 1 10  ? 40.795 -30.356 -16.828 1.00 22.02 ?  10  LEU   B H    1 
ATOM   3879 H HA   . LEU   B 1 10  ? 39.136 -31.067 -18.836 1.00 21.90 ?  10  LEU   B HA   1 
ATOM   3880 H HB2  . LEU   B 1 10  ? 40.185 -32.752 -17.520 1.00 22.75 ?  10  LEU   B HB2  1 
ATOM   3881 H HB3  . LEU   B 1 10  ? 39.387 -32.213 -16.261 1.00 22.75 ?  10  LEU   B HB3  1 
ATOM   3882 H HG   . LEU   B 1 10  ? 37.381 -32.795 -17.472 1.00 24.62 ?  10  LEU   B HG   1 
ATOM   3883 H HD11 . LEU   B 1 10  ? 37.609 -34.429 -19.133 1.00 26.12 ?  10  LEU   B HD11 1 
ATOM   3884 H HD12 . LEU   B 1 10  ? 38.235 -33.039 -19.580 1.00 26.12 ?  10  LEU   B HD12 1 
ATOM   3885 H HD13 . LEU   B 1 10  ? 39.183 -34.218 -19.092 1.00 26.12 ?  10  LEU   B HD13 1 
ATOM   3886 H HD21 . LEU   B 1 10  ? 37.408 -35.009 -16.787 1.00 25.71 ?  10  LEU   B HD21 1 
ATOM   3887 H HD22 . LEU   B 1 10  ? 38.980 -34.921 -16.577 1.00 25.71 ?  10  LEU   B HD22 1 
ATOM   3888 H HD23 . LEU   B 1 10  ? 38.007 -34.064 -15.659 1.00 25.71 ?  10  LEU   B HD23 1 
ATOM   3889 N N    . LYS   B 1 11  ? 37.044 -29.999 -18.138 1.00 18.76 ?  11  LYS   B N    1 
ATOM   3890 C CA   . LYS   B 1 11  ? 35.848 -29.282 -17.721 1.00 20.90 ?  11  LYS   B CA   1 
ATOM   3891 C C    . LYS   B 1 11  ? 34.963 -30.209 -16.893 1.00 20.15 ?  11  LYS   B C    1 
ATOM   3892 O O    . LYS   B 1 11  ? 34.583 -31.292 -17.355 1.00 21.88 ?  11  LYS   B O    1 
ATOM   3893 C CB   . LYS   B 1 11  ? 35.109 -28.797 -18.967 1.00 24.55 ?  11  LYS   B CB   1 
ATOM   3894 C CG   . LYS   B 1 11  ? 33.939 -27.868 -18.709 1.00 28.11 ?  11  LYS   B CG   1 
ATOM   3895 C CD   . LYS   B 1 11  ? 33.190 -27.586 -20.006 1.00 30.89 ?  11  LYS   B CD   1 
ATOM   3896 C CE   . LYS   B 1 11  ? 32.165 -26.479 -19.835 1.00 32.92 ?  11  LYS   B CE   1 
ATOM   3897 N NZ   . LYS   B 1 11  ? 32.813 -25.157 -19.621 1.00 34.08 ?  11  LYS   B NZ   1 
ATOM   3898 H H    . LYS   B 1 11  ? 37.014 -30.284 -18.947 1.00 22.51 ?  11  LYS   B H    1 
ATOM   3899 H HA   . LYS   B 1 11  ? 36.096 -28.513 -17.182 1.00 25.08 ?  11  LYS   B HA   1 
ATOM   3900 H HB2  . LYS   B 1 11  ? 35.738 -28.320 -19.532 1.00 29.46 ?  11  LYS   B HB2  1 
ATOM   3901 H HB3  . LYS   B 1 11  ? 34.768 -29.569 -19.442 1.00 29.46 ?  11  LYS   B HB3  1 
ATOM   3902 H HG2  . LYS   B 1 11  ? 33.325 -28.285 -18.086 1.00 33.72 ?  11  LYS   B HG2  1 
ATOM   3903 H HG3  . LYS   B 1 11  ? 34.265 -27.027 -18.354 1.00 33.72 ?  11  LYS   B HG3  1 
ATOM   3904 H HD2  . LYS   B 1 11  ? 33.824 -27.311 -20.688 1.00 37.06 ?  11  LYS   B HD2  1 
ATOM   3905 H HD3  . LYS   B 1 11  ? 32.726 -28.391 -20.288 1.00 37.06 ?  11  LYS   B HD3  1 
ATOM   3906 H HE2  . LYS   B 1 11  ? 31.618 -26.424 -20.634 1.00 39.51 ?  11  LYS   B HE2  1 
ATOM   3907 H HE3  . LYS   B 1 11  ? 31.612 -26.678 -19.064 1.00 39.51 ?  11  LYS   B HE3  1 
ATOM   3908 H HZ1  . LYS   B 1 11  ? 32.192 -24.523 -19.546 1.00 40.89 ?  11  LYS   B HZ1  1 
ATOM   3909 H HZ2  . LYS   B 1 11  ? 33.301 -25.174 -18.877 1.00 40.89 ?  11  LYS   B HZ2  1 
ATOM   3910 H HZ3  . LYS   B 1 11  ? 33.342 -24.963 -20.310 1.00 40.89 ?  11  LYS   B HZ3  1 
ATOM   3911 N N    . LEU   B 1 12  ? 34.632 -29.788 -15.672 1.00 18.29 ?  12  LEU   B N    1 
ATOM   3912 C CA   . LEU   B 1 12  ? 33.673 -30.495 -14.828 1.00 17.94 ?  12  LEU   B CA   1 
ATOM   3913 C C    . LEU   B 1 12  ? 32.281 -29.889 -14.915 1.00 17.70 ?  12  LEU   B C    1 
ATOM   3914 O O    . LEU   B 1 12  ? 31.297 -30.606 -15.090 1.00 18.18 ?  12  LEU   B O    1 
ATOM   3915 C CB   . LEU   B 1 12  ? 34.141 -30.515 -13.367 1.00 17.36 ?  12  LEU   B CB   1 
ATOM   3916 C CG   . LEU   B 1 12  ? 35.483 -31.193 -13.091 1.00 17.57 ?  12  LEU   B CG   1 
ATOM   3917 C CD1  . LEU   B 1 12  ? 35.812 -31.156 -11.609 1.00 17.63 ?  12  LEU   B CD1  1 
ATOM   3918 C CD2  . LEU   B 1 12  ? 35.481 -32.625 -13.603 1.00 18.26 ?  12  LEU   B CD2  1 
ATOM   3919 H H    . LEU   B 1 12  ? 34.952 -29.076 -15.303 1.00 21.95 ?  12  LEU   B H    1 
ATOM   3920 H HA   . LEU   B 1 12  ? 33.607 -31.411 -15.134 1.00 21.53 ?  12  LEU   B HA   1 
ATOM   3921 H HB2  . LEU   B 1 12  ? 34.211 -29.601 -13.057 1.00 20.83 ?  12  LEU   B HB2  1 
ATOM   3922 H HB3  . LEU   B 1 12  ? 33.472 -30.983 -12.841 1.00 20.83 ?  12  LEU   B HB3  1 
ATOM   3923 H HG   . LEU   B 1 12  ? 36.181 -30.708 -13.560 1.00 21.08 ?  12  LEU   B HG   1 
ATOM   3924 H HD11 . LEU   B 1 12  ? 36.671 -31.590 -11.465 1.00 21.15 ?  12  LEU   B HD11 1 
ATOM   3925 H HD12 . LEU   B 1 12  ? 35.856 -30.234 -11.315 1.00 21.15 ?  12  LEU   B HD12 1 
ATOM   3926 H HD13 . LEU   B 1 12  ? 35.120 -31.628 -11.119 1.00 21.15 ?  12  LEU   B HD13 1 
ATOM   3927 H HD21 . LEU   B 1 12  ? 36.281 -33.073 -13.290 1.00 21.91 ?  12  LEU   B HD21 1 
ATOM   3928 H HD22 . LEU   B 1 12  ? 34.693 -33.078 -13.267 1.00 21.91 ?  12  LEU   B HD22 1 
ATOM   3929 H HD23 . LEU   B 1 12  ? 35.467 -32.612 -14.574 1.00 21.91 ?  12  LEU   B HD23 1 
ATOM   3930 N N    . THR   B 1 13  ? 32.187 -28.572 -14.792 1.00 17.43 ?  13  THR   B N    1 
ATOM   3931 C CA   . THR   B 1 13  ? 30.960 -27.819 -14.993 1.00 17.42 ?  13  THR   B CA   1 
ATOM   3932 C C    . THR   B 1 13  ? 31.291 -26.621 -15.876 1.00 19.73 ?  13  THR   B C    1 
ATOM   3933 O O    . THR   B 1 13  ? 32.433 -26.432 -16.310 1.00 20.44 ?  13  THR   B O    1 
ATOM   3934 C CB   . THR   B 1 13  ? 30.364 -27.346 -13.662 1.00 17.16 ?  13  THR   B CB   1 
ATOM   3935 O OG1  . THR   B 1 13  ? 31.215 -26.330 -13.114 1.00 16.90 ?  13  THR   B OG1  1 
ATOM   3936 C CG2  . THR   B 1 13  ? 30.246 -28.502 -12.671 1.00 17.75 ?  13  THR   B CG2  1 
ATOM   3937 H H    . THR   B 1 13  ? 32.850 -28.071 -14.577 1.00 20.91 ?  13  THR   B H    1 
ATOM   3938 H HA   . THR   B 1 13  ? 30.302 -28.375 -15.438 1.00 20.90 ?  13  THR   B HA   1 
ATOM   3939 H HB   . THR   B 1 13  ? 29.470 -26.982 -13.809 1.00 20.59 ?  13  THR   B HB   1 
ATOM   3940 H HG1  . THR   B 1 13  ? 30.909 -25.565 -13.311 1.00 20.28 ?  13  THR   B HG1  1 
ATOM   3941 H HG21 . THR   B 1 13  ? 29.743 -28.223 -11.888 1.00 21.30 ?  13  THR   B HG21 1 
ATOM   3942 H HG22 . THR   B 1 13  ? 29.786 -29.248 -13.088 1.00 21.30 ?  13  THR   B HG22 1 
ATOM   3943 H HG23 . THR   B 1 13  ? 31.128 -28.791 -12.393 1.00 21.30 ?  13  THR   B HG23 1 
ATOM   3944 N N    A ASP   B 1 14  ? 30.279 -25.793 -16.135 0.84 20.56 ?  14  ASP   B N    1 
ATOM   3945 N N    B ASP   B 1 14  ? 30.281 -25.785 -16.128 0.16 20.55 ?  14  ASP   B N    1 
ATOM   3946 C CA   A ASP   B 1 14  ? 30.489 -24.632 -16.991 0.84 22.41 ?  14  ASP   B CA   1 
ATOM   3947 C CA   B ASP   B 1 14  ? 30.483 -24.628 -16.993 0.16 21.32 ?  14  ASP   B CA   1 
ATOM   3948 C C    A ASP   B 1 14  ? 31.580 -23.712 -16.456 0.84 20.47 ?  14  ASP   B C    1 
ATOM   3949 C C    B ASP   B 1 14  ? 31.514 -23.652 -16.440 0.16 19.61 ?  14  ASP   B C    1 
ATOM   3950 O O    A ASP   B 1 14  ? 32.211 -22.990 -17.239 0.84 22.01 ?  14  ASP   B O    1 
ATOM   3951 O O    B ASP   B 1 14  ? 32.032 -22.827 -17.201 0.16 19.77 ?  14  ASP   B O    1 
ATOM   3952 C CB   A ASP   B 1 14  ? 29.184 -23.856 -17.157 0.84 26.06 ?  14  ASP   B CB   1 
ATOM   3953 C CB   B ASP   B 1 14  ? 29.163 -23.894 -17.227 0.16 23.63 ?  14  ASP   B CB   1 
ATOM   3954 C CG   A ASP   B 1 14  ? 28.227 -24.520 -18.125 0.84 29.90 ?  14  ASP   B CG   1 
ATOM   3955 C CG   B ASP   B 1 14  ? 28.253 -24.624 -18.198 0.16 25.54 ?  14  ASP   B CG   1 
ATOM   3956 O OD1  A ASP   B 1 14  ? 28.630 -25.484 -18.813 0.84 31.36 ?  14  ASP   B OD1  1 
ATOM   3957 O OD1  B ASP   B 1 14  ? 28.772 -25.361 -19.063 0.16 26.21 ?  14  ASP   B OD1  1 
ATOM   3958 O OD2  A ASP   B 1 14  ? 27.062 -24.081 -18.192 0.84 31.46 -1 14  ASP   B OD2  1 
ATOM   3959 O OD2  B ASP   B 1 14  ? 27.019 -24.461 -18.098 0.16 26.25 -1 14  ASP   B OD2  1 
ATOM   3960 H H    A ASP   B 1 14  ? 29.479 -25.880 -15.829 0.84 24.67 ?  14  ASP   B H    1 
ATOM   3961 H H    B ASP   B 1 14  ? 29.483 -25.866 -15.815 0.16 24.66 ?  14  ASP   B H    1 
ATOM   3962 H HA   A ASP   B 1 14  ? 30.769 -24.935 -17.865 0.84 26.89 ?  14  ASP   B HA   1 
ATOM   3963 H HA   B ASP   B 1 14  ? 30.806 -24.938 -17.851 0.16 25.58 ?  14  ASP   B HA   1 
ATOM   3964 H HB2  A ASP   B 1 14  ? 28.735 -23.801 -16.300 0.84 31.28 ?  14  ASP   B HB2  1 
ATOM   3965 H HB2  B ASP   B 1 14  ? 28.692 -23.814 -16.384 0.16 28.35 ?  14  ASP   B HB2  1 
ATOM   3966 H HB3  A ASP   B 1 14  ? 29.387 -22.964 -17.484 0.84 31.28 ?  14  ASP   B HB3  1 
ATOM   3967 H HB3  B ASP   B 1 14  ? 29.357 -23.009 -17.582 0.16 28.35 ?  14  ASP   B HB3  1 
ATOM   3968 N N    . ASN   B 1 15  ? 31.814 -23.712 -15.139 1.00 17.89 ?  15  ASN   B N    1 
ATOM   3969 C CA   . ASN   B 1 15  ? 32.778 -22.794 -14.538 1.00 15.70 ?  15  ASN   B CA   1 
ATOM   3970 C C    . ASN   B 1 15  ? 33.871 -23.447 -13.700 1.00 14.63 ?  15  ASN   B C    1 
ATOM   3971 O O    . ASN   B 1 15  ? 34.720 -22.719 -13.173 1.00 14.71 ?  15  ASN   B O    1 
ATOM   3972 C CB   . ASN   B 1 15  ? 32.065 -21.740 -13.678 1.00 15.60 ?  15  ASN   B CB   1 
ATOM   3973 C CG   . ASN   B 1 15  ? 31.444 -22.337 -12.437 1.00 15.55 ?  15  ASN   B CG   1 
ATOM   3974 O OD1  . ASN   B 1 15  ? 30.500 -23.136 -12.523 1.00 16.94 ?  15  ASN   B OD1  1 
ATOM   3975 N ND2  . ASN   B 1 15  ? 31.967 -21.977 -11.274 1.00 14.60 ?  15  ASN   B ND2  1 
ATOM   3976 H H    A ASN   B 1 15  ? 31.413 -24.228 -14.573 0.84 21.46 ?  15  ASN   B H    1 
ATOM   3977 H H    B ASN   B 1 15  ? 31.452 -24.263 -14.582 0.16 21.46 ?  15  ASN   B H    1 
ATOM   3978 H HA   . ASN   B 1 15  ? 33.222 -22.316 -15.245 1.00 18.84 ?  15  ASN   B HA   1 
ATOM   3979 H HB2  . ASN   B 1 15  ? 32.712 -21.064 -13.403 1.00 18.72 ?  15  ASN   B HB2  1 
ATOM   3980 H HB3  . ASN   B 1 15  ? 31.359 -21.320 -14.198 1.00 18.72 ?  15  ASN   B HB3  1 
ATOM   3981 H HD21 . ASN   B 1 15  ? 31.648 -22.286 -10.537 1.00 17.51 ?  15  ASN   B HD21 1 
ATOM   3982 H HD22 . ASN   B 1 15  ? 32.632 -21.422 -11.246 1.00 17.51 ?  15  ASN   B HD22 1 
ATOM   3983 N N    . VAL   B 1 16  ? 33.885 -24.769 -13.552 1.00 14.25 ?  16  VAL   B N    1 
ATOM   3984 C CA   . VAL   B 1 16  ? 34.888 -25.458 -12.746 1.00 13.99 ?  16  VAL   B CA   1 
ATOM   3985 C C    . VAL   B 1 16  ? 35.679 -26.397 -13.643 1.00 14.06 ?  16  VAL   B C    1 
ATOM   3986 O O    . VAL   B 1 16  ? 35.098 -27.268 -14.308 1.00 15.44 ?  16  VAL   B O    1 
ATOM   3987 C CB   . VAL   B 1 16  ? 34.258 -26.229 -11.572 1.00 14.39 ?  16  VAL   B CB   1 
ATOM   3988 C CG1  . VAL   B 1 16  ? 35.346 -26.955 -10.779 1.00 14.56 ?  16  VAL   B CG1  1 
ATOM   3989 C CG2  . VAL   B 1 16  ? 33.453 -25.289 -10.682 1.00 15.20 ?  16  VAL   B CG2  1 
ATOM   3990 H H    . VAL   B 1 16  ? 33.306 -25.301 -13.910 1.00 17.10 ?  16  VAL   B H    1 
ATOM   3991 H HA   . VAL   B 1 16  ? 35.501 -24.805 -12.377 1.00 16.79 ?  16  VAL   B HA   1 
ATOM   3992 H HB   . VAL   B 1 16  ? 33.654 -26.901 -11.927 1.00 17.26 ?  16  VAL   B HB   1 
ATOM   3993 H HG11 . VAL   B 1 16  ? 34.970 -27.254 -9.936  1.00 17.47 ?  16  VAL   B HG11 1 
ATOM   3994 H HG12 . VAL   B 1 16  ? 35.659 -27.716 -11.290 1.00 17.47 ?  16  VAL   B HG12 1 
ATOM   3995 H HG13 . VAL   B 1 16  ? 36.077 -26.339 -10.613 1.00 17.47 ?  16  VAL   B HG13 1 
ATOM   3996 H HG21 . VAL   B 1 16  ? 33.115 -25.789 -9.922  1.00 18.24 ?  16  VAL   B HG21 1 
ATOM   3997 H HG22 . VAL   B 1 16  ? 34.027 -24.572 -10.379 1.00 18.24 ?  16  VAL   B HG22 1 
ATOM   3998 H HG23 . VAL   B 1 16  ? 32.712 -24.929 -11.195 1.00 18.24 ?  16  VAL   B HG23 1 
ATOM   3999 N N    . TYR   B 1 17  ? 37.006 -26.235 -13.621 1.00 14.53 ?  17  TYR   B N    1 
ATOM   4000 C CA   . TYR   B 1 17  ? 37.950 -26.989 -14.430 1.00 14.99 ?  17  TYR   B CA   1 
ATOM   4001 C C    . TYR   B 1 17  ? 39.002 -27.598 -13.512 1.00 14.22 ?  17  TYR   B C    1 
ATOM   4002 O O    . TYR   B 1 17  ? 39.277 -27.068 -12.432 1.00 14.59 ?  17  TYR   B O    1 
ATOM   4003 C CB   . TYR   B 1 17  ? 38.652 -26.065 -15.432 1.00 17.22 ?  17  TYR   B CB   1 
ATOM   4004 C CG   . TYR   B 1 17  ? 37.722 -25.299 -16.340 1.00 20.32 ?  17  TYR   B CG   1 
ATOM   4005 C CD1  . TYR   B 1 17  ? 37.134 -24.107 -15.930 1.00 21.52 ?  17  TYR   B CD1  1 
ATOM   4006 C CD2  . TYR   B 1 17  ? 37.435 -25.765 -17.615 1.00 22.12 ?  17  TYR   B CD2  1 
ATOM   4007 C CE1  . TYR   B 1 17  ? 36.280 -23.404 -16.766 1.00 23.05 ?  17  TYR   B CE1  1 
ATOM   4008 C CE2  . TYR   B 1 17  ? 36.587 -25.071 -18.457 1.00 23.59 ?  17  TYR   B CE2  1 
ATOM   4009 C CZ   . TYR   B 1 17  ? 36.013 -23.894 -18.027 1.00 24.22 ?  17  TYR   B CZ   1 
ATOM   4010 O OH   . TYR   B 1 17  ? 35.171 -23.204 -18.865 1.00 26.17 ?  17  TYR   B OH   1 
ATOM   4011 H H    . TYR   B 1 17  ? 37.401 -25.659 -13.111 1.00 17.43 ?  17  TYR   B H    1 
ATOM   4012 H HA   . TYR   B 1 17  ? 37.489 -27.697 -14.911 1.00 17.99 ?  17  TYR   B HA   1 
ATOM   4013 H HB2  . TYR   B 1 17  ? 39.187 -25.423 -14.946 1.00 20.66 ?  17  TYR   B HB2  1 
ATOM   4014 H HB3  . TYR   B 1 17  ? 39.218 -26.606 -15.999 1.00 20.66 ?  17  TYR   B HB3  1 
ATOM   4015 H HD1  . TYR   B 1 17  ? 37.313 -23.777 -15.081 1.00 25.83 ?  17  TYR   B HD1  1 
ATOM   4016 H HD2  . TYR   B 1 17  ? 37.815 -26.560 -17.910 1.00 26.54 ?  17  TYR   B HD2  1 
ATOM   4017 H HE1  . TYR   B 1 17  ? 35.892 -22.607 -16.480 1.00 27.66 ?  17  TYR   B HE1  1 
ATOM   4018 H HE2  . TYR   B 1 17  ? 36.399 -25.398 -19.310 1.00 28.31 ?  17  TYR   B HE2  1 
ATOM   4019 H HH   . TYR   B 1 17  ? 35.091 -23.606 -19.598 1.00 31.40 ?  17  TYR   B HH   1 
ATOM   4020 N N    . ILE   B 1 18  ? 39.615 -28.703 -13.945 1.00 14.16 ?  18  ILE   B N    1 
ATOM   4021 C CA   . ILE   B 1 18  ? 40.546 -29.428 -13.086 1.00 14.07 ?  18  ILE   B CA   1 
ATOM   4022 C C    . ILE   B 1 18  ? 41.707 -29.981 -13.904 1.00 14.47 ?  18  ILE   B C    1 
ATOM   4023 O O    . ILE   B 1 18  ? 41.549 -30.370 -15.065 1.00 16.08 ?  18  ILE   B O    1 
ATOM   4024 C CB   . ILE   B 1 18  ? 39.798 -30.528 -12.287 1.00 14.68 ?  18  ILE   B CB   1 
ATOM   4025 C CG1  . ILE   B 1 18  ? 40.651 -31.071 -11.138 1.00 14.96 ?  18  ILE   B CG1  1 
ATOM   4026 C CG2  . ILE   B 1 18  ? 39.311 -31.651 -13.216 1.00 14.85 ?  18  ILE   B CG2  1 
ATOM   4027 C CD1  . ILE   B 1 18  ? 39.832 -31.864 -10.126 1.00 16.30 ?  18  ILE   B CD1  1 
ATOM   4028 H H    . ILE   B 1 18  ? 39.510 -29.049 -14.724 1.00 16.99 ?  18  ILE   B H    1 
ATOM   4029 H HA   . ILE   B 1 18  ? 40.911 -28.809 -12.435 1.00 16.88 ?  18  ILE   B HA   1 
ATOM   4030 H HB   . ILE   B 1 18  ? 39.009 -30.124 -11.890 1.00 17.61 ?  18  ILE   B HB   1 
ATOM   4031 H HG12 . ILE   B 1 18  ? 41.334 -31.652 -11.496 1.00 17.95 ?  18  ILE   B HG12 1 
ATOM   4032 H HG13 . ILE   B 1 18  ? 41.059 -30.322 -10.670 1.00 17.95 ?  18  ILE   B HG13 1 
ATOM   4033 H HG21 . ILE   B 1 18  ? 38.714 -32.235 -12.721 1.00 17.81 ?  18  ILE   B HG21 1 
ATOM   4034 H HG22 . ILE   B 1 18  ? 38.838 -31.253 -13.963 1.00 17.81 ?  18  ILE   B HG22 1 
ATOM   4035 H HG23 . ILE   B 1 18  ? 40.076 -32.152 -13.534 1.00 17.81 ?  18  ILE   B HG23 1 
ATOM   4036 H HD11 . ILE   B 1 18  ? 40.413 -32.143 -9.399  1.00 19.56 ?  18  ILE   B HD11 1 
ATOM   4037 H HD12 . ILE   B 1 18  ? 39.119 -31.303 -9.782  1.00 19.56 ?  18  ILE   B HD12 1 
ATOM   4038 H HD13 . ILE   B 1 18  ? 39.457 -32.644 -10.565 1.00 19.56 ?  18  ILE   B HD13 1 
ATOM   4039 N N    . LYS   B 1 19  ? 42.886 -30.017 -13.279 1.00 15.31 ?  19  LYS   B N    1 
ATOM   4040 C CA   . LYS   B 1 19  ? 44.099 -30.491 -13.931 1.00 15.79 ?  19  LYS   B CA   1 
ATOM   4041 C C    . LYS   B 1 19  ? 44.998 -31.163 -12.904 1.00 15.50 ?  19  LYS   B C    1 
ATOM   4042 O O    . LYS   B 1 19  ? 45.084 -30.722 -11.756 1.00 15.10 ?  19  LYS   B O    1 
ATOM   4043 C CB   . LYS   B 1 19  ? 44.865 -29.326 -14.574 1.00 17.45 ?  19  LYS   B CB   1 
ATOM   4044 C CG   . LYS   B 1 19  ? 46.073 -29.733 -15.402 1.00 18.96 ?  19  LYS   B CG   1 
ATOM   4045 C CD   . LYS   B 1 19  ? 46.794 -28.503 -15.940 1.00 20.98 ?  19  LYS   B CD   1 
ATOM   4046 C CE   . LYS   B 1 19  ? 47.960 -28.882 -16.834 1.00 22.93 ?  19  LYS   B CE   1 
ATOM   4047 N NZ   . LYS   B 1 19  ? 48.736 -27.696 -17.283 1.00 24.05 ?  19  LYS   B NZ   1 
ATOM   4048 H H    . LYS   B 1 19  ? 42.999 -29.772 -12.460 1.00 18.36 ?  19  LYS   B H    1 
ATOM   4049 H HA   . LYS   B 1 19  ? 43.864 -31.136 -14.618 1.00 18.94 ?  19  LYS   B HA   1 
ATOM   4050 H HB2  . LYS   B 1 19  ? 44.256 -28.849 -15.158 1.00 20.93 ?  19  LYS   B HB2  1 
ATOM   4051 H HB3  . LYS   B 1 19  ? 45.170 -28.735 -13.868 1.00 20.93 ?  19  LYS   B HB3  1 
ATOM   4052 H HG2  . LYS   B 1 19  ? 46.686 -30.237 -14.845 1.00 22.75 ?  19  LYS   B HG2  1 
ATOM   4053 H HG3  . LYS   B 1 19  ? 45.774 -30.275 -16.151 1.00 22.75 ?  19  LYS   B HG3  1 
ATOM   4054 H HD2  . LYS   B 1 19  ? 46.169 -27.972 -16.459 1.00 25.17 ?  19  LYS   B HD2  1 
ATOM   4055 H HD3  . LYS   B 1 19  ? 47.135 -27.986 -15.194 1.00 25.17 ?  19  LYS   B HD3  1 
ATOM   4056 H HE2  . LYS   B 1 19  ? 48.555 -29.470 -16.343 1.00 27.51 ?  19  LYS   B HE2  1 
ATOM   4057 H HE3  . LYS   B 1 19  ? 47.617 -29.339 -17.620 1.00 27.51 ?  19  LYS   B HE3  1 
ATOM   4058 H HZ1  . LYS   B 1 19  ? 49.380 -27.951 -17.843 1.00 28.86 ?  19  LYS   B HZ1  1 
ATOM   4059 H HZ2  . LYS   B 1 19  ? 48.200 -27.122 -17.702 1.00 28.86 ?  19  LYS   B HZ2  1 
ATOM   4060 H HZ3  . LYS   B 1 19  ? 49.105 -27.292 -16.583 1.00 28.86 ?  19  LYS   B HZ3  1 
ATOM   4061 N N    . ASN   B 1 20  ? 45.683 -32.220 -13.333 1.00 16.64 ?  20  ASN   B N    1 
ATOM   4062 C CA   . ASN   B 1 20  ? 46.720 -32.852 -12.520 1.00 17.57 ?  20  ASN   B CA   1 
ATOM   4063 C C    . ASN   B 1 20  ? 47.993 -32.034 -12.713 1.00 17.92 ?  20  ASN   B C    1 
ATOM   4064 O O    . ASN   B 1 20  ? 48.649 -32.124 -13.755 1.00 19.91 ?  20  ASN   B O    1 
ATOM   4065 C CB   . ASN   B 1 20  ? 46.896 -34.306 -12.955 1.00 19.04 ?  20  ASN   B CB   1 
ATOM   4066 C CG   . ASN   B 1 20  ? 48.059 -35.009 -12.268 1.00 20.45 ?  20  ASN   B CG   1 
ATOM   4067 O OD1  . ASN   B 1 20  ? 48.748 -35.833 -12.884 1.00 22.51 ?  20  ASN   B OD1  1 
ATOM   4068 N ND2  . ASN   B 1 20  ? 48.268 -34.717 -10.993 1.00 20.16 ?  20  ASN   B ND2  1 
ATOM   4069 H H    . ASN   B 1 20  ? 45.562 -32.596 -14.097 1.00 19.97 ?  20  ASN   B H    1 
ATOM   4070 H HA   . ASN   B 1 20  ? 46.453 -32.830 -11.585 1.00 21.09 ?  20  ASN   B HA   1 
ATOM   4071 H HB2  . ASN   B 1 20  ? 46.085 -34.797 -12.742 1.00 22.84 ?  20  ASN   B HB2  1 
ATOM   4072 H HB3  . ASN   B 1 20  ? 47.052 -34.326 -13.909 1.00 22.84 ?  20  ASN   B HB3  1 
ATOM   4073 H HD21 . ASN   B 1 20  ? 48.914 -35.088 -10.569 1.00 24.19 ?  20  ASN   B HD21 1 
ATOM   4074 H HD22 . ASN   B 1 20  ? 47.760 -34.148 -10.587 1.00 24.19 ?  20  ASN   B HD22 1 
ATOM   4075 N N    . ALA   B 1 21  ? 48.334 -31.211 -11.719 1.00 17.63 ?  21  ALA   B N    1 
ATOM   4076 C CA   . ALA   B 1 21  ? 49.445 -30.281 -11.861 1.00 18.32 ?  21  ALA   B CA   1 
ATOM   4077 C C    . ALA   B 1 21  ? 49.907 -29.800 -10.493 1.00 17.50 ?  21  ALA   B C    1 
ATOM   4078 O O    . ALA   B 1 21  ? 49.161 -29.830 -9.510  1.00 17.14 ?  21  ALA   B O    1 
ATOM   4079 C CB   . ALA   B 1 21  ? 49.055 -29.089 -12.737 1.00 19.62 ?  21  ALA   B CB   1 
ATOM   4080 H H    . ALA   B 1 21  ? 47.928 -31.168 -10.955 1.00 21.15 ?  21  ALA   B H    1 
ATOM   4081 H HA   . ALA   B 1 21  ? 50.181 -30.742 -12.283 1.00 21.98 ?  21  ALA   B HA   1 
ATOM   4082 H HB1  . ALA   B 1 21  ? 49.843 -28.551 -12.888 1.00 23.54 ?  21  ALA   B HB1  1 
ATOM   4083 H HB2  . ALA   B 1 21  ? 48.712 -29.423 -13.580 1.00 23.54 ?  21  ALA   B HB2  1 
ATOM   4084 H HB3  . ALA   B 1 21  ? 48.371 -28.572 -12.283 1.00 23.54 ?  21  ALA   B HB3  1 
ATOM   4085 N N    . ASP   B 1 22  ? 51.167 -29.358 -10.465 1.00 16.86 ?  22  ASP   B N    1 
ATOM   4086 C CA   . ASP   B 1 22  ? 51.776 -28.665 -9.334  1.00 16.00 ?  22  ASP   B CA   1 
ATOM   4087 C C    . ASP   B 1 22  ? 51.374 -27.193 -9.420  1.00 14.85 ?  22  ASP   B C    1 
ATOM   4088 O O    . ASP   B 1 22  ? 51.688 -26.521 -10.408 1.00 15.16 ?  22  ASP   B O    1 
ATOM   4089 C CB   . ASP   B 1 22  ? 53.293 -28.851 -9.475  1.00 17.41 ?  22  ASP   B CB   1 
ATOM   4090 C CG   . ASP   B 1 22  ? 54.114 -28.085 -8.445  1.00 18.94 ?  22  ASP   B CG   1 
ATOM   4091 O OD1  . ASP   B 1 22  ? 53.741 -26.969 -8.050  1.00 19.08 ?  22  ASP   B OD1  1 
ATOM   4092 O OD2  . ASP   B 1 22  ? 55.188 -28.597 -8.058  1.00 21.22 -1 22  ASP   B OD2  1 
ATOM   4093 H H    . ASP   B 1 22  ? 51.715 -29.458 -11.125 1.00 20.23 ?  22  ASP   B H    1 
ATOM   4094 H HA   . ASP   B 1 22  ? 51.475 -29.050 -8.491  1.00 19.20 ?  22  ASP   B HA   1 
ATOM   4095 H HB2  . ASP   B 1 22  ? 53.509 -29.789 -9.384  1.00 20.89 ?  22  ASP   B HB2  1 
ATOM   4096 H HB3  . ASP   B 1 22  ? 53.564 -28.530 -10.349 1.00 20.89 ?  22  ASP   B HB3  1 
ATOM   4097 N N    . ILE   B 1 23  ? 50.664 -26.695 -8.401  1.00 14.02 ?  23  ILE   B N    1 
ATOM   4098 C CA   . ILE   B 1 23  ? 50.071 -25.357 -8.476  1.00 13.41 ?  23  ILE   B CA   1 
ATOM   4099 C C    . ILE   B 1 23  ? 51.125 -24.267 -8.612  1.00 13.29 ?  23  ILE   B C    1 
ATOM   4100 O O    . ILE   B 1 23  ? 50.859 -23.224 -9.217  1.00 12.73 ?  23  ILE   B O    1 
ATOM   4101 C CB   . ILE   B 1 23  ? 49.134 -25.114 -7.279  1.00 13.67 ?  23  ILE   B CB   1 
ATOM   4102 C CG1  . ILE   B 1 23  ? 48.304 -23.845 -7.488  1.00 14.12 ?  23  ILE   B CG1  1 
ATOM   4103 C CG2  . ILE   B 1 23  ? 49.914 -25.088 -5.977  1.00 14.89 ?  23  ILE   B CG2  1 
ATOM   4104 C CD1  . ILE   B 1 23  ? 47.182 -23.682 -6.480  1.00 14.65 ?  23  ILE   B CD1  1 
ATOM   4105 H H    . ILE   B 1 23  ? 50.517 -27.113 -7.664  1.00 16.83 ?  23  ILE   B H    1 
ATOM   4106 H HA   . ILE   B 1 23  ? 49.526 -25.324 -9.275  1.00 16.09 ?  23  ILE   B HA   1 
ATOM   4107 H HB   . ILE   B 1 23  ? 48.517 -25.861 -7.237  1.00 16.40 ?  23  ILE   B HB   1 
ATOM   4108 H HG12 . ILE   B 1 23  ? 48.890 -23.073 -7.413  1.00 16.94 ?  23  ILE   B HG12 1 
ATOM   4109 H HG13 . ILE   B 1 23  ? 47.911 -23.869 -8.377  1.00 16.94 ?  23  ILE   B HG13 1 
ATOM   4110 H HG21 . ILE   B 1 23  ? 49.288 -25.070 -5.237  1.00 17.87 ?  23  ILE   B HG21 1 
ATOM   4111 H HG22 . ILE   B 1 23  ? 50.467 -25.883 -5.923  1.00 17.87 ?  23  ILE   B HG22 1 
ATOM   4112 H HG23 . ILE   B 1 23  ? 50.472 -24.295 -5.959  1.00 17.87 ?  23  ILE   B HG23 1 
ATOM   4113 H HD11 . ILE   B 1 23  ? 46.663 -22.898 -6.713  1.00 17.58 ?  23  ILE   B HD11 1 
ATOM   4114 H HD12 . ILE   B 1 23  ? 46.620 -24.474 -6.510  1.00 17.58 ?  23  ILE   B HD12 1 
ATOM   4115 H HD13 . ILE   B 1 23  ? 47.565 -23.580 -5.598  1.00 17.58 ?  23  ILE   B HD13 1 
ATOM   4116 N N    . VAL   B 1 24  ? 52.319 -24.471 -8.052  1.00 13.51 ?  24  VAL   B N    1 
ATOM   4117 C CA   . VAL   B 1 24  ? 53.394 -23.491 -8.218  1.00 14.26 ?  24  VAL   B CA   1 
ATOM   4118 C C    . VAL   B 1 24  ? 53.848 -23.445 -9.671  1.00 14.36 ?  24  VAL   B C    1 
ATOM   4119 O O    . VAL   B 1 24  ? 53.986 -22.369 -10.267 1.00 14.90 ?  24  VAL   B O    1 
ATOM   4120 C CB   . VAL   B 1 24  ? 54.568 -23.812 -7.272  1.00 15.04 ?  24  VAL   B CB   1 
ATOM   4121 C CG1  . VAL   B 1 24  ? 55.782 -22.938 -7.594  1.00 15.41 ?  24  VAL   B CG1  1 
ATOM   4122 C CG2  . VAL   B 1 24  ? 54.155 -23.627 -5.835  1.00 15.90 ?  24  VAL   B CG2  1 
ATOM   4123 H H    . VAL   B 1 24  ? 52.532 -25.157 -7.580  1.00 16.21 ?  24  VAL   B H    1 
ATOM   4124 H HA   . VAL   B 1 24  ? 53.060 -22.613 -7.985  1.00 17.11 ?  24  VAL   B HA   1 
ATOM   4125 H HB   . VAL   B 1 24  ? 54.829 -24.740 -7.388  1.00 18.05 ?  24  VAL   B HB   1 
ATOM   4126 H HG11 . VAL   B 1 24  ? 56.377 -22.934 -6.827  1.00 18.49 ?  24  VAL   B HG11 1 
ATOM   4127 H HG12 . VAL   B 1 24  ? 56.239 -23.306 -8.364  1.00 18.49 ?  24  VAL   B HG12 1 
ATOM   4128 H HG13 . VAL   B 1 24  ? 55.479 -22.037 -7.780  1.00 18.49 ?  24  VAL   B HG13 1 
ATOM   4129 H HG21 . VAL   B 1 24  ? 54.878 -23.910 -5.256  1.00 19.08 ?  24  VAL   B HG21 1 
ATOM   4130 H HG22 . VAL   B 1 24  ? 53.958 -22.688 -5.683  1.00 19.08 ?  24  VAL   B HG22 1 
ATOM   4131 H HG23 . VAL   B 1 24  ? 53.363 -24.162 -5.661  1.00 19.08 ?  24  VAL   B HG23 1 
ATOM   4132 N N    . GLU   B 1 25  ? 54.113 -24.618 -10.255 1.00 15.25 ?  25  GLU   B N    1 
ATOM   4133 C CA   . GLU   B 1 25  ? 54.504 -24.660 -11.658 1.00 16.43 ?  25  GLU   B CA   1 
ATOM   4134 C C    . GLU   B 1 25  ? 53.394 -24.119 -12.547 1.00 15.39 ?  25  GLU   B C    1 
ATOM   4135 O O    . GLU   B 1 25  ? 53.659 -23.408 -13.525 1.00 16.16 ?  25  GLU   B O    1 
ATOM   4136 C CB   . GLU   B 1 25  ? 54.896 -26.086 -12.046 1.00 19.91 ?  25  GLU   B CB   1 
ATOM   4137 C CG   . GLU   B 1 25  ? 56.206 -26.529 -11.407 1.00 25.07 ?  25  GLU   B CG   1 
ATOM   4138 C CD   . GLU   B 1 25  ? 57.310 -25.487 -11.520 1.00 30.28 ?  25  GLU   B CD   1 
ATOM   4139 O OE1  . GLU   B 1 25  ? 57.693 -25.141 -12.658 1.00 31.83 ?  25  GLU   B OE1  1 
ATOM   4140 O OE2  . GLU   B 1 25  ? 57.781 -24.993 -10.469 1.00 31.68 -1 25  GLU   B OE2  1 
ATOM   4141 H H    . GLU   B 1 25  ? 54.070 -25.386 -9.864  1.00 18.30 ?  25  GLU   B H    1 
ATOM   4142 H HA   . GLU   B 1 25  ? 55.262 -24.079 -11.784 1.00 19.71 ?  25  GLU   B HA   1 
ATOM   4143 H HB2  . GLU   B 1 25  ? 54.199 -26.699 -11.751 1.00 23.88 ?  25  GLU   B HB2  1 
ATOM   4144 H HB3  . GLU   B 1 25  ? 54.993 -26.138 -13.009 1.00 23.88 ?  25  GLU   B HB3  1 
ATOM   4145 H HG2  . GLU   B 1 25  ? 56.062 -26.686 -10.466 1.00 30.08 ?  25  GLU   B HG2  1 
ATOM   4146 H HG3  . GLU   B 1 25  ? 56.512 -27.337 -11.846 1.00 30.08 ?  25  GLU   B HG3  1 
ATOM   4147 N N    . GLU   B 1 26  ? 52.142 -24.428 -12.208 1.00 14.51 ?  26  GLU   B N    1 
ATOM   4148 C CA   . GLU   B 1 26  ? 51.019 -23.901 -12.975 1.00 14.89 ?  26  GLU   B CA   1 
ATOM   4149 C C    . GLU   B 1 26  ? 50.972 -22.382 -12.900 1.00 14.28 ?  26  GLU   B C    1 
ATOM   4150 O O    . GLU   B 1 26  ? 50.779 -21.708 -13.916 1.00 15.39 ?  26  GLU   B O    1 
ATOM   4151 C CB   . GLU   B 1 26  ? 49.703 -24.484 -12.460 1.00 16.68 ?  26  GLU   B CB   1 
ATOM   4152 C CG   . GLU   B 1 26  ? 49.275 -25.764 -13.139 1.00 20.39 ?  26  GLU   B CG   1 
ATOM   4153 C CD   . GLU   B 1 26  ? 49.011 -25.603 -14.636 1.00 22.19 ?  26  GLU   B CD   1 
ATOM   4154 O OE1  . GLU   B 1 26  ? 48.030 -24.940 -15.039 1.00 22.82 ?  26  GLU   B OE1  1 
ATOM   4155 O OE2  . GLU   B 1 26  ? 49.779 -26.180 -15.413 1.00 24.28 -1 26  GLU   B OE2  1 
ATOM   4156 H H    . GLU   B 1 26  ? 51.915 -24.936 -11.545 1.00 17.41 ?  26  GLU   B H    1 
ATOM   4157 H HA   . GLU   B 1 26  ? 51.125 -24.155 -13.902 1.00 17.87 ?  26  GLU   B HA   1 
ATOM   4158 H HB2  . GLU   B 1 26  ? 49.791 -24.672 -11.512 1.00 20.01 ?  26  GLU   B HB2  1 
ATOM   4159 H HB3  . GLU   B 1 26  ? 48.999 -23.830 -12.598 1.00 20.01 ?  26  GLU   B HB3  1 
ATOM   4160 H HG2  . GLU   B 1 26  ? 49.981 -26.415 -13.029 1.00 24.47 ?  26  GLU   B HG2  1 
ATOM   4161 H HG3  . GLU   B 1 26  ? 48.456 -26.080 -12.728 1.00 24.47 ?  26  GLU   B HG3  1 
ATOM   4162 N N    . ALA   B 1 27  ? 51.119 -21.827 -11.696 1.00 13.33 ?  27  ALA   B N    1 
ATOM   4163 C CA   . ALA   B 1 27  ? 51.078 -20.376 -11.555 1.00 13.77 ?  27  ALA   B CA   1 
ATOM   4164 C C    . ALA   B 1 27  ? 52.150 -19.714 -12.411 1.00 14.70 ?  27  ALA   B C    1 
ATOM   4165 O O    . ALA   B 1 27  ? 51.892 -18.708 -13.088 1.00 15.57 ?  27  ALA   B O    1 
ATOM   4166 C CB   . ALA   B 1 27  ? 51.218 -19.989 -10.084 1.00 14.01 ?  27  ALA   B CB   1 
ATOM   4167 H H    . ALA   B 1 27  ? 51.236 -22.260 -10.958 1.00 15.99 ?  27  ALA   B H    1 
ATOM   4168 H HA   . ALA   B 1 27  ? 50.220 -20.055 -11.863 1.00 16.52 ?  27  ALA   B HA   1 
ATOM   4169 H HB1  . ALA   B 1 27  ? 51.183 -19.025 -10.004 1.00 16.81 ?  27  ALA   B HB1  1 
ATOM   4170 H HB2  . ALA   B 1 27  ? 50.481 -20.387 -9.584  1.00 16.81 ?  27  ALA   B HB2  1 
ATOM   4171 H HB3  . ALA   B 1 27  ? 52.060 -20.323 -9.743  1.00 16.81 ?  27  ALA   B HB3  1 
ATOM   4172 N N    . LYS   B 1 28  ? 53.361 -20.270 -12.406 1.00 16.09 ?  28  LYS   B N    1 
ATOM   4173 C CA   . LYS   B 1 28  ? 54.440 -19.658 -13.173 1.00 18.27 ?  28  LYS   B CA   1 
ATOM   4174 C C    . LYS   B 1 28  ? 54.183 -19.737 -14.672 1.00 18.88 ?  28  LYS   B C    1 
ATOM   4175 O O    . LYS   B 1 28  ? 54.592 -18.837 -15.417 1.00 19.89 ?  28  LYS   B O    1 
ATOM   4176 C CB   . LYS   B 1 28  ? 55.790 -20.272 -12.786 1.00 20.59 ?  28  LYS   B CB   1 
ATOM   4177 C CG   . LYS   B 1 28  ? 56.202 -19.901 -11.365 1.00 23.12 ?  28  LYS   B CG   1 
ATOM   4178 C CD   . LYS   B 1 28  ? 57.628 -20.306 -11.025 1.00 26.99 ?  28  LYS   B CD   1 
ATOM   4179 C CE   . LYS   B 1 28  ? 57.724 -21.772 -10.674 1.00 29.78 ?  28  LYS   B CE   1 
ATOM   4180 N NZ   . LYS   B 1 28  ? 59.089 -22.125 -10.188 1.00 32.42 ?  28  LYS   B NZ   1 
ATOM   4181 H H    . LYS   B 1 28  ? 53.582 -20.984 -11.975 1.00 19.31 ?  28  LYS   B H    1 
ATOM   4182 H HA   . LYS   B 1 28  ? 54.481 -18.718 -12.945 1.00 21.92 ?  28  LYS   B HA   1 
ATOM   4183 H HB2  . LYS   B 1 28  ? 55.733 -21.239 -12.838 1.00 24.70 ?  28  LYS   B HB2  1 
ATOM   4184 H HB3  . LYS   B 1 28  ? 56.477 -19.946 -13.391 1.00 24.70 ?  28  LYS   B HB3  1 
ATOM   4185 H HG2  . LYS   B 1 28  ? 56.129 -18.938 -11.263 1.00 27.74 ?  28  LYS   B HG2  1 
ATOM   4186 H HG3  . LYS   B 1 28  ? 55.606 -20.345 -10.744 1.00 27.74 ?  28  LYS   B HG3  1 
ATOM   4187 H HD2  . LYS   B 1 28  ? 58.197 -20.136 -11.791 1.00 32.38 ?  28  LYS   B HD2  1 
ATOM   4188 H HD3  . LYS   B 1 28  ? 57.928 -19.787 -10.262 1.00 32.38 ?  28  LYS   B HD3  1 
ATOM   4189 H HE2  . LYS   B 1 28  ? 57.087 -21.975 -9.971  1.00 35.73 ?  28  LYS   B HE2  1 
ATOM   4190 H HE3  . LYS   B 1 28  ? 57.534 -22.304 -11.463 1.00 35.73 ?  28  LYS   B HE3  1 
ATOM   4191 H HZ1  . LYS   B 1 28  ? 59.126 -22.991 -9.986  1.00 38.91 ?  28  LYS   B HZ1  1 
ATOM   4192 H HZ2  . LYS   B 1 28  ? 59.692 -21.949 -10.818 1.00 38.91 ?  28  LYS   B HZ2  1 
ATOM   4193 H HZ3  . LYS   B 1 28  ? 59.284 -21.651 -9.460  1.00 38.91 ?  28  LYS   B HZ3  1 
ATOM   4194 N N    . LYS   B 1 29  ? 53.480 -20.775 -15.129 1.00 19.98 ?  29  LYS   B N    1 
ATOM   4195 C CA   . LYS   B 1 29  ? 53.187 -20.922 -16.550 1.00 22.75 ?  29  LYS   B CA   1 
ATOM   4196 C C    . LYS   B 1 29  ? 51.934 -20.165 -16.983 1.00 21.75 ?  29  LYS   B C    1 
ATOM   4197 O O    . LYS   B 1 29  ? 51.924 -19.559 -18.060 1.00 23.37 ?  29  LYS   B O    1 
ATOM   4198 C CB   . LYS   B 1 29  ? 53.051 -22.405 -16.905 1.00 27.29 ?  29  LYS   B CB   1 
ATOM   4199 C CG   . LYS   B 1 29  ? 52.917 -22.681 -18.392 1.00 31.41 ?  29  LYS   B CG   1 
ATOM   4200 C CD   . LYS   B 1 29  ? 53.167 -24.149 -18.708 1.00 34.62 ?  29  LYS   B CD   1 
ATOM   4201 C CE   . LYS   B 1 29  ? 52.083 -25.052 -18.136 1.00 36.98 ?  29  LYS   B CE   1 
ATOM   4202 N NZ   . LYS   B 1 29  ? 52.345 -26.490 -18.441 1.00 38.37 ?  29  LYS   B NZ   1 
ATOM   4203 H H    . LYS   B 1 29  ? 53.166 -21.411 -14.630 1.00 23.97 ?  29  LYS   B H    1 
ATOM   4204 H HA   . LYS   B 1 29  ? 53.930 -20.565 -17.052 1.00 27.29 ?  29  LYS   B HA   1 
ATOM   4205 H HB2  . LYS   B 1 29  ? 53.843 -22.869 -16.591 1.00 32.75 ?  29  LYS   B HB2  1 
ATOM   4206 H HB3  . LYS   B 1 29  ? 52.266 -22.760 -16.467 1.00 32.75 ?  29  LYS   B HB3  1 
ATOM   4207 H HG2  . LYS   B 1 29  ? 52.018 -22.458 -18.679 1.00 37.69 ?  29  LYS   B HG2  1 
ATOM   4208 H HG3  . LYS   B 1 29  ? 53.567 -22.150 -18.878 1.00 37.69 ?  29  LYS   B HG3  1 
ATOM   4209 H HD2  . LYS   B 1 29  ? 53.184 -24.268 -19.670 1.00 41.54 ?  29  LYS   B HD2  1 
ATOM   4210 H HD3  . LYS   B 1 29  ? 54.017 -24.416 -18.324 1.00 41.54 ?  29  LYS   B HD3  1 
ATOM   4211 H HE2  . LYS   B 1 29  ? 52.052 -24.949 -17.172 1.00 44.37 ?  29  LYS   B HE2  1 
ATOM   4212 H HE3  . LYS   B 1 29  ? 51.227 -24.810 -18.526 1.00 44.37 ?  29  LYS   B HE3  1 
ATOM   4213 H HZ1  . LYS   B 1 29  ? 51.699 -26.998 -18.098 1.00 46.04 ?  29  LYS   B HZ1  1 
ATOM   4214 H HZ2  . LYS   B 1 29  ? 52.372 -26.615 -19.322 1.00 46.04 ?  29  LYS   B HZ2  1 
ATOM   4215 H HZ3  . LYS   B 1 29  ? 53.124 -26.739 -18.090 1.00 46.04 ?  29  LYS   B HZ3  1 
ATOM   4216 N N    . VAL   B 1 30  ? 50.877 -20.196 -16.166 1.00 19.75 ?  30  VAL   B N    1 
ATOM   4217 C CA   . VAL   B 1 30  ? 49.586 -19.612 -16.540 1.00 19.69 ?  30  VAL   B CA   1 
ATOM   4218 C C    . VAL   B 1 30  ? 49.583 -18.097 -16.397 1.00 18.20 ?  30  VAL   B C    1 
ATOM   4219 O O    . VAL   B 1 30  ? 48.836 -17.400 -17.100 1.00 19.39 ?  30  VAL   B O    1 
ATOM   4220 C CB   . VAL   B 1 30  ? 48.481 -20.232 -15.662 1.00 20.79 ?  30  VAL   B CB   1 
ATOM   4221 C CG1  . VAL   B 1 30  ? 47.191 -19.430 -15.747 1.00 21.21 ?  30  VAL   B CG1  1 
ATOM   4222 C CG2  . VAL   B 1 30  ? 48.246 -21.681 -16.042 1.00 21.05 ?  30  VAL   B CG2  1 
ATOM   4223 H H    . VAL   B 1 30  ? 50.875 -20.572 -15.382 1.00 23.70 ?  30  VAL   B H    1 
ATOM   4224 H HA   . VAL   B 1 30  ? 49.396 -19.842 -17.462 1.00 23.63 ?  30  VAL   B HA   1 
ATOM   4225 H HB   . VAL   B 1 30  ? 48.772 -20.222 -14.738 1.00 24.94 ?  30  VAL   B HB   1 
ATOM   4226 H HG11 . VAL   B 1 30  ? 46.450 -20.019 -15.535 1.00 25.45 ?  30  VAL   B HG11 1 
ATOM   4227 H HG12 . VAL   B 1 30  ? 47.224 -18.704 -15.108 1.00 25.45 ?  30  VAL   B HG12 1 
ATOM   4228 H HG13 . VAL   B 1 30  ? 47.083 -19.091 -16.645 1.00 25.45 ?  30  VAL   B HG13 1 
ATOM   4229 H HG21 . VAL   B 1 30  ? 47.559 -22.055 -15.463 1.00 25.25 ?  30  VAL   B HG21 1 
ATOM   4230 H HG22 . VAL   B 1 30  ? 47.951 -21.723 -16.966 1.00 25.25 ?  30  VAL   B HG22 1 
ATOM   4231 H HG23 . VAL   B 1 30  ? 49.071 -22.176 -15.934 1.00 25.25 ?  30  VAL   B HG23 1 
ATOM   4232 N N    . LYS   B 1 31  ? 50.369 -17.581 -15.467 1.00 17.69 ?  31  LYS   B N    1 
ATOM   4233 C CA   . LYS   B 1 31  ? 50.390 -16.170 -15.119 1.00 18.06 ?  31  LYS   B CA   1 
ATOM   4234 C C    . LYS   B 1 31  ? 48.993 -15.699 -14.720 1.00 16.15 ?  31  LYS   B C    1 
ATOM   4235 O O    . LYS   B 1 31  ? 48.446 -14.781 -15.342 1.00 17.07 ?  31  LYS   B O    1 
ATOM   4236 C CB   . LYS   B 1 31  ? 51.011 -15.358 -16.263 1.00 21.03 ?  31  LYS   B CB   1 
ATOM   4237 C CG   . LYS   B 1 31  ? 52.436 -15.812 -16.605 1.00 24.27 ?  31  LYS   B CG   1 
ATOM   4238 C CD   . LYS   B 1 31  ? 53.033 -15.006 -17.750 1.00 27.59 ?  31  LYS   B CD   1 
ATOM   4239 C CE   . LYS   B 1 31  ? 54.527 -15.252 -17.897 1.00 29.89 ?  31  LYS   B CE   1 
ATOM   4240 N NZ   . LYS   B 1 31  ? 55.254 -14.853 -16.661 1.00 31.67 ?  31  LYS   B NZ   1 
ATOM   4241 H H    . LYS   B 1 31  ? 50.919 -18.060 -15.014 1.00 21.23 ?  31  LYS   B H    1 
ATOM   4242 H HA   . LYS   B 1 31  ? 50.955 -16.072 -14.350 1.00 21.67 ?  31  LYS   B HA   1 
ATOM   4243 H HB2  . LYS   B 1 31  ? 50.470 -15.455 -17.063 1.00 25.23 ?  31  LYS   B HB2  1 
ATOM   4244 H HB3  . LYS   B 1 31  ? 51.051 -14.427 -15.998 1.00 25.23 ?  31  LYS   B HB3  1 
ATOM   4245 H HG2  . LYS   B 1 31  ? 52.995 -15.700 -15.819 1.00 29.12 ?  31  LYS   B HG2  1 
ATOM   4246 H HG3  . LYS   B 1 31  ? 52.416 -16.748 -16.866 1.00 29.12 ?  31  LYS   B HG3  1 
ATOM   4247 H HD2  . LYS   B 1 31  ? 52.599 -15.264 -18.576 1.00 33.10 ?  31  LYS   B HD2  1 
ATOM   4248 H HD3  . LYS   B 1 31  ? 52.896 -14.063 -17.576 1.00 33.10 ?  31  LYS   B HD3  1 
ATOM   4249 H HE2  . LYS   B 1 31  ? 54.691 -16.197 -18.055 1.00 35.87 ?  31  LYS   B HE2  1 
ATOM   4250 H HE3  . LYS   B 1 31  ? 54.873 -14.725 -18.637 1.00 35.87 ?  31  LYS   B HE3  1 
ATOM   4251 H HZ1  . LYS   B 1 31  ? 56.132 -14.880 -16.800 1.00 38.01 ?  31  LYS   B HZ1  1 
ATOM   4252 H HZ2  . LYS   B 1 31  ? 55.022 -14.025 -16.429 1.00 38.01 ?  31  LYS   B HZ2  1 
ATOM   4253 H HZ3  . LYS   B 1 31  ? 55.048 -15.407 -15.996 1.00 38.01 ?  31  LYS   B HZ3  1 
ATOM   4254 N N    . PRO   B 1 32  ? 48.392 -16.297 -13.685 1.00 14.50 ?  32  PRO   B N    1 
ATOM   4255 C CA   . PRO   B 1 32  ? 47.015 -15.941 -13.315 1.00 13.63 ?  32  PRO   B CA   1 
ATOM   4256 C C    . PRO   B 1 32  ? 46.934 -14.594 -12.613 1.00 13.70 ?  32  PRO   B C    1 
ATOM   4257 O O    . PRO   B 1 32  ? 47.862 -14.164 -11.921 1.00 15.23 ?  32  PRO   B O    1 
ATOM   4258 C CB   . PRO   B 1 32  ? 46.629 -17.057 -12.337 1.00 13.53 ?  32  PRO   B CB   1 
ATOM   4259 C CG   . PRO   B 1 32  ? 47.938 -17.387 -11.673 1.00 13.95 ?  32  PRO   B CG   1 
ATOM   4260 C CD   . PRO   B 1 32  ? 48.978 -17.278 -12.749 1.00 14.51 ?  32  PRO   B CD   1 
ATOM   4261 H HA   . PRO   B 1 32  ? 46.429 -15.958 -14.091 1.00 16.35 ?  32  PRO   B HA   1 
ATOM   4262 H HB2  . PRO   B 1 32  ? 45.981 -16.726 -11.693 1.00 16.23 ?  32  PRO   B HB2  1 
ATOM   4263 H HB3  . PRO   B 1 32  ? 46.279 -17.822 -12.823 1.00 16.23 ?  32  PRO   B HB3  1 
ATOM   4264 H HG2  . PRO   B 1 32  ? 48.119 -16.744 -10.967 1.00 16.74 ?  32  PRO   B HG2  1 
ATOM   4265 H HG3  . PRO   B 1 32  ? 47.914 -18.286 -11.318 1.00 16.74 ?  32  PRO   B HG3  1 
ATOM   4266 H HD2  . PRO   B 1 32  ? 49.810 -16.940 -12.381 1.00 17.41 ?  32  PRO   B HD2  1 
ATOM   4267 H HD3  . PRO   B 1 32  ? 49.100 -18.134 -13.184 1.00 17.41 ?  32  PRO   B HD3  1 
ATOM   4268 N N    . THR   B 1 33  ? 45.780 -13.941 -12.775 1.00 13.37 ?  33  THR   B N    1 
ATOM   4269 C CA   . THR   B 1 33  ? 45.488 -12.763 -11.969 1.00 13.47 ?  33  THR   B CA   1 
ATOM   4270 C C    . THR   B 1 33  ? 45.444 -13.113 -10.489 1.00 13.32 ?  33  THR   B C    1 
ATOM   4271 O O    . THR   B 1 33  ? 45.920 -12.334 -9.648  1.00 14.04 ?  33  THR   B O    1 
ATOM   4272 C CB   . THR   B 1 33  ? 44.169 -12.127 -12.413 1.00 14.23 ?  33  THR   B CB   1 
ATOM   4273 O OG1  . THR   B 1 33  ? 44.212 -11.874 -13.819 1.00 14.16 ?  33  THR   B OG1  1 
ATOM   4274 C CG2  . THR   B 1 33  ? 43.926 -10.825 -11.669 1.00 15.93 ?  33  THR   B CG2  1 
ATOM   4275 H H    . THR   B 1 33  ? 45.155 -14.164 -13.329 1.00 16.05 ?  33  THR   B H    1 
ATOM   4276 H HA   . THR   B 1 33  ? 46.189 -12.111 -12.102 1.00 16.16 ?  33  THR   B HA   1 
ATOM   4277 H HB   . THR   B 1 33  ? 43.431 -12.733 -12.221 1.00 17.08 ?  33  THR   B HB   1 
ATOM   4278 H HG1  . THR   B 1 33  ? 43.491 -11.511 -14.076 1.00 16.99 ?  33  THR   B HG1  1 
ATOM   4279 H HG21 . THR   B 1 33  ? 43.177 -10.354 -12.059 1.00 19.11 ?  33  THR   B HG21 1 
ATOM   4280 H HG22 . THR   B 1 33  ? 43.737 -11.007 -10.735 1.00 19.11 ?  33  THR   B HG22 1 
ATOM   4281 H HG23 . THR   B 1 33  ? 44.717 -10.265 -11.727 1.00 19.11 ?  33  THR   B HG23 1 
ATOM   4282 N N    . VAL   B 1 34  ? 44.886 -14.280 -10.150 1.00 12.47 ?  34  VAL   B N    1 
ATOM   4283 C CA   . VAL   B 1 34  ? 44.692 -14.678 -8.759  1.00 12.18 ?  34  VAL   B CA   1 
ATOM   4284 C C    . VAL   B 1 34  ? 45.123 -16.126 -8.592  1.00 10.92 ?  34  VAL   B C    1 
ATOM   4285 O O    . VAL   B 1 34  ? 44.606 -17.014 -9.278  1.00 11.62 ?  34  VAL   B O    1 
ATOM   4286 C CB   . VAL   B 1 34  ? 43.221 -14.540 -8.315  1.00 13.03 ?  34  VAL   B CB   1 
ATOM   4287 C CG1  . VAL   B 1 34  ? 43.057 -14.984 -6.866  1.00 13.50 ?  34  VAL   B CG1  1 
ATOM   4288 C CG2  . VAL   B 1 34  ? 42.719 -13.120 -8.511  1.00 13.98 ?  34  VAL   B CG2  1 
ATOM   4289 H H    . VAL   B 1 34  ? 44.620 -14.871 -10.719 1.00 14.96 ?  34  VAL   B H    1 
ATOM   4290 H HA   . VAL   B 1 34  ? 45.243 -14.125 -8.182  1.00 14.61 ?  34  VAL   B HA   1 
ATOM   4291 H HB   . VAL   B 1 34  ? 42.676 -15.121 -8.867  1.00 15.64 ?  34  VAL   B HB   1 
ATOM   4292 H HG11 . VAL   B 1 34  ? 42.199 -14.674 -6.536  1.00 16.20 ?  34  VAL   B HG11 1 
ATOM   4293 H HG12 . VAL   B 1 34  ? 43.091 -15.954 -6.824  1.00 16.20 ?  34  VAL   B HG12 1 
ATOM   4294 H HG13 . VAL   B 1 34  ? 43.772 -14.604 -6.334  1.00 16.20 ?  34  VAL   B HG13 1 
ATOM   4295 H HG21 . VAL   B 1 34  ? 41.802 -13.064 -8.198  1.00 16.77 ?  34  VAL   B HG21 1 
ATOM   4296 H HG22 . VAL   B 1 34  ? 43.280 -12.513 -8.007  1.00 16.77 ?  34  VAL   B HG22 1 
ATOM   4297 H HG23 . VAL   B 1 34  ? 42.758 -12.899 -9.457  1.00 16.77 ?  34  VAL   B HG23 1 
ATOM   4298 N N    . VAL   B 1 35  ? 46.023 -16.374 -7.647  1.00 10.35 ?  35  VAL   B N    1 
ATOM   4299 C CA   . VAL   B 1 35  ? 46.263 -17.719 -7.129  1.00 10.36 ?  35  VAL   B CA   1 
ATOM   4300 C C    . VAL   B 1 35  ? 45.723 -17.774 -5.709  1.00 10.11 ?  35  VAL   B C    1 
ATOM   4301 O O    . VAL   B 1 35  ? 45.945 -16.853 -4.916  1.00 10.38 ?  35  VAL   B O    1 
ATOM   4302 C CB   . VAL   B 1 35  ? 47.747 -18.139 -7.208  1.00 11.21 ?  35  VAL   B CB   1 
ATOM   4303 C CG1  . VAL   B 1 35  ? 48.643 -17.300 -6.285  1.00 12.03 ?  35  VAL   B CG1  1 
ATOM   4304 C CG2  . VAL   B 1 35  ? 47.901 -19.635 -6.894  1.00 11.89 ?  35  VAL   B CG2  1 
ATOM   4305 H H    . VAL   B 1 35  ? 46.515 -15.769 -7.282  1.00 12.41 ?  35  VAL   B H    1 
ATOM   4306 H HA   . VAL   B 1 35  ? 45.747 -18.349 -7.655  1.00 12.43 ?  35  VAL   B HA   1 
ATOM   4307 H HB   . VAL   B 1 35  ? 48.051 -18.001 -8.117  1.00 13.45 ?  35  VAL   B HB   1 
ATOM   4308 H HG11 . VAL   B 1 35  ? 49.566 -17.523 -6.466  1.00 14.43 ?  35  VAL   B HG11 1 
ATOM   4309 H HG12 . VAL   B 1 35  ? 48.479 -16.365 -6.458  1.00 14.43 ?  35  VAL   B HG12 1 
ATOM   4310 H HG13 . VAL   B 1 35  ? 48.424 -17.514 -5.362  1.00 14.43 ?  35  VAL   B HG13 1 
ATOM   4311 H HG21 . VAL   B 1 35  ? 48.827 -19.890 -6.992  1.00 14.26 ?  35  VAL   B HG21 1 
ATOM   4312 H HG22 . VAL   B 1 35  ? 47.604 -19.804 -5.982  1.00 14.26 ?  35  VAL   B HG22 1 
ATOM   4313 H HG23 . VAL   B 1 35  ? 47.349 -20.150 -7.512  1.00 14.26 ?  35  VAL   B HG23 1 
ATOM   4314 N N    . VAL   B 1 36  ? 45.006 -18.849 -5.392  1.00 10.05 ?  36  VAL   B N    1 
ATOM   4315 C CA   . VAL   B 1 36  ? 44.461 -19.057 -4.061  1.00 10.01 ?  36  VAL   B CA   1 
ATOM   4316 C C    . VAL   B 1 36  ? 45.467 -19.820 -3.208  1.00 9.78  ?  36  VAL   B C    1 
ATOM   4317 O O    . VAL   B 1 36  ? 46.011 -20.853 -3.629  1.00 10.71 ?  36  VAL   B O    1 
ATOM   4318 C CB   . VAL   B 1 36  ? 43.124 -19.815 -4.137  1.00 10.52 ?  36  VAL   B CB   1 
ATOM   4319 C CG1  . VAL   B 1 36  ? 42.623 -20.184 -2.746  1.00 11.48 ?  36  VAL   B CG1  1 
ATOM   4320 C CG2  . VAL   B 1 36  ? 42.094 -18.989 -4.895  1.00 11.23 ?  36  VAL   B CG2  1 
ATOM   4321 H H    . VAL   B 1 36  ? 44.828 -19.486 -5.942  1.00 12.06 ?  36  VAL   B H    1 
ATOM   4322 H HA   . VAL   B 1 36  ? 44.296 -18.196 -3.642  1.00 12.02 ?  36  VAL   B HA   1 
ATOM   4323 H HB   . VAL   B 1 36  ? 43.259 -20.639 -4.632  1.00 12.62 ?  36  VAL   B HB   1 
ATOM   4324 H HG11 . VAL   B 1 36  ? 41.682 -20.416 -2.804  1.00 13.78 ?  36  VAL   B HG11 1 
ATOM   4325 H HG12 . VAL   B 1 36  ? 43.131 -20.931 -2.410  1.00 13.78 ?  36  VAL   B HG12 1 
ATOM   4326 H HG13 . VAL   B 1 36  ? 42.730 -19.412 -2.162  1.00 13.78 ?  36  VAL   B HG13 1 
ATOM   4327 H HG21 . VAL   B 1 36  ? 41.252 -19.468 -4.914  1.00 13.48 ?  36  VAL   B HG21 1 
ATOM   4328 H HG22 . VAL   B 1 36  ? 41.980 -18.136 -4.447  1.00 13.48 ?  36  VAL   B HG22 1 
ATOM   4329 H HG23 . VAL   B 1 36  ? 42.410 -18.842 -5.804  1.00 13.48 ?  36  VAL   B HG23 1 
ATOM   4330 N N    . ASN   B 1 37  ? 45.680 -19.330 -1.990  1.00 9.97  ?  37  ASN   B N    1 
ATOM   4331 C CA   . ASN   B 1 37  ? 46.434 -20.055 -0.981  1.00 10.42 ?  37  ASN   B CA   1 
ATOM   4332 C C    . ASN   B 1 37  ? 45.488 -20.728 0.005   1.00 10.42 ?  37  ASN   B C    1 
ATOM   4333 O O    . ASN   B 1 37  ? 44.480 -20.149 0.416   1.00 10.87 ?  37  ASN   B O    1 
ATOM   4334 C CB   . ASN   B 1 37  ? 47.368 -19.110 -0.224  1.00 10.76 ?  37  ASN   B CB   1 
ATOM   4335 C CG   . ASN   B 1 37  ? 48.218 -19.824 0.791   1.00 10.96 ?  37  ASN   B CG   1 
ATOM   4336 O OD1  . ASN   B 1 37  ? 48.556 -20.998 0.616   1.00 11.36 ?  37  ASN   B OD1  1 
ATOM   4337 N ND2  . ASN   B 1 37  ? 48.571 -19.125 1.862   1.00 10.92 ?  37  ASN   B ND2  1 
ATOM   4338 H H    . ASN   B 1 37  ? 45.390 -18.568 -1.713  1.00 11.96 ?  37  ASN   B H    1 
ATOM   4339 H HA   . ASN   B 1 37  ? 46.968 -20.747 -1.401  1.00 12.50 ?  37  ASN   B HA   1 
ATOM   4340 H HB2  . ASN   B 1 37  ? 47.962 -18.685 -0.861  1.00 12.91 ?  37  ASN   B HB2  1 
ATOM   4341 H HB3  . ASN   B 1 37  ? 46.844 -18.448 0.243   1.00 12.91 ?  37  ASN   B HB3  1 
ATOM   4342 H HD21 . ASN   B 1 37  ? 49.066 -19.487 2.468   1.00 13.11 ?  37  ASN   B HD21 1 
ATOM   4343 H HD22 . ASN   B 1 37  ? 48.324 -18.313 1.947   1.00 13.11 ?  37  ASN   B HD22 1 
ATOM   4344 N N    . ALA   B 1 38  ? 45.839 -21.958 0.386   1.00 10.61 ?  38  ALA   B N    1 
ATOM   4345 C CA   . ALA   B 1 38  ? 45.183 -22.707 1.461   1.00 11.14 ?  38  ALA   B CA   1 
ATOM   4346 C C    . ALA   B 1 38  ? 45.768 -22.222 2.787   1.00 11.17 ?  38  ALA   B C    1 
ATOM   4347 O O    . ALA   B 1 38  ? 46.674 -22.828 3.371   1.00 11.80 ?  38  ALA   B O    1 
ATOM   4348 C CB   . ALA   B 1 38  ? 45.399 -24.201 1.264   1.00 12.39 ?  38  ALA   B CB   1 
ATOM   4349 H H    . ALA   B 1 38  ? 46.492 -22.393 0.035   1.00 12.73 ?  38  ALA   B H    1 
ATOM   4350 H HA   . ALA   B 1 38  ? 44.229 -22.525 1.455   1.00 13.37 ?  38  ALA   B HA   1 
ATOM   4351 H HB1  . ALA   B 1 38  ? 44.951 -24.683 1.987   1.00 14.87 ?  38  ALA   B HB1  1 
ATOM   4352 H HB2  . ALA   B 1 38  ? 45.013 -24.467 0.415   1.00 14.87 ?  38  ALA   B HB2  1 
ATOM   4353 H HB3  . ALA   B 1 38  ? 46.343 -24.393 1.280   1.00 14.87 ?  38  ALA   B HB3  1 
ATOM   4354 N N    . ALA   B 1 39  ? 45.252 -21.080 3.245   1.00 11.03 ?  39  ALA   B N    1 
ATOM   4355 C CA   . ALA   B 1 39  ? 45.803 -20.347 4.375   1.00 11.17 ?  39  ALA   B CA   1 
ATOM   4356 C C    . ALA   B 1 39  ? 45.186 -20.796 5.698   1.00 11.21 ?  39  ALA   B C    1 
ATOM   4357 O O    . ALA   B 1 39  ? 44.153 -21.467 5.745   1.00 12.05 ?  39  ALA   B O    1 
ATOM   4358 C CB   . ALA   B 1 39  ? 45.566 -18.846 4.185   1.00 11.94 ?  39  ALA   B CB   1 
ATOM   4359 H H    . ALA   B 1 39  ? 44.560 -20.702 2.901   1.00 13.24 ?  39  ALA   B H    1 
ATOM   4360 H HA   . ALA   B 1 39  ? 46.758 -20.499 4.419   1.00 13.40 ?  39  ALA   B HA   1 
ATOM   4361 H HB1  . ALA   B 1 39  ? 45.939 -18.369 4.943   1.00 14.32 ?  39  ALA   B HB1  1 
ATOM   4362 H HB2  . ALA   B 1 39  ? 46.004 -18.559 3.367   1.00 14.32 ?  39  ALA   B HB2  1 
ATOM   4363 H HB3  . ALA   B 1 39  ? 44.613 -18.680 4.125   1.00 14.32 ?  39  ALA   B HB3  1 
ATOM   4364 N N    . ASN   B 1 40  ? 45.830 -20.378 6.786   1.00 12.07 ?  40  ASN   B N    1 
ATOM   4365 C CA   . ASN   B 1 40  ? 45.264 -20.425 8.126   1.00 12.56 ?  40  ASN   B CA   1 
ATOM   4366 C C    . ASN   B 1 40  ? 45.085 -18.998 8.648   1.00 12.32 ?  40  ASN   B C    1 
ATOM   4367 O O    . ASN   B 1 40  ? 45.498 -18.017 8.021   1.00 12.27 ?  40  ASN   B O    1 
ATOM   4368 C CB   . ASN   B 1 40  ? 46.115 -21.299 9.062   1.00 13.40 ?  40  ASN   B CB   1 
ATOM   4369 C CG   . ASN   B 1 40  ? 47.570 -20.892 9.087   1.00 14.54 ?  40  ASN   B CG   1 
ATOM   4370 O OD1  . ASN   B 1 40  ? 47.896 -19.711 9.152   1.00 16.33 ?  40  ASN   B OD1  1 
ATOM   4371 N ND2  . ASN   B 1 40  ? 48.455 -21.871 9.044   1.00 14.69 ?  40  ASN   B ND2  1 
ATOM   4372 H H    . ASN   B 1 40  ? 46.629 -20.057 6.766   1.00 14.48 ?  40  ASN   B H    1 
ATOM   4373 H HA   . ASN   B 1 40  ? 44.384 -20.822 8.079   1.00 15.08 ?  40  ASN   B HA   1 
ATOM   4374 H HB2  . ASN   B 1 40  ? 45.767 -21.227 9.965   1.00 16.08 ?  40  ASN   B HB2  1 
ATOM   4375 H HB3  . ASN   B 1 40  ? 46.065 -22.220 8.760   1.00 16.08 ?  40  ASN   B HB3  1 
ATOM   4376 H HD21 . ASN   B 1 40  ? 49.296 -21.692 9.057   1.00 17.62 ?  40  ASN   B HD21 1 
ATOM   4377 H HD22 . ASN   B 1 40  ? 48.191 -22.689 9.000   1.00 17.62 ?  40  ASN   B HD22 1 
ATOM   4378 N N    . VAL   B 1 41  ? 44.432 -18.873 9.806   1.00 12.82 ?  41  VAL   B N    1 
ATOM   4379 C CA   . VAL   B 1 41  ? 43.976 -17.550 10.247  1.00 13.48 ?  41  VAL   B CA   1 
ATOM   4380 C C    . VAL   B 1 41  ? 45.128 -16.597 10.550  1.00 13.19 ?  41  VAL   B C    1 
ATOM   4381 O O    . VAL   B 1 41  ? 44.950 -15.375 10.472  1.00 13.20 ?  41  VAL   B O    1 
ATOM   4382 C CB   . VAL   B 1 41  ? 42.987 -17.622 11.428  1.00 14.76 ?  41  VAL   B CB   1 
ATOM   4383 C CG1  . VAL   B 1 41  ? 41.686 -18.302 11.015  1.00 15.39 ?  41  VAL   B CG1  1 
ATOM   4384 C CG2  . VAL   B 1 41  ? 43.617 -18.305 12.628  1.00 15.87 ?  41  VAL   B CG2  1 
ATOM   4385 H H    . VAL   B 1 41  ? 44.249 -19.515 10.343  1.00 15.38 ?  41  VAL   B H    1 
ATOM   4386 H HA   . VAL   B 1 41  ? 43.485 -17.156 9.514   1.00 16.18 ?  41  VAL   B HA   1 
ATOM   4387 H HB   . VAL   B 1 41  ? 42.761 -16.716 11.697  1.00 17.71 ?  41  VAL   B HB   1 
ATOM   4388 H HG11 . VAL   B 1 41  ? 41.072 -18.295 11.767  1.00 18.47 ?  41  VAL   B HG11 1 
ATOM   4389 H HG12 . VAL   B 1 41  ? 41.301 -17.818 10.269  1.00 18.47 ?  41  VAL   B HG12 1 
ATOM   4390 H HG13 . VAL   B 1 41  ? 41.879 -19.216 10.755  1.00 18.47 ?  41  VAL   B HG13 1 
ATOM   4391 H HG21 . VAL   B 1 41  ? 42.970 -18.335 13.351  1.00 19.04 ?  41  VAL   B HG21 1 
ATOM   4392 H HG22 . VAL   B 1 41  ? 43.874 -19.206 12.380  1.00 19.04 ?  41  VAL   B HG22 1 
ATOM   4393 H HG23 . VAL   B 1 41  ? 44.397 -17.801 12.905  1.00 19.04 ?  41  VAL   B HG23 1 
ATOM   4394 N N    . TYR   B 1 42  ? 46.297 -17.113 10.931  1.00 13.44 ?  42  TYR   B N    1 
ATOM   4395 C CA   . TYR   B 1 42  ? 47.449 -16.264 11.202  1.00 14.20 ?  42  TYR   B CA   1 
ATOM   4396 C C    . TYR   B 1 42  ? 48.414 -16.193 10.023  1.00 13.37 ?  42  TYR   B C    1 
ATOM   4397 O O    . TYR   B 1 42  ? 49.502 -15.616 10.156  1.00 14.44 ?  42  TYR   B O    1 
ATOM   4398 C CB   . TYR   B 1 42  ? 48.145 -16.669 12.507  1.00 16.29 ?  42  TYR   B CB   1 
ATOM   4399 C CG   . TYR   B 1 42  ? 47.544 -15.984 13.730  1.00 16.56 ?  42  TYR   B CG   1 
ATOM   4400 C CD1  . TYR   B 1 42  ? 47.772 -14.632 13.971  1.00 15.70 ?  42  TYR   B CD1  1 
ATOM   4401 C CD2  . TYR   B 1 42  ? 46.749 -16.679 14.631  1.00 18.10 ?  42  TYR   B CD2  1 
ATOM   4402 C CE1  . TYR   B 1 42  ? 47.229 -13.992 15.071  1.00 16.85 ?  42  TYR   B CE1  1 
ATOM   4403 C CE2  . TYR   B 1 42  ? 46.203 -16.048 15.740  1.00 18.22 ?  42  TYR   B CE2  1 
ATOM   4404 C CZ   . TYR   B 1 42  ? 46.445 -14.701 15.956  1.00 18.63 ?  42  TYR   B CZ   1 
ATOM   4405 O OH   . TYR   B 1 42  ? 45.910 -14.056 17.054  1.00 21.95 ?  42  TYR   B OH   1 
ATOM   4406 H H    . TYR   B 1 42  ? 46.444 -17.960 11.031  1.00 16.12 ?  42  TYR   B H    1 
ATOM   4407 H HA   . TYR   B 1 42  ? 47.119 -15.365 11.336  1.00 17.04 ?  42  TYR   B HA   1 
ATOM   4408 H HB2  . TYR   B 1 42  ? 48.061 -17.627 12.628  1.00 19.55 ?  42  TYR   B HB2  1 
ATOM   4409 H HB3  . TYR   B 1 42  ? 49.081 -16.421 12.452  1.00 19.55 ?  42  TYR   B HB3  1 
ATOM   4410 H HD1  . TYR   B 1 42  ? 48.304 -14.148 13.373  1.00 18.84 ?  42  TYR   B HD1  1 
ATOM   4411 H HD2  . TYR   B 1 42  ? 46.580 -17.583 14.485  1.00 21.71 ?  42  TYR   B HD2  1 
ATOM   4412 H HE1  . TYR   B 1 42  ? 47.400 -13.090 15.211  1.00 20.21 ?  42  TYR   B HE1  1 
ATOM   4413 H HE2  . TYR   B 1 42  ? 45.671 -16.526 16.331  1.00 21.86 ?  42  TYR   B HE2  1 
ATOM   4414 H HH   . TYR   B 1 42  ? 46.145 -13.253 17.045  1.00 26.34 ?  42  TYR   B HH   1 
ATOM   4415 N N    . LEU   B 1 43  ? 48.017 -16.711 8.862   1.00 12.21 ?  43  LEU   B N    1 
ATOM   4416 C CA   . LEU   B 1 43  ? 48.829 -16.637 7.651   1.00 12.18 ?  43  LEU   B CA   1 
ATOM   4417 C C    . LEU   B 1 43  ? 50.244 -17.142 7.909   1.00 12.38 ?  43  LEU   B C    1 
ATOM   4418 O O    . LEU   B 1 43  ? 51.227 -16.546 7.465   1.00 13.00 ?  43  LEU   B O    1 
ATOM   4419 C CB   . LEU   B 1 43  ? 48.841 -15.231 7.047   1.00 12.32 ?  43  LEU   B CB   1 
ATOM   4420 C CG   . LEU   B 1 43  ? 47.487 -14.617 6.668   1.00 12.28 ?  43  LEU   B CG   1 
ATOM   4421 C CD1  . LEU   B 1 43  ? 47.694 -13.218 6.092   1.00 13.53 ?  43  LEU   B CD1  1 
ATOM   4422 C CD2  . LEU   B 1 43  ? 46.729 -15.503 5.691   1.00 12.29 ?  43  LEU   B CD2  1 
ATOM   4423 H H    . LEU   B 1 43  ? 47.272 -17.130 8.750   1.00 14.65 ?  43  LEU   B H    1 
ATOM   4424 H HA   . LEU   B 1 43  ? 48.433 -17.228 6.989   1.00 14.61 ?  43  LEU   B HA   1 
ATOM   4425 H HB2  . LEU   B 1 43  ? 49.258 -14.635 7.686   1.00 14.79 ?  43  LEU   B HB2  1 
ATOM   4426 H HB3  . LEU   B 1 43  ? 49.375 -15.262 6.239   1.00 14.79 ?  43  LEU   B HB3  1 
ATOM   4427 H HG   . LEU   B 1 43  ? 46.949 -14.529 7.468   1.00 14.73 ?  43  LEU   B HG   1 
ATOM   4428 H HD11 . LEU   B 1 43  ? 46.829 -12.841 5.858   1.00 16.23 ?  43  LEU   B HD11 1 
ATOM   4429 H HD12 . LEU   B 1 43  ? 48.124 -12.660 6.761   1.00 16.23 ?  43  LEU   B HD12 1 
ATOM   4430 H HD13 . LEU   B 1 43  ? 48.252 -13.277 5.302   1.00 16.23 ?  43  LEU   B HD13 1 
ATOM   4431 H HD21 . LEU   B 1 43  ? 45.926 -15.041 5.402   1.00 14.75 ?  43  LEU   B HD21 1 
ATOM   4432 H HD22 . LEU   B 1 43  ? 47.296 -15.691 4.927   1.00 14.75 ?  43  LEU   B HD22 1 
ATOM   4433 H HD23 . LEU   B 1 43  ? 46.490 -16.332 6.137   1.00 14.75 ?  43  LEU   B HD23 1 
ATOM   4434 N N    . LYS   B 1 44  ? 50.345 -18.261 8.627   1.00 12.26 ?  44  LYS   B N    1 
ATOM   4435 C CA   . LYS   B 1 44  ? 51.612 -18.941 8.863   1.00 12.98 ?  44  LYS   B CA   1 
ATOM   4436 C C    . LYS   B 1 44  ? 51.728 -20.057 7.832   1.00 12.56 ?  44  LYS   B C    1 
ATOM   4437 O O    . LYS   B 1 44  ? 51.033 -21.075 7.920   1.00 14.01 ?  44  LYS   B O    1 
ATOM   4438 C CB   . LYS   B 1 44  ? 51.668 -19.460 10.299  1.00 14.60 ?  44  LYS   B CB   1 
ATOM   4439 C CG   . LYS   B 1 44  ? 51.857 -18.355 11.326  1.00 17.32 ?  44  LYS   B CG   1 
ATOM   4440 C CD   . LYS   B 1 44  ? 53.065 -17.499 10.941  1.00 20.78 ?  44  LYS   B CD   1 
ATOM   4441 C CE   . LYS   B 1 44  ? 53.526 -16.583 12.045  1.00 23.66 ?  44  LYS   B CE   1 
ATOM   4442 N NZ   . LYS   B 1 44  ? 54.716 -15.787 11.644  1.00 25.07 ?  44  LYS   B NZ   1 
ATOM   4443 H H    . LYS   B 1 44  ? 49.672 -18.648 8.999   1.00 14.70 ?  44  LYS   B H    1 
ATOM   4444 H HA   . LYS   B 1 44  ? 52.341 -18.326 8.701   1.00 15.57 ?  44  LYS   B HA   1 
ATOM   4445 H HB2  . LYS   B 1 44  ? 50.830 -19.914 10.503  1.00 17.52 ?  44  LYS   B HB2  1 
ATOM   4446 H HB3  . LYS   B 1 44  ? 52.406 -20.077 10.384  1.00 17.52 ?  44  LYS   B HB3  1 
ATOM   4447 H HG2  . LYS   B 1 44  ? 51.069 -17.793 11.351  1.00 20.78 ?  44  LYS   B HG2  1 
ATOM   4448 H HG3  . LYS   B 1 44  ? 52.022 -18.751 12.200  1.00 20.78 ?  44  LYS   B HG3  1 
ATOM   4449 H HD2  . LYS   B 1 44  ? 53.798 -18.092 10.692  1.00 24.93 ?  44  LYS   B HD2  1 
ATOM   4450 H HD3  . LYS   B 1 44  ? 52.822 -16.943 10.184  1.00 24.93 ?  44  LYS   B HD3  1 
ATOM   4451 H HE2  . LYS   B 1 44  ? 52.813 -15.966 12.248  1.00 28.39 ?  44  LYS   B HE2  1 
ATOM   4452 H HE3  . LYS   B 1 44  ? 53.757 -17.113 12.822  1.00 28.39 ?  44  LYS   B HE3  1 
ATOM   4453 H HZ1  . LYS   B 1 44  ? 54.960 -15.252 12.311  1.00 30.09 ?  44  LYS   B HZ1  1 
ATOM   4454 H HZ2  . LYS   B 1 44  ? 55.393 -16.325 11.440  1.00 30.09 ?  44  LYS   B HZ2  1 
ATOM   4455 H HZ3  . LYS   B 1 44  ? 54.521 -15.286 10.931  1.00 30.09 ?  44  LYS   B HZ3  1 
ATOM   4456 N N    . HIS   B 1 45  ? 52.583 -19.841 6.834   1.00 12.09 ?  45  HIS   B N    1 
ATOM   4457 C CA   . HIS   B 1 45  ? 52.595 -20.668 5.629   1.00 12.36 ?  45  HIS   B CA   1 
ATOM   4458 C C    . HIS   B 1 45  ? 53.612 -21.793 5.785   1.00 14.62 ?  45  HIS   B C    1 
ATOM   4459 O O    . HIS   B 1 45  ? 54.669 -21.812 5.164   1.00 16.75 ?  45  HIS   B O    1 
ATOM   4460 C CB   . HIS   B 1 45  ? 52.905 -19.816 4.410   1.00 12.63 ?  45  HIS   B CB   1 
ATOM   4461 C CG   . HIS   B 1 45  ? 52.036 -18.610 4.301   1.00 12.19 ?  45  HIS   B CG   1 
ATOM   4462 N ND1  . HIS   B 1 45  ? 50.659 -18.685 4.269   1.00 12.45 ?  45  HIS   B ND1  1 
ATOM   4463 C CD2  . HIS   B 1 45  ? 52.356 -17.298 4.233   1.00 13.23 ?  45  HIS   B CD2  1 
ATOM   4464 C CE1  . HIS   B 1 45  ? 50.173 -17.460 4.167   1.00 12.37 ?  45  HIS   B CE1  1 
ATOM   4465 N NE2  . HIS   B 1 45  ? 51.179 -16.601 4.144   1.00 12.90 ?  45  HIS   B NE2  1 
ATOM   4466 H H    . HIS   B 1 45  ? 53.164 -19.207 6.825   1.00 14.51 ?  45  HIS   B H    1 
ATOM   4467 H HA   . HIS   B 1 45  ? 51.714 -21.065 5.507   1.00 14.83 ?  45  HIS   B HA   1 
ATOM   4468 H HB2  . HIS   B 1 45  ? 53.823 -19.524 4.457   1.00 15.15 ?  45  HIS   B HB2  1 
ATOM   4469 H HB3  . HIS   B 1 45  ? 52.770 -20.358 3.610   1.00 15.15 ?  45  HIS   B HB3  1 
ATOM   4470 H HD2  . HIS   B 1 45  ? 53.213 -16.937 4.237   1.00 15.87 ?  45  HIS   B HD2  1 
ATOM   4471 H HE1  . HIS   B 1 45  ? 49.270 -17.236 4.114   1.00 14.85 ?  45  HIS   B HE1  1 
ATOM   4472 H HE2  . HIS   B 1 45  ? 51.106 -15.745 4.088   1.00 15.48 ?  45  HIS   B HE2  1 
ATOM   4473 N N    A GLY   B 1 46  ? 53.252 -22.759 6.624   0.84 15.09 ?  46  GLY   B N    1 
ATOM   4474 N N    B GLY   B 1 46  ? 53.259 -22.750 6.636   0.16 15.39 ?  46  GLY   B N    1 
ATOM   4475 C CA   A GLY   B 1 46  ? 54.170 -23.824 6.987   0.84 16.62 ?  46  GLY   B CA   1 
ATOM   4476 C CA   B GLY   B 1 46  ? 54.175 -23.818 6.972   0.16 16.28 ?  46  GLY   B CA   1 
ATOM   4477 C C    A GLY   B 1 46  ? 54.215 -25.028 6.065   0.84 18.32 ?  46  GLY   B C    1 
ATOM   4478 C C    B GLY   B 1 46  ? 54.199 -24.971 5.989   0.16 17.24 ?  46  GLY   B C    1 
ATOM   4479 O O    A GLY   B 1 46  ? 55.286 -25.425 5.595   0.84 21.52 ?  46  GLY   B O    1 
ATOM   4480 O O    B GLY   B 1 46  ? 55.235 -25.251 5.379   0.16 17.67 ?  46  GLY   B O    1 
ATOM   4481 H H    A GLY   B 1 46  ? 52.482 -22.802 7.015   0.84 18.11 ?  46  GLY   B H    1 
ATOM   4482 H H    B GLY   B 1 46  ? 52.495 -22.795 7.036   0.16 18.47 ?  46  GLY   B H    1 
ATOM   4483 H HA2  A GLY   B 1 46  ? 55.063 -23.454 7.041   0.84 19.94 ?  46  GLY   B HA2  1 
ATOM   4484 H HA2  B GLY   B 1 46  ? 55.071 -23.454 7.025   0.16 19.53 ?  46  GLY   B HA2  1 
ATOM   4485 H HA3  A GLY   B 1 46  ? 53.929 -24.150 7.869   0.84 19.94 ?  46  GLY   B HA3  1 
ATOM   4486 H HA3  B GLY   B 1 46  ? 53.940 -24.167 7.845   0.16 19.53 ?  46  GLY   B HA3  1 
ATOM   4487 N N    . GLY   B 1 47  ? 53.063 -25.646 5.818   1.00 17.97 ?  47  GLY   B N    1 
ATOM   4488 C CA   . GLY   B 1 47  ? 53.008 -26.906 5.105   1.00 15.97 ?  47  GLY   B CA   1 
ATOM   4489 C C    . GLY   B 1 47  ? 52.096 -26.874 3.894   1.00 14.14 ?  47  GLY   B C    1 
ATOM   4490 O O    . GLY   B 1 47  ? 51.444 -25.869 3.598   1.00 14.02 ?  47  GLY   B O    1 
ATOM   4491 H H    A GLY   B 1 47  ? 52.296 -25.367 6.086   0.84 21.57 ?  47  GLY   B H    1 
ATOM   4492 H H    B GLY   B 1 47  ? 52.301 -25.387 6.118   0.16 21.57 ?  47  GLY   B H    1 
ATOM   4493 H HA2  . GLY   B 1 47  ? 53.897 -27.154 4.808   1.00 19.16 ?  47  GLY   B HA2  1 
ATOM   4494 H HA3  . GLY   B 1 47  ? 52.692 -27.599 5.710   1.00 19.16 ?  47  GLY   B HA3  1 
ATOM   4495 N N    . GLY   B 1 48  ? 52.046 -28.017 3.208   1.00 13.53 ?  48  GLY   B N    1 
ATOM   4496 C CA   . GLY   B 1 48  ? 51.123 -28.161 2.100   1.00 13.20 ?  48  GLY   B CA   1 
ATOM   4497 C C    . GLY   B 1 48  ? 51.266 -27.053 1.082   1.00 12.49 ?  48  GLY   B C    1 
ATOM   4498 O O    . GLY   B 1 48  ? 52.370 -26.588 0.774   1.00 13.04 ?  48  GLY   B O    1 
ATOM   4499 H H    . GLY   B 1 48  ? 52.537 -28.703 3.360   1.00 16.23 ?  48  GLY   B H    1 
ATOM   4500 H HA2  . GLY   B 1 48  ? 51.281 -29.010 1.658   1.00 15.84 ?  48  GLY   B HA2  1 
ATOM   4501 H HA3  . GLY   B 1 48  ? 50.213 -28.153 2.435   1.00 15.84 ?  48  GLY   B HA3  1 
ATOM   4502 N N    . VAL   B 1 49  ? 50.121 -26.623 0.549   1.00 12.40 ?  49  VAL   B N    1 
ATOM   4503 C CA   . VAL   B 1 49  ? 50.104 -25.594 -0.489  1.00 12.70 ?  49  VAL   B CA   1 
ATOM   4504 C C    . VAL   B 1 49  ? 50.759 -24.307 0.002   1.00 11.73 ?  49  VAL   B C    1 
ATOM   4505 O O    . VAL   B 1 49  ? 51.545 -23.685 -0.721  1.00 12.28 ?  49  VAL   B O    1 
ATOM   4506 C CB   . VAL   B 1 49  ? 48.663 -25.343 -0.973  1.00 13.79 ?  49  VAL   B CB   1 
ATOM   4507 C CG1  . VAL   B 1 49  ? 48.593 -24.085 -1.830  1.00 13.89 ?  49  VAL   B CG1  1 
ATOM   4508 C CG2  . VAL   B 1 49  ? 48.142 -26.546 -1.747  1.00 15.44 ?  49  VAL   B CG2  1 
ATOM   4509 H H    . VAL   B 1 49  ? 49.336 -26.910 0.769   1.00 14.88 ?  49  VAL   B H    1 
ATOM   4510 H HA   . VAL   B 1 49  ? 50.613 -25.911 -1.252  1.00 15.23 ?  49  VAL   B HA   1 
ATOM   4511 H HB   . VAL   B 1 49  ? 48.089 -25.211 -0.203  1.00 16.55 ?  49  VAL   B HB   1 
ATOM   4512 H HG11 . VAL   B 1 49  ? 47.769 -24.100 -2.344  1.00 16.67 ?  49  VAL   B HG11 1 
ATOM   4513 H HG12 . VAL   B 1 49  ? 48.604 -23.304 -1.253  1.00 16.67 ?  49  VAL   B HG12 1 
ATOM   4514 H HG13 . VAL   B 1 49  ? 49.354 -24.067 -2.430  1.00 16.67 ?  49  VAL   B HG13 1 
ATOM   4515 H HG21 . VAL   B 1 49  ? 47.234 -26.368 -2.037  1.00 18.53 ?  49  VAL   B HG21 1 
ATOM   4516 H HG22 . VAL   B 1 49  ? 48.712 -26.694 -2.521  1.00 18.53 ?  49  VAL   B HG22 1 
ATOM   4517 H HG23 . VAL   B 1 49  ? 48.161 -27.324 -1.170  1.00 18.53 ?  49  VAL   B HG23 1 
ATOM   4518 N N    . ALA   B 1 50  ? 50.417 -23.863 1.213   1.00 11.78 ?  50  ALA   B N    1 
ATOM   4519 C CA   . ALA   B 1 50  ? 50.939 -22.586 1.692   1.00 11.40 ?  50  ALA   B CA   1 
ATOM   4520 C C    . ALA   B 1 50  ? 52.458 -22.617 1.794   1.00 11.73 ?  50  ALA   B C    1 
ATOM   4521 O O    . ALA   B 1 50  ? 53.136 -21.645 1.430   1.00 11.44 ?  50  ALA   B O    1 
ATOM   4522 C CB   . ALA   B 1 50  ? 50.311 -22.231 3.038   1.00 11.78 ?  50  ALA   B CB   1 
ATOM   4523 H H    . ALA   B 1 50  ? 49.903 -24.278 1.764   1.00 14.13 ?  50  ALA   B H    1 
ATOM   4524 H HA   . ALA   B 1 50  ? 50.705 -21.894 1.063   1.00 13.67 ?  50  ALA   B HA   1 
ATOM   4525 H HB1  . ALA   B 1 50  ? 50.667 -21.379 3.340   1.00 14.13 ?  50  ALA   B HB1  1 
ATOM   4526 H HB2  . ALA   B 1 50  ? 49.348 -22.166 2.931   1.00 14.13 ?  50  ALA   B HB2  1 
ATOM   4527 H HB3  . ALA   B 1 50  ? 50.524 -22.923 3.685   1.00 14.13 ?  50  ALA   B HB3  1 
ATOM   4528 N N    . GLY   B 1 51  ? 53.011 -23.714 2.307   1.00 12.25 ?  51  GLY   B N    1 
ATOM   4529 C CA   . GLY   B 1 51  ? 54.455 -23.812 2.381   1.00 13.20 ?  51  GLY   B CA   1 
ATOM   4530 C C    . GLY   B 1 51  ? 55.105 -23.763 1.013   1.00 12.88 ?  51  GLY   B C    1 
ATOM   4531 O O    . GLY   B 1 51  ? 56.149 -23.130 0.831   1.00 13.74 ?  51  GLY   B O    1 
ATOM   4532 H H    . GLY   B 1 51  ? 52.585 -24.400 2.609   1.00 14.69 ?  51  GLY   B H    1 
ATOM   4533 H HA2  . GLY   B 1 51  ? 54.806 -23.079 2.916   1.00 15.84 ?  51  GLY   B HA2  1 
ATOM   4534 H HA3  . GLY   B 1 51  ? 54.707 -24.647 2.810   1.00 15.84 ?  51  GLY   B HA3  1 
ATOM   4535 N N    . ALA   B 1 52  ? 54.499 -24.426 0.030   1.00 12.46 ?  52  ALA   B N    1 
ATOM   4536 C CA   . ALA   B 1 52  ? 55.059 -24.430 -1.316  1.00 12.95 ?  52  ALA   B CA   1 
ATOM   4537 C C    . ALA   B 1 52  ? 54.982 -23.050 -1.960  1.00 12.29 ?  52  ALA   B C    1 
ATOM   4538 O O    . ALA   B 1 52  ? 55.955 -22.596 -2.584  1.00 12.94 ?  52  ALA   B O    1 
ATOM   4539 C CB   . ALA   B 1 52  ? 54.348 -25.468 -2.175  1.00 13.48 ?  52  ALA   B CB   1 
ATOM   4540 H H    . ALA   B 1 52  ? 53.764 -24.865 0.116   1.00 14.95 ?  52  ALA   B H    1 
ATOM   4541 H HA   . ALA   B 1 52  ? 55.993 -24.677 -1.259  1.00 15.54 ?  52  ALA   B HA   1 
ATOM   4542 H HB1  . ALA   B 1 52  ? 54.737 -25.458 -3.063  1.00 16.17 ?  52  ALA   B HB1  1 
ATOM   4543 H HB2  . ALA   B 1 52  ? 54.467 -26.343 -1.771  1.00 16.17 ?  52  ALA   B HB2  1 
ATOM   4544 H HB3  . ALA   B 1 52  ? 53.406 -25.249 -2.221  1.00 16.17 ?  52  ALA   B HB3  1 
ATOM   4545 N N    . LEU   B 1 53  ? 53.836 -22.375 -1.840  1.00 11.87 ?  53  LEU   B N    1 
ATOM   4546 C CA   . LEU   B 1 53  ? 53.721 -21.035 -2.410  1.00 12.27 ?  53  LEU   B CA   1 
ATOM   4547 C C    . LEU   B 1 53  ? 54.728 -20.096 -1.762  1.00 12.17 ?  53  LEU   B C    1 
ATOM   4548 O O    . LEU   B 1 53  ? 55.429 -19.341 -2.447  1.00 12.69 ?  53  LEU   B O    1 
ATOM   4549 C CB   . LEU   B 1 53  ? 52.297 -20.495 -2.246  1.00 12.40 ?  53  LEU   B CB   1 
ATOM   4550 C CG   . LEU   B 1 53  ? 51.164 -21.216 -2.986  1.00 12.55 ?  53  LEU   B CG   1 
ATOM   4551 C CD1  . LEU   B 1 53  ? 49.826 -20.606 -2.622  1.00 14.27 ?  53  LEU   B CD1  1 
ATOM   4552 C CD2  . LEU   B 1 53  ? 51.376 -21.206 -4.497  1.00 14.77 ?  53  LEU   B CD2  1 
ATOM   4553 H H    . LEU   B 1 53  ? 53.130 -22.661 -1.442  1.00 14.24 ?  53  LEU   B H    1 
ATOM   4554 H HA   . LEU   B 1 53  ? 53.921 -21.079 -3.361  1.00 14.72 ?  53  LEU   B HA   1 
ATOM   4555 H HB2  . LEU   B 1 53  ? 52.076 -20.523 -1.303  1.00 14.88 ?  53  LEU   B HB2  1 
ATOM   4556 H HB3  . LEU   B 1 53  ? 52.289 -19.577 -2.550  1.00 14.88 ?  53  LEU   B HB3  1 
ATOM   4557 H HG   . LEU   B 1 53  ? 51.148 -22.142 -2.698  1.00 15.06 ?  53  LEU   B HG   1 
ATOM   4558 H HD11 . LEU   B 1 53  ? 49.124 -21.079 -3.097  1.00 17.12 ?  53  LEU   B HD11 1 
ATOM   4559 H HD12 . LEU   B 1 53  ? 49.690 -20.695 -1.662  1.00 17.12 ?  53  LEU   B HD12 1 
ATOM   4560 H HD13 . LEU   B 1 53  ? 49.825 -19.671 -2.870  1.00 17.12 ?  53  LEU   B HD13 1 
ATOM   4561 H HD21 . LEU   B 1 53  ? 50.657 -21.700 -4.921  1.00 17.72 ?  53  LEU   B HD21 1 
ATOM   4562 H HD22 . LEU   B 1 53  ? 51.377 -20.290 -4.812  1.00 17.72 ?  53  LEU   B HD22 1 
ATOM   4563 H HD23 . LEU   B 1 53  ? 52.227 -21.628 -4.702  1.00 17.72 ?  53  LEU   B HD23 1 
ATOM   4564 N N    . ASN   B 1 54  ? 54.821 -20.128 -0.434  1.00 11.69 ?  54  ASN   B N    1 
ATOM   4565 C CA   . ASN   B 1 54  ? 55.733 -19.214 0.237   1.00 12.65 ?  54  ASN   B CA   1 
ATOM   4566 C C    . ASN   B 1 54  ? 57.177 -19.488 -0.160  1.00 12.66 ?  54  ASN   B C    1 
ATOM   4567 O O    . ASN   B 1 54  ? 57.950 -18.550 -0.397  1.00 13.02 ?  54  ASN   B O    1 
ATOM   4568 C CB   . ASN   B 1 54  ? 55.573 -19.294 1.747   1.00 13.34 ?  54  ASN   B CB   1 
ATOM   4569 C CG   . ASN   B 1 54  ? 56.551 -18.376 2.458   1.00 13.21 ?  54  ASN   B CG   1 
ATOM   4570 O OD1  . ASN   B 1 54  ? 56.569 -17.168 2.208   1.00 13.63 ?  54  ASN   B OD1  1 
ATOM   4571 N ND2  . ASN   B 1 54  ? 57.394 -18.943 3.311   1.00 14.68 ?  54  ASN   B ND2  1 
ATOM   4572 H H    . ASN   B 1 54  ? 54.380 -20.655 0.083   1.00 14.03 ?  54  ASN   B H    1 
ATOM   4573 H HA   . ASN   B 1 54  ? 55.519 -18.309 -0.038  1.00 15.18 ?  54  ASN   B HA   1 
ATOM   4574 H HB2  . ASN   B 1 54  ? 54.671 -19.021 1.988   1.00 16.01 ?  54  ASN   B HB2  1 
ATOM   4575 H HB3  . ASN   B 1 54  ? 55.740 -20.200 2.042   1.00 16.01 ?  54  ASN   B HB3  1 
ATOM   4576 H HD21 . ASN   B 1 54  ? 57.973 -18.458 3.728   1.00 17.62 ?  54  ASN   B HD21 1 
ATOM   4577 H HD22 . ASN   B 1 54  ? 57.363 -19.788 3.449   1.00 17.62 ?  54  ASN   B HD22 1 
ATOM   4578 N N    . LYS   B 1 55  ? 57.564 -20.765 -0.222  1.00 13.31 ?  55  LYS   B N    1 
ATOM   4579 C CA   . LYS   B 1 55  ? 58.919 -21.108 -0.645  1.00 14.32 ?  55  LYS   B CA   1 
ATOM   4580 C C    . LYS   B 1 55  ? 59.215 -20.565 -2.036  1.00 13.90 ?  55  LYS   B C    1 
ATOM   4581 O O    . LYS   B 1 55  ? 60.311 -20.053 -2.289  1.00 14.76 ?  55  LYS   B O    1 
ATOM   4582 C CB   . LYS   B 1 55  ? 59.106 -22.625 -0.604  1.00 15.77 ?  55  LYS   B CB   1 
ATOM   4583 C CG   . LYS   B 1 55  ? 60.491 -23.083 -1.017  1.00 19.45 ?  55  LYS   B CG   1 
ATOM   4584 C CD   . LYS   B 1 55  ? 60.679 -24.581 -0.818  1.00 22.92 ?  55  LYS   B CD   1 
ATOM   4585 C CE   . LYS   B 1 55  ? 60.698 -24.968 0.661   1.00 25.79 ?  55  LYS   B CE   1 
ATOM   4586 N NZ   . LYS   B 1 55  ? 61.065 -26.392 0.861   1.00 27.40 ?  55  LYS   B NZ   1 
ATOM   4587 H H    . LYS   B 1 55  ? 57.065 -21.439 -0.028  1.00 15.97 ?  55  LYS   B H    1 
ATOM   4588 H HA   . LYS   B 1 55  ? 59.553 -20.715 -0.027  1.00 17.18 ?  55  LYS   B HA   1 
ATOM   4589 H HB2  . LYS   B 1 55  ? 58.948 -22.932 0.303   1.00 18.92 ?  55  LYS   B HB2  1 
ATOM   4590 H HB3  . LYS   B 1 55  ? 58.468 -23.039 -1.205  1.00 18.92 ?  55  LYS   B HB3  1 
ATOM   4591 H HG2  . LYS   B 1 55  ? 60.628 -22.887 -1.957  1.00 23.34 ?  55  LYS   B HG2  1 
ATOM   4592 H HG3  . LYS   B 1 55  ? 61.155 -22.622 -0.480  1.00 23.34 ?  55  LYS   B HG3  1 
ATOM   4593 H HD2  . LYS   B 1 55  ? 59.947 -25.057 -1.242  1.00 27.50 ?  55  LYS   B HD2  1 
ATOM   4594 H HD3  . LYS   B 1 55  ? 61.525 -24.855 -1.208  1.00 27.50 ?  55  LYS   B HD3  1 
ATOM   4595 H HE2  . LYS   B 1 55  ? 61.348 -24.411 1.123   1.00 30.95 ?  55  LYS   B HE2  1 
ATOM   4596 H HE3  . LYS   B 1 55  ? 59.813 -24.822 1.037   1.00 30.95 ?  55  LYS   B HE3  1 
ATOM   4597 H HZ1  . LYS   B 1 55  ? 61.043 -26.590 1.728   1.00 32.88 ?  55  LYS   B HZ1  1 
ATOM   4598 H HZ2  . LYS   B 1 55  ? 60.488 -26.914 0.429   1.00 32.88 ?  55  LYS   B HZ2  1 
ATOM   4599 H HZ3  . LYS   B 1 55  ? 61.882 -26.540 0.548   1.00 32.88 ?  55  LYS   B HZ3  1 
ATOM   4600 N N    . ALA   B 1 56  ? 58.246 -20.652 -2.950  1.00 13.60 ?  56  ALA   B N    1 
ATOM   4601 C CA   . ALA   B 1 56  ? 58.465 -20.146 -4.301  1.00 14.37 ?  56  ALA   B CA   1 
ATOM   4602 C C    . ALA   B 1 56  ? 58.738 -18.648 -4.299  1.00 14.08 ?  56  ALA   B C    1 
ATOM   4603 O O    . ALA   B 1 56  ? 59.473 -18.150 -5.164  1.00 15.44 ?  56  ALA   B O    1 
ATOM   4604 C CB   . ALA   B 1 56  ? 57.265 -20.472 -5.188  1.00 15.29 ?  56  ALA   B CB   1 
ATOM   4605 H H    . ALA   B 1 56  ? 57.464 -20.984 -2.811  1.00 16.31 ?  56  ALA   B H    1 
ATOM   4606 H HA   . ALA   B 1 56  ? 59.242 -20.581 -4.674  1.00 17.24 ?  56  ALA   B HA   1 
ATOM   4607 H HB1  . ALA   B 1 56  ? 57.433 -20.129 -6.081  1.00 18.34 ?  56  ALA   B HB1  1 
ATOM   4608 H HB2  . ALA   B 1 56  ? 57.151 -21.434 -5.219  1.00 18.34 ?  56  ALA   B HB2  1 
ATOM   4609 H HB3  . ALA   B 1 56  ? 56.472 -20.054 -4.818  1.00 18.34 ?  56  ALA   B HB3  1 
ATOM   4610 N N    . THR   B 1 57  ? 58.170 -17.917 -3.337  1.00 13.70 ?  57  THR   B N    1 
ATOM   4611 C CA   . THR   B 1 57  ? 58.406 -16.482 -3.214  1.00 13.83 ?  57  THR   B CA   1 
ATOM   4612 C C    . THR   B 1 57  ? 59.656 -16.155 -2.403  1.00 14.72 ?  57  THR   B C    1 
ATOM   4613 O O    . THR   B 1 57  ? 59.894 -14.979 -2.099  1.00 15.13 ?  57  THR   B O    1 
ATOM   4614 C CB   . THR   B 1 57  ? 57.207 -15.754 -2.578  1.00 13.24 ?  57  THR   B CB   1 
ATOM   4615 O OG1  . THR   B 1 57  ? 57.189 -15.969 -1.161  1.00 13.68 ?  57  THR   B OG1  1 
ATOM   4616 C CG2  . THR   B 1 57  ? 55.883 -16.174 -3.209  1.00 13.32 ?  57  THR   B CG2  1 
ATOM   4617 H H    . THR   B 1 57  ? 57.631 -18.227 -2.739  1.00 16.44 ?  57  THR   B H    1 
ATOM   4618 H HA   . THR   B 1 57  ? 58.527 -16.112 -4.101  1.00 16.60 ?  57  THR   B HA   1 
ATOM   4619 H HB   . THR   B 1 57  ? 57.311 -14.802 -2.739  1.00 15.88 ?  57  THR   B HB   1 
ATOM   4620 H HG1  . THR   B 1 57  ? 57.125 -16.790 -0.995  1.00 16.42 ?  57  THR   B HG1  1 
ATOM   4621 H HG21 . THR   B 1 57  ? 55.161 -15.639 -2.852  1.00 15.98 ?  57  THR   B HG21 1 
ATOM   4622 H HG22 . THR   B 1 57  ? 55.923 -16.055 -4.171  1.00 15.98 ?  57  THR   B HG22 1 
ATOM   4623 H HG23 . THR   B 1 57  ? 55.708 -17.109 -3.017  1.00 15.98 ?  57  THR   B HG23 1 
ATOM   4624 N N    . ASN   B 1 58  ? 60.451 -17.158 -2.039  1.00 15.31 ?  58  ASN   B N    1 
ATOM   4625 C CA   . ASN   B 1 58  ? 61.652 -16.939 -1.236  1.00 18.36 ?  58  ASN   B CA   1 
ATOM   4626 C C    . ASN   B 1 58  ? 61.316 -16.225 0.073   1.00 16.12 ?  58  ASN   B C    1 
ATOM   4627 O O    . ASN   B 1 58  ? 62.052 -15.345 0.532   1.00 16.76 ?  58  ASN   B O    1 
ATOM   4628 C CB   . ASN   B 1 58  ? 62.736 -16.191 -2.018  1.00 26.04 ?  58  ASN   B CB   1 
ATOM   4629 C CG   . ASN   B 1 58  ? 64.105 -16.308 -1.374  1.00 35.20 ?  58  ASN   B CG   1 
ATOM   4630 O OD1  . ASN   B 1 58  ? 64.397 -17.284 -0.682  1.00 38.09 ?  58  ASN   B OD1  1 
ATOM   4631 N ND2  . ASN   B 1 58  ? 64.953 -15.309 -1.597  1.00 43.34 ?  58  ASN   B ND2  1 
ATOM   4632 H H    . ASN   B 1 58  ? 60.317 -17.986 -2.242  1.00 18.37 ?  58  ASN   B H    1 
ATOM   4633 H HA   . ASN   B 1 58  ? 62.021 -17.808 -1.006  1.00 22.03 ?  58  ASN   B HA   1 
ATOM   4634 H HB2  . ASN   B 1 58  ? 62.795 -16.560 -2.915  1.00 31.24 ?  58  ASN   B HB2  1 
ATOM   4635 H HB3  . ASN   B 1 58  ? 62.508 -15.251 -2.060  1.00 31.24 ?  58  ASN   B HB3  1 
ATOM   4636 H HD21 . ASN   B 1 58  ? 65.743 -15.328 -1.255  1.00 52.00 ?  58  ASN   B HD21 1 
ATOM   4637 H HD22 . ASN   B 1 58  ? 64.713 -14.643 -2.084  1.00 52.00 ?  58  ASN   B HD22 1 
ATOM   4638 N N    . ASN   B 1 59  ? 60.194 -16.614 0.682   1.00 14.85 ?  59  ASN   B N    1 
ATOM   4639 C CA   . ASN   B 1 59  ? 59.720 -16.139 1.983   1.00 14.60 ?  59  ASN   B CA   1 
ATOM   4640 C C    . ASN   B 1 59  ? 59.115 -14.737 1.929   1.00 14.25 ?  59  ASN   B C    1 
ATOM   4641 O O    . ASN   B 1 59  ? 58.678 -14.239 2.972   1.00 14.33 ?  59  ASN   B O    1 
ATOM   4642 C CB   . ASN   B 1 59  ? 60.793 -16.188 3.086   1.00 16.04 ?  59  ASN   B CB   1 
ATOM   4643 C CG   . ASN   B 1 59  ? 60.205 -16.379 4.466   1.00 17.12 ?  59  ASN   B CG   1 
ATOM   4644 O OD1  . ASN   B 1 59  ? 59.384 -17.270 4.683   1.00 17.46 ?  59  ASN   B OD1  1 
ATOM   4645 N ND2  . ASN   B 1 59  ? 60.619 -15.541 5.409   1.00 18.09 ?  59  ASN   B ND2  1 
ATOM   4646 H H    . ASN   B 1 59  ? 59.662 -17.202 0.341   1.00 17.81 ?  59  ASN   B H    1 
ATOM   4647 H HA   . ASN   B 1 59  ? 59.012 -16.737 2.270   1.00 17.52 ?  59  ASN   B HA   1 
ATOM   4648 H HB2  . ASN   B 1 59  ? 61.392 -16.930 2.921   1.00 19.25 ?  59  ASN   B HB2  1 
ATOM   4649 H HB3  . ASN   B 1 59  ? 61.283 -15.354 3.094   1.00 19.25 ?  59  ASN   B HB3  1 
ATOM   4650 H HD21 . ASN   B 1 59  ? 60.309 -15.608 6.211   1.00 21.70 ?  59  ASN   B HD21 1 
ATOM   4651 H HD22 . ASN   B 1 59  ? 61.190 -14.930 5.219   1.00 21.70 ?  59  ASN   B HD22 1 
ATOM   4652 N N    . ALA   B 1 60  ? 59.063 -14.086 0.762   1.00 14.34 ?  60  ALA   B N    1 
ATOM   4653 C CA   . ALA   B 1 60  ? 58.457 -12.758 0.684   1.00 13.97 ?  60  ALA   B CA   1 
ATOM   4654 C C    . ALA   B 1 60  ? 56.986 -12.787 1.081   1.00 13.05 ?  60  ALA   B C    1 
ATOM   4655 O O    . ALA   B 1 60  ? 56.478 -11.837 1.692   1.00 13.68 ?  60  ALA   B O    1 
ATOM   4656 C CB   . ALA   B 1 60  ? 58.618 -12.188 -0.725  1.00 15.03 ?  60  ALA   B CB   1 
ATOM   4657 H H    . ALA   B 1 60  ? 59.373 -14.388 0.021   1.00 17.21 ?  60  ALA   B H    1 
ATOM   4658 H HA   . ALA   B 1 60  ? 58.918 -12.169 1.298   1.00 16.76 ?  60  ALA   B HA   1 
ATOM   4659 H HB1  . ALA   B 1 60  ? 58.214 -11.311 -0.758  1.00 18.03 ?  60  ALA   B HB1  1 
ATOM   4660 H HB2  . ALA   B 1 60  ? 59.568 -12.124 -0.931  1.00 18.03 ?  60  ALA   B HB2  1 
ATOM   4661 H HB3  . ALA   B 1 60  ? 58.186 -12.782 -1.358  1.00 18.03 ?  60  ALA   B HB3  1 
ATOM   4662 N N    . MET   B 1 61  ? 56.281 -13.864 0.735   1.00 12.75 ?  61  MET   B N    1 
ATOM   4663 C CA   . MET   B 1 61  ? 54.886 -13.985 1.130   1.00 12.32 ?  61  MET   B CA   1 
ATOM   4664 C C    . MET   B 1 61  ? 54.750 -13.991 2.652   1.00 12.61 ?  61  MET   B C    1 
ATOM   4665 O O    . MET   B 1 61  ? 53.845 -13.351 3.205   1.00 12.17 ?  61  MET   B O    1 
ATOM   4666 C CB   . MET   B 1 61  ? 54.311 -15.257 0.502   1.00 12.48 ?  61  MET   B CB   1 
ATOM   4667 C CG   . MET   B 1 61  ? 52.871 -15.553 0.911   1.00 12.33 ?  61  MET   B CG   1 
ATOM   4668 S SD   . MET   B 1 61  ? 52.226 -17.056 0.152   1.00 12.90 ?  61  MET   B SD   1 
ATOM   4669 C CE   . MET   B 1 61  ? 51.969 -16.483 -1.525  1.00 14.32 ?  61  MET   B CE   1 
ATOM   4670 H H    . MET   B 1 61  ? 56.584 -14.527 0.274   1.00 15.30 ?  61  MET   B H    1 
ATOM   4671 H HA   . MET   B 1 61  ? 54.390 -13.234 0.769   1.00 14.78 ?  61  MET   B HA   1 
ATOM   4672 H HB2  . MET   B 1 61  ? 54.331 -15.169 -0.468  1.00 14.97 ?  61  MET   B HB2  1 
ATOM   4673 H HB3  . MET   B 1 61  ? 54.857 -16.015 0.768   1.00 14.97 ?  61  MET   B HB3  1 
ATOM   4674 H HG2  . MET   B 1 61  ? 52.832 -15.666 1.873   1.00 14.79 ?  61  MET   B HG2  1 
ATOM   4675 H HG3  . MET   B 1 61  ? 52.309 -14.811 0.640   1.00 14.79 ?  61  MET   B HG3  1 
ATOM   4676 H HE1  . MET   B 1 61  ? 51.592 -17.205 -2.050  1.00 17.18 ?  61  MET   B HE1  1 
ATOM   4677 H HE2  . MET   B 1 61  ? 51.362 -15.727 -1.514  1.00 17.18 ?  61  MET   B HE2  1 
ATOM   4678 H HE3  . MET   B 1 61  ? 52.824 -16.214 -1.901  1.00 17.18 ?  61  MET   B HE3  1 
ATOM   4679 N N    . GLN   B 1 62  ? 55.634 -14.712 3.348   1.00 12.60 ?  62  GLN   B N    1 
ATOM   4680 C CA   . GLN   B 1 62  ? 55.530 -14.774 4.802   1.00 12.64 ?  62  GLN   B CA   1 
ATOM   4681 C C    . GLN   B 1 62  ? 55.811 -13.420 5.439   1.00 13.17 ?  62  GLN   B C    1 
ATOM   4682 O O    . GLN   B 1 62  ? 55.127 -13.026 6.389   1.00 13.47 ?  62  GLN   B O    1 
ATOM   4683 C CB   . GLN   B 1 62  ? 56.482 -15.829 5.363   1.00 13.10 ?  62  GLN   B CB   1 
ATOM   4684 C CG   . GLN   B 1 62  ? 56.257 -16.093 6.843   1.00 13.52 ?  62  GLN   B CG   1 
ATOM   4685 C CD   . GLN   B 1 62  ? 54.882 -16.686 7.090   1.00 13.06 ?  62  GLN   B CD   1 
ATOM   4686 O OE1  . GLN   B 1 62  ? 54.624 -17.839 6.737   1.00 13.52 ?  62  GLN   B OE1  1 
ATOM   4687 N NE2  . GLN   B 1 62  ? 53.975 -15.893 7.651   1.00 13.71 ?  62  GLN   B NE2  1 
ATOM   4688 H H    . GLN   B 1 62  ? 56.279 -15.169 3.006   1.00 15.12 ?  62  GLN   B H    1 
ATOM   4689 H HA   . GLN   B 1 62  ? 54.624 -15.031 5.034   1.00 15.17 ?  62  GLN   B HA   1 
ATOM   4690 H HB2  . GLN   B 1 62  ? 56.355 -16.661 4.884   1.00 15.71 ?  62  GLN   B HB2  1 
ATOM   4691 H HB3  . GLN   B 1 62  ? 57.397 -15.518 5.248   1.00 15.71 ?  62  GLN   B HB3  1 
ATOM   4692 H HG2  . GLN   B 1 62  ? 56.925 -16.726 7.155   1.00 16.22 ?  62  GLN   B HG2  1 
ATOM   4693 H HG3  . GLN   B 1 62  ? 56.328 -15.262 7.335   1.00 16.22 ?  62  GLN   B HG3  1 
ATOM   4694 H HE21 . GLN   B 1 62  ? 54.186 -15.092 7.875   1.00 16.45 ?  62  GLN   B HE21 1 
ATOM   4695 H HE22 . GLN   B 1 62  ? 53.184 -16.192 7.801   1.00 16.45 ?  62  GLN   B HE22 1 
ATOM   4696 N N    . VAL   B 1 63  ? 56.824 -12.702 4.949   1.00 13.35 ?  63  VAL   B N    1 
ATOM   4697 C CA   . VAL   B 1 63  ? 57.130 -11.386 5.509   1.00 14.35 ?  63  VAL   B CA   1 
ATOM   4698 C C    . VAL   B 1 63  ? 55.936 -10.453 5.329   1.00 13.73 ?  63  VAL   B C    1 
ATOM   4699 O O    . VAL   B 1 63  ? 55.518 -9.750  6.262   1.00 14.69 ?  63  VAL   B O    1 
ATOM   4700 C CB   . VAL   B 1 63  ? 58.420 -10.824 4.884   1.00 15.83 ?  63  VAL   B CB   1 
ATOM   4701 C CG1  . VAL   B 1 63  ? 58.650 -9.385  5.332   1.00 16.53 ?  63  VAL   B CG1  1 
ATOM   4702 C CG2  . VAL   B 1 63  ? 59.602 -11.696 5.277   1.00 16.50 ?  63  VAL   B CG2  1 
ATOM   4703 H H    . VAL   B 1 63  ? 57.336 -12.946 4.302   1.00 16.01 ?  63  VAL   B H    1 
ATOM   4704 H HA   . VAL   B 1 63  ? 57.286 -11.483 6.457   1.00 17.22 ?  63  VAL   B HA   1 
ATOM   4705 H HB   . VAL   B 1 63  ? 58.347 -10.835 3.917   1.00 19.00 ?  63  VAL   B HB   1 
ATOM   4706 H HG11 . VAL   B 1 63  ? 59.565 -9.136  5.136   1.00 19.83 ?  63  VAL   B HG11 1 
ATOM   4707 H HG12 . VAL   B 1 63  ? 58.039 -8.804  4.854   1.00 19.83 ?  63  VAL   B HG12 1 
ATOM   4708 H HG13 . VAL   B 1 63  ? 58.489 -9.325  6.288   1.00 19.83 ?  63  VAL   B HG13 1 
ATOM   4709 H HG21 . VAL   B 1 63  ? 60.413 -11.319 4.898   1.00 19.80 ?  63  VAL   B HG21 1 
ATOM   4710 H HG22 . VAL   B 1 63  ? 59.672 -11.713 6.246   1.00 19.80 ?  63  VAL   B HG22 1 
ATOM   4711 H HG23 . VAL   B 1 63  ? 59.463 -12.592 4.939   1.00 19.80 ?  63  VAL   B HG23 1 
ATOM   4712 N N    . GLU   B 1 64  ? 55.369 -10.437 4.123   1.00 13.45 ?  64  GLU   B N    1 
ATOM   4713 C CA   . GLU   B 1 64  ? 54.200 -9.601  3.852   1.00 12.99 ?  64  GLU   B CA   1 
ATOM   4714 C C    . GLU   B 1 64  ? 53.017 -10.008 4.728   1.00 12.64 ?  64  GLU   B C    1 
ATOM   4715 O O    . GLU   B 1 64  ? 52.267 -9.150  5.226   1.00 13.03 ?  64  GLU   B O    1 
ATOM   4716 C CB   . GLU   B 1 64  ? 53.836 -9.736  2.372   1.00 13.14 ?  64  GLU   B CB   1 
ATOM   4717 C CG   . GLU   B 1 64  ? 52.573 -9.011  1.943   1.00 13.30 ?  64  GLU   B CG   1 
ATOM   4718 C CD   . GLU   B 1 64  ? 52.031 -9.514  0.608   1.00 13.86 ?  64  GLU   B CD   1 
ATOM   4719 O OE1  . GLU   B 1 64  ? 52.203 -10.724 0.292   1.00 14.66 ?  64  GLU   B OE1  1 
ATOM   4720 O OE2  . GLU   B 1 64  ? 51.412 -8.694  -0.117  1.00 14.90 -1 64  GLU   B OE2  1 
ATOM   4721 H H    . GLU   B 1 64  ? 55.640 -10.897 3.444   1.00 16.14 ?  64  GLU   B H    1 
ATOM   4722 H HA   . GLU   B 1 64  ? 54.415 -8.673  4.034   1.00 15.59 ?  64  GLU   B HA   1 
ATOM   4723 H HB2  . GLU   B 1 64  ? 54.567 -9.373  1.841   1.00 15.76 ?  64  GLU   B HB2  1 
ATOM   4724 H HB3  . GLU   B 1 64  ? 53.722 -10.672 2.167   1.00 15.76 ?  64  GLU   B HB3  1 
ATOM   4725 H HG2  . GLU   B 1 64  ? 51.877 -9.142  2.609   1.00 15.96 ?  64  GLU   B HG2  1 
ATOM   4726 H HG3  . GLU   B 1 64  ? 52.765 -8.065  1.852   1.00 15.96 ?  64  GLU   B HG3  1 
ATOM   4727 N N    . SER   B 1 65  ? 52.838 -11.316 4.920   1.00 12.66 ?  65  SER   B N    1 
ATOM   4728 C CA   . SER   B 1 65  ? 51.726 -11.822 5.715   1.00 12.77 ?  65  SER   B CA   1 
ATOM   4729 C C    . SER   B 1 65  ? 51.857 -11.421 7.178   1.00 12.55 ?  65  SER   B C    1 
ATOM   4730 O O    . SER   B 1 65  ? 50.859 -11.053 7.815   1.00 13.10 ?  65  SER   B O    1 
ATOM   4731 C CB   . SER   B 1 65  ? 51.640 -13.344 5.580   1.00 12.91 ?  65  SER   B CB   1 
ATOM   4732 O OG   . SER   B 1 65  ? 51.304 -13.731 4.255   1.00 12.76 ?  65  SER   B OG   1 
ATOM   4733 H H    . SER   B 1 65  ? 53.353 -11.933 4.608   1.00 15.19 ?  65  SER   B H    1 
ATOM   4734 H HA   . SER   B 1 65  ? 50.897 -11.445 5.377   1.00 15.32 ?  65  SER   B HA   1 
ATOM   4735 H HB2  . SER   B 1 65  ? 52.497 -13.731 5.806   1.00 15.49 ?  65  SER   B HB2  1 
ATOM   4736 H HB3  . SER   B 1 65  ? 50.956 -13.677 6.182   1.00 15.49 ?  65  SER   B HB3  1 
ATOM   4737 H HG   . SER   B 1 65  ? 51.884 -13.438 3.712   1.00 15.31 ?  65  SER   B HG   1 
ATOM   4738 N N    . ASP   B 1 66  ? 53.065 -11.528 7.744   1.00 12.96 ?  66  ASP   B N    1 
ATOM   4739 C CA   . ASP   B 1 66  ? 53.260 -11.137 9.138   1.00 13.38 ?  66  ASP   B CA   1 
ATOM   4740 C C    . ASP   B 1 66  ? 52.945 -9.659  9.342   1.00 13.43 ?  66  ASP   B C    1 
ATOM   4741 O O    . ASP   B 1 66  ? 52.373 -9.272  10.367  1.00 14.16 ?  66  ASP   B O    1 
ATOM   4742 C CB   . ASP   B 1 66  ? 54.694 -11.442 9.582   1.00 14.77 ?  66  ASP   B CB   1 
ATOM   4743 C CG   . ASP   B 1 66  ? 54.961 -12.933 9.744   1.00 16.57 ?  66  ASP   B CG   1 
ATOM   4744 O OD1  . ASP   B 1 66  ? 54.008 -13.743 9.666   1.00 17.40 ?  66  ASP   B OD1  1 
ATOM   4745 O OD2  . ASP   B 1 66  ? 56.138 -13.295 9.959   1.00 19.14 -1 66  ASP   B OD2  1 
ATOM   4746 H H    . ASP   B 1 66  ? 53.764 -11.830 7.353   1.00 15.56 ?  66  ASP   B H    1 
ATOM   4747 H HA   . ASP   B 1 66  ? 52.662 -11.645 9.705   1.00 16.05 ?  66  ASP   B HA   1 
ATOM   4748 H HB2  . ASP   B 1 66  ? 55.311 -11.102 8.914   1.00 17.72 ?  66  ASP   B HB2  1 
ATOM   4749 H HB3  . ASP   B 1 66  ? 54.862 -11.008 10.436  1.00 17.72 ?  66  ASP   B HB3  1 
ATOM   4750 N N    . ASP   B 1 67  ? 53.318 -8.815  8.381   1.00 13.13 ?  67  ASP   B N    1 
ATOM   4751 C CA   . ASP   B 1 67  ? 52.971 -7.403  8.478   1.00 13.71 ?  67  ASP   B CA   1 
ATOM   4752 C C    . ASP   B 1 67  ? 51.459 -7.197  8.391   1.00 13.73 ?  67  ASP   B C    1 
ATOM   4753 O O    . ASP   B 1 67  ? 50.890 -6.395  9.143   1.00 14.42 ?  67  ASP   B O    1 
ATOM   4754 C CB   . ASP   B 1 67  ? 53.696 -6.626  7.387   1.00 15.09 ?  67  ASP   B CB   1 
ATOM   4755 C CG   . ASP   B 1 67  ? 53.271 -5.188  7.344   1.00 16.63 ?  67  ASP   B CG   1 
ATOM   4756 O OD1  . ASP   B 1 67  ? 53.775 -4.382  8.161   1.00 18.06 ?  67  ASP   B OD1  1 
ATOM   4757 O OD2  . ASP   B 1 67  ? 52.401 -4.881  6.510   1.00 17.80 -1 67  ASP   B OD2  1 
ATOM   4758 H H    . ASP   B 1 67  ? 53.772 -9.029  7.684   1.00 15.76 ?  67  ASP   B H    1 
ATOM   4759 H HA   . ASP   B 1 67  ? 53.271 -7.060  9.334   1.00 16.45 ?  67  ASP   B HA   1 
ATOM   4760 H HB2  . ASP   B 1 67  ? 54.654 -6.651  7.554   1.00 18.10 ?  67  ASP   B HB2  1 
ATOM   4761 H HB3  . ASP   B 1 67  ? 53.504 -7.027  6.523   1.00 18.10 ?  67  ASP   B HB3  1 
ATOM   4762 N N    . TYR   B 1 68  ? 50.785 -7.928  7.496   1.00 13.57 ?  68  TYR   B N    1 
ATOM   4763 C CA   . TYR   B 1 68  ? 49.326 -7.851  7.421   1.00 14.28 ?  68  TYR   B CA   1 
ATOM   4764 C C    . TYR   B 1 68  ? 48.689 -8.194  8.765   1.00 13.63 ?  68  TYR   B C    1 
ATOM   4765 O O    . TYR   B 1 68  ? 47.752 -7.520  9.214   1.00 14.53 ?  68  TYR   B O    1 
ATOM   4766 C CB   . TYR   B 1 68  ? 48.792 -8.782  6.323   1.00 15.03 ?  68  TYR   B CB   1 
ATOM   4767 C CG   . TYR   B 1 68  ? 47.284 -8.933  6.383   1.00 16.02 ?  68  TYR   B CG   1 
ATOM   4768 C CD1  . TYR   B 1 68  ? 46.694 -9.885  7.209   1.00 16.76 ?  68  TYR   B CD1  1 
ATOM   4769 C CD2  . TYR   B 1 68  ? 46.454 -8.098  5.657   1.00 17.12 ?  68  TYR   B CD2  1 
ATOM   4770 C CE1  . TYR   B 1 68  ? 45.328 -10.006 7.300   1.00 17.92 ?  68  TYR   B CE1  1 
ATOM   4771 C CE2  . TYR   B 1 68  ? 45.073 -8.226  5.732   1.00 17.97 ?  68  TYR   B CE2  1 
ATOM   4772 C CZ   . TYR   B 1 68  ? 44.529 -9.176  6.558   1.00 18.03 ?  68  TYR   B CZ   1 
ATOM   4773 O OH   . TYR   B 1 68  ? 43.161 -9.292  6.650   1.00 19.17 ?  68  TYR   B OH   1 
ATOM   4774 H H    . TYR   B 1 68  ? 51.147 -8.473  6.929   1.00 16.29 ?  68  TYR   B H    1 
ATOM   4775 H HA   . TYR   B 1 68  ? 49.076 -6.947  7.195   1.00 17.13 ?  68  TYR   B HA   1 
ATOM   4776 H HB2  . TYR   B 1 68  ? 49.020 -8.413  5.458   1.00 18.03 ?  68  TYR   B HB2  1 
ATOM   4777 H HB3  . TYR   B 1 68  ? 49.186 -9.660  6.430   1.00 18.03 ?  68  TYR   B HB3  1 
ATOM   4778 H HD1  . TYR   B 1 68  ? 47.231 -10.453 7.715   1.00 20.10 ?  68  TYR   B HD1  1 
ATOM   4779 H HD2  . TYR   B 1 68  ? 46.824 -7.447  5.112   1.00 20.54 ?  68  TYR   B HD2  1 
ATOM   4780 H HE1  . TYR   B 1 68  ? 44.945 -10.661 7.848   1.00 21.50 ?  68  TYR   B HE1  1 
ATOM   4781 H HE2  . TYR   B 1 68  ? 44.519 -7.660  5.246   1.00 21.56 ?  68  TYR   B HE2  1 
ATOM   4782 H HH   . TYR   B 1 68  ? 42.775 -8.737  6.143   1.00 23.00 ?  68  TYR   B HH   1 
ATOM   4783 N N    . ILE   B 1 69  ? 49.169 -9.266  9.407   1.00 13.68 ?  69  ILE   B N    1 
ATOM   4784 C CA   . ILE   B 1 69  ? 48.617 -9.696  10.690  1.00 14.05 ?  69  ILE   B CA   1 
ATOM   4785 C C    . ILE   B 1 69  ? 48.872 -8.652  11.769  1.00 13.90 ?  69  ILE   B C    1 
ATOM   4786 O O    . ILE   B 1 69  ? 48.002 -8.376  12.601  1.00 14.07 ?  69  ILE   B O    1 
ATOM   4787 C CB   . ILE   B 1 69  ? 49.190 -11.073 11.081  1.00 14.87 ?  69  ILE   B CB   1 
ATOM   4788 C CG1  . ILE   B 1 69  ? 48.664 -12.175 10.148  1.00 15.45 ?  69  ILE   B CG1  1 
ATOM   4789 C CG2  . ILE   B 1 69  ? 48.900 -11.384 12.543  1.00 16.10 ?  69  ILE   B CG2  1 
ATOM   4790 C CD1  . ILE   B 1 69  ? 47.193 -12.510 10.318  1.00 15.85 ?  69  ILE   B CD1  1 
ATOM   4791 H H    . ILE   B 1 69  ? 49.816 -9.756  9.124   1.00 16.41 ?  69  ILE   B H    1 
ATOM   4792 H HA   . ILE   B 1 69  ? 47.659 -9.791  10.596  1.00 16.86 ?  69  ILE   B HA   1 
ATOM   4793 H HB   . ILE   B 1 69  ? 50.153 -11.031 10.976  1.00 17.84 ?  69  ILE   B HB   1 
ATOM   4794 H HG12 . ILE   B 1 69  ? 48.799 -11.889 9.230   1.00 18.54 ?  69  ILE   B HG12 1 
ATOM   4795 H HG13 . ILE   B 1 69  ? 49.175 -12.984 10.313  1.00 18.54 ?  69  ILE   B HG13 1 
ATOM   4796 H HG21 . ILE   B 1 69  ? 49.032 -12.334 12.692  1.00 19.32 ?  69  ILE   B HG21 1 
ATOM   4797 H HG22 . ILE   B 1 69  ? 49.509 -10.879 13.105  1.00 19.32 ?  69  ILE   B HG22 1 
ATOM   4798 H HG23 . ILE   B 1 69  ? 47.983 -11.144 12.743  1.00 19.32 ?  69  ILE   B HG23 1 
ATOM   4799 H HD11 . ILE   B 1 69  ? 46.959 -13.202 9.680   1.00 19.02 ?  69  ILE   B HD11 1 
ATOM   4800 H HD12 . ILE   B 1 69  ? 47.046 -12.831 11.221  1.00 19.02 ?  69  ILE   B HD12 1 
ATOM   4801 H HD13 . ILE   B 1 69  ? 46.667 -11.716 10.155  1.00 19.02 ?  69  ILE   B HD13 1 
ATOM   4802 N N    . ALA   B 1 70  ? 50.067 -8.065  11.793  1.00 13.83 ?  70  ALA   B N    1 
ATOM   4803 C CA   . ALA   B 1 70  ? 50.347 -7.027  12.781  1.00 13.85 ?  70  ALA   B CA   1 
ATOM   4804 C C    . ALA   B 1 70  ? 49.344 -5.885  12.677  1.00 14.32 ?  70  ALA   B C    1 
ATOM   4805 O O    . ALA   B 1 70  ? 48.896 -5.346  13.695  1.00 14.48 ?  70  ALA   B O    1 
ATOM   4806 C CB   . ALA   B 1 70  ? 51.772 -6.508  12.599  1.00 14.40 ?  70  ALA   B CB   1 
ATOM   4807 H H    . ALA   B 1 70  ? 50.714 -8.245  11.263  1.00 16.59 ?  70  ALA   B H    1 
ATOM   4808 H HA   . ALA   B 1 70  ? 50.282 -7.406  13.672  1.00 16.62 ?  70  ALA   B HA   1 
ATOM   4809 H HB1  . ALA   B 1 70  ? 51.966 -5.854  13.290  1.00 17.28 ?  70  ALA   B HB1  1 
ATOM   4810 H HB2  . ALA   B 1 70  ? 52.395 -7.252  12.671  1.00 17.28 ?  70  ALA   B HB2  1 
ATOM   4811 H HB3  . ALA   B 1 70  ? 51.855 -6.098  11.723  1.00 17.28 ?  70  ALA   B HB3  1 
ATOM   4812 N N    . THR   B 1 71  ? 48.965 -5.518  11.457  1.00 14.62 ?  71  THR   B N    1 
ATOM   4813 C CA   . THR   B 1 71  ? 48.077 -4.380  11.252  1.00 15.65 ?  71  THR   B CA   1 
ATOM   4814 C C    . THR   B 1 71  ? 46.610 -4.746  11.457  1.00 16.02 ?  71  THR   B C    1 
ATOM   4815 O O    . THR   B 1 71  ? 45.831 -3.930  11.970  1.00 17.46 ?  71  THR   B O    1 
ATOM   4816 C CB   . THR   B 1 71  ? 48.291 -3.817  9.845   1.00 17.28 ?  71  THR   B CB   1 
ATOM   4817 O OG1  . THR   B 1 71  ? 49.615 -3.282  9.743   1.00 19.43 ?  71  THR   B OG1  1 
ATOM   4818 C CG2  . THR   B 1 71  ? 47.270 -2.735  9.518   1.00 18.20 ?  71  THR   B CG2  1 
ATOM   4819 H H    . THR   B 1 71  ? 49.209 -5.912  10.734  1.00 17.54 ?  71  THR   B H    1 
ATOM   4820 H HA   . THR   B 1 71  ? 48.303 -3.683  11.889  1.00 18.77 ?  71  THR   B HA   1 
ATOM   4821 H HB   . THR   B 1 71  ? 48.200 -4.527  9.195   1.00 20.73 ?  71  THR   B HB   1 
ATOM   4822 H HG1  . THR   B 1 71  ? 49.742 -2.951  8.977   1.00 23.31 ?  71  THR   B HG1  1 
ATOM   4823 H HG21 . THR   B 1 71  ? 47.575 -2.208  8.761   1.00 21.84 ?  71  THR   B HG21 1 
ATOM   4824 H HG22 . THR   B 1 71  ? 46.418 -3.137  9.296   1.00 21.84 ?  71  THR   B HG22 1 
ATOM   4825 H HG23 . THR   B 1 71  ? 47.155 -2.145  10.281  1.00 21.84 ?  71  THR   B HG23 1 
ATOM   4826 N N    . ASN   B 1 72  ? 46.215 -5.961  11.065  1.00 15.60 ?  72  ASN   B N    1 
ATOM   4827 C CA   . ASN   B 1 72  ? 44.812 -6.318  10.932  1.00 16.02 ?  72  ASN   B CA   1 
ATOM   4828 C C    . ASN   B 1 72  ? 44.340 -7.417  11.872  1.00 16.56 ?  72  ASN   B C    1 
ATOM   4829 O O    . ASN   B 1 72  ? 43.126 -7.576  12.039  1.00 17.79 ?  72  ASN   B O    1 
ATOM   4830 C CB   . ASN   B 1 72  ? 44.514 -6.745  9.487   1.00 16.81 ?  72  ASN   B CB   1 
ATOM   4831 C CG   . ASN   B 1 72  ? 44.780 -5.638  8.495   1.00 17.93 ?  72  ASN   B CG   1 
ATOM   4832 O OD1  . ASN   B 1 72  ? 45.789 -5.645  7.785   1.00 18.91 ?  72  ASN   B OD1  1 
ATOM   4833 N ND2  . ASN   B 1 72  ? 43.894 -4.661  8.460   1.00 19.40 ?  72  ASN   B ND2  1 
ATOM   4834 H H    . ASN   B 1 72  ? 46.760 -6.604  10.866  1.00 18.71 ?  72  ASN   B H    1 
ATOM   4835 H HA   . ASN   B 1 72  ? 44.283 -5.530  11.114  1.00 19.22 ?  72  ASN   B HA   1 
ATOM   4836 H HB2  . ASN   B 1 72  ? 45.083 -7.499  9.254   1.00 20.17 ?  72  ASN   B HB2  1 
ATOM   4837 H HB3  . ASN   B 1 72  ? 43.584 -6.994  9.415   1.00 20.17 ?  72  ASN   B HB3  1 
ATOM   4838 H HD21 . ASN   B 1 72  ? 43.997 -4.004  7.914   1.00 23.28 ?  72  ASN   B HD21 1 
ATOM   4839 H HD22 . ASN   B 1 72  ? 43.204 -4.689  8.972   1.00 23.28 ?  72  ASN   B HD22 1 
ATOM   4840 N N    . GLY   B 1 73  ? 45.243 -8.169  12.491  1.00 15.99 ?  73  GLY   B N    1 
ATOM   4841 C CA   . GLY   B 1 73  ? 44.848 -9.306  13.285  1.00 15.22 ?  73  GLY   B CA   1 
ATOM   4842 C C    . GLY   B 1 73  ? 44.484 -10.488 12.413  1.00 14.04 ?  73  GLY   B C    1 
ATOM   4843 O O    . GLY   B 1 73  ? 44.472 -10.401 11.182  1.00 14.24 ?  73  GLY   B O    1 
ATOM   4844 H H    . GLY   B 1 73  ? 46.095 -8.031  12.467  1.00 19.19 ?  73  GLY   B H    1 
ATOM   4845 H HA2  . GLY   B 1 73  ? 45.579 -9.560  13.873  1.00 18.27 ?  73  GLY   B HA2  1 
ATOM   4846 H HA3  . GLY   B 1 73  ? 44.082 -9.069  13.834  1.00 18.27 ?  73  GLY   B HA3  1 
ATOM   4847 N N    . PRO   B 1 74  ? 44.171 -11.614 13.044  1.00 14.62 ?  74  PRO   B N    1 
ATOM   4848 C CA   . PRO   B 1 74  ? 43.936 -12.844 12.289  1.00 14.27 ?  74  PRO   B CA   1 
ATOM   4849 C C    . PRO   B 1 74  ? 42.633 -12.792 11.503  1.00 13.38 ?  74  PRO   B C    1 
ATOM   4850 O O    . PRO   B 1 74  ? 41.694 -12.053 11.818  1.00 14.77 ?  74  PRO   B O    1 
ATOM   4851 C CB   . PRO   B 1 74  ? 43.876 -13.916 13.384  1.00 15.55 ?  74  PRO   B CB   1 
ATOM   4852 C CG   . PRO   B 1 74  ? 43.419 -13.185 14.597  1.00 17.18 ?  74  PRO   B CG   1 
ATOM   4853 C CD   . PRO   B 1 74  ? 44.056 -11.826 14.497  1.00 16.58 ?  74  PRO   B CD   1 
ATOM   4854 H HA   . PRO   B 1 74  ? 44.683 -13.020 11.689  1.00 17.12 ?  74  PRO   B HA   1 
ATOM   4855 H HB2  . PRO   B 1 74  ? 43.241 -14.601 13.128  1.00 18.66 ?  74  PRO   B HB2  1 
ATOM   4856 H HB3  . PRO   B 1 74  ? 44.760 -14.294 13.517  1.00 18.66 ?  74  PRO   B HB3  1 
ATOM   4857 H HG2  . PRO   B 1 74  ? 42.452 -13.114 14.586  1.00 20.62 ?  74  PRO   B HG2  1 
ATOM   4858 H HG3  . PRO   B 1 74  ? 43.723 -13.652 15.389  1.00 20.62 ?  74  PRO   B HG3  1 
ATOM   4859 H HD2  . PRO   B 1 74  ? 43.479 -11.153 14.898  1.00 19.89 ?  74  PRO   B HD2  1 
ATOM   4860 H HD3  . PRO   B 1 74  ? 44.934 -11.831 14.910  1.00 19.89 ?  74  PRO   B HD3  1 
ATOM   4861 N N    . LEU   B 1 75  ? 42.598 -13.610 10.456  1.00 12.85 ?  75  LEU   B N    1 
ATOM   4862 C CA   . LEU   B 1 75  ? 41.386 -13.826 9.685   1.00 12.90 ?  75  LEU   B CA   1 
ATOM   4863 C C    . LEU   B 1 75  ? 40.411 -14.692 10.481  1.00 13.46 ?  75  LEU   B C    1 
ATOM   4864 O O    . LEU   B 1 75  ? 40.748 -15.250 11.525  1.00 14.45 ?  75  LEU   B O    1 
ATOM   4865 C CB   . LEU   B 1 75  ? 41.714 -14.532 8.370   1.00 12.55 ?  75  LEU   B CB   1 
ATOM   4866 C CG   . LEU   B 1 75  ? 42.552 -13.776 7.333   1.00 14.36 ?  75  LEU   B CG   1 
ATOM   4867 C CD1  . LEU   B 1 75  ? 42.715 -14.602 6.061   1.00 16.15 ?  75  LEU   B CD1  1 
ATOM   4868 C CD2  . LEU   B 1 75  ? 41.963 -12.432 7.007   1.00 17.65 ?  75  LEU   B CD2  1 
ATOM   4869 H H    . LEU   B 1 75  ? 43.272 -14.063 10.169  1.00 15.42 ?  75  LEU   B H    1 
ATOM   4870 H HA   . LEU   B 1 75  ? 40.962 -12.978 9.491   1.00 15.47 ?  75  LEU   B HA   1 
ATOM   4871 H HB2  . LEU   B 1 75  ? 42.197 -15.348 8.576   1.00 15.06 ?  75  LEU   B HB2  1 
ATOM   4872 H HB3  . LEU   B 1 75  ? 40.877 -14.764 7.934   1.00 15.06 ?  75  LEU   B HB3  1 
ATOM   4873 H HG   . LEU   B 1 75  ? 43.438 -13.628 7.697   1.00 17.23 ?  75  LEU   B HG   1 
ATOM   4874 H HD11 . LEU   B 1 75  ? 43.254 -14.101 5.423   1.00 19.38 ?  75  LEU   B HD11 1 
ATOM   4875 H HD12 . LEU   B 1 75  ? 43.158 -15.437 6.278   1.00 19.38 ?  75  LEU   B HD12 1 
ATOM   4876 H HD13 . LEU   B 1 75  ? 41.841 -14.779 5.681   1.00 19.38 ?  75  LEU   B HD13 1 
ATOM   4877 H HD21 . LEU   B 1 75  ? 42.466 -12.034 6.280   1.00 21.18 ?  75  LEU   B HD21 1 
ATOM   4878 H HD22 . LEU   B 1 75  ? 41.038 -12.550 6.747   1.00 21.18 ?  75  LEU   B HD22 1 
ATOM   4879 H HD23 . LEU   B 1 75  ? 42.017 -11.867 7.794   1.00 21.18 ?  75  LEU   B HD23 1 
ATOM   4880 N N    . LYS   B 1 76  ? 39.183 -14.794 9.972   1.00 14.55 ?  76  LYS   B N    1 
ATOM   4881 C CA   . LYS   B 1 76  ? 38.196 -15.755 10.449  1.00 15.91 ?  76  LYS   B CA   1 
ATOM   4882 C C    . LYS   B 1 76  ? 38.286 -17.025 9.606   1.00 14.35 ?  76  LYS   B C    1 
ATOM   4883 O O    . LYS   B 1 76  ? 38.547 -16.963 8.404   1.00 14.06 ?  76  LYS   B O    1 
ATOM   4884 C CB   . LYS   B 1 76  ? 36.775 -15.188 10.278  1.00 18.34 ?  76  LYS   B CB   1 
ATOM   4885 C CG   . LYS   B 1 76  ? 36.507 -13.789 10.869  1.00 20.41 ?  76  LYS   B CG   1 
ATOM   4886 C CD   . LYS   B 1 76  ? 35.100 -13.260 10.510  1.00 21.70 ?  76  LYS   B CD   1 
ATOM   4887 C CE   . LYS   B 1 76  ? 34.837 -11.887 11.120  1.00 23.44 ?  76  LYS   B CE   1 
ATOM   4888 N NZ   . LYS   B 1 76  ? 33.533 -11.303 10.690  1.00 24.30 ?  76  LYS   B NZ   1 
ATOM   4889 H H    . LYS   B 1 76  ? 38.896 -14.308 9.330   1.00 17.46 ?  76  LYS   B H    1 
ATOM   4890 H HA   . LYS   B 1 76  ? 38.348 -15.975 11.384  1.00 19.09 ?  76  LYS   B HA   1 
ATOM   4891 H HB2  . LYS   B 1 76  ? 36.582 -15.139 9.328   1.00 22.01 ?  76  LYS   B HB2  1 
ATOM   4892 H HB3  . LYS   B 1 76  ? 36.150 -15.799 10.699  1.00 22.01 ?  76  LYS   B HB3  1 
ATOM   4893 H HG2  . LYS   B 1 76  ? 36.577 -13.834 11.835  1.00 24.49 ?  76  LYS   B HG2  1 
ATOM   4894 H HG3  . LYS   B 1 76  ? 37.164 -13.166 10.516  1.00 24.49 ?  76  LYS   B HG3  1 
ATOM   4895 H HD2  . LYS   B 1 76  ? 35.023 -13.181 9.545   1.00 26.04 ?  76  LYS   B HD2  1 
ATOM   4896 H HD3  . LYS   B 1 76  ? 34.431 -13.874 10.849  1.00 26.04 ?  76  LYS   B HD3  1 
ATOM   4897 H HE2  . LYS   B 1 76  ? 34.826 -11.968 12.086  1.00 28.12 ?  76  LYS   B HE2  1 
ATOM   4898 H HE3  . LYS   B 1 76  ? 35.542 -11.280 10.845  1.00 28.12 ?  76  LYS   B HE3  1 
ATOM   4899 H HZ1  . LYS   B 1 76  ? 33.416 -10.503 11.067  1.00 29.16 ?  76  LYS   B HZ1  1 
ATOM   4900 H HZ2  . LYS   B 1 76  ? 33.515 -11.208 9.805   1.00 29.16 ?  76  LYS   B HZ2  1 
ATOM   4901 H HZ3  . LYS   B 1 76  ? 32.862 -11.835 10.936  1.00 29.16 ?  76  LYS   B HZ3  1 
ATOM   4902 N N    . VAL   B 1 77  ? 38.040 -18.182 10.231  1.00 15.05 ?  77  VAL   B N    1 
ATOM   4903 C CA   . VAL   B 1 77  ? 37.829 -19.391 9.441   1.00 14.97 ?  77  VAL   B CA   1 
ATOM   4904 C C    . VAL   B 1 77  ? 36.636 -19.150 8.528   1.00 14.22 ?  77  VAL   B C    1 
ATOM   4905 O O    . VAL   B 1 77  ? 35.571 -18.704 8.976   1.00 14.01 ?  77  VAL   B O    1 
ATOM   4906 C CB   . VAL   B 1 77  ? 37.629 -20.618 10.345  1.00 16.27 ?  77  VAL   B CB   1 
ATOM   4907 C CG1  . VAL   B 1 77  ? 37.363 -21.856 9.492   1.00 16.81 ?  77  VAL   B CG1  1 
ATOM   4908 C CG2  . VAL   B 1 77  ? 38.853 -20.837 11.236  1.00 18.02 ?  77  VAL   B CG2  1 
ATOM   4909 H H    . VAL   B 1 77  ? 37.995 -18.289 11.081  1.00 18.05 ?  77  VAL   B H    1 
ATOM   4910 H HA   . VAL   B 1 77  ? 38.599 -19.547 8.883   1.00 17.96 ?  77  VAL   B HA   1 
ATOM   4911 H HB   . VAL   B 1 77  ? 36.854 -20.471 10.916  1.00 19.52 ?  77  VAL   B HB   1 
ATOM   4912 H HG11 . VAL   B 1 77  ? 37.407 -22.642 10.059  1.00 20.17 ?  77  VAL   B HG11 1 
ATOM   4913 H HG12 . VAL   B 1 77  ? 36.479 -21.788 9.093   1.00 20.17 ?  77  VAL   B HG12 1 
ATOM   4914 H HG13 . VAL   B 1 77  ? 38.037 -21.911 8.798   1.00 20.17 ?  77  VAL   B HG13 1 
ATOM   4915 H HG21 . VAL   B 1 77  ? 38.718 -21.642 11.757  1.00 21.63 ?  77  VAL   B HG21 1 
ATOM   4916 H HG22 . VAL   B 1 77  ? 39.634 -20.928 10.672  1.00 21.63 ?  77  VAL   B HG22 1 
ATOM   4917 H HG23 . VAL   B 1 77  ? 38.953 -20.072 11.824  1.00 21.63 ?  77  VAL   B HG23 1 
ATOM   4918 N N    . GLY   B 1 78  ? 36.814 -19.420 7.237   1.00 13.72 ?  78  GLY   B N    1 
ATOM   4919 C CA   . GLY   B 1 78  ? 35.834 -19.091 6.227   1.00 13.18 ?  78  GLY   B CA   1 
ATOM   4920 C C    . GLY   B 1 78  ? 36.083 -17.777 5.526   1.00 12.54 ?  78  GLY   B C    1 
ATOM   4921 O O    . GLY   B 1 78  ? 35.408 -17.493 4.533   1.00 13.00 ?  78  GLY   B O    1 
ATOM   4922 H H    . GLY   B 1 78  ? 37.512 -19.807 6.921   1.00 16.47 ?  78  GLY   B H    1 
ATOM   4923 H HA2  . GLY   B 1 78  ? 35.818 -19.786 5.554   1.00 15.81 ?  78  GLY   B HA2  1 
ATOM   4924 H HA3  . GLY   B 1 78  ? 34.954 -19.044 6.634   1.00 15.81 ?  78  GLY   B HA3  1 
ATOM   4925 N N    . GLY   B 1 79  ? 37.032 -16.972 6.015   1.00 12.56 ?  79  GLY   B N    1 
ATOM   4926 C CA   . GLY   B 1 79  ? 37.337 -15.679 5.440   1.00 12.20 ?  79  GLY   B CA   1 
ATOM   4927 C C    . GLY   B 1 79  ? 38.570 -15.705 4.544   1.00 12.06 ?  79  GLY   B C    1 
ATOM   4928 O O    . GLY   B 1 79  ? 39.184 -16.742 4.293   1.00 12.44 ?  79  GLY   B O    1 
ATOM   4929 H H    . GLY   B 1 79  ? 37.515 -17.159 6.698   1.00 15.08 ?  79  GLY   B H    1 
ATOM   4930 H HA2  . GLY   B 1 79  ? 36.587 -15.370 4.907   1.00 14.63 ?  79  GLY   B HA2  1 
ATOM   4931 H HA3  . GLY   B 1 79  ? 37.491 -15.034 6.150   1.00 14.63 ?  79  GLY   B HA3  1 
ATOM   4932 N N    . SER   B 1 80  ? 38.938 -14.511 4.071   1.00 11.91 ?  80  SER   B N    1 
ATOM   4933 C CA   . SER   B 1 80  ? 40.043 -14.371 3.133   1.00 11.74 ?  80  SER   B CA   1 
ATOM   4934 C C    . SER   B 1 80  ? 40.623 -12.965 3.199   1.00 11.56 ?  80  SER   B C    1 
ATOM   4935 O O    . SER   B 1 80  ? 40.008 -12.032 3.720   1.00 12.92 ?  80  SER   B O    1 
ATOM   4936 C CB   . SER   B 1 80  ? 39.599 -14.657 1.696   1.00 12.38 ?  80  SER   B CB   1 
ATOM   4937 O OG   . SER   B 1 80  ? 38.767 -13.624 1.197   1.00 13.36 ?  80  SER   B OG   1 
ATOM   4938 H H    . SER   B 1 80  ? 38.563 -13.767 4.281   1.00 14.28 ?  80  SER   B H    1 
ATOM   4939 H HA   . SER   B 1 80  ? 40.736 -15.001 3.374   1.00 14.08 ?  80  SER   B HA   1 
ATOM   4940 H HB2  . SER   B 1 80  ? 40.381 -14.729 1.128   1.00 14.85 ?  80  SER   B HB2  1 
ATOM   4941 H HB3  . SER   B 1 80  ? 39.103 -15.494 1.680   1.00 14.85 ?  80  SER   B HB3  1 
ATOM   4942 H HG   . SER   B 1 80  ? 38.078 -13.555 1.678   1.00 16.03 ?  80  SER   B HG   1 
ATOM   4943 N N    . CYS   B 1 81  ? 41.812 -12.820 2.620   1.00 11.14 ?  81  CYS   B N    1 
ATOM   4944 C CA   . CYS   B 1 81  ? 42.355 -11.506 2.303   1.00 11.43 ?  81  CYS   B CA   1 
ATOM   4945 C C    . CYS   B 1 81  ? 43.129 -11.589 0.995   1.00 10.74 ?  81  CYS   B C    1 
ATOM   4946 O O    . CYS   B 1 81  ? 43.642 -12.649 0.616   1.00 11.78 ?  81  CYS   B O    1 
ATOM   4947 C CB   . CYS   B 1 81  ? 43.247 -10.944 3.423   1.00 12.12 ?  81  CYS   B CB   1 
ATOM   4948 S SG   . CYS   B 1 81  ? 44.770 -11.887 3.682   1.00 12.93 ?  81  CYS   B SG   1 
ATOM   4949 H H    . CYS   B 1 81  ? 42.328 -13.473 2.385   1.00 13.36 ?  81  CYS   B H    1 
ATOM   4950 H HA   . CYS   B 1 81  ? 41.620 -10.885 2.173   1.00 13.71 ?  81  CYS   B HA   1 
ATOM   4951 H HB2  . CYS   B 1 81  ? 43.500 -10.033 3.200   1.00 14.54 ?  81  CYS   B HB2  1 
ATOM   4952 H HB3  . CYS   B 1 81  ? 42.743 -10.947 4.255   1.00 14.54 ?  81  CYS   B HB3  1 
ATOM   4953 H HG   . CYS   B 1 81  ? 45.392 -11.385 4.581   1.00 15.52 ?  81  CYS   B HG   1 
ATOM   4954 N N    . VAL   B 1 82  ? 43.233 -10.441 0.323   1.00 11.29 ?  82  VAL   B N    1 
ATOM   4955 C CA   . VAL   B 1 82  ? 43.998 -10.315 -0.914  1.00 11.42 ?  82  VAL   B CA   1 
ATOM   4956 C C    . VAL   B 1 82  ? 45.339 -9.674  -0.591  1.00 11.86 ?  82  VAL   B C    1 
ATOM   4957 O O    . VAL   B 1 82  ? 45.390 -8.556  -0.057  1.00 12.69 ?  82  VAL   B O    1 
ATOM   4958 C CB   . VAL   B 1 82  ? 43.255 -9.474  -1.964  1.00 12.61 ?  82  VAL   B CB   1 
ATOM   4959 C CG1  . VAL   B 1 82  ? 44.111 -9.333  -3.217  1.00 13.97 ?  82  VAL   B CG1  1 
ATOM   4960 C CG2  . VAL   B 1 82  ? 41.899 -10.083 -2.295  1.00 13.69 ?  82  VAL   B CG2  1 
ATOM   4961 H H    . VAL   B 1 82  ? 42.849 -9.700  0.560   1.00 13.54 ?  82  VAL   B H    1 
ATOM   4962 H HA   . VAL   B 1 82  ? 44.156 -11.194 -1.288  1.00 13.70 ?  82  VAL   B HA   1 
ATOM   4963 H HB   . VAL   B 1 82  ? 43.102 -8.586  -1.610  1.00 15.13 ?  82  VAL   B HB   1 
ATOM   4964 H HG11 . VAL   B 1 82  ? 43.552 -9.024  -3.949  1.00 16.76 ?  82  VAL   B HG11 1 
ATOM   4965 H HG12 . VAL   B 1 82  ? 44.816 -8.685  -3.051  1.00 16.76 ?  82  VAL   B HG12 1 
ATOM   4966 H HG13 . VAL   B 1 82  ? 44.496 -10.193 -3.438  1.00 16.76 ?  82  VAL   B HG13 1 
ATOM   4967 H HG21 . VAL   B 1 82  ? 41.469 -9.549  -2.985  1.00 16.43 ?  82  VAL   B HG21 1 
ATOM   4968 H HG22 . VAL   B 1 82  ? 42.028 -10.990 -2.618  1.00 16.43 ?  82  VAL   B HG22 1 
ATOM   4969 H HG23 . VAL   B 1 82  ? 41.351 -10.091 -1.496  1.00 16.43 ?  82  VAL   B HG23 1 
ATOM   4970 N N    . LEU   B 1 83  ? 46.421 -10.358 -0.958  1.00 11.53 ?  83  LEU   B N    1 
ATOM   4971 C CA   . LEU   B 1 83  ? 47.773 -9.834  -0.838  1.00 11.31 ?  83  LEU   B CA   1 
ATOM   4972 C C    . LEU   B 1 83  ? 48.473 -9.975  -2.188  1.00 11.16 ?  83  LEU   B C    1 
ATOM   4973 O O    . LEU   B 1 83  ? 47.872 -10.401 -3.180  1.00 10.95 ?  83  LEU   B O    1 
ATOM   4974 C CB   . LEU   B 1 83  ? 48.526 -10.510 0.317   1.00 12.01 ?  83  LEU   B CB   1 
ATOM   4975 C CG   . LEU   B 1 83  ? 47.997 -10.155 1.713   1.00 13.13 ?  83  LEU   B CG   1 
ATOM   4976 C CD1  . LEU   B 1 83  ? 48.619 -11.015 2.796   1.00 13.79 ?  83  LEU   B CD1  1 
ATOM   4977 C CD2  . LEU   B 1 83  ? 48.189 -8.672  2.041   1.00 14.37 ?  83  LEU   B CD2  1 
ATOM   4978 H H    . LEU   B 1 83  ? 46.389 -11.155 -1.288  1.00 13.83 ?  83  LEU   B H    1 
ATOM   4979 H HA   . LEU   B 1 83  ? 47.717 -8.889  -0.644  1.00 13.57 ?  83  LEU   B HA   1 
ATOM   4980 H HB2  . LEU   B 1 83  ? 48.468 -11.467 0.213   1.00 14.42 ?  83  LEU   B HB2  1 
ATOM   4981 H HB3  . LEU   B 1 83  ? 49.458 -10.231 0.279   1.00 14.42 ?  83  LEU   B HB3  1 
ATOM   4982 H HG   . LEU   B 1 83  ? 47.044 -10.326 1.723   1.00 15.75 ?  83  LEU   B HG   1 
ATOM   4983 H HD11 . LEU   B 1 83  ? 48.241 -10.762 3.654   1.00 16.55 ?  83  LEU   B HD11 1 
ATOM   4984 H HD12 . LEU   B 1 83  ? 48.416 -11.947 2.610   1.00 16.55 ?  83  LEU   B HD12 1 
ATOM   4985 H HD13 . LEU   B 1 83  ? 49.576 -10.878 2.800   1.00 16.55 ?  83  LEU   B HD13 1 
ATOM   4986 H HD21 . LEU   B 1 83  ? 47.967 -8.525  2.975   1.00 17.25 ?  83  LEU   B HD21 1 
ATOM   4987 H HD22 . LEU   B 1 83  ? 49.111 -8.427  1.878   1.00 17.25 ?  83  LEU   B HD22 1 
ATOM   4988 H HD23 . LEU   B 1 83  ? 47.601 -8.144  1.477   1.00 17.25 ?  83  LEU   B HD23 1 
ATOM   4989 N N    . SER   B 1 84  ? 49.749 -9.607  -2.242  1.00 12.47 ?  84  SER   B N    1 
ATOM   4990 C CA   . SER   B 1 84  ? 50.487 -9.725  -3.491  1.00 12.65 ?  84  SER   B CA   1 
ATOM   4991 C C    . SER   B 1 84  ? 50.639 -11.185 -3.904  1.00 12.01 ?  84  SER   B C    1 
ATOM   4992 O O    . SER   B 1 84  ? 50.758 -12.082 -3.070  1.00 11.78 ?  84  SER   B O    1 
ATOM   4993 C CB   . SER   B 1 84  ? 51.883 -9.119  -3.345  1.00 14.51 ?  84  SER   B CB   1 
ATOM   4994 O OG   . SER   B 1 84  ? 52.631 -9.329  -4.527  1.00 16.10 ?  84  SER   B OG   1 
ATOM   4995 H H    . SER   B 1 84  ? 50.198 -9.280  -1.585  1.00 14.96 ?  84  SER   B H    1 
ATOM   4996 H HA   . SER   B 1 84  ? 50.019 -9.256  -4.197  1.00 15.18 ?  84  SER   B HA   1 
ATOM   4997 H HB2  . SER   B 1 84  ? 51.798 -8.162  -3.184  1.00 17.40 ?  84  SER   B HB2  1 
ATOM   4998 H HB3  . SER   B 1 84  ? 52.340 -9.539  -2.601  1.00 17.40 ?  84  SER   B HB3  1 
ATOM   4999 H HG   . SER   B 1 84  ? 53.399 -8.986  -4.448  1.00 19.32 ?  84  SER   B HG   1 
ATOM   5000 N N    . GLY   B 1 85  ? 50.703 -11.408 -5.210  1.00 12.74 ?  85  GLY   B N    1 
ATOM   5001 C CA   . GLY   B 1 85  ? 51.056 -12.702 -5.743  1.00 13.39 ?  85  GLY   B CA   1 
ATOM   5002 C C    . GLY   B 1 85  ? 52.529 -12.893 -6.044  1.00 12.74 ?  85  GLY   B C    1 
ATOM   5003 O O    . GLY   B 1 85  ? 52.907 -13.970 -6.509  1.00 13.06 ?  85  GLY   B O    1 
ATOM   5004 H H    . GLY   B 1 85  ? 50.558 -10.817 -5.810  1.00 15.29 ?  85  GLY   B H    1 
ATOM   5005 H HA2  . GLY   B 1 85  ? 50.794 -13.390 -5.109  1.00 16.07 ?  85  GLY   B HA2  1 
ATOM   5006 H HA3  . GLY   B 1 85  ? 50.572 -12.851 -6.563  1.00 16.07 ?  85  GLY   B HA3  1 
ATOM   5007 N N    . HIS   B 1 86  ? 53.381 -11.891 -5.818  1.00 12.83 ?  86  HIS   B N    1 
ATOM   5008 C CA   . HIS   B 1 86  ? 54.846 -12.058 -5.903  1.00 12.81 ?  86  HIS   B CA   1 
ATOM   5009 C C    . HIS   B 1 86  ? 55.220 -12.567 -7.293  1.00 12.75 ?  86  HIS   B C    1 
ATOM   5010 O O    . HIS   B 1 86  ? 54.824 -11.952 -8.295  1.00 13.64 ?  86  HIS   B O    1 
ATOM   5011 C CB   . HIS   B 1 86  ? 55.342 -12.896 -4.728  1.00 13.48 ?  86  HIS   B CB   1 
ATOM   5012 C CG   . HIS   B 1 86  ? 55.017 -12.295 -3.402  1.00 13.32 ?  86  HIS   B CG   1 
ATOM   5013 N ND1  . HIS   B 1 86  ? 55.831 -11.368 -2.788  1.00 14.73 ?  86  HIS   B ND1  1 
ATOM   5014 C CD2  . HIS   B 1 86  ? 53.940 -12.448 -2.594  1.00 13.82 ?  86  HIS   B CD2  1 
ATOM   5015 C CE1  . HIS   B 1 86  ? 55.272 -10.982 -1.656  1.00 14.53 ?  86  HIS   B CE1  1 
ATOM   5016 N NE2  . HIS   B 1 86  ? 54.124 -11.620 -1.514  1.00 13.99 ?  86  HIS   B NE2  1 
ATOM   5017 H H    . HIS   B 1 86  ? 53.140 -11.094 -5.612  1.00 15.40 ?  86  HIS   B H    1 
ATOM   5018 H HA   . HIS   B 1 86  ? 55.252 -11.185 -5.809  1.00 15.37 ?  86  HIS   B HA   1 
ATOM   5019 H HB2  . HIS   B 1 86  ? 54.938 -13.776 -4.768  1.00 16.18 ?  86  HIS   B HB2  1 
ATOM   5020 H HB3  . HIS   B 1 86  ? 56.312 -12.979 -4.786  1.00 16.18 ?  86  HIS   B HB3  1 
ATOM   5021 H HD2  . HIS   B 1 86  ? 53.209 -13.005 -2.747  1.00 16.58 ?  86  HIS   B HD2  1 
ATOM   5022 H HE1  . HIS   B 1 86  ? 55.632 -10.373 -1.053  1.00 17.43 ?  86  HIS   B HE1  1 
ATOM   5023 H HE2  . HIS   B 1 86  ? 53.584 -11.541 -0.848  1.00 16.78 ?  86  HIS   B HE2  1 
ATOM   5024 N N    . ASN   B 1 87  ? 55.982 -13.654 -7.405  1.00 13.22 ?  87  ASN   B N    1 
ATOM   5025 C CA   . ASN   B 1 87  ? 56.379 -14.230 -8.682  1.00 13.97 ?  87  ASN   B CA   1 
ATOM   5026 C C    . ASN   B 1 87  ? 55.394 -15.271 -9.188  1.00 13.50 ?  87  ASN   B C    1 
ATOM   5027 O O    . ASN   B 1 87  ? 55.706 -15.976 -10.152 1.00 15.26 ?  87  ASN   B O    1 
ATOM   5028 C CB   . ASN   B 1 87  ? 57.774 -14.861 -8.568  1.00 15.74 ?  87  ASN   B CB   1 
ATOM   5029 C CG   . ASN   B 1 87  ? 57.831 -15.972 -7.526  1.00 16.54 ?  87  ASN   B CG   1 
ATOM   5030 O OD1  . ASN   B 1 87  ? 57.200 -15.885 -6.474  1.00 15.93 ?  87  ASN   B OD1  1 
ATOM   5031 N ND2  . ASN   B 1 87  ? 58.585 -17.033 -7.828  1.00 18.26 ?  87  ASN   B ND2  1 
ATOM   5032 H H    . ASN   B 1 87  ? 56.285 -14.091 -6.729  1.00 15.86 ?  87  ASN   B H    1 
ATOM   5033 H HA   . ASN   B 1 87  ? 56.426 -13.524 -9.339  1.00 16.77 ?  87  ASN   B HA   1 
ATOM   5034 H HB2  . ASN   B 1 87  ? 58.019 -15.243 -9.426  1.00 18.89 ?  87  ASN   B HB2  1 
ATOM   5035 H HB3  . ASN   B 1 87  ? 58.410 -14.176 -8.314  1.00 18.89 ?  87  ASN   B HB3  1 
ATOM   5036 H HD21 . ASN   B 1 87  ? 58.653 -17.684 -7.272  1.00 21.91 ?  87  ASN   B HD21 1 
ATOM   5037 H HD22 . ASN   B 1 87  ? 59.008 -17.062 -8.578  1.00 21.91 ?  87  ASN   B HD22 1 
ATOM   5038 N N    . LEU   B 1 88  ? 54.214 -15.372 -8.570  1.00 12.78 ?  88  LEU   B N    1 
ATOM   5039 C CA   . LEU   B 1 88  ? 53.233 -16.398 -8.898  1.00 13.03 ?  88  LEU   B CA   1 
ATOM   5040 C C    . LEU   B 1 88  ? 52.005 -15.877 -9.623  1.00 12.88 ?  88  LEU   B C    1 
ATOM   5041 O O    . LEU   B 1 88  ? 51.411 -16.621 -10.415 1.00 14.81 ?  88  LEU   B O    1 
ATOM   5042 C CB   . LEU   B 1 88  ? 52.759 -17.085 -7.615  1.00 13.85 ?  88  LEU   B CB   1 
ATOM   5043 C CG   . LEU   B 1 88  ? 53.875 -17.749 -6.819  1.00 16.12 ?  88  LEU   B CG   1 
ATOM   5044 C CD1  . LEU   B 1 88  ? 53.380 -18.100 -5.428  1.00 17.46 ?  88  LEU   B CD1  1 
ATOM   5045 C CD2  . LEU   B 1 88  ? 54.359 -18.984 -7.552  1.00 18.77 ?  88  LEU   B CD2  1 
ATOM   5046 H H    . LEU   B 1 88  ? 53.955 -14.844 -7.934  1.00 15.33 ?  88  LEU   B H    1 
ATOM   5047 H HA   . LEU   B 1 88  ? 53.647 -17.060 -9.459  1.00 15.63 ?  88  LEU   B HA   1 
ATOM   5048 H HB2  . LEU   B 1 88  ? 52.334 -16.428 -7.041  1.00 16.62 ?  88  LEU   B HB2  1 
ATOM   5049 H HB3  . LEU   B 1 88  ? 52.113 -17.773 -7.853  1.00 16.62 ?  88  LEU   B HB3  1 
ATOM   5050 H HG   . LEU   B 1 88  ? 54.616 -17.131 -6.735  1.00 19.35 ?  88  LEU   B HG   1 
ATOM   5051 H HD11 . LEU   B 1 88  ? 54.024 -18.688 -5.006  1.00 20.95 ?  88  LEU   B HD11 1 
ATOM   5052 H HD12 . LEU   B 1 88  ? 53.287 -17.284 -4.912  1.00 20.95 ?  88  LEU   B HD12 1 
ATOM   5053 H HD13 . LEU   B 1 88  ? 52.522 -18.544 -5.503  1.00 20.95 ?  88  LEU   B HD13 1 
ATOM   5054 H HD21 . LEU   B 1 88  ? 55.012 -19.439 -7.000  1.00 22.52 ?  88  LEU   B HD21 1 
ATOM   5055 H HD22 . LEU   B 1 88  ? 53.603 -19.567 -7.723  1.00 22.52 ?  88  LEU   B HD22 1 
ATOM   5056 H HD23 . LEU   B 1 88  ? 54.766 -18.715 -8.392  1.00 22.52 ?  88  LEU   B HD23 1 
ATOM   5057 N N    . ALA   B 1 89  ? 51.596 -14.643 -9.352  1.00 12.28 ?  89  ALA   B N    1 
ATOM   5058 C CA   . ALA   B 1 89  ? 50.307 -14.149 -9.810  1.00 11.70 ?  89  ALA   B CA   1 
ATOM   5059 C C    . ALA   B 1 89  ? 50.277 -12.661 -9.522  1.00 11.76 ?  89  ALA   B C    1 
ATOM   5060 O O    . ALA   B 1 89  ? 51.110 -12.142 -8.778  1.00 12.73 ?  89  ALA   B O    1 
ATOM   5061 C CB   . ALA   B 1 89  ? 49.155 -14.824 -9.070  1.00 11.98 ?  89  ALA   B CB   1 
ATOM   5062 H H    . ALA   B 1 89  ? 52.036 -14.067 -8.885  1.00 14.73 ?  89  ALA   B H    1 
ATOM   5063 H HA   . ALA   B 1 89  ? 50.205 -14.292 -10.767 1.00 14.04 ?  89  ALA   B HA   1 
ATOM   5064 H HB1  . ALA   B 1 89  ? 48.311 -14.491 -9.428  1.00 14.37 ?  89  ALA   B HB1  1 
ATOM   5065 H HB2  . ALA   B 1 89  ? 49.212 -15.782 -9.211  1.00 14.37 ?  89  ALA   B HB2  1 
ATOM   5066 H HB3  . ALA   B 1 89  ? 49.220 -14.618 -8.130  1.00 14.37 ?  89  ALA   B HB3  1 
ATOM   5067 N N    . LYS   B 1 90  ? 49.296 -11.968 -10.093 1.00 12.87 ?  90  LYS   B N    1 
ATOM   5068 C CA   . LYS   B 1 90  ? 49.101 -10.583 -9.686  1.00 12.90 ?  90  LYS   B CA   1 
ATOM   5069 C C    . LYS   B 1 90  ? 48.783 -10.511 -8.198  1.00 12.88 ?  90  LYS   B C    1 
ATOM   5070 O O    . LYS   B 1 90  ? 49.421 -9.755  -7.447  1.00 13.93 ?  90  LYS   B O    1 
ATOM   5071 C CB   . LYS   B 1 90  ? 48.016 -9.924  -10.536 1.00 14.48 ?  90  LYS   B CB   1 
ATOM   5072 C CG   . LYS   B 1 90  ? 47.717 -8.483  -10.152 1.00 15.15 ?  90  LYS   B CG   1 
ATOM   5073 C CD   . LYS   B 1 90  ? 48.918 -7.585  -10.257 1.00 17.56 ?  90  LYS   B CD   1 
ATOM   5074 C CE   . LYS   B 1 90  ? 48.479 -6.173  -9.965  1.00 19.80 ?  90  LYS   B CE   1 
ATOM   5075 N NZ   . LYS   B 1 90  ? 49.619 -5.232  -9.890  1.00 19.90 ?  90  LYS   B NZ   1 
ATOM   5076 H H    . LYS   B 1 90  ? 48.751 -12.265 -10.690 1.00 15.44 ?  90  LYS   B H    1 
ATOM   5077 H HA   . LYS   B 1 90  ? 49.924 -10.099 -9.834  1.00 15.47 ?  90  LYS   B HA   1 
ATOM   5078 H HB2  . LYS   B 1 90  ? 48.303 -9.926  -11.467 1.00 17.38 ?  90  LYS   B HB2  1 
ATOM   5079 H HB3  . LYS   B 1 90  ? 47.194 -10.433 -10.453 1.00 17.38 ?  90  LYS   B HB3  1 
ATOM   5080 H HG2  . LYS   B 1 90  ? 47.029 -8.135  -10.743 1.00 18.17 ?  90  LYS   B HG2  1 
ATOM   5081 H HG3  . LYS   B 1 90  ? 47.398 -8.459  -9.233  1.00 18.17 ?  90  LYS   B HG3  1 
ATOM   5082 H HD2  . LYS   B 1 90  ? 49.584 -7.846  -9.601  1.00 21.07 ?  90  LYS   B HD2  1 
ATOM   5083 H HD3  . LYS   B 1 90  ? 49.281 -7.624  -11.155 1.00 21.07 ?  90  LYS   B HD3  1 
ATOM   5084 H HE2  . LYS   B 1 90  ? 47.890 -5.865  -10.674 1.00 23.76 ?  90  LYS   B HE2  1 
ATOM   5085 H HE3  . LYS   B 1 90  ? 48.018 -6.145  -9.114  1.00 23.76 ?  90  LYS   B HE3  1 
ATOM   5086 H HZ1  . LYS   B 1 90  ? 49.329 -4.404  -9.720  1.00 23.88 ?  90  LYS   B HZ1  1 
ATOM   5087 H HZ2  . LYS   B 1 90  ? 50.180 -5.475  -9.243  1.00 23.88 ?  90  LYS   B HZ2  1 
ATOM   5088 H HZ3  . LYS   B 1 90  ? 50.063 -5.220  -10.664 1.00 23.88 ?  90  LYS   B HZ3  1 
ATOM   5089 N N    . HIS   B 1 91  ? 47.822 -11.327 -7.751  1.00 11.45 ?  91  HIS   B N    1 
ATOM   5090 C CA   . HIS   B 1 91  ? 47.354 -11.348 -6.377  1.00 11.57 ?  91  HIS   B CA   1 
ATOM   5091 C C    . HIS   B 1 91  ? 47.348 -12.776 -5.860  1.00 10.89 ?  91  HIS   B C    1 
ATOM   5092 O O    . HIS   B 1 91  ? 47.117 -13.728 -6.615  1.00 11.17 ?  91  HIS   B O    1 
ATOM   5093 C CB   . HIS   B 1 91  ? 45.902 -10.866 -6.259  1.00 13.11 ?  91  HIS   B CB   1 
ATOM   5094 C CG   . HIS   B 1 91  ? 45.689 -9.458  -6.690  1.00 16.35 ?  91  HIS   B CG   1 
ATOM   5095 N ND1  . HIS   B 1 91  ? 46.303 -8.387  -6.077  1.00 18.83 ?  91  HIS   B ND1  1 
ATOM   5096 C CD2  . HIS   B 1 91  ? 44.896 -8.938  -7.653  1.00 18.59 ?  91  HIS   B CD2  1 
ATOM   5097 C CE1  . HIS   B 1 91  ? 45.916 -7.266  -6.661  1.00 19.71 ?  91  HIS   B CE1  1 
ATOM   5098 N NE2  . HIS   B 1 91  ? 45.056 -7.573  -7.616  1.00 19.78 ?  91  HIS   B NE2  1 
ATOM   5099 H H    . HIS   B 1 91  ? 47.414 -11.899 -8.251  1.00 13.74 ?  91  HIS   B H    1 
ATOM   5100 H HA   . HIS   B 1 91  ? 47.928 -10.798 -5.814  1.00 13.88 ?  91  HIS   B HA   1 
ATOM   5101 H HB2  . HIS   B 1 91  ? 45.339 -11.430 -6.808  1.00 15.73 ?  91  HIS   B HB2  1 
ATOM   5102 H HB3  . HIS   B 1 91  ? 45.624 -10.934 -5.329  1.00 15.73 ?  91  HIS   B HB3  1 
ATOM   5103 H HD1  . HIS   B 1 91  ? 46.859 -8.440  -5.420  1.00 22.60 ?  91  HIS   B HD1  1 
ATOM   5104 H HD2  . HIS   B 1 91  ? 44.356 -9.407  -8.239  1.00 22.30 ?  91  HIS   B HD2  1 
ATOM   5105 H HE1  . HIS   B 1 91  ? 46.197 -6.406  -6.429  1.00 23.65 ?  91  HIS   B HE1  1 
ATOM   5106 N N    . CYS   B 1 92  ? 47.542 -12.910 -4.554  1.00 10.79 ?  92  CYS   B N    1 
ATOM   5107 C CA   . CYS   B 1 92  ? 47.242 -14.143 -3.839  1.00 10.61 ?  92  CYS   B CA   1 
ATOM   5108 C C    . CYS   B 1 92  ? 46.024 -13.908 -2.955  1.00 10.24 ?  92  CYS   B C    1 
ATOM   5109 O O    . CYS   B 1 92  ? 46.019 -13.005 -2.107  1.00 11.08 ?  92  CYS   B O    1 
ATOM   5110 C CB   . CYS   B 1 92  ? 48.421 -14.601 -2.989  1.00 10.99 ?  92  CYS   B CB   1 
ATOM   5111 S SG   . CYS   B 1 92  ? 48.067 -16.140 -2.091  1.00 11.12 ?  92  CYS   B SG   1 
ATOM   5112 H H    . CYS   B 1 92  ? 47.865 -12.293 -4.048  1.00 12.94 ?  92  CYS   B H    1 
ATOM   5113 H HA   . CYS   B 1 92  ? 47.040 -14.845 -4.480  1.00 12.73 ?  92  CYS   B HA   1 
ATOM   5114 H HB2  . CYS   B 1 92  ? 49.186 -14.753 -3.560  1.00 13.19 ?  92  CYS   B HB2  1 
ATOM   5115 H HB3  . CYS   B 1 92  ? 48.619 -13.914 -2.335  1.00 13.19 ?  92  CYS   B HB3  1 
ATOM   5116 H HG   . CYS   B 1 92  ? 49.043 -16.450 -1.468  1.00 13.35 ?  92  CYS   B HG   1 
ATOM   5117 N N    . LEU   B 1 93  ? 44.987 -14.716 -3.169  1.00 10.07 ?  93  LEU   B N    1 
ATOM   5118 C CA   . LEU   B 1 93  ? 43.811 -14.732 -2.310  1.00 10.36 ?  93  LEU   B CA   1 
ATOM   5119 C C    . LEU   B 1 93  ? 44.033 -15.798 -1.246  1.00 9.87  ?  93  LEU   B C    1 
ATOM   5120 O O    . LEU   B 1 93  ? 43.988 -17.000 -1.541  1.00 10.33 ?  93  LEU   B O    1 
ATOM   5121 C CB   . LEU   B 1 93  ? 42.547 -15.021 -3.116  1.00 10.88 ?  93  LEU   B CB   1 
ATOM   5122 C CG   . LEU   B 1 93  ? 41.248 -15.043 -2.308  1.00 11.48 ?  93  LEU   B CG   1 
ATOM   5123 C CD1  . LEU   B 1 93  ? 40.885 -13.650 -1.830  1.00 11.87 ?  93  LEU   B CD1  1 
ATOM   5124 C CD2  . LEU   B 1 93  ? 40.126 -15.638 -3.141  1.00 11.48 ?  93  LEU   B CD2  1 
ATOM   5125 H H    . LEU   B 1 93  ? 44.948 -15.293 -3.819  1.00 12.09 ?  93  LEU   B H    1 
ATOM   5126 H HA   . LEU   B 1 93  ? 43.722 -13.873 -1.877  1.00 12.43 ?  93  LEU   B HA   1 
ATOM   5127 H HB2  . LEU   B 1 93  ? 42.452 -14.329 -3.793  1.00 13.05 ?  93  LEU   B HB2  1 
ATOM   5128 H HB3  . LEU   B 1 93  ? 42.636 -15.882 -3.541  1.00 13.05 ?  93  LEU   B HB3  1 
ATOM   5129 H HG   . LEU   B 1 93  ? 41.368 -15.599 -1.524  1.00 13.77 ?  93  LEU   B HG   1 
ATOM   5130 H HD11 . LEU   B 1 93  ? 40.036 -13.685 -1.365  1.00 14.24 ?  93  LEU   B HD11 1 
ATOM   5131 H HD12 . LEU   B 1 93  ? 41.579 -13.328 -1.233  1.00 14.24 ?  93  LEU   B HD12 1 
ATOM   5132 H HD13 . LEU   B 1 93  ? 40.816 -13.061 -2.601  1.00 14.24 ?  93  LEU   B HD13 1 
ATOM   5133 H HD21 . LEU   B 1 93  ? 39.307 -15.640 -2.617  1.00 13.78 ?  93  LEU   B HD21 1 
ATOM   5134 H HD22 . LEU   B 1 93  ? 40.003 -15.103 -3.940  1.00 13.78 ?  93  LEU   B HD22 1 
ATOM   5135 H HD23 . LEU   B 1 93  ? 40.361 -16.547 -3.384  1.00 13.78 ?  93  LEU   B HD23 1 
ATOM   5136 N N    . HIS   B 1 94  ? 44.309 -15.363 -0.023  1.00 9.85  ?  94  HIS   B N    1 
ATOM   5137 C CA   . HIS   B 1 94  ? 44.526 -16.271 1.097   1.00 10.25 ?  94  HIS   B CA   1 
ATOM   5138 C C    . HIS   B 1 94  ? 43.167 -16.628 1.676   1.00 10.60 ?  94  HIS   B C    1 
ATOM   5139 O O    . HIS   B 1 94  ? 42.496 -15.756 2.230   1.00 11.99 ?  94  HIS   B O    1 
ATOM   5140 C CB   . HIS   B 1 94  ? 45.402 -15.601 2.156   1.00 10.60 ?  94  HIS   B CB   1 
ATOM   5141 C CG   . HIS   B 1 94  ? 46.781 -15.293 1.683   1.00 10.38 ?  94  HIS   B CG   1 
ATOM   5142 N ND1  . HIS   B 1 94  ? 47.810 -16.205 1.766   1.00 10.74 ?  94  HIS   B ND1  1 
ATOM   5143 C CD2  . HIS   B 1 94  ? 47.285 -14.183 1.089   1.00 10.65 ?  94  HIS   B CD2  1 
ATOM   5144 C CE1  . HIS   B 1 94  ? 48.900 -15.650 1.258   1.00 10.75 ?  94  HIS   B CE1  1 
ATOM   5145 N NE2  . HIS   B 1 94  ? 48.609 -14.428 0.840   1.00 10.87 ?  94  HIS   B NE2  1 
ATOM   5146 H H    . HIS   B 1 94  ? 44.376 -14.529 0.191   1.00 11.82 ?  94  HIS   B H    1 
ATOM   5147 H HA   . HIS   B 1 94  ? 44.963 -17.081 0.786   1.00 12.30 ?  94  HIS   B HA   1 
ATOM   5148 H HB2  . HIS   B 1 94  ? 44.989 -14.773 2.426   1.00 12.72 ?  94  HIS   B HB2  1 
ATOM   5149 H HB3  . HIS   B 1 94  ? 45.483 -16.201 2.915   1.00 12.72 ?  94  HIS   B HB3  1 
ATOM   5150 H HD2  . HIS   B 1 94  ? 46.826 -13.399 0.892   1.00 12.78 ?  94  HIS   B HD2  1 
ATOM   5151 H HE1  . HIS   B 1 94  ? 49.736 -16.062 1.196   1.00 12.90 ?  94  HIS   B HE1  1 
ATOM   5152 H HE2  . HIS   B 1 94  ? 49.164 -13.882 0.470   1.00 13.05 ?  94  HIS   B HE2  1 
ATOM   5153 N N    . VAL   B 1 95  ? 42.742 -17.885 1.532   1.00 10.26 ?  95  VAL   B N    1 
ATOM   5154 C CA   . VAL   B 1 95  ? 41.415 -18.325 1.960   1.00 10.42 ?  95  VAL   B CA   1 
ATOM   5155 C C    . VAL   B 1 95  ? 41.581 -19.363 3.056   1.00 10.75 ?  95  VAL   B C    1 
ATOM   5156 O O    . VAL   B 1 95  ? 42.348 -20.320 2.900   1.00 11.52 ?  95  VAL   B O    1 
ATOM   5157 C CB   . VAL   B 1 95  ? 40.597 -18.924 0.799   1.00 11.04 ?  95  VAL   B CB   1 
ATOM   5158 C CG1  . VAL   B 1 95  ? 39.216 -19.376 1.284   1.00 12.13 ?  95  VAL   B CG1  1 
ATOM   5159 C CG2  . VAL   B 1 95  ? 40.481 -17.939 -0.340  1.00 10.86 ?  95  VAL   B CG2  1 
ATOM   5160 H H    . VAL   B 1 95  ? 43.211 -18.514 1.178   1.00 12.31 ?  95  VAL   B H    1 
ATOM   5161 H HA   . VAL   B 1 95  ? 40.922 -17.573 2.324   1.00 12.50 ?  95  VAL   B HA   1 
ATOM   5162 H HB   . VAL   B 1 95  ? 41.058 -19.706 0.463   1.00 13.25 ?  95  VAL   B HB   1 
ATOM   5163 H HG11 . VAL   B 1 95  ? 38.655 -19.567 0.513   1.00 14.56 ?  95  VAL   B HG11 1 
ATOM   5164 H HG12 . VAL   B 1 95  ? 39.311 -20.179 1.823   1.00 14.56 ?  95  VAL   B HG12 1 
ATOM   5165 H HG13 . VAL   B 1 95  ? 38.814 -18.669 1.812   1.00 14.56 ?  95  VAL   B HG13 1 
ATOM   5166 H HG21 . VAL   B 1 95  ? 39.906 -18.321 -1.024  1.00 13.03 ?  95  VAL   B HG21 1 
ATOM   5167 H HG22 . VAL   B 1 95  ? 40.091 -17.117 -0.003  1.00 13.03 ?  95  VAL   B HG22 1 
ATOM   5168 H HG23 . VAL   B 1 95  ? 41.361 -17.772 -0.698  1.00 13.03 ?  95  VAL   B HG23 1 
ATOM   5169 N N    . VAL   B 1 96  ? 40.852 -19.189 4.151   1.00 11.38 ?  96  VAL   B N    1 
ATOM   5170 C CA   . VAL   B 1 96  ? 40.925 -20.102 5.291   1.00 11.53 ?  96  VAL   B CA   1 
ATOM   5171 C C    . VAL   B 1 96  ? 39.739 -21.067 5.238   1.00 12.43 ?  96  VAL   B C    1 
ATOM   5172 O O    . VAL   B 1 96  ? 38.619 -20.718 5.617   1.00 13.02 ?  96  VAL   B O    1 
ATOM   5173 C CB   . VAL   B 1 96  ? 40.969 -19.356 6.628   1.00 12.50 ?  96  VAL   B CB   1 
ATOM   5174 C CG1  . VAL   B 1 96  ? 41.146 -20.350 7.773   1.00 13.26 ?  96  VAL   B CG1  1 
ATOM   5175 C CG2  . VAL   B 1 96  ? 42.081 -18.321 6.643   1.00 13.04 ?  96  VAL   B CG2  1 
ATOM   5176 H H    . VAL   B 1 96  ? 40.297 -18.542 4.266   1.00 13.66 ?  96  VAL   B H    1 
ATOM   5177 H HA   . VAL   B 1 96  ? 41.742 -20.627 5.222   1.00 13.83 ?  96  VAL   B HA   1 
ATOM   5178 H HB   . VAL   B 1 96  ? 40.126 -18.896 6.762   1.00 15.00 ?  96  VAL   B HB   1 
ATOM   5179 H HG11 . VAL   B 1 96  ? 41.322 -19.858 8.595   1.00 15.91 ?  96  VAL   B HG11 1 
ATOM   5180 H HG12 . VAL   B 1 96  ? 40.336 -20.873 7.874   1.00 15.91 ?  96  VAL   B HG12 1 
ATOM   5181 H HG13 . VAL   B 1 96  ? 41.896 -20.933 7.576   1.00 15.91 ?  96  VAL   B HG13 1 
ATOM   5182 H HG21 . VAL   B 1 96  ? 42.123 -17.909 7.525   1.00 15.65 ?  96  VAL   B HG21 1 
ATOM   5183 H HG22 . VAL   B 1 96  ? 42.923 -18.749 6.439   1.00 15.65 ?  96  VAL   B HG22 1 
ATOM   5184 H HG23 . VAL   B 1 96  ? 41.887 -17.636 5.978   1.00 15.65 ?  96  VAL   B HG23 1 
ATOM   5185 N N    . GLY   B 1 97  ? 39.981 -22.298 4.799   1.00 12.26 ?  97  GLY   B N    1 
ATOM   5186 C CA   . GLY   B 1 97  ? 39.010 -23.358 4.953   1.00 12.74 ?  97  GLY   B CA   1 
ATOM   5187 C C    . GLY   B 1 97  ? 39.126 -23.966 6.333   1.00 13.54 ?  97  GLY   B C    1 
ATOM   5188 O O    . GLY   B 1 97  ? 40.161 -23.837 6.998   1.00 13.92 ?  97  GLY   B O    1 
ATOM   5189 H H    . GLY   B 1 97  ? 40.717 -22.541 4.410   1.00 14.70 ?  97  GLY   B H    1 
ATOM   5190 H HA2  . GLY   B 1 97  ? 38.118 -22.991 4.831   1.00 15.29 ?  97  GLY   B HA2  1 
ATOM   5191 H HA3  . GLY   B 1 97  ? 39.160 -24.041 4.281   1.00 15.29 ?  97  GLY   B HA3  1 
ATOM   5192 N N    . PRO   B 1 98  ? 38.076 -24.653 6.789   1.00 14.25 ?  98  PRO   B N    1 
ATOM   5193 C CA   . PRO   B 1 98  ? 38.165 -25.352 8.075   1.00 15.08 ?  98  PRO   B CA   1 
ATOM   5194 C C    . PRO   B 1 98  ? 39.187 -26.475 8.032   1.00 14.58 ?  98  PRO   B C    1 
ATOM   5195 O O    . PRO   B 1 98  ? 39.288 -27.216 7.053   1.00 15.13 ?  98  PRO   B O    1 
ATOM   5196 C CB   . PRO   B 1 98  ? 36.749 -25.900 8.277   1.00 15.42 ?  98  PRO   B CB   1 
ATOM   5197 C CG   . PRO   B 1 98  ? 36.195 -26.031 6.903   1.00 14.88 ?  98  PRO   B CG   1 
ATOM   5198 C CD   . PRO   B 1 98  ? 36.763 -24.853 6.148   1.00 13.95 ?  98  PRO   B CD   1 
ATOM   5199 H HA   . PRO   B 1 98  ? 38.386 -24.737 8.783   1.00 18.10 ?  98  PRO   B HA   1 
ATOM   5200 H HB2  . PRO   B 1 98  ? 36.791 -26.769 8.712   1.00 18.50 ?  98  PRO   B HB2  1 
ATOM   5201 H HB3  . PRO   B 1 98  ? 36.227 -25.276 8.799   1.00 18.50 ?  98  PRO   B HB3  1 
ATOM   5202 H HG2  . PRO   B 1 98  ? 36.489 -26.869 6.509   1.00 17.85 ?  98  PRO   B HG2  1 
ATOM   5203 H HG3  . PRO   B 1 98  ? 35.228 -25.988 6.935   1.00 17.85 ?  98  PRO   B HG3  1 
ATOM   5204 H HD2  . PRO   B 1 98  ? 36.866 -25.075 5.204   1.00 16.74 ?  98  PRO   B HD2  1 
ATOM   5205 H HD3  . PRO   B 1 98  ? 36.205 -24.071 6.268   1.00 16.74 ?  98  PRO   B HD3  1 
ATOM   5206 N N    . ASN   B 1 99  ? 39.934 -26.605 9.118   1.00 15.59 ?  99  ASN   B N    1 
ATOM   5207 C CA   . ASN   B 1 99  ? 40.911 -27.677 9.282   1.00 16.51 ?  99  ASN   B CA   1 
ATOM   5208 C C    . ASN   B 1 99  ? 40.274 -28.760 10.152  1.00 18.48 ?  99  ASN   B C    1 
ATOM   5209 O O    . ASN   B 1 99  ? 40.180 -28.615 11.373  1.00 19.27 ?  99  ASN   B O    1 
ATOM   5210 C CB   . ASN   B 1 99  ? 42.179 -27.118 9.912   1.00 16.95 ?  99  ASN   B CB   1 
ATOM   5211 C CG   . ASN   B 1 99  ? 43.314 -28.119 9.918   1.00 17.82 ?  99  ASN   B CG   1 
ATOM   5212 O OD1  . ASN   B 1 99  ? 43.095 -29.316 10.069  1.00 18.77 ?  99  ASN   B OD1  1 
ATOM   5213 N ND2  . ASN   B 1 99  ? 44.534 -27.633 9.746   1.00 18.12 ?  99  ASN   B ND2  1 
ATOM   5214 H H    . ASN   B 1 99  ? 39.891 -26.076 9.789   1.00 18.71 ?  99  ASN   B H    1 
ATOM   5215 H HA   . ASN   B 1 99  ? 41.128 -28.066 8.420   1.00 19.81 ?  99  ASN   B HA   1 
ATOM   5216 H HB2  . ASN   B 1 99  ? 42.461 -26.344 9.413   1.00 20.34 ?  99  ASN   B HB2  1 
ATOM   5217 H HB3  . ASN   B 1 99  ? 41.986 -26.876 10.834  1.00 20.34 ?  99  ASN   B HB3  1 
ATOM   5218 H HD21 . ASN   B 1 99  ? 45.211 -28.161 9.740   1.00 21.75 ?  99  ASN   B HD21 1 
ATOM   5219 H HD22 . ASN   B 1 99  ? 44.643 -26.787 9.644   1.00 21.75 ?  99  ASN   B HD22 1 
ATOM   5220 N N    A VAL   B 1 100 ? 39.819 -29.841 9.513   0.84 20.17 ?  100 VAL   B N    1 
ATOM   5221 N N    B VAL   B 1 100 ? 39.826 -29.845 9.514   0.16 20.46 ?  100 VAL   B N    1 
ATOM   5222 C CA   A VAL   B 1 100 ? 39.196 -30.938 10.252  0.84 22.89 ?  100 VAL   B CA   1 
ATOM   5223 C CA   B VAL   B 1 100 ? 39.201 -30.943 10.249  0.16 22.52 ?  100 VAL   B CA   1 
ATOM   5224 C C    A VAL   B 1 100 ? 40.194 -31.603 11.192  0.84 23.35 ?  100 VAL   B C    1 
ATOM   5225 C C    B VAL   B 1 100 ? 40.196 -31.598 11.196  0.16 23.22 ?  100 VAL   B C    1 
ATOM   5226 O O    A VAL   B 1 100 ? 39.813 -32.109 12.254  0.84 24.05 ?  100 VAL   B O    1 
ATOM   5227 O O    B VAL   B 1 100 ? 39.818 -32.080 12.270  0.16 23.49 ?  100 VAL   B O    1 
ATOM   5228 C CB   A VAL   B 1 100 ? 38.550 -31.945 9.278   0.84 25.65 ?  100 VAL   B CB   1 
ATOM   5229 C CB   B VAL   B 1 100 ? 38.571 -31.958 9.272   0.16 23.83 ?  100 VAL   B CB   1 
ATOM   5230 C CG1  A VAL   B 1 100 ? 38.080 -33.190 10.018  0.84 26.60 ?  100 VAL   B CG1  1 
ATOM   5231 C CG1  B VAL   B 1 100 ? 38.045 -33.178 10.020  0.16 24.37 ?  100 VAL   B CG1  1 
ATOM   5232 C CG2  A VAL   B 1 100 ? 37.387 -31.297 8.539   0.84 26.29 ?  100 VAL   B CG2  1 
ATOM   5233 C CG2  B VAL   B 1 100 ? 37.455 -31.299 8.478   0.16 24.07 ?  100 VAL   B CG2  1 
ATOM   5234 H H    A VAL   B 1 100 ? 39.846 -29.958 8.660   0.84 24.20 ?  100 VAL   B H    1 
ATOM   5235 H H    B VAL   B 1 100 ? 39.868 -29.966 8.665   0.16 24.55 ?  100 VAL   B H    1 
ATOM   5236 H HA   A VAL   B 1 100 ? 38.480 -30.574 10.796  0.84 27.46 ?  100 VAL   B HA   1 
ATOM   5237 H HA   B VAL   B 1 100 ? 38.481 -30.584 10.789  0.16 27.02 ?  100 VAL   B HA   1 
ATOM   5238 H HB   A VAL   B 1 100 ? 39.207 -32.220 8.623   0.84 30.77 ?  100 VAL   B HB   1 
ATOM   5239 H HB   B VAL   B 1 100 ? 39.247 -32.262 8.647   0.16 28.59 ?  100 VAL   B HB   1 
ATOM   5240 H HG11 A VAL   B 1 100 ? 37.487 -33.696 9.438   0.84 31.91 ?  100 VAL   B HG11 1 
ATOM   5241 H HG11 B VAL   B 1 100 ? 37.470 -33.688 9.425   0.16 29.25 ?  100 VAL   B HG11 1 
ATOM   5242 H HG12 A VAL   B 1 100 ? 38.849 -33.733 10.253  0.84 31.91 ?  100 VAL   B HG12 1 
ATOM   5243 H HG12 B VAL   B 1 100 ? 38.793 -33.728 10.303  0.16 29.25 ?  100 VAL   B HG12 1 
ATOM   5244 H HG13 A VAL   B 1 100 ? 37.604 -32.923 10.820  0.84 31.91 ?  100 VAL   B HG13 1 
ATOM   5245 H HG13 B VAL   B 1 100 ? 37.538 -32.883 10.791  0.16 29.25 ?  100 VAL   B HG13 1 
ATOM   5246 H HG21 A VAL   B 1 100 ? 36.998 -31.948 7.931   0.84 31.55 ?  100 VAL   B HG21 1 
ATOM   5247 H HG21 B VAL   B 1 100 ? 37.056 -31.956 7.887   0.16 28.88 ?  100 VAL   B HG21 1 
ATOM   5248 H HG22 A VAL   B 1 100 ? 36.720 -31.012 9.185   0.84 31.55 ?  100 VAL   B HG22 1 
ATOM   5249 H HG22 B VAL   B 1 100 ? 36.787 -30.960 9.096   0.16 28.88 ?  100 VAL   B HG22 1 
ATOM   5250 H HG23 A VAL   B 1 100 ? 37.715 -30.535 8.041   0.84 31.55 ?  100 VAL   B HG23 1 
ATOM   5251 H HG23 B VAL   B 1 100 ? 37.827 -30.569 7.960   0.16 28.88 ?  100 VAL   B HG23 1 
ATOM   5252 N N    . ASN   B 1 101 ? 41.477 -31.631 10.821  1.00 23.59 ?  101 ASN   B N    1 
ATOM   5253 C CA   . ASN   B 1 101 ? 42.506 -32.169 11.709  1.00 25.91 ?  101 ASN   B CA   1 
ATOM   5254 C C    . ASN   B 1 101 ? 42.693 -31.332 12.968  1.00 27.99 ?  101 ASN   B C    1 
ATOM   5255 O O    . ASN   B 1 101 ? 43.344 -31.800 13.911  1.00 29.26 ?  101 ASN   B O    1 
ATOM   5256 C CB   . ASN   B 1 101 ? 43.839 -32.303 10.968  1.00 25.90 ?  101 ASN   B CB   1 
ATOM   5257 C CG   . ASN   B 1 101 ? 43.834 -33.438 9.966   1.00 25.74 ?  101 ASN   B CG   1 
ATOM   5258 O OD1  . ASN   B 1 101 ? 43.165 -34.445 10.167  1.00 26.72 ?  101 ASN   B OD1  1 
ATOM   5259 N ND2  . ASN   B 1 101 ? 44.578 -33.277 8.879   1.00 25.42 ?  101 ASN   B ND2  1 
ATOM   5260 H H    A ASN   B 1 101 ? 41.767 -31.360 10.058  0.84 28.31 ?  101 ASN   B H    1 
ATOM   5261 H H    B ASN   B 1 101 ? 41.768 -31.354 10.060  0.16 28.31 ?  101 ASN   B H    1 
ATOM   5262 H HA   . ASN   B 1 101 ? 42.236 -33.054 11.987  1.00 31.09 ?  101 ASN   B HA   1 
ATOM   5263 H HB2  . ASN   B 1 101 ? 44.026 -31.483 10.487  1.00 31.08 ?  101 ASN   B HB2  1 
ATOM   5264 H HB3  . ASN   B 1 101 ? 44.542 -32.475 11.614  1.00 31.08 ?  101 ASN   B HB3  1 
ATOM   5265 H HD21 . ASN   B 1 101 ? 44.607 -33.895 8.281   1.00 30.50 ?  101 ASN   B HD21 1 
ATOM   5266 H HD22 . ASN   B 1 101 ? 45.027 -32.552 8.770   1.00 30.50 ?  101 ASN   B HD22 1 
ATOM   5267 N N    . LYS   B 1 102 ? 42.149 -30.113 12.998  1.00 30.22 ?  102 LYS   B N    1 
ATOM   5268 C CA   . LYS   B 1 102 ? 42.131 -29.272 14.189  1.00 33.15 ?  102 LYS   B CA   1 
ATOM   5269 C C    . LYS   B 1 102 ? 40.753 -29.216 14.835  1.00 32.40 ?  102 LYS   B C    1 
ATOM   5270 O O    . LYS   B 1 102 ? 40.538 -28.408 15.744  1.00 32.99 ?  102 LYS   B O    1 
ATOM   5271 C CB   . LYS   B 1 102 ? 42.577 -27.849 13.846  1.00 36.62 ?  102 LYS   B CB   1 
ATOM   5272 C CG   . LYS   B 1 102 ? 44.041 -27.701 13.477  1.00 40.13 ?  102 LYS   B CG   1 
ATOM   5273 C CD   . LYS   B 1 102 ? 44.327 -26.273 13.034  1.00 43.03 ?  102 LYS   B CD   1 
ATOM   5274 C CE   . LYS   B 1 102 ? 45.811 -26.013 12.851  1.00 45.38 ?  102 LYS   B CE   1 
ATOM   5275 N NZ   . LYS   B 1 102 ? 46.065 -24.606 12.424  1.00 46.75 ?  102 LYS   B NZ   1 
ATOM   5276 H H    . LYS   B 1 102 ? 41.768 -29.743 12.321  1.00 36.26 ?  102 LYS   B H    1 
ATOM   5277 H HA   . LYS   B 1 102 ? 42.757 -29.631 14.836  1.00 39.78 ?  102 LYS   B HA   1 
ATOM   5278 H HB2  . LYS   B 1 102 ? 42.051 -27.535 13.095  1.00 43.94 ?  102 LYS   B HB2  1 
ATOM   5279 H HB3  . LYS   B 1 102 ? 42.412 -27.281 14.617  1.00 43.94 ?  102 LYS   B HB3  1 
ATOM   5280 H HG2  . LYS   B 1 102 ? 44.594 -27.900 14.249  1.00 48.16 ?  102 LYS   B HG2  1 
ATOM   5281 H HG3  . LYS   B 1 102 ? 44.253 -28.300 12.744  1.00 48.16 ?  102 LYS   B HG3  1 
ATOM   5282 H HD2  . LYS   B 1 102 ? 43.884 -26.110 12.186  1.00 51.63 ?  102 LYS   B HD2  1 
ATOM   5283 H HD3  . LYS   B 1 102 ? 43.993 -25.659 13.707  1.00 51.63 ?  102 LYS   B HD3  1 
ATOM   5284 H HE2  . LYS   B 1 102 ? 46.270 -26.163 13.693  1.00 54.46 ?  102 LYS   B HE2  1 
ATOM   5285 H HE3  . LYS   B 1 102 ? 46.160 -26.606 12.167  1.00 54.46 ?  102 LYS   B HE3  1 
ATOM   5286 H HZ1  . LYS   B 1 102 ? 46.938 -24.471 12.322  1.00 56.09 ?  102 LYS   B HZ1  1 
ATOM   5287 H HZ2  . LYS   B 1 102 ? 45.654 -24.445 11.651  1.00 56.09 ?  102 LYS   B HZ2  1 
ATOM   5288 H HZ3  . LYS   B 1 102 ? 45.754 -24.042 13.039  1.00 56.09 ?  102 LYS   B HZ3  1 
ATOM   5289 N N    . GLY   B 1 103 ? 39.809 -30.033 14.373  1.00 31.29 ?  103 GLY   B N    1 
ATOM   5290 C CA   . GLY   B 1 103 ? 38.480 -30.065 14.948  1.00 30.62 ?  103 GLY   B CA   1 
ATOM   5291 C C    . GLY   B 1 103 ? 37.549 -28.968 14.487  1.00 29.26 ?  103 GLY   B C    1 
ATOM   5292 O O    . GLY   B 1 103 ? 36.469 -28.812 15.067  1.00 29.71 ?  103 GLY   B O    1 
ATOM   5293 H H    . GLY   B 1 103 ? 39.918 -30.579 13.720  1.00 37.54 ?  103 GLY   B H    1 
ATOM   5294 H HA2  . GLY   B 1 103 ? 38.064 -30.914 14.731  1.00 36.74 ?  103 GLY   B HA2  1 
ATOM   5295 H HA3  . GLY   B 1 103 ? 38.552 -30.008 15.915  1.00 36.74 ?  103 GLY   B HA3  1 
ATOM   5296 N N    A GLU   B 1 104 ? 37.925 -28.210 13.460  0.84 27.39 ?  104 GLU   B N    1 
ATOM   5297 N N    B GLU   B 1 104 ? 37.925 -28.203 13.468  0.16 28.98 ?  104 GLU   B N    1 
ATOM   5298 C CA   A GLU   B 1 104 ? 37.092 -27.118 12.983  0.84 25.75 ?  104 GLU   B CA   1 
ATOM   5299 C CA   B GLU   B 1 104 ? 37.089 -27.107 13.004  0.16 28.58 ?  104 GLU   B CA   1 
ATOM   5300 C C    A GLU   B 1 104 ? 35.925 -27.653 12.159  0.84 26.38 ?  104 GLU   B C    1 
ATOM   5301 C C    B GLU   B 1 104 ? 35.927 -27.636 12.168  0.16 28.74 ?  104 GLU   B C    1 
ATOM   5302 O O    A GLU   B 1 104 ? 35.987 -28.742 11.581  0.84 27.12 ?  104 GLU   B O    1 
ATOM   5303 O O    B GLU   B 1 104 ? 36.018 -28.687 11.527  0.16 28.91 ?  104 GLU   B O    1 
ATOM   5304 C CB   A GLU   B 1 104 ? 37.935 -26.123 12.182  0.84 24.32 ?  104 GLU   B CB   1 
ATOM   5305 C CB   B GLU   B 1 104 ? 37.925 -26.111 12.202  0.16 27.95 ?  104 GLU   B CB   1 
ATOM   5306 C CG   A GLU   B 1 104 ? 39.042 -25.509 13.028  0.84 23.11 ?  104 GLU   B CG   1 
ATOM   5307 C CG   B GLU   B 1 104 ? 39.034 -25.473 13.029  0.16 27.32 ?  104 GLU   B CG   1 
ATOM   5308 C CD   A GLU   B 1 104 ? 39.986 -24.610 12.254  0.84 21.57 ?  104 GLU   B CD   1 
ATOM   5309 C CD   B GLU   B 1 104 ? 39.953 -24.591 12.207  0.16 26.70 ?  104 GLU   B CD   1 
ATOM   5310 O OE1  A GLU   B 1 104 ? 39.988 -24.638 11.004  0.84 19.50 ?  104 GLU   B OE1  1 
ATOM   5311 O OE1  B GLU   B 1 104 ? 39.859 -24.620 10.962  0.16 26.34 ?  104 GLU   B OE1  1 
ATOM   5312 O OE2  A GLU   B 1 104 ? 40.738 -23.871 12.919  0.84 22.41 -1 104 GLU   B OE2  1 
ATOM   5313 O OE2  B GLU   B 1 104 ? 40.773 -23.867 12.811  0.16 26.64 -1 104 GLU   B OE2  1 
ATOM   5314 H H    A GLU   B 1 104 ? 38.663 -28.306 13.028  0.84 32.87 ?  104 GLU   B H    1 
ATOM   5315 H H    B GLU   B 1 104 ? 38.661 -28.296 13.034  0.16 34.78 ?  104 GLU   B H    1 
ATOM   5316 H HA   A GLU   B 1 104 ? 36.727 -26.647 13.746  0.84 30.90 ?  104 GLU   B HA   1 
ATOM   5317 H HA   B GLU   B 1 104 ? 36.722 -26.642 13.771  0.16 34.29 ?  104 GLU   B HA   1 
ATOM   5318 H HB2  A GLU   B 1 104 ? 38.346 -26.580 11.432  0.84 29.18 ?  104 GLU   B HB2  1 
ATOM   5319 H HB2  B GLU   B 1 104 ? 38.336 -26.571 11.454  0.16 33.54 ?  104 GLU   B HB2  1 
ATOM   5320 H HB3  A GLU   B 1 104 ? 37.365 -25.404 11.864  0.84 29.18 ?  104 GLU   B HB3  1 
ATOM   5321 H HB3  B GLU   B 1 104 ? 37.347 -25.401 11.879  0.16 33.54 ?  104 GLU   B HB3  1 
ATOM   5322 H HG2  A GLU   B 1 104 ? 38.644 -24.973 13.732  0.84 27.74 ?  104 GLU   B HG2  1 
ATOM   5323 H HG2  B GLU   B 1 104 ? 38.635 -24.925 13.724  0.16 32.78 ?  104 GLU   B HG2  1 
ATOM   5324 H HG3  A GLU   B 1 104 ? 39.573 -26.219 13.422  0.84 27.74 ?  104 GLU   B HG3  1 
ATOM   5325 H HG3  B GLU   B 1 104 ? 39.571 -26.174 13.433  0.16 32.78 ?  104 GLU   B HG3  1 
ATOM   5326 N N    A ASP   B 1 105 ? 34.849 -26.870 12.120  0.84 26.61 ?  105 ASP   B N    1 
ATOM   5327 N N    B ASP   B 1 105 ? 34.825 -26.889 12.185  0.16 28.79 ?  105 ASP   B N    1 
ATOM   5328 C CA   A ASP   B 1 105 ? 33.573 -27.332 11.588  0.84 27.52 ?  105 ASP   B CA   1 
ATOM   5329 C CA   B ASP   B 1 105 ? 33.574 -27.359 11.604  0.16 28.70 ?  105 ASP   B CA   1 
ATOM   5330 C C    A ASP   B 1 105 ? 33.626 -27.371 10.065  0.84 25.72 ?  105 ASP   B C    1 
ATOM   5331 C C    B ASP   B 1 105 ? 33.671 -27.385 10.081  0.16 27.33 ?  105 ASP   B C    1 
ATOM   5332 O O    A ASP   B 1 105 ? 33.776 -26.330 9.414   0.84 24.62 ?  105 ASP   B O    1 
ATOM   5333 O O    B ASP   B 1 105 ? 33.903 -26.351 9.446   0.16 27.36 ?  105 ASP   B O    1 
ATOM   5334 C CB   A ASP   B 1 105 ? 32.452 -26.408 12.065  0.84 30.35 ?  105 ASP   B CB   1 
ATOM   5335 C CB   B ASP   B 1 105 ? 32.430 -26.453 12.054  0.16 29.93 ?  105 ASP   B CB   1 
ATOM   5336 C CG   A ASP   B 1 105 ? 31.078 -26.886 11.635  0.84 32.66 ?  105 ASP   B CG   1 
ATOM   5337 C CG   B ASP   B 1 105 ? 31.066 -27.020 11.706  0.16 30.84 ?  105 ASP   B CG   1 
ATOM   5338 O OD1  A ASP   B 1 105 ? 30.988 -27.957 10.999  0.84 32.84 ?  105 ASP   B OD1  1 
ATOM   5339 O OD1  B ASP   B 1 105 ? 31.011 -28.072 11.035  0.16 31.03 ?  105 ASP   B OD1  1 
ATOM   5340 O OD2  A ASP   B 1 105 ? 30.084 -26.190 11.937  0.84 34.19 -1 105 ASP   B OD2  1 
ATOM   5341 O OD2  B ASP   B 1 105 ? 30.049 -26.417 12.108  0.16 31.32 -1 105 ASP   B OD2  1 
ATOM   5342 H H    A ASP   B 1 105 ? 34.836 -26.055 12.390  0.84 31.92 ?  105 ASP   B H    1 
ATOM   5343 H H    B ASP   B 1 105 ? 34.777 -26.102 12.528  0.16 34.54 ?  105 ASP   B H    1 
ATOM   5344 H HA   A ASP   B 1 105 ? 33.389 -28.228 11.913  0.84 33.02 ?  105 ASP   B HA   1 
ATOM   5345 H HA   B ASP   B 1 105 ? 33.387 -28.260 11.915  0.16 34.44 ?  105 ASP   B HA   1 
ATOM   5346 H HB2  A ASP   B 1 105 ? 32.474 -26.360 13.037  0.84 36.42 ?  105 ASP   B HB2  1 
ATOM   5347 H HB2  B ASP   B 1 105 ? 32.473 -26.341 13.019  0.16 35.91 ?  105 ASP   B HB2  1 
ATOM   5348 H HB3  A ASP   B 1 105 ? 32.588 -25.524 11.690  0.84 36.42 ?  105 ASP   B HB3  1 
ATOM   5349 H HB3  B ASP   B 1 105 ? 32.518 -25.590 11.619  0.16 35.91 ?  105 ASP   B HB3  1 
ATOM   5350 N N    . ILE   B 1 106 ? 33.489 -28.574 9.499   1.00 25.85 ?  106 ILE   B N    1 
ATOM   5351 C CA   . ILE   B 1 106 ? 33.491 -28.734 8.048   1.00 24.35 ?  106 ILE   B CA   1 
ATOM   5352 C C    . ILE   B 1 106 ? 32.395 -27.908 7.376   1.00 22.75 ?  106 ILE   B C    1 
ATOM   5353 O O    . ILE   B 1 106 ? 32.496 -27.592 6.186   1.00 21.42 ?  106 ILE   B O    1 
ATOM   5354 C CB   . ILE   B 1 106 ? 33.399 -30.241 7.704   1.00 24.95 ?  106 ILE   B CB   1 
ATOM   5355 C CG1  . ILE   B 1 106 ? 33.641 -30.487 6.215   1.00 25.43 ?  106 ILE   B CG1  1 
ATOM   5356 C CG2  . ILE   B 1 106 ? 32.050 -30.812 8.126   1.00 25.90 ?  106 ILE   B CG2  1 
ATOM   5357 C CD1  . ILE   B 1 106 ? 34.998 -30.036 5.748   1.00 25.71 ?  106 ILE   B CD1  1 
ATOM   5358 H H    A ILE   B 1 106 ? 33.405 -29.310 9.936   0.84 31.02 ?  106 ILE   B H    1 
ATOM   5359 H H    B ILE   B 1 106 ? 33.369 -29.308 9.931   0.16 31.02 ?  106 ILE   B H    1 
ATOM   5360 H HA   . ILE   B 1 106 ? 34.340 -28.412 7.715   1.00 29.22 ?  106 ILE   B HA   1 
ATOM   5361 H HB   . ILE   B 1 106 ? 34.088 -30.709 8.202   1.00 29.93 ?  106 ILE   B HB   1 
ATOM   5362 H HG12 . ILE   B 1 106 ? 33.573 -31.441 6.040   1.00 30.51 ?  106 ILE   B HG12 1 
ATOM   5363 H HG13 . ILE   B 1 106 ? 32.974 -30.011 5.702   1.00 30.51 ?  106 ILE   B HG13 1 
ATOM   5364 H HG21 . ILE   B 1 106 ? 32.062 -31.775 7.999   1.00 31.08 ?  106 ILE   B HG21 1 
ATOM   5365 H HG22 . ILE   B 1 106 ? 31.899 -30.607 9.062   1.00 31.08 ?  106 ILE   B HG22 1 
ATOM   5366 H HG23 . ILE   B 1 106 ? 31.353 -30.417 7.583   1.00 31.08 ?  106 ILE   B HG23 1 
ATOM   5367 H HD11 . ILE   B 1 106 ? 35.181 -30.429 4.881   1.00 30.85 ?  106 ILE   B HD11 1 
ATOM   5368 H HD12 . ILE   B 1 106 ? 35.004 -29.068 5.679   1.00 30.85 ?  106 ILE   B HD12 1 
ATOM   5369 H HD13 . ILE   B 1 106 ? 35.668 -30.326 6.389   1.00 30.85 ?  106 ILE   B HD13 1 
ATOM   5370 N N    A GLN   B 1 107 ? 31.341 -27.553 8.115   0.84 23.46 ?  107 GLN   B N    1 
ATOM   5371 N N    B GLN   B 1 107 ? 31.351 -27.534 8.118   0.16 23.44 ?  107 GLN   B N    1 
ATOM   5372 C CA   A GLN   B 1 107 ? 30.268 -26.744 7.547   0.84 24.02 ?  107 GLN   B CA   1 
ATOM   5373 C CA   B GLN   B 1 107 ? 30.271 -26.736 7.545   0.16 23.95 ?  107 GLN   B CA   1 
ATOM   5374 C C    A GLN   B 1 107 ? 30.761 -25.391 7.043   0.84 22.05 ?  107 GLN   B C    1 
ATOM   5375 C C    B GLN   B 1 107 ? 30.752 -25.375 7.058   0.16 21.97 ?  107 GLN   B C    1 
ATOM   5376 O O    A GLN   B 1 107 ? 30.126 -24.806 6.161   0.84 22.95 ?  107 GLN   B O    1 
ATOM   5377 O O    B GLN   B 1 107 ? 30.086 -24.761 6.217   0.16 22.23 ?  107 GLN   B O    1 
ATOM   5378 C CB   A GLN   B 1 107 ? 29.164 -26.551 8.591   0.84 27.78 ?  107 GLN   B CB   1 
ATOM   5379 C CB   B GLN   B 1 107 ? 29.155 -26.562 8.578   0.16 26.41 ?  107 GLN   B CB   1 
ATOM   5380 C CG   A GLN   B 1 107 ? 27.834 -26.056 8.033   0.84 31.66 ?  107 GLN   B CG   1 
ATOM   5381 C CG   B GLN   B 1 107 ? 27.830 -26.060 8.014   0.16 28.70 ?  107 GLN   B CG   1 
ATOM   5382 C CD   A GLN   B 1 107 ? 27.757 -24.542 7.932   0.84 34.54 ?  107 GLN   B CD   1 
ATOM   5383 C CD   B GLN   B 1 107 ? 27.724 -24.545 8.000   0.16 30.46 ?  107 GLN   B CD   1 
ATOM   5384 O OE1  A GLN   B 1 107 ? 28.599 -23.826 8.479   0.84 35.77 ?  107 GLN   B OE1  1 
ATOM   5385 O OE1  B GLN   B 1 107 ? 28.555 -23.846 8.581   0.16 31.24 ?  107 GLN   B OE1  1 
ATOM   5386 N NE2  A GLN   B 1 107 ? 26.739 -24.046 7.232   0.84 35.57 ?  107 GLN   B NE2  1 
ATOM   5387 N NE2  B GLN   B 1 107 ? 26.693 -24.032 7.336   0.16 30.98 ?  107 GLN   B NE2  1 
ATOM   5388 H H    A GLN   B 1 107 ? 31.227 -27.772 8.936   0.84 28.15 ?  107 GLN   B H    1 
ATOM   5389 H H    B GLN   B 1 107 ? 31.246 -27.729 8.943   0.16 28.13 ?  107 GLN   B H    1 
ATOM   5390 H HA   A GLN   B 1 107 ? 29.885 -27.224 6.792   0.84 28.83 ?  107 GLN   B HA   1 
ATOM   5391 H HA   B GLN   B 1 107 ? 29.902 -27.210 6.784   0.16 28.74 ?  107 GLN   B HA   1 
ATOM   5392 H HB2  A GLN   B 1 107 ? 28.998 -27.401 9.025   0.84 33.33 ?  107 GLN   B HB2  1 
ATOM   5393 H HB2  B GLN   B 1 107 ? 28.987 -27.420 8.992   0.16 31.69 ?  107 GLN   B HB2  1 
ATOM   5394 H HB3  A GLN   B 1 107 ? 29.469 -25.905 9.246   0.84 33.33 ?  107 GLN   B HB3  1 
ATOM   5395 H HB3  B GLN   B 1 107 ? 29.451 -25.929 9.250   0.16 31.69 ?  107 GLN   B HB3  1 
ATOM   5396 H HG2  A GLN   B 1 107 ? 27.706 -26.419 7.144   0.84 37.99 ?  107 GLN   B HG2  1 
ATOM   5397 H HG2  B GLN   B 1 107 ? 27.734 -26.373 7.102   0.16 34.43 ?  107 GLN   B HG2  1 
ATOM   5398 H HG3  A GLN   B 1 107 ? 27.117 -26.357 8.618   0.84 37.99 ?  107 GLN   B HG3  1 
ATOM   5399 H HG3  B GLN   B 1 107 ? 27.105 -26.407 8.560   0.16 34.43 ?  107 GLN   B HG3  1 
ATOM   5400 H HE21 A GLN   B 1 107 ? 26.170 -24.577 6.863   0.84 42.68 ?  107 GLN   B HE21 1 
ATOM   5401 H HE21 B GLN   B 1 107 ? 26.133 -24.552 6.941   0.16 37.17 ?  107 GLN   B HE21 1 
ATOM   5402 H HE22 A GLN   B 1 107 ? 26.646 -23.194 7.148   0.84 42.68 ?  107 GLN   B HE22 1 
ATOM   5403 H HE22 B GLN   B 1 107 ? 26.586 -23.179 7.301   0.16 37.17 ?  107 GLN   B HE22 1 
ATOM   5404 N N    . LEU   B 1 108 ? 31.887 -24.891 7.560   1.00 19.86 ?  108 LEU   B N    1 
ATOM   5405 C CA   . LEU   B 1 108 ? 32.427 -23.593 7.150   1.00 17.86 ?  108 LEU   B CA   1 
ATOM   5406 C C    . LEU   B 1 108 ? 33.080 -23.616 5.777   1.00 16.01 ?  108 LEU   B C    1 
ATOM   5407 O O    . LEU   B 1 108 ? 33.516 -22.559 5.293   1.00 15.72 ?  108 LEU   B O    1 
ATOM   5408 C CB   . LEU   B 1 108 ? 33.431 -23.099 8.188   1.00 18.44 ?  108 LEU   B CB   1 
ATOM   5409 C CG   . LEU   B 1 108 ? 32.805 -22.615 9.493   1.00 19.71 ?  108 LEU   B CG   1 
ATOM   5410 C CD1  . LEU   B 1 108 ? 33.830 -22.579 10.614  1.00 20.17 ?  108 LEU   B CD1  1 
ATOM   5411 C CD2  . LEU   B 1 108 ? 32.206 -21.236 9.283   1.00 20.61 ?  108 LEU   B CD2  1 
ATOM   5412 H H    A LEU   B 1 108 ? 32.355 -25.289 8.157   0.84 23.83 ?  108 LEU   B H    1 
ATOM   5413 H H    B LEU   B 1 108 ? 32.361 -25.297 8.148   0.16 23.83 ?  108 LEU   B H    1 
ATOM   5414 H HA   . LEU   B 1 108 ? 31.697 -22.960 7.116   1.00 21.43 ?  108 LEU   B HA   1 
ATOM   5415 H HB2  . LEU   B 1 108 ? 34.035 -23.825 8.405   1.00 22.13 ?  108 LEU   B HB2  1 
ATOM   5416 H HB3  . LEU   B 1 108 ? 33.926 -22.360 7.807   1.00 22.13 ?  108 LEU   B HB3  1 
ATOM   5417 H HG   . LEU   B 1 108 ? 32.090 -23.220 9.753   1.00 23.65 ?  108 LEU   B HG   1 
ATOM   5418 H HD11 . LEU   B 1 108 ? 33.396 -22.282 11.431  1.00 24.20 ?  108 LEU   B HD11 1 
ATOM   5419 H HD12 . LEU   B 1 108 ? 34.195 -23.468 10.739  1.00 24.20 ?  108 LEU   B HD12 1 
ATOM   5420 H HD13 . LEU   B 1 108 ? 34.538 -21.961 10.375  1.00 24.20 ?  108 LEU   B HD13 1 
ATOM   5421 H HD21 . LEU   B 1 108 ? 31.854 -20.914 10.126  1.00 24.73 ?  108 LEU   B HD21 1 
ATOM   5422 H HD22 . LEU   B 1 108 ? 32.899 -20.638 8.962   1.00 24.73 ?  108 LEU   B HD22 1 
ATOM   5423 H HD23 . LEU   B 1 108 ? 31.493 -21.297 8.628   1.00 24.73 ?  108 LEU   B HD23 1 
ATOM   5424 N N    . LEU   B 1 109 ? 33.144 -24.781 5.139   1.00 15.21 ?  109 LEU   B N    1 
ATOM   5425 C CA   . LEU   B 1 109 ? 33.777 -24.885 3.835   1.00 14.18 ?  109 LEU   B CA   1 
ATOM   5426 C C    . LEU   B 1 109 ? 33.014 -24.096 2.776   1.00 13.72 ?  109 LEU   B C    1 
ATOM   5427 O O    . LEU   B 1 109 ? 33.630 -23.502 1.884   1.00 13.39 ?  109 LEU   B O    1 
ATOM   5428 C CB   . LEU   B 1 109 ? 33.903 -26.357 3.454   1.00 14.39 ?  109 LEU   B CB   1 
ATOM   5429 C CG   . LEU   B 1 109 ? 34.685 -26.695 2.189   1.00 14.06 ?  109 LEU   B CG   1 
ATOM   5430 C CD1  . LEU   B 1 109 ? 36.060 -26.042 2.190   1.00 14.25 ?  109 LEU   B CD1  1 
ATOM   5431 C CD2  . LEU   B 1 109 ? 34.800 -28.207 2.058   1.00 14.73 ?  109 LEU   B CD2  1 
ATOM   5432 H H    . LEU   B 1 109 ? 32.831 -25.524 5.434   1.00 18.25 ?  109 LEU   B H    1 
ATOM   5433 H HA   . LEU   B 1 109 ? 34.670 -24.516 3.884   1.00 17.01 ?  109 LEU   B HA   1 
ATOM   5434 H HB2  . LEU   B 1 109 ? 34.341 -26.822 4.184   1.00 17.27 ?  109 LEU   B HB2  1 
ATOM   5435 H HB3  . LEU   B 1 109 ? 33.010 -26.722 3.339   1.00 17.27 ?  109 LEU   B HB3  1 
ATOM   5436 H HG   . LEU   B 1 109 ? 34.194 -26.376 1.414   1.00 16.87 ?  109 LEU   B HG   1 
ATOM   5437 H HD11 . LEU   B 1 109 ? 36.582 -26.402 1.455   1.00 17.09 ?  109 LEU   B HD11 1 
ATOM   5438 H HD12 . LEU   B 1 109 ? 35.951 -25.087 2.083   1.00 17.09 ?  109 LEU   B HD12 1 
ATOM   5439 H HD13 . LEU   B 1 109 ? 36.498 -26.239 3.033   1.00 17.09 ?  109 LEU   B HD13 1 
ATOM   5440 H HD21 . LEU   B 1 109 ? 35.368 -28.419 1.298   1.00 17.67 ?  109 LEU   B HD21 1 
ATOM   5441 H HD22 . LEU   B 1 109 ? 35.188 -28.568 2.869   1.00 17.67 ?  109 LEU   B HD22 1 
ATOM   5442 H HD23 . LEU   B 1 109 ? 33.915 -28.586 1.919   1.00 17.67 ?  109 LEU   B HD23 1 
ATOM   5443 N N    . LYS   B 1 110 ? 31.678 -24.063 2.854   1.00 13.50 ?  110 LYS   B N    1 
ATOM   5444 C CA   . LYS   B 1 110 ? 30.922 -23.300 1.863   1.00 13.13 ?  110 LYS   B CA   1 
ATOM   5445 C C    . LYS   B 1 110 ? 31.257 -21.812 1.955   1.00 12.89 ?  110 LYS   B C    1 
ATOM   5446 O O    . LYS   B 1 110 ? 31.514 -21.158 0.939   1.00 12.57 ?  110 LYS   B O    1 
ATOM   5447 C CB   . LYS   B 1 110 ? 29.418 -23.550 2.008   1.00 13.87 ?  110 LYS   B CB   1 
ATOM   5448 C CG   . LYS   B 1 110 ? 28.612 -22.922 0.875   1.00 13.94 ?  110 LYS   B CG   1 
ATOM   5449 C CD   . LYS   B 1 110 ? 27.151 -23.365 0.894   1.00 14.55 ?  110 LYS   B CD   1 
ATOM   5450 C CE   . LYS   B 1 110 ? 26.377 -22.840 -0.318  1.00 15.42 ?  110 LYS   B CE   1 
ATOM   5451 N NZ   . LYS   B 1 110 ? 26.717 -23.544 -1.583  1.00 15.58 ?  110 LYS   B NZ   1 
ATOM   5452 H H    . LYS   B 1 110 ? 31.204 -24.471 3.444   1.00 16.20 ?  110 LYS   B H    1 
ATOM   5453 H HA   . LYS   B 1 110 ? 31.181 -23.604 0.977   1.00 15.75 ?  110 LYS   B HA   1 
ATOM   5454 H HB2  . LYS   B 1 110 ? 29.250 -24.510 1.994   1.00 16.64 ?  110 LYS   B HB2  1 
ATOM   5455 H HB3  . LYS   B 1 110 ? 29.109 -23.173 2.843   1.00 16.64 ?  110 LYS   B HB3  1 
ATOM   5456 H HG2  . LYS   B 1 110 ? 28.627 -21.956 0.967   1.00 16.73 ?  110 LYS   B HG2  1 
ATOM   5457 H HG3  . LYS   B 1 110 ? 28.990 -23.183 0.022   1.00 16.73 ?  110 LYS   B HG3  1 
ATOM   5458 H HD2  . LYS   B 1 110 ? 27.111 -24.338 0.880   1.00 17.46 ?  110 LYS   B HD2  1 
ATOM   5459 H HD3  . LYS   B 1 110 ? 26.721 -23.029 1.697   1.00 17.46 ?  110 LYS   B HD3  1 
ATOM   5460 H HE2  . LYS   B 1 110 ? 25.427 -22.954 -0.163  1.00 18.50 ?  110 LYS   B HE2  1 
ATOM   5461 H HE3  . LYS   B 1 110 ? 26.583 -21.901 -0.439  1.00 18.50 ?  110 LYS   B HE3  1 
ATOM   5462 H HZ1  . LYS   B 1 110 ? 26.247 -23.206 -2.257  1.00 18.69 ?  110 LYS   B HZ1  1 
ATOM   5463 H HZ2  . LYS   B 1 110 ? 27.585 -23.452 -1.758  1.00 18.69 ?  110 LYS   B HZ2  1 
ATOM   5464 H HZ3  . LYS   B 1 110 ? 26.531 -24.413 -1.506  1.00 18.69 ?  110 LYS   B HZ3  1 
ATOM   5465 N N    . SER   B 1 111 ? 31.279 -21.267 3.176   1.00 13.19 ?  111 SER   B N    1 
ATOM   5466 C CA   . SER   B 1 111 ? 31.668 -19.869 3.357   1.00 13.08 ?  111 SER   B CA   1 
ATOM   5467 C C    . SER   B 1 111 ? 33.050 -19.607 2.768   1.00 12.57 ?  111 SER   B C    1 
ATOM   5468 O O    . SER   B 1 111 ? 33.281 -18.570 2.128   1.00 13.05 ?  111 SER   B O    1 
ATOM   5469 C CB   . SER   B 1 111 ? 31.663 -19.513 4.843   1.00 14.07 ?  111 SER   B CB   1 
ATOM   5470 O OG   . SER   B 1 111 ? 30.356 -19.504 5.375   1.00 16.11 ?  111 SER   B OG   1 
ATOM   5471 H H    . SER   B 1 111 ? 31.077 -21.686 3.902   1.00 15.83 ?  111 SER   B H    1 
ATOM   5472 H HA   . SER   B 1 111 ? 31.031 -19.300 2.906   1.00 15.69 ?  111 SER   B HA   1 
ATOM   5473 H HB2  . SER   B 1 111 ? 32.188 -20.170 5.329   1.00 16.88 ?  111 SER   B HB2  1 
ATOM   5474 H HB3  . SER   B 1 111 ? 32.046 -18.634 4.958   1.00 16.88 ?  111 SER   B HB3  1 
ATOM   5475 H HG   . SER   B 1 111 ? 30.373 -19.309 6.198   1.00 19.33 ?  111 SER   B HG   1 
ATOM   5476 N N    . ALA   B 1 112 ? 33.989 -20.528 2.989   1.00 12.93 ?  112 ALA   B N    1 
ATOM   5477 C CA   . ALA   B 1 112 ? 35.332 -20.356 2.445   1.00 12.57 ?  112 ALA   B CA   1 
ATOM   5478 C C    . ALA   B 1 112 ? 35.299 -20.253 0.922   1.00 11.80 ?  112 ALA   B C    1 
ATOM   5479 O O    . ALA   B 1 112 ? 35.928 -19.364 0.331   1.00 12.13 ?  112 ALA   B O    1 
ATOM   5480 C CB   . ALA   B 1 112 ? 36.236 -21.502 2.909   1.00 13.15 ?  112 ALA   B CB   1 
ATOM   5481 H H    . ALA   B 1 112 ? 33.875 -21.250 3.456   1.00 15.52 ?  112 ALA   B H    1 
ATOM   5482 H HA   . ALA   B 1 112 ? 35.699 -19.532 2.793   1.00 15.08 ?  112 ALA   B HA   1 
ATOM   5483 H HB1  . ALA   B 1 112 ? 37.127 -21.362 2.543   1.00 15.78 ?  112 ALA   B HB1  1 
ATOM   5484 H HB2  . ALA   B 1 112 ? 36.280 -21.497 3.881   1.00 15.78 ?  112 ALA   B HB2  1 
ATOM   5485 H HB3  . ALA   B 1 112 ? 35.876 -22.342 2.598   1.00 15.78 ?  112 ALA   B HB3  1 
ATOM   5486 N N    . TYR   B 1 113 ? 34.571 -21.158 0.262   1.00 11.72 ?  113 TYR   B N    1 
ATOM   5487 C CA   . TYR   B 1 113 ? 34.498 -21.107 -1.193  1.00 11.77 ?  113 TYR   B CA   1 
ATOM   5488 C C    . TYR   B 1 113 ? 33.790 -19.857 -1.708  1.00 11.46 ?  113 TYR   B C    1 
ATOM   5489 O O    . TYR   B 1 113 ? 34.060 -19.422 -2.831  1.00 11.52 ?  113 TYR   B O    1 
ATOM   5490 C CB   . TYR   B 1 113 ? 33.829 -22.366 -1.744  1.00 11.81 ?  113 TYR   B CB   1 
ATOM   5491 C CG   . TYR   B 1 113 ? 34.788 -23.514 -2.002  1.00 12.08 ?  113 TYR   B CG   1 
ATOM   5492 C CD1  . TYR   B 1 113 ? 35.781 -23.409 -2.971  1.00 12.47 ?  113 TYR   B CD1  1 
ATOM   5493 C CD2  . TYR   B 1 113 ? 34.684 -24.707 -1.304  1.00 12.53 ?  113 TYR   B CD2  1 
ATOM   5494 C CE1  . TYR   B 1 113 ? 36.664 -24.445 -3.219  1.00 12.31 ?  113 TYR   B CE1  1 
ATOM   5495 C CE2  . TYR   B 1 113 ? 35.558 -25.758 -1.550  1.00 12.88 ?  113 TYR   B CE2  1 
ATOM   5496 C CZ   . TYR   B 1 113 ? 36.539 -25.627 -2.516  1.00 12.80 ?  113 TYR   B CZ   1 
ATOM   5497 O OH   . TYR   B 1 113 ? 37.418 -26.653 -2.785  1.00 13.44 ?  113 TYR   B OH   1 
ATOM   5498 H H    . TYR   B 1 113 ? 34.111 -21.789 0.631   1.00 14.07 ?  113 TYR   B H    1 
ATOM   5499 H HA   . TYR   B 1 113 ? 35.398 -21.086 -1.531  1.00 14.13 ?  113 TYR   B HA   1 
ATOM   5500 H HB2  . TYR   B 1 113 ? 33.165 -22.680 -1.107  1.00 14.17 ?  113 TYR   B HB2  1 
ATOM   5501 H HB3  . TYR   B 1 113 ? 33.393 -22.147 -2.584  1.00 14.17 ?  113 TYR   B HB3  1 
ATOM   5502 H HD1  . TYR   B 1 113 ? 35.871 -22.615 -3.454  1.00 14.96 ?  113 TYR   B HD1  1 
ATOM   5503 H HD2  . TYR   B 1 113 ? 34.016 -24.799 -0.667  1.00 15.03 ?  113 TYR   B HD2  1 
ATOM   5504 H HE1  . TYR   B 1 113 ? 37.327 -24.360 -3.876  1.00 14.77 ?  113 TYR   B HE1  1 
ATOM   5505 H HE2  . TYR   B 1 113 ? 35.467 -26.552 -1.081  1.00 15.46 ?  113 TYR   B HE2  1 
ATOM   5506 H HH   . TYR   B 1 113 ? 37.233 -27.317 -2.305  1.00 16.13 ?  113 TYR   B HH   1 
ATOM   5507 N N    . GLU   B 1 114 ? 32.864 -19.284 -0.933  1.00 11.70 ?  114 GLU   B N    1 
ATOM   5508 C CA   . GLU   B 1 114 ? 32.178 -18.075 -1.385  1.00 11.56 ?  114 GLU   B CA   1 
ATOM   5509 C C    . GLU   B 1 114 ? 33.162 -16.952 -1.680  1.00 11.52 ?  114 GLU   B C    1 
ATOM   5510 O O    . GLU   B 1 114 ? 32.886 -16.096 -2.522  1.00 11.70 ?  114 GLU   B O    1 
ATOM   5511 C CB   . GLU   B 1 114 ? 31.119 -17.651 -0.367  1.00 12.15 ?  114 GLU   B CB   1 
ATOM   5512 C CG   . GLU   B 1 114 ? 29.896 -18.566 -0.440  1.00 12.31 ?  114 GLU   B CG   1 
ATOM   5513 C CD   . GLU   B 1 114 ? 28.883 -18.380 0.674   1.00 12.29 ?  114 GLU   B CD   1 
ATOM   5514 O OE1  . GLU   B 1 114 ? 29.170 -17.760 1.717   1.00 12.94 ?  114 GLU   B OE1  1 
ATOM   5515 O OE2  . GLU   B 1 114 ? 27.757 -18.914 0.518   1.00 13.05 -1 114 GLU   B OE2  1 
ATOM   5516 H H    . GLU   B 1 114 ? 32.605 -19.582 -0.166  1.00 14.03 ?  114 GLU   B H    1 
ATOM   5517 H HA   . GLU   B 1 114 ? 31.718 -18.272 -2.210  1.00 13.87 ?  114 GLU   B HA   1 
ATOM   5518 H HB2  . GLU   B 1 114 ? 31.488 -17.706 0.530   1.00 14.58 ?  114 GLU   B HB2  1 
ATOM   5519 H HB3  . GLU   B 1 114 ? 30.830 -16.746 -0.558  1.00 14.58 ?  114 GLU   B HB3  1 
ATOM   5520 H HG2  . GLU   B 1 114 ? 29.448 -18.411 -1.281  1.00 14.77 ?  114 GLU   B HG2  1 
ATOM   5521 H HG3  . GLU   B 1 114 ? 30.207 -19.489 -0.402  1.00 14.77 ?  114 GLU   B HG3  1 
ATOM   5522 N N    . ASN   B 1 115 ? 34.327 -16.945 -1.027  1.00 11.42 ?  115 ASN   B N    1 
ATOM   5523 C CA   . ASN   B 1 115 ? 35.321 -15.910 -1.324  1.00 11.40 ?  115 ASN   B CA   1 
ATOM   5524 C C    . ASN   B 1 115 ? 35.727 -15.929 -2.791  1.00 11.06 ?  115 ASN   B C    1 
ATOM   5525 O O    . ASN   B 1 115 ? 36.116 -14.890 -3.344  1.00 11.42 ?  115 ASN   B O    1 
ATOM   5526 C CB   . ASN   B 1 115 ? 36.559 -16.089 -0.442  1.00 11.80 ?  115 ASN   B CB   1 
ATOM   5527 C CG   . ASN   B 1 115 ? 36.292 -15.824 1.019   1.00 12.45 ?  115 ASN   B CG   1 
ATOM   5528 O OD1  . ASN   B 1 115 ? 36.300 -14.680 1.461   1.00 14.23 ?  115 ASN   B OD1  1 
ATOM   5529 N ND2  . ASN   B 1 115 ? 36.121 -16.891 1.794   1.00 12.64 ?  115 ASN   B ND2  1 
ATOM   5530 H H    . ASN   B 1 115 ? 34.564 -17.507 -0.413  1.00 13.70 ?  115 ASN   B H    1 
ATOM   5531 H HA   . ASN   B 1 115 ? 34.942 -15.040 -1.127  1.00 13.68 ?  115 ASN   B HA   1 
ATOM   5532 H HB2  . ASN   B 1 115 ? 36.880 -17.000 -0.532  1.00 14.16 ?  115 ASN   B HB2  1 
ATOM   5533 H HB3  . ASN   B 1 115 ? 37.244 -15.467 -0.733  1.00 14.16 ?  115 ASN   B HB3  1 
ATOM   5534 H HD21 . ASN   B 1 115 ? 35.976 -16.791 2.637   1.00 15.17 ?  115 ASN   B HD21 1 
ATOM   5535 H HD22 . ASN   B 1 115 ? 36.143 -17.681 1.454   1.00 15.17 ?  115 ASN   B HD22 1 
ATOM   5536 N N    . PHE   B 1 116 ? 35.698 -17.108 -3.426  1.00 11.00 ?  116 PHE   B N    1 
ATOM   5537 C CA   . PHE   B 1 116 ? 36.134 -17.200 -4.815  1.00 11.34 ?  116 PHE   B CA   1 
ATOM   5538 C C    . PHE   B 1 116 ? 35.231 -16.373 -5.727  1.00 10.88 ?  116 PHE   B C    1 
ATOM   5539 O O    . PHE   B 1 116 ? 35.663 -15.951 -6.804  1.00 11.18 ?  116 PHE   B O    1 
ATOM   5540 C CB   . PHE   B 1 116 ? 36.110 -18.650 -5.339  1.00 10.92 ?  116 PHE   B CB   1 
ATOM   5541 C CG   . PHE   B 1 116 ? 37.177 -19.602 -4.784  1.00 10.95 ?  116 PHE   B CG   1 
ATOM   5542 C CD1  . PHE   B 1 116 ? 37.830 -19.418 -3.575  1.00 11.83 ?  116 PHE   B CD1  1 
ATOM   5543 C CD2  . PHE   B 1 116 ? 37.477 -20.740 -5.519  1.00 11.16 ?  116 PHE   B CD2  1 
ATOM   5544 C CE1  . PHE   B 1 116 ? 38.761 -20.357 -3.120  1.00 11.84 ?  116 PHE   B CE1  1 
ATOM   5545 C CE2  . PHE   B 1 116 ? 38.401 -21.678 -5.074  1.00 11.53 ?  116 PHE   B CE2  1 
ATOM   5546 C CZ   . PHE   B 1 116 ? 39.038 -21.492 -3.878  1.00 11.54 ?  116 PHE   B CZ   1 
ATOM   5547 H H    . PHE   B 1 116 ? 35.432 -17.851 -3.079  1.00 13.19 ?  116 PHE   B H    1 
ATOM   5548 H HA   . PHE   B 1 116 ? 37.039 -16.865 -4.891  1.00 13.60 ?  116 PHE   B HA   1 
ATOM   5549 H HB2  . PHE   B 1 116 ? 35.239 -19.033 -5.128  1.00 13.11 ?  116 PHE   B HB2  1 
ATOM   5550 H HB3  . PHE   B 1 116 ? 36.217 -18.626 -6.303  1.00 13.11 ?  116 PHE   B HB3  1 
ATOM   5551 H HD1  . PHE   B 1 116 ? 37.634 -18.670 -3.057  1.00 14.19 ?  116 PHE   B HD1  1 
ATOM   5552 H HD2  . PHE   B 1 116 ? 37.037 -20.888 -6.326  1.00 13.39 ?  116 PHE   B HD2  1 
ATOM   5553 H HE1  . PHE   B 1 116 ? 39.194 -20.223 -2.310  1.00 14.20 ?  116 PHE   B HE1  1 
ATOM   5554 H HE2  . PHE   B 1 116 ? 38.585 -22.430 -5.587  1.00 13.84 ?  116 PHE   B HE2  1 
ATOM   5555 H HZ   . PHE   B 1 116 ? 39.668 -22.107 -3.581  1.00 13.84 ?  116 PHE   B HZ   1 
ATOM   5556 N N    . ASN   B 1 117 ? 33.964 -16.171 -5.341  1.00 11.20 ?  117 ASN   B N    1 
ATOM   5557 C CA   . ASN   B 1 117 ? 33.021 -15.475 -6.212  1.00 11.62 ?  117 ASN   B CA   1 
ATOM   5558 C C    . ASN   B 1 117 ? 33.334 -13.995 -6.362  1.00 11.93 ?  117 ASN   B C    1 
ATOM   5559 O O    . ASN   B 1 117 ? 32.731 -13.336 -7.215  1.00 13.07 ?  117 ASN   B O    1 
ATOM   5560 C CB   . ASN   B 1 117 ? 31.594 -15.696 -5.725  1.00 12.08 ?  117 ASN   B CB   1 
ATOM   5561 C CG   . ASN   B 1 117 ? 31.145 -17.106 -5.972  1.00 12.05 ?  117 ASN   B CG   1 
ATOM   5562 O OD1  . ASN   B 1 117 ? 31.501 -17.697 -6.995  1.00 13.08 ?  117 ASN   B OD1  1 
ATOM   5563 N ND2  . ASN   B 1 117 ? 30.418 -17.681 -5.025  1.00 12.13 ?  117 ASN   B ND2  1 
ATOM   5564 H H    . ASN   B 1 117 ? 33.640 -16.422 -4.585  1.00 13.44 ?  117 ASN   B H    1 
ATOM   5565 H HA   . ASN   B 1 117 ? 33.083 -15.872 -7.090  1.00 13.95 ?  117 ASN   B HA   1 
ATOM   5566 H HB2  . ASN   B 1 117 ? 31.549 -15.521 -4.769  1.00 14.50 ?  117 ASN   B HB2  1 
ATOM   5567 H HB3  . ASN   B 1 117 ? 31.000 -15.088 -6.199  1.00 14.50 ?  117 ASN   B HB3  1 
ATOM   5568 H HD21 . ASN   B 1 117 ? 30.143 -18.488 -5.122  1.00 14.56 ?  117 ASN   B HD21 1 
ATOM   5569 H HD22 . ASN   B 1 117 ? 30.199 -17.234 -4.319  1.00 14.56 ?  117 ASN   B HD22 1 
ATOM   5570 N N    . GLN   B 1 118 ? 34.272 -13.470 -5.583  1.00 11.58 ?  118 GLN   B N    1 
ATOM   5571 C CA   . GLN   B 1 118 ? 34.702 -12.081 -5.718  1.00 12.20 ?  118 GLN   B CA   1 
ATOM   5572 C C    . GLN   B 1 118 ? 35.769 -11.888 -6.792  1.00 12.60 ?  118 GLN   B C    1 
ATOM   5573 O O    . GLN   B 1 118 ? 36.233 -10.758 -6.981  1.00 13.81 ?  118 GLN   B O    1 
ATOM   5574 C CB   . GLN   B 1 118 ? 35.174 -11.548 -4.362  1.00 12.88 ?  118 GLN   B CB   1 
ATOM   5575 C CG   . GLN   B 1 118 ? 34.086 -11.590 -3.293  1.00 13.07 ?  118 GLN   B CG   1 
ATOM   5576 C CD   . GLN   B 1 118 ? 32.914 -10.678 -3.621  1.00 12.79 ?  118 GLN   B CD   1 
ATOM   5577 O OE1  . GLN   B 1 118 ? 33.106 -9.536  -4.059  1.00 13.59 ?  118 GLN   B OE1  1 
ATOM   5578 N NE2  . GLN   B 1 118 ? 31.701 -11.169 -3.416  1.00 13.84 ?  118 GLN   B NE2  1 
ATOM   5579 H H    . GLN   B 1 118 ? 34.694 -13.904 -4.965  1.00 13.90 ?  118 GLN   B H    1 
ATOM   5580 H HA   . GLN   B 1 118 ? 33.937 -11.557 -5.986  1.00 14.64 ?  118 GLN   B HA   1 
ATOM   5581 H HB2  . GLN   B 1 118 ? 35.921 -12.078 -4.051  1.00 15.46 ?  118 GLN   B HB2  1 
ATOM   5582 H HB3  . GLN   B 1 118 ? 35.448 -10.620 -4.466  1.00 15.46 ?  118 GLN   B HB3  1 
ATOM   5583 H HG2  . GLN   B 1 118 ? 33.751 -12.499 -3.221  1.00 15.68 ?  118 GLN   B HG2  1 
ATOM   5584 H HG3  . GLN   B 1 118 ? 34.464 -11.308 -2.445  1.00 15.68 ?  118 GLN   B HG3  1 
ATOM   5585 H HE21 . GLN   B 1 118 ? 31.607 -11.969 -3.108  1.00 16.60 ?  118 GLN   B HE21 1 
ATOM   5586 H HE22 . GLN   B 1 118 ? 31.013 -10.690 -3.588  1.00 16.60 ?  118 GLN   B HE22 1 
ATOM   5587 N N    . HIS   B 1 119 ? 36.121 -12.946 -7.527  1.00 11.57 ?  119 HIS   B N    1 
ATOM   5588 C CA   . HIS   B 1 119 ? 37.163 -12.900 -8.543  1.00 12.10 ?  119 HIS   B CA   1 
ATOM   5589 C C    . HIS   B 1 119 ? 36.685 -13.631 -9.783  1.00 11.93 ?  119 HIS   B C    1 
ATOM   5590 O O    . HIS   B 1 119 ? 36.181 -14.750 -9.684  1.00 12.65 ?  119 HIS   B O    1 
ATOM   5591 C CB   . HIS   B 1 119 ? 38.443 -13.531 -7.994  1.00 12.77 ?  119 HIS   B CB   1 
ATOM   5592 C CG   . HIS   B 1 119 ? 38.925 -12.835 -6.767  1.00 13.89 ?  119 HIS   B CG   1 
ATOM   5593 N ND1  . HIS   B 1 119 ? 39.725 -11.714 -6.819  1.00 15.37 ?  119 HIS   B ND1  1 
ATOM   5594 C CD2  . HIS   B 1 119 ? 38.630 -13.031 -5.461  1.00 14.95 ?  119 HIS   B CD2  1 
ATOM   5595 C CE1  . HIS   B 1 119 ? 39.933 -11.274 -5.591  1.00 16.51 ?  119 HIS   B CE1  1 
ATOM   5596 N NE2  . HIS   B 1 119 ? 39.276 -12.051 -4.750  1.00 16.41 ?  119 HIS   B NE2  1 
ATOM   5597 H H    . HIS   B 1 119 ? 35.748 -13.719 -7.460  1.00 13.89 ?  119 HIS   B H    1 
ATOM   5598 H HA   . HIS   B 1 119 ? 37.345 -11.974 -8.781  1.00 14.52 ?  119 HIS   B HA   1 
ATOM   5599 H HB2  . HIS   B 1 119 ? 38.268 -14.456 -7.773  1.00 15.32 ?  119 HIS   B HB2  1 
ATOM   5600 H HB3  . HIS   B 1 119 ? 39.136 -13.472 -8.671  1.00 15.32 ?  119 HIS   B HB3  1 
ATOM   5601 H HD2  . HIS   B 1 119 ? 38.095 -13.707 -5.113  1.00 17.94 ?  119 HIS   B HD2  1 
ATOM   5602 H HE1  . HIS   B 1 119 ? 40.467 -10.548 -5.358  1.00 19.81 ?  119 HIS   B HE1  1 
ATOM   5603 H HE2  . HIS   B 1 119 ? 39.280 -11.974 -3.893  1.00 19.69 ?  119 HIS   B HE2  1 
ATOM   5604 N N    . GLU   B 1 120 ? 36.838 -13.010 -10.952 1.00 12.72 ?  120 GLU   B N    1 
ATOM   5605 C CA   . GLU   B 1 120 ? 36.253 -13.594 -12.156 1.00 13.90 ?  120 GLU   B CA   1 
ATOM   5606 C C    . GLU   B 1 120 ? 36.928 -14.898 -12.568 1.00 12.89 ?  120 GLU   B C    1 
ATOM   5607 O O    . GLU   B 1 120 ? 36.268 -15.771 -13.143 1.00 13.13 ?  120 GLU   B O    1 
ATOM   5608 C CB   . GLU   B 1 120 ? 36.275 -12.585 -13.301 1.00 17.94 ?  120 GLU   B CB   1 
ATOM   5609 C CG   . GLU   B 1 120 ? 35.303 -11.437 -13.092 1.00 23.64 ?  120 GLU   B CG   1 
ATOM   5610 C CD   . GLU   B 1 120 ? 35.158 -10.553 -14.313 1.00 29.53 ?  120 GLU   B CD   1 
ATOM   5611 O OE1  . GLU   B 1 120 ? 36.162 -10.358 -15.032 1.00 31.81 ?  120 GLU   B OE1  1 
ATOM   5612 O OE2  . GLU   B 1 120 ? 34.038 -10.055 -14.549 1.00 32.99 -1 120 GLU   B OE2  1 
ATOM   5613 H H    . GLU   B 1 120 ? 37.257 -12.265 -11.077 1.00 15.26 ?  120 GLU   B H    1 
ATOM   5614 H HA   . GLU   B 1 120 ? 35.326 -13.799 -11.977 1.00 16.68 ?  120 GLU   B HA   1 
ATOM   5615 H HB2  . GLU   B 1 120 ? 37.163 -12.208 -13.382 1.00 21.52 ?  120 GLU   B HB2  1 
ATOM   5616 H HB3  . GLU   B 1 120 ? 36.028 -13.033 -14.127 1.00 21.52 ?  120 GLU   B HB3  1 
ATOM   5617 H HG2  . GLU   B 1 120 ? 34.425 -11.797 -12.884 1.00 28.37 ?  120 GLU   B HG2  1 
ATOM   5618 H HG3  . GLU   B 1 120 ? 35.616 -10.883 -12.362 1.00 28.37 ?  120 GLU   B HG3  1 
ATOM   5619 N N    . VAL   B 1 121 ? 38.228 -15.041 -12.304 1.00 12.69 ?  121 VAL   B N    1 
ATOM   5620 C CA   . VAL   B 1 121 ? 38.977 -16.249 -12.652 1.00 12.44 ?  121 VAL   B CA   1 
ATOM   5621 C C    . VAL   B 1 121 ? 40.086 -16.454 -11.626 1.00 12.02 ?  121 VAL   B C    1 
ATOM   5622 O O    . VAL   B 1 121 ? 40.757 -15.498 -11.223 1.00 12.59 ?  121 VAL   B O    1 
ATOM   5623 C CB   . VAL   B 1 121 ? 39.493 -16.205 -14.110 1.00 14.15 ?  121 VAL   B CB   1 
ATOM   5624 C CG1  . VAL   B 1 121 ? 40.357 -14.974 -14.366 1.00 15.10 ?  121 VAL   B CG1  1 
ATOM   5625 C CG2  . VAL   B 1 121 ? 40.236 -17.487 -14.456 1.00 15.77 ?  121 VAL   B CG2  1 
ATOM   5626 H H    . VAL   B 1 121 ? 38.710 -14.437 -11.925 1.00 15.23 ?  121 VAL   B H    1 
ATOM   5627 H HA   . VAL   B 1 121 ? 38.371 -17.002 -12.589 1.00 14.93 ?  121 VAL   B HA   1 
ATOM   5628 H HB   . VAL   B 1 121 ? 38.726 -16.148 -14.708 1.00 16.98 ?  121 VAL   B HB   1 
ATOM   5629 H HG11 . VAL   B 1 121 ? 40.667 -14.989 -15.287 1.00 18.11 ?  121 VAL   B HG11 1 
ATOM   5630 H HG12 . VAL   B 1 121 ? 39.826 -14.176 -14.212 1.00 18.11 ?  121 VAL   B HG12 1 
ATOM   5631 H HG13 . VAL   B 1 121 ? 41.115 -14.990 -13.763 1.00 18.11 ?  121 VAL   B HG13 1 
ATOM   5632 H HG21 . VAL   B 1 121 ? 40.433 -17.492 -15.408 1.00 18.93 ?  121 VAL   B HG21 1 
ATOM   5633 H HG22 . VAL   B 1 121 ? 41.063 -17.520 -13.950 1.00 18.93 ?  121 VAL   B HG22 1 
ATOM   5634 H HG23 . VAL   B 1 121 ? 39.678 -18.247 -14.233 1.00 18.93 ?  121 VAL   B HG23 1 
ATOM   5635 N N    . LEU   B 1 122 ? 40.263 -17.707 -11.192 1.00 11.30 ?  122 LEU   B N    1 
ATOM   5636 C CA   . LEU   B 1 122 ? 41.247 -18.059 -10.173 1.00 11.11 ?  122 LEU   B CA   1 
ATOM   5637 C C    . LEU   B 1 122 ? 41.906 -19.391 -10.498 1.00 10.86 ?  122 LEU   B C    1 
ATOM   5638 O O    . LEU   B 1 122 ? 41.250 -20.317 -10.994 1.00 12.11 ?  122 LEU   B O    1 
ATOM   5639 C CB   . LEU   B 1 122 ? 40.603 -18.292 -8.794  1.00 12.95 ?  122 LEU   B CB   1 
ATOM   5640 C CG   . LEU   B 1 122 ? 39.564 -17.270 -8.315  1.00 12.93 ?  122 LEU   B CG   1 
ATOM   5641 C CD1  . LEU   B 1 122 ? 38.163 -17.632 -8.795  1.00 14.31 ?  122 LEU   B CD1  1 
ATOM   5642 C CD2  . LEU   B 1 122 ? 39.604 -17.155 -6.806  1.00 12.73 ?  122 LEU   B CD2  1 
ATOM   5643 H H    . LEU   B 1 122 ? 39.812 -18.383 -11.479 1.00 13.55 ?  122 LEU   B H    1 
ATOM   5644 H HA   . LEU   B 1 122 ? 41.922 -17.363 -10.102 1.00 13.33 ?  122 LEU   B HA   1 
ATOM   5645 H HB2  . LEU   B 1 122 ? 40.162 -19.150 -8.812  1.00 15.54 ?  122 LEU   B HB2  1 
ATOM   5646 H HB3  . LEU   B 1 122 ? 41.310 -18.303 -8.133  1.00 15.54 ?  122 LEU   B HB3  1 
ATOM   5647 H HG   . LEU   B 1 122 ? 39.786 -16.395 -8.679  1.00 15.52 ?  122 LEU   B HG   1 
ATOM   5648 H HD11 . LEU   B 1 122 ? 37.530 -16.995 -8.424  1.00 17.17 ?  122 LEU   B HD11 1 
ATOM   5649 H HD12 . LEU   B 1 122 ? 38.142 -17.588 -9.764  1.00 17.17 ?  122 LEU   B HD12 1 
ATOM   5650 H HD13 . LEU   B 1 122 ? 37.950 -18.525 -8.495  1.00 17.17 ?  122 LEU   B HD13 1 
ATOM   5651 H HD21 . LEU   B 1 122 ? 38.923 -16.532 -6.513  1.00 15.28 ?  122 LEU   B HD21 1 
ATOM   5652 H HD22 . LEU   B 1 122 ? 39.443 -18.030 -6.419  1.00 15.28 ?  122 LEU   B HD22 1 
ATOM   5653 H HD23 . LEU   B 1 122 ? 40.482 -16.834 -6.536  1.00 15.28 ?  122 LEU   B HD23 1 
ATOM   5654 N N    . LEU   B 1 123 ? 43.192 -19.498 -10.138 1.00 10.80 ?  123 LEU   B N    1 
ATOM   5655 C CA   . LEU   B 1 123 ? 43.905 -20.770 -10.015 1.00 10.98 ?  123 LEU   B CA   1 
ATOM   5656 C C    . LEU   B 1 123 ? 43.880 -21.163 -8.542  1.00 10.92 ?  123 LEU   B C    1 
ATOM   5657 O O    . LEU   B 1 123 ? 44.232 -20.338 -7.687  1.00 11.07 ?  123 LEU   B O    1 
ATOM   5658 C CB   . LEU   B 1 123 ? 45.353 -20.587 -10.476 1.00 11.57 ?  123 LEU   B CB   1 
ATOM   5659 C CG   . LEU   B 1 123 ? 46.296 -21.770 -10.228 1.00 11.81 ?  123 LEU   B CG   1 
ATOM   5660 C CD1  . LEU   B 1 123 ? 45.873 -23.011 -11.007 1.00 12.42 ?  123 LEU   B CD1  1 
ATOM   5661 C CD2  . LEU   B 1 123 ? 47.712 -21.376 -10.601 1.00 12.63 ?  123 LEU   B CD2  1 
ATOM   5662 H H    . LEU   B 1 123 ? 43.684 -18.819 -9.943  1.00 12.96 ?  123 LEU   B H    1 
ATOM   5663 H HA   . LEU   B 1 123 ? 43.468 -21.458 -10.547 1.00 13.18 ?  123 LEU   B HA   1 
ATOM   5664 H HB2  . LEU   B 1 123 ? 45.347 -20.423 -11.433 1.00 13.89 ?  123 LEU   B HB2  1 
ATOM   5665 H HB3  . LEU   B 1 123 ? 45.723 -19.822 -10.018 1.00 13.89 ?  123 LEU   B HB3  1 
ATOM   5666 H HG   . LEU   B 1 123 ? 46.289 -21.996 -9.283  1.00 14.17 ?  123 LEU   B HG   1 
ATOM   5667 H HD11 . LEU   B 1 123 ? 46.507 -23.722 -10.834 1.00 14.90 ?  123 LEU   B HD11 1 
ATOM   5668 H HD12 . LEU   B 1 123 ? 44.986 -23.278 -10.716 1.00 14.90 ?  123 LEU   B HD12 1 
ATOM   5669 H HD13 . LEU   B 1 123 ? 45.861 -22.797 -11.952 1.00 14.90 ?  123 LEU   B HD13 1 
ATOM   5670 H HD21 . LEU   B 1 123 ? 48.301 -22.127 -10.442 1.00 15.15 ?  123 LEU   B HD21 1 
ATOM   5671 H HD22 . LEU   B 1 123 ? 47.730 -21.130 -11.539 1.00 15.15 ?  123 LEU   B HD22 1 
ATOM   5672 H HD23 . LEU   B 1 123 ? 47.979 -20.620 -10.055 1.00 15.15 ?  123 LEU   B HD23 1 
ATOM   5673 N N    . ALA   B 1 124 ? 43.446 -22.393 -8.236  1.00 10.84 ?  124 ALA   B N    1 
ATOM   5674 C CA   . ALA   B 1 124 ? 43.186 -22.714 -6.842  1.00 10.99 ?  124 ALA   B CA   1 
ATOM   5675 C C    . ALA   B 1 124 ? 43.457 -24.174 -6.508  1.00 10.77 ?  124 ALA   B C    1 
ATOM   5676 O O    . ALA   B 1 124 ? 43.326 -25.052 -7.374  1.00 11.31 ?  124 ALA   B O    1 
ATOM   5677 C CB   . ALA   B 1 124 ? 41.724 -22.407 -6.485  1.00 11.33 ?  124 ALA   B CB   1 
ATOM   5678 H H    . ALA   B 1 124 ? 43.287 -23.032 -8.797  1.00 13.00 ?  124 ALA   B H    1 
ATOM   5679 H HA   . ALA   B 1 124 ? 43.753 -22.161 -6.290  1.00 13.18 ?  124 ALA   B HA   1 
ATOM   5680 H HB1  . ALA   B 1 124 ? 41.568 -22.627 -5.553  1.00 13.59 ?  124 ALA   B HB1  1 
ATOM   5681 H HB2  . ALA   B 1 124 ? 41.555 -21.463 -6.634  1.00 13.59 ?  124 ALA   B HB2  1 
ATOM   5682 H HB3  . ALA   B 1 124 ? 41.139 -22.939 -7.050  1.00 13.59 ?  124 ALA   B HB3  1 
ATOM   5683 N N    . PRO   B 1 125 ? 43.760 -24.465 -5.246  1.00 10.97 ?  125 PRO   B N    1 
ATOM   5684 C CA   . PRO   B 1 125 ? 43.697 -25.829 -4.724  1.00 11.81 ?  125 PRO   B CA   1 
ATOM   5685 C C    . PRO   B 1 125 ? 42.295 -26.109 -4.179  1.00 11.76 ?  125 PRO   B C    1 
ATOM   5686 O O    . PRO   B 1 125 ? 41.492 -25.195 -3.975  1.00 12.29 ?  125 PRO   B O    1 
ATOM   5687 C CB   . PRO   B 1 125 ? 44.686 -25.754 -3.555  1.00 12.73 ?  125 PRO   B CB   1 
ATOM   5688 C CG   . PRO   B 1 125 ? 44.431 -24.367 -2.978  1.00 12.82 ?  125 PRO   B CG   1 
ATOM   5689 C CD   . PRO   B 1 125 ? 44.077 -23.499 -4.176  1.00 11.73 ?  125 PRO   B CD   1 
ATOM   5690 H HA   . PRO   B 1 125 ? 43.971 -26.496 -5.372  1.00 14.17 ?  125 PRO   B HA   1 
ATOM   5691 H HB2  . PRO   B 1 125 ? 44.485 -26.443 -2.898  1.00 15.28 ?  125 PRO   B HB2  1 
ATOM   5692 H HB3  . PRO   B 1 125 ? 45.596 -25.836 -3.877  1.00 15.28 ?  125 PRO   B HB3  1 
ATOM   5693 H HG2  . PRO   B 1 125 ? 43.692 -24.396 -2.348  1.00 15.39 ?  125 PRO   B HG2  1 
ATOM   5694 H HG3  . PRO   B 1 125 ? 45.236 -24.036 -2.539  1.00 15.39 ?  125 PRO   B HG3  1 
ATOM   5695 H HD2  . PRO   B 1 125 ? 43.305 -22.943 -3.981  1.00 14.08 ?  125 PRO   B HD2  1 
ATOM   5696 H HD3  . PRO   B 1 125 ? 44.842 -22.950 -4.434  1.00 14.08 ?  125 PRO   B HD3  1 
ATOM   5697 N N    . LEU   B 1 126 ? 42.026 -27.389 -3.901  1.00 12.14 ?  126 LEU   B N    1 
ATOM   5698 C CA   . LEU   B 1 126 ? 40.804 -27.757 -3.192  1.00 12.85 ?  126 LEU   B CA   1 
ATOM   5699 C C    . LEU   B 1 126 ? 40.915 -27.358 -1.728  1.00 13.02 ?  126 LEU   B C    1 
ATOM   5700 O O    . LEU   B 1 126 ? 41.808 -27.818 -1.010  1.00 14.67 ?  126 LEU   B O    1 
ATOM   5701 C CB   . LEU   B 1 126 ? 40.544 -29.253 -3.314  1.00 14.20 ?  126 LEU   B CB   1 
ATOM   5702 C CG   . LEU   B 1 126 ? 40.014 -29.728 -4.669  1.00 15.01 ?  126 LEU   B CG   1 
ATOM   5703 C CD1  . LEU   B 1 126 ? 40.064 -31.237 -4.760  1.00 17.15 ?  126 LEU   B CD1  1 
ATOM   5704 C CD2  . LEU   B 1 126 ? 38.595 -29.237 -4.911  1.00 15.15 ?  126 LEU   B CD2  1 
ATOM   5705 H H    . LEU   B 1 126 ? 42.536 -28.057 -4.101  1.00 14.56 ?  126 LEU   B H    1 
ATOM   5706 H HA   . LEU   B 1 126 ? 40.057 -27.283 -3.581  1.00 15.41 ?  126 LEU   B HA   1 
ATOM   5707 H HB2  . LEU   B 1 126 ? 41.374 -29.723 -3.147  1.00 17.04 ?  126 LEU   B HB2  1 
ATOM   5708 H HB3  . LEU   B 1 126 ? 39.890 -29.504 -2.642  1.00 17.04 ?  126 LEU   B HB3  1 
ATOM   5709 H HG   . LEU   B 1 126 ? 40.577 -29.366 -5.370  1.00 18.01 ?  126 LEU   B HG   1 
ATOM   5710 H HD11 . LEU   B 1 126 ? 39.721 -31.511 -5.625  1.00 20.57 ?  126 LEU   B HD11 1 
ATOM   5711 H HD12 . LEU   B 1 126 ? 40.980 -31.528 -4.656  1.00 20.57 ?  126 LEU   B HD12 1 
ATOM   5712 H HD13 . LEU   B 1 126 ? 39.513 -31.612 -4.053  1.00 20.57 ?  126 LEU   B HD13 1 
ATOM   5713 H HD21 . LEU   B 1 126 ? 38.255 -29.638 -5.727  1.00 18.18 ?  126 LEU   B HD21 1 
ATOM   5714 H HD22 . LEU   B 1 126 ? 38.036 -29.494 -4.161  1.00 18.18 ?  126 LEU   B HD22 1 
ATOM   5715 H HD23 . LEU   B 1 126 ? 38.601 -28.269 -5.000  1.00 18.18 ?  126 LEU   B HD23 1 
ATOM   5716 N N    . LEU   B 1 127 ? 39.990 -26.520 -1.274  1.00 12.69 ?  127 LEU   B N    1 
ATOM   5717 C CA   . LEU   B 1 127 ? 40.041 -26.031 0.093   1.00 12.97 ?  127 LEU   B CA   1 
ATOM   5718 C C    . LEU   B 1 127 ? 39.766 -27.152 1.087   1.00 12.80 ?  127 LEU   B C    1 
ATOM   5719 O O    . LEU   B 1 127 ? 38.945 -28.048 0.852   1.00 13.14 ?  127 LEU   B O    1 
ATOM   5720 C CB   . LEU   B 1 127 ? 39.031 -24.902 0.302   1.00 13.76 ?  127 LEU   B CB   1 
ATOM   5721 C CG   . LEU   B 1 127 ? 39.206 -23.641 -0.541  1.00 14.22 ?  127 LEU   B CG   1 
ATOM   5722 C CD1  . LEU   B 1 127 ? 38.081 -22.668 -0.208  1.00 14.30 ?  127 LEU   B CD1  1 
ATOM   5723 C CD2  . LEU   B 1 127 ? 40.562 -22.988 -0.315  1.00 14.93 ?  127 LEU   B CD2  1 
ATOM   5724 H H    . LEU   B 1 127 ? 39.330 -26.212 -1.737  1.00 15.23 ?  127 LEU   B H    1 
ATOM   5725 H HA   . LEU   B 1 127 ? 40.931 -25.675 0.268   1.00 15.56 ?  127 LEU   B HA   1 
ATOM   5726 H HB2  . LEU   B 1 127 ? 38.147 -25.254 0.114   1.00 16.51 ?  127 LEU   B HB2  1 
ATOM   5727 H HB3  . LEU   B 1 127 ? 39.074 -24.630 1.232   1.00 16.51 ?  127 LEU   B HB3  1 
ATOM   5728 H HG   . LEU   B 1 127 ? 39.124 -23.871 -1.479  1.00 17.06 ?  127 LEU   B HG   1 
ATOM   5729 H HD11 . LEU   B 1 127 ? 38.190 -21.862 -0.739  1.00 17.16 ?  127 LEU   B HD11 1 
ATOM   5730 H HD12 . LEU   B 1 127 ? 37.227 -23.082 -0.409  1.00 17.16 ?  127 LEU   B HD12 1 
ATOM   5731 H HD13 . LEU   B 1 127 ? 38.124 -22.445 0.738   1.00 17.16 ?  127 LEU   B HD13 1 
ATOM   5732 H HD21 . LEU   B 1 127 ? 40.595 -22.149 -0.803  1.00 17.91 ?  127 LEU   B HD21 1 
ATOM   5733 H HD22 . LEU   B 1 127 ? 40.680 -22.823 0.634   1.00 17.91 ?  127 LEU   B HD22 1 
ATOM   5734 H HD23 . LEU   B 1 127 ? 41.255 -23.585 -0.636  1.00 17.91 ?  127 LEU   B HD23 1 
ATOM   5735 N N    . SER   B 1 128 ? 40.451 -27.070 2.218   1.00 12.76 ?  128 SER   B N    1 
ATOM   5736 C CA   . SER   B 1 128 ? 40.340 -27.985 3.343   1.00 13.42 ?  128 SER   B CA   1 
ATOM   5737 C C    . SER   B 1 128 ? 40.832 -29.393 3.018   1.00 14.51 ?  128 SER   B C    1 
ATOM   5738 O O    . SER   B 1 128 ? 40.746 -30.275 3.876   1.00 15.81 ?  128 SER   B O    1 
ATOM   5739 C CB   . SER   B 1 128 ? 38.940 -27.993 3.973   1.00 13.84 ?  128 SER   B CB   1 
ATOM   5740 O OG   . SER   B 1 128 ? 38.623 -26.718 4.520   1.00 14.36 ?  128 SER   B OG   1 
ATOM   5741 H H    . SER   B 1 128 ? 41.032 -26.447 2.362   1.00 15.31 ?  128 SER   B H    1 
ATOM   5742 H HA   . SER   B 1 128 ? 40.934 -27.650 4.027   1.00 16.10 ?  128 SER   B HA   1 
ATOM   5743 H HB2  . SER   B 1 128 ? 38.286 -28.229 3.298   1.00 16.61 ?  128 SER   B HB2  1 
ATOM   5744 H HB3  . SER   B 1 128 ? 38.925 -28.663 4.688   1.00 16.61 ?  128 SER   B HB3  1 
ATOM   5745 H HG   . SER   B 1 128 ? 39.188 -26.517 5.110   1.00 17.24 ?  128 SER   B HG   1 
ATOM   5746 N N    . ALA   B 1 129 ? 41.402 -29.614 1.829   1.00 15.22 ?  129 ALA   B N    1 
ATOM   5747 C CA   . ALA   B 1 129 ? 41.953 -30.910 1.463   1.00 16.41 ?  129 ALA   B CA   1 
ATOM   5748 C C    . ALA   B 1 129 ? 43.340 -31.094 2.067   1.00 15.47 ?  129 ALA   B C    1 
ATOM   5749 O O    . ALA   B 1 129 ? 43.900 -30.196 2.711   1.00 15.46 ?  129 ALA   B O    1 
ATOM   5750 C CB   . ALA   B 1 129 ? 42.013 -31.053 -0.056  1.00 18.65 ?  129 ALA   B CB   1 
ATOM   5751 H H    . ALA   B 1 129 ? 41.481 -29.017 1.210   1.00 18.27 ?  129 ALA   B H    1 
ATOM   5752 H HA   . ALA   B 1 129 ? 41.376 -31.606 1.806   1.00 19.69 ?  129 ALA   B HA   1 
ATOM   5753 H HB1  . ALA   B 1 129 ? 42.375 -31.928 -0.276  1.00 22.38 ?  129 ALA   B HB1  1 
ATOM   5754 H HB2  . ALA   B 1 129 ? 41.118 -30.967 -0.418  1.00 22.38 ?  129 ALA   B HB2  1 
ATOM   5755 H HB3  . ALA   B 1 129 ? 42.586 -30.360 -0.419  1.00 22.38 ?  129 ALA   B HB3  1 
ATOM   5756 N N    . GLY   B 1 130 ? 43.897 -32.284 1.846   1.00 15.16 ?  130 GLY   B N    1 
ATOM   5757 C CA   . GLY   B 1 130 ? 45.284 -32.524 2.196   1.00 16.07 ?  130 GLY   B CA   1 
ATOM   5758 C C    . GLY   B 1 130 ? 45.494 -32.425 3.686   1.00 16.09 ?  130 GLY   B C    1 
ATOM   5759 O O    . GLY   B 1 130 ? 44.794 -33.065 4.485   1.00 16.85 ?  130 GLY   B O    1 
ATOM   5760 H H    . GLY   B 1 130 ? 43.498 -32.960 1.495   1.00 18.19 ?  130 GLY   B H    1 
ATOM   5761 H HA2  . GLY   B 1 130 ? 45.548 -33.413 1.903   1.00 19.29 ?  130 GLY   B HA2  1 
ATOM   5762 H HA3  . GLY   B 1 130 ? 45.852 -31.873 1.755   1.00 19.29 ?  130 GLY   B HA3  1 
ATOM   5763 N N    . ILE   B 1 131 ? 46.471 -31.596 4.071   1.00 16.50 ?  131 ILE   B N    1 
ATOM   5764 C CA   . ILE   B 1 131 ? 46.829 -31.457 5.475   1.00 17.21 ?  131 ILE   B CA   1 
ATOM   5765 C C    . ILE   B 1 131 ? 45.713 -30.855 6.311   1.00 16.22 ?  131 ILE   B C    1 
ATOM   5766 O O    . ILE   B 1 131 ? 45.788 -30.918 7.542   1.00 17.26 ?  131 ILE   B O    1 
ATOM   5767 C CB   . ILE   B 1 131 ? 48.158 -30.688 5.659   1.00 18.98 ?  131 ILE   B CB   1 
ATOM   5768 C CG1  . ILE   B 1 131 ? 48.005 -29.210 5.268   1.00 19.92 ?  131 ILE   B CG1  1 
ATOM   5769 C CG2  . ILE   B 1 131 ? 49.273 -31.349 4.851   1.00 19.94 ?  131 ILE   B CG2  1 
ATOM   5770 C CD1  . ILE   B 1 131 ? 49.205 -28.348 5.624   1.00 21.23 ?  131 ILE   B CD1  1 
ATOM   5771 H H    . ILE   B 1 131 ? 46.935 -31.108 3.538   1.00 19.80 ?  131 ILE   B H    1 
ATOM   5772 H HA   . ILE   B 1 131 ? 46.972 -32.349 5.822   1.00 20.65 ?  131 ILE   B HA   1 
ATOM   5773 H HB   . ILE   B 1 131 ? 48.396 -30.730 6.597   1.00 22.77 ?  131 ILE   B HB   1 
ATOM   5774 H HG12 . ILE   B 1 131 ? 47.874 -29.156 4.309   1.00 23.90 ?  131 ILE   B HG12 1 
ATOM   5775 H HG13 . ILE   B 1 131 ? 47.234 -28.837 5.725   1.00 23.90 ?  131 ILE   B HG13 1 
ATOM   5776 H HG21 . ILE   B 1 131 ? 50.114 -30.941 5.093   1.00 23.93 ?  131 ILE   B HG21 1 
ATOM   5777 H HG22 . ILE   B 1 131 ? 49.283 -32.294 5.055   1.00 23.93 ?  131 ILE   B HG22 1 
ATOM   5778 H HG23 . ILE   B 1 131 ? 49.092 -31.213 3.907   1.00 23.93 ?  131 ILE   B HG23 1 
ATOM   5779 H HD11 . ILE   B 1 131 ? 48.997 -27.423 5.415   1.00 25.47 ?  131 ILE   B HD11 1 
ATOM   5780 H HD12 . ILE   B 1 131 ? 49.387 -28.440 6.572   1.00 25.47 ?  131 ILE   B HD12 1 
ATOM   5781 H HD13 . ILE   B 1 131 ? 49.968 -28.642 5.107   1.00 25.47 ?  131 ILE   B HD13 1 
ATOM   5782 N N    . PHE   B 1 132 ? 44.680 -30.277 5.683   1.00 15.10 ?  132 PHE   B N    1 
ATOM   5783 C CA   . PHE   B 1 132 ? 43.523 -29.772 6.417   1.00 15.51 ?  132 PHE   B CA   1 
ATOM   5784 C C    . PHE   B 1 132 ? 42.496 -30.858 6.736   1.00 16.70 ?  132 PHE   B C    1 
ATOM   5785 O O    . PHE   B 1 132 ? 41.580 -30.606 7.526   1.00 18.51 ?  132 PHE   B O    1 
ATOM   5786 C CB   . PHE   B 1 132 ? 42.851 -28.636 5.637   1.00 14.40 ?  132 PHE   B CB   1 
ATOM   5787 C CG   . PHE   B 1 132 ? 43.552 -27.293 5.751   1.00 14.91 ?  132 PHE   B CG   1 
ATOM   5788 C CD1  . PHE   B 1 132 ? 44.851 -27.111 5.292   1.00 15.92 ?  132 PHE   B CD1  1 
ATOM   5789 C CD2  . PHE   B 1 132 ? 42.876 -26.194 6.267   1.00 14.43 ?  132 PHE   B CD2  1 
ATOM   5790 C CE1  . PHE   B 1 132 ? 45.467 -25.869 5.384   1.00 16.32 ?  132 PHE   B CE1  1 
ATOM   5791 C CE2  . PHE   B 1 132 ? 43.483 -24.951 6.357   1.00 14.95 ?  132 PHE   B CE2  1 
ATOM   5792 C CZ   . PHE   B 1 132 ? 44.778 -24.791 5.917   1.00 16.09 ?  132 PHE   B CZ   1 
ATOM   5793 H H    . PHE   B 1 132 ? 44.628 -30.167 4.829   1.00 18.12 ?  132 PHE   B H    1 
ATOM   5794 H HA   . PHE   B 1 132 ? 43.828 -29.402 7.258   1.00 18.61 ?  132 PHE   B HA   1 
ATOM   5795 H HB2  . PHE   B 1 132 ? 42.833 -28.874 4.698   1.00 17.27 ?  132 PHE   B HB2  1 
ATOM   5796 H HB3  . PHE   B 1 132 ? 41.945 -28.522 5.966   1.00 17.27 ?  132 PHE   B HB3  1 
ATOM   5797 H HD1  . PHE   B 1 132 ? 45.323 -27.832 4.937   1.00 19.10 ?  132 PHE   B HD1  1 
ATOM   5798 H HD2  . PHE   B 1 132 ? 42.000 -26.301 6.565   1.00 17.31 ?  132 PHE   B HD2  1 
ATOM   5799 H HE1  . PHE   B 1 132 ? 46.342 -25.761 5.089   1.00 19.59 ?  132 PHE   B HE1  1 
ATOM   5800 H HE2  . PHE   B 1 132 ? 43.017 -24.229 6.718   1.00 17.94 ?  132 PHE   B HE2  1 
ATOM   5801 H HZ   . PHE   B 1 132 ? 45.190 -23.957 5.982   1.00 19.31 ?  132 PHE   B HZ   1 
ATOM   5802 N N    . GLY   B 1 133 ? 42.606 -32.049 6.138   1.00 16.29 ?  133 GLY   B N    1 
ATOM   5803 C CA   . GLY   B 1 133 ? 41.895 -33.219 6.621   1.00 17.31 ?  133 GLY   B CA   1 
ATOM   5804 C C    . GLY   B 1 133 ? 40.499 -33.477 6.085   1.00 17.68 ?  133 GLY   B C    1 
ATOM   5805 O O    . GLY   B 1 133 ? 39.907 -34.494 6.456   1.00 19.64 ?  133 GLY   B O    1 
ATOM   5806 H H    . GLY   B 1 133 ? 43.096 -32.195 5.444   1.00 19.55 ?  133 GLY   B H    1 
ATOM   5807 H HA2  . GLY   B 1 133 ? 42.431 -33.998 6.418   1.00 20.77 ?  133 GLY   B HA2  1 
ATOM   5808 H HA3  . GLY   B 1 133 ? 41.827 -33.149 7.584   1.00 20.77 ?  133 GLY   B HA3  1 
ATOM   5809 N N    . ALA   B 1 134 ? 39.939 -32.609 5.251   1.00 16.83 ?  134 ALA   B N    1 
ATOM   5810 C CA   . ALA   B 1 134 ? 38.613 -32.888 4.717   1.00 16.92 ?  134 ALA   B CA   1 
ATOM   5811 C C    . ALA   B 1 134 ? 38.701 -33.883 3.563   1.00 16.99 ?  134 ALA   B C    1 
ATOM   5812 O O    . ALA   B 1 134 ? 39.755 -34.074 2.951   1.00 18.15 ?  134 ALA   B O    1 
ATOM   5813 C CB   . ALA   B 1 134 ? 37.941 -31.602 4.237   1.00 17.46 ?  134 ALA   B CB   1 
ATOM   5814 H H    . ALA   B 1 134 ? 40.288 -31.862 4.995   1.00 20.20 ?  134 ALA   B H    1 
ATOM   5815 H HA   . ALA   B 1 134 ? 38.060 -33.271 5.418   1.00 20.31 ?  134 ALA   B HA   1 
ATOM   5816 H HB1  . ALA   B 1 134 ? 37.056 -31.814 3.903   1.00 20.95 ?  134 ALA   B HB1  1 
ATOM   5817 H HB2  . ALA   B 1 134 ? 37.873 -30.980 4.980   1.00 20.95 ?  134 ALA   B HB2  1 
ATOM   5818 H HB3  . ALA   B 1 134 ? 38.477 -31.211 3.529   1.00 20.95 ?  134 ALA   B HB3  1 
ATOM   5819 N N    . ASP   B 1 135 ? 37.570 -34.515 3.275   1.00 17.03 ?  135 ASP   B N    1 
ATOM   5820 C CA   . ASP   B 1 135 ? 37.477 -35.413 2.134   1.00 17.83 ?  135 ASP   B CA   1 
ATOM   5821 C C    . ASP   B 1 135 ? 37.576 -34.580 0.862   1.00 16.78 ?  135 ASP   B C    1 
ATOM   5822 O O    . ASP   B 1 135 ? 36.721 -33.711 0.636   1.00 16.69 ?  135 ASP   B O    1 
ATOM   5823 C CB   . ASP   B 1 135 ? 36.138 -36.153 2.192   1.00 19.61 ?  135 ASP   B CB   1 
ATOM   5824 C CG   . ASP   B 1 135 ? 35.947 -37.134 1.044   1.00 21.62 ?  135 ASP   B CG   1 
ATOM   5825 O OD1  . ASP   B 1 135 ? 36.811 -37.190 0.144   1.00 21.73 ?  135 ASP   B OD1  1 
ATOM   5826 O OD2  . ASP   B 1 135 ? 34.933 -37.875 1.058   1.00 24.69 -1 135 ASP   B OD2  1 
ATOM   5827 H H    . ASP   B 1 135 ? 36.840 -34.432 3.723   1.00 20.43 ?  135 ASP   B H    1 
ATOM   5828 H HA   . ASP   B 1 135 ? 38.199 -36.057 2.171   1.00 21.39 ?  135 ASP   B HA   1 
ATOM   5829 H HB2  . ASP   B 1 135 ? 36.099 -36.655 3.018   1.00 23.54 ?  135 ASP   B HB2  1 
ATOM   5830 H HB3  . ASP   B 1 135 ? 35.424 -35.499 2.163   1.00 23.54 ?  135 ASP   B HB3  1 
ATOM   5831 N N    . PRO   B 1 136 ? 38.586 -34.788 0.015   1.00 16.99 ?  136 PRO   B N    1 
ATOM   5832 C CA   . PRO   B 1 136 ? 38.686 -33.964 -1.201  1.00 16.45 ?  136 PRO   B CA   1 
ATOM   5833 C C    . PRO   B 1 136 ? 37.496 -34.113 -2.127  1.00 15.76 ?  136 PRO   B C    1 
ATOM   5834 O O    . PRO   B 1 136 ? 37.167 -33.162 -2.844  1.00 15.13 ?  136 PRO   B O    1 
ATOM   5835 C CB   . PRO   B 1 136 ? 39.994 -34.443 -1.849  1.00 17.47 ?  136 PRO   B CB   1 
ATOM   5836 C CG   . PRO   B 1 136 ? 40.187 -35.838 -1.313  1.00 18.53 ?  136 PRO   B CG   1 
ATOM   5837 C CD   . PRO   B 1 136 ? 39.660 -35.790 0.094   1.00 18.20 ?  136 PRO   B CD   1 
ATOM   5838 H HA   . PRO   B 1 136 ? 38.780 -33.027 -0.968  1.00 19.73 ?  136 PRO   B HA   1 
ATOM   5839 H HB2  . PRO   B 1 136 ? 39.903 -34.457 -2.816  1.00 20.96 ?  136 PRO   B HB2  1 
ATOM   5840 H HB3  . PRO   B 1 136 ? 40.726 -33.868 -1.581  1.00 20.96 ?  136 PRO   B HB3  1 
ATOM   5841 H HG2  . PRO   B 1 136 ? 39.680 -36.471 -1.847  1.00 22.23 ?  136 PRO   B HG2  1 
ATOM   5842 H HG3  . PRO   B 1 136 ? 41.130 -36.066 -1.316  1.00 22.23 ?  136 PRO   B HG3  1 
ATOM   5843 H HD2  . PRO   B 1 136 ? 39.295 -36.651 0.352   1.00 21.84 ?  136 PRO   B HD2  1 
ATOM   5844 H HD3  . PRO   B 1 136 ? 40.349 -35.495 0.712   1.00 21.84 ?  136 PRO   B HD3  1 
ATOM   5845 N N    . ILE   B 1 137 ? 36.841 -35.277 -2.136  1.00 16.30 ?  137 ILE   B N    1 
ATOM   5846 C CA   . ILE   B 1 137 ? 35.628 -35.446 -2.931  1.00 16.57 ?  137 ILE   B CA   1 
ATOM   5847 C C    . ILE   B 1 137 ? 34.552 -34.480 -2.456  1.00 16.18 ?  137 ILE   B C    1 
ATOM   5848 O O    . ILE   B 1 137 ? 33.832 -33.876 -3.259  1.00 15.63 ?  137 ILE   B O    1 
ATOM   5849 C CB   . ILE   B 1 137 ? 35.156 -36.913 -2.869  1.00 18.62 ?  137 ILE   B CB   1 
ATOM   5850 C CG1  . ILE   B 1 137 ? 36.143 -37.822 -3.605  1.00 20.72 ?  137 ILE   B CG1  1 
ATOM   5851 C CG2  . ILE   B 1 137 ? 33.754 -37.053 -3.449  1.00 19.28 ?  137 ILE   B CG2  1 
ATOM   5852 C CD1  . ILE   B 1 137 ? 35.833 -39.305 -3.469  1.00 23.20 ?  137 ILE   B CD1  1 
ATOM   5853 H H    . ILE   B 1 137 ? 37.076 -35.978 -1.697  1.00 19.56 ?  137 ILE   B H    1 
ATOM   5854 H HA   . ILE   B 1 137 ? 35.825 -35.241 -3.860  1.00 19.89 ?  137 ILE   B HA   1 
ATOM   5855 H HB   . ILE   B 1 137 ? 35.126 -37.187 -1.944  1.00 22.34 ?  137 ILE   B HB   1 
ATOM   5856 H HG12 . ILE   B 1 137 ? 36.127 -37.608 -4.551  1.00 24.86 ?  137 ILE   B HG12 1 
ATOM   5857 H HG13 . ILE   B 1 137 ? 37.029 -37.676 -3.247  1.00 24.86 ?  137 ILE   B HG13 1 
ATOM   5858 H HG21 . ILE   B 1 137 ? 33.540 -37.996 -3.558  1.00 23.13 ?  137 ILE   B HG21 1 
ATOM   5859 H HG22 . ILE   B 1 137 ? 33.115 -36.652 -2.840  1.00 23.13 ?  137 ILE   B HG22 1 
ATOM   5860 H HG23 . ILE   B 1 137 ? 33.718 -36.611 -4.310  1.00 23.13 ?  137 ILE   B HG23 1 
ATOM   5861 H HD11 . ILE   B 1 137 ? 36.594 -39.813 -3.788  1.00 27.84 ?  137 ILE   B HD11 1 
ATOM   5862 H HD12 . ILE   B 1 137 ? 35.666 -39.512 -2.535  1.00 27.84 ?  137 ILE   B HD12 1 
ATOM   5863 H HD13 . ILE   B 1 137 ? 35.049 -39.522 -4.000  1.00 27.84 ?  137 ILE   B HD13 1 
ATOM   5864 N N    . HIS   B 1 138 ? 34.423 -34.326 -1.141  1.00 16.04 ?  138 HIS   B N    1 
ATOM   5865 C CA   . HIS   B 1 138 ? 33.471 -33.363 -0.607  1.00 16.57 ?  138 HIS   B CA   1 
ATOM   5866 C C    . HIS   B 1 138 ? 33.888 -31.933 -0.922  1.00 15.65 ?  138 HIS   B C    1 
ATOM   5867 O O    . HIS   B 1 138 ? 33.040 -31.091 -1.233  1.00 15.95 ?  138 HIS   B O    1 
ATOM   5868 C CB   . HIS   B 1 138 ? 33.342 -33.542 0.897   1.00 17.63 ?  138 HIS   B CB   1 
ATOM   5869 C CG   . HIS   B 1 138 ? 32.403 -32.566 1.526   1.00 18.46 ?  138 HIS   B CG   1 
ATOM   5870 N ND1  . HIS   B 1 138 ? 31.064 -32.507 1.200   1.00 19.74 ?  138 HIS   B ND1  1 
ATOM   5871 C CD2  . HIS   B 1 138 ? 32.613 -31.586 2.434   1.00 18.92 ?  138 HIS   B CD2  1 
ATOM   5872 C CE1  . HIS   B 1 138 ? 30.487 -31.543 1.894   1.00 19.66 ?  138 HIS   B CE1  1 
ATOM   5873 N NE2  . HIS   B 1 138 ? 31.404 -30.970 2.652   1.00 19.06 ?  138 HIS   B NE2  1 
ATOM   5874 H H    . HIS   B 1 138 ? 34.870 -34.761 -0.553  1.00 19.24 ?  138 HIS   B H    1 
ATOM   5875 H HA   . HIS   B 1 138 ? 32.601 -33.523 -1.011  1.00 19.88 ?  138 HIS   B HA   1 
ATOM   5876 H HB2  . HIS   B 1 138 ? 33.005 -34.435 1.077   1.00 21.16 ?  138 HIS   B HB2  1 
ATOM   5877 H HB3  . HIS   B 1 138 ? 34.211 -33.426 1.303   1.00 21.16 ?  138 HIS   B HB3  1 
ATOM   5878 H HD1  . HIS   B 1 138 ? 30.667 -33.023 0.634   1.00 23.68 ?  138 HIS   B HD1  1 
ATOM   5879 H HD2  . HIS   B 1 138 ? 33.415 -31.374 2.845   1.00 22.70 ?  138 HIS   B HD2  1 
ATOM   5880 H HE1  . HIS   B 1 138 ? 29.582 -31.315 1.855   1.00 23.59 ?  138 HIS   B HE1  1 
ATOM   5881 N N    . SER   B 1 139 ? 35.181 -31.628 -0.831  1.00 14.83 ?  139 SER   B N    1 
ATOM   5882 C CA   . SER   B 1 139 ? 35.619 -30.277 -1.151  1.00 14.30 ?  139 SER   B CA   1 
ATOM   5883 C C    . SER   B 1 139 ? 35.286 -29.926 -2.594  1.00 13.59 ?  139 SER   B C    1 
ATOM   5884 O O    . SER   B 1 139 ? 34.843 -28.809 -2.878  1.00 13.95 ?  139 SER   B O    1 
ATOM   5885 C CB   . SER   B 1 139 ? 37.111 -30.134 -0.875  1.00 14.60 ?  139 SER   B CB   1 
ATOM   5886 O OG   . SER   B 1 139 ? 37.517 -28.802 -1.143  1.00 15.02 ?  139 SER   B OG   1 
ATOM   5887 H H    . SER   B 1 139 ? 35.803 -32.170 -0.600  1.00 17.80 ?  139 SER   B H    1 
ATOM   5888 H HA   . SER   B 1 139 ? 35.147 -29.654 -0.582  1.00 17.16 ?  139 SER   B HA   1 
ATOM   5889 H HB2  . SER   B 1 139 ? 37.283 -30.341 0.061   1.00 17.52 ?  139 SER   B HB2  1 
ATOM   5890 H HB3  . SER   B 1 139 ? 37.606 -30.745 -1.444  1.00 17.52 ?  139 SER   B HB3  1 
ATOM   5891 H HG   . SER   B 1 139 ? 38.344 -28.722 -0.987  1.00 18.02 ?  139 SER   B HG   1 
ATOM   5892 N N    . LEU   B 1 140 ? 35.471 -30.872 -3.516  1.00 13.50 ?  140 LEU   B N    1 
ATOM   5893 C CA   . LEU   B 1 140 ? 35.107 -30.624 -4.905  1.00 13.61 ?  140 LEU   B CA   1 
ATOM   5894 C C    . LEU   B 1 140 ? 33.603 -30.394 -5.039  1.00 13.92 ?  140 LEU   B C    1 
ATOM   5895 O O    . LEU   B 1 140 ? 33.168 -29.503 -5.776  1.00 13.74 ?  140 LEU   B O    1 
ATOM   5896 C CB   . LEU   B 1 140 ? 35.578 -31.790 -5.778  1.00 13.98 ?  140 LEU   B CB   1 
ATOM   5897 C CG   . LEU   B 1 140 ? 35.216 -31.678 -7.250  1.00 14.00 ?  140 LEU   B CG   1 
ATOM   5898 C CD1  . LEU   B 1 140 ? 35.769 -30.402 -7.845  1.00 14.84 ?  140 LEU   B CD1  1 
ATOM   5899 C CD2  . LEU   B 1 140 ? 35.699 -32.907 -7.999  1.00 14.93 ?  140 LEU   B CD2  1 
ATOM   5900 H H    . LEU   B 1 140 ? 35.801 -31.650 -3.367  1.00 16.20 ?  140 LEU   B H    1 
ATOM   5901 H HA   . LEU   B 1 140 ? 35.565 -29.822 -5.210  1.00 16.33 ?  140 LEU   B HA   1 
ATOM   5902 H HB2  . LEU   B 1 140 ? 36.548 -31.848 -5.724  1.00 16.77 ?  140 LEU   B HB2  1 
ATOM   5903 H HB3  . LEU   B 1 140 ? 35.185 -32.608 -5.445  1.00 16.77 ?  140 LEU   B HB3  1 
ATOM   5904 H HG   . LEU   B 1 140 ? 34.250 -31.643 -7.330  1.00 16.80 ?  140 LEU   B HG   1 
ATOM   5905 H HD11 . LEU   B 1 140 ? 35.660 -30.433 -8.807  1.00 17.80 ?  140 LEU   B HD11 1 
ATOM   5906 H HD12 . LEU   B 1 140 ? 35.275 -29.645 -7.483  1.00 17.80 ?  140 LEU   B HD12 1 
ATOM   5907 H HD13 . LEU   B 1 140 ? 36.705 -30.327 -7.616  1.00 17.80 ?  140 LEU   B HD13 1 
ATOM   5908 H HD21 . LEU   B 1 140 ? 35.451 -32.815 -8.933  1.00 17.91 ?  140 LEU   B HD21 1 
ATOM   5909 H HD22 . LEU   B 1 140 ? 36.657 -32.971 -7.910  1.00 17.91 ?  140 LEU   B HD22 1 
ATOM   5910 H HD23 . LEU   B 1 140 ? 35.269 -33.687 -7.618  1.00 17.91 ?  140 LEU   B HD23 1 
ATOM   5911 N N    . ARG   B 1 141 ? 32.798 -31.187 -4.325  1.00 13.95 ?  141 ARG   B N    1 
ATOM   5912 C CA   . ARG   B 1 141 ? 31.348 -31.012 -4.305  1.00 14.78 ?  141 ARG   B CA   1 
ATOM   5913 C C    . ARG   B 1 141 ? 30.970 -29.600 -3.877  1.00 14.64 ?  141 ARG   B C    1 
ATOM   5914 O O    . ARG   B 1 141 ? 30.172 -28.922 -4.541  1.00 14.66 ?  141 ARG   B O    1 
ATOM   5915 C CB   . ARG   B 1 141 ? 30.758 -32.044 -3.332  1.00 16.18 ?  141 ARG   B CB   1 
ATOM   5916 C CG   . ARG   B 1 141 ? 29.292 -31.919 -3.007  1.00 18.15 ?  141 ARG   B CG   1 
ATOM   5917 C CD   . ARG   B 1 141 ? 28.481 -32.555 -4.072  1.00 19.92 ?  141 ARG   B CD   1 
ATOM   5918 N NE   . ARG   B 1 141 ? 28.220 -31.646 -5.175  1.00 20.15 ?  141 ARG   B NE   1 
ATOM   5919 C CZ   . ARG   B 1 141 ? 28.217 -31.990 -6.455  1.00 20.00 ?  141 ARG   B CZ   1 
ATOM   5920 N NH1  . ARG   B 1 141 ? 28.652 -33.176 -6.857  1.00 19.75 ?  141 ARG   B NH1  1 
ATOM   5921 N NH2  . ARG   B 1 141 ? 27.759 -31.123 -7.355  1.00 20.89 ?  141 ARG   B NH2  1 
ATOM   5922 H H    . ARG   B 1 141 ? 33.080 -31.834 -3.839  1.00 16.73 ?  141 ARG   B H    1 
ATOM   5923 H HA   . ARG   B 1 141 ? 30.987 -31.172 -5.187  1.00 17.73 ?  141 ARG   B HA   1 
ATOM   5924 H HB2  . ARG   B 1 141 ? 30.907 -32.928 -3.707  1.00 19.41 ?  141 ARG   B HB2  1 
ATOM   5925 H HB3  . ARG   B 1 141 ? 31.242 -31.977 -2.495  1.00 19.41 ?  141 ARG   B HB3  1 
ATOM   5926 H HG2  . ARG   B 1 141 ? 29.116 -32.370 -2.169  1.00 21.78 ?  141 ARG   B HG2  1 
ATOM   5927 H HG3  . ARG   B 1 141 ? 29.041 -30.982 -2.942  1.00 21.78 ?  141 ARG   B HG3  1 
ATOM   5928 H HD2  . ARG   B 1 141 ? 28.955 -33.335 -4.411  1.00 23.90 ?  141 ARG   B HD2  1 
ATOM   5929 H HD3  . ARG   B 1 141 ? 27.634 -32.831 -3.697  1.00 23.90 ?  141 ARG   B HD3  1 
ATOM   5930 H HE   . ARG   B 1 141 ? 28.034 -30.828 -4.979  1.00 24.18 ?  141 ARG   B HE   1 
ATOM   5931 H HH11 . ARG   B 1 141 ? 28.944 -33.748 -6.288  1.00 23.70 ?  141 ARG   B HH11 1 
ATOM   5932 H HH12 . ARG   B 1 141 ? 28.652 -33.366 -7.693  1.00 23.70 ?  141 ARG   B HH12 1 
ATOM   5933 H HH21 . ARG   B 1 141 ? 27.480 -30.345 -7.104  1.00 25.07 ?  141 ARG   B HH21 1 
ATOM   5934 H HH22 . ARG   B 1 141 ? 27.771 -31.320 -8.192  1.00 25.07 ?  141 ARG   B HH22 1 
ATOM   5935 N N    . VAL   B 1 142 ? 31.517 -29.147 -2.750  1.00 14.35 ?  142 VAL   B N    1 
ATOM   5936 C CA   . VAL   B 1 142 ? 31.178 -27.816 -2.268  1.00 13.86 ?  142 VAL   B CA   1 
ATOM   5937 C C    . VAL   B 1 142 ? 31.654 -26.760 -3.258  1.00 13.74 ?  142 VAL   B C    1 
ATOM   5938 O O    . VAL   B 1 142 ? 30.953 -25.774 -3.520  1.00 14.26 ?  142 VAL   B O    1 
ATOM   5939 C CB   . VAL   B 1 142 ? 31.717 -27.592 -0.842  1.00 14.40 ?  142 VAL   B CB   1 
ATOM   5940 C CG1  . VAL   B 1 142 ? 31.408 -26.168 -0.368  1.00 14.35 ?  142 VAL   B CG1  1 
ATOM   5941 C CG2  . VAL   B 1 142 ? 31.129 -28.615 0.120   1.00 15.34 ?  142 VAL   B CG2  1 
ATOM   5942 H H    . VAL   B 1 142 ? 32.076 -29.581 -2.255  1.00 17.22 ?  142 VAL   B H    1 
ATOM   5943 H HA   . VAL   B 1 142 ? 30.214 -27.748 -2.217  1.00 16.64 ?  142 VAL   B HA   1 
ATOM   5944 H HB   . VAL   B 1 142 ? 32.679 -27.703 -0.843  1.00 17.27 ?  142 VAL   B HB   1 
ATOM   5945 H HG11 . VAL   B 1 142 ? 31.591 -26.107 0.581   1.00 17.22 ?  142 VAL   B HG11 1 
ATOM   5946 H HG12 . VAL   B 1 142 ? 31.975 -25.546 -0.853  1.00 17.22 ?  142 VAL   B HG12 1 
ATOM   5947 H HG13 . VAL   B 1 142 ? 30.477 -25.974 -0.542  1.00 17.22 ?  142 VAL   B HG13 1 
ATOM   5948 H HG21 . VAL   B 1 142 ? 31.443 -28.425 1.017   1.00 18.41 ?  142 VAL   B HG21 1 
ATOM   5949 H HG22 . VAL   B 1 142 ? 30.159 -28.555 0.090   1.00 18.41 ?  142 VAL   B HG22 1 
ATOM   5950 H HG23 . VAL   B 1 142 ? 31.412 -29.502 -0.150  1.00 18.41 ?  142 VAL   B HG23 1 
ATOM   5951 N N    . CYS   B 1 143 ? 32.837 -26.960 -3.844  1.00 13.14 ?  143 CYS   B N    1 
ATOM   5952 C CA   . CYS   B 1 143 ? 33.331 -26.017 -4.843  1.00 13.12 ?  143 CYS   B CA   1 
ATOM   5953 C C    . CYS   B 1 143 ? 32.333 -25.871 -5.987  1.00 13.13 ?  143 CYS   B C    1 
ATOM   5954 O O    . CYS   B 1 143 ? 31.925 -24.759 -6.343  1.00 13.56 ?  143 CYS   B O    1 
ATOM   5955 C CB   . CYS   B 1 143 ? 34.690 -26.490 -5.366  1.00 13.58 ?  143 CYS   B CB   1 
ATOM   5956 S SG   . CYS   B 1 143 ? 35.439 -25.398 -6.592  1.00 13.46 ?  143 CYS   B SG   1 
ATOM   5957 H H    . CYS   B 1 143 ? 33.362 -27.616 -3.681  1.00 15.77 ?  143 CYS   B H    1 
ATOM   5958 H HA   . CYS   B 1 143 ? 33.450 -25.145 -4.436  1.00 15.74 ?  143 CYS   B HA   1 
ATOM   5959 H HB2  . CYS   B 1 143 ? 35.307 -26.561 -4.621  1.00 16.29 ?  143 CYS   B HB2  1 
ATOM   5960 H HB3  . CYS   B 1 143 ? 34.579 -27.358 -5.776  1.00 16.29 ?  143 CYS   B HB3  1 
ATOM   5961 H HG   . CYS   B 1 143 ? 36.515 -25.832 -6.902  1.00 16.15 ?  143 CYS   B HG   1 
ATOM   5962 N N    . VAL   B 1 144 ? 31.927 -26.993 -6.579  1.00 13.76 ?  144 VAL   B N    1 
ATOM   5963 C CA   . VAL   B 1 144 ? 31.021 -26.934 -7.723  1.00 14.69 ?  144 VAL   B CA   1 
ATOM   5964 C C    . VAL   B 1 144 ? 29.679 -26.326 -7.345  1.00 14.78 ?  144 VAL   B C    1 
ATOM   5965 O O    . VAL   B 1 144 ? 29.062 -25.614 -8.149  1.00 16.12 ?  144 VAL   B O    1 
ATOM   5966 C CB   . VAL   B 1 144 ? 30.864 -28.341 -8.314  1.00 17.31 ?  144 VAL   B CB   1 
ATOM   5967 C CG1  . VAL   B 1 144 ? 29.580 -28.462 -9.131  1.00 19.78 ?  144 VAL   B CG1  1 
ATOM   5968 C CG2  . VAL   B 1 144 ? 32.104 -28.724 -9.127  1.00 17.56 ?  144 VAL   B CG2  1 
ATOM   5969 H H    . VAL   B 1 144 ? 32.162 -27.788 -6.347  1.00 16.51 ?  144 VAL   B H    1 
ATOM   5970 H HA   . VAL   B 1 144 ? 31.411 -26.372 -8.405  1.00 17.63 ?  144 VAL   B HA   1 
ATOM   5971 H HB   . VAL   B 1 144 ? 30.800 -28.977 -7.583  1.00 20.76 ?  144 VAL   B HB   1 
ATOM   5972 H HG11 . VAL   B 1 144 ? 29.648 -29.247 -9.702  1.00 23.74 ?  144 VAL   B HG11 1 
ATOM   5973 H HG12 . VAL   B 1 144 ? 28.830 -28.565 -8.526  1.00 23.74 ?  144 VAL   B HG12 1 
ATOM   5974 H HG13 . VAL   B 1 144 ? 29.474 -27.670 -9.674  1.00 23.74 ?  144 VAL   B HG13 1 
ATOM   5975 H HG21 . VAL   B 1 144 ? 31.985 -29.617 -9.486  1.00 21.07 ?  144 VAL   B HG21 1 
ATOM   5976 H HG22 . VAL   B 1 144 ? 32.210 -28.088 -9.854  1.00 21.07 ?  144 VAL   B HG22 1 
ATOM   5977 H HG23 . VAL   B 1 144 ? 32.880 -28.698 -8.549  1.00 21.07 ?  144 VAL   B HG23 1 
ATOM   5978 N N    . ASP   B 1 145 ? 29.220 -26.564 -6.122  1.00 14.91 ?  145 ASP   B N    1 
ATOM   5979 C CA   . ASP   B 1 145 ? 27.909 -26.102 -5.686  1.00 15.43 ?  145 ASP   B CA   1 
ATOM   5980 C C    . ASP   B 1 145 ? 27.932 -24.677 -5.145  1.00 15.07 ?  145 ASP   B C    1 
ATOM   5981 O O    . ASP   B 1 145 ? 26.869 -24.133 -4.821  1.00 17.05 ?  145 ASP   B O    1 
ATOM   5982 C CB   . ASP   B 1 145 ? 27.334 -27.029 -4.605  1.00 17.02 ?  145 ASP   B CB   1 
ATOM   5983 C CG   . ASP   B 1 145 ? 26.960 -28.398 -5.124  1.00 18.51 ?  145 ASP   B CG   1 
ATOM   5984 O OD1  . ASP   B 1 145 ? 26.850 -28.578 -6.353  1.00 19.16 ?  145 ASP   B OD1  1 
ATOM   5985 O OD2  . ASP   B 1 145 ? 26.762 -29.287 -4.277  1.00 20.72 -1 145 ASP   B OD2  1 
ATOM   5986 H H    . ASP   B 1 145 ? 29.660 -26.981 -5.517  1.00 17.89 ?  145 ASP   B H    1 
ATOM   5987 H HA   . ASP   B 1 145 ? 27.310 -26.101 -6.445  1.00 18.52 ?  145 ASP   B HA   1 
ATOM   5988 H HB2  . ASP   B 1 145 ? 27.991 -27.150 -3.913  1.00 20.42 ?  145 ASP   B HB2  1 
ATOM   5989 H HB3  . ASP   B 1 145 ? 26.531 -26.620 -4.244  1.00 20.42 ?  145 ASP   B HB3  1 
ATOM   5990 N N    . THR   B 1 146 ? 29.109 -24.056 -5.038  1.00 13.67 ?  146 THR   B N    1 
ATOM   5991 C CA   . THR   B 1 146 ? 29.247 -22.735 -4.432  1.00 13.09 ?  146 THR   B CA   1 
ATOM   5992 C C    . THR   B 1 146 ? 29.875 -21.707 -5.354  1.00 12.93 ?  146 THR   B C    1 
ATOM   5993 O O    . THR   B 1 146 ? 29.419 -20.549 -5.398  1.00 13.40 ?  146 THR   B O    1 
ATOM   5994 C CB   . THR   B 1 146 ? 30.071 -22.839 -3.142  1.00 13.61 ?  146 THR   B CB   1 
ATOM   5995 O OG1  . THR   B 1 146 ? 29.493 -23.832 -2.283  1.00 13.67 ?  146 THR   B OG1  1 
ATOM   5996 C CG2  . THR   B 1 146 ? 30.141 -21.498 -2.422  1.00 13.72 ?  146 THR   B CG2  1 
ATOM   5997 H H    . THR   B 1 146 ? 29.857 -24.385 -5.320  1.00 16.40 ?  146 THR   B H    1 
ATOM   5998 H HA   . THR   B 1 146 ? 28.371 -22.410 -4.194  1.00 15.71 ?  146 THR   B HA   1 
ATOM   5999 H HB   . THR   B 1 146 ? 30.978 -23.099 -3.365  1.00 16.32 ?  146 THR   B HB   1 
ATOM   6000 H HG1  . THR   B 1 146 ? 29.530 -24.588 -2.660  1.00 16.40 ?  146 THR   B HG1  1 
ATOM   6001 H HG21 . THR   B 1 146 ? 30.491 -21.620 -1.528  1.00 16.46 ?  146 THR   B HG21 1 
ATOM   6002 H HG22 . THR   B 1 146 ? 30.724 -20.890 -2.908  1.00 16.46 ?  146 THR   B HG22 1 
ATOM   6003 H HG23 . THR   B 1 146 ? 29.256 -21.106 -2.366  1.00 16.46 ?  146 THR   B HG23 1 
ATOM   6004 N N    . VAL   B 1 147 ? 30.940 -22.079 -6.057  1.00 12.65 ?  147 VAL   B N    1 
ATOM   6005 C CA   . VAL   B 1 147 ? 31.662 -21.133 -6.894  1.00 12.40 ?  147 VAL   B CA   1 
ATOM   6006 C C    . VAL   B 1 147 ? 30.929 -20.999 -8.217  1.00 12.89 ?  147 VAL   B C    1 
ATOM   6007 O O    . VAL   B 1 147 ? 30.562 -22.003 -8.842  1.00 13.84 ?  147 VAL   B O    1 
ATOM   6008 C CB   . VAL   B 1 147 ? 33.117 -21.587 -7.097  1.00 12.68 ?  147 VAL   B CB   1 
ATOM   6009 C CG1  . VAL   B 1 147 ? 33.880 -20.555 -7.903  1.00 12.83 ?  147 VAL   B CG1  1 
ATOM   6010 C CG2  . VAL   B 1 147 ? 33.788 -21.806 -5.756  1.00 12.80 ?  147 VAL   B CG2  1 
ATOM   6011 H H    . VAL   B 1 147 ? 31.261 -22.879 -6.073  1.00 15.18 ?  147 VAL   B H    1 
ATOM   6012 H HA   . VAL   B 1 147 ? 31.675 -20.266 -6.466  1.00 14.88 ?  147 VAL   B HA   1 
ATOM   6013 H HB   . VAL   B 1 147 ? 33.133 -22.426 -7.588  1.00 15.22 ?  147 VAL   B HB   1 
ATOM   6014 H HG11 . VAL   B 1 147 ? 34.824 -20.781 -7.894  1.00 15.39 ?  147 VAL   B HG11 1 
ATOM   6015 H HG12 . VAL   B 1 147 ? 33.550 -20.552 -8.814  1.00 15.39 ?  147 VAL   B HG12 1 
ATOM   6016 H HG13 . VAL   B 1 147 ? 33.748 -19.682 -7.499  1.00 15.39 ?  147 VAL   B HG13 1 
ATOM   6017 H HG21 . VAL   B 1 147 ? 34.732 -21.990 -5.900  1.00 15.36 ?  147 VAL   B HG21 1 
ATOM   6018 H HG22 . VAL   B 1 147 ? 33.687 -21.005 -5.220  1.00 15.36 ?  147 VAL   B HG22 1 
ATOM   6019 H HG23 . VAL   B 1 147 ? 33.370 -22.559 -5.312  1.00 15.36 ?  147 VAL   B HG23 1 
ATOM   6020 N N    . ARG   B 1 148 ? 30.727 -19.752 -8.643  1.00 12.90 ?  148 ARG   B N    1 
ATOM   6021 C CA   . ARG   B 1 148 ? 30.098 -19.436 -9.914  1.00 13.23 ?  148 ARG   B CA   1 
ATOM   6022 C C    . ARG   B 1 148 ? 31.051 -18.760 -10.886 1.00 13.18 ?  148 ARG   B C    1 
ATOM   6023 O O    . ARG   B 1 148 ? 30.764 -18.736 -12.086 1.00 14.50 ?  148 ARG   B O    1 
ATOM   6024 C CB   . ARG   B 1 148 ? 28.864 -18.545 -9.691  1.00 13.50 ?  148 ARG   B CB   1 
ATOM   6025 C CG   . ARG   B 1 148 ? 27.779 -19.255 -8.888  1.00 14.38 ?  148 ARG   B CG   1 
ATOM   6026 C CD   . ARG   B 1 148 ? 26.575 -18.362 -8.568  1.00 15.12 ?  148 ARG   B CD   1 
ATOM   6027 N NE   . ARG   B 1 148 ? 26.958 -17.159 -7.838  1.00 15.03 ?  148 ARG   B NE   1 
ATOM   6028 C CZ   . ARG   B 1 148 ? 27.265 -17.123 -6.547  1.00 14.23 ?  148 ARG   B CZ   1 
ATOM   6029 N NH1  . ARG   B 1 148 ? 27.198 -18.206 -5.785  1.00 13.90 ?  148 ARG   B NH1  1 
ATOM   6030 N NH2  . ARG   B 1 148 ? 27.662 -15.972 -6.008  1.00 14.31 ?  148 ARG   B NH2  1 
ATOM   6031 H H    . ARG   B 1 148 ? 30.959 -19.056 -8.195  1.00 15.47 ?  148 ARG   B H    1 
ATOM   6032 H HA   . ARG   B 1 148 ? 29.796 -20.261 -10.324 1.00 15.87 ?  148 ARG   B HA   1 
ATOM   6033 H HB2  . ARG   B 1 148 ? 29.131 -17.752 -9.201  1.00 16.20 ?  148 ARG   B HB2  1 
ATOM   6034 H HB3  . ARG   B 1 148 ? 28.492 -18.300 -10.551 1.00 16.20 ?  148 ARG   B HB3  1 
ATOM   6035 H HG2  . ARG   B 1 148 ? 27.457 -20.016 -9.399  1.00 17.25 ?  148 ARG   B HG2  1 
ATOM   6036 H HG3  . ARG   B 1 148 ? 28.156 -19.561 -8.048  1.00 17.25 ?  148 ARG   B HG3  1 
ATOM   6037 H HD2  . ARG   B 1 148 ? 26.151 -18.090 -9.395  1.00 18.15 ?  148 ARG   B HD2  1 
ATOM   6038 H HD3  . ARG   B 1 148 ? 25.945 -18.861 -8.020  1.00 18.15 ?  148 ARG   B HD3  1 
ATOM   6039 H HE   . ARG   B 1 148 ? 26.996 -16.426 -8.276  1.00 18.04 ?  148 ARG   B HE   1 
ATOM   6040 H HH11 . ARG   B 1 148 ? 26.938 -18.957 -6.114  1.00 16.67 ?  148 ARG   B HH11 1 
ATOM   6041 H HH12 . ARG   B 1 148 ? 27.394 -18.156 -4.946  1.00 16.67 ?  148 ARG   B HH12 1 
ATOM   6042 H HH21 . ARG   B 1 148 ? 27.715 -15.265 -6.497  1.00 17.17 ?  148 ARG   B HH21 1 
ATOM   6043 H HH22 . ARG   B 1 148 ? 27.864 -15.932 -5.174  1.00 17.17 ?  148 ARG   B HH22 1 
ATOM   6044 N N    . THR   B 1 149 ? 32.158 -18.205 -10.398 1.00 12.94 ?  149 THR   B N    1 
ATOM   6045 C CA   . THR   B 1 149 ? 33.200 -17.644 -11.243 1.00 12.90 ?  149 THR   B CA   1 
ATOM   6046 C C    . THR   B 1 149 ? 34.087 -18.783 -11.750 1.00 12.53 ?  149 THR   B C    1 
ATOM   6047 O O    . THR   B 1 149 ? 33.894 -19.953 -11.409 1.00 13.24 ?  149 THR   B O    1 
ATOM   6048 C CB   . THR   B 1 149 ? 33.970 -16.590 -10.460 1.00 13.09 ?  149 THR   B CB   1 
ATOM   6049 O OG1  . THR   B 1 149 ? 34.428 -17.186 -9.245  1.00 13.08 ?  149 THR   B OG1  1 
ATOM   6050 C CG2  . THR   B 1 149 ? 33.080 -15.381 -10.162 1.00 13.95 ?  149 THR   B CG2  1 
ATOM   6051 H H    . THR   B 1 149 ? 32.324 -18.135 -9.558  1.00 15.52 ?  149 THR   B H    1 
ATOM   6052 H HA   . THR   B 1 149 ? 32.792 -17.210 -12.009 1.00 15.47 ?  149 THR   B HA   1 
ATOM   6053 H HB   . THR   B 1 149 ? 34.730 -16.295 -10.980 1.00 15.70 ?  149 THR   B HB   1 
ATOM   6054 H HG1  . THR   B 1 149 ? 34.848 -16.612 -8.786  1.00 15.70 ?  149 THR   B HG1  1 
ATOM   6055 H HG21 . THR   B 1 149 ? 33.586 -14.710 -9.675  1.00 16.74 ?  149 THR   B HG21 1 
ATOM   6056 H HG22 . THR   B 1 149 ? 32.761 -14.991 -10.993 1.00 16.74 ?  149 THR   B HG22 1 
ATOM   6057 H HG23 . THR   B 1 149 ? 32.317 -15.649 -9.628  1.00 16.74 ?  149 THR   B HG23 1 
ATOM   6058 N N    . ASN   B 1 150 ? 35.051 -18.464 -12.601 1.00 12.76 ?  150 ASN   B N    1 
ATOM   6059 C CA   . ASN   B 1 150 ? 35.819 -19.491 -13.296 1.00 13.35 ?  150 ASN   B CA   1 
ATOM   6060 C C    . ASN   B 1 150 ? 36.983 -19.940 -12.423 1.00 13.04 ?  150 ASN   B C    1 
ATOM   6061 O O    . ASN   B 1 150 ? 37.916 -19.173 -12.169 1.00 13.79 ?  150 ASN   B O    1 
ATOM   6062 C CB   . ASN   B 1 150 ? 36.284 -18.965 -14.646 1.00 15.19 ?  150 ASN   B CB   1 
ATOM   6063 C CG   . ASN   B 1 150 ? 35.134 -18.745 -15.585 1.00 17.62 ?  150 ASN   B CG   1 
ATOM   6064 O OD1  . ASN   B 1 150 ? 34.244 -19.582 -15.682 1.00 18.93 ?  150 ASN   B OD1  1 
ATOM   6065 N ND2  . ASN   B 1 150 ? 35.115 -17.603 -16.250 1.00 19.46 ?  150 ASN   B ND2  1 
ATOM   6066 H H    . ASN   B 1 150 ? 35.286 -17.655 -12.792 1.00 15.31 ?  150 ASN   B H    1 
ATOM   6067 H HA   . ASN   B 1 150 ? 35.239 -20.258 -13.456 1.00 16.02 ?  150 ASN   B HA   1 
ATOM   6068 H HB2  . ASN   B 1 150 ? 36.735 -18.116 -14.517 1.00 18.23 ?  150 ASN   B HB2  1 
ATOM   6069 H HB3  . ASN   B 1 150 ? 36.883 -19.608 -15.049 1.00 18.23 ?  150 ASN   B HB3  1 
ATOM   6070 H HD21 . ASN   B 1 150 ? 34.472 -17.432 -16.798 1.00 23.35 ?  150 ASN   B HD21 1 
ATOM   6071 H HD22 . ASN   B 1 150 ? 35.751 -17.031 -16.147 1.00 23.35 ?  150 ASN   B HD22 1 
ATOM   6072 N N    . VAL   B 1 151 ? 36.937 -21.186 -11.967 1.00 12.44 ?  151 VAL   B N    1 
ATOM   6073 C CA   . VAL   B 1 151 ? 37.955 -21.716 -11.076 1.00 12.58 ?  151 VAL   B CA   1 
ATOM   6074 C C    . VAL   B 1 151 ? 38.663 -22.888 -11.747 1.00 12.40 ?  151 VAL   B C    1 
ATOM   6075 O O    . VAL   B 1 151 ? 38.020 -23.824 -12.249 1.00 13.38 ?  151 VAL   B O    1 
ATOM   6076 C CB   . VAL   B 1 151 ? 37.399 -22.049 -9.677  1.00 13.84 ?  151 VAL   B CB   1 
ATOM   6077 C CG1  . VAL   B 1 151 ? 36.223 -23.039 -9.752  1.00 14.89 ?  151 VAL   B CG1  1 
ATOM   6078 C CG2  . VAL   B 1 151 ? 38.512 -22.549 -8.768  1.00 14.57 ?  151 VAL   B CG2  1 
ATOM   6079 H H    . VAL   B 1 151 ? 36.311 -21.750 -12.164 1.00 14.93 ?  151 VAL   B H    1 
ATOM   6080 H HA   . VAL   B 1 151 ? 38.623 -21.020 -10.949 1.00 15.09 ?  151 VAL   B HA   1 
ATOM   6081 H HB   . VAL   B 1 151 ? 37.060 -21.226 -9.285  1.00 16.60 ?  151 VAL   B HB   1 
ATOM   6082 H HG11 . VAL   B 1 151 ? 35.911 -23.228 -8.852  1.00 17.86 ?  151 VAL   B HG11 1 
ATOM   6083 H HG12 . VAL   B 1 151 ? 35.503 -22.638 -10.270 1.00 17.86 ?  151 VAL   B HG12 1 
ATOM   6084 H HG13 . VAL   B 1 151 ? 36.520 -23.856 -10.178 1.00 17.86 ?  151 VAL   B HG13 1 
ATOM   6085 H HG21 . VAL   B 1 151 ? 38.170 -22.615 -7.862  1.00 17.48 ?  151 VAL   B HG21 1 
ATOM   6086 H HG22 . VAL   B 1 151 ? 38.805 -23.420 -9.074  1.00 17.48 ?  151 VAL   B HG22 1 
ATOM   6087 H HG23 . VAL   B 1 151 ? 39.251 -21.920 -8.795  1.00 17.48 ?  151 VAL   B HG23 1 
ATOM   6088 N N    . TYR   B 1 152 ? 39.998 -22.801 -11.769 1.00 11.98 ?  152 TYR   B N    1 
ATOM   6089 C CA   . TYR   B 1 152 ? 40.900 -23.785 -12.348 1.00 12.33 ?  152 TYR   B CA   1 
ATOM   6090 C C    . TYR   B 1 152 ? 41.621 -24.458 -11.184 1.00 11.77 ?  152 TYR   B C    1 
ATOM   6091 O O    . TYR   B 1 152 ? 42.470 -23.842 -10.530 1.00 11.85 ?  152 TYR   B O    1 
ATOM   6092 C CB   . TYR   B 1 152 ? 41.871 -23.078 -13.298 1.00 13.13 ?  152 TYR   B CB   1 
ATOM   6093 C CG   . TYR   B 1 152 ? 41.191 -22.614 -14.565 1.00 13.85 ?  152 TYR   B CG   1 
ATOM   6094 C CD1  . TYR   B 1 152 ? 40.512 -21.399 -14.624 1.00 14.19 ?  152 TYR   B CD1  1 
ATOM   6095 C CD2  . TYR   B 1 152 ? 41.198 -23.416 -15.696 1.00 15.03 ?  152 TYR   B CD2  1 
ATOM   6096 C CE1  . TYR   B 1 152 ? 39.870 -21.000 -15.781 1.00 15.22 ?  152 TYR   B CE1  1 
ATOM   6097 C CE2  . TYR   B 1 152 ? 40.562 -23.029 -16.851 1.00 15.91 ?  152 TYR   B CE2  1 
ATOM   6098 C CZ   . TYR   B 1 152 ? 39.904 -21.816 -16.894 1.00 15.79 ?  152 TYR   B CZ   1 
ATOM   6099 O OH   . TYR   B 1 152 ? 39.275 -21.444 -18.058 1.00 18.35 ?  152 TYR   B OH   1 
ATOM   6100 H H    . TYR   B 1 152 ? 40.430 -22.134 -11.424 1.00 14.38 ?  152 TYR   B H    1 
ATOM   6101 H HA   . TYR   B 1 152 ? 40.392 -24.451 -12.844 1.00 14.79 ?  152 TYR   B HA   1 
ATOM   6102 H HB2  . TYR   B 1 152 ? 42.238 -22.301 -12.849 1.00 15.76 ?  152 TYR   B HB2  1 
ATOM   6103 H HB3  . TYR   B 1 152 ? 42.583 -23.691 -13.538 1.00 15.76 ?  152 TYR   B HB3  1 
ATOM   6104 H HD1  . TYR   B 1 152 ? 40.485 -20.852 -13.871 1.00 17.02 ?  152 TYR   B HD1  1 
ATOM   6105 H HD2  . TYR   B 1 152 ? 41.641 -24.237 -15.672 1.00 18.03 ?  152 TYR   B HD2  1 
ATOM   6106 H HE1  . TYR   B 1 152 ? 39.422 -20.188 -15.811 1.00 18.26 ?  152 TYR   B HE1  1 
ATOM   6107 H HE2  . TYR   B 1 152 ? 40.584 -23.577 -17.602 1.00 19.09 ?  152 TYR   B HE2  1 
ATOM   6108 H HH   . TYR   B 1 152 ? 38.905 -20.696 -17.952 1.00 22.02 ?  152 TYR   B HH   1 
ATOM   6109 N N    . LEU   B 1 153 ? 41.257 -25.713 -10.916 1.00 11.73 ?  153 LEU   B N    1 
ATOM   6110 C CA   . LEU   B 1 153 ? 41.764 -26.466 -9.778  1.00 11.76 ?  153 LEU   B CA   1 
ATOM   6111 C C    . LEU   B 1 153 ? 42.993 -27.269 -10.173 1.00 12.37 ?  153 LEU   B C    1 
ATOM   6112 O O    . LEU   B 1 153 ? 42.977 -27.994 -11.171 1.00 13.35 ?  153 LEU   B O    1 
ATOM   6113 C CB   . LEU   B 1 153 ? 40.679 -27.417 -9.264  1.00 12.30 ?  153 LEU   B CB   1 
ATOM   6114 C CG   . LEU   B 1 153 ? 39.425 -26.762 -8.686  1.00 13.07 ?  153 LEU   B CG   1 
ATOM   6115 C CD1  . LEU   B 1 153 ? 38.329 -27.805 -8.536  1.00 13.42 ?  153 LEU   B CD1  1 
ATOM   6116 C CD2  . LEU   B 1 153 ? 39.726 -26.107 -7.344  1.00 13.42 ?  153 LEU   B CD2  1 
ATOM   6117 H H    . LEU   B 1 153 ? 40.690 -26.161 -11.396 1.00 14.07 ?  153 LEU   B H    1 
ATOM   6118 H HA   . LEU   B 1 153 ? 41.994 -25.851 -9.069  1.00 14.11 ?  153 LEU   B HA   1 
ATOM   6119 H HB2  . LEU   B 1 153 ? 40.391 -27.982 -9.996  1.00 14.76 ?  153 LEU   B HB2  1 
ATOM   6120 H HB3  . LEU   B 1 153 ? 41.062 -27.966 -8.562  1.00 14.76 ?  153 LEU   B HB3  1 
ATOM   6121 H HG   . LEU   B 1 153 ? 39.112 -26.068 -9.291  1.00 15.68 ?  153 LEU   B HG   1 
ATOM   6122 H HD11 . LEU   B 1 153 ? 37.530 -27.372 -8.196  1.00 16.10 ?  153 LEU   B HD11 1 
ATOM   6123 H HD12 . LEU   B 1 153 ? 38.154 -28.194 -9.403  1.00 16.10 ?  153 LEU   B HD12 1 
ATOM   6124 H HD13 . LEU   B 1 153 ? 38.630 -28.483 -7.915  1.00 16.10 ?  153 LEU   B HD13 1 
ATOM   6125 H HD21 . LEU   B 1 153 ? 38.913 -25.727 -6.980  1.00 16.10 ?  153 LEU   B HD21 1 
ATOM   6126 H HD22 . LEU   B 1 153 ? 40.077 -26.780 -6.735  1.00 16.10 ?  153 LEU   B HD22 1 
ATOM   6127 H HD23 . LEU   B 1 153 ? 40.390 -25.407 -7.470  1.00 16.10 ?  153 LEU   B HD23 1 
ATOM   6128 N N    . ALA   B 1 154 ? 44.043 -27.160 -9.366  1.00 12.12 ?  154 ALA   B N    1 
ATOM   6129 C CA   . ALA   B 1 154 ? 45.274 -27.916 -9.547  1.00 13.34 ?  154 ALA   B CA   1 
ATOM   6130 C C    . ALA   B 1 154 ? 45.339 -28.997 -8.475  1.00 13.77 ?  154 ALA   B C    1 
ATOM   6131 O O    . ALA   B 1 154 ? 45.269 -28.700 -7.276  1.00 15.23 ?  154 ALA   B O    1 
ATOM   6132 C CB   . ALA   B 1 154 ? 46.497 -27.004 -9.473  1.00 14.24 ?  154 ALA   B CB   1 
ATOM   6133 H H    . ALA   B 1 154 ? 44.057 -26.636 -8.678  1.00 14.55 ?  154 ALA   B H    1 
ATOM   6134 H HA   . ALA   B 1 154 ? 45.265 -28.344 -10.410 1.00 16.01 ?  154 ALA   B HA   1 
ATOM   6135 H HB1  . ALA   B 1 154 ? 47.298 -27.535 -9.595  1.00 17.09 ?  154 ALA   B HB1  1 
ATOM   6136 H HB2  . ALA   B 1 154 ? 46.436 -26.333 -10.172 1.00 17.09 ?  154 ALA   B HB2  1 
ATOM   6137 H HB3  . ALA   B 1 154 ? 46.521 -26.567 -8.603  1.00 17.09 ?  154 ALA   B HB3  1 
ATOM   6138 N N    . VAL   B 1 155 ? 45.463 -30.244 -8.909  1.00 13.21 ?  155 VAL   B N    1 
ATOM   6139 C CA   . VAL   B 1 155 ? 45.570 -31.391 -8.015  1.00 13.34 ?  155 VAL   B CA   1 
ATOM   6140 C C    . VAL   B 1 155 ? 46.909 -32.067 -8.295  1.00 13.13 ?  155 VAL   B C    1 
ATOM   6141 O O    . VAL   B 1 155 ? 47.147 -32.558 -9.407  1.00 14.97 ?  155 VAL   B O    1 
ATOM   6142 C CB   . VAL   B 1 155 ? 44.409 -32.382 -8.211  1.00 14.66 ?  155 VAL   B CB   1 
ATOM   6143 C CG1  . VAL   B 1 155 ? 44.583 -33.582 -7.292  1.00 14.86 ?  155 VAL   B CG1  1 
ATOM   6144 C CG2  . VAL   B 1 155 ? 43.070 -31.696 -7.962  1.00 15.64 ?  155 VAL   B CG2  1 
ATOM   6145 H H    . VAL   B 1 155 ? 45.491 -30.455 -9.740  1.00 15.85 ?  155 VAL   B H    1 
ATOM   6146 H HA   . VAL   B 1 155 ? 45.560 -31.093 -7.093  1.00 16.01 ?  155 VAL   B HA   1 
ATOM   6147 H HB   . VAL   B 1 155 ? 44.413 -32.701 -9.127  1.00 17.59 ?  155 VAL   B HB   1 
ATOM   6148 H HG11 . VAL   B 1 155 ? 43.755 -34.086 -7.265  1.00 17.83 ?  155 VAL   B HG11 1 
ATOM   6149 H HG12 . VAL   B 1 155 ? 45.299 -34.145 -7.632  1.00 17.83 ?  155 VAL   B HG12 1 
ATOM   6150 H HG13 . VAL   B 1 155 ? 44.807 -33.269 -6.400  1.00 17.83 ?  155 VAL   B HG13 1 
ATOM   6151 H HG21 . VAL   B 1 155 ? 42.359 -32.349 -8.051  1.00 18.76 ?  155 VAL   B HG21 1 
ATOM   6152 H HG22 . VAL   B 1 155 ? 43.070 -31.326 -7.064  1.00 18.76 ?  155 VAL   B HG22 1 
ATOM   6153 H HG23 . VAL   B 1 155 ? 42.953 -30.987 -8.612  1.00 18.76 ?  155 VAL   B HG23 1 
ATOM   6154 N N    . PHE   B 1 156 ? 47.776 -32.107 -7.281  1.00 13.61 ?  156 PHE   B N    1 
ATOM   6155 C CA   . PHE   B 1 156 ? 49.153 -32.562 -7.486  1.00 14.81 ?  156 PHE   B CA   1 
ATOM   6156 C C    . PHE   B 1 156 ? 49.249 -34.062 -7.772  1.00 15.85 ?  156 PHE   B C    1 
ATOM   6157 O O    . PHE   B 1 156 ? 49.974 -34.487 -8.682  1.00 17.67 ?  156 PHE   B O    1 
ATOM   6158 C CB   . PHE   B 1 156 ? 49.983 -32.198 -6.256  1.00 15.24 ?  156 PHE   B CB   1 
ATOM   6159 C CG   . PHE   B 1 156 ? 51.405 -32.657 -6.318  1.00 15.45 ?  156 PHE   B CG   1 
ATOM   6160 C CD1  . PHE   B 1 156 ? 52.285 -32.107 -7.226  1.00 17.00 ?  156 PHE   B CD1  1 
ATOM   6161 C CD2  . PHE   B 1 156 ? 51.866 -33.623 -5.447  1.00 15.90 ?  156 PHE   B CD2  1 
ATOM   6162 C CE1  . PHE   B 1 156 ? 53.604 -32.517 -7.276  1.00 17.97 ?  156 PHE   B CE1  1 
ATOM   6163 C CE2  . PHE   B 1 156 ? 53.184 -34.039 -5.491  1.00 17.33 ?  156 PHE   B CE2  1 
ATOM   6164 C CZ   . PHE   B 1 156 ? 54.047 -33.488 -6.412  1.00 17.96 ?  156 PHE   B CZ   1 
ATOM   6165 H H    . PHE   B 1 156 ? 47.594 -31.875 -6.472  1.00 16.33 ?  156 PHE   B H    1 
ATOM   6166 H HA   . PHE   B 1 156 ? 49.527 -32.089 -8.243  1.00 17.77 ?  156 PHE   B HA   1 
ATOM   6167 H HB2  . PHE   B 1 156 ? 49.989 -31.232 -6.160  1.00 18.28 ?  156 PHE   B HB2  1 
ATOM   6168 H HB3  . PHE   B 1 156 ? 49.578 -32.602 -5.474  1.00 18.28 ?  156 PHE   B HB3  1 
ATOM   6169 H HD1  . PHE   B 1 156 ? 51.993 -31.445 -7.813  1.00 20.40 ?  156 PHE   B HD1  1 
ATOM   6170 H HD2  . PHE   B 1 156 ? 51.279 -34.004 -4.831  1.00 19.07 ?  156 PHE   B HD2  1 
ATOM   6171 H HE1  . PHE   B 1 156 ? 54.190 -32.138 -7.896  1.00 21.56 ?  156 PHE   B HE1  1 
ATOM   6172 H HE2  . PHE   B 1 156 ? 53.480 -34.704 -4.908  1.00 20.80 ?  156 PHE   B HE2  1 
ATOM   6173 H HZ   . PHE   B 1 156 ? 54.932 -33.770 -6.442  1.00 21.54 ?  156 PHE   B HZ   1 
ATOM   6174 N N    . ASP   B 1 157 ? 48.577 -34.883 -6.977  1.00 16.09 ?  157 ASP   B N    1 
ATOM   6175 C CA   . ASP   B 1 157 ? 48.726 -36.329 -7.071  1.00 17.26 ?  157 ASP   B CA   1 
ATOM   6176 C C    . ASP   B 1 157 ? 47.812 -36.875 -8.164  1.00 17.27 ?  157 ASP   B C    1 
ATOM   6177 O O    . ASP   B 1 157 ? 46.585 -36.756 -8.067  1.00 16.91 ?  157 ASP   B O    1 
ATOM   6178 C CB   . ASP   B 1 157 ? 48.363 -36.936 -5.722  1.00 18.78 ?  157 ASP   B CB   1 
ATOM   6179 C CG   . ASP   B 1 157 ? 48.502 -38.443 -5.699  1.00 20.67 ?  157 ASP   B CG   1 
ATOM   6180 O OD1  . ASP   B 1 157 ? 48.841 -39.047 -6.743  1.00 21.19 ?  157 ASP   B OD1  1 
ATOM   6181 O OD2  . ASP   B 1 157 ? 48.283 -39.022 -4.617  1.00 23.24 -1 157 ASP   B OD2  1 
ATOM   6182 H H    . ASP   B 1 157 ? 48.026 -34.624 -6.373  1.00 19.31 ?  157 ASP   B H    1 
ATOM   6183 H HA   . ASP   B 1 157 ? 49.648 -36.555 -7.282  1.00 20.71 ?  157 ASP   B HA   1 
ATOM   6184 H HB2  . ASP   B 1 157 ? 48.939 -36.550 -5.043  1.00 22.54 ?  157 ASP   B HB2  1 
ATOM   6185 H HB3  . ASP   B 1 157 ? 47.436 -36.720 -5.525  1.00 22.54 ?  157 ASP   B HB3  1 
ATOM   6186 N N    . LYS   B 1 158 ? 48.411 -37.498 -9.190  1.00 18.13 ?  158 LYS   B N    1 
ATOM   6187 C CA   . LYS   B 1 158 ? 47.635 -38.117 -10.268 1.00 19.49 ?  158 LYS   B CA   1 
ATOM   6188 C C    . LYS   B 1 158 ? 46.572 -39.074 -9.732  1.00 19.37 ?  158 LYS   B C    1 
ATOM   6189 O O    . LYS   B 1 158 ? 45.463 -39.153 -10.276 1.00 19.59 ?  158 LYS   B O    1 
ATOM   6190 C CB   . LYS   B 1 158 ? 48.577 -38.846 -11.233 1.00 21.09 ?  158 LYS   B CB   1 
ATOM   6191 C CG   . LYS   B 1 158 ? 47.889 -39.743 -12.255 1.00 23.31 ?  158 LYS   B CG   1 
ATOM   6192 C CD   . LYS   B 1 158 ? 47.059 -38.947 -13.240 1.00 25.49 ?  158 LYS   B CD   1 
ATOM   6193 C CE   . LYS   B 1 158 ? 46.437 -39.855 -14.289 1.00 27.37 ?  158 LYS   B CE   1 
ATOM   6194 N NZ   . LYS   B 1 158 ? 45.396 -39.146 -15.088 1.00 27.51 ?  158 LYS   B NZ   1 
ATOM   6195 H H    . LYS   B 1 158 ? 49.266 -37.573 -9.285  1.00 21.76 ?  158 LYS   B H    1 
ATOM   6196 H HA   . LYS   B 1 158 ? 47.185 -37.420 -10.770 1.00 23.39 ?  158 LYS   B HA   1 
ATOM   6197 H HB2  . LYS   B 1 158 ? 49.086 -38.183 -11.732 1.00 25.30 ?  158 LYS   B HB2  1 
ATOM   6198 H HB3  . LYS   B 1 158 ? 49.183 -39.400 -10.721 1.00 25.30 ?  158 LYS   B HB3  1 
ATOM   6199 H HG2  . LYS   B 1 158 ? 48.568 -40.220 -12.758 1.00 27.98 ?  158 LYS   B HG2  1 
ATOM   6200 H HG3  . LYS   B 1 158 ? 47.310 -40.381 -11.807 1.00 27.98 ?  158 LYS   B HG3  1 
ATOM   6201 H HD2  . LYS   B 1 158 ? 46.345 -38.492 -12.767 1.00 30.59 ?  158 LYS   B HD2  1 
ATOM   6202 H HD3  . LYS   B 1 158 ? 47.627 -38.304 -13.693 1.00 30.59 ?  158 LYS   B HD3  1 
ATOM   6203 H HE2  . LYS   B 1 158 ? 47.126 -40.163 -14.897 1.00 32.84 ?  158 LYS   B HE2  1 
ATOM   6204 H HE3  . LYS   B 1 158 ? 46.017 -40.612 -13.849 1.00 32.84 ?  158 LYS   B HE3  1 
ATOM   6205 H HZ1  . LYS   B 1 158 ? 45.047 -39.697 -15.693 1.00 33.00 ?  158 LYS   B HZ1  1 
ATOM   6206 H HZ2  . LYS   B 1 158 ? 44.747 -38.855 -14.553 1.00 33.00 ?  158 LYS   B HZ2  1 
ATOM   6207 H HZ3  . LYS   B 1 158 ? 45.759 -38.449 -15.507 1.00 33.00 ?  158 LYS   B HZ3  1 
ATOM   6208 N N    . ASN   B 1 159 ? 46.898 -39.841 -8.690  1.00 19.46 ?  159 ASN   B N    1 
ATOM   6209 C CA   . ASN   B 1 159 ? 45.938 -40.813 -8.176  1.00 19.83 ?  159 ASN   B CA   1 
ATOM   6210 C C    . ASN   B 1 159 ? 44.745 -40.136 -7.501  1.00 18.97 ?  159 ASN   B C    1 
ATOM   6211 O O    . ASN   B 1 159 ? 43.612 -40.627 -7.611  1.00 19.32 ?  159 ASN   B O    1 
ATOM   6212 C CB   . ASN   B 1 159 ? 46.643 -41.794 -7.246  1.00 21.28 ?  159 ASN   B CB   1 
ATOM   6213 C CG   . ASN   B 1 159 ? 47.678 -42.626 -7.972  1.00 22.87 ?  159 ASN   B CG   1 
ATOM   6214 O OD1  . ASN   B 1 159 ? 47.420 -43.135 -9.068  1.00 23.90 ?  159 ASN   B OD1  1 
ATOM   6215 N ND2  . ASN   B 1 159 ? 48.860 -42.761 -7.376  1.00 23.79 ?  159 ASN   B ND2  1 
ATOM   6216 H H    . ASN   B 1 159 ? 47.648 -39.810 -8.276  1.00 23.35 ?  159 ASN   B H    1 
ATOM   6217 H HA   . ASN   B 1 159 ? 45.593 -41.319 -8.928  1.00 23.80 ?  159 ASN   B HA   1 
ATOM   6218 H HB2  . ASN   B 1 159 ? 47.090 -41.304 -6.543  1.00 25.54 ?  159 ASN   B HB2  1 
ATOM   6219 H HB3  . ASN   B 1 159 ? 45.986 -42.400 -6.872  1.00 25.54 ?  159 ASN   B HB3  1 
ATOM   6220 H HD21 . ASN   B 1 159 ? 49.486 -43.225 -7.750  1.00 28.54 ?  159 ASN   B HD21 1 
ATOM   6221 H HD22 . ASN   B 1 159 ? 49.002 -42.399 -6.609  1.00 28.54 ?  159 ASN   B HD22 1 
ATOM   6222 N N    . LEU   B 1 160 ? 44.956 -38.999 -6.831  1.00 18.02 ?  160 LEU   B N    1 
ATOM   6223 C CA   . LEU   B 1 160 ? 43.819 -38.272 -6.283  1.00 17.16 ?  160 LEU   B CA   1 
ATOM   6224 C C    . LEU   B 1 160 ? 43.028 -37.601 -7.394  1.00 16.50 ?  160 LEU   B C    1 
ATOM   6225 O O    . LEU   B 1 160 ? 41.791 -37.594 -7.369  1.00 16.36 ?  160 LEU   B O    1 
ATOM   6226 C CB   . LEU   B 1 160 ? 44.277 -37.247 -5.248  1.00 16.94 ?  160 LEU   B CB   1 
ATOM   6227 C CG   . LEU   B 1 160 ? 43.158 -36.344 -4.713  1.00 16.60 ?  160 LEU   B CG   1 
ATOM   6228 C CD1  . LEU   B 1 160 ? 42.025 -37.163 -4.100  1.00 17.02 ?  160 LEU   B CD1  1 
ATOM   6229 C CD2  . LEU   B 1 160 ? 43.702 -35.353 -3.699  1.00 17.01 ?  160 LEU   B CD2  1 
ATOM   6230 H H    . LEU   B 1 160 ? 45.727 -38.635 -6.693  1.00 21.62 ?  160 LEU   B H    1 
ATOM   6231 H HA   . LEU   B 1 160 ? 43.233 -38.902 -5.843  1.00 20.59 ?  160 LEU   B HA   1 
ATOM   6232 H HB2  . LEU   B 1 160 ? 44.666 -37.724 -4.496  1.00 20.32 ?  160 LEU   B HB2  1 
ATOM   6233 H HB3  . LEU   B 1 160 ? 44.955 -36.678 -5.653  1.00 20.32 ?  160 LEU   B HB3  1 
ATOM   6234 H HG   . LEU   B 1 160 ? 42.789 -35.835 -5.450  1.00 19.91 ?  160 LEU   B HG   1 
ATOM   6235 H HD11 . LEU   B 1 160 ? 41.389 -36.560 -3.690  1.00 20.42 ?  160 LEU   B HD11 1 
ATOM   6236 H HD12 . LEU   B 1 160 ? 41.589 -37.679 -4.798  1.00 20.42 ?  160 LEU   B HD12 1 
ATOM   6237 H HD13 . LEU   B 1 160 ? 42.393 -37.763 -3.430  1.00 20.42 ?  160 LEU   B HD13 1 
ATOM   6238 H HD21 . LEU   B 1 160 ? 42.980 -34.778 -3.405  1.00 20.41 ?  160 LEU   B HD21 1 
ATOM   6239 H HD22 . LEU   B 1 160 ? 44.068 -35.840 -2.945  1.00 20.41 ?  160 LEU   B HD22 1 
ATOM   6240 H HD23 . LEU   B 1 160 ? 44.398 -34.822 -4.119  1.00 20.41 ?  160 LEU   B HD23 1 
ATOM   6241 N N    . TYR   B 1 161 ? 43.726 -37.030 -8.379  1.00 16.66 ?  161 TYR   B N    1 
ATOM   6242 C CA   . TYR   B 1 161 ? 43.053 -36.462 -9.542  1.00 16.56 ?  161 TYR   B CA   1 
ATOM   6243 C C    . TYR   B 1 161 ? 42.111 -37.484 -10.169 1.00 16.37 ?  161 TYR   B C    1 
ATOM   6244 O O    . TYR   B 1 161 ? 40.939 -37.190 -10.432 1.00 16.19 ?  161 TYR   B O    1 
ATOM   6245 C CB   . TYR   B 1 161 ? 44.099 -35.981 -10.557 1.00 16.99 ?  161 TYR   B CB   1 
ATOM   6246 C CG   . TYR   B 1 161 ? 43.526 -35.514 -11.873 1.00 17.35 ?  161 TYR   B CG   1 
ATOM   6247 C CD1  . TYR   B 1 161 ? 43.135 -34.193 -12.043 1.00 17.04 ?  161 TYR   B CD1  1 
ATOM   6248 C CD2  . TYR   B 1 161 ? 43.355 -36.392 -12.939 1.00 18.04 ?  161 TYR   B CD2  1 
ATOM   6249 C CE1  . TYR   B 1 161 ? 42.605 -33.756 -13.233 1.00 18.39 ?  161 TYR   B CE1  1 
ATOM   6250 C CE2  . TYR   B 1 161 ? 42.820 -35.965 -14.134 1.00 18.99 ?  161 TYR   B CE2  1 
ATOM   6251 C CZ   . TYR   B 1 161 ? 42.446 -34.647 -14.276 1.00 19.26 ?  161 TYR   B CZ   1 
ATOM   6252 O OH   . TYR   B 1 161 ? 41.911 -34.201 -15.461 1.00 21.33 ?  161 TYR   B OH   1 
ATOM   6253 H H    . TYR   B 1 161 ? 44.582 -36.967 -8.400  1.00 19.99 ?  161 TYR   B H    1 
ATOM   6254 H HA   . TYR   B 1 161 ? 42.526 -35.698 -9.267  1.00 19.87 ?  161 TYR   B HA   1 
ATOM   6255 H HB2  . TYR   B 1 161 ? 44.587 -35.235 -10.173 1.00 20.39 ?  161 TYR   B HB2  1 
ATOM   6256 H HB3  . TYR   B 1 161 ? 44.710 -36.707 -10.749 1.00 20.39 ?  161 TYR   B HB3  1 
ATOM   6257 H HD1  . TYR   B 1 161 ? 43.244 -33.586 -11.343 1.00 20.44 ?  161 TYR   B HD1  1 
ATOM   6258 H HD2  . TYR   B 1 161 ? 43.600 -37.282 -12.847 1.00 21.64 ?  161 TYR   B HD2  1 
ATOM   6259 H HE1  . TYR   B 1 161 ? 42.355 -32.860 -13.328 1.00 22.07 ?  161 TYR   B HE1  1 
ATOM   6260 H HE2  . TYR   B 1 161 ? 42.707 -36.556 -14.841 1.00 22.78 ?  161 TYR   B HE2  1 
ATOM   6261 H HH   . TYR   B 1 161 ? 41.861 -34.835 -16.010 1.00 25.59 ?  161 TYR   B HH   1 
ATOM   6262 N N    . ASP   B 1 162 ? 42.607 -38.704 -10.397 1.00 16.91 ?  162 ASP   B N    1 
ATOM   6263 C CA   . ASP   B 1 162 ? 41.779 -39.742 -11.005 1.00 17.37 ?  162 ASP   B CA   1 
ATOM   6264 C C    . ASP   B 1 162 ? 40.573 -40.076 -10.135 1.00 16.79 ?  162 ASP   B C    1 
ATOM   6265 O O    . ASP   B 1 162 ? 39.468 -40.291 -10.649 1.00 17.19 ?  162 ASP   B O    1 
ATOM   6266 C CB   . ASP   B 1 162 ? 42.605 -41.005 -11.255 1.00 19.12 ?  162 ASP   B CB   1 
ATOM   6267 C CG   . ASP   B 1 162 ? 43.606 -40.848 -12.382 1.00 20.48 ?  162 ASP   B CG   1 
ATOM   6268 O OD1  . ASP   B 1 162 ? 43.486 -39.899 -13.180 1.00 20.57 ?  162 ASP   B OD1  1 
ATOM   6269 O OD2  . ASP   B 1 162 ? 44.509 -41.706 -12.484 1.00 22.28 -1 162 ASP   B OD2  1 
ATOM   6270 H H    . ASP   B 1 162 ? 43.412 -38.947 -10.212 1.00 20.29 ?  162 ASP   B H    1 
ATOM   6271 H HA   . ASP   B 1 162 ? 41.450 -39.421 -11.856 1.00 20.85 ?  162 ASP   B HA   1 
ATOM   6272 H HB2  . ASP   B 1 162 ? 43.099 -41.223 -10.451 1.00 22.95 ?  162 ASP   B HB2  1 
ATOM   6273 H HB3  . ASP   B 1 162 ? 42.006 -41.728 -11.489 1.00 22.95 ?  162 ASP   B HB3  1 
ATOM   6274 N N    . LYS   B 1 163 ? 40.765 -40.145 -8.816  1.00 16.32 ?  163 LYS   B N    1 
ATOM   6275 C CA   . LYS   B 1 163 ? 39.644 -40.426 -7.927  1.00 17.18 ?  163 LYS   B CA   1 
ATOM   6276 C C    . LYS   B 1 163 ? 38.599 -39.318 -7.989  1.00 16.17 ?  163 LYS   B C    1 
ATOM   6277 O O    . LYS   B 1 163 ? 37.390 -39.589 -7.997  1.00 16.68 ?  163 LYS   B O    1 
ATOM   6278 C CB   . LYS   B 1 163 ? 40.133 -40.618 -6.494  1.00 20.35 ?  163 LYS   B CB   1 
ATOM   6279 C CG   . LYS   B 1 163 ? 39.046 -41.125 -5.571  1.00 26.34 ?  163 LYS   B CG   1 
ATOM   6280 C CD   . LYS   B 1 163 ? 39.526 -41.306 -4.146  1.00 31.86 ?  163 LYS   B CD   1 
ATOM   6281 C CE   . LYS   B 1 163 ? 38.447 -41.981 -3.310  1.00 35.89 ?  163 LYS   B CE   1 
ATOM   6282 N NZ   . LYS   B 1 163 ? 38.515 -41.600 -1.873  1.00 39.86 ?  163 LYS   B NZ   1 
ATOM   6283 H H    . LYS   B 1 163 ? 41.522 -40.029 -8.420  1.00 19.59 ?  163 LYS   B H    1 
ATOM   6284 H HA   . LYS   B 1 163 ? 39.221 -41.248 -8.211  1.00 20.61 ?  163 LYS   B HA   1 
ATOM   6285 H HB2  . LYS   B 1 163 ? 40.855 -41.269 -6.491  1.00 24.42 ?  163 LYS   B HB2  1 
ATOM   6286 H HB3  . LYS   B 1 163 ? 40.450 -39.771 -6.148  1.00 24.42 ?  163 LYS   B HB3  1 
ATOM   6287 H HG2  . LYS   B 1 163 ? 38.316 -40.487 -5.561  1.00 31.61 ?  163 LYS   B HG2  1 
ATOM   6288 H HG3  . LYS   B 1 163 ? 38.731 -41.984 -5.895  1.00 31.61 ?  163 LYS   B HG3  1 
ATOM   6289 H HD2  . LYS   B 1 163 ? 40.317 -41.869 -4.139  1.00 38.22 ?  163 LYS   B HD2  1 
ATOM   6290 H HD3  . LYS   B 1 163 ? 39.722 -40.441 -3.756  1.00 38.22 ?  163 LYS   B HD3  1 
ATOM   6291 H HE2  . LYS   B 1 163 ? 37.574 -41.731 -3.653  1.00 43.07 ?  163 LYS   B HE2  1 
ATOM   6292 H HE3  . LYS   B 1 163 ? 38.559 -42.943 -3.370  1.00 43.07 ?  163 LYS   B HE3  1 
ATOM   6293 H HZ1  . LYS   B 1 163 ? 37.869 -42.012 -1.420  1.00 47.84 ?  163 LYS   B HZ1  1 
ATOM   6294 H HZ2  . LYS   B 1 163 ? 39.302 -41.835 -1.534  1.00 47.84 ?  163 LYS   B HZ2  1 
ATOM   6295 H HZ3  . LYS   B 1 163 ? 38.412 -40.720 -1.788  1.00 47.84 ?  163 LYS   B HZ3  1 
ATOM   6296 N N    . LEU   B 1 164 ? 39.050 -38.062 -8.035  1.00 15.12 ?  164 LEU   B N    1 
ATOM   6297 C CA   . LEU   B 1 164 ? 38.139 -36.923 -8.095  1.00 14.66 ?  164 LEU   B CA   1 
ATOM   6298 C C    . LEU   B 1 164 ? 37.357 -36.907 -9.405  1.00 14.82 ?  164 LEU   B C    1 
ATOM   6299 O O    . LEU   B 1 164 ? 36.132 -36.721 -9.408  1.00 15.84 ?  164 LEU   B O    1 
ATOM   6300 C CB   . LEU   B 1 164 ? 38.932 -35.627 -7.927  1.00 14.35 ?  164 LEU   B CB   1 
ATOM   6301 C CG   . LEU   B 1 164 ? 39.468 -35.357 -6.525  1.00 15.07 ?  164 LEU   B CG   1 
ATOM   6302 C CD1  . LEU   B 1 164 ? 40.572 -34.310 -6.578  1.00 15.19 ?  164 LEU   B CD1  1 
ATOM   6303 C CD2  . LEU   B 1 164 ? 38.366 -34.909 -5.586  1.00 16.46 ?  164 LEU   B CD2  1 
ATOM   6304 H H    . LEU   B 1 164 ? 39.885 -37.845 -8.033  1.00 18.15 ?  164 LEU   B H    1 
ATOM   6305 H HA   . LEU   B 1 164 ? 37.507 -36.983 -7.369  1.00 17.59 ?  164 LEU   B HA   1 
ATOM   6306 H HB2  . LEU   B 1 164 ? 39.697 -35.652 -8.530  1.00 17.22 ?  164 LEU   B HB2  1 
ATOM   6307 H HB3  . LEU   B 1 164 ? 38.362 -34.882 -8.166  1.00 17.22 ?  164 LEU   B HB3  1 
ATOM   6308 H HG   . LEU   B 1 164 ? 39.859 -36.169 -6.173  1.00 18.08 ?  164 LEU   B HG   1 
ATOM   6309 H HD11 . LEU   B 1 164 ? 40.900 -34.143 -5.677  1.00 18.23 ?  164 LEU   B HD11 1 
ATOM   6310 H HD12 . LEU   B 1 164 ? 41.304 -34.641 -7.131  1.00 18.23 ?  164 LEU   B HD12 1 
ATOM   6311 H HD13 . LEU   B 1 164 ? 40.223 -33.490 -6.958  1.00 18.23 ?  164 LEU   B HD13 1 
ATOM   6312 H HD21 . LEU   B 1 164 ? 38.749 -34.706 -4.719  1.00 19.75 ?  164 LEU   B HD21 1 
ATOM   6313 H HD22 . LEU   B 1 164 ? 37.937 -34.121 -5.952  1.00 19.75 ?  164 LEU   B HD22 1 
ATOM   6314 H HD23 . LEU   B 1 164 ? 37.720 -35.628 -5.502  1.00 19.75 ?  164 LEU   B HD23 1 
ATOM   6315 N N    . VAL   B 1 165 ? 38.050 -37.072 -10.533 1.00 16.41 ?  165 VAL   B N    1 
ATOM   6316 C CA   . VAL   B 1 165 ? 37.395 -37.012 -11.837 1.00 17.65 ?  165 VAL   B CA   1 
ATOM   6317 C C    . VAL   B 1 165 ? 36.468 -38.208 -12.020 1.00 19.40 ?  165 VAL   B C    1 
ATOM   6318 O O    . VAL   B 1 165 ? 35.305 -38.065 -12.423 1.00 20.38 ?  165 VAL   B O    1 
ATOM   6319 C CB   . VAL   B 1 165 ? 38.448 -36.934 -12.958 1.00 18.61 ?  165 VAL   B CB   1 
ATOM   6320 C CG1  . VAL   B 1 165 ? 37.795 -37.050 -14.315 1.00 19.77 ?  165 VAL   B CG1  1 
ATOM   6321 C CG2  . VAL   B 1 165 ? 39.236 -35.638 -12.856 1.00 18.44 ?  165 VAL   B CG2  1 
ATOM   6322 H H    . VAL   B 1 165 ? 38.899 -37.211 -10.571 1.00 19.69 ?  165 VAL   B H    1 
ATOM   6323 H HA   . VAL   B 1 165 ? 36.856 -36.210 -11.884 1.00 21.18 ?  165 VAL   B HA   1 
ATOM   6324 H HB   . VAL   B 1 165 ? 39.076 -37.666 -12.859 1.00 22.33 ?  165 VAL   B HB   1 
ATOM   6325 H HG11 . VAL   B 1 165 ? 38.421 -36.763 -14.994 1.00 23.72 ?  165 VAL   B HG11 1 
ATOM   6326 H HG12 . VAL   B 1 165 ? 37.554 -37.980 -14.465 1.00 23.72 ?  165 VAL   B HG12 1 
ATOM   6327 H HG13 . VAL   B 1 165 ? 37.003 -36.496 -14.332 1.00 23.72 ?  165 VAL   B HG13 1 
ATOM   6328 H HG21 . VAL   B 1 165 ? 39.874 -35.593 -13.587 1.00 22.13 ?  165 VAL   B HG21 1 
ATOM   6329 H HG22 . VAL   B 1 165 ? 38.623 -34.887 -12.910 1.00 22.13 ?  165 VAL   B HG22 1 
ATOM   6330 H HG23 . VAL   B 1 165 ? 39.709 -35.615 -12.008 1.00 22.13 ?  165 VAL   B HG23 1 
ATOM   6331 N N    . SER   B 1 166 ? 36.975 -39.407 -11.724 1.00 20.13 ?  166 SER   B N    1 
ATOM   6332 C CA   . SER   B 1 166 ? 36.219 -40.617 -12.011 1.00 20.96 ?  166 SER   B CA   1 
ATOM   6333 C C    . SER   B 1 166 ? 34.964 -40.713 -11.157 1.00 21.18 ?  166 SER   B C    1 
ATOM   6334 O O    . SER   B 1 166 ? 33.995 -41.342 -11.578 1.00 22.49 ?  166 SER   B O    1 
ATOM   6335 C CB   . SER   B 1 166 ? 37.089 -41.871 -11.849 1.00 21.61 ?  166 SER   B CB   1 
ATOM   6336 O OG   . SER   B 1 166 ? 37.454 -42.093 -10.498 1.00 21.94 ?  166 SER   B OG   1 
ATOM   6337 H H    . SER   B 1 166 ? 37.750 -39.544 -11.371 1.00 24.15 ?  166 SER   B H    1 
ATOM   6338 H HA   . SER   B 1 166 ? 35.939 -40.592 -12.939 1.00 25.15 ?  166 SER   B HA   1 
ATOM   6339 H HB2  . SER   B 1 166 ? 36.591 -42.642 -12.166 1.00 25.93 ?  166 SER   B HB2  1 
ATOM   6340 H HB3  . SER   B 1 166 ? 37.896 -41.766 -12.381 1.00 25.93 ?  166 SER   B HB3  1 
ATOM   6341 H HG   . SER   B 1 166 ? 37.902 -41.443 -10.213 1.00 26.33 ?  166 SER   B HG   1 
ATOM   6342 N N    . SER   B 1 167 ? 34.945 -40.096 -9.977  1.00 19.57 ?  167 SER   B N    1 
ATOM   6343 C CA   . SER   B 1 167 ? 33.790 -40.159 -9.087  1.00 18.92 ?  167 SER   B CA   1 
ATOM   6344 C C    . SER   B 1 167 ? 32.871 -38.942 -9.183  1.00 18.81 ?  167 SER   B C    1 
ATOM   6345 O O    . SER   B 1 167 ? 31.799 -38.942 -8.568  1.00 19.19 ?  167 SER   B O    1 
ATOM   6346 C CB   . SER   B 1 167 ? 34.238 -40.342 -7.631  1.00 18.67 ?  167 SER   B CB   1 
ATOM   6347 O OG   . SER   B 1 167 ? 34.906 -39.185 -7.150  1.00 18.52 ?  167 SER   B OG   1 
ATOM   6348 H H    . SER   B 1 167 ? 35.598 -39.637 -9.671  1.00 23.48 ?  167 SER   B H    1 
ATOM   6349 H HA   . SER   B 1 167 ? 33.262 -40.938 -9.328  1.00 22.71 ?  167 SER   B HA   1 
ATOM   6350 H HB2  . SER   B 1 167 ? 33.456 -40.513 -7.083  1.00 22.40 ?  167 SER   B HB2  1 
ATOM   6351 H HB3  . SER   B 1 167 ? 34.842 -41.108 -7.585  1.00 22.40 ?  167 SER   B HB3  1 
ATOM   6352 H HG   . SER   B 1 167 ? 35.587 -39.042 -7.621  1.00 22.22 ?  167 SER   B HG   1 
ATOM   6353 N N    . PHE   B 1 168 ? 33.249 -37.907 -9.934  1.00 18.81 ?  168 PHE   B N    1 
ATOM   6354 C CA   . PHE   B 1 168 ? 32.419 -36.701 -9.990  1.00 18.54 ?  168 PHE   B CA   1 
ATOM   6355 C C    . PHE   B 1 168 ? 31.107 -36.955 -10.726 1.00 16.12 ?  168 PHE   B C    1 
ATOM   6356 O O    . PHE   B 1 168 ? 30.066 -36.360 -10.385 1.00 16.74 ?  168 PHE   B O    1 
ATOM   6357 C CB   . PHE   B 1 168 ? 33.177 -35.554 -10.656 1.00 19.34 ?  168 PHE   B CB   1 
ATOM   6358 C CG   . PHE   B 1 168 ? 32.361 -34.307 -10.793 1.00 19.27 ?  168 PHE   B CG   1 
ATOM   6359 C CD1  . PHE   B 1 168 ? 32.023 -33.570 -9.668  1.00 20.38 ?  168 PHE   B CD1  1 
ATOM   6360 C CD2  . PHE   B 1 168 ? 31.915 -33.880 -12.030 1.00 18.52 ?  168 PHE   B CD2  1 
ATOM   6361 C CE1  . PHE   B 1 168 ? 31.257 -32.425 -9.771  1.00 20.57 ?  168 PHE   B CE1  1 
ATOM   6362 C CE2  . PHE   B 1 168 ? 31.158 -32.720 -12.146 1.00 19.25 ?  168 PHE   B CE2  1 
ATOM   6363 C CZ   . PHE   B 1 168 ? 30.824 -31.994 -11.011 1.00 19.73 ?  168 PHE   B CZ   1 
ATOM   6364 H H    . PHE   B 1 168 ? 33.972 -37.871 -10.402 1.00 22.57 ?  168 PHE   B H    1 
ATOM   6365 H HA   . PHE   B 1 168 ? 32.203 -36.427 -9.087  1.00 22.24 ?  168 PHE   B HA   1 
ATOM   6366 H HB2  . PHE   B 1 168 ? 33.956 -35.337 -10.120 1.00 23.21 ?  168 PHE   B HB2  1 
ATOM   6367 H HB3  . PHE   B 1 168 ? 33.451 -35.826 -11.544 1.00 23.21 ?  168 PHE   B HB3  1 
ATOM   6368 H HD1  . PHE   B 1 168 ? 32.310 -33.863 -8.833  1.00 24.45 ?  168 PHE   B HD1  1 
ATOM   6369 H HD2  . PHE   B 1 168 ? 32.138 -34.359 -12.794 1.00 22.22 ?  168 PHE   B HD2  1 
ATOM   6370 H HE1  . PHE   B 1 168 ? 31.037 -31.946 -9.006  1.00 24.69 ?  168 PHE   B HE1  1 
ATOM   6371 H HE2  . PHE   B 1 168 ? 30.861 -32.436 -12.984 1.00 23.10 ?  168 PHE   B HE2  1 
ATOM   6372 H HZ   . PHE   B 1 168 ? 30.307 -31.224 -11.086 1.00 23.68 ?  168 PHE   B HZ   1 
ATOM   6373 N N    . LEU   B 1 169 ? 31.138 -37.834 -11.725 1.00 16.64 ?  169 LEU   B N    1 
ATOM   6374 C CA   . LEU   B 1 169 ? 29.959 -38.149 -12.518 1.00 18.63 ?  169 LEU   B CA   1 
ATOM   6375 C C    . LEU   B 1 169 ? 29.960 -39.596 -13.005 1.00 21.17 ?  169 LEU   B C    1 
ATOM   6376 O O    . LEU   B 1 169 ? 29.066 -40.023 -13.738 1.00 23.63 ?  169 LEU   B O    1 
ATOM   6377 C CB   . LEU   B 1 169 ? 29.876 -37.209 -13.720 1.00 20.44 ?  169 LEU   B CB   1 
ATOM   6378 C CG   . LEU   B 1 169 ? 28.609 -36.360 -13.805 1.00 23.73 ?  169 LEU   B CG   1 
ATOM   6379 C CD1  . LEU   B 1 169 ? 28.540 -35.685 -15.156 1.00 24.94 ?  169 LEU   B CD1  1 
ATOM   6380 C CD2  . LEU   B 1 169 ? 27.362 -37.192 -13.556 1.00 24.06 ?  169 LEU   B CD2  1 
ATOM   6381 O OXT  . LEU   B 1 169 ? 30.861 -40.368 -12.685 1.00 22.25 -1 169 LEU   B OXT  1 
ATOM   6382 H H    . LEU   B 1 169 ? 31.845 -38.262 -11.972 1.00 19.97 ?  169 LEU   B H    1 
ATOM   6383 H HA   . LEU   B 1 169 ? 29.176 -38.014 -11.969 1.00 22.35 ?  169 LEU   B HA   1 
ATOM   6384 H HB2  . LEU   B 1 169 ? 30.630 -36.596 -13.689 1.00 24.52 ?  169 LEU   B HB2  1 
ATOM   6385 H HB3  . LEU   B 1 169 ? 29.922 -37.734 -14.535 1.00 24.52 ?  169 LEU   B HB3  1 
ATOM   6386 H HG   . LEU   B 1 169 ? 28.646 -35.665 -13.127 1.00 28.47 ?  169 LEU   B HG   1 
ATOM   6387 H HD11 . LEU   B 1 169 ? 27.748 -35.127 -15.189 1.00 29.92 ?  169 LEU   B HD11 1 
ATOM   6388 H HD12 . LEU   B 1 169 ? 29.334 -35.143 -15.276 1.00 29.92 ?  169 LEU   B HD12 1 
ATOM   6389 H HD13 . LEU   B 1 169 ? 28.495 -36.367 -15.843 1.00 29.92 ?  169 LEU   B HD13 1 
ATOM   6390 H HD21 . LEU   B 1 169 ? 26.605 -36.767 -13.983 1.00 28.88 ?  169 LEU   B HD21 1 
ATOM   6391 H HD22 . LEU   B 1 169 ? 27.497 -38.080 -13.926 1.00 28.88 ?  169 LEU   B HD22 1 
ATOM   6392 H HD23 . LEU   B 1 169 ? 27.213 -37.254 -12.600 1.00 28.88 ?  169 LEU   B HD23 1 
HETATM 6393 N N2   B A1A6Q C 2 .   ? 14.779 0.123   4.195   0.16 12.03 ?  201 A1A6Q A N2   1 
HETATM 6394 C C3   B A1A6Q C 2 .   ? 14.110 0.897   -0.195  0.16 14.17 ?  201 A1A6Q A C3   1 
HETATM 6395 C C6   B A1A6Q C 2 .   ? 14.850 0.080   5.579   0.16 11.66 ?  201 A1A6Q A C6   1 
HETATM 6396 C C9   B A1A6Q C 2 .   ? 15.518 3.946   4.146   0.16 9.86  ?  201 A1A6Q A C9   1 
HETATM 6397 C C1   B A1A6Q C 2 .   ? 15.661 -0.665  0.867   0.16 14.14 ?  201 A1A6Q A C1   1 
HETATM 6398 C C10  B A1A6Q C 2 .   ? 15.687 4.500   5.417   0.16 8.10  ?  201 A1A6Q A C10  1 
HETATM 6399 C C2   B A1A6Q C 2 .   ? 16.287 -0.051  -0.414  0.16 14.40 ?  201 A1A6Q A C2   1 
HETATM 6400 C C4   B A1A6Q C 2 .   ? 14.479 0.294   1.202   0.16 13.52 ?  201 A1A6Q A C4   1 
HETATM 6401 C C5   B A1A6Q C 2 .   ? 14.969 1.319   3.531   0.16 11.63 ?  201 A1A6Q A C5   1 
HETATM 6402 C C7   B A1A6Q C 2 .   ? 15.282 2.292   5.732   0.16 10.29 ?  201 A1A6Q A C7   1 
HETATM 6403 C C8   B A1A6Q C 2 .   ? 15.243 2.514   4.308   0.16 10.55 ?  201 A1A6Q A C8   1 
HETATM 6404 N N1   B A1A6Q C 2 .   ? 14.894 1.371   2.127   0.16 12.34 ?  201 A1A6Q A N1   1 
HETATM 6405 N N3   B A1A6Q C 2 .   ? 15.090 1.114   6.394   0.16 10.95 ?  201 A1A6Q A N3   1 
HETATM 6406 N N4   B A1A6Q C 2 .   ? 15.550 3.493   6.314   0.16 9.20  ?  201 A1A6Q A N4   1 
HETATM 6407 O O1   B A1A6Q C 2 .   ? 15.149 -1.961  0.656   0.16 14.33 ?  201 A1A6Q A O1   1 
HETATM 6408 O O2   B A1A6Q C 2 .   ? 15.247 0.706   -1.045  0.16 14.52 ?  201 A1A6Q A O2   1 
HETATM 6409 H H6   B A1A6Q C 2 .   ? 13.150 0.437   -0.577  0.16 17.00 ?  201 A1A6Q A H6   1 
HETATM 6410 H H7   B A1A6Q C 2 .   ? 13.824 2.001   -0.126  0.16 17.00 ?  201 A1A6Q A H7   1 
HETATM 6411 H H9   B A1A6Q C 2 .   ? 14.676 -0.907  6.103   0.16 13.99 ?  201 A1A6Q A H9   1 
HETATM 6412 H H10  B A1A6Q C 2 .   ? 15.568 4.539   3.246   0.16 11.82 ?  201 A1A6Q A H10  1 
HETATM 6413 H H1   B A1A6Q C 2 .   ? 16.394 -0.624  1.716   0.16 16.96 ?  201 A1A6Q A H1   1 
HETATM 6414 H H11  B A1A6Q C 2 .   ? 15.903 5.500   5.821   0.16 9.72  ?  201 A1A6Q A H11  1 
HETATM 6415 H H5   B A1A6Q C 2 .   ? 17.219 0.549   -0.137  0.16 17.28 ?  201 A1A6Q A H5   1 
HETATM 6416 H H4   B A1A6Q C 2 .   ? 16.716 -0.840  -1.100  0.16 17.28 ?  201 A1A6Q A H4   1 
HETATM 6417 H H2   B A1A6Q C 2 .   ? 13.611 -0.324  1.586   0.16 16.22 ?  201 A1A6Q A H2   1 
HETATM 6418 H H8   B A1A6Q C 2 .   ? 15.144 2.236   1.647   0.16 14.80 ?  201 A1A6Q A H8   1 
HETATM 6419 H H12  B A1A6Q C 2 .   ? 15.632 3.629   7.352   0.16 11.04 ?  201 A1A6Q A H12  1 
HETATM 6420 H H3   B A1A6Q C 2 .   ? 15.825 -2.646  0.744   0.16 17.20 ?  201 A1A6Q A H3   1 
HETATM 6421 O O    . HOH   D 3 .   ? 26.868 11.415  1.666   1.00 16.80 ?  301 HOH   A O    1 
HETATM 6422 O O    . HOH   D 3 .   ? 4.722  3.863   0.649   1.00 25.04 ?  302 HOH   A O    1 
HETATM 6423 O O    . HOH   D 3 .   ? 7.640  -6.325  -6.524  1.00 40.73 ?  303 HOH   A O    1 
HETATM 6424 O O    . HOH   D 3 .   ? 28.547 -10.665 -14.016 1.00 40.27 ?  304 HOH   A O    1 
HETATM 6425 O O    . HOH   D 3 .   ? 34.364 -1.862  12.537  1.00 36.62 ?  305 HOH   A O    1 
HETATM 6426 O O    . HOH   D 3 .   ? 14.820 -4.670  20.585  1.00 41.19 ?  306 HOH   A O    1 
HETATM 6427 O O    . HOH   D 3 .   ? -0.457 -3.095  3.126   1.00 36.20 ?  307 HOH   A O    1 
HETATM 6428 O O    . HOH   D 3 .   ? 0.681  -4.535  0.299   1.00 30.46 ?  308 HOH   A O    1 
HETATM 6429 O O    . HOH   D 3 .   ? 12.145 0.291   14.903  1.00 32.13 ?  309 HOH   A O    1 
HETATM 6430 O O    . HOH   D 3 .   ? 15.198 -12.234 18.762  1.00 31.93 ?  310 HOH   A O    1 
HETATM 6431 O O    . HOH   D 3 .   ? 18.631 -19.407 13.538  1.00 36.96 ?  311 HOH   A O    1 
HETATM 6432 O O    . HOH   D 3 .   ? 18.630 -2.379  -16.365 1.00 42.30 ?  312 HOH   A O    1 
HETATM 6433 O O    B HOH   D 3 .   ? 14.892 7.156   7.519   0.16 14.38 ?  313 HOH   A O    1 
HETATM 6434 O O    . HOH   D 3 .   ? 7.959  -12.592 -0.856  1.00 21.76 ?  314 HOH   A O    1 
HETATM 6435 O O    . HOH   D 3 .   ? 15.583 11.963  8.007   1.00 34.38 ?  315 HOH   A O    1 
HETATM 6436 O O    . HOH   D 3 .   ? 16.330 2.982   -1.560  1.00 18.63 ?  316 HOH   A O    1 
HETATM 6437 O O    . HOH   D 3 .   ? 36.099 -5.083  -0.537  1.00 26.57 ?  317 HOH   A O    1 
HETATM 6438 O O    . HOH   D 3 .   ? 11.678 -10.839 -10.061 1.00 40.78 ?  318 HOH   A O    1 
HETATM 6439 O O    . HOH   D 3 .   ? 42.435 10.553  5.173   1.00 19.82 ?  319 HOH   A O    1 
HETATM 6440 O O    . HOH   D 3 .   ? 14.767 -14.017 16.712  1.00 21.53 ?  320 HOH   A O    1 
HETATM 6441 O O    . HOH   D 3 .   ? 28.998 0.450   -9.686  1.00 20.99 ?  321 HOH   A O    1 
HETATM 6442 O O    . HOH   D 3 .   ? 30.251 -13.298 -8.572  1.00 21.07 ?  322 HOH   A O    1 
HETATM 6443 O O    . HOH   D 3 .   ? 19.879 -12.480 -9.002  1.00 25.02 ?  323 HOH   A O    1 
HETATM 6444 O O    . HOH   D 3 .   ? -0.605 -8.534  2.231   1.00 39.94 ?  324 HOH   A O    1 
HETATM 6445 O O    . HOH   D 3 .   ? 30.943 6.226   -12.289 1.00 29.93 ?  325 HOH   A O    1 
HETATM 6446 O O    . HOH   D 3 .   ? 6.927  -8.191  11.878  1.00 20.89 ?  326 HOH   A O    1 
HETATM 6447 O O    . HOH   D 3 .   ? 34.042 -0.991  -8.891  1.00 27.45 ?  327 HOH   A O    1 
HETATM 6448 O O    . HOH   D 3 .   ? 3.635  -9.349  10.025  1.00 32.53 ?  328 HOH   A O    1 
HETATM 6449 O O    . HOH   D 3 .   ? 9.071  -10.201 19.300  1.00 39.27 ?  329 HOH   A O    1 
HETATM 6450 O O    . HOH   D 3 .   ? 26.500 -19.343 -1.840  1.00 14.38 ?  330 HOH   A O    1 
HETATM 6451 O O    . HOH   D 3 .   ? 27.431 -6.039  -13.999 1.00 35.16 ?  331 HOH   A O    1 
HETATM 6452 O O    . HOH   D 3 .   ? 17.155 -18.079 15.062  1.00 23.66 ?  332 HOH   A O    1 
HETATM 6453 O O    . HOH   D 3 .   ? 8.041  -21.557 3.961   1.00 44.79 ?  333 HOH   A O    1 
HETATM 6454 O O    . HOH   D 3 .   ? 21.833 -13.808 -8.119  1.00 37.22 ?  334 HOH   A O    1 
HETATM 6455 O O    . HOH   D 3 .   ? 22.400 5.309   19.057  1.00 42.45 ?  335 HOH   A O    1 
HETATM 6456 O O    . HOH   D 3 .   ? 37.568 2.822   10.226  1.00 27.17 ?  336 HOH   A O    1 
HETATM 6457 O O    . HOH   D 3 .   ? 31.038 -18.158 7.771   1.00 20.49 ?  337 HOH   A O    1 
HETATM 6458 O O    . HOH   D 3 .   ? 20.105 4.546   -7.570  1.00 19.34 ?  338 HOH   A O    1 
HETATM 6459 O O    . HOH   D 3 .   ? 20.629 -19.734 -5.061  1.00 28.78 ?  339 HOH   A O    1 
HETATM 6460 O O    . HOH   D 3 .   ? 28.250 -6.358  19.644  1.00 41.11 ?  340 HOH   A O    1 
HETATM 6461 O O    . HOH   D 3 .   ? 14.159 -4.533  -11.859 1.00 28.79 ?  341 HOH   A O    1 
HETATM 6462 O O    . HOH   D 3 .   ? 27.313 13.778  2.898   1.00 27.61 ?  342 HOH   A O    1 
HETATM 6463 O O    . HOH   D 3 .   ? 18.892 -22.013 6.896   1.00 30.80 ?  343 HOH   A O    1 
HETATM 6464 O O    . HOH   D 3 .   ? 28.364 -0.138  -13.377 1.00 33.24 ?  344 HOH   A O    1 
HETATM 6465 O O    . HOH   D 3 .   ? 44.332 7.111   6.462   1.00 26.29 ?  345 HOH   A O    1 
HETATM 6466 O O    B HOH   D 3 .   ? 19.177 -0.536  -2.428  0.16 12.08 ?  346 HOH   A O    1 
HETATM 6467 O O    . HOH   D 3 .   ? 22.764 12.516  1.647   1.00 15.21 ?  347 HOH   A O    1 
HETATM 6468 O O    A HOH   D 3 .   ? 17.510 -1.725  0.462   0.84 18.26 ?  348 HOH   A O    1 
HETATM 6469 O O    . HOH   D 3 .   ? 38.307 10.118  7.186   1.00 39.97 ?  349 HOH   A O    1 
HETATM 6470 O O    . HOH   D 3 .   ? 15.098 3.841   17.824  1.00 37.27 ?  350 HOH   A O    1 
HETATM 6471 O O    . HOH   D 3 .   ? 17.148 -17.851 -5.049  1.00 26.49 ?  351 HOH   A O    1 
HETATM 6472 O O    . HOH   D 3 .   ? 9.838  -21.399 5.700   1.00 19.29 ?  352 HOH   A O    1 
HETATM 6473 O O    . HOH   D 3 .   ? 38.579 4.963   6.996   1.00 15.85 ?  353 HOH   A O    1 
HETATM 6474 O O    . HOH   D 3 .   ? 39.788 -1.001  -5.191  1.00 20.73 ?  354 HOH   A O    1 
HETATM 6475 O O    . HOH   D 3 .   ? 22.232 -19.274 11.350  1.00 33.64 ?  355 HOH   A O    1 
HETATM 6476 O O    . HOH   D 3 .   ? 13.283 -1.413  -6.585  1.00 18.02 ?  356 HOH   A O    1 
HETATM 6477 O O    . HOH   D 3 .   ? 35.789 -12.693 6.832   1.00 16.14 ?  357 HOH   A O    1 
HETATM 6478 O O    . HOH   D 3 .   ? 42.590 4.281   5.445   1.00 31.32 ?  358 HOH   A O    1 
HETATM 6479 O O    . HOH   D 3 .   ? 24.046 -2.083  -2.056  1.00 10.53 ?  359 HOH   A O    1 
HETATM 6480 O O    . HOH   D 3 .   ? 15.215 -21.625 14.215  1.00 17.34 ?  360 HOH   A O    1 
HETATM 6481 O O    . HOH   D 3 .   ? 13.574 -15.218 -7.536  1.00 26.90 ?  361 HOH   A O    1 
HETATM 6482 O O    . HOH   D 3 .   ? 31.692 8.207   14.867  1.00 23.18 ?  362 HOH   A O    1 
HETATM 6483 O O    A HOH   D 3 .   ? 14.289 0.552   6.824   0.84 23.83 ?  363 HOH   A O    1 
HETATM 6484 O O    . HOH   D 3 .   ? 21.880 -21.914 8.403   1.00 27.18 ?  364 HOH   A O    1 
HETATM 6485 O O    . HOH   D 3 .   ? 31.091 -13.937 -2.492  1.00 14.15 ?  365 HOH   A O    1 
HETATM 6486 O O    . HOH   D 3 .   ? 37.222 -2.869  9.720   1.00 40.28 ?  366 HOH   A O    1 
HETATM 6487 O O    A HOH   D 3 .   ? 14.649 -3.670  3.115   0.84 18.79 ?  367 HOH   A O    1 
HETATM 6488 O O    A HOH   D 3 .   ? 21.260 -2.403  -2.033  0.84 13.96 ?  368 HOH   A O    1 
HETATM 6489 O O    . HOH   D 3 .   ? 30.824 3.077   8.284   1.00 12.23 ?  369 HOH   A O    1 
HETATM 6490 O O    . HOH   D 3 .   ? 16.498 -22.065 0.941   1.00 26.65 ?  370 HOH   A O    1 
HETATM 6491 O O    . HOH   D 3 .   ? 33.685 -7.160  4.308   1.00 16.85 ?  371 HOH   A O    1 
HETATM 6492 O O    B HOH   D 3 .   ? 14.913 -2.592  3.385   0.16 13.01 ?  372 HOH   A O    1 
HETATM 6493 O O    . HOH   D 3 .   ? 37.346 11.958  4.934   1.00 29.45 ?  373 HOH   A O    1 
HETATM 6494 O O    . HOH   D 3 .   ? 14.340 -21.231 -4.283  1.00 29.76 ?  374 HOH   A O    1 
HETATM 6495 O O    . HOH   D 3 .   ? 17.025 -19.315 4.874   1.00 15.20 ?  375 HOH   A O    1 
HETATM 6496 O O    . HOH   D 3 .   ? 24.428 3.589   -1.792  1.00 15.47 ?  376 HOH   A O    1 
HETATM 6497 O O    . HOH   D 3 .   ? 31.889 -9.329  -6.666  1.00 22.08 ?  377 HOH   A O    1 
HETATM 6498 O O    . HOH   D 3 .   ? 24.733 -17.536 12.717  1.00 24.17 ?  378 HOH   A O    1 
HETATM 6499 O O    . HOH   D 3 .   ? 27.515 -10.644 14.039  1.00 16.77 ?  379 HOH   A O    1 
HETATM 6500 O O    B HOH   D 3 .   ? 18.833 -1.936  0.471   0.16 14.67 ?  380 HOH   A O    1 
HETATM 6501 O O    . HOH   D 3 .   ? 18.564 9.440   9.000   1.00 21.51 ?  381 HOH   A O    1 
HETATM 6502 O O    . HOH   D 3 .   ? 43.937 8.479   -3.084  1.00 26.05 ?  382 HOH   A O    1 
HETATM 6503 O O    . HOH   D 3 .   ? 43.378 7.842   2.729   1.00 27.05 ?  383 HOH   A O    1 
HETATM 6504 O O    . HOH   D 3 .   ? 8.922  -12.097 17.217  1.00 42.50 ?  384 HOH   A O    1 
HETATM 6505 O O    B HOH   D 3 .   ? 21.440 -2.033  -2.816  0.16 10.10 ?  385 HOH   A O    1 
HETATM 6506 O O    . HOH   D 3 .   ? 13.982 -5.008  17.555  1.00 23.90 ?  386 HOH   A O    1 
HETATM 6507 O O    . HOH   D 3 .   ? 14.423 -24.745 11.610  1.00 33.75 ?  387 HOH   A O    1 
HETATM 6508 O O    . HOH   D 3 .   ? 31.780 -7.268  -9.869  1.00 21.54 ?  388 HOH   A O    1 
HETATM 6509 O O    . HOH   D 3 .   ? 22.648 -11.979 21.822  1.00 39.15 ?  389 HOH   A O    1 
HETATM 6510 O O    . HOH   D 3 .   ? 21.390 3.164   -0.341  1.00 13.39 ?  390 HOH   A O    1 
HETATM 6511 O O    . HOH   D 3 .   ? 24.285 -7.820  14.451  1.00 17.09 ?  391 HOH   A O    1 
HETATM 6512 O O    . HOH   D 3 .   ? 24.609 2.007   -7.013  1.00 18.61 ?  392 HOH   A O    1 
HETATM 6513 O O    . HOH   D 3 .   ? 25.738 -0.776  -7.319  1.00 15.41 ?  393 HOH   A O    1 
HETATM 6514 O O    . HOH   D 3 .   ? 23.964 -15.682 -9.171  1.00 31.24 ?  394 HOH   A O    1 
HETATM 6515 O O    . HOH   D 3 .   ? 21.220 10.306  15.046  1.00 33.60 ?  395 HOH   A O    1 
HETATM 6516 O O    . HOH   D 3 .   ? 11.030 1.593   12.722  1.00 23.43 ?  396 HOH   A O    1 
HETATM 6517 O O    . HOH   D 3 .   ? 16.021 6.935   2.954   1.00 16.66 ?  397 HOH   A O    1 
HETATM 6518 O O    . HOH   D 3 .   ? 6.465  -5.616  11.160  1.00 20.57 ?  398 HOH   A O    1 
HETATM 6519 O O    A HOH   D 3 .   ? 18.972 -0.677  -1.604  0.84 11.91 ?  399 HOH   A O    1 
HETATM 6520 O O    . HOH   D 3 .   ? 37.585 -2.047  5.796   1.00 27.48 ?  400 HOH   A O    1 
HETATM 6521 O O    . HOH   D 3 .   ? 30.706 1.838   16.698  1.00 21.72 ?  401 HOH   A O    1 
HETATM 6522 O O    . HOH   D 3 .   ? 32.799 -9.252  5.956   1.00 19.88 ?  402 HOH   A O    1 
HETATM 6523 O O    . HOH   D 3 .   ? 20.576 -20.036 2.765   1.00 17.90 ?  403 HOH   A O    1 
HETATM 6524 O O    . HOH   D 3 .   ? 14.051 -23.100 7.396   1.00 18.22 ?  404 HOH   A O    1 
HETATM 6525 O O    . HOH   D 3 .   ? 16.240 16.668  8.701   1.00 28.87 ?  405 HOH   A O    1 
HETATM 6526 O O    B HOH   D 3 .   ? 12.700 -2.670  -0.644  0.16 22.80 ?  406 HOH   A O    1 
HETATM 6527 O O    . HOH   D 3 .   ? 23.487 11.368  4.103   1.00 12.39 ?  407 HOH   A O    1 
HETATM 6528 O O    . HOH   D 3 .   ? 26.949 4.174   -0.641  1.00 12.84 ?  408 HOH   A O    1 
HETATM 6529 O O    A HOH   D 3 .   ? 15.814 -0.964  5.292   0.84 24.04 ?  409 HOH   A O    1 
HETATM 6530 O O    . HOH   D 3 .   ? 30.078 -10.114 13.016  1.00 20.72 ?  410 HOH   A O    1 
HETATM 6531 O O    . HOH   D 3 .   ? 27.292 2.288   18.725  1.00 31.37 ?  411 HOH   A O    1 
HETATM 6532 O O    . HOH   D 3 .   ? 38.111 -1.338  -1.929  1.00 19.62 ?  412 HOH   A O    1 
HETATM 6533 O O    . HOH   D 3 .   ? 10.455 -22.206 -1.258  1.00 47.56 ?  413 HOH   A O    1 
HETATM 6534 O O    . HOH   D 3 .   ? 15.877 2.121   24.805  1.00 43.52 ?  414 HOH   A O    1 
HETATM 6535 O O    . HOH   D 3 .   ? 40.924 -8.286  -6.758  1.00 35.00 ?  415 HOH   A O    1 
HETATM 6536 O O    . HOH   D 3 .   ? 5.180  2.697   5.276   1.00 30.69 ?  416 HOH   A O    1 
HETATM 6537 O O    . HOH   D 3 .   ? 24.079 3.952   -4.820  1.00 21.79 ?  417 HOH   A O    1 
HETATM 6538 O O    . HOH   D 3 .   ? 15.170 -8.059  -9.640  1.00 21.67 ?  418 HOH   A O    1 
HETATM 6539 O O    . HOH   D 3 .   ? 14.520 -0.509  -12.092 1.00 25.80 ?  419 HOH   A O    1 
HETATM 6540 O O    . HOH   D 3 .   ? 41.656 1.497   4.977   1.00 36.99 ?  420 HOH   A O    1 
HETATM 6541 O O    . HOH   D 3 .   ? 23.954 -20.307 -1.384  1.00 16.55 ?  421 HOH   A O    1 
HETATM 6542 O O    . HOH   D 3 .   ? 6.737  -3.414  12.996  1.00 30.27 ?  422 HOH   A O    1 
HETATM 6543 O O    . HOH   D 3 .   ? 27.961 0.841   -7.128  1.00 14.00 ?  423 HOH   A O    1 
HETATM 6544 O O    . HOH   D 3 .   ? 30.362 -12.960 13.523  1.00 19.09 ?  424 HOH   A O    1 
HETATM 6545 O O    . HOH   D 3 .   ? 35.128 -5.228  -3.115  1.00 17.94 ?  425 HOH   A O    1 
HETATM 6546 O O    . HOH   D 3 .   ? 32.675 -4.286  -9.907  1.00 27.48 ?  426 HOH   A O    1 
HETATM 6547 O O    . HOH   D 3 .   ? 16.220 -14.216 20.299  1.00 40.89 ?  427 HOH   A O    1 
HETATM 6548 O O    . HOH   D 3 .   ? 36.758 -4.948  5.411   1.00 24.31 ?  428 HOH   A O    1 
HETATM 6549 O O    . HOH   D 3 .   ? 10.399 -13.732 -1.680  1.00 18.13 ?  429 HOH   A O    1 
HETATM 6550 O O    . HOH   D 3 .   ? 45.011 -0.635  2.953   1.00 40.43 ?  430 HOH   A O    1 
HETATM 6551 O O    . HOH   D 3 .   ? 27.115 -3.306  19.397  1.00 34.25 ?  431 HOH   A O    1 
HETATM 6552 O O    . HOH   D 3 .   ? 32.591 -10.643 3.212   1.00 31.68 ?  432 HOH   A O    1 
HETATM 6553 O O    . HOH   D 3 .   ? 22.684 8.129   18.435  1.00 43.76 ?  433 HOH   A O    1 
HETATM 6554 O O    . HOH   D 3 .   ? 21.290 -9.282  21.334  1.00 44.56 ?  434 HOH   A O    1 
HETATM 6555 O O    . HOH   D 3 .   ? 11.683 -10.792 17.049  1.00 23.74 ?  435 HOH   A O    1 
HETATM 6556 O O    A HOH   D 3 .   ? 11.081 -0.394  1.956   0.84 20.45 ?  436 HOH   A O    1 
HETATM 6557 O O    A HOH   D 3 .   ? 18.876 2.024   -0.725  0.84 12.51 ?  437 HOH   A O    1 
HETATM 6558 O O    . HOH   D 3 .   ? 23.565 -8.078  17.074  1.00 21.23 ?  438 HOH   A O    1 
HETATM 6559 O O    . HOH   D 3 .   ? 23.359 -20.970 1.296   1.00 18.92 ?  439 HOH   A O    1 
HETATM 6560 O O    . HOH   D 3 .   ? 37.747 -8.847  -3.499  1.00 23.35 ?  440 HOH   A O    1 
HETATM 6561 O O    . HOH   D 3 .   ? 20.602 -17.784 24.831  1.00 49.56 ?  441 HOH   A O    1 
HETATM 6562 O O    . HOH   D 3 .   ? 19.450 -11.092 24.047  1.00 62.71 ?  442 HOH   A O    1 
HETATM 6563 O O    . HOH   D 3 .   ? 18.485 4.898   -15.099 1.00 47.29 ?  443 HOH   A O    1 
HETATM 6564 O O    . HOH   D 3 .   ? 9.445  -16.298 -2.047  1.00 39.39 ?  444 HOH   A O    1 
HETATM 6565 O O    . HOH   D 3 .   ? -1.420 -5.010  7.698   1.00 37.15 ?  445 HOH   A O    1 
HETATM 6566 O O    . HOH   D 3 .   ? 34.435 -8.085  -0.575  1.00 25.87 ?  446 HOH   A O    1 
HETATM 6567 O O    B HOH   D 3 .   ? 11.130 -0.817  1.930   0.16 12.70 ?  447 HOH   A O    1 
HETATM 6568 O O    . HOH   D 3 .   ? 23.261 7.585   -3.165  1.00 28.29 ?  448 HOH   A O    1 
HETATM 6569 O O    B HOH   D 3 .   ? 11.062 6.390   9.902   0.16 16.77 ?  449 HOH   A O    1 
HETATM 6570 O O    . HOH   D 3 .   ? 30.592 14.790  2.824   1.00 18.87 ?  450 HOH   A O    1 
HETATM 6571 O O    . HOH   D 3 .   ? 18.444 -16.116 16.387  1.00 35.05 ?  451 HOH   A O    1 
HETATM 6572 O O    . HOH   D 3 .   ? 21.618 -14.738 18.006  1.00 46.77 ?  452 HOH   A O    1 
HETATM 6573 O O    . HOH   D 3 .   ? 31.359 -12.766 0.001   1.00 19.60 ?  453 HOH   A O    1 
HETATM 6574 O O    B HOH   D 3 .   ? 11.880 -1.480  -2.807  0.16 11.22 ?  454 HOH   A O    1 
HETATM 6575 O O    A HOH   D 3 .   ? 14.041 -0.355  3.484   0.84 23.23 ?  455 HOH   A O    1 
HETATM 6576 O O    . HOH   D 3 .   ? 29.881 -16.086 10.668  1.00 36.09 ?  456 HOH   A O    1 
HETATM 6577 O O    . HOH   D 3 .   ? 27.815 7.060   -6.413  1.00 37.06 ?  457 HOH   A O    1 
HETATM 6578 O O    B HOH   D 3 .   ? 19.203 2.292   -1.031  0.16 11.68 ?  458 HOH   A O    1 
HETATM 6579 O O    . HOH   D 3 .   ? 32.492 -15.946 10.839  1.00 34.21 ?  459 HOH   A O    1 
HETATM 6580 O O    . HOH   D 3 .   ? 25.420 8.225   -4.768  1.00 24.88 ?  460 HOH   A O    1 
HETATM 6581 O O    . HOH   D 3 .   ? 29.874 -1.932  -12.724 1.00 43.30 ?  461 HOH   A O    1 
HETATM 6582 O O    . HOH   D 3 .   ? 19.919 -17.368 -5.076  1.00 23.78 ?  462 HOH   A O    1 
HETATM 6583 O O    . HOH   D 3 .   ? 24.842 5.621   20.763  1.00 51.84 ?  463 HOH   A O    1 
HETATM 6584 O O    . HOH   D 3 .   ? 11.986 -13.404 16.355  1.00 44.85 ?  464 HOH   A O    1 
HETATM 6585 O O    . HOH   D 3 .   ? 23.211 -22.366 -3.307  1.00 35.17 ?  465 HOH   A O    1 
HETATM 6586 O O    . HOH   D 3 .   ? 24.597 14.557  7.867   1.00 35.53 ?  466 HOH   A O    1 
HETATM 6587 O O    . HOH   D 3 .   ? 26.944 11.640  -1.342  1.00 29.58 ?  467 HOH   A O    1 
HETATM 6588 O O    . HOH   D 3 .   ? 23.488 13.710  5.551   1.00 18.40 ?  468 HOH   A O    1 
HETATM 6589 O O    . HOH   D 3 .   ? 27.506 -11.389 16.570  1.00 36.56 ?  469 HOH   A O    1 
HETATM 6590 O O    . HOH   D 3 .   ? 22.012 5.262   -5.974  1.00 27.31 ?  470 HOH   A O    1 
HETATM 6591 O O    . HOH   D 3 .   ? 15.747 -21.543 3.656   1.00 22.44 ?  471 HOH   A O    1 
HETATM 6592 O O    . HOH   D 3 .   ? 18.774 10.850  11.312  1.00 32.07 ?  472 HOH   A O    1 
HETATM 6593 O O    . HOH   D 3 .   ? 12.328 1.572   17.365  1.00 39.36 ?  473 HOH   A O    1 
HETATM 6594 O O    . HOH   D 3 .   ? 39.641 -7.012  -3.530  1.00 42.51 ?  474 HOH   A O    1 
HETATM 6595 O O    . HOH   D 3 .   ? 10.971 -14.966 -6.083  1.00 34.59 ?  475 HOH   A O    1 
HETATM 6596 O O    . HOH   D 3 .   ? 25.848 10.788  -3.789  1.00 25.72 ?  476 HOH   A O    1 
HETATM 6597 O O    . HOH   D 3 .   ? 35.132 7.437   12.231  1.00 43.29 ?  477 HOH   A O    1 
HETATM 6598 O O    . HOH   D 3 .   ? 28.878 8.985   17.466  1.00 37.93 ?  478 HOH   A O    1 
HETATM 6599 O O    . HOH   D 3 .   ? 18.085 -16.207 -8.856  1.00 39.97 ?  479 HOH   A O    1 
HETATM 6600 O O    . HOH   D 3 .   ? 13.969 -10.316 -10.889 1.00 31.95 ?  480 HOH   A O    1 
HETATM 6601 O O    . HOH   D 3 .   ? 23.156 11.807  -4.092  1.00 18.92 ?  481 HOH   A O    1 
HETATM 6602 O O    . HOH   D 3 .   ? 17.351 -18.744 19.792  1.00 46.00 ?  482 HOH   A O    1 
HETATM 6603 O O    . HOH   D 3 .   ? 30.858 0.738   19.178  1.00 38.04 ?  483 HOH   A O    1 
HETATM 6604 O O    . HOH   D 3 .   ? 40.997 -3.987  -0.364  1.00 35.43 ?  484 HOH   A O    1 
HETATM 6605 O O    . HOH   D 3 .   ? 15.739 -17.163 -7.025  1.00 31.54 ?  485 HOH   A O    1 
HETATM 6606 O O    . HOH   D 3 .   ? 16.815 -20.615 16.160  1.00 26.99 ?  486 HOH   A O    1 
HETATM 6607 O O    . HOH   D 3 .   ? 28.621 -4.628  -12.274 1.00 37.06 ?  487 HOH   A O    1 
HETATM 6608 O O    B HOH   D 3 .   ? 10.528 1.473   0.076   0.16 20.01 ?  488 HOH   A O    1 
HETATM 6609 O O    . HOH   D 3 .   ? 41.771 9.324   -4.055  1.00 30.52 ?  489 HOH   A O    1 
HETATM 6610 O O    . HOH   D 3 .   ? 44.548 10.463  -1.600  1.00 31.88 ?  490 HOH   A O    1 
HETATM 6611 O O    . HOH   D 3 .   ? 23.308 -12.922 19.329  1.00 43.34 ?  491 HOH   A O    1 
HETATM 6612 O O    . HOH   D 3 .   ? 8.214  -3.088  -5.671  1.00 40.19 ?  492 HOH   A O    1 
HETATM 6613 O O    . HOH   D 3 .   ? 28.707 -7.873  -15.293 1.00 43.87 ?  493 HOH   A O    1 
HETATM 6614 O O    . HOH   D 3 .   ? 31.488 -0.608  -10.556 1.00 26.23 ?  494 HOH   A O    1 
HETATM 6615 O O    . HOH   D 3 .   ? 18.446 -23.229 1.896   1.00 42.24 ?  495 HOH   A O    1 
HETATM 6616 O O    B HOH   D 3 .   ? 11.144 1.311   -2.494  0.16 16.57 ?  496 HOH   A O    1 
HETATM 6617 O O    . HOH   D 3 .   ? 16.023 -6.700  -11.790 1.00 41.33 ?  497 HOH   A O    1 
HETATM 6618 O O    . HOH   D 3 .   ? 39.180 2.370   7.582   1.00 29.87 ?  498 HOH   A O    1 
HETATM 6619 O O    . HOH   D 3 .   ? 40.561 -0.246  -7.796  1.00 33.84 ?  499 HOH   A O    1 
HETATM 6620 O O    . HOH   D 3 .   ? 20.023 -22.351 4.158   1.00 28.11 ?  500 HOH   A O    1 
HETATM 6621 O O    . HOH   D 3 .   ? 30.785 5.814   -14.702 1.00 34.47 ?  501 HOH   A O    1 
HETATM 6622 O O    . HOH   D 3 .   ? 14.100 -25.356 8.882   1.00 29.23 ?  502 HOH   A O    1 
HETATM 6623 O O    . HOH   D 3 .   ? 16.167 -23.389 5.690   1.00 26.77 ?  503 HOH   A O    1 
HETATM 6624 O O    . HOH   D 3 .   ? 30.774 -5.787  -11.822 1.00 44.82 ?  504 HOH   A O    1 
HETATM 6625 O O    . HOH   D 3 .   ? 37.413 -6.669  7.509   1.00 23.80 ?  505 HOH   A O    1 
HETATM 6626 O O    B HOH   D 3 .   ? 14.793 7.874   4.934   0.16 18.42 ?  506 HOH   A O    1 
HETATM 6627 O O    . HOH   D 3 .   ? 23.126 -23.778 1.620   1.00 29.68 ?  507 HOH   A O    1 
HETATM 6628 O O    . HOH   D 3 .   ? 39.547 -0.025  6.607   1.00 29.77 ?  508 HOH   A O    1 
HETATM 6629 O O    . HOH   D 3 .   ? 29.008 14.460  0.891   1.00 41.94 ?  509 HOH   A O    1 
HETATM 6630 O O    . HOH   D 3 .   ? 38.042 13.964  6.754   1.00 40.47 ?  510 HOH   A O    1 
HETATM 6631 O O    . HOH   D 3 .   ? 20.541 -16.140 -7.363  1.00 29.07 ?  511 HOH   A O    1 
HETATM 6632 O O    . HOH   D 3 .   ? 36.494 -6.496  10.141  1.00 42.89 ?  512 HOH   A O    1 
HETATM 6633 O O    . HOH   D 3 .   ? 22.038 -24.068 4.445   1.00 26.11 ?  513 HOH   A O    1 
HETATM 6634 O O    . HOH   D 3 .   ? 17.383 -6.669  -14.202 1.00 36.90 ?  514 HOH   A O    1 
HETATM 6635 O O    A HOH   D 3 .   ? 14.863 8.632   4.925   0.84 38.19 ?  515 HOH   A O    1 
HETATM 6636 O O    . HOH   D 3 .   ? 24.109 9.030   -7.222  1.00 34.65 ?  516 HOH   A O    1 
HETATM 6637 O O    . HOH   D 3 .   ? 16.423 -21.159 18.789  1.00 34.61 ?  517 HOH   A O    1 
HETATM 6638 O O    . HOH   D 3 .   ? 15.905 -12.209 27.475  1.00 41.40 ?  518 HOH   A O    1 
HETATM 6639 O O    . HOH   D 3 .   ? 14.677 -22.809 19.867  1.00 31.39 ?  519 HOH   A O    1 
HETATM 6640 O O    . HOH   E 3 .   ? 29.844 -22.426 5.467   1.00 20.41 ?  201 HOH   B O    1 
HETATM 6641 O O    . HOH   E 3 .   ? 48.139 -6.894  15.568  1.00 31.59 ?  202 HOH   B O    1 
HETATM 6642 O O    . HOH   E 3 .   ? 41.815 -35.967 -17.300 1.00 31.27 ?  203 HOH   B O    1 
HETATM 6643 O O    . HOH   E 3 .   ? 27.827 -41.753 -15.187 1.00 35.93 ?  204 HOH   B O    1 
HETATM 6644 O O    . HOH   E 3 .   ? 59.204 -18.731 6.810   1.00 37.73 ?  205 HOH   B O    1 
HETATM 6645 O O    . HOH   E 3 .   ? 37.970 -39.474 -0.228  1.00 41.13 ?  206 HOH   B O    1 
HETATM 6646 O O    . HOH   E 3 .   ? 49.453 -22.683 -19.772 1.00 48.03 ?  207 HOH   B O    1 
HETATM 6647 O O    . HOH   E 3 .   ? 41.398 -7.776  5.482   1.00 37.26 ?  208 HOH   B O    1 
HETATM 6648 O O    . HOH   E 3 .   ? 27.728 -29.218 -1.857  1.00 34.34 ?  209 HOH   B O    1 
HETATM 6649 O O    . HOH   E 3 .   ? 47.443 -7.384  -3.951  1.00 40.35 ?  210 HOH   B O    1 
HETATM 6650 O O    . HOH   E 3 .   ? 58.229 -12.983 8.389   1.00 32.27 ?  211 HOH   B O    1 
HETATM 6651 O O    . HOH   E 3 .   ? 29.919 -26.303 4.002   1.00 27.31 ?  212 HOH   B O    1 
HETATM 6652 O O    . HOH   E 3 .   ? 56.379 -19.732 7.289   1.00 31.89 ?  213 HOH   B O    1 
HETATM 6653 O O    . HOH   E 3 .   ? 50.273 -3.366  7.186   1.00 34.22 ?  214 HOH   B O    1 
HETATM 6654 O O    . HOH   E 3 .   ? 52.953 -13.467 -20.394 1.00 35.79 ?  215 HOH   B O    1 
HETATM 6655 O O    . HOH   E 3 .   ? 30.232 -41.048 -8.164  1.00 16.49 ?  216 HOH   B O    1 
HETATM 6656 O O    . HOH   E 3 .   ? 29.869 -34.219 -0.442  1.00 34.28 ?  217 HOH   B O    1 
HETATM 6657 O O    . HOH   E 3 .   ? 54.507 -9.354  -8.757  1.00 18.97 ?  218 HOH   B O    1 
HETATM 6658 O O    . HOH   E 3 .   ? 44.465 -7.263  2.081   1.00 34.08 ?  219 HOH   B O    1 
HETATM 6659 O O    . HOH   E 3 .   ? 57.776 -24.462 5.031   1.00 35.97 ?  220 HOH   B O    1 
HETATM 6660 O O    . HOH   E 3 .   ? 56.711 -30.791 -7.776  1.00 29.94 ?  221 HOH   B O    1 
HETATM 6661 O O    . HOH   E 3 .   ? 55.428 -16.518 -14.351 1.00 34.24 ?  222 HOH   B O    1 
HETATM 6662 O O    . HOH   E 3 .   ? 50.750 -6.101  0.216   1.00 27.71 ?  223 HOH   B O    1 
HETATM 6663 O O    . HOH   E 3 .   ? 45.158 -34.963 6.847   1.00 38.62 ?  224 HOH   B O    1 
HETATM 6664 O O    . HOH   E 3 .   ? 57.426 -16.245 -12.226 1.00 18.93 ?  225 HOH   B O    1 
HETATM 6665 O O    . HOH   E 3 .   ? 39.359 -10.918 6.104   1.00 26.07 ?  226 HOH   B O    1 
HETATM 6666 O O    . HOH   E 3 .   ? 57.216 -26.845 -7.645  1.00 39.36 ?  227 HOH   B O    1 
HETATM 6667 O O    . HOH   E 3 .   ? 37.130 -19.781 -18.110 1.00 39.08 ?  228 HOH   B O    1 
HETATM 6668 O O    . HOH   E 3 .   ? 34.570 -36.392 -7.211  1.00 18.01 ?  229 HOH   B O    1 
HETATM 6669 O O    . HOH   E 3 .   ? 41.384 -9.664  13.081  1.00 22.05 ?  230 HOH   B O    1 
HETATM 6670 O O    . HOH   E 3 .   ? 48.554 -36.556 -15.501 1.00 41.91 ?  231 HOH   B O    1 
HETATM 6671 O O    . HOH   E 3 .   ? 35.995 -43.294 -8.538  1.00 33.81 ?  232 HOH   B O    1 
HETATM 6672 O O    . HOH   E 3 .   ? 41.529 -39.181 -14.932 1.00 21.94 ?  233 HOH   B O    1 
HETATM 6673 O O    . HOH   E 3 .   ? 44.972 -43.553 -10.529 1.00 27.88 ?  234 HOH   B O    1 
HETATM 6674 O O    . HOH   E 3 .   ? 40.646 -16.067 14.130  1.00 25.48 ?  235 HOH   B O    1 
HETATM 6675 O O    . HOH   E 3 .   ? 46.378 -1.609  13.308  1.00 26.56 ?  236 HOH   B O    1 
HETATM 6676 O O    . HOH   E 3 .   ? 35.140 -8.004  -3.058  1.00 17.88 ?  237 HOH   B O    1 
HETATM 6677 O O    . HOH   E 3 .   ? 32.821 -43.810 -11.370 1.00 20.04 ?  238 HOH   B O    1 
HETATM 6678 O O    . HOH   E 3 .   ? 39.522 -11.140 0.318   1.00 17.07 ?  239 HOH   B O    1 
HETATM 6679 O O    . HOH   E 3 .   ? 50.760 -12.981 -0.476  1.00 12.35 ?  240 HOH   B O    1 
HETATM 6680 O O    . HOH   E 3 .   ? 25.465 -25.981 -1.380  1.00 31.19 ?  241 HOH   B O    1 
HETATM 6681 O O    . HOH   E 3 .   ? 42.665 -22.886 3.835   1.00 11.85 ?  242 HOH   B O    1 
HETATM 6682 O O    . HOH   E 3 .   ? 51.695 -6.497  4.399   1.00 19.60 ?  243 HOH   B O    1 
HETATM 6683 O O    . HOH   E 3 .   ? 43.092 -43.259 -8.235  1.00 28.63 ?  244 HOH   B O    1 
HETATM 6684 O O    . HOH   E 3 .   ? 28.398 -19.700 -13.117 1.00 23.55 ?  245 HOH   B O    1 
HETATM 6685 O O    . HOH   E 3 .   ? 43.208 -32.390 -17.088 1.00 24.01 ?  246 HOH   B O    1 
HETATM 6686 O O    . HOH   E 3 .   ? 30.904 -28.791 4.269   1.00 25.38 ?  247 HOH   B O    1 
HETATM 6687 O O    . HOH   E 3 .   ? 44.554 -27.811 -0.733  1.00 23.39 ?  248 HOH   B O    1 
HETATM 6688 O O    . HOH   E 3 .   ? 42.609 -25.389 2.619   1.00 15.38 ?  249 HOH   B O    1 
HETATM 6689 O O    . HOH   E 3 .   ? 34.233 -18.533 11.399  1.00 24.34 ?  250 HOH   B O    1 
HETATM 6690 O O    . HOH   E 3 .   ? 29.742 -25.239 -10.814 1.00 17.29 ?  251 HOH   B O    1 
HETATM 6691 O O    . HOH   E 3 .   ? 48.070 -24.528 -17.789 1.00 31.33 ?  252 HOH   B O    1 
HETATM 6692 O O    . HOH   E 3 .   ? 40.364 -12.763 -11.539 1.00 15.25 ?  253 HOH   B O    1 
HETATM 6693 O O    . HOH   E 3 .   ? 41.890 -23.534 9.296   1.00 17.16 ?  254 HOH   B O    1 
HETATM 6694 O O    . HOH   E 3 .   ? 57.662 -24.411 -3.835  1.00 22.27 ?  255 HOH   B O    1 
HETATM 6695 O O    . HOH   E 3 .   ? 51.555 -13.858 11.004  1.00 27.68 ?  256 HOH   B O    1 
HETATM 6696 O O    . HOH   E 3 .   ? 34.917 -24.645 13.852  1.00 29.35 ?  257 HOH   B O    1 
HETATM 6697 O O    . HOH   E 3 .   ? 30.888 -15.749 2.630   1.00 14.15 ?  258 HOH   B O    1 
HETATM 6698 O O    . HOH   E 3 .   ? 38.950 -12.036 12.387  1.00 35.25 ?  259 HOH   B O    1 
HETATM 6699 O O    . HOH   E 3 .   ? 58.207 -10.628 -4.080  1.00 19.72 ?  260 HOH   B O    1 
HETATM 6700 O O    . HOH   E 3 .   ? 49.366 -28.727 -6.939  1.00 15.69 ?  261 HOH   B O    1 
HETATM 6701 O O    . HOH   E 3 .   ? 38.460 -11.082 -2.247  1.00 18.41 ?  262 HOH   B O    1 
HETATM 6702 O O    . HOH   E 3 .   ? 51.001 -39.997 -8.267  1.00 30.31 ?  263 HOH   B O    1 
HETATM 6703 O O    . HOH   E 3 .   ? 33.532 -16.995 8.063   1.00 19.32 ?  264 HOH   B O    1 
HETATM 6704 O O    . HOH   E 3 .   ? 57.523 -9.237  1.406   1.00 20.17 ?  265 HOH   B O    1 
HETATM 6705 O O    . HOH   E 3 .   ? 31.838 -17.995 -14.584 1.00 31.25 ?  266 HOH   B O    1 
HETATM 6706 O O    . HOH   E 3 .   ? 48.052 -22.778 5.830   1.00 17.57 ?  267 HOH   B O    1 
HETATM 6707 O O    . HOH   E 3 .   ? 30.592 -42.280 -10.629 1.00 29.05 ?  268 HOH   B O    1 
HETATM 6708 O O    . HOH   E 3 .   ? 49.760 -0.519  10.299  1.00 32.41 ?  269 HOH   B O    1 
HETATM 6709 O O    . HOH   E 3 .   ? 34.942 -33.369 -19.233 1.00 28.72 ?  270 HOH   B O    1 
HETATM 6710 O O    . HOH   E 3 .   ? 28.503 -30.846 -14.738 1.00 29.61 ?  271 HOH   B O    1 
HETATM 6711 O O    . HOH   E 3 .   ? 42.364 -9.907  9.364   1.00 21.23 ?  272 HOH   B O    1 
HETATM 6712 O O    . HOH   E 3 .   ? 46.659 -31.272 -4.821  1.00 21.33 ?  273 HOH   B O    1 
HETATM 6713 O O    . HOH   E 3 .   ? 27.153 -31.847 -10.023 1.00 21.00 ?  274 HOH   B O    1 
HETATM 6714 O O    . HOH   E 3 .   ? 57.107 -12.138 12.358  1.00 37.48 ?  275 HOH   B O    1 
HETATM 6715 O O    . HOH   E 3 .   ? 43.407 -15.807 -12.193 1.00 14.40 ?  276 HOH   B O    1 
HETATM 6716 O O    . HOH   E 3 .   ? 42.403 -34.724 3.742   1.00 24.79 ?  277 HOH   B O    1 
HETATM 6717 O O    . HOH   E 3 .   ? 46.876 -29.597 9.813   1.00 30.92 ?  278 HOH   B O    1 
HETATM 6718 O O    . HOH   E 3 .   ? 28.274 -34.364 -9.439  1.00 19.59 ?  279 HOH   B O    1 
HETATM 6719 O O    . HOH   E 3 .   ? 56.953 -8.634  8.450   1.00 19.61 ?  280 HOH   B O    1 
HETATM 6720 O O    . HOH   E 3 .   ? 27.983 -22.887 -8.023  1.00 17.70 ?  281 HOH   B O    1 
HETATM 6721 O O    . HOH   E 3 .   ? 56.222 -23.553 -14.760 1.00 27.40 ?  282 HOH   B O    1 
HETATM 6722 O O    . HOH   E 3 .   ? 48.434 -25.078 3.093   1.00 13.27 ?  283 HOH   B O    1 
HETATM 6723 O O    . HOH   E 3 .   ? 34.480 -12.777 2.610   1.00 25.26 ?  284 HOH   B O    1 
HETATM 6724 O O    . HOH   E 3 .   ? 33.559 -15.316 -13.988 1.00 21.16 ?  285 HOH   B O    1 
HETATM 6725 O O    . HOH   E 3 .   ? 27.602 -26.725 -15.653 1.00 32.36 ?  286 HOH   B O    1 
HETATM 6726 O O    . HOH   E 3 .   ? 48.731 -20.037 5.919   1.00 14.27 ?  287 HOH   B O    1 
HETATM 6727 O O    . HOH   E 3 .   ? 51.260 -37.627 -9.624  1.00 24.80 ?  288 HOH   B O    1 
HETATM 6728 O O    . HOH   E 3 .   ? 35.124 -33.593 4.497   1.00 28.85 ?  289 HOH   B O    1 
HETATM 6729 O O    . HOH   E 3 .   ? 36.856 -12.771 -1.530  1.00 25.78 ?  290 HOH   B O    1 
HETATM 6730 O O    . HOH   E 3 .   ? 41.185 -5.500  11.535  1.00 43.77 ?  291 HOH   B O    1 
HETATM 6731 O O    . HOH   E 3 .   ? 45.352 -33.427 -15.934 1.00 24.26 ?  292 HOH   B O    1 
HETATM 6732 O O    . HOH   E 3 .   ? 59.792 -15.349 8.176   1.00 31.98 ?  293 HOH   B O    1 
HETATM 6733 O O    . HOH   E 3 .   ? 45.929 -40.411 -3.652  1.00 28.30 ?  294 HOH   B O    1 
HETATM 6734 O O    . HOH   E 3 .   ? 47.099 -33.995 -4.647  1.00 17.57 ?  295 HOH   B O    1 
HETATM 6735 O O    . HOH   E 3 .   ? 40.276 -10.838 -9.530  1.00 17.37 ?  296 HOH   B O    1 
HETATM 6736 O O    . HOH   E 3 .   ? 42.855 -20.323 -20.758 1.00 35.86 ?  297 HOH   B O    1 
HETATM 6737 O O    . HOH   E 3 .   ? 42.731 -12.295 -18.521 1.00 29.10 ?  298 HOH   B O    1 
HETATM 6738 O O    . HOH   E 3 .   ? 44.643 -27.485 1.960   1.00 15.91 ?  299 HOH   B O    1 
HETATM 6739 O O    . HOH   E 3 .   ? 62.826 -20.144 -0.815  1.00 39.37 ?  300 HOH   B O    1 
HETATM 6740 O O    . HOH   E 3 .   ? 52.654 -35.638 -8.645  1.00 27.53 ?  301 HOH   B O    1 
HETATM 6741 O O    . HOH   E 3 .   ? 52.541 -10.436 13.042  1.00 22.48 ?  302 HOH   B O    1 
HETATM 6742 O O    . HOH   E 3 .   ? 42.333 -9.925  -14.921 1.00 36.00 ?  303 HOH   B O    1 
HETATM 6743 O O    . HOH   E 3 .   ? 37.346 -35.688 7.210   1.00 33.65 ?  304 HOH   B O    1 
HETATM 6744 O O    . HOH   E 3 .   ? 49.953 -24.673 5.812   1.00 34.00 ?  305 HOH   B O    1 
HETATM 6745 O O    . HOH   E 3 .   ? 37.561 -18.134 13.117  1.00 29.96 ?  306 HOH   B O    1 
HETATM 6746 O O    . HOH   E 3 .   ? 32.846 -34.616 -5.920  1.00 17.28 ?  307 HOH   B O    1 
HETATM 6747 O O    . HOH   E 3 .   ? 43.551 -15.400 18.195  1.00 31.51 ?  308 HOH   B O    1 
HETATM 6748 O O    . HOH   E 3 .   ? 44.086 -29.376 -4.665  1.00 23.22 ?  309 HOH   B O    1 
HETATM 6749 O O    . HOH   E 3 .   ? 25.974 -21.489 -3.559  1.00 16.56 ?  310 HOH   B O    1 
HETATM 6750 O O    . HOH   E 3 .   ? 48.179 -32.648 -16.618 1.00 41.93 ?  311 HOH   B O    1 
HETATM 6751 O O    . HOH   E 3 .   ? 62.698 -13.569 4.709   1.00 26.48 ?  312 HOH   B O    1 
HETATM 6752 O O    . HOH   E 3 .   ? 53.130 -16.049 -12.771 1.00 26.98 ?  313 HOH   B O    1 
HETATM 6753 O O    . HOH   E 3 .   ? 53.484 -30.234 4.520   1.00 18.48 ?  314 HOH   B O    1 
HETATM 6754 O O    . HOH   E 3 .   ? 37.875 -10.252 -10.784 1.00 17.66 ?  315 HOH   B O    1 
HETATM 6755 O O    . HOH   E 3 .   ? 52.582 -29.242 -13.056 1.00 25.36 ?  316 HOH   B O    1 
HETATM 6756 O O    . HOH   E 3 .   ? 51.701 -5.939  -7.900  1.00 43.64 ?  317 HOH   B O    1 
HETATM 6757 O O    . HOH   E 3 .   ? 41.739 -8.100  1.370   1.00 24.60 ?  318 HOH   B O    1 
HETATM 6758 O O    . HOH   E 3 .   ? 43.219 -21.461 10.649  1.00 16.11 ?  319 HOH   B O    1 
HETATM 6759 O O    . HOH   E 3 .   ? 43.158 -34.566 0.062   1.00 21.44 ?  320 HOH   B O    1 
HETATM 6760 O O    . HOH   E 3 .   ? 44.609 -24.647 9.570   1.00 20.15 ?  321 HOH   B O    1 
HETATM 6761 O O    . HOH   E 3 .   ? 37.179 -30.610 -21.065 1.00 31.23 ?  322 HOH   B O    1 
HETATM 6762 O O    . HOH   E 3 .   ? 38.366 -12.767 7.926   1.00 18.65 ?  323 HOH   B O    1 
HETATM 6763 O O    . HOH   E 3 .   ? 26.366 -21.040 -6.285  1.00 16.69 ?  324 HOH   B O    1 
HETATM 6764 O O    . HOH   E 3 .   ? 38.392 -9.369  -13.290 1.00 27.64 ?  325 HOH   B O    1 
HETATM 6765 O O    . HOH   E 3 .   ? 41.219 -24.526 15.808  1.00 42.88 ?  326 HOH   B O    1 
HETATM 6766 O O    . HOH   E 3 .   ? 59.981 -17.154 -10.491 1.00 33.46 ?  327 HOH   B O    1 
HETATM 6767 O O    . HOH   E 3 .   ? 51.469 -32.981 -10.843 1.00 38.82 ?  328 HOH   B O    1 
HETATM 6768 O O    . HOH   E 3 .   ? 53.652 -12.574 -22.305 1.00 34.90 ?  329 HOH   B O    1 
HETATM 6769 O O    . HOH   E 3 .   ? 36.742 -12.419 4.265   1.00 18.75 ?  330 HOH   B O    1 
HETATM 6770 O O    . HOH   E 3 .   ? 27.988 -14.804 -9.460  1.00 34.55 ?  331 HOH   B O    1 
HETATM 6771 O O    . HOH   E 3 .   ? 33.608 -31.184 11.052  1.00 35.35 ?  332 HOH   B O    1 
HETATM 6772 O O    . HOH   E 3 .   ? 57.644 -22.046 3.253   1.00 27.85 ?  333 HOH   B O    1 
HETATM 6773 O O    . HOH   E 3 .   ? 47.183 -24.515 8.146   1.00 25.59 ?  334 HOH   B O    1 
HETATM 6774 O O    . HOH   E 3 .   ? 44.219 -1.734  7.590   1.00 45.06 ?  335 HOH   B O    1 
HETATM 6775 O O    . HOH   E 3 .   ? 45.793 -36.259 -16.110 1.00 33.91 ?  336 HOH   B O    1 
HETATM 6776 O O    . HOH   E 3 .   ? 39.508 -23.536 -20.323 1.00 36.66 ?  337 HOH   B O    1 
HETATM 6777 O O    . HOH   E 3 .   ? 47.502 -27.471 1.989   1.00 15.05 ?  338 HOH   B O    1 
HETATM 6778 O O    . HOH   E 3 .   ? 42.871 -43.526 -14.410 1.00 43.99 ?  339 HOH   B O    1 
HETATM 6779 O O    . HOH   E 3 .   ? 48.635 -11.953 -14.026 1.00 26.73 ?  340 HOH   B O    1 
HETATM 6780 O O    . HOH   E 3 .   ? 46.884 -19.876 12.294  1.00 31.51 ?  341 HOH   B O    1 
HETATM 6781 O O    . HOH   E 3 .   ? 37.074 -15.113 -16.527 1.00 38.19 ?  342 HOH   B O    1 
HETATM 6782 O O    . HOH   E 3 .   ? 37.101 -45.196 -9.798  1.00 35.50 ?  343 HOH   B O    1 
HETATM 6783 O O    . HOH   E 3 .   ? 28.871 -42.940 -12.377 1.00 35.50 ?  344 HOH   B O    1 
HETATM 6784 O O    . HOH   E 3 .   ? 38.470 -12.273 -16.299 1.00 41.35 ?  345 HOH   B O    1 
HETATM 6785 O O    . HOH   E 3 .   ? 33.021 -14.686 1.033   1.00 19.25 ?  346 HOH   B O    1 
HETATM 6786 O O    . HOH   E 3 .   ? 39.874 -44.304 -11.230 1.00 38.57 ?  347 HOH   B O    1 
HETATM 6787 O O    . HOH   E 3 .   ? 33.787 -9.366  -8.838  1.00 31.26 ?  348 HOH   B O    1 
HETATM 6788 O O    . HOH   E 3 .   ? 40.416 -43.490 -9.157  1.00 25.70 ?  349 HOH   B O    1 
HETATM 6789 O O    . HOH   E 3 .   ? 27.801 -26.597 -0.615  1.00 30.23 ?  350 HOH   B O    1 
HETATM 6790 O O    . HOH   E 3 .   ? 38.607 -22.306 15.069  1.00 41.55 ?  351 HOH   B O    1 
HETATM 6791 O O    . HOH   E 3 .   ? 55.649 -8.262  10.809  1.00 24.11 ?  352 HOH   B O    1 
HETATM 6792 O O    . HOH   E 3 .   ? 62.568 -20.128 -4.870  1.00 41.45 ?  353 HOH   B O    1 
HETATM 6793 O O    . HOH   E 3 .   ? 34.608 -10.346 7.573   1.00 23.88 ?  354 HOH   B O    1 
HETATM 6794 O O    . HOH   E 3 .   ? 44.216 -37.373 -17.816 1.00 33.33 ?  355 HOH   B O    1 
HETATM 6795 O O    . HOH   E 3 .   ? 56.624 -7.301  3.104   1.00 28.22 ?  356 HOH   B O    1 
HETATM 6796 O O    . HOH   E 3 .   ? 23.210 -23.722 6.748   1.00 33.41 ?  357 HOH   B O    1 
HETATM 6797 O O    . HOH   E 3 .   ? 36.161 -8.528  -9.748  1.00 33.58 ?  358 HOH   B O    1 
HETATM 6798 O O    . HOH   E 3 .   ? 34.110 -7.762  11.481  1.00 39.90 ?  359 HOH   B O    1 
HETATM 6799 O O    . HOH   E 3 .   ? 61.542 -19.907 1.636   1.00 34.23 ?  360 HOH   B O    1 
HETATM 6800 O O    . HOH   E 3 .   ? 43.206 -12.698 -21.210 1.00 38.02 ?  361 HOH   B O    1 
HETATM 6801 O O    . HOH   E 3 .   ? 56.982 -21.564 -16.456 1.00 39.18 ?  362 HOH   B O    1 
HETATM 6802 O O    . HOH   E 3 .   ? 40.241 -8.838  9.902   1.00 35.56 ?  363 HOH   B O    1 
HETATM 6803 O O    . HOH   E 3 .   ? 27.155 -25.975 -11.438 1.00 31.87 ?  364 HOH   B O    1 
HETATM 6804 O O    . HOH   E 3 .   ? 40.148 -11.361 -13.966 1.00 32.33 ?  365 HOH   B O    1 
HETATM 6805 O O    . HOH   E 3 .   ? 54.246 -5.741  2.951   1.00 37.12 ?  366 HOH   B O    1 
HETATM 6806 O O    . HOH   E 3 .   ? 32.515 -23.652 14.053  1.00 38.38 ?  367 HOH   B O    1 
HETATM 6807 O O    . HOH   E 3 .   ? 59.014 -10.465 9.184   1.00 38.10 ?  368 HOH   B O    1 
HETATM 6808 O O    . HOH   E 3 .   ? 36.244 -8.736  8.969   1.00 36.56 ?  369 HOH   B O    1 
HETATM 6809 O O    . HOH   E 3 .   ? 39.886 -7.054  7.817   1.00 39.97 ?  370 HOH   B O    1 
HETATM 6810 O O    . HOH   E 3 .   ? 56.108 -7.832  -0.599  1.00 36.10 ?  371 HOH   B O    1 
HETATM 6811 O O    . HOH   E 3 .   ? 41.832 -10.021 -17.451 1.00 56.86 ?  372 HOH   B O    1 
HETATM 6812 O O    . HOH   E 3 .   ? 52.056 -12.960 13.332  1.00 29.83 ?  373 HOH   B O    1 
HETATM 6813 O O    . HOH   E 3 .   ? 48.482 -26.502 8.731   1.00 39.13 ?  374 HOH   B O    1 
HETATM 6814 O O    . HOH   E 3 .   ? 41.881 -6.802  -4.871  1.00 46.02 ?  375 HOH   B O    1 
HETATM 6815 O O    . HOH   E 3 .   ? 63.096 -12.382 6.917   1.00 35.59 ?  376 HOH   B O    1 
HETATM 6816 O O    . HOH   E 3 .   ? 38.035 -10.556 10.094  1.00 29.16 ?  377 HOH   B O    1 
HETATM 6817 O O    . HOH   E 3 .   ? 36.572 -22.809 13.286  1.00 26.29 ?  378 HOH   B O    1 
HETATM 6818 O O    . HOH   E 3 .   ? 44.120 -5.607  -3.511  1.00 40.11 ?  379 HOH   B O    1 
HETATM 6819 O O    . HOH   E 3 .   ? 42.708 -17.080 -23.230 1.00 42.13 ?  380 HOH   B O    1 
HETATM 6820 O O    . HOH   E 3 .   ? 40.112 -7.651  3.228   1.00 34.66 ?  381 HOH   B O    1 
HETATM 6821 O O    . HOH   E 3 .   ? 52.847 -29.926 7.186   1.00 24.00 ?  382 HOH   B O    1 
HETATM 6822 O O    . HOH   E 3 .   ? 60.516 -22.247 2.814   1.00 45.31 ?  383 HOH   B O    1 
HETATM 6823 O O    . HOH   E 3 .   ? 39.750 -14.090 15.745  1.00 47.88 ?  384 HOH   B O    1 
HETATM 6824 O O    . HOH   E 3 .   ? 25.828 -18.862 -11.927 1.00 37.10 ?  385 HOH   B O    1 
HETATM 6825 O O    . HOH   E 3 .   ? 46.860 -5.391  2.928   1.00 39.98 ?  386 HOH   B O    1 
HETATM 6826 O O    . HOH   E 3 .   ? 40.996 -9.788  15.819  1.00 45.41 ?  387 HOH   B O    1 
HETATM 6827 O O    . HOH   E 3 .   ? 23.945 -20.850 -7.701  1.00 28.06 ?  388 HOH   B O    1 
HETATM 6828 O O    . HOH   E 3 .   ? 35.387 -20.339 13.350  1.00 29.86 ?  389 HOH   B O    1 
HETATM 6829 O O    . HOH   E 3 .   ? 35.362 -33.727 7.274   1.00 39.02 ?  390 HOH   B O    1 
HETATM 6830 O O    . HOH   E 3 .   ? 40.713 -6.620  -0.841  1.00 24.70 ?  391 HOH   B O    1 
HETATM 6831 O O    . HOH   E 3 .   ? 44.105 -31.778 -3.868  1.00 33.85 ?  392 HOH   B O    1 
HETATM 6832 O O    . HOH   E 3 .   ? 27.940 -27.119 2.185   1.00 30.88 ?  393 HOH   B O    1 
HETATM 6833 O O    . HOH   E 3 .   ? 26.645 -27.998 -13.504 1.00 36.53 ?  394 HOH   B O    1 
HETATM 6834 O O    . HOH   E 3 .   ? 24.617 -20.663 -10.493 1.00 37.68 ?  395 HOH   B O    1 
HETATM 6835 O O    . HOH   E 3 .   ? 34.388 -33.479 9.574   1.00 32.79 ?  396 HOH   B O    1 
HETATM 6836 O O    . HOH   E 3 .   ? 50.654 -30.828 8.660   1.00 28.86 ?  397 HOH   B O    1 
HETATM 6837 O O    . HOH   E 3 .   ? 26.852 -30.683 -12.651 1.00 28.88 ?  398 HOH   B O    1 
HETATM 6838 O O    . HOH   E 3 .   ? 45.800 -20.256 15.213  1.00 49.50 ?  399 HOH   B O    1 
HETATM 6839 O O    . HOH   E 3 .   ? 57.679 -6.474  -2.367  1.00 34.08 ?  400 HOH   B O    1 
HETATM 6840 O O    . HOH   E 3 .   ? 40.868 -11.814 -22.308 1.00 41.24 ?  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   ? 0.5953 0.5809 0.6521 -0.0002 -0.0323 0.0802  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.5861 0.5816 0.6176 -0.0051 -0.0190 0.0427  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.5922 0.5785 0.6415 -0.0011 -0.0330 0.0782  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.5833 0.5791 0.6134 -0.0056 -0.0199 0.0447  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5758 0.5674 0.6090 -0.0064 -0.0339 0.0767  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5715 0.5686 0.5939 -0.0090 -0.0253 0.0573  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5774 0.5679 0.6141 -0.0038 -0.0344 0.0823  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5742 0.5706 0.5989 -0.0082 -0.0255 0.0573  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6027 0.5853 0.6528 0.0025  -0.0279 0.0781  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.5902 0.5854 0.6220 -0.0034 -0.0152 0.0359  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6069 0.5884 0.6576 0.0031  -0.0248 0.0778  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.5931 0.5880 0.6269 -0.0028 -0.0135 0.0328  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6052 0.5864 0.6581 0.0045  -0.0249 0.0784  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.5920 0.5868 0.6270 -0.0025 -0.0135 0.0331  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.5538 0.5532 0.5626 -0.0139 -0.0299 0.0710  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5136 0.5221 0.4787 -0.0268 -0.0288 0.0764  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.4676 0.4897 0.4303 -0.0362 -0.0158 0.0564  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.4703 0.4914 0.4193 -0.0359 -0.0207 0.0602  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5172 0.5201 0.4426 -0.0307 -0.0413 0.0965  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5199 0.5159 0.4087 -0.0347 -0.0487 0.1196  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5228 0.5115 0.3872 -0.0357 -0.0469 0.1305  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5188 0.5150 0.3960 -0.0357 -0.0519 0.1315  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4180 0.4504 0.3845 -0.0451 -0.0065 0.0317  5   SER   A N   
47   C CA  . SER   A 5   ? 0.3708 0.4138 0.3458 -0.0496 0.0035  0.0059  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3194 0.3668 0.2919 -0.0454 0.0171  -0.0118 5   SER   A C   
49   O O   . SER   A 5   ? 0.3278 0.3825 0.2948 -0.0333 0.0216  -0.0280 5   SER   A O   
50   C CB  . SER   A 5   ? 0.3793 0.4254 0.3585 -0.0534 0.0054  -0.0003 5   SER   A CB  
51   O OG  . SER   A 5   ? 0.3861 0.4370 0.3654 -0.0539 0.0130  -0.0031 5   SER   A OG  
57   N N   A PHE   A 6   ? 0.2765 0.3279 0.2607 -0.0608 0.0350  -0.0058 6   PHE   A N   
58   N N   B PHE   A 6   ? 0.2986 0.3399 0.2775 -0.0373 0.0183  -0.0113 6   PHE   A N   
59   C CA  A PHE   A 6   ? 0.2442 0.2926 0.2423 -0.0708 0.0430  0.0122  6   PHE   A CA  
60   C CA  B PHE   A 6   ? 0.2772 0.3105 0.2619 -0.0283 0.0176  -0.0077 6   PHE   A CA  
61   C C   A PHE   A 6   ? 0.2419 0.2995 0.2558 -0.0785 0.0622  0.0168  6   PHE   A C   
62   C C   B PHE   A 6   ? 0.2652 0.2944 0.2634 -0.0234 0.0215  -0.0067 6   PHE   A C   
63   O O   A PHE   A 6   ? 0.2502 0.3108 0.2778 -0.0875 0.0555  0.0277  6   PHE   A O   
64   O O   B PHE   A 6   ? 0.2666 0.2971 0.2723 -0.0240 0.0209  -0.0079 6   PHE   A O   
65   C CB  A PHE   A 6   ? 0.2288 0.2608 0.2214 -0.0599 0.0362  0.0240  6   PHE   A CB  
66   C CB  B PHE   A 6   ? 0.2684 0.2967 0.2434 -0.0245 0.0138  -0.0043 6   PHE   A CB  
67   C CG  A PHE   A 6   ? 0.2193 0.2422 0.2104 -0.0488 0.0319  0.0346  6   PHE   A CG  
68   C CG  B PHE   A 6   ? 0.2599 0.2837 0.2293 -0.0217 0.0092  -0.0006 6   PHE   A CG  
69   C CD1 A PHE   A 6   ? 0.2137 0.2328 0.2080 -0.0417 0.0304  0.0457  6   PHE   A CD1 
70   C CD1 B PHE   A 6   ? 0.2561 0.2778 0.2228 -0.0204 0.0079  0.0022  6   PHE   A CD1 
71   C CD2 A PHE   A 6   ? 0.2229 0.2423 0.2261 -0.0370 0.0327  0.0354  6   PHE   A CD2 
72   C CD2 B PHE   A 6   ? 0.2564 0.2781 0.2260 -0.0201 0.0073  0.0006  6   PHE   A CD2 
73   C CE1 A PHE   A 6   ? 0.2111 0.2333 0.2167 -0.0388 0.0320  0.0471  6   PHE   A CE1 
74   C CE1 B PHE   A 6   ? 0.2539 0.2743 0.2205 -0.0198 0.0073  0.0043  6   PHE   A CE1 
75   C CE2 A PHE   A 6   ? 0.2201 0.2421 0.2379 -0.0341 0.0352  0.0321  6   PHE   A CE2 
76   C CE2 B PHE   A 6   ? 0.2538 0.2740 0.2236 -0.0202 0.0070  0.0018  6   PHE   A CE2 
77   C CZ  A PHE   A 6   ? 0.2134 0.2375 0.2239 -0.0389 0.0381  0.0342  6   PHE   A CZ  
78   C CZ  B PHE   A 6   ? 0.2531 0.2729 0.2209 -0.0202 0.0069  0.0028  6   PHE   A CZ  
97   N N   A SER   A 7   ? 0.2348 0.2940 0.2467 -0.0714 0.0826  0.0167  7   SER   A N   
98   N N   B SER   A 7   ? 0.2519 0.2761 0.2582 -0.0184 0.0234  -0.0034 7   SER   A N   
99   C CA  A SER   A 7   ? 0.2395 0.2967 0.2695 -0.0577 0.0834  -0.0069 7   SER   A CA  
100  C CA  B SER   A 7   ? 0.2415 0.2607 0.2549 -0.0130 0.0242  -0.0019 7   SER   A CA  
101  C C   A SER   A 7   ? 0.2271 0.2640 0.2623 -0.0590 0.0886  0.0012  7   SER   A C   
102  C C   B SER   A 7   ? 0.2311 0.2447 0.2387 -0.0092 0.0258  -0.0002 7   SER   A C   
103  O O   A SER   A 7   ? 0.2352 0.2550 0.2689 -0.0645 0.0853  0.0145  7   SER   A O   
104  O O   B SER   A 7   ? 0.2330 0.2432 0.2375 -0.0089 0.0266  0.0018  7   SER   A O   
105  C CB  A SER   A 7   ? 0.2567 0.3281 0.2951 -0.0454 0.0839  -0.0130 7   SER   A CB  
106  C CB  B SER   A 7   ? 0.2430 0.2614 0.2669 -0.0115 0.0250  0.0010  7   SER   A CB  
107  O OG  A SER   A 7   ? 0.2720 0.3484 0.3254 -0.0382 0.0856  -0.0080 7   SER   A OG  
108  O OG  B SER   A 7   ? 0.2445 0.2613 0.2773 -0.0098 0.0259  0.0055  7   SER   A OG  
119  N N   A GLY   A 8   ? 0.2096 0.2426 0.2766 -0.0586 0.0774  -0.0072 8   GLY   A N   
120  N N   B GLY   A 8   ? 0.2190 0.2320 0.2285 -0.0072 0.0247  -0.0003 8   GLY   A N   
121  C CA  A GLY   A 8   ? 0.1992 0.2231 0.2815 -0.0435 0.0686  0.0016  8   GLY   A CA  
122  C CA  B GLY   A 8   ? 0.2093 0.2197 0.2217 -0.0052 0.0205  0.0030  8   GLY   A CA  
123  C C   A GLY   A 8   ? 0.1815 0.2115 0.2753 -0.0285 0.0637  0.0037  8   GLY   A C   
124  C C   B GLY   A 8   ? 0.1979 0.2081 0.2130 -0.0042 0.0174  0.0059  8   GLY   A C   
125  O O   A GLY   A 8   ? 0.1828 0.2137 0.2992 -0.0098 0.0541  -0.0105 8   GLY   A O   
126  O O   B GLY   A 8   ? 0.1985 0.2083 0.2181 -0.0016 0.0148  0.0038  8   GLY   A O   
133  N N   A TYR   A 9   ? 0.1651 0.1970 0.2495 -0.0212 0.0556  0.0120  9   TYR   A N   
134  N N   B TYR   A 9   ? 0.1867 0.1971 0.2004 -0.0052 0.0153  0.0141  9   TYR   A N   
135  C CA  A TYR   A 9   ? 0.1575 0.1822 0.2237 -0.0193 0.0471  0.0220  9   TYR   A CA  
136  C CA  B TYR   A 9   ? 0.1780 0.1883 0.1861 -0.0095 0.0154  0.0186  9   TYR   A CA  
137  C C   A TYR   A 9   ? 0.1552 0.1707 0.2309 -0.0206 0.0421  0.0497  9   TYR   A C   
138  C C   B TYR   A 9   ? 0.1718 0.1834 0.1818 -0.0124 0.0144  0.0273  9   TYR   A C   
139  O O   A TYR   A 9   ? 0.1694 0.1885 0.2517 -0.0256 0.0296  0.0537  9   TYR   A O   
140  O O   B TYR   A 9   ? 0.1710 0.1885 0.1860 -0.0175 0.0175  0.0314  9   TYR   A O   
141  C CB  A TYR   A 9   ? 0.1515 0.1886 0.2248 -0.0165 0.0368  0.0073  9   TYR   A CB  
142  C CB  B TYR   A 9   ? 0.1740 0.1875 0.1804 -0.0102 0.0149  0.0138  9   TYR   A CB  
143  C CG  A TYR   A 9   ? 0.1485 0.1904 0.2264 -0.0079 0.0494  -0.0003 9   TYR   A CG  
144  C CG  B TYR   A 9   ? 0.1698 0.1873 0.1758 -0.0118 0.0206  0.0099  9   TYR   A CG  
145  C CD1 A TYR   A 9   ? 0.1501 0.1966 0.2290 -0.0159 0.0529  0.0003  9   TYR   A CD1 
146  C CD1 B TYR   A 9   ? 0.1687 0.1884 0.1765 -0.0176 0.0249  0.0078  9   TYR   A CD1 
147  C CD2 A TYR   A 9   ? 0.1451 0.1845 0.2285 -0.0106 0.0392  0.0153  9   TYR   A CD2 
148  C CD2 B TYR   A 9   ? 0.1674 0.1863 0.1660 -0.0108 0.0173  0.0092  9   TYR   A CD2 
149  C CE1 A TYR   A 9   ? 0.1592 0.2005 0.2416 -0.0194 0.0541  -0.0008 9   TYR   A CE1 
150  C CE1 B TYR   A 9   ? 0.1672 0.1862 0.1742 -0.0193 0.0265  0.0050  9   TYR   A CE1 
151  C CE2 A TYR   A 9   ? 0.1503 0.1893 0.2339 -0.0131 0.0405  0.0028  9   TYR   A CE2 
152  C CE2 B TYR   A 9   ? 0.1656 0.1857 0.1655 -0.0113 0.0202  0.0073  9   TYR   A CE2 
153  C CZ  A TYR   A 9   ? 0.1543 0.1969 0.2485 -0.0281 0.0552  -0.0041 9   TYR   A CZ  
154  C CZ  B TYR   A 9   ? 0.1641 0.1833 0.1743 -0.0145 0.0272  0.0059  9   TYR   A CZ  
155  O OH  A TYR   A 9   ? 0.1663 0.2063 0.2768 -0.0397 0.0631  -0.0187 9   TYR   A OH  
156  O OH  B TYR   A 9   ? 0.1636 0.1836 0.1901 -0.0144 0.0332  0.0078  9   TYR   A OH  
175  N N   A LEU   A 10  ? 0.1529 0.1557 0.2338 -0.0158 0.0308  0.0391  10  LEU   A N   
176  N N   B LEU   A 10  ? 0.1663 0.1756 0.1733 -0.0115 0.0077  0.0280  10  LEU   A N   
177  C CA  A LEU   A 10  ? 0.1469 0.1540 0.2279 -0.0116 0.0243  0.0497  10  LEU   A CA  
178  C CA  B LEU   A 10  ? 0.1611 0.1701 0.1694 -0.0108 0.0017  0.0276  10  LEU   A CA  
179  C C   A LEU   A 10  ? 0.1412 0.1464 0.2264 -0.0173 0.0212  0.0555  10  LEU   A C   
180  C C   B LEU   A 10  ? 0.1547 0.1591 0.1582 -0.0155 -0.0031 0.0291  10  LEU   A C   
181  O O   A LEU   A 10  ? 0.1426 0.1413 0.2349 -0.0196 0.0360  0.0501  10  LEU   A O   
182  O O   B LEU   A 10  ? 0.1523 0.1534 0.1620 -0.0203 0.0024  0.0355  10  LEU   A O   
183  C CB  A LEU   A 10  ? 0.1563 0.1658 0.2522 -0.0039 0.0179  0.0595  10  LEU   A CB  
184  C CB  B LEU   A 10  ? 0.1615 0.1731 0.1777 -0.0088 -0.0019 0.0286  10  LEU   A CB  
185  C CG  A LEU   A 10  ? 0.1820 0.1817 0.2836 -0.0026 -0.0116 0.0638  10  LEU   A CG  
186  C CG  B LEU   A 10  ? 0.1632 0.1757 0.1939 -0.0049 -0.0095 0.0295  10  LEU   A CG  
187  C CD1 A LEU   A 10  ? 0.2070 0.1899 0.3035 -0.0223 -0.0042 0.0500  10  LEU   A CD1 
188  C CD1 B LEU   A 10  ? 0.1644 0.1768 0.2015 -0.0102 -0.0071 0.0284  10  LEU   A CD1 
189  C CD2 A LEU   A 10  ? 0.2055 0.2099 0.3025 0.0024  0.0060  0.0426  10  LEU   A CD2 
190  C CD2 B LEU   A 10  ? 0.1719 0.1810 0.2037 -0.0009 -0.0199 0.0275  10  LEU   A CD2 
213  N N   A LYS   A 11  ? 0.1360 0.1517 0.2060 -0.0237 0.0257  0.0451  11  LYS   A N   
214  N N   B LYS   A 11  ? 0.1523 0.1528 0.1462 -0.0179 -0.0101 0.0241  11  LYS   A N   
215  C CA  A LYS   A 11  ? 0.1402 0.1506 0.2058 -0.0271 0.0185  0.0386  11  LYS   A CA  
216  C CA  B LYS   A 11  ? 0.1531 0.1486 0.1360 -0.0162 -0.0082 0.0251  11  LYS   A CA  
217  C C   A LYS   A 11  ? 0.1409 0.1638 0.2014 -0.0314 0.0235  0.0259  11  LYS   A C   
218  C C   B LYS   A 11  ? 0.1441 0.1420 0.1317 -0.0221 -0.0071 0.0192  11  LYS   A C   
219  O O   A LYS   A 11  ? 0.1559 0.1944 0.2449 -0.0584 0.0323  0.0089  11  LYS   A O   
220  O O   B LYS   A 11  ? 0.1384 0.1390 0.1264 -0.0294 -0.0014 0.0027  11  LYS   A O   
221  C CB  A LYS   A 11  ? 0.1455 0.1496 0.2067 -0.0278 0.0111  0.0327  11  LYS   A CB  
222  C CB  B LYS   A 11  ? 0.1595 0.1478 0.1386 -0.0122 -0.0036 0.0234  11  LYS   A CB  
223  C CG  A LYS   A 11  ? 0.1598 0.1489 0.2002 -0.0262 0.0218  0.0378  11  LYS   A CG  
224  C CG  B LYS   A 11  ? 0.1646 0.1494 0.1385 -0.0073 -0.0015 0.0232  11  LYS   A CG  
225  C CD  A LYS   A 11  ? 0.1756 0.1556 0.2037 -0.0244 0.0156  0.0395  11  LYS   A CD  
226  C CD  B LYS   A 11  ? 0.1690 0.1513 0.1440 -0.0040 0.0010  0.0251  11  LYS   A CD  
227  C CE  A LYS   A 11  ? 0.1874 0.1450 0.2008 -0.0230 0.0139  0.0434  11  LYS   A CE  
228  C CE  B LYS   A 11  ? 0.1736 0.1504 0.1458 0.0009  0.0017  0.0293  11  LYS   A CE  
229  N NZ  A LYS   A 11  ? 0.1937 0.1373 0.2026 -0.0078 -0.0030 0.0242  11  LYS   A NZ  
230  N NZ  B LYS   A 11  ? 0.1762 0.1492 0.1428 0.0071  -0.0020 0.0353  11  LYS   A NZ  
257  N N   A LEU   A 12  ? 0.1288 0.1521 0.1802 -0.0275 0.0192  0.0261  12  LEU   A N   
258  N N   B LEU   A 12  ? 0.1384 0.1460 0.1341 -0.0137 -0.0083 0.0183  12  LEU   A N   
259  C CA  A LEU   A 12  ? 0.1369 0.1595 0.1901 -0.0226 0.0053  0.0385  12  LEU   A CA  
260  C CA  B LEU   A 12  ? 0.1376 0.1525 0.1436 -0.0088 -0.0027 0.0172  12  LEU   A CA  
261  C C   A LEU   A 12  ? 0.1439 0.1511 0.1870 -0.0297 0.0073  0.0414  12  LEU   A C   
262  C C   B LEU   A 12  ? 0.1428 0.1537 0.1384 -0.0078 -0.0002 0.0201  12  LEU   A C   
263  O O   A LEU   A 12  ? 0.1471 0.1570 0.1849 -0.0256 0.0181  0.0269  12  LEU   A O   
264  O O   B LEU   A 12  ? 0.1480 0.1552 0.1389 -0.0040 -0.0020 0.0136  12  LEU   A O   
265  C CB  A LEU   A 12  ? 0.1439 0.1592 0.2057 -0.0220 0.0007  0.0524  12  LEU   A CB  
266  C CB  B LEU   A 12  ? 0.1354 0.1580 0.1544 -0.0062 0.0054  0.0196  12  LEU   A CB  
267  C CG  A LEU   A 12  ? 0.1525 0.1749 0.2378 -0.0162 0.0141  0.0675  12  LEU   A CG  
268  C CG  B LEU   A 12  ? 0.1316 0.1599 0.1683 -0.0052 0.0139  0.0191  12  LEU   A CG  
269  C CD1 A LEU   A 12  ? 0.1700 0.1851 0.2540 -0.0080 0.0180  0.0766  12  LEU   A CD1 
270  C CD1 B LEU   A 12  ? 0.1289 0.1612 0.1743 -0.0040 0.0210  0.0205  12  LEU   A CD1 
271  C CD2 A LEU   A 12  ? 0.1518 0.1868 0.2617 -0.0141 0.0159  0.0587  12  LEU   A CD2 
272  C CD2 B LEU   A 12  ? 0.1316 0.1623 0.1735 -0.0054 0.0120  0.0139  12  LEU   A CD2 
295  N N   A THR   A 13  ? 0.1358 0.1494 0.2082 -0.0271 0.0066  0.0347  13  THR   A N   
296  N N   B THR   A 13  ? 0.1434 0.1529 0.1470 -0.0101 -0.0003 0.0223  13  THR   A N   
297  C CA  A THR   A 13  ? 0.1418 0.1452 0.2060 -0.0239 0.0193  0.0331  13  THR   A CA  
298  C CA  B THR   A 13  ? 0.1475 0.1537 0.1533 -0.0162 0.0089  0.0222  13  THR   A CA  
299  C C   A THR   A 13  ? 0.1449 0.1405 0.2187 -0.0220 0.0146  0.0308  13  THR   A C   
300  C C   B THR   A 13  ? 0.1534 0.1550 0.1629 -0.0154 0.0092  0.0263  13  THR   A C   
301  O O   A THR   A 13  ? 0.1419 0.1410 0.2057 -0.0156 0.0154  0.0329  13  THR   A O   
302  O O   B THR   A 13  ? 0.1549 0.1544 0.1653 -0.0190 0.0058  0.0316  13  THR   A O   
303  C CB  A THR   A 13  ? 0.1498 0.1657 0.2262 -0.0190 0.0188  0.0397  13  THR   A CB  
304  C CB  B THR   A 13  ? 0.1477 0.1582 0.1580 -0.0168 0.0176  0.0209  13  THR   A CB  
305  O OG1 A THR   A 13  ? 0.1480 0.1682 0.2525 -0.0305 0.0138  0.0417  13  THR   A OG1 
306  O OG1 B THR   A 13  ? 0.1438 0.1604 0.1615 -0.0196 0.0260  0.0194  13  THR   A OG1 
307  C CG2 A THR   A 13  ? 0.1564 0.1851 0.2413 -0.0227 0.0194  0.0278  13  THR   A CG2 
308  C CG2 B THR   A 13  ? 0.1500 0.1607 0.1641 -0.0138 0.0167  0.0159  13  THR   A CG2 
323  N N   A ASP   A 14  ? 0.1491 0.1413 0.2324 -0.0249 0.0120  0.0378  14  ASP   A N   
324  N N   B ASP   A 14  ? 0.1570 0.1560 0.1697 -0.0127 0.0100  0.0264  14  ASP   A N   
325  C CA  A ASP   A 14  ? 0.1470 0.1480 0.2369 -0.0143 0.0026  0.0465  14  ASP   A CA  
326  C CA  B ASP   A 14  ? 0.1609 0.1582 0.1783 -0.0081 0.0006  0.0276  14  ASP   A CA  
327  C C   A ASP   A 14  ? 0.1463 0.1503 0.2228 -0.0162 -0.0036 0.0465  14  ASP   A C   
328  C C   B ASP   A 14  ? 0.1556 0.1570 0.1661 -0.0077 -0.0049 0.0326  14  ASP   A C   
329  O O   A ASP   A 14  ? 0.1625 0.1689 0.2450 -0.0392 -0.0098 0.0544  14  ASP   A O   
330  O O   B ASP   A 14  ? 0.1585 0.1617 0.1687 -0.0083 -0.0106 0.0380  14  ASP   A O   
331  C CB  A ASP   A 14  ? 0.1655 0.1724 0.2884 -0.0226 0.0079  0.0611  14  ASP   A CB  
332  C CB  B ASP   A 14  ? 0.1712 0.1604 0.2101 -0.0084 -0.0051 0.0270  14  ASP   A CB  
333  C CG  A ASP   A 14  ? 0.1972 0.2279 0.3620 -0.0261 0.0117  0.0546  14  ASP   A CG  
334  C CG  B ASP   A 14  ? 0.1753 0.1670 0.2372 -0.0062 -0.0073 0.0315  14  ASP   A CG  
335  O OD1 A ASP   A 14  ? 0.2126 0.2369 0.3818 -0.0228 -0.0003 0.0508  14  ASP   A OD1 
336  O OD1 B ASP   A 14  ? 0.1781 0.1674 0.2496 -0.0006 -0.0146 0.0355  14  ASP   A OD1 
337  O OD2 A ASP   A 14  ? 0.2263 0.2681 0.4132 -0.0134 0.0065  0.0448  14  ASP   A OD2 
338  O OD2 B ASP   A 14  ? 0.1799 0.1738 0.2468 -0.0075 -0.0100 0.0312  14  ASP   A OD2 
347  N N   A ASN   A 15  ? 0.1357 0.1364 0.2249 -0.0190 0.0076  0.0494  15  ASN   A N   
348  N N   B ASN   A 15  ? 0.1497 0.1520 0.1664 -0.0082 -0.0001 0.0349  15  ASN   A N   
349  C CA  A ASN   A 15  ? 0.1390 0.1405 0.2426 -0.0189 -0.0005 0.0410  15  ASN   A CA  
350  C CA  B ASN   A 15  ? 0.1467 0.1508 0.1675 -0.0084 0.0005  0.0282  15  ASN   A CA  
351  C C   A ASN   A 15  ? 0.1399 0.1364 0.2587 -0.0191 0.0005  0.0488  15  ASN   A C   
352  C C   B ASN   A 15  ? 0.1460 0.1509 0.1711 -0.0121 0.0047  0.0240  15  ASN   A C   
353  O O   A ASN   A 15  ? 0.1395 0.1452 0.2863 -0.0222 -0.0127 0.0516  15  ASN   A O   
354  O O   B ASN   A 15  ? 0.1474 0.1502 0.1819 -0.0102 0.0039  0.0243  15  ASN   A O   
355  C CB  A ASN   A 15  ? 0.1340 0.1455 0.2320 -0.0118 0.0042  0.0362  15  ASN   A CB  
356  C CB  B ASN   A 15  ? 0.1436 0.1516 0.1636 -0.0019 0.0012  0.0256  15  ASN   A CB  
357  C CG  A ASN   A 15  ? 0.1446 0.1470 0.2462 -0.0114 0.0064  0.0243  15  ASN   A CG  
358  C CG  B ASN   A 15  ? 0.1412 0.1515 0.1661 0.0040  0.0054  0.0208  15  ASN   A CG  
359  O OD1 A ASN   A 15  ? 0.1532 0.1510 0.2639 -0.0268 0.0004  0.0348  15  ASN   A OD1 
360  O OD1 B ASN   A 15  ? 0.1383 0.1553 0.1727 0.0015  0.0093  0.0198  15  ASN   A OD1 
361  N ND2 A ASN   A 15  ? 0.1407 0.1543 0.2148 -0.0134 0.0215  0.0248  15  ASN   A ND2 
362  N ND2 B ASN   A 15  ? 0.1408 0.1455 0.1582 0.0116  0.0090  0.0204  15  ASN   A ND2 
375  N N   A VAL   A 16  ? 0.1460 0.1371 0.2428 -0.0139 0.0036  0.0564  16  VAL   A N   
376  N N   B VAL   A 16  ? 0.1451 0.1547 0.1661 -0.0175 0.0049  0.0250  16  VAL   A N   
377  C CA  A VAL   A 16  ? 0.1402 0.1416 0.2348 -0.0119 0.0181  0.0497  16  VAL   A CA  
378  C CA  B VAL   A 16  ? 0.1425 0.1581 0.1662 -0.0201 0.0111  0.0205  16  VAL   A CA  
379  C C   A VAL   A 16  ? 0.1272 0.1366 0.2278 -0.0122 0.0070  0.0424  16  VAL   A C   
380  C C   B VAL   A 16  ? 0.1411 0.1598 0.1615 -0.0208 0.0092  0.0252  16  VAL   A C   
381  O O   A VAL   A 16  ? 0.1210 0.1369 0.2391 -0.0156 0.0151  0.0404  16  VAL   A O   
382  O O   B VAL   A 16  ? 0.1368 0.1606 0.1620 -0.0218 0.0137  0.0290  16  VAL   A O   
383  C CB  A VAL   A 16  ? 0.1429 0.1543 0.2218 0.0011  0.0239  0.0676  16  VAL   A CB  
384  C CB  B VAL   A 16  ? 0.1404 0.1609 0.1695 -0.0218 0.0139  0.0139  16  VAL   A CB  
385  C CG1 A VAL   A 16  ? 0.1526 0.1660 0.2251 0.0045  0.0322  0.0595  16  VAL   A CG1 
386  C CG1 B VAL   A 16  ? 0.1406 0.1621 0.1748 -0.0189 0.0115  0.0109  16  VAL   A CG1 
387  C CG2 A VAL   A 16  ? 0.1467 0.1722 0.2380 0.0043  0.0371  0.0630  16  VAL   A CG2 
388  C CG2 B VAL   A 16  ? 0.1374 0.1620 0.1738 -0.0285 0.0191  0.0074  16  VAL   A CG2 
407  N N   A TYR   A 17  ? 0.1239 0.1363 0.2259 -0.0096 0.0199  0.0430  17  TYR   A N   
408  N N   B TYR   A 17  ? 0.1444 0.1596 0.1598 -0.0192 0.0093  0.0250  17  TYR   A N   
409  C CA  A TYR   A 17  ? 0.1322 0.1373 0.2142 -0.0137 0.0149  0.0451  17  TYR   A CA  
410  C CA  B TYR   A 17  ? 0.1494 0.1602 0.1570 -0.0210 0.0085  0.0251  17  TYR   A CA  
411  C C   A TYR   A 17  ? 0.1360 0.1329 0.2341 -0.0127 0.0204  0.0422  17  TYR   A C   
412  C C   B TYR   A 17  ? 0.1498 0.1621 0.1581 -0.0210 0.0137  0.0322  17  TYR   A C   
413  O O   A TYR   A 17  ? 0.1304 0.1347 0.2279 -0.0123 0.0234  0.0499  17  TYR   A O   
414  O O   B TYR   A 17  ? 0.1489 0.1637 0.1573 -0.0231 0.0169  0.0426  17  TYR   A O   
415  C CB  A TYR   A 17  ? 0.1443 0.1384 0.2168 -0.0191 0.0117  0.0425  17  TYR   A CB  
416  C CB  B TYR   A 17  ? 0.1563 0.1592 0.1601 -0.0209 0.0035  0.0205  17  TYR   A CB  
417  C CG  A TYR   A 17  ? 0.1615 0.1489 0.2210 -0.0227 0.0036  0.0332  17  TYR   A CG  
418  C CG  B TYR   A 17  ? 0.1634 0.1597 0.1655 -0.0196 -0.0025 0.0166  17  TYR   A CG  
419  C CD1 A TYR   A 17  ? 0.1685 0.1624 0.2289 -0.0128 -0.0060 0.0364  17  TYR   A CD1 
420  C CD1 B TYR   A 17  ? 0.1645 0.1614 0.1719 -0.0170 -0.0051 0.0195  17  TYR   A CD1 
421  C CD2 A TYR   A 17  ? 0.1728 0.1556 0.2070 -0.0333 0.0107  0.0324  17  TYR   A CD2 
422  C CD2 B TYR   A 17  ? 0.1696 0.1617 0.1646 -0.0213 -0.0043 0.0144  17  TYR   A CD2 
423  C CE1 A TYR   A 17  ? 0.1827 0.1631 0.2297 -0.0124 -0.0150 0.0382  17  TYR   A CE1 
424  C CE1 B TYR   A 17  ? 0.1677 0.1619 0.1770 -0.0156 -0.0104 0.0202  17  TYR   A CE1 
425  C CE2 A TYR   A 17  ? 0.1879 0.1579 0.2086 -0.0316 0.0036  0.0219  17  TYR   A CE2 
426  C CE2 B TYR   A 17  ? 0.1747 0.1627 0.1693 -0.0200 -0.0079 0.0128  17  TYR   A CE2 
427  C CZ  A TYR   A 17  ? 0.1965 0.1562 0.2208 -0.0225 -0.0185 0.0385  17  TYR   A CZ  
428  C CZ  B TYR   A 17  ? 0.1762 0.1626 0.1758 -0.0175 -0.0143 0.0178  17  TYR   A CZ  
429  O OH  A TYR   A 17  ? 0.2136 0.1572 0.2279 -0.0231 -0.0165 0.0395  17  TYR   A OH  
430  O OH  B TYR   A 17  ? 0.1854 0.1633 0.1825 -0.0173 -0.0186 0.0193  17  TYR   A OH  
449  N N   A ILE   A 18  ? 0.1370 0.1374 0.2318 -0.0086 0.0241  0.0552  18  ILE   A N   
450  N N   B ILE   A 18  ? 0.1488 0.1635 0.1585 -0.0181 0.0178  0.0343  18  ILE   A N   
451  C CA  A ILE   A 18  ? 0.1380 0.1427 0.2320 -0.0102 0.0319  0.0502  18  ILE   A CA  
452  C CA  B ILE   A 18  ? 0.1486 0.1658 0.1618 -0.0156 0.0253  0.0312  18  ILE   A CA  
453  C C   A ILE   A 18  ? 0.1418 0.1501 0.2408 -0.0123 0.0275  0.0503  18  ILE   A C   
454  C C   B ILE   A 18  ? 0.1543 0.1695 0.1681 -0.0108 0.0210  0.0287  18  ILE   A C   
455  O O   A ILE   A 18  ? 0.1366 0.1641 0.2463 -0.0184 0.0386  0.0657  18  ILE   A O   
456  O O   B ILE   A 18  ? 0.1534 0.1719 0.1656 -0.0125 0.0179  0.0277  18  ILE   A O   
457  C CB  A ILE   A 18  ? 0.1481 0.1491 0.2174 -0.0016 0.0241  0.0682  18  ILE   A CB  
458  C CB  B ILE   A 18  ? 0.1462 0.1668 0.1608 -0.0179 0.0357  0.0343  18  ILE   A CB  
459  C CG1 A ILE   A 18  ? 0.1642 0.1638 0.2341 0.0045  0.0092  0.0736  18  ILE   A CG1 
460  C CG1 B ILE   A 18  ? 0.1456 0.1694 0.1645 -0.0241 0.0401  0.0358  18  ILE   A CG1 
461  C CG2 A ILE   A 18  ? 0.1503 0.1537 0.2284 -0.0026 0.0240  0.0477  18  ILE   A CG2 
462  C CG2 B ILE   A 18  ? 0.1496 0.1698 0.1634 -0.0212 0.0383  0.0358  18  ILE   A CG2 
463  C CD1 A ILE   A 18  ? 0.1856 0.1773 0.2492 0.0086  -0.0011 0.0698  18  ILE   A CD1 
464  C CD1 B ILE   A 18  ? 0.1460 0.1726 0.1672 -0.0263 0.0456  0.0351  18  ILE   A CD1 
487  N N   A LYS   A 19  ? 0.1421 0.1525 0.2480 -0.0061 0.0512  0.0407  19  LYS   A N   
488  N N   B LYS   A 19  ? 0.1597 0.1717 0.1867 -0.0051 0.0309  0.0258  19  LYS   A N   
489  C CA  A LYS   A 19  ? 0.1542 0.1652 0.2707 -0.0080 0.0508  0.0475  19  LYS   A CA  
490  C CA  B LYS   A 19  ? 0.1657 0.1753 0.2115 -0.0006 0.0360  0.0280  19  LYS   A CA  
491  C C   A LYS   A 19  ? 0.1450 0.1545 0.2822 0.0022  0.0469  0.0475  19  LYS   A C   
492  C C   B LYS   A 19  ? 0.1600 0.1688 0.2384 0.0006  0.0415  0.0392  19  LYS   A C   
493  O O   A LYS   A 19  ? 0.1373 0.1488 0.2862 0.0020  0.0338  0.0553  19  LYS   A O   
494  O O   B LYS   A 19  ? 0.1602 0.1682 0.2276 0.0026  0.0401  0.0424  19  LYS   A O   
495  C CB  A LYS   A 19  ? 0.1683 0.1822 0.2745 -0.0042 0.0681  0.0453  19  LYS   A CB  
496  C CB  B LYS   A 19  ? 0.1768 0.1838 0.2155 0.0035  0.0382  0.0185  19  LYS   A CB  
497  C CG  A LYS   A 19  ? 0.2073 0.2069 0.2754 0.0042  0.0721  0.0341  19  LYS   A CG  
498  C CG  B LYS   A 19  ? 0.1888 0.1918 0.2201 0.0061  0.0379  0.0115  19  LYS   A CG  
499  C CD  A LYS   A 19  ? 0.2420 0.2261 0.2689 0.0023  0.0756  0.0363  19  LYS   A CD  
500  C CD  B LYS   A 19  ? 0.1998 0.1992 0.2254 0.0058  0.0379  0.0084  19  LYS   A CD  
501  C CE  A LYS   A 19  ? 0.2610 0.2344 0.2687 -0.0047 0.0712  0.0330  19  LYS   A CE  
502  C CE  B LYS   A 19  ? 0.2051 0.2030 0.2288 0.0040  0.0383  0.0061  19  LYS   A CE  
503  N NZ  A LYS   A 19  ? 0.2746 0.2388 0.2639 -0.0151 0.0767  0.0212  19  LYS   A NZ  
504  N NZ  B LYS   A 19  ? 0.2082 0.2054 0.2297 0.0033  0.0388  -0.0002 19  LYS   A NZ  
531  N N   . ASN   A 20  ? 0.1546 0.1656 0.2857 -0.0003 0.0473  0.0484  20  ASN   A N   
532  C CA  . ASN   A 20  ? 0.1699 0.1851 0.3050 0.0258  0.0562  0.0530  20  ASN   A CA  
533  C C   . ASN   A 20  ? 0.1888 0.1849 0.2926 0.0136  0.0713  0.0394  20  ASN   A C   
534  O O   . ASN   A 20  ? 0.2189 0.2018 0.3091 -0.0056 0.0728  0.0242  20  ASN   A O   
535  C CB  . ASN   A 20  ? 0.1766 0.2058 0.3340 0.0365  0.0584  0.0690  20  ASN   A CB  
536  C CG  . ASN   A 20  ? 0.1901 0.2209 0.3678 0.0501  0.0669  0.0781  20  ASN   A CG  
537  O OD1 . ASN   A 20  ? 0.2201 0.2316 0.4130 0.0596  0.0847  0.0696  20  ASN   A OD1 
538  N ND2 . ASN   A 20  ? 0.1970 0.2204 0.3777 0.0509  0.0512  0.0828  20  ASN   A ND2 
546  N N   A ALA   A 21  ? 0.1855 0.1787 0.3088 0.0145  0.0597  0.0314  21  ALA   A N   
547  N N   B ALA   A 21  ? 0.1902 0.1839 0.2642 0.0099  0.0582  0.0271  21  ALA   A N   
548  C CA  A ALA   A 21  ? 0.1862 0.1782 0.3096 0.0119  0.0569  0.0349  21  ALA   A CA  
549  C CA  B ALA   A 21  ? 0.1937 0.1844 0.2387 0.0071  0.0496  0.0204  21  ALA   A CA  
550  C C   A ALA   A 21  ? 0.1797 0.1749 0.3028 0.0115  0.0600  0.0298  21  ALA   A C   
551  C C   B ALA   A 21  ? 0.1895 0.1832 0.2182 0.0077  0.0479  0.0148  21  ALA   A C   
552  O O   A ALA   A 21  ? 0.1851 0.1804 0.3098 0.0102  0.0622  0.0337  21  ALA   A O   
553  O O   B ALA   A 21  ? 0.1893 0.1814 0.2145 0.0110  0.0490  0.0111  21  ALA   A O   
554  C CB  A ALA   A 21  ? 0.2032 0.1885 0.3214 0.0030  0.0467  0.0502  21  ALA   A CB  
555  C CB  B ALA   A 21  ? 0.2009 0.1862 0.2397 0.0060  0.0449  0.0212  21  ALA   A CB  
566  N N   A ASP   A 22  ? 0.1877 0.1718 0.2969 0.0006  0.0560  0.0336  22  ASP   A N   
567  N N   B ASP   A 22  ? 0.1886 0.1837 0.2069 0.0026  0.0472  0.0155  22  ASP   A N   
568  C CA  A ASP   A 22  ? 0.1902 0.1777 0.2861 -0.0007 0.0458  0.0303  22  ASP   A CA  
569  C CA  B ASP   A 22  ? 0.1882 0.1853 0.2007 -0.0000 0.0411  0.0118  22  ASP   A CA  
570  C C   A ASP   A 22  ? 0.1751 0.1899 0.2520 -0.0052 0.0475  0.0311  22  ASP   A C   
571  C C   B ASP   A 22  ? 0.1819 0.1866 0.1883 -0.0069 0.0351  0.0127  22  ASP   A C   
572  O O   A ASP   A 22  ? 0.1798 0.2022 0.2578 -0.0075 0.0535  0.0322  22  ASP   A O   
573  O O   B ASP   A 22  ? 0.1783 0.1840 0.1873 -0.0099 0.0347  0.0107  22  ASP   A O   
574  C CB  A ASP   A 22  ? 0.2133 0.1820 0.3293 0.0005  0.0401  0.0155  22  ASP   A CB  
575  C CB  B ASP   A 22  ? 0.1938 0.1850 0.2098 0.0049  0.0432  0.0086  22  ASP   A CB  
576  C CG  A ASP   A 22  ? 0.2329 0.1846 0.3694 -0.0052 0.0265  0.0182  22  ASP   A CG  
577  C CG  B ASP   A 22  ? 0.1972 0.1819 0.2196 0.0102  0.0451  0.0119  22  ASP   A CG  
578  O OD1 A ASP   A 22  ? 0.2241 0.1841 0.3808 -0.0184 0.0091  0.0378  22  ASP   A OD1 
579  O OD1 B ASP   A 22  ? 0.1981 0.1804 0.2130 0.0096  0.0419  0.0213  22  ASP   A OD1 
580  O OD2 A ASP   A 22  ? 0.2601 0.1991 0.3953 0.0087  0.0321  -0.0004 22  ASP   A OD2 
581  O OD2 B ASP   A 22  ? 0.2004 0.1833 0.2286 0.0126  0.0472  0.0131  22  ASP   A OD2 
590  N N   A ILE   A 23  ? 0.1739 0.1840 0.2277 -0.0021 0.0466  0.0334  23  ILE   A N   
591  N N   B ILE   A 23  ? 0.1834 0.1903 0.1811 -0.0066 0.0297  0.0149  23  ILE   A N   
592  C CA  A ILE   A 23  ? 0.1718 0.1731 0.2191 -0.0095 0.0486  0.0298  23  ILE   A CA  
593  C CA  B ILE   A 23  ? 0.1846 0.1936 0.1789 -0.0075 0.0208  0.0151  23  ILE   A CA  
594  C C   A ILE   A 23  ? 0.1686 0.1904 0.2079 -0.0104 0.0566  0.0160  23  ILE   A C   
595  C C   B ILE   A 23  ? 0.1918 0.2038 0.1836 -0.0084 0.0225  0.0099  23  ILE   A C   
596  O O   A ILE   A 23  ? 0.1740 0.1989 0.2142 -0.0043 0.0505  0.0194  23  ILE   A O   
597  O O   B ILE   A 23  ? 0.1921 0.2044 0.1816 -0.0058 0.0228  0.0092  23  ILE   A O   
598  C CB  A ILE   A 23  ? 0.1844 0.1695 0.1936 -0.0029 0.0398  0.0277  23  ILE   A CB  
599  C CB  B ILE   A 23  ? 0.1799 0.1871 0.1662 -0.0059 0.0112  0.0168  23  ILE   A CB  
600  C CG1 A ILE   A 23  ? 0.1899 0.1691 0.1835 0.0062  0.0361  0.0213  23  ILE   A CG1 
601  C CG1 B ILE   A 23  ? 0.1781 0.1832 0.1619 -0.0067 0.0029  0.0142  23  ILE   A CG1 
602  C CG2 A ILE   A 23  ? 0.1898 0.1699 0.1995 -0.0017 0.0405  0.0392  23  ILE   A CG2 
603  C CG2 B ILE   A 23  ? 0.1779 0.1834 0.1624 -0.0028 0.0094  0.0160  23  ILE   A CG2 
604  C CD1 A ILE   A 23  ? 0.1986 0.1691 0.1852 0.0072  0.0207  0.0144  23  ILE   A CD1 
605  C CD1 B ILE   A 23  ? 0.1774 0.1807 0.1617 -0.0054 -0.0035 0.0158  23  ILE   A CD1 
628  N N   A VAL   A 24  ? 0.1814 0.1984 0.2180 -0.0241 0.0555  0.0163  24  VAL   A N   
629  N N   B VAL   A 24  ? 0.2015 0.2125 0.1977 -0.0133 0.0192  0.0097  24  VAL   A N   
630  C CA  A VAL   A 24  ? 0.1988 0.2054 0.2368 -0.0338 0.0579  0.0087  24  VAL   A CA  
631  C CA  B VAL   A 24  ? 0.2122 0.2200 0.2126 -0.0144 0.0176  0.0078  24  VAL   A CA  
632  C C   A VAL   A 24  ? 0.2067 0.2201 0.2403 -0.0323 0.0628  -0.0042 24  VAL   A C   
633  C C   B VAL   A 24  ? 0.2210 0.2298 0.2216 -0.0133 0.0204  0.0018  24  VAL   A C   
634  O O   A VAL   A 24  ? 0.2203 0.2216 0.2411 -0.0194 0.0663  -0.0068 24  VAL   A O   
635  O O   B VAL   A 24  ? 0.2235 0.2292 0.2197 -0.0100 0.0216  0.0017  24  VAL   A O   
636  C CB  A VAL   A 24  ? 0.2077 0.2120 0.2627 -0.0395 0.0553  0.0148  24  VAL   A CB  
637  C CB  B VAL   A 24  ? 0.2139 0.2210 0.2249 -0.0161 0.0121  0.0115  24  VAL   A CB  
638  C CG1 A VAL   A 24  ? 0.2185 0.2206 0.2805 -0.0377 0.0496  0.0075  24  VAL   A CG1 
639  C CG1 B VAL   A 24  ? 0.2163 0.2224 0.2317 -0.0163 0.0094  0.0143  24  VAL   A CG1 
640  C CG2 A VAL   A 24  ? 0.2193 0.2245 0.2687 -0.0301 0.0701  0.0296  24  VAL   A CG2 
641  C CG2 B VAL   A 24  ? 0.2161 0.2229 0.2256 -0.0172 0.0110  0.0118  24  VAL   A CG2 
660  N N   A GLU   A 25  ? 0.2125 0.2551 0.2444 -0.0311 0.0839  -0.0174 25  GLU   A N   
661  N N   B GLU   A 25  ? 0.2290 0.2432 0.2344 -0.0153 0.0244  -0.0033 25  GLU   A N   
662  C CA  A GLU   A 25  ? 0.2310 0.2892 0.2595 -0.0292 0.0960  -0.0183 25  GLU   A CA  
663  C CA  B GLU   A 25  ? 0.2375 0.2563 0.2488 -0.0186 0.0259  -0.0041 25  GLU   A CA  
664  C C   A GLU   A 25  ? 0.2214 0.2929 0.2318 -0.0402 0.0977  -0.0103 25  GLU   A C   
665  C C   B GLU   A 25  ? 0.2328 0.2574 0.2378 -0.0241 0.0290  -0.0043 25  GLU   A C   
666  O O   A GLU   A 25  ? 0.2297 0.3065 0.2459 -0.0461 0.0958  -0.0000 25  GLU   A O   
667  O O   B GLU   A 25  ? 0.2347 0.2603 0.2404 -0.0239 0.0272  -0.0064 25  GLU   A O   
668  C CB  A GLU   A 25  ? 0.2609 0.3183 0.2984 -0.0164 0.1062  -0.0123 25  GLU   A CB  
669  C CB  B GLU   A 25  ? 0.2500 0.2670 0.2792 -0.0155 0.0259  -0.0017 25  GLU   A CB  
670  C CG  A GLU   A 25  ? 0.2997 0.3443 0.3620 -0.0130 0.0830  -0.0071 25  GLU   A CG  
671  C CG  B GLU   A 25  ? 0.2638 0.2766 0.3106 -0.0133 0.0226  0.0005  25  GLU   A CG  
672  C CD  A GLU   A 25  ? 0.3317 0.3690 0.4181 -0.0116 0.0703  -0.0035 25  GLU   A CD  
673  C CD  B GLU   A 25  ? 0.2739 0.2840 0.3386 -0.0126 0.0196  0.0015  25  GLU   A CD  
674  O OE1 A GLU   A 25  ? 0.3424 0.3772 0.4316 -0.0083 0.0595  -0.0123 25  GLU   A OE1 
675  O OE1 B GLU   A 25  ? 0.2770 0.2860 0.3488 -0.0105 0.0183  0.0021  25  GLU   A OE1 
676  O OE2 A GLU   A 25  ? 0.3460 0.3797 0.4528 -0.0127 0.0645  -0.0092 25  GLU   A OE2 
677  O OE2 B GLU   A 25  ? 0.2790 0.2868 0.3510 -0.0152 0.0194  0.0004  25  GLU   A OE2 
690  N N   A GLU   A 26  ? 0.2069 0.2779 0.2323 -0.0570 0.0986  -0.0128 26  GLU   A N   
691  N N   B GLU   A 26  ? 0.2269 0.2544 0.2270 -0.0319 0.0369  -0.0057 26  GLU   A N   
692  C CA  A GLU   A 26  ? 0.2238 0.2653 0.2256 -0.0700 0.0865  0.0029  26  GLU   A CA  
693  C CA  B GLU   A 26  ? 0.2248 0.2509 0.2160 -0.0391 0.0410  -0.0034 26  GLU   A CA  
694  C C   A GLU   A 26  ? 0.2247 0.2483 0.2031 -0.0647 0.0703  0.0058  26  GLU   A C   
695  C C   B GLU   A 26  ? 0.2178 0.2412 0.2013 -0.0472 0.0520  -0.0007 26  GLU   A C   
696  O O   A GLU   A 26  ? 0.2358 0.2478 0.1973 -0.0735 0.0653  0.0073  26  GLU   A O   
697  O O   B GLU   A 26  ? 0.2206 0.2413 0.1963 -0.0459 0.0553  -0.0043 26  GLU   A O   
698  C CB  A GLU   A 26  ? 0.2538 0.2620 0.2533 -0.0803 0.0703  0.0124  26  GLU   A CB  
699  C CB  B GLU   A 26  ? 0.2305 0.2562 0.2247 -0.0367 0.0290  -0.0026 26  GLU   A CB  
700  C CG  A GLU   A 26  ? 0.2797 0.2708 0.3130 -0.0863 0.0661  0.0068  26  GLU   A CG  
701  C CG  B GLU   A 26  ? 0.2361 0.2601 0.2337 -0.0343 0.0214  -0.0018 26  GLU   A CG  
702  C CD  A GLU   A 26  ? 0.2905 0.2761 0.3438 -0.0976 0.0918  0.0025  26  GLU   A CD  
703  C CD  B GLU   A 26  ? 0.2394 0.2626 0.2366 -0.0339 0.0187  -0.0018 26  GLU   A CD  
704  O OE1 A GLU   A 26  ? 0.2806 0.3084 0.3347 -0.0801 0.1269  -0.0469 26  GLU   A OE1 
705  O OE1 B GLU   A 26  ? 0.2402 0.2691 0.2389 -0.0285 0.0227  -0.0043 26  GLU   A OE1 
706  O OE2 A GLU   A 26  ? 0.3081 0.2753 0.3585 -0.0975 0.0862  0.0133  26  GLU   A OE2 
707  O OE2 B GLU   A 26  ? 0.2406 0.2602 0.2267 -0.0371 0.0150  -0.0051 26  GLU   A OE2 
720  N N   . ALA   A 27  ? 0.2078 0.2312 0.1945 -0.0583 0.0596  0.0046  27  ALA   A N   
721  C CA  . ALA   A 27  ? 0.2134 0.2314 0.1825 -0.0500 0.0559  -0.0011 27  ALA   A CA  
722  C C   . ALA   A 27  ? 0.2401 0.2416 0.1888 -0.0549 0.0633  -0.0172 27  ALA   A C   
723  O O   . ALA   A 27  ? 0.2468 0.2360 0.1979 -0.0574 0.0531  -0.0120 27  ALA   A O   
724  C CB  . ALA   A 27  ? 0.1980 0.2235 0.1876 -0.0492 0.0454  0.0041  27  ALA   A CB  
731  N N   . LYS   A 28  ? 0.2717 0.2672 0.1962 -0.0537 0.0635  -0.0467 28  LYS   A N   
732  C CA  . LYS   A 28  ? 0.3168 0.3075 0.2415 -0.0450 0.0596  -0.0641 28  LYS   A CA  
733  C C   . LYS   A 28  ? 0.3371 0.3444 0.2332 -0.0502 0.0701  -0.0527 28  LYS   A C   
734  O O   . LYS   A 28  ? 0.3425 0.3565 0.2700 -0.0487 0.0480  -0.0424 28  LYS   A O   
735  C CB  . LYS   A 28  ? 0.3410 0.3217 0.2906 -0.0273 0.0490  -0.0755 28  LYS   A CB  
736  C CG  . LYS   A 28  ? 0.3599 0.3379 0.3476 -0.0116 0.0432  -0.0700 28  LYS   A CG  
737  C CD  . LYS   A 28  ? 0.3746 0.3593 0.4104 -0.0005 0.0367  -0.0739 28  LYS   A CD  
738  C CE  . LYS   A 28  ? 0.3863 0.3711 0.4596 0.0045  0.0291  -0.0775 28  LYS   A CE  
739  N NZ  . LYS   A 28  ? 0.3968 0.3759 0.4863 0.0100  0.0290  -0.0685 28  LYS   A NZ  
753  N N   . LYS   A 29  ? 0.3484 0.3692 0.2176 -0.0606 0.1008  -0.0324 29  LYS   A N   
754  C CA  . LYS   A 29  ? 0.3689 0.3958 0.2439 -0.0672 0.1079  -0.0115 29  LYS   A CA  
755  C C   . LYS   A 29  ? 0.3644 0.3825 0.2118 -0.0761 0.0981  -0.0024 29  LYS   A C   
756  O O   . LYS   A 29  ? 0.3749 0.3905 0.2312 -0.0648 0.0892  -0.0054 29  LYS   A O   
757  C CB  . LYS   A 29  ? 0.3892 0.4314 0.3087 -0.0598 0.1190  -0.0023 29  LYS   A CB  
758  C CG  . LYS   A 29  ? 0.4087 0.4569 0.3909 -0.0515 0.1183  -0.0015 29  LYS   A CG  
759  C CD  . LYS   A 29  ? 0.4261 0.4779 0.4689 -0.0443 0.1119  -0.0037 29  LYS   A CD  
760  C CE  . LYS   A 29  ? 0.4394 0.4939 0.5247 -0.0403 0.1074  -0.0024 29  LYS   A CE  
761  N NZ  . LYS   A 29  ? 0.4465 0.5048 0.5550 -0.0386 0.1061  -0.0026 29  LYS   A NZ  
775  N N   . VAL   A 30  ? 0.3447 0.3585 0.1931 -0.0926 0.0931  0.0036  30  VAL   A N   
776  C CA  . VAL   A 30  ? 0.3364 0.3397 0.1750 -0.1060 0.0629  0.0244  30  VAL   A CA  
777  C C   . VAL   A 30  ? 0.3360 0.3261 0.1421 -0.1061 0.0474  0.0346  30  VAL   A C   
778  O O   . VAL   A 30  ? 0.3465 0.3329 0.1479 -0.1032 0.0450  0.0384  30  VAL   A O   
779  C CB  . VAL   A 30  ? 0.3351 0.3354 0.2160 -0.1127 0.0393  0.0290  30  VAL   A CB  
780  C CG1 . VAL   A 30  ? 0.3449 0.3366 0.2295 -0.1096 0.0169  0.0361  30  VAL   A CG1 
781  C CG2 . VAL   A 30  ? 0.3301 0.3326 0.2438 -0.1198 0.0484  0.0365  30  VAL   A CG2 
791  N N   . LYS   A 31  ? 0.3247 0.3055 0.1346 -0.1105 0.0267  0.0189  31  LYS   A N   
792  C CA  . LYS   A 31  ? 0.3364 0.3057 0.1562 -0.0958 0.0083  0.0130  31  LYS   A CA  
793  C C   . LYS   A 31  ? 0.3128 0.2802 0.1290 -0.0771 0.0037  0.0457  31  LYS   A C   
794  O O   . LYS   A 31  ? 0.3195 0.2904 0.1431 -0.0704 -0.0098 0.0642  31  LYS   A O   
795  C CB  . LYS   A 31  ? 0.3777 0.3394 0.2720 -0.0884 -0.0158 -0.0154 31  LYS   A CB  
796  C CG  . LYS   A 31  ? 0.4228 0.3746 0.4055 -0.0713 -0.0354 -0.0266 31  LYS   A CG  
797  C CD  . LYS   A 31  ? 0.4584 0.4018 0.5083 -0.0613 -0.0528 -0.0360 31  LYS   A CD  
798  C CE  . LYS   A 31  ? 0.4788 0.4211 0.5736 -0.0575 -0.0659 -0.0447 31  LYS   A CE  
799  N NZ  . LYS   A 31  ? 0.4881 0.4337 0.6039 -0.0573 -0.0713 -0.0487 31  LYS   A NZ  
813  N N   . PRO   A 32  ? 0.2750 0.2495 0.1211 -0.0691 0.0043  0.0373  32  PRO   A N   
814  C CA  . PRO   A 32  ? 0.2661 0.2353 0.1506 -0.0621 -0.0026 0.0450  32  PRO   A CA  
815  C C   . PRO   A 32  ? 0.2626 0.2310 0.1630 -0.0526 -0.0052 0.0541  32  PRO   A C   
816  O O   . PRO   A 32  ? 0.2569 0.2250 0.1640 -0.0487 -0.0248 0.0572  32  PRO   A O   
817  C CB  . PRO   A 32  ? 0.2540 0.2443 0.1563 -0.0605 -0.0104 0.0313  32  PRO   A CB  
818  C CG  . PRO   A 32  ? 0.2470 0.2454 0.1271 -0.0565 -0.0145 0.0221  32  PRO   A CG  
819  C CD  . PRO   A 32  ? 0.2546 0.2394 0.1186 -0.0609 -0.0021 0.0308  32  PRO   A CD  
827  N N   . THR   A 33  ? 0.2676 0.2269 0.1601 -0.0514 -0.0068 0.0587  33  THR   A N   
828  C CA  . THR   A 33  ? 0.2620 0.2253 0.1608 -0.0359 -0.0249 0.0571  33  THR   A CA  
829  C C   . THR   A 33  ? 0.2223 0.2077 0.1618 -0.0360 -0.0269 0.0405  33  THR   A C   
830  O O   . THR   A 33  ? 0.2154 0.2135 0.1592 -0.0325 -0.0393 0.0504  33  THR   A O   
831  C CB  . THR   A 33  ? 0.2885 0.2439 0.1761 -0.0235 -0.0372 0.0750  33  THR   A CB  
832  O OG1 . THR   A 33  ? 0.3095 0.2579 0.2064 -0.0136 -0.0298 0.0879  33  THR   A OG1 
833  C CG2 . THR   A 33  ? 0.2922 0.2530 0.2047 -0.0139 -0.0429 0.0688  33  THR   A CG2 
841  N N   . VAL   A 34  ? 0.1982 0.1939 0.1413 -0.0346 -0.0206 0.0425  34  VAL   A N   
842  C CA  . VAL   A 34  ? 0.1786 0.1773 0.1318 -0.0262 -0.0068 0.0428  34  VAL   A CA  
843  C C   . VAL   A 34  ? 0.1640 0.1674 0.1336 -0.0254 -0.0018 0.0296  34  VAL   A C   
844  O O   . VAL   A 34  ? 0.1704 0.1679 0.1468 -0.0329 0.0001  0.0328  34  VAL   A O   
845  C CB  . VAL   A 34  ? 0.1831 0.1692 0.1544 -0.0216 -0.0059 0.0267  34  VAL   A CB  
846  C CG1 . VAL   A 34  ? 0.1849 0.1703 0.1544 -0.0194 0.0093  0.0180  34  VAL   A CG1 
847  C CG2 . VAL   A 34  ? 0.1889 0.1807 0.1832 -0.0146 -0.0093 0.0262  34  VAL   A CG2 
857  N N   . VAL   A 35  ? 0.1502 0.1581 0.1303 -0.0286 -0.0072 0.0249  35  VAL   A N   
858  C CA  . VAL   A 35  ? 0.1452 0.1545 0.1353 -0.0245 0.0024  0.0205  35  VAL   A CA  
859  C C   . VAL   A 35  ? 0.1316 0.1429 0.1353 -0.0173 0.0091  0.0188  35  VAL   A C   
860  O O   . VAL   A 35  ? 0.1350 0.1504 0.1417 -0.0201 0.0098  0.0135  35  VAL   A O   
861  C CB  . VAL   A 35  ? 0.1509 0.1620 0.1449 -0.0141 0.0159  0.0076  35  VAL   A CB  
862  C CG1 . VAL   A 35  ? 0.1652 0.1631 0.1474 -0.0074 0.0070  -0.0030 35  VAL   A CG1 
863  C CG2 . VAL   A 35  ? 0.1471 0.1602 0.1769 -0.0131 0.0212  0.0041  35  VAL   A CG2 
873  N N   . VAL   A 36  ? 0.1262 0.1405 0.1212 -0.0180 0.0043  0.0212  36  VAL   A N   
874  C CA  . VAL   A 36  ? 0.1273 0.1278 0.1180 -0.0088 0.0089  0.0150  36  VAL   A CA  
875  C C   . VAL   A 36  ? 0.1262 0.1301 0.1285 -0.0138 0.0146  0.0188  36  VAL   A C   
876  O O   . VAL   A 36  ? 0.1283 0.1300 0.1525 -0.0045 0.0184  0.0178  36  VAL   A O   
877  C CB  . VAL   A 36  ? 0.1280 0.1197 0.1327 -0.0134 0.0063  0.0205  36  VAL   A CB  
878  C CG1 . VAL   A 36  ? 0.1343 0.1267 0.1517 -0.0186 0.0119  0.0156  36  VAL   A CG1 
879  C CG2 . VAL   A 36  ? 0.1317 0.1228 0.1610 -0.0034 -0.0053 0.0261  36  VAL   A CG2 
889  N N   . ASN   A 37  ? 0.1221 0.1200 0.1192 -0.0048 0.0074  0.0155  37  ASN   A N   
890  C CA  . ASN   A 37  ? 0.1190 0.1173 0.1231 0.0003  0.0067  0.0181  37  ASN   A CA  
891  C C   . ASN   A 37  ? 0.1155 0.1211 0.1175 -0.0006 0.0154  0.0261  37  ASN   A C   
892  O O   . ASN   A 37  ? 0.1252 0.1296 0.1168 0.0050  0.0078  0.0102  37  ASN   A O   
893  C CB  . ASN   A 37  ? 0.1187 0.1186 0.1348 -0.0001 0.0042  0.0109  37  ASN   A CB  
894  C CG  . ASN   A 37  ? 0.1192 0.1212 0.1387 -0.0020 0.0064  0.0149  37  ASN   A CG  
895  O OD1 . ASN   A 37  ? 0.1177 0.1205 0.1564 0.0010  0.0056  0.0163  37  ASN   A OD1 
896  N ND2 . ASN   A 37  ? 0.1222 0.1266 0.1388 -0.0035 0.0019  0.0281  37  ASN   A ND2 
903  N N   A ALA   A 38  ? 0.1175 0.1251 0.1353 0.0006  0.0123  0.0073  38  ALA   A N   
904  N N   B ALA   A 38  ? 0.1200 0.1265 0.1241 -0.0035 0.0083  0.0199  38  ALA   A N   
905  C CA  A ALA   A 38  ? 0.1241 0.1228 0.1401 -0.0006 -0.0000 0.0019  38  ALA   A CA  
906  C CA  B ALA   A 38  ? 0.1249 0.1316 0.1257 -0.0053 -0.0016 0.0172  38  ALA   A CA  
907  C C   A ALA   A 38  ? 0.1222 0.1226 0.1327 0.0060  -0.0078 0.0026  38  ALA   A C   
908  C C   B ALA   A 38  ? 0.1247 0.1330 0.1293 -0.0027 -0.0085 0.0199  38  ALA   A C   
909  O O   A ALA   A 38  ? 0.1218 0.1236 0.1445 0.0022  -0.0107 0.0043  38  ALA   A O   
910  O O   B ALA   A 38  ? 0.1173 0.1355 0.1362 -0.0063 -0.0166 0.0244  38  ALA   A O   
911  C CB  A ALA   A 38  ? 0.1262 0.1474 0.1702 -0.0117 -0.0083 0.0063  38  ALA   A CB  
912  C CB  B ALA   A 38  ? 0.1273 0.1359 0.1305 -0.0069 -0.0049 0.0079  38  ALA   A CB  
923  N N   A ALA   A 39  ? 0.1207 0.1208 0.1438 0.0031  0.0046  0.0103  39  ALA   A N   
924  N N   B ALA   A 39  ? 0.1333 0.1306 0.1310 -0.0010 -0.0031 0.0233  39  ALA   A N   
925  C CA  A ALA   A 39  ? 0.1225 0.1159 0.1353 0.0022  0.0118  0.0108  39  ALA   A CA  
926  C CA  B ALA   A 39  ? 0.1430 0.1319 0.1379 0.0029  -0.0025 0.0218  39  ALA   A CA  
927  C C   A ALA   A 39  ? 0.1221 0.1148 0.1432 0.0024  0.0090  0.0073  39  ALA   A C   
928  C C   B ALA   A 39  ? 0.1404 0.1257 0.1347 -0.0025 0.0004  0.0188  39  ALA   A C   
929  O O   A ALA   A 39  ? 0.1335 0.1224 0.1334 -0.0005 0.0111  0.0070  39  ALA   A O   
930  O O   B ALA   A 39  ? 0.1366 0.1241 0.1364 -0.0106 0.0025  0.0214  39  ALA   A O   
931  C CB  A ALA   A 39  ? 0.1185 0.1190 0.1503 0.0023  -0.0088 -0.0008 39  ALA   A CB  
932  C CB  B ALA   A 39  ? 0.1532 0.1391 0.1464 0.0089  -0.0070 0.0171  39  ALA   A CB  
943  N N   A ASN   A 40  ? 0.1351 0.1241 0.1435 -0.0069 0.0222  0.0087  40  ASN   A N   
944  N N   B ASN   A 40  ? 0.1436 0.1234 0.1298 -0.0020 0.0060  0.0157  40  ASN   A N   
945  C CA  A ASN   A 40  ? 0.1408 0.1222 0.1551 -0.0022 0.0109  0.0091  40  ASN   A CA  
946  C CA  B ASN   A 40  ? 0.1457 0.1213 0.1333 -0.0012 0.0063  0.0134  40  ASN   A CA  
947  C C   A ASN   A 40  ? 0.1423 0.1146 0.1472 -0.0090 0.0242  0.0144  40  ASN   A C   
948  C C   B ASN   A 40  ? 0.1479 0.1173 0.1319 -0.0040 0.0181  0.0143  40  ASN   A C   
949  O O   A ASN   A 40  ? 0.1355 0.1188 0.1480 -0.0061 0.0202  0.0177  40  ASN   A O   
950  O O   B ASN   A 40  ? 0.1467 0.1171 0.1253 -0.0041 0.0180  0.0125  40  ASN   A O   
951  C CB  A ASN   A 40  ? 0.1492 0.1324 0.1617 0.0018  0.0004  0.0093  40  ASN   A CB  
952  C CB  B ASN   A 40  ? 0.1460 0.1251 0.1363 0.0016  -0.0013 0.0086  40  ASN   A CB  
953  C CG  A ASN   A 40  ? 0.1611 0.1350 0.1867 0.0022  0.0001  0.0123  40  ASN   A CG  
954  C CG  B ASN   A 40  ? 0.1491 0.1266 0.1481 0.0033  -0.0047 0.0053  40  ASN   A CG  
955  O OD1 A ASN   A 40  ? 0.1690 0.1373 0.2174 -0.0031 0.0042  0.0064  40  ASN   A OD1 
956  O OD1 B ASN   A 40  ? 0.1526 0.1280 0.1620 0.0044  -0.0101 0.0004  40  ASN   A OD1 
957  N ND2 A ASN   A 40  ? 0.1688 0.1424 0.2089 0.0029  -0.0015 0.0002  40  ASN   A ND2 
958  N ND2 B ASN   A 40  ? 0.1493 0.1296 0.1551 0.0024  -0.0025 0.0013  40  ASN   A ND2 
971  N N   . VAL   A 41  ? 0.1515 0.1162 0.1406 -0.0053 0.0224  0.0147  41  VAL   A N   
972  C CA  . VAL   A 41  ? 0.1590 0.1220 0.1568 -0.0011 0.0363  0.0174  41  VAL   A CA  
973  C C   . VAL   A 41  ? 0.1501 0.1246 0.1612 -0.0003 0.0378  0.0159  41  VAL   A C   
974  O O   . VAL   A 41  ? 0.1537 0.1202 0.1792 0.0017  0.0322  0.0072  41  VAL   A O   
975  C CB  . VAL   A 41  ? 0.1762 0.1402 0.1607 -0.0105 0.0545  0.0065  41  VAL   A CB  
976  C CG1 . VAL   A 41  ? 0.1873 0.1405 0.1794 -0.0043 0.0541  -0.0050 41  VAL   A CG1 
977  C CG2 . VAL   A 41  ? 0.2020 0.1500 0.1580 -0.0203 0.0559  0.0088  41  VAL   A CG2 
988  N N   A TYR   A 42  ? 0.1399 0.1219 0.1726 -0.0015 0.0391  0.0253  42  TYR   A N   
989  N N   B TYR   A 42  ? 0.1486 0.1257 0.1523 -0.0016 0.0268  0.0178  42  TYR   A N   
990  C CA  A TYR   A 42  ? 0.1412 0.1152 0.1783 -0.0047 0.0386  0.0299  42  TYR   A CA  
991  C CA  B TYR   A 42  ? 0.1486 0.1269 0.1520 -0.0024 0.0186  0.0174  42  TYR   A CA  
992  C C   A TYR   A 42  ? 0.1316 0.1200 0.1801 -0.0063 0.0312  0.0267  42  TYR   A C   
993  C C   B TYR   A 42  ? 0.1392 0.1246 0.1531 -0.0040 0.0180  0.0150  42  TYR   A C   
994  O O   A TYR   A 42  ? 0.1294 0.1193 0.2106 -0.0144 0.0256  0.0088  42  TYR   A O   
995  O O   B TYR   A 42  ? 0.1381 0.1252 0.1565 -0.0057 0.0184  0.0124  42  TYR   A O   
996  C CB  A TYR   A 42  ? 0.1692 0.1285 0.1817 -0.0074 0.0432  0.0308  42  TYR   A CB  
997  C CB  B TYR   A 42  ? 0.1594 0.1339 0.1554 -0.0021 0.0121  0.0160  42  TYR   A CB  
998  C CG  A TYR   A 42  ? 0.1908 0.1374 0.1777 -0.0104 0.0331  0.0405  42  TYR   A CG  
999  C CG  B TYR   A 42  ? 0.1688 0.1384 0.1590 -0.0009 0.0035  0.0166  42  TYR   A CG  
1000 C CD1 A TYR   A 42  ? 0.1973 0.1544 0.1794 -0.0144 0.0402  0.0331  42  TYR   A CD1 
1001 C CD1 B TYR   A 42  ? 0.1702 0.1427 0.1578 -0.0021 0.0017  0.0177  42  TYR   A CD1 
1002 C CD2 A TYR   A 42  ? 0.1994 0.1627 0.1923 -0.0088 0.0238  0.0256  42  TYR   A CD2 
1003 C CD2 B TYR   A 42  ? 0.1730 0.1438 0.1665 0.0002  0.0015  0.0130  42  TYR   A CD2 
1004 C CE1 A TYR   A 42  ? 0.1971 0.1660 0.1820 -0.0216 0.0435  0.0287  42  TYR   A CE1 
1005 C CE1 B TYR   A 42  ? 0.1706 0.1473 0.1627 -0.0046 0.0011  0.0151  42  TYR   A CE1 
1006 C CE2 A TYR   A 42  ? 0.2020 0.1753 0.2053 -0.0225 0.0207  0.0258  42  TYR   A CE2 
1007 C CE2 B TYR   A 42  ? 0.1752 0.1496 0.1697 -0.0018 0.0000  0.0129  42  TYR   A CE2 
1008 C CZ  A TYR   A 42  ? 0.2030 0.1795 0.1876 -0.0284 0.0363  0.0308  42  TYR   A CZ  
1009 C CZ  B TYR   A 42  ? 0.1726 0.1529 0.1684 -0.0049 0.0030  0.0118  42  TYR   A CZ  
1010 O OH  A TYR   A 42  ? 0.2143 0.2063 0.2177 -0.0305 0.0300  0.0225  42  TYR   A OH  
1011 O OH  B TYR   A 42  ? 0.1711 0.1636 0.1789 -0.0087 0.0072  0.0061  42  TYR   A OH  
1030 N N   . LEU   A 43  ? 0.1326 0.1214 0.1529 -0.0057 0.0133  0.0126  43  LEU   A N   
1031 C CA  . LEU   A 43  ? 0.1247 0.1165 0.1596 -0.0077 0.0202  0.0092  43  LEU   A CA  
1032 C C   . LEU   A 43  ? 0.1223 0.1248 0.1642 -0.0033 0.0099  0.0101  43  LEU   A C   
1033 O O   . LEU   A 43  ? 0.1412 0.1269 0.1794 0.0038  -0.0081 0.0047  43  LEU   A O   
1034 C CB  . LEU   A 43  ? 0.1272 0.1147 0.1603 -0.0093 0.0125  0.0067  43  LEU   A CB  
1035 C CG  . LEU   A 43  ? 0.1328 0.1186 0.1690 -0.0023 0.0054  0.0089  43  LEU   A CG  
1036 C CD1 . LEU   A 43  ? 0.1385 0.1262 0.1947 -0.0004 -0.0023 0.0116  43  LEU   A CD1 
1037 C CD2 . LEU   A 43  ? 0.1493 0.1225 0.1724 -0.0017 0.0082  0.0110  43  LEU   A CD2 
1050 N N   A LYS   A 44  ? 0.1280 0.1198 0.1643 -0.0051 0.0104  0.0123  44  LYS   A N   
1051 N N   B LYS   A 44  ? 0.1388 0.1413 0.1643 -0.0054 0.0061  0.0081  44  LYS   A N   
1052 C CA  A LYS   A 44  ? 0.1418 0.1188 0.1621 -0.0034 0.0225  0.0199  44  LYS   A CA  
1053 C CA  B LYS   A 44  ? 0.1576 0.1586 0.1729 -0.0061 0.0044  0.0072  44  LYS   A CA  
1054 C C   A LYS   A 44  ? 0.1299 0.1159 0.1499 0.0009  0.0132  0.0104  44  LYS   A C   
1055 C C   B LYS   A 44  ? 0.1530 0.1551 0.1546 -0.0050 0.0012  0.0058  44  LYS   A C   
1056 O O   A LYS   A 44  ? 0.1416 0.1366 0.1585 -0.0009 0.0150  -0.0037 44  LYS   A O   
1057 O O   B LYS   A 44  ? 0.1541 0.1565 0.1499 -0.0046 0.0026  0.0050  44  LYS   A O   
1058 C CB  A LYS   A 44  ? 0.1722 0.1279 0.2006 0.0037  0.0365  0.0350  44  LYS   A CB  
1059 C CB  B LYS   A 44  ? 0.1795 0.1775 0.2070 -0.0068 0.0058  0.0075  44  LYS   A CB  
1060 C CG  A LYS   A 44  ? 0.2073 0.1575 0.2643 0.0004  0.0596  0.0456  44  LYS   A CG  
1061 C CG  B LYS   A 44  ? 0.1998 0.1953 0.2470 -0.0078 0.0101  0.0083  44  LYS   A CG  
1062 C CD  A LYS   A 44  ? 0.2444 0.2200 0.3687 -0.0104 0.0365  0.0353  44  LYS   A CD  
1063 C CD  B LYS   A 44  ? 0.2183 0.2159 0.2901 -0.0105 0.0068  0.0067  44  LYS   A CD  
1064 C CE  A LYS   A 44  ? 0.2622 0.2598 0.4345 -0.0163 0.0242  0.0328  44  LYS   A CE  
1065 C CE  B LYS   A 44  ? 0.2304 0.2326 0.3205 -0.0128 0.0042  0.0074  44  LYS   A CE  
1066 N NZ  A LYS   A 44  ? 0.2711 0.2849 0.4693 -0.0183 0.0282  0.0355  44  LYS   A NZ  
1067 N NZ  B LYS   A 44  ? 0.2370 0.2447 0.3365 -0.0158 0.0048  0.0092  44  LYS   A NZ  
1094 N N   A HIS   A 45  ? 0.1169 0.1180 0.1491 0.0055  0.0057  0.0198  45  HIS   A N   
1095 N N   B HIS   A 45  ? 0.1484 0.1530 0.1469 -0.0052 -0.0029 0.0061  45  HIS   A N   
1096 C CA  A HIS   A 45  ? 0.1158 0.1193 0.1560 0.0073  -0.0027 0.0200  45  HIS   A CA  
1097 C CA  B HIS   A 45  ? 0.1446 0.1496 0.1450 -0.0068 -0.0064 0.0054  45  HIS   A CA  
1098 C C   A HIS   A 45  ? 0.1236 0.1364 0.1641 0.0087  -0.0012 0.0229  45  HIS   A C   
1099 C C   B HIS   A 45  ? 0.1463 0.1506 0.1466 -0.0069 -0.0014 0.0077  45  HIS   A C   
1100 O O   A HIS   A 45  ? 0.1326 0.1354 0.1822 0.0130  -0.0020 0.0097  45  HIS   A O   
1101 O O   B HIS   A 45  ? 0.1528 0.1484 0.1608 -0.0025 -0.0003 0.0085  45  HIS   A O   
1102 C CB  A HIS   A 45  ? 0.1164 0.1180 0.1555 0.0051  -0.0003 0.0081  45  HIS   A CB  
1103 C CB  B HIS   A 45  ? 0.1369 0.1456 0.1376 -0.0038 -0.0138 0.0023  45  HIS   A CB  
1104 C CG  A HIS   A 45  ? 0.1152 0.1190 0.1445 -0.0006 0.0076  0.0094  45  HIS   A CG  
1105 C CG  B HIS   A 45  ? 0.1253 0.1430 0.1253 -0.0037 -0.0096 0.0020  45  HIS   A CG  
1106 N ND1 A HIS   A 45  ? 0.1121 0.1220 0.1604 -0.0008 0.0060  0.0125  45  HIS   A ND1 
1107 N ND1 B HIS   A 45  ? 0.1190 0.1428 0.1295 -0.0020 -0.0105 0.0081  45  HIS   A ND1 
1108 C CD2 A HIS   A 45  ? 0.1231 0.1220 0.1517 -0.0073 -0.0014 0.0211  45  HIS   A CD2 
1109 C CD2 B HIS   A 45  ? 0.1169 0.1353 0.1133 -0.0034 -0.0097 -0.0039 45  HIS   A CD2 
1110 C CE1 A HIS   A 45  ? 0.1213 0.1242 0.1434 -0.0073 0.0085  0.0254  45  HIS   A CE1 
1111 C CE1 B HIS   A 45  ? 0.1157 0.1344 0.1080 -0.0057 -0.0140 -0.0076 45  HIS   A CE1 
1112 N NE2 A HIS   A 45  ? 0.1236 0.1212 0.1438 -0.0012 0.0065  0.0233  45  HIS   A NE2 
1113 N NE2 B HIS   A 45  ? 0.1137 0.1324 0.1002 -0.0085 -0.0164 -0.0149 45  HIS   A NE2 
1128 N N   A GLY   A 46  ? 0.1358 0.1470 0.1901 0.0206  -0.0171 0.0284  46  GLY   A N   
1129 N N   B GLY   A 46  ? 0.1432 0.1496 0.1434 -0.0110 -0.0002 0.0062  46  GLY   A N   
1130 C CA  A GLY   A 46  ? 0.1418 0.1615 0.2034 0.0180  -0.0099 0.0387  46  GLY   A CA  
1131 C CA  B GLY   A 46  ? 0.1372 0.1507 0.1354 -0.0117 0.0080  0.0081  46  GLY   A CA  
1132 C C   A GLY   A 46  ? 0.1410 0.1502 0.1958 0.0278  -0.0150 0.0502  46  GLY   A C   
1133 C C   B GLY   A 46  ? 0.1326 0.1475 0.1158 -0.0097 0.0173  0.0121  46  GLY   A C   
1134 O O   A GLY   A 46  ? 0.1478 0.1555 0.2120 0.0246  -0.0185 0.0408  46  GLY   A O   
1135 O O   B GLY   A 46  ? 0.1303 0.1473 0.1034 -0.0134 0.0225  0.0068  46  GLY   A O   
1142 N N   A GLY   A 47  ? 0.1403 0.1465 0.1976 0.0250  -0.0120 0.0271  47  GLY   A N   
1143 N N   B GLY   A 47  ? 0.1337 0.1471 0.1172 -0.0034 0.0148  0.0083  47  GLY   A N   
1144 C CA  A GLY   A 47  ? 0.1471 0.1492 0.1977 0.0230  -0.0269 0.0263  47  GLY   A CA  
1145 C CA  B GLY   A 47  ? 0.1275 0.1453 0.1122 -0.0003 0.0106  0.0109  47  GLY   A CA  
1146 C C   A GLY   A 47  ? 0.1424 0.1422 0.1729 0.0240  -0.0278 0.0135  47  GLY   A C   
1147 C C   B GLY   A 47  ? 0.1212 0.1373 0.0966 0.0041  0.0021  0.0106  47  GLY   A C   
1148 O O   A GLY   A 47  ? 0.1447 0.1472 0.1814 0.0236  -0.0275 0.0198  47  GLY   A O   
1149 O O   B GLY   A 47  ? 0.1161 0.1369 0.0962 0.0036  -0.0069 0.0252  47  GLY   A O   
1156 N N   A GLY   A 48  ? 0.1422 0.1492 0.1721 0.0227  -0.0273 0.0063  48  GLY   A N   
1157 N N   B GLY   A 48  ? 0.1186 0.1335 0.0932 0.0036  0.0018  0.0062  48  GLY   A N   
1158 C CA  A GLY   A 48  ? 0.1372 0.1393 0.1815 0.0130  -0.0283 -0.0055 48  GLY   A CA  
1159 C CA  B GLY   A 48  ? 0.1126 0.1223 0.0805 0.0031  0.0048  0.0041  48  GLY   A CA  
1160 C C   A GLY   A 48  ? 0.1292 0.1301 0.1589 0.0061  -0.0178 -0.0014 48  GLY   A C   
1161 C C   B GLY   A 48  ? 0.1149 0.1220 0.0924 -0.0025 0.0054  0.0138  48  GLY   A C   
1162 O O   A GLY   A 48  ? 0.1375 0.1249 0.1617 0.0039  -0.0064 -0.0029 48  GLY   A O   
1163 O O   B GLY   A 48  ? 0.1207 0.1193 0.0919 -0.0114 0.0164  0.0198  48  GLY   A O   
1170 N N   A VAL   A 49  ? 0.1240 0.1279 0.1835 -0.0011 -0.0256 -0.0067 49  VAL   A N   
1171 N N   B VAL   A 49  ? 0.1116 0.1253 0.1144 0.0010  -0.0054 0.0047  49  VAL   A N   
1172 C CA  A VAL   A 49  ? 0.1340 0.1236 0.1696 -0.0049 0.0034  -0.0020 49  VAL   A CA  
1173 C CA  B VAL   A 49  ? 0.1045 0.1283 0.1190 0.0068  -0.0008 0.0067  49  VAL   A CA  
1174 C C   A VAL   A 49  ? 0.1254 0.1164 0.1496 0.0030  0.0027  -0.0055 49  VAL   A C   
1175 C C   B VAL   A 49  ? 0.1088 0.1241 0.1115 0.0081  0.0056  -0.0030 49  VAL   A C   
1176 O O   A VAL   A 49  ? 0.1209 0.1262 0.1537 -0.0073 0.0098  -0.0042 49  VAL   A O   
1177 O O   B VAL   A 49  ? 0.1136 0.1218 0.1088 0.0109  0.0101  -0.0018 49  VAL   A O   
1178 C CB  A VAL   A 49  ? 0.1578 0.1242 0.1966 -0.0051 -0.0009 -0.0006 49  VAL   A CB  
1179 C CB  B VAL   A 49  ? 0.0913 0.1306 0.1322 0.0136  -0.0044 0.0158  49  VAL   A CB  
1180 C CG1 A VAL   A 49  ? 0.1684 0.1209 0.2048 -0.0034 0.0033  0.0067  49  VAL   A CG1 
1181 C CG1 B VAL   A 49  ? 0.0712 0.1291 0.1261 0.0242  -0.0046 0.0247  49  VAL   A CG1 
1182 C CG2 A VAL   A 49  ? 0.1668 0.1413 0.2461 -0.0248 -0.0066 -0.0029 49  VAL   A CG2 
1183 C CG2 B VAL   A 49  ? 0.0995 0.1365 0.1387 0.0103  0.0008  0.0122  49  VAL   A CG2 
1202 N N   A ALA   A 50  ? 0.1197 0.1173 0.1382 -0.0011 -0.0125 0.0110  50  ALA   A N   
1203 N N   B ALA   A 50  ? 0.1113 0.1250 0.1088 0.0076  0.0069  -0.0055 50  ALA   A N   
1204 C CA  A ALA   A 50  ? 0.1226 0.1165 0.1447 -0.0077 -0.0038 0.0150  50  ALA   A CA  
1205 C CA  B ALA   A 50  ? 0.1130 0.1224 0.1107 0.0014  0.0015  -0.0046 50  ALA   A CA  
1206 C C   A ALA   A 50  ? 0.1193 0.1229 0.1386 -0.0080 -0.0067 0.0046  50  ALA   A C   
1207 C C   B ALA   A 50  ? 0.1147 0.1220 0.1104 0.0027  -0.0029 -0.0058 50  ALA   A C   
1208 O O   A ALA   A 50  ? 0.1205 0.1255 0.1503 -0.0023 -0.0028 0.0066  50  ALA   A O   
1209 O O   B ALA   A 50  ? 0.1134 0.1186 0.1070 0.0061  0.0024  -0.0042 50  ALA   A O   
1210 C CB  A ALA   A 50  ? 0.1192 0.1192 0.1476 -0.0063 0.0014  -0.0003 50  ALA   A CB  
1211 C CB  B ALA   A 50  ? 0.1153 0.1214 0.1115 0.0012  0.0080  -0.0101 50  ALA   A CB  
1222 N N   A GLY   A 51  ? 0.1210 0.1162 0.1663 0.0065  -0.0129 0.0060  51  GLY   A N   
1223 N N   B GLY   A 51  ? 0.1196 0.1237 0.1234 0.0067  -0.0092 -0.0073 51  GLY   A N   
1224 C CA  A GLY   A 51  ? 0.1339 0.1101 0.1781 0.0101  -0.0145 0.0037  51  GLY   A CA  
1225 C CA  B GLY   A 51  ? 0.1246 0.1252 0.1327 0.0071  -0.0101 -0.0105 51  GLY   A CA  
1226 C C   A GLY   A 51  ? 0.1177 0.1192 0.1723 0.0077  -0.0013 -0.0071 51  GLY   A C   
1227 C C   B GLY   A 51  ? 0.1208 0.1284 0.1413 0.0056  -0.0078 -0.0133 51  GLY   A C   
1228 O O   A GLY   A 51  ? 0.1223 0.1287 0.1842 0.0001  -0.0027 -0.0111 51  GLY   A O   
1229 O O   B GLY   A 51  ? 0.1222 0.1298 0.1357 0.0054  -0.0160 -0.0137 51  GLY   A O   
1236 N N   . ALA   A 52  ? 0.1202 0.1320 0.1534 0.0026  -0.0051 -0.0166 52  ALA   A N   
1237 C CA  . ALA   A 52  ? 0.1225 0.1407 0.1648 -0.0006 0.0034  -0.0148 52  ALA   A CA  
1238 C C   . ALA   A 52  ? 0.1226 0.1378 0.1473 -0.0062 0.0109  -0.0095 52  ALA   A C   
1239 O O   . ALA   A 52  ? 0.1318 0.1437 0.1679 -0.0025 0.0125  -0.0136 52  ALA   A O   
1240 C CB  . ALA   A 52  ? 0.1273 0.1725 0.1851 -0.0052 -0.0017 -0.0096 52  ALA   A CB  
1247 N N   A LEU   A 53  ? 0.1176 0.1346 0.1476 -0.0059 0.0064  -0.0068 53  LEU   A N   
1248 N N   B LEU   A 53  ? 0.1205 0.1377 0.1359 -0.0085 0.0039  -0.0089 53  LEU   A N   
1249 C CA  A LEU   A 53  ? 0.1283 0.1400 0.1435 -0.0043 0.0050  0.0025  53  LEU   A CA  
1250 C CA  B LEU   A 53  ? 0.1214 0.1429 0.1297 -0.0073 -0.0027 -0.0078 53  LEU   A CA  
1251 C C   A LEU   A 53  ? 0.1256 0.1399 0.1301 0.0005  0.0030  0.0002  53  LEU   A C   
1252 C C   B LEU   A 53  ? 0.1235 0.1442 0.1234 -0.0035 -0.0045 -0.0038 53  LEU   A C   
1253 O O   A LEU   A 53  ? 0.1406 0.1554 0.1459 -0.0145 0.0032  -0.0080 53  LEU   A O   
1254 O O   B LEU   A 53  ? 0.1268 0.1450 0.1232 -0.0046 -0.0099 -0.0042 53  LEU   A O   
1255 C CB  A LEU   A 53  ? 0.1446 0.1416 0.1436 -0.0074 0.0100  0.0093  53  LEU   A CB  
1256 C CB  B LEU   A 53  ? 0.1184 0.1437 0.1276 -0.0131 -0.0073 -0.0116 53  LEU   A CB  
1257 C CG  A LEU   A 53  ? 0.1565 0.1400 0.1541 -0.0126 0.0124  0.0108  53  LEU   A CG  
1258 C CG  B LEU   A 53  ? 0.1203 0.1432 0.1266 -0.0165 -0.0130 -0.0201 53  LEU   A CG  
1259 C CD1 A LEU   A 53  ? 0.1508 0.1426 0.1492 -0.0043 -0.0001 0.0110  53  LEU   A CD1 
1260 C CD1 B LEU   A 53  ? 0.1174 0.1420 0.1103 -0.0186 -0.0179 -0.0335 53  LEU   A CD1 
1261 C CD2 A LEU   A 53  ? 0.1855 0.1578 0.1830 -0.0277 0.0189  0.0171  53  LEU   A CD2 
1262 C CD2 B LEU   A 53  ? 0.1273 0.1444 0.1411 -0.0193 -0.0016 -0.0178 53  LEU   A CD2 
1285 N N   A ASN   A 54  ? 0.1238 0.1292 0.1257 -0.0033 -0.0002 0.0030  54  ASN   A N   
1286 N N   B ASN   A 54  ? 0.1261 0.1459 0.1231 -0.0002 -0.0024 -0.0034 54  ASN   A N   
1287 C CA  A ASN   A 54  ? 0.1150 0.1242 0.1437 -0.0033 -0.0046 -0.0016 54  ASN   A CA  
1288 C CA  B ASN   A 54  ? 0.1260 0.1464 0.1264 0.0007  -0.0010 -0.0044 54  ASN   A CA  
1289 C C   A ASN   A 54  ? 0.1297 0.1280 0.1501 -0.0072 -0.0015 -0.0044 54  ASN   A C   
1290 C C   B ASN   A 54  ? 0.1321 0.1440 0.1286 -0.0012 -0.0015 -0.0040 54  ASN   A C   
1291 O O   A ASN   A 54  ? 0.1260 0.1365 0.1556 -0.0043 -0.0038 -0.0118 54  ASN   A O   
1292 O O   B ASN   A 54  ? 0.1336 0.1420 0.1260 -0.0012 -0.0020 -0.0045 54  ASN   A O   
1293 C CB  A ASN   A 54  ? 0.1098 0.1227 0.1710 -0.0062 -0.0134 -0.0009 54  ASN   A CB  
1294 C CB  B ASN   A 54  ? 0.1259 0.1480 0.1275 0.0058  0.0047  -0.0037 54  ASN   A CB  
1295 C CG  A ASN   A 54  ? 0.1162 0.1195 0.1604 -0.0005 -0.0023 -0.0057 54  ASN   A CG  
1296 C CG  B ASN   A 54  ? 0.1254 0.1472 0.1155 0.0092  0.0102  -0.0085 54  ASN   A CG  
1297 O OD1 A ASN   A 54  ? 0.1144 0.1255 0.1579 -0.0036 -0.0053 0.0096  54  ASN   A OD1 
1298 O OD1 B ASN   A 54  ? 0.1260 0.1496 0.1186 0.0056  0.0071  -0.0073 54  ASN   A OD1 
1299 N ND2 A ASN   A 54  ? 0.1193 0.1224 0.1782 -0.0101 -0.0143 0.0018  54  ASN   A ND2 
1300 N ND2 B ASN   A 54  ? 0.1252 0.1456 0.1132 0.0129  0.0120  -0.0092 54  ASN   A ND2 
1313 N N   A LYS   A 55  ? 0.1182 0.1350 0.1591 0.0011  -0.0059 -0.0133 55  LYS   A N   
1314 N N   B LYS   A 55  ? 0.1324 0.1451 0.1358 -0.0004 -0.0008 -0.0091 55  LYS   A N   
1315 C CA  A LYS   A 55  ? 0.1284 0.1421 0.1721 0.0043  -0.0080 -0.0198 55  LYS   A CA  
1316 C CA  B LYS   A 55  ? 0.1375 0.1476 0.1512 -0.0011 -0.0008 -0.0156 55  LYS   A CA  
1317 C C   A LYS   A 55  ? 0.1273 0.1491 0.1722 -0.0048 0.0031  -0.0197 55  LYS   A C   
1318 C C   B LYS   A 55  ? 0.1358 0.1528 0.1588 -0.0033 0.0014  -0.0207 55  LYS   A C   
1319 O O   A LYS   A 55  ? 0.1354 0.1608 0.1822 0.0030  0.0021  -0.0318 55  LYS   A O   
1320 O O   B LYS   A 55  ? 0.1367 0.1530 0.1568 0.0023  0.0021  -0.0232 55  LYS   A O   
1321 C CB  A LYS   A 55  ? 0.1372 0.1452 0.1899 0.0143  -0.0096 -0.0244 55  LYS   A CB  
1322 C CB  B LYS   A 55  ? 0.1438 0.1477 0.1634 0.0001  -0.0022 -0.0142 55  LYS   A CB  
1323 C CG  A LYS   A 55  ? 0.1482 0.1683 0.2059 0.0232  -0.0200 -0.0312 55  LYS   A CG  
1324 C CG  B LYS   A 55  ? 0.1508 0.1528 0.1769 0.0022  -0.0044 -0.0154 55  LYS   A CG  
1325 C CD  A LYS   A 55  ? 0.1632 0.1927 0.2047 0.0273  -0.0049 -0.0275 55  LYS   A CD  
1326 C CD  B LYS   A 55  ? 0.1570 0.1577 0.1875 0.0036  0.0017  -0.0154 55  LYS   A CD  
1327 C CE  A LYS   A 55  ? 0.1824 0.2330 0.2188 0.0386  -0.0097 -0.0309 55  LYS   A CE  
1328 C CE  B LYS   A 55  ? 0.1640 0.1647 0.1982 0.0084  0.0013  -0.0164 55  LYS   A CE  
1329 N NZ  A LYS   A 55  ? 0.1842 0.2592 0.2304 0.0508  -0.0149 -0.0211 55  LYS   A NZ  
1330 N NZ  B LYS   A 55  ? 0.1668 0.1667 0.2049 0.0124  0.0015  -0.0146 55  LYS   A NZ  
1357 N N   . ALA   A 56  ? 0.1369 0.1599 0.1629 -0.0088 0.0031  -0.0268 56  ALA   A N   
1358 C CA  . ALA   A 56  ? 0.1474 0.1750 0.1640 -0.0087 0.0104  -0.0178 56  ALA   A CA  
1359 C C   . ALA   A 56  ? 0.1558 0.1847 0.1462 -0.0088 0.0187  -0.0292 56  ALA   A C   
1360 O O   . ALA   A 56  ? 0.1600 0.2171 0.1605 -0.0009 0.0162  -0.0248 56  ALA   A O   
1361 C CB  . ALA   A 56  ? 0.1544 0.1922 0.1723 -0.0166 0.0088  -0.0101 56  ALA   A CB  
1368 N N   . THR   A 57  ? 0.1402 0.1649 0.1407 -0.0059 0.0126  -0.0169 57  THR   A N   
1369 C CA  . THR   A 57  ? 0.1445 0.1605 0.1412 -0.0064 0.0001  -0.0151 57  THR   A CA  
1370 C C   . THR   A 57  ? 0.1431 0.1697 0.1487 -0.0033 -0.0022 -0.0229 57  THR   A C   
1371 O O   . THR   A 57  ? 0.1365 0.1746 0.1742 -0.0124 -0.0081 -0.0334 57  THR   A O   
1372 C CB  . THR   A 57  ? 0.1445 0.1560 0.1450 -0.0027 0.0029  -0.0067 57  THR   A CB  
1373 O OG1 . THR   A 57  ? 0.1329 0.1567 0.1440 -0.0070 0.0017  -0.0114 57  THR   A OG1 
1374 C CG2 . THR   A 57  ? 0.1520 0.1597 0.1277 -0.0033 -0.0072 0.0017  57  THR   A CG2 
1382 N N   . ASN   A 58  ? 0.1413 0.1683 0.1748 -0.0070 0.0072  -0.0363 58  ASN   A N   
1383 C CA  . ASN   A 58  ? 0.1658 0.1557 0.1941 -0.0104 0.0147  -0.0448 58  ASN   A CA  
1384 C C   . ASN   A 58  ? 0.1444 0.1455 0.1841 0.0016  -0.0065 -0.0266 58  ASN   A C   
1385 O O   . ASN   A 58  ? 0.1454 0.1588 0.1906 -0.0144 -0.0023 -0.0303 58  ASN   A O   
1386 C CB  . ASN   A 58  ? 0.2123 0.1761 0.2296 -0.0221 0.0341  -0.0517 58  ASN   A CB  
1387 C CG  . ASN   A 58  ? 0.2485 0.2006 0.2927 -0.0219 0.0361  -0.0364 58  ASN   A CG  
1388 O OD1 . ASN   A 58  ? 0.2763 0.1985 0.3327 0.0145  0.0626  -0.0389 58  ASN   A OD1 
1389 N ND2 . ASN   A 58  ? 0.2566 0.2158 0.3179 -0.0256 0.0281  -0.0341 58  ASN   A ND2 
1396 N N   . ASN   A 59  ? 0.1217 0.1416 0.1670 -0.0076 -0.0084 -0.0177 59  ASN   A N   
1397 C CA  . ASN   A 59  ? 0.1237 0.1292 0.1754 0.0002  -0.0081 -0.0119 59  ASN   A CA  
1398 C C   . ASN   A 59  ? 0.1294 0.1288 0.1611 -0.0011 -0.0049 -0.0042 59  ASN   A C   
1399 O O   . ASN   A 59  ? 0.1309 0.1340 0.1569 -0.0093 -0.0005 -0.0002 59  ASN   A O   
1400 C CB  . ASN   A 59  ? 0.1294 0.1251 0.1830 0.0054  -0.0131 -0.0155 59  ASN   A CB  
1401 C CG  . ASN   A 59  ? 0.1374 0.1334 0.1804 -0.0005 -0.0198 -0.0009 59  ASN   A CG  
1402 O OD1 . ASN   A 59  ? 0.1494 0.1394 0.1628 -0.0082 -0.0271 0.0055  59  ASN   A OD1 
1403 N ND2 . ASN   A 59  ? 0.1465 0.1375 0.1922 -0.0102 -0.0169 0.0021  59  ASN   A ND2 
1410 N N   . ALA   A 60  ? 0.1229 0.1334 0.1590 -0.0012 -0.0046 -0.0019 60  ALA   A N   
1411 C CA  . ALA   A 60  ? 0.1255 0.1366 0.1715 -0.0078 -0.0037 -0.0006 60  ALA   A CA  
1412 C C   . ALA   A 60  ? 0.1246 0.1285 0.1732 -0.0029 -0.0055 -0.0060 60  ALA   A C   
1413 O O   . ALA   A 60  ? 0.1196 0.1366 0.1858 -0.0018 -0.0079 -0.0057 60  ALA   A O   
1414 C CB  . ALA   A 60  ? 0.1382 0.1523 0.1699 -0.0040 -0.0135 -0.0169 60  ALA   A CB  
1420 N N   . MET   A 61  ? 0.1244 0.1274 0.1498 -0.0059 0.0015  -0.0120 61  MET   A N   
1421 C CA  . MET   A 61  ? 0.1214 0.1278 0.1514 -0.0097 -0.0010 0.0002  61  MET   A CA  
1422 C C   . MET   A 61  ? 0.1191 0.1221 0.1543 -0.0081 -0.0069 -0.0049 61  MET   A C   
1423 O O   . MET   A 61  ? 0.1223 0.1233 0.1558 -0.0054 0.0063  0.0024  61  MET   A O   
1424 C CB  . MET   A 61  ? 0.1315 0.1249 0.1353 -0.0046 -0.0051 -0.0039 61  MET   A CB  
1425 C CG  . MET   A 61  ? 0.1283 0.1329 0.1645 -0.0028 -0.0026 -0.0026 61  MET   A CG  
1426 S SD  . MET   A 61  ? 0.1309 0.1339 0.2047 -0.0111 -0.0007 -0.0166 61  MET   A SD  
1427 C CE  . MET   A 61  ? 0.1487 0.1500 0.2138 -0.0094 0.0128  -0.0123 61  MET   A CE  
1437 N N   . GLN   A 62  ? 0.1240 0.1173 0.1586 -0.0076 -0.0038 -0.0024 62  GLN   A N   
1438 C CA  . GLN   A 62  ? 0.1212 0.1164 0.1726 -0.0043 -0.0017 0.0070  62  GLN   A CA  
1439 C C   . GLN   A 62  ? 0.1232 0.1122 0.1741 0.0001  0.0088  -0.0019 62  GLN   A C   
1440 O O   . GLN   A 62  ? 0.1254 0.1250 0.1577 -0.0016 0.0042  0.0021  62  GLN   A O   
1441 C CB  . GLN   A 62  ? 0.1209 0.1130 0.1761 -0.0049 0.0026  0.0056  62  GLN   A CB  
1442 C CG  . GLN   A 62  ? 0.1251 0.1172 0.1718 -0.0044 0.0003  0.0155  62  GLN   A CG  
1443 C CD  . GLN   A 62  ? 0.1349 0.1200 0.1614 -0.0043 0.0116  0.0118  62  GLN   A CD  
1444 O OE1 . GLN   A 62  ? 0.1366 0.1343 0.1614 -0.0031 0.0046  0.0017  62  GLN   A OE1 
1445 N NE2 . GLN   A 62  ? 0.1383 0.1233 0.1712 0.0008  0.0005  -0.0058 62  GLN   A NE2 
1454 N N   . VAL   A 63  ? 0.1186 0.1207 0.1897 -0.0068 0.0069  -0.0150 63  VAL   A N   
1455 C CA  . VAL   A 63  ? 0.1185 0.1338 0.2052 -0.0122 0.0004  -0.0199 63  VAL   A CA  
1456 C C   . VAL   A 63  ? 0.1069 0.1286 0.1890 -0.0106 -0.0136 -0.0182 63  VAL   A C   
1457 O O   . VAL   A 63  ? 0.1115 0.1331 0.2020 -0.0132 -0.0052 -0.0071 63  VAL   A O   
1458 C CB  . VAL   A 63  ? 0.1349 0.1508 0.2257 -0.0108 -0.0026 -0.0361 63  VAL   A CB  
1459 C CG1 . VAL   A 63  ? 0.1565 0.1730 0.2481 -0.0054 -0.0162 -0.0609 63  VAL   A CG1 
1460 C CG2 . VAL   A 63  ? 0.1499 0.1454 0.2429 -0.0141 0.0225  -0.0393 63  VAL   A CG2 
1470 N N   . GLU   A 64  ? 0.1186 0.1348 0.1756 -0.0058 -0.0037 -0.0063 64  GLU   A N   
1471 C CA  . GLU   A 64  ? 0.1184 0.1269 0.1844 -0.0054 -0.0059 -0.0020 64  GLU   A CA  
1472 C C   . GLU   A 64  ? 0.1149 0.1283 0.1750 -0.0058 0.0033  0.0016  64  GLU   A C   
1473 O O   . GLU   A 64  ? 0.1238 0.1356 0.1761 -0.0034 -0.0013 0.0041  64  GLU   A O   
1474 C CB  . GLU   A 64  ? 0.1285 0.1433 0.1890 -0.0078 -0.0026 -0.0064 64  GLU   A CB  
1475 C CG  . GLU   A 64  ? 0.1401 0.1471 0.1872 -0.0060 0.0019  0.0006  64  GLU   A CG  
1476 C CD  . GLU   A 64  ? 0.1488 0.1560 0.1979 -0.0127 0.0077  -0.0052 64  GLU   A CD  
1477 O OE1 . GLU   A 64  ? 0.1441 0.1691 0.2220 -0.0166 0.0134  0.0021  64  GLU   A OE1 
1478 O OE2 . GLU   A 64  ? 0.1634 0.1597 0.1950 -0.0214 0.0004  0.0042  64  GLU   A OE2 
1485 N N   . SER   A 65  ? 0.1135 0.1307 0.1658 0.0035  0.0008  0.0030  65  SER   A N   
1486 C CA  . SER   A 65  ? 0.1210 0.1249 0.1619 -0.0013 -0.0041 -0.0028 65  SER   A CA  
1487 C C   . SER   A 65  ? 0.1171 0.1316 0.1744 -0.0046 -0.0026 0.0035  65  SER   A C   
1488 O O   . SER   A 65  ? 0.1257 0.1348 0.1779 -0.0017 0.0082  -0.0029 65  SER   A O   
1489 C CB  . SER   A 65  ? 0.1191 0.1261 0.1652 -0.0069 0.0042  0.0072  65  SER   A CB  
1490 O OG  . SER   A 65  ? 0.1173 0.1356 0.1700 -0.0061 -0.0045 0.0123  65  SER   A OG  
1496 N N   . ASP   A 66  ? 0.1189 0.1264 0.1779 -0.0032 0.0094  0.0123  66  ASP   A N   
1497 C CA  . ASP   A 66  ? 0.1343 0.1356 0.1950 -0.0007 0.0110  0.0167  66  ASP   A CA  
1498 C C   . ASP   A 66  ? 0.1294 0.1324 0.1919 -0.0039 0.0123  0.0204  66  ASP   A C   
1499 O O   . ASP   A 66  ? 0.1377 0.1478 0.2103 -0.0039 0.0293  0.0204  66  ASP   A O   
1500 C CB  . ASP   A 66  ? 0.1451 0.1443 0.2188 0.0082  0.0163  0.0333  66  ASP   A CB  
1501 C CG  . ASP   A 66  ? 0.1660 0.1592 0.2471 0.0019  0.0089  0.0524  66  ASP   A CG  
1502 O OD1 . ASP   A 66  ? 0.1622 0.1910 0.2244 -0.0027 -0.0000 0.0560  66  ASP   A OD1 
1503 O OD2 . ASP   A 66  ? 0.1854 0.1739 0.3396 0.0223  -0.0091 0.0282  66  ASP   A OD2 
1508 N N   . ASP   A 67  ? 0.1197 0.1345 0.2084 -0.0038 0.0060  0.0174  67  ASP   A N   
1509 C CA  . ASP   A 67  ? 0.1230 0.1508 0.2142 -0.0038 0.0041  0.0260  67  ASP   A CA  
1510 C C   . ASP   A 67  ? 0.1265 0.1501 0.2145 -0.0000 0.0102  0.0299  67  ASP   A C   
1511 O O   . ASP   A 67  ? 0.1202 0.1605 0.2326 0.0000  0.0284  0.0363  67  ASP   A O   
1512 C CB  . ASP   A 67  ? 0.1369 0.1634 0.2398 -0.0073 -0.0173 0.0331  67  ASP   A CB  
1513 C CG  . ASP   A 67  ? 0.1371 0.1784 0.2691 -0.0041 -0.0295 0.0396  67  ASP   A CG  
1514 O OD1 . ASP   A 67  ? 0.1354 0.1952 0.3533 -0.0132 -0.0407 0.0531  67  ASP   A OD1 
1515 O OD2 . ASP   A 67  ? 0.1337 0.1805 0.2638 0.0052  -0.0175 0.0331  67  ASP   A OD2 
1520 N N   . TYR   A 68  ? 0.1298 0.1365 0.1968 0.0010  0.0134  0.0304  68  TYR   A N   
1521 C CA  . TYR   A 68  ? 0.1364 0.1386 0.1968 0.0010  0.0290  0.0239  68  TYR   A CA  
1522 C C   . TYR   A 68  ? 0.1266 0.1409 0.2069 0.0021  0.0302  0.0204  68  TYR   A C   
1523 O O   . TYR   A 68  ? 0.1346 0.1441 0.2077 0.0073  0.0279  0.0234  68  TYR   A O   
1524 C CB  . TYR   A 68  ? 0.1377 0.1358 0.2238 0.0103  0.0400  0.0279  68  TYR   A CB  
1525 C CG  . TYR   A 68  ? 0.1448 0.1556 0.2437 0.0066  0.0539  0.0345  68  TYR   A CG  
1526 C CD1 . TYR   A 68  ? 0.1568 0.1650 0.2734 -0.0202 0.0495  -0.0033 68  TYR   A CD1 
1527 C CD2 . TYR   A 68  ? 0.1673 0.1577 0.2806 0.0153  0.0563  0.0496  68  TYR   A CD2 
1528 C CE1 . TYR   A 68  ? 0.1672 0.1755 0.3047 -0.0191 0.0643  -0.0114 68  TYR   A CE1 
1529 C CE2 . TYR   A 68  ? 0.1685 0.1628 0.2946 0.0038  0.0652  0.0273  68  TYR   A CE2 
1530 C CZ  . TYR   A 68  ? 0.1676 0.1659 0.3198 -0.0228 0.0576  -0.0079 68  TYR   A CZ  
1531 O OH  . TYR   A 68  ? 0.1965 0.1647 0.3356 -0.0158 0.0301  -0.0400 68  TYR   A OH  
1541 N N   . ILE   A 69  ? 0.1193 0.1317 0.1903 -0.0006 0.0265  0.0145  69  ILE   A N   
1542 C CA  . ILE   A 69  ? 0.1288 0.1385 0.1878 -0.0001 0.0209  0.0052  69  ILE   A CA  
1543 C C   . ILE   A 69  ? 0.1319 0.1352 0.1793 0.0027  0.0232  0.0216  69  ILE   A C   
1544 O O   . ILE   A 69  ? 0.1380 0.1486 0.1744 -0.0018 0.0245  0.0249  69  ILE   A O   
1545 C CB  . ILE   A 69  ? 0.1364 0.1615 0.1925 0.0058  0.0134  -0.0068 69  ILE   A CB  
1546 C CG1 . ILE   A 69  ? 0.1388 0.1710 0.2052 0.0046  0.0165  -0.0215 69  ILE   A CG1 
1547 C CG2 . ILE   A 69  ? 0.1605 0.1810 0.2100 0.0171  0.0091  -0.0119 69  ILE   A CG2 
1548 C CD1 . ILE   A 69  ? 0.1357 0.1830 0.2217 -0.0030 0.0126  -0.0288 69  ILE   A CD1 
1560 N N   . ALA   A 70  ? 0.1457 0.1340 0.1976 -0.0048 0.0217  0.0180  70  ALA   A N   
1561 C CA  . ALA   A 70  ? 0.1461 0.1472 0.2125 -0.0175 0.0281  0.0275  70  ALA   A CA  
1562 C C   . ALA   A 70  ? 0.1435 0.1644 0.1976 -0.0161 0.0307  0.0256  70  ALA   A C   
1563 O O   . ALA   A 70  ? 0.1621 0.1979 0.2254 0.0054  0.0470  0.0405  70  ALA   A O   
1564 C CB  . ALA   A 70  ? 0.1473 0.1441 0.2403 -0.0205 0.0191  0.0211  70  ALA   A CB  
1570 N N   . THR   A 71  ? 0.1383 0.1599 0.1924 -0.0052 0.0251  0.0231  71  THR   A N   
1571 C CA  . THR   A 71  ? 0.1457 0.1784 0.2325 0.0049  0.0227  0.0255  71  THR   A CA  
1572 C C   . THR   A 71  ? 0.1323 0.1736 0.2447 0.0091  0.0337  0.0270  71  THR   A C   
1573 O O   . THR   A 71  ? 0.1402 0.2019 0.2871 0.0114  0.0380  -0.0057 71  THR   A O   
1574 C CB  . THR   A 71  ? 0.1679 0.2054 0.2571 0.0167  -0.0103 0.0285  71  THR   A CB  
1575 O OG1 . THR   A 71  ? 0.1893 0.2213 0.2753 0.0071  -0.0349 0.0242  71  THR   A OG1 
1576 C CG2 . THR   A 71  ? 0.1769 0.2205 0.2816 0.0229  -0.0166 0.0333  71  THR   A CG2 
1584 N N   . ASN   A 72  ? 0.1351 0.1568 0.2240 0.0128  0.0285  0.0222  72  ASN   A N   
1585 C CA  . ASN   A 72  ? 0.1390 0.1603 0.2337 0.0188  0.0393  0.0264  72  ASN   A CA  
1586 C C   . ASN   A 72  ? 0.1574 0.1577 0.2252 0.0129  0.0459  0.0145  72  ASN   A C   
1587 O O   . ASN   A 72  ? 0.1746 0.1533 0.2575 0.0182  0.0465  0.0036  72  ASN   A O   
1588 C CB  . ASN   A 72  ? 0.1607 0.1628 0.2347 0.0156  0.0321  0.0287  72  ASN   A CB  
1589 C CG  . ASN   A 72  ? 0.1852 0.1762 0.2311 0.0281  0.0302  0.0300  72  ASN   A CG  
1590 O OD1 . ASN   A 72  ? 0.2055 0.2071 0.2466 0.0279  0.0379  0.0333  72  ASN   A OD1 
1591 N ND2 . ASN   A 72  ? 0.2033 0.1798 0.2354 0.0461  0.0134  0.0237  72  ASN   A ND2 
1598 N N   . GLY   A 73  ? 0.1603 0.1565 0.2023 0.0086  0.0441  0.0128  73  GLY   A N   
1599 C CA  . GLY   A 73  ? 0.1662 0.1535 0.1879 -0.0053 0.0466  0.0081  73  GLY   A CA  
1600 C C   . GLY   A 73  ? 0.1657 0.1456 0.1734 0.0018  0.0550  0.0171  73  GLY   A C   
1601 O O   . GLY   A 73  ? 0.1609 0.1474 0.1948 0.0076  0.0395  0.0239  73  GLY   A O   
1605 N N   . PRO   A 74  ? 0.1719 0.1425 0.1784 -0.0153 0.0449  0.0141  74  PRO   A N   
1606 C CA  . PRO   A 74  ? 0.1665 0.1396 0.1955 -0.0048 0.0398  0.0193  74  PRO   A CA  
1607 C C   . PRO   A 74  ? 0.1574 0.1314 0.1939 0.0018  0.0266  0.0089  74  PRO   A C   
1608 O O   . PRO   A 74  ? 0.1654 0.1360 0.2200 0.0025  0.0383  -0.0050 74  PRO   A O   
1609 C CB  . PRO   A 74  ? 0.1835 0.1667 0.2227 -0.0029 0.0430  0.0218  74  PRO   A CB  
1610 C CG  . PRO   A 74  ? 0.2089 0.1965 0.2602 -0.0207 0.0294  0.0065  74  PRO   A CG  
1611 C CD  . PRO   A 74  ? 0.1928 0.1758 0.2031 -0.0230 0.0281  -0.0004 74  PRO   A CD  
1619 N N   . LEU   A 75  ? 0.1534 0.1213 0.1762 0.0009  0.0226  0.0045  75  LEU   A N   
1620 C CA  . LEU   A 75  ? 0.1539 0.1167 0.1592 0.0030  0.0165  0.0072  75  LEU   A CA  
1621 C C   . LEU   A 75  ? 0.1619 0.1308 0.1711 0.0024  0.0140  0.0108  75  LEU   A C   
1622 O O   . LEU   A 75  ? 0.1984 0.1492 0.1701 0.0138  0.0121  0.0088  75  LEU   A O   
1623 C CB  . LEU   A 75  ? 0.1624 0.1270 0.1649 -0.0068 0.0097  0.0160  75  LEU   A CB  
1624 C CG  . LEU   A 75  ? 0.1834 0.1575 0.1774 -0.0397 0.0051  0.0162  75  LEU   A CG  
1625 C CD1 . LEU   A 75  ? 0.2012 0.2061 0.1806 -0.0375 0.0026  0.0033  75  LEU   A CD1 
1626 C CD2 . LEU   A 75  ? 0.2152 0.2024 0.2327 -0.0173 0.0130  0.0294  75  LEU   A CD2 
1638 N N   . LYS   A 76  ? 0.1665 0.1332 0.1746 -0.0055 0.0095  0.0009  76  LYS   A N   
1639 C CA  . LYS   A 76  ? 0.1639 0.1542 0.1728 -0.0082 0.0177  -0.0065 76  LYS   A CA  
1640 C C   . LYS   A 76  ? 0.1546 0.1376 0.1572 0.0015  0.0187  -0.0003 76  LYS   A C   
1641 O O   . LYS   A 76  ? 0.1577 0.1312 0.1507 -0.0009 0.0203  0.0067  76  LYS   A O   
1642 C CB  . LYS   A 76  ? 0.1658 0.1797 0.2120 0.0006  0.0158  -0.0310 76  LYS   A CB  
1643 C CG  . LYS   A 76  ? 0.1761 0.1711 0.2661 0.0118  0.0129  -0.0257 76  LYS   A CG  
1644 C CD  . LYS   A 76  ? 0.1829 0.1689 0.3122 0.0127  0.0031  -0.0329 76  LYS   A CD  
1645 C CE  . LYS   A 76  ? 0.1961 0.1906 0.3573 0.0041  0.0069  -0.0476 76  LYS   A CE  
1646 N NZ  . LYS   A 76  ? 0.1980 0.1889 0.3979 -0.0101 0.0021  -0.0530 76  LYS   A NZ  
1660 N N   . VAL   A 77  ? 0.1660 0.1434 0.1486 0.0019  0.0212  0.0130  77  VAL   A N   
1661 C CA  . VAL   A 77  ? 0.1621 0.1461 0.1553 0.0069  0.0199  0.0169  77  VAL   A CA  
1662 C C   . VAL   A 77  ? 0.1604 0.1438 0.1444 0.0066  0.0202  -0.0002 77  VAL   A C   
1663 O O   . VAL   A 77  ? 0.1681 0.1449 0.1477 0.0092  0.0322  -0.0072 77  VAL   A O   
1664 C CB  . VAL   A 77  ? 0.1823 0.1648 0.1527 0.0023  0.0104  0.0250  77  VAL   A CB  
1665 C CG1 . VAL   A 77  ? 0.1780 0.1730 0.1829 0.0107  -0.0012 0.0135  77  VAL   A CG1 
1666 C CG2 . VAL   A 77  ? 0.2107 0.1806 0.1747 -0.0005 -0.0106 0.0301  77  VAL   A CG2 
1676 N N   . GLY   A 78  ? 0.1561 0.1376 0.1416 0.0053  0.0202  0.0048  78  GLY   A N   
1677 C CA  . GLY   A 78  ? 0.1506 0.1338 0.1642 -0.0004 0.0285  0.0145  78  GLY   A CA  
1678 C C   . GLY   A 78  ? 0.1431 0.1263 0.1555 0.0046  0.0232  0.0131  78  GLY   A C   
1679 O O   . GLY   A 78  ? 0.1402 0.1357 0.1698 0.0018  0.0195  0.0263  78  GLY   A O   
1683 N N   . GLY   A 79  ? 0.1487 0.1230 0.1475 0.0018  0.0139  0.0120  79  GLY   A N   
1684 C CA  . GLY   A 79  ? 0.1409 0.1283 0.1536 0.0025  0.0247  0.0153  79  GLY   A CA  
1685 C C   . GLY   A 79  ? 0.1285 0.1239 0.1589 0.0050  0.0128  0.0064  79  GLY   A C   
1686 O O   . GLY   A 79  ? 0.1329 0.1291 0.1677 0.0189  0.0127  0.0068  79  GLY   A O   
1690 N N   . SER   A 80  ? 0.1218 0.1389 0.1771 0.0033  0.0201  0.0024  80  SER   A N   
1691 C CA  . SER   A 80  ? 0.1237 0.1336 0.1697 -0.0008 0.0081  0.0032  80  SER   A CA  
1692 C C   . SER   A 80  ? 0.1242 0.1346 0.1658 -0.0031 0.0077  0.0119  80  SER   A C   
1693 O O   . SER   A 80  ? 0.1199 0.1575 0.1874 0.0093  0.0084  0.0011  80  SER   A O   
1694 C CB  . SER   A 80  ? 0.1412 0.1310 0.1925 -0.0088 0.0075  0.0108  80  SER   A CB  
1695 O OG  . SER   A 80  ? 0.1646 0.1316 0.2222 0.0019  -0.0065 0.0212  80  SER   A OG  
1701 N N   . CYS   A 81  ? 0.1195 0.1284 0.1645 0.0006  0.0012  0.0115  81  CYS   A N   
1702 C CA  . CYS   A 81  ? 0.1192 0.1395 0.1568 -0.0059 -0.0027 0.0209  81  CYS   A CA  
1703 C C   . CYS   A 81  ? 0.1172 0.1350 0.1752 -0.0034 -0.0023 0.0248  81  CYS   A C   
1704 O O   . CYS   A 81  ? 0.1210 0.1609 0.1799 0.0007  0.0036  0.0376  81  CYS   A O   
1705 C CB  . CYS   A 81  ? 0.1218 0.1454 0.1768 -0.0121 -0.0023 0.0227  81  CYS   A CB  
1706 S SG  . CYS   A 81  ? 0.1409 0.1311 0.1918 -0.0126 0.0016  0.0180  81  CYS   A SG  
1712 N N   . VAL   A 82  ? 0.1160 0.1431 0.1698 -0.0020 -0.0047 0.0218  82  VAL   A N   
1713 C CA  . VAL   A 82  ? 0.1338 0.1468 0.1726 0.0029  -0.0001 0.0303  82  VAL   A CA  
1714 C C   . VAL   A 82  ? 0.1345 0.1506 0.1739 -0.0003 -0.0061 0.0268  82  VAL   A C   
1715 O O   . VAL   A 82  ? 0.1282 0.1614 0.1940 -0.0011 -0.0034 -0.0023 82  VAL   A O   
1716 C CB  . VAL   A 82  ? 0.1664 0.1598 0.1813 0.0021  0.0006  0.0350  82  VAL   A CB  
1717 C CG1 . VAL   A 82  ? 0.1882 0.1748 0.1984 0.0045  0.0045  0.0282  82  VAL   A CG1 
1718 C CG2 . VAL   A 82  ? 0.1721 0.1629 0.2067 -0.0008 -0.0019 0.0395  82  VAL   A CG2 
1728 N N   . LEU   A 83  ? 0.1273 0.1483 0.1611 -0.0108 -0.0073 0.0109  83  LEU   A N   
1729 C CA  . LEU   A 83  ? 0.1270 0.1498 0.1621 -0.0086 -0.0095 0.0057  83  LEU   A CA  
1730 C C   . LEU   A 83  ? 0.1346 0.1466 0.1600 -0.0092 -0.0106 0.0171  83  LEU   A C   
1731 O O   . LEU   A 83  ? 0.1459 0.1495 0.1670 -0.0114 -0.0042 0.0210  83  LEU   A O   
1732 C CB  . LEU   A 83  ? 0.1401 0.1564 0.1638 -0.0112 -0.0114 0.0192  83  LEU   A CB  
1733 C CG  . LEU   A 83  ? 0.1506 0.1642 0.1663 -0.0093 0.0010  0.0081  83  LEU   A CG  
1734 C CD1 . LEU   A 83  ? 0.1555 0.1692 0.1776 -0.0213 -0.0001 0.0260  83  LEU   A CD1 
1735 C CD2 . LEU   A 83  ? 0.1494 0.1820 0.1784 -0.0160 0.0133  0.0143  83  LEU   A CD2 
1747 N N   . SER   A 84  ? 0.1494 0.1541 0.1529 -0.0137 -0.0055 0.0197  84  SER   A N   
1748 C CA  . SER   A 84  ? 0.1588 0.1604 0.1474 -0.0099 -0.0007 0.0121  84  SER   A CA  
1749 C C   . SER   A 84  ? 0.1639 0.1519 0.1432 -0.0151 -0.0026 0.0107  84  SER   A C   
1750 O O   . SER   A 84  ? 0.1601 0.1686 0.1310 -0.0115 -0.0109 0.0111  84  SER   A O   
1751 C CB  . SER   A 84  ? 0.1641 0.1860 0.1549 -0.0128 -0.0046 -0.0005 84  SER   A CB  
1752 O OG  . SER   A 84  ? 0.1719 0.2070 0.1642 -0.0100 -0.0165 -0.0079 84  SER   A OG  
1758 N N   . GLY   A 85  ? 0.1786 0.1691 0.1436 -0.0145 0.0165  0.0065  85  GLY   A N   
1759 C CA  . GLY   A 85  ? 0.1819 0.1792 0.1652 -0.0250 0.0212  -0.0005 85  GLY   A CA  
1760 C C   . GLY   A 85  ? 0.1726 0.1845 0.1416 -0.0207 0.0116  0.0002  85  GLY   A C   
1761 O O   . GLY   A 85  ? 0.1776 0.1974 0.1505 -0.0263 0.0221  -0.0120 85  GLY   A O   
1765 N N   . HIS   A 86  ? 0.1726 0.1778 0.1372 -0.0180 -0.0044 0.0037  86  HIS   A N   
1766 C CA  . HIS   A 86  ? 0.1884 0.1849 0.1256 -0.0226 -0.0035 0.0067  86  HIS   A CA  
1767 C C   . HIS   A 86  ? 0.2148 0.1956 0.1345 -0.0238 -0.0045 0.0025  86  HIS   A C   
1768 O O   . HIS   A 86  ? 0.2262 0.2192 0.1345 -0.0150 0.0046  0.0031  86  HIS   A O   
1769 C CB  . HIS   A 86  ? 0.1851 0.1791 0.1378 -0.0176 0.0078  0.0086  86  HIS   A CB  
1770 C CG  . HIS   A 86  ? 0.1821 0.1763 0.1530 -0.0137 0.0028  0.0120  86  HIS   A CG  
1771 N ND1 . HIS   A 86  ? 0.1870 0.1808 0.1836 -0.0229 -0.0013 0.0130  86  HIS   A ND1 
1772 C CD2 . HIS   A 86  ? 0.1810 0.1758 0.1531 -0.0069 0.0062  0.0137  86  HIS   A CD2 
1773 C CE1 . HIS   A 86  ? 0.1804 0.1792 0.1750 -0.0224 0.0175  0.0193  86  HIS   A CE1 
1774 N NE2 . HIS   A 86  ? 0.1775 0.1743 0.1603 -0.0023 0.0160  0.0280  86  HIS   A NE2 
1782 N N   . ASN   A 87  ? 0.2273 0.2005 0.1514 -0.0232 0.0225  -0.0126 87  ASN   A N   
1783 C CA  . ASN   A 87  ? 0.2486 0.2157 0.1556 -0.0195 0.0472  -0.0156 87  ASN   A CA  
1784 C C   . ASN   A 87  ? 0.2504 0.2333 0.1775 -0.0232 0.0681  -0.0033 87  ASN   A C   
1785 O O   . ASN   A 87  ? 0.2754 0.2540 0.2181 -0.0356 0.0951  -0.0038 87  ASN   A O   
1786 C CB  . ASN   A 87  ? 0.2676 0.2229 0.1651 -0.0095 0.0474  -0.0104 87  ASN   A CB  
1787 C CG  . ASN   A 87  ? 0.2850 0.2347 0.1692 0.0052  0.0593  -0.0093 87  ASN   A CG  
1788 O OD1 . ASN   A 87  ? 0.3047 0.2296 0.1811 0.0277  0.0573  0.0016  87  ASN   A OD1 
1789 N ND2 . ASN   A 87  ? 0.2874 0.2624 0.1866 0.0029  0.0621  -0.0069 87  ASN   A ND2 
1796 N N   . LEU   A 88  ? 0.2239 0.2264 0.1705 -0.0246 0.0403  0.0069  88  LEU   A N   
1797 C CA  . LEU   A 88  ? 0.2037 0.2247 0.1903 -0.0283 0.0324  0.0182  88  LEU   A CA  
1798 C C   . LEU   A 88  ? 0.1946 0.2214 0.1897 -0.0321 0.0322  0.0269  88  LEU   A C   
1799 O O   . LEU   A 88  ? 0.1979 0.2277 0.2186 -0.0328 0.0353  0.0486  88  LEU   A O   
1800 C CB  . LEU   A 88  ? 0.2067 0.2334 0.2059 -0.0357 -0.0021 0.0367  88  LEU   A CB  
1801 C CG  . LEU   A 88  ? 0.2279 0.2456 0.2389 -0.0344 -0.0155 0.0325  88  LEU   A CG  
1802 C CD1 . LEU   A 88  ? 0.2398 0.2540 0.2314 -0.0387 -0.0232 0.0119  88  LEU   A CD1 
1803 C CD2 . LEU   A 88  ? 0.2443 0.2558 0.2775 -0.0257 -0.0155 0.0220  88  LEU   A CD2 
1815 N N   . ALA   A 89  ? 0.1953 0.2064 0.1586 -0.0290 0.0270  0.0014  89  ALA   A N   
1816 C CA  . ALA   A 89  ? 0.2019 0.2004 0.1459 -0.0210 0.0149  0.0149  89  ALA   A CA  
1817 C C   . ALA   A 89  ? 0.2093 0.2077 0.1542 -0.0154 -0.0041 0.0135  89  ALA   A C   
1818 O O   . ALA   A 89  ? 0.2040 0.2046 0.1891 -0.0211 -0.0092 -0.0105 89  ALA   A O   
1819 C CB  . ALA   A 89  ? 0.1887 0.1985 0.1369 -0.0137 0.0091  0.0224  89  ALA   A CB  
1825 N N   . LYS   A 90  ? 0.2182 0.2256 0.1549 -0.0264 -0.0182 0.0309  90  LYS   A N   
1826 C CA  . LYS   A 90  ? 0.2295 0.2398 0.1536 -0.0242 -0.0269 0.0306  90  LYS   A CA  
1827 C C   . LYS   A 90  ? 0.2014 0.2199 0.1457 -0.0246 -0.0231 0.0104  90  LYS   A C   
1828 O O   . LYS   A 90  ? 0.2034 0.2355 0.1804 -0.0240 -0.0260 -0.0014 90  LYS   A O   
1829 C CB  . LYS   A 90  ? 0.2580 0.2766 0.1917 -0.0221 -0.0338 0.0483  90  LYS   A CB  
1830 C CG  . LYS   A 90  ? 0.2899 0.3065 0.2895 -0.0230 -0.0289 0.0453  90  LYS   A CG  
1831 C CD  . LYS   A 90  ? 0.3207 0.3307 0.3828 -0.0256 -0.0167 0.0548  90  LYS   A CD  
1832 C CE  . LYS   A 90  ? 0.3466 0.3559 0.4602 -0.0264 -0.0088 0.0554  90  LYS   A CE  
1833 N NZ  . LYS   A 90  ? 0.3664 0.3803 0.5048 -0.0261 -0.0026 0.0461  90  LYS   A NZ  
1847 N N   . HIS   A 91  ? 0.1889 0.1949 0.1142 -0.0218 -0.0264 0.0226  91  HIS   A N   
1848 C CA  . HIS   A 91  ? 0.1679 0.1741 0.1359 -0.0159 -0.0266 0.0295  91  HIS   A CA  
1849 C C   . HIS   A 91  ? 0.1528 0.1599 0.1367 -0.0147 -0.0094 0.0268  91  HIS   A C   
1850 O O   . HIS   A 91  ? 0.1570 0.1730 0.1458 -0.0151 0.0015  0.0263  91  HIS   A O   
1851 C CB  . HIS   A 91  ? 0.1885 0.2035 0.1882 0.0064  -0.0511 0.0290  91  HIS   A CB  
1852 C CG  . HIS   A 91  ? 0.2338 0.2567 0.2629 0.0148  -0.0683 0.0125  91  HIS   A CG  
1853 N ND1 . HIS   A 91  ? 0.2497 0.2867 0.3006 0.0206  -0.0773 -0.0141 91  HIS   A ND1 
1854 C CD2 . HIS   A 91  ? 0.2597 0.2798 0.2793 0.0232  -0.0824 0.0213  91  HIS   A CD2 
1855 C CE1 . HIS   A 91  ? 0.2629 0.2970 0.3134 0.0247  -0.0787 -0.0024 91  HIS   A CE1 
1856 N NE2 . HIS   A 91  ? 0.2739 0.2942 0.2996 0.0300  -0.0843 0.0107  91  HIS   A NE2 
1864 N N   . CYS   A 92  ? 0.1410 0.1529 0.1411 -0.0199 -0.0102 0.0237  92  CYS   A N   
1865 C CA  . CYS   A 92  ? 0.1396 0.1467 0.1463 -0.0094 -0.0016 0.0206  92  CYS   A CA  
1866 C C   . CYS   A 92  ? 0.1322 0.1416 0.1406 -0.0055 0.0005  0.0185  92  CYS   A C   
1867 O O   . CYS   A 92  ? 0.1304 0.1475 0.1544 -0.0157 -0.0042 0.0137  92  CYS   A O   
1868 C CB  . CYS   A 92  ? 0.1380 0.1459 0.1538 -0.0069 -0.0004 0.0129  92  CYS   A CB  
1869 S SG  . CYS   A 92  ? 0.1394 0.1377 0.1396 -0.0118 -0.0017 0.0124  92  CYS   A SG  
1875 N N   . LEU   A 93  ? 0.1306 0.1320 0.1407 -0.0091 0.0065  0.0152  93  LEU   A N   
1876 C CA  . LEU   A 93  ? 0.1244 0.1289 0.1448 -0.0005 0.0046  0.0160  93  LEU   A CA  
1877 C C   . LEU   A 93  ? 0.1198 0.1180 0.1401 -0.0014 0.0104  0.0094  93  LEU   A C   
1878 O O   . LEU   A 93  ? 0.1183 0.1316 0.1242 -0.0024 -0.0006 0.0154  93  LEU   A O   
1879 C CB  . LEU   A 93  ? 0.1285 0.1292 0.1585 -0.0058 -0.0029 0.0238  93  LEU   A CB  
1880 C CG  . LEU   A 93  ? 0.1351 0.1305 0.1546 -0.0051 0.0000  0.0208  93  LEU   A CG  
1881 C CD1 . LEU   A 93  ? 0.1424 0.1304 0.1898 -0.0015 0.0138  0.0151  93  LEU   A CD1 
1882 C CD2 . LEU   A 93  ? 0.1433 0.1321 0.1757 -0.0064 0.0006  0.0242  93  LEU   A CD2 
1894 N N   . HIS   A 94  ? 0.1164 0.1157 0.1269 -0.0008 0.0097  0.0134  94  HIS   A N   
1895 C CA  . HIS   A 94  ? 0.1175 0.1148 0.1396 -0.0023 -0.0019 0.0183  94  HIS   A CA  
1896 C C   . HIS   A 94  ? 0.1086 0.1159 0.1444 -0.0045 -0.0022 0.0097  94  HIS   A C   
1897 O O   . HIS   A 94  ? 0.1099 0.1394 0.1740 -0.0006 0.0009  -0.0056 94  HIS   A O   
1898 C CB  . HIS   A 94  ? 0.1115 0.1143 0.1504 -0.0049 -0.0015 0.0205  94  HIS   A CB  
1899 C CG  . HIS   A 94  ? 0.1196 0.1182 0.1402 -0.0066 -0.0051 0.0228  94  HIS   A CG  
1900 N ND1 . HIS   A 94  ? 0.1192 0.1174 0.1507 -0.0032 -0.0013 0.0155  94  HIS   A ND1 
1901 C CD2 . HIS   A 94  ? 0.1312 0.1281 0.1454 -0.0051 -0.0090 0.0153  94  HIS   A CD2 
1902 C CE1 . HIS   A 94  ? 0.1235 0.1210 0.1460 -0.0081 -0.0070 0.0078  94  HIS   A CE1 
1903 N NE2 . HIS   A 94  ? 0.1315 0.1249 0.1382 -0.0074 -0.0036 0.0085  94  HIS   A NE2 
1911 N N   . VAL   A 95  ? 0.1106 0.1138 0.1221 -0.0023 0.0078  0.0041  95  VAL   A N   
1912 C CA  . VAL   A 95  ? 0.1149 0.1181 0.1251 -0.0023 0.0119  0.0140  95  VAL   A CA  
1913 C C   . VAL   A 95  ? 0.1160 0.1222 0.1207 -0.0135 0.0013  0.0110  95  VAL   A C   
1914 O O   . VAL   A 95  ? 0.1201 0.1317 0.1264 0.0079  0.0050  0.0057  95  VAL   A O   
1915 C CB  . VAL   A 95  ? 0.1222 0.1171 0.1511 -0.0126 0.0075  0.0074  95  VAL   A CB  
1916 C CG1 . VAL   A 95  ? 0.1373 0.1208 0.1685 -0.0160 0.0046  -0.0023 95  VAL   A CG1 
1917 C CG2 . VAL   A 95  ? 0.1247 0.1262 0.1499 -0.0144 0.0098  0.0274  95  VAL   A CG2 
1927 N N   . VAL   A 96  ? 0.1226 0.1170 0.1185 -0.0055 0.0025  0.0111  96  VAL   A N   
1928 C CA  . VAL   A 96  ? 0.1354 0.1207 0.1445 0.0003  0.0114  0.0215  96  VAL   A CA  
1929 C C   . VAL   A 96  ? 0.1342 0.1254 0.1333 -0.0010 0.0124  0.0183  96  VAL   A C   
1930 O O   . VAL   A 96  ? 0.1403 0.1326 0.1528 -0.0035 0.0153  -0.0014 96  VAL   A O   
1931 C CB  . VAL   A 96  ? 0.1365 0.1224 0.1432 -0.0015 0.0231  0.0147  96  VAL   A CB  
1932 C CG1 . VAL   A 96  ? 0.1531 0.1346 0.1263 -0.0021 0.0194  0.0102  96  VAL   A CG1 
1933 C CG2 . VAL   A 96  ? 0.1339 0.1289 0.1672 -0.0122 0.0216  0.0175  96  VAL   A CG2 
1943 N N   . GLY   A 97  ? 0.1291 0.1253 0.1384 -0.0056 0.0070  0.0073  97  GLY   A N   
1944 C CA  . GLY   A 97  ? 0.1449 0.1376 0.1502 -0.0032 0.0030  0.0101  97  GLY   A CA  
1945 C C   . GLY   A 97  ? 0.1416 0.1512 0.1335 -0.0052 0.0049  0.0104  97  GLY   A C   
1946 O O   . GLY   A 97  ? 0.1530 0.1557 0.1475 -0.0090 0.0022  0.0155  97  GLY   A O   
1950 N N   A PRO   A 98  ? 0.1492 0.1571 0.1270 -0.0005 -0.0017 0.0149  98  PRO   A N   
1951 N N   B PRO   A 98  ? 0.1486 0.1566 0.1388 -0.0010 0.0051  0.0163  98  PRO   A N   
1952 C CA  A PRO   A 98  ? 0.1577 0.1785 0.1388 -0.0053 0.0005  0.0073  98  PRO   A CA  
1953 C CA  B PRO   A 98  ? 0.1554 0.1642 0.1475 -0.0004 0.0033  0.0157  98  PRO   A CA  
1954 C C   A PRO   A 98  ? 0.1608 0.1880 0.1183 -0.0137 0.0020  0.0207  98  PRO   A C   
1955 C C   B PRO   A 98  ? 0.1692 0.1683 0.1501 -0.0026 -0.0005 0.0205  98  PRO   A C   
1956 O O   A PRO   A 98  ? 0.1574 0.1663 0.1347 -0.0103 0.0001  0.0152  98  PRO   A O   
1957 O O   B PRO   A 98  ? 0.1685 0.1672 0.1561 -0.0013 0.0013  0.0166  98  PRO   A O   
1958 C CB  A PRO   A 98  ? 0.1686 0.1894 0.1283 0.0031  -0.0069 -0.0103 98  PRO   A CB  
1959 C CB  B PRO   A 98  ? 0.1530 0.1665 0.1441 0.0034  0.0054  0.0119  98  PRO   A CB  
1960 C CG  A PRO   A 98  ? 0.1707 0.1776 0.1406 0.0031  -0.0097 -0.0126 98  PRO   A CG  
1961 C CG  B PRO   A 98  ? 0.1551 0.1640 0.1432 0.0021  0.0054  0.0138  98  PRO   A CG  
1962 C CD  A PRO   A 98  ? 0.1582 0.1574 0.1366 -0.0014 -0.0106 -0.0018 98  PRO   A CD  
1963 C CD  B PRO   A 98  ? 0.1507 0.1571 0.1390 0.0006  0.0040  0.0166  98  PRO   A CD  
1978 N N   A ASN   A 99  ? 0.1677 0.2158 0.1299 -0.0133 -0.0023 0.0538  99  ASN   A N   
1979 N N   B ASN   A 99  ? 0.1844 0.1728 0.1524 -0.0026 -0.0050 0.0308  99  ASN   A N   
1980 C CA  A ASN   A 99  ? 0.1868 0.2333 0.1457 -0.0192 -0.0063 0.0707  99  ASN   A CA  
1981 C CA  B ASN   A 99  ? 0.2002 0.1797 0.1606 -0.0017 -0.0115 0.0385  99  ASN   A CA  
1982 C C   A ASN   A 99  ? 0.2050 0.2746 0.1285 -0.0310 -0.0009 0.0722  99  ASN   A C   
1983 C C   B ASN   A 99  ? 0.2093 0.1863 0.1613 0.0069  -0.0153 0.0416  99  ASN   A C   
1984 O O   A ASN   A 99  ? 0.2158 0.3032 0.1457 -0.0241 -0.0106 0.0637  99  ASN   A O   
1985 O O   B ASN   A 99  ? 0.2068 0.1735 0.1506 0.0180  -0.0221 0.0446  99  ASN   A O   
1986 C CB  A ASN   A 99  ? 0.1915 0.2180 0.1760 -0.0191 -0.0153 0.0675  99  ASN   A CB  
1987 C CB  B ASN   A 99  ? 0.2070 0.1838 0.1790 -0.0067 -0.0176 0.0422  99  ASN   A CB  
1988 C CG  A ASN   A 99  ? 0.1912 0.2095 0.2039 -0.0191 -0.0232 0.0464  99  ASN   A CG  
1989 C CG  B ASN   A 99  ? 0.2112 0.1914 0.1972 -0.0107 -0.0174 0.0467  99  ASN   A CG  
1990 O OD1 A ASN   A 99  ? 0.2045 0.2248 0.1990 -0.0054 -0.0259 0.0393  99  ASN   A OD1 
1991 O OD1 B ASN   A 99  ? 0.2149 0.1941 0.1942 -0.0138 -0.0228 0.0581  99  ASN   A OD1 
1992 N ND2 A ASN   A 99  ? 0.1912 0.1980 0.2407 -0.0130 -0.0293 0.0518  99  ASN   A ND2 
1993 N ND2 B ASN   A 99  ? 0.2110 0.1952 0.2064 -0.0081 -0.0119 0.0439  99  ASN   A ND2 
2006 N N   A VAL   A 100 ? 0.2194 0.2822 0.1192 -0.0522 -0.0245 0.0534  100 VAL   A N   
2007 N N   B VAL   A 100 ? 0.2217 0.2098 0.1824 0.0048  -0.0144 0.0338  100 VAL   A N   
2008 C CA  A VAL   A 100 ? 0.2476 0.3068 0.1484 -0.0618 -0.0294 0.0486  100 VAL   A CA  
2009 C CA  B VAL   A 100 ? 0.2349 0.2349 0.2157 0.0052  -0.0139 0.0231  100 VAL   A CA  
2010 C C   A VAL   A 100 ? 0.2597 0.3231 0.1444 -0.0637 -0.0312 0.0823  100 VAL   A C   
2011 C C   B VAL   A 100 ? 0.2447 0.2549 0.2315 0.0097  -0.0136 0.0229  100 VAL   A C   
2012 O O   A VAL   A 100 ? 0.2725 0.3347 0.1795 -0.0554 -0.0066 0.0792  100 VAL   A O   
2013 O O   B VAL   A 100 ? 0.2452 0.2588 0.2392 0.0135  -0.0102 0.0162  100 VAL   A O   
2014 C CB  A VAL   A 100 ? 0.2738 0.3140 0.1944 -0.0648 -0.0375 0.0313  100 VAL   A CB  
2015 C CB  B VAL   A 100 ? 0.2392 0.2372 0.2346 0.0042  -0.0150 0.0151  100 VAL   A CB  
2016 C CG1 A VAL   A 100 ? 0.2776 0.3178 0.2129 -0.0681 -0.0305 0.0305  100 VAL   A CG1 
2017 C CG1 B VAL   A 100 ? 0.2378 0.2354 0.2417 0.0031  -0.0143 0.0115  100 VAL   A CG1 
2018 C CG2 A VAL   A 100 ? 0.2927 0.3223 0.2063 -0.0647 -0.0358 0.0268  100 VAL   A CG2 
2019 C CG2 B VAL   A 100 ? 0.2432 0.2396 0.2410 0.0037  -0.0143 0.0131  100 VAL   A CG2 
2038 N N   A ASN   A 101 ? 0.2685 0.3297 0.1828 -0.0684 -0.0408 0.1160  101 ASN   A N   
2039 N N   B ASN   A 101 ? 0.2559 0.2675 0.2448 0.0095  -0.0149 0.0277  101 ASN   A N   
2040 C CA  A ASN   A 101 ? 0.2986 0.3414 0.2160 -0.0708 -0.0495 0.1366  101 ASN   A CA  
2041 C CA  B ASN   A 101 ? 0.2687 0.2777 0.2557 0.0089  -0.0141 0.0297  101 ASN   A CA  
2042 C C   A ASN   A 101 ? 0.3293 0.3725 0.2366 -0.0767 -0.0158 0.1591  101 ASN   A C   
2043 C C   B ASN   A 101 ? 0.2844 0.2934 0.2749 0.0052  -0.0102 0.0331  101 ASN   A C   
2044 O O   A ASN   A 101 ? 0.3462 0.3755 0.2834 -0.0702 -0.0153 0.1513  101 ASN   A O   
2045 O O   B ASN   A 101 ? 0.2873 0.2921 0.2715 0.0067  -0.0118 0.0373  101 ASN   A O   
2046 C CB  A ASN   A 101 ? 0.3051 0.3249 0.2167 -0.0626 -0.0776 0.1161  101 ASN   A CB  
2047 C CB  B ASN   A 101 ? 0.2659 0.2721 0.2471 0.0113  -0.0176 0.0276  101 ASN   A CB  
2048 C CG  A ASN   A 101 ? 0.3105 0.3067 0.2173 -0.0587 -0.0862 0.0802  101 ASN   A CG  
2049 C CG  B ASN   A 101 ? 0.2637 0.2673 0.2426 0.0117  -0.0202 0.0255  101 ASN   A CG  
2050 O OD1 A ASN   A 101 ? 0.3070 0.3140 0.2312 -0.0441 -0.0883 0.0413  101 ASN   A OD1 
2051 O OD1 B ASN   A 101 ? 0.2671 0.2688 0.2441 0.0079  -0.0195 0.0255  101 ASN   A OD1 
2052 N ND2 A ASN   A 101 ? 0.3145 0.2871 0.2260 -0.0650 -0.0808 0.0904  101 ASN   A ND2 
2053 N ND2 B ASN   A 101 ? 0.2606 0.2626 0.2403 0.0152  -0.0202 0.0211  101 ASN   A ND2 
2066 N N   A LYS   A 102 ? 0.3405 0.4091 0.2687 -0.0915 0.0004  0.1532  102 LYS   A N   
2067 N N   B LYS   A 102 ? 0.2965 0.3096 0.3006 -0.0019 -0.0073 0.0286  102 LYS   A N   
2068 C CA  A LYS   A 102 ? 0.3573 0.4404 0.2817 -0.0895 -0.0000 0.1376  102 LYS   A CA  
2069 C CA  B LYS   A 102 ? 0.3092 0.3249 0.3231 -0.0073 -0.0050 0.0224  102 LYS   A CA  
2070 C C   A LYS   A 102 ? 0.3622 0.4622 0.2572 -0.0743 0.0007  0.1260  102 LYS   A C   
2071 C C   B LYS   A 102 ? 0.3114 0.3311 0.3255 -0.0083 -0.0042 0.0206  102 LYS   A C   
2072 O O   A LYS   A 102 ? 0.3671 0.4780 0.2580 -0.0635 0.0024  0.1142  102 LYS   A O   
2073 O O   B LYS   A 102 ? 0.3129 0.3338 0.3285 -0.0076 -0.0047 0.0183  102 LYS   A O   
2074 C CB  A LYS   A 102 ? 0.3713 0.4473 0.3230 -0.0945 -0.0086 0.1195  102 LYS   A CB  
2075 C CB  B LYS   A 102 ? 0.3187 0.3331 0.3416 -0.0101 -0.0060 0.0181  102 LYS   A CB  
2076 C CG  A LYS   A 102 ? 0.3831 0.4512 0.3596 -0.0968 -0.0157 0.0934  102 LYS   A CG  
2077 C CG  B LYS   A 102 ? 0.3271 0.3393 0.3578 -0.0122 -0.0076 0.0143  102 LYS   A CG  
2078 C CD  A LYS   A 102 ? 0.3963 0.4568 0.3992 -0.0983 -0.0299 0.0667  102 LYS   A CD  
2079 C CD  B LYS   A 102 ? 0.3332 0.3444 0.3727 -0.0147 -0.0099 0.0107  102 LYS   A CD  
2080 C CE  A LYS   A 102 ? 0.4077 0.4624 0.4274 -0.1007 -0.0395 0.0498  102 LYS   A CE  
2081 C CE  B LYS   A 102 ? 0.3380 0.3478 0.3829 -0.0163 -0.0117 0.0086  102 LYS   A CE  
2082 N NZ  A LYS   A 102 ? 0.4143 0.4648 0.4479 -0.1066 -0.0353 0.0374  102 LYS   A NZ  
2083 N NZ  B LYS   A 102 ? 0.3403 0.3493 0.3901 -0.0181 -0.0119 0.0077  102 LYS   A NZ  
2110 N N   A GLY   A 103 ? 0.3590 0.4704 0.2559 -0.0642 -0.0091 0.0999  103 GLY   A N   
2111 N N   B GLY   A 103 ? 0.3117 0.3336 0.3257 -0.0090 -0.0052 0.0197  103 GLY   A N   
2112 C CA  A GLY   A 103 ? 0.3573 0.4738 0.2454 -0.0521 -0.0092 0.0787  103 GLY   A CA  
2113 C CA  B GLY   A 103 ? 0.3108 0.3338 0.3200 -0.0096 -0.0071 0.0186  103 GLY   A CA  
2114 C C   A GLY   A 103 ? 0.3505 0.4777 0.2388 -0.0425 -0.0018 0.0517  103 GLY   A C   
2115 C C   B GLY   A 103 ? 0.3093 0.3336 0.3118 -0.0087 -0.0085 0.0150  103 GLY   A C   
2116 O O   A GLY   A 103 ? 0.3576 0.4838 0.2574 -0.0352 -0.0021 0.0346  103 GLY   A O   
2117 O O   B GLY   A 103 ? 0.3095 0.3346 0.3173 -0.0100 -0.0092 0.0145  103 GLY   A O   
2124 N N   A GLU   A 104 ? 0.3312 0.4698 0.1954 -0.0446 0.0093  0.0425  104 GLU   A N   
2125 N N   B GLU   A 104 ? 0.3074 0.3306 0.2928 -0.0061 -0.0096 0.0157  104 GLU   A N   
2126 C CA  A GLU   A 104 ? 0.3072 0.4546 0.1712 -0.0520 0.0143  0.0301  104 GLU   A CA  
2127 C CA  B GLU   A 104 ? 0.3047 0.3269 0.2758 -0.0041 -0.0112 0.0134  104 GLU   A CA  
2128 C C   A GLU   A 104 ? 0.3093 0.4602 0.1728 -0.0528 0.0204  0.0055  104 GLU   A C   
2129 C C   B GLU   A 104 ? 0.3064 0.3277 0.2784 0.0005  -0.0089 0.0098  104 GLU   A C   
2130 O O   A GLU   A 104 ? 0.3008 0.4579 0.2022 -0.0539 0.0127  -0.0027 104 GLU   A O   
2131 O O   B GLU   A 104 ? 0.3056 0.3245 0.2754 0.0014  -0.0108 0.0119  104 GLU   A O   
2132 C CB  A GLU   A 104 ? 0.2769 0.4315 0.1415 -0.0583 0.0187  0.0530  104 GLU   A CB  
2133 C CB  B GLU   A 104 ? 0.3006 0.3231 0.2622 -0.0054 -0.0146 0.0151  104 GLU   A CB  
2134 C CG  A GLU   A 104 ? 0.2559 0.4121 0.1564 -0.0566 0.0123  0.0680  104 GLU   A CG  
2135 C CG  B GLU   A 104 ? 0.2975 0.3200 0.2552 -0.0055 -0.0185 0.0158  104 GLU   A CG  
2136 C CD  A GLU   A 104 ? 0.2354 0.3947 0.1633 -0.0574 0.0111  0.0793  104 GLU   A CD  
2137 C CD  B GLU   A 104 ? 0.2946 0.3165 0.2524 -0.0061 -0.0215 0.0154  104 GLU   A CD  
2138 O OE1 A GLU   A 104 ? 0.2123 0.3814 0.1328 -0.0574 0.0044  0.0802  104 GLU   A OE1 
2139 O OE1 B GLU   A 104 ? 0.2943 0.3168 0.2481 -0.0059 -0.0256 0.0153  104 GLU   A OE1 
2140 O OE2 A GLU   A 104 ? 0.2514 0.3871 0.1938 -0.0572 0.0154  0.0992  104 GLU   A OE2 
2141 O OE2 B GLU   A 104 ? 0.2943 0.3136 0.2572 -0.0065 -0.0207 0.0156  104 GLU   A OE2 
2154 N N   A ASP   A 105 ? 0.3155 0.4667 0.1787 -0.0512 0.0295  -0.0186 105 ASP   A N   
2155 N N   B ASP   A 105 ? 0.3102 0.3334 0.2933 0.0031  -0.0055 0.0037  105 ASP   A N   
2156 C CA  A ASP   A 105 ? 0.3136 0.4691 0.2195 -0.0465 0.0383  -0.0519 105 ASP   A CA  
2157 C CA  B ASP   A 105 ? 0.3127 0.3375 0.3123 0.0057  -0.0014 -0.0052 105 ASP   A CA  
2158 C C   A ASP   A 105 ? 0.2765 0.4501 0.1921 -0.0593 0.0277  -0.0707 105 ASP   A C   
2159 C C   B ASP   A 105 ? 0.3119 0.3364 0.3027 0.0016  -0.0010 -0.0071 105 ASP   A C   
2160 O O   A ASP   A 105 ? 0.2542 0.4322 0.1495 -0.0608 0.0234  -0.0954 105 ASP   A O   
2161 O O   B ASP   A 105 ? 0.3121 0.3382 0.2967 0.0014  -0.0003 -0.0082 105 ASP   A O   
2162 C CB  A ASP   A 105 ? 0.3457 0.4901 0.2977 -0.0338 0.0493  -0.0690 105 ASP   A CB  
2163 C CB  B ASP   A 105 ? 0.3155 0.3415 0.3414 0.0106  0.0018  -0.0122 105 ASP   A CB  
2164 C CG  A ASP   A 105 ? 0.3763 0.5052 0.3643 -0.0232 0.0525  -0.0827 105 ASP   A CG  
2165 C CG  B ASP   A 105 ? 0.3176 0.3438 0.3664 0.0142  0.0047  -0.0190 105 ASP   A CG  
2166 O OD1 A ASP   A 105 ? 0.3814 0.5108 0.3668 -0.0253 0.0571  -0.0962 105 ASP   A OD1 
2167 O OD1 B ASP   A 105 ? 0.3184 0.3443 0.3769 0.0134  0.0058  -0.0213 105 ASP   A OD1 
2168 O OD2 A ASP   A 105 ? 0.4008 0.5111 0.4126 -0.0174 0.0531  -0.0766 105 ASP   A OD2 
2169 O OD2 B ASP   A 105 ? 0.3172 0.3449 0.3769 0.0161  0.0073  -0.0201 105 ASP   A OD2 
2178 N N   A ILE   A 106 ? 0.2600 0.4282 0.2197 -0.0658 -0.0016 -0.0660 106 ILE   A N   
2179 N N   B ILE   A 106 ? 0.3100 0.3323 0.3013 -0.0021 -0.0036 -0.0086 106 ILE   A N   
2180 C CA  A ILE   A 106 ? 0.2349 0.4110 0.2381 -0.0765 -0.0233 -0.0725 106 ILE   A CA  
2181 C CA  B ILE   A 106 ? 0.3084 0.3305 0.3018 -0.0074 -0.0056 -0.0107 106 ILE   A CA  
2182 C C   A ILE   A 106 ? 0.2197 0.3856 0.2551 -0.0930 -0.0201 -0.0890 106 ILE   A C   
2183 C C   B ILE   A 106 ? 0.3049 0.3243 0.2990 -0.0087 -0.0025 -0.0115 106 ILE   A C   
2184 O O   A ILE   A 106 ? 0.1996 0.3755 0.2669 -0.0982 0.0027  -0.0914 106 ILE   A O   
2185 O O   B ILE   A 106 ? 0.3045 0.3249 0.2944 -0.0089 -0.0027 -0.0156 106 ILE   A O   
2186 C CB  A ILE   A 106 ? 0.2359 0.4215 0.2834 -0.0632 -0.0373 -0.0419 106 ILE   A CB  
2187 C CB  B ILE   A 106 ? 0.3108 0.3344 0.3092 -0.0098 -0.0108 -0.0080 106 ILE   A CB  
2188 C CG1 A ILE   A 106 ? 0.2224 0.4245 0.3055 -0.0444 -0.0399 -0.0155 106 ILE   A CG1 
2189 C CG1 B ILE   A 106 ? 0.3109 0.3366 0.3129 -0.0104 -0.0132 -0.0053 106 ILE   A CG1 
2190 C CG2 A ILE   A 106 ? 0.2489 0.4255 0.3004 -0.0632 -0.0444 -0.0436 106 ILE   A CG2 
2191 C CG2 B ILE   A 106 ? 0.3125 0.3350 0.3116 -0.0102 -0.0126 -0.0086 106 ILE   A CG2 
2192 C CD1 A ILE   A 106 ? 0.2174 0.4227 0.3137 -0.0295 -0.0289 -0.0047 106 ILE   A CD1 
2193 C CD1 B ILE   A 106 ? 0.3114 0.3368 0.3154 -0.0099 -0.0137 -0.0049 106 ILE   A CD1 
2216 N N   A GLN   A 107 ? 0.2378 0.3678 0.2760 -0.0920 -0.0058 -0.1057 107 GLN   A N   
2217 N N   B GLN   A 107 ? 0.3017 0.3158 0.3061 -0.0087 0.0030  -0.0086 107 GLN   A N   
2218 C CA  A GLN   A 107 ? 0.2629 0.3448 0.3547 -0.0747 0.0242  -0.0983 107 GLN   A CA  
2219 C CA  B GLN   A 107 ? 0.2977 0.3055 0.3227 -0.0069 0.0092  -0.0079 107 GLN   A CA  
2220 C C   A GLN   A 107 ? 0.2355 0.2828 0.3384 -0.0599 0.0469  -0.0752 107 GLN   A C   
2221 C C   B GLN   A 107 ? 0.2720 0.2747 0.2842 -0.0035 0.0158  0.0004  107 GLN   A C   
2222 O O   A GLN   A 107 ? 0.2432 0.2664 0.4026 -0.0553 0.0510  -0.0706 107 GLN   A O   
2223 O O   B GLN   A 107 ? 0.2726 0.2739 0.2855 -0.0016 0.0201  0.0005  107 GLN   A O   
2224 C CB  A GLN   A 107 ? 0.3059 0.3751 0.4446 -0.0785 0.0142  -0.1052 107 GLN   A CB  
2225 C CB  B GLN   A 107 ? 0.3181 0.3245 0.3782 -0.0086 0.0059  -0.0120 107 GLN   A CB  
2226 C CG  A GLN   A 107 ? 0.3475 0.4073 0.5445 -0.0785 0.0048  -0.0998 107 GLN   A CG  
2227 C CG  B GLN   A 107 ? 0.3364 0.3427 0.4331 -0.0102 0.0028  -0.0145 107 GLN   A CG  
2228 C CD  A GLN   A 107 ? 0.3820 0.4354 0.6304 -0.0779 0.0032  -0.0881 107 GLN   A CD  
2229 C CD  B GLN   A 107 ? 0.3515 0.3579 0.4770 -0.0117 0.0007  -0.0148 107 GLN   A CD  
2230 O OE1 A GLN   A 107 ? 0.3990 0.4426 0.6653 -0.0764 0.0041  -0.0854 107 GLN   A OE1 
2231 O OE1 B GLN   A 107 ? 0.3556 0.3617 0.4957 -0.0118 -0.0001 -0.0156 107 GLN   A OE1 
2232 N NE2 A GLN   A 107 ? 0.3922 0.4540 0.6588 -0.0800 0.0004  -0.0877 107 GLN   A NE2 
2233 N NE2 B GLN   A 107 ? 0.3584 0.3642 0.4929 -0.0132 0.0004  -0.0149 107 GLN   A NE2 
2250 N N   A LEU   A 108 ? 0.1994 0.2277 0.2694 -0.0517 0.0450  -0.0728 108 LEU   A N   
2251 N N   B LEU   A 108 ? 0.2443 0.2431 0.2521 -0.0024 0.0184  0.0046  108 LEU   A N   
2252 C CA  A LEU   A 108 ? 0.1782 0.1816 0.2330 -0.0231 0.0354  -0.0243 108 LEU   A CA  
2253 C CA  B LEU   A 108 ? 0.2142 0.2107 0.2234 0.0015  0.0189  0.0094  108 LEU   A CA  
2254 C C   A LEU   A 108 ? 0.1548 0.1432 0.2185 -0.0065 0.0199  0.0115  108 LEU   A C   
2255 C C   B LEU   A 108 ? 0.1822 0.1782 0.2118 0.0037  0.0178  0.0145  108 LEU   A C   
2256 O O   A LEU   A 108 ? 0.1435 0.1457 0.2486 -0.0013 0.0291  0.0106  108 LEU   A O   
2257 O O   B LEU   A 108 ? 0.1823 0.1783 0.2110 0.0036  0.0216  0.0141  108 LEU   A O   
2258 C CB  A LEU   A 108 ? 0.1868 0.1884 0.2137 -0.0264 0.0438  -0.0216 108 LEU   A CB  
2259 C CB  B LEU   A 108 ? 0.2156 0.2134 0.2125 0.0020  0.0186  0.0075  108 LEU   A CB  
2260 C CG  A LEU   A 108 ? 0.2024 0.2097 0.2268 -0.0280 0.0486  -0.0229 108 LEU   A CG  
2261 C CG  B LEU   A 108 ? 0.2164 0.2144 0.2115 0.0023  0.0182  0.0037  108 LEU   A CG  
2262 C CD1 A LEU   A 108 ? 0.2210 0.2168 0.2352 -0.0333 0.0599  -0.0202 108 LEU   A CD1 
2263 C CD1 B LEU   A 108 ? 0.2194 0.2161 0.2124 0.0017  0.0206  0.0059  108 LEU   A CD1 
2264 C CD2 A LEU   A 108 ? 0.2004 0.2319 0.2660 -0.0265 0.0386  -0.0198 108 LEU   A CD2 
2265 C CD2 B LEU   A 108 ? 0.2149 0.2138 0.2138 0.0040  0.0162  -0.0035 108 LEU   A CD2 
2288 N N   . LEU   A 109 ? 0.1528 0.1507 0.2117 0.0054  0.0186  0.0228  109 LEU   A N   
2289 C CA  . LEU   A 109 ? 0.1443 0.1388 0.1917 0.0017  0.0104  0.0249  109 LEU   A CA  
2290 C C   . LEU   A 109 ? 0.1319 0.1308 0.2006 -0.0124 0.0093  0.0096  109 LEU   A C   
2291 O O   . LEU   A 109 ? 0.1409 0.1271 0.2127 -0.0042 -0.0057 0.0030  109 LEU   A O   
2292 C CB  . LEU   A 109 ? 0.1499 0.1510 0.2137 0.0070  0.0027  0.0340  109 LEU   A CB  
2293 C CG  . LEU   A 109 ? 0.1442 0.1563 0.2207 0.0074  0.0110  0.0426  109 LEU   A CG  
2294 C CD1 . LEU   A 109 ? 0.1499 0.1501 0.2427 0.0012  0.0221  0.0217  109 LEU   A CD1 
2295 C CD2 . LEU   A 109 ? 0.1515 0.1739 0.2454 0.0076  0.0121  0.0490  109 LEU   A CD2 
2308 N N   . LYS   A 110 ? 0.1359 0.1321 0.1866 -0.0094 0.0064  0.0132  110 LYS   A N   
2309 C CA  . LYS   A 110 ? 0.1366 0.1227 0.1870 -0.0103 0.0028  0.0149  110 LYS   A CA  
2310 C C   . LYS   A 110 ? 0.1365 0.1201 0.1857 -0.0074 0.0005  0.0039  110 LYS   A C   
2311 O O   . LYS   A 110 ? 0.1306 0.1221 0.1931 -0.0094 0.0052  0.0006  110 LYS   A O   
2312 C CB  . LYS   A 110 ? 0.1387 0.1327 0.2092 -0.0081 -0.0080 0.0040  110 LYS   A CB  
2313 C CG  . LYS   A 110 ? 0.1454 0.1316 0.2211 -0.0055 -0.0135 -0.0026 110 LYS   A CG  
2314 C CD  . LYS   A 110 ? 0.1466 0.1344 0.2298 -0.0119 -0.0039 -0.0053 110 LYS   A CD  
2315 C CE  . LYS   A 110 ? 0.1581 0.1390 0.2561 -0.0038 0.0089  -0.0113 110 LYS   A CE  
2316 N NZ  . LYS   A 110 ? 0.1599 0.1463 0.2747 -0.0145 0.0160  -0.0009 110 LYS   A NZ  
2330 N N   . SER   A 111 ? 0.1355 0.1274 0.1716 -0.0032 0.0013  0.0075  111 SER   A N   
2331 C CA  . SER   A 111 ? 0.1274 0.1312 0.1851 -0.0016 0.0072  0.0047  111 SER   A CA  
2332 C C   . SER   A 111 ? 0.1193 0.1228 0.1847 -0.0078 0.0070  0.0170  111 SER   A C   
2333 O O   . SER   A 111 ? 0.1322 0.1186 0.2000 -0.0040 0.0077  0.0136  111 SER   A O   
2334 C CB  . SER   A 111 ? 0.1483 0.1540 0.2006 -0.0046 0.0193  -0.0037 111 SER   A CB  
2335 O OG  . SER   A 111 ? 0.1952 0.1718 0.2087 -0.0018 0.0239  -0.0115 111 SER   A OG  
2341 N N   . ALA   A 112 ? 0.1289 0.1156 0.1977 -0.0010 0.0153  0.0123  112 ALA   A N   
2342 C CA  . ALA   A 112 ? 0.1287 0.1135 0.1907 -0.0044 0.0159  0.0074  112 ALA   A CA  
2343 C C   . ALA   A 112 ? 0.1243 0.1138 0.1950 -0.0031 0.0106  0.0019  112 ALA   A C   
2344 O O   . ALA   A 112 ? 0.1270 0.1159 0.1915 -0.0154 0.0158  0.0137  112 ALA   A O   
2345 C CB  . ALA   A 112 ? 0.1419 0.1177 0.1920 -0.0039 0.0165  0.0110  112 ALA   A CB  
2351 N N   . TYR   A 113 ? 0.1170 0.1178 0.1958 -0.0031 0.0090  0.0192  113 TYR   A N   
2352 C CA  . TYR   A 113 ? 0.1118 0.1232 0.1965 -0.0004 0.0098  0.0211  113 TYR   A CA  
2353 C C   . TYR   A 113 ? 0.1122 0.1190 0.1818 -0.0114 0.0102  0.0157  113 TYR   A C   
2354 O O   . TYR   A 113 ? 0.1201 0.1181 0.1878 -0.0038 0.0160  0.0097  113 TYR   A O   
2355 C CB  . TYR   A 113 ? 0.1148 0.1246 0.1993 -0.0052 -0.0030 0.0253  113 TYR   A CB  
2356 C CG  . TYR   A 113 ? 0.1204 0.1352 0.1850 -0.0092 0.0124  0.0295  113 TYR   A CG  
2357 C CD1 . TYR   A 113 ? 0.1220 0.1467 0.1771 -0.0035 0.0140  0.0309  113 TYR   A CD1 
2358 C CD2 . TYR   A 113 ? 0.1233 0.1416 0.1836 -0.0117 0.0083  0.0288  113 TYR   A CD2 
2359 C CE1 . TYR   A 113 ? 0.1250 0.1566 0.1853 0.0011  0.0135  0.0397  113 TYR   A CE1 
2360 C CE2 . TYR   A 113 ? 0.1275 0.1539 0.1827 -0.0147 0.0028  0.0340  113 TYR   A CE2 
2361 C CZ  . TYR   A 113 ? 0.1245 0.1547 0.1777 0.0003  0.0153  0.0423  113 TYR   A CZ  
2362 O OH  . TYR   A 113 ? 0.1203 0.1670 0.1955 0.0107  0.0139  0.0450  113 TYR   A OH  
2372 N N   . GLU   A 114 ? 0.1161 0.1192 0.1862 -0.0085 0.0125  0.0136  114 GLU   A N   
2373 C CA  . GLU   A 114 ? 0.1158 0.1107 0.2033 0.0005  0.0126  0.0242  114 GLU   A CA  
2374 C C   . GLU   A 114 ? 0.1150 0.1177 0.1863 -0.0017 0.0129  0.0144  114 GLU   A C   
2375 O O   . GLU   A 114 ? 0.1331 0.1181 0.1796 0.0000  0.0075  0.0111  114 GLU   A O   
2376 C CB  . GLU   A 114 ? 0.1159 0.1189 0.1924 -0.0020 0.0094  0.0187  114 GLU   A CB  
2377 C CG  . GLU   A 114 ? 0.1287 0.1165 0.1996 -0.0002 0.0105  0.0079  114 GLU   A CG  
2378 C CD  . GLU   A 114 ? 0.1347 0.1219 0.2095 -0.0027 0.0038  0.0056  114 GLU   A CD  
2379 O OE1 . GLU   A 114 ? 0.1408 0.1218 0.2140 -0.0084 0.0196  -0.0017 114 GLU   A OE1 
2380 O OE2 . GLU   A 114 ? 0.1502 0.1261 0.2282 -0.0100 0.0093  -0.0092 114 GLU   A OE2 
2387 N N   . ASN   A 115 ? 0.1217 0.1139 0.1757 -0.0070 0.0112  0.0067  115 ASN   A N   
2388 C CA  . ASN   A 115 ? 0.1185 0.1231 0.1848 -0.0113 0.0128  0.0083  115 ASN   A CA  
2389 C C   . ASN   A 115 ? 0.1216 0.1169 0.1750 -0.0097 0.0072  0.0089  115 ASN   A C   
2390 O O   . ASN   A 115 ? 0.1258 0.1338 0.1743 -0.0097 0.0121  0.0162  115 ASN   A O   
2391 C CB  . ASN   A 115 ? 0.1267 0.1279 0.1707 -0.0112 0.0163  0.0103  115 ASN   A CB  
2392 C CG  . ASN   A 115 ? 0.1301 0.1484 0.1895 -0.0094 0.0175  0.0143  115 ASN   A CG  
2393 O OD1 . ASN   A 115 ? 0.1358 0.2413 0.2155 -0.0111 0.0246  0.0241  115 ASN   A OD1 
2394 N ND2 . ASN   A 115 ? 0.1278 0.1339 0.1897 -0.0101 0.0218  0.0188  115 ASN   A ND2 
2401 N N   . PHE   A 116 ? 0.1184 0.1213 0.1832 -0.0041 0.0126  0.0229  116 PHE   A N   
2402 C CA  . PHE   A 116 ? 0.1227 0.1300 0.1697 -0.0040 0.0144  0.0220  116 PHE   A CA  
2403 C C   . PHE   A 116 ? 0.1198 0.1317 0.1831 -0.0075 0.0152  0.0258  116 PHE   A C   
2404 O O   . PHE   A 116 ? 0.1267 0.1351 0.1904 0.0010  0.0108  0.0283  116 PHE   A O   
2405 C CB  . PHE   A 116 ? 0.1182 0.1178 0.1935 -0.0012 0.0213  0.0199  116 PHE   A CB  
2406 C CG  . PHE   A 116 ? 0.1190 0.1177 0.1859 -0.0038 0.0175  0.0126  116 PHE   A CG  
2407 C CD1 . PHE   A 116 ? 0.1268 0.1199 0.1673 -0.0022 0.0154  0.0195  116 PHE   A CD1 
2408 C CD2 . PHE   A 116 ? 0.1289 0.1223 0.1965 -0.0036 0.0235  0.0193  116 PHE   A CD2 
2409 C CE1 . PHE   A 116 ? 0.1328 0.1195 0.1772 -0.0124 0.0143  0.0135  116 PHE   A CE1 
2410 C CE2 . PHE   A 116 ? 0.1270 0.1207 0.2022 -0.0003 0.0227  0.0111  116 PHE   A CE2 
2411 C CZ  . PHE   A 116 ? 0.1305 0.1114 0.1866 0.0026  0.0104  0.0153  116 PHE   A CZ  
2421 N N   . ASN   A 117 ? 0.1201 0.1222 0.1889 -0.0044 0.0120  0.0275  117 ASN   A N   
2422 C CA  . ASN   A 117 ? 0.1259 0.1234 0.1997 0.0022  0.0156  0.0271  117 ASN   A CA  
2423 C C   . ASN   A 117 ? 0.1243 0.1349 0.2067 -0.0007 0.0157  0.0235  117 ASN   A C   
2424 O O   . ASN   A 117 ? 0.1341 0.1380 0.2206 -0.0030 0.0000  0.0351  117 ASN   A O   
2425 C CB  . ASN   A 117 ? 0.1193 0.1235 0.2002 0.0050  0.0095  0.0355  117 ASN   A CB  
2426 C CG  . ASN   A 117 ? 0.1210 0.1304 0.1898 -0.0015 0.0149  0.0272  117 ASN   A CG  
2427 O OD1 . ASN   A 117 ? 0.1246 0.1482 0.2025 -0.0092 0.0121  0.0195  117 ASN   A OD1 
2428 N ND2 . ASN   A 117 ? 0.1226 0.1303 0.1919 -0.0031 0.0085  0.0210  117 ASN   A ND2 
2435 N N   . GLN   A 118 ? 0.1226 0.1323 0.2069 -0.0041 0.0048  0.0288  118 GLN   A N   
2436 C CA  . GLN   A 118 ? 0.1272 0.1417 0.2071 -0.0054 0.0008  0.0177  118 GLN   A CA  
2437 C C   . GLN   A 118 ? 0.1305 0.1506 0.2008 -0.0061 -0.0048 0.0244  118 GLN   A C   
2438 O O   . GLN   A 118 ? 0.1307 0.1819 0.2323 0.0050  -0.0099 0.0055  118 GLN   A O   
2439 C CB  . GLN   A 118 ? 0.1243 0.1486 0.2216 -0.0021 0.0086  0.0263  118 GLN   A CB  
2440 C CG  . GLN   A 118 ? 0.1213 0.1497 0.2194 -0.0014 0.0071  0.0336  118 GLN   A CG  
2441 C CD  . GLN   A 118 ? 0.1154 0.1503 0.2338 0.0013  0.0145  0.0324  118 GLN   A CD  
2442 O OE1 . GLN   A 118 ? 0.1240 0.1655 0.2503 0.0126  -0.0016 0.0170  118 GLN   A OE1 
2443 N NE2 . GLN   A 118 ? 0.1336 0.1490 0.2304 0.0038  0.0069  0.0308  118 GLN   A NE2 
2452 N N   . HIS   A 119 ? 0.1351 0.1448 0.1859 -0.0015 0.0009  0.0201  119 HIS   A N   
2453 C CA  . HIS   A 119 ? 0.1449 0.1475 0.1934 -0.0048 0.0056  0.0303  119 HIS   A CA  
2454 C C   . HIS   A 119 ? 0.1534 0.1528 0.1901 -0.0068 0.0022  0.0377  119 HIS   A C   
2455 O O   . HIS   A 119 ? 0.1525 0.1708 0.1910 -0.0234 0.0044  0.0359  119 HIS   A O   
2456 C CB  . HIS   A 119 ? 0.1486 0.1461 0.2045 0.0007  0.0189  0.0292  119 HIS   A CB  
2457 C CG  . HIS   A 119 ? 0.1501 0.1547 0.2432 0.0039  0.0169  0.0376  119 HIS   A CG  
2458 N ND1 . HIS   A 119 ? 0.1635 0.1797 0.2970 -0.0105 0.0130  0.0261  119 HIS   A ND1 
2459 C CD2 . HIS   A 119 ? 0.1615 0.1669 0.2620 0.0126  0.0338  0.0594  119 HIS   A CD2 
2460 C CE1 . HIS   A 119 ? 0.1654 0.1798 0.3129 -0.0126 0.0290  0.0514  119 HIS   A CE1 
2461 N NE2 . HIS   A 119 ? 0.1734 0.1708 0.2996 -0.0011 0.0451  0.0726  119 HIS   A NE2 
2469 N N   . GLU   A 120 ? 0.1599 0.1781 0.1886 0.0024  -0.0028 0.0563  120 GLU   A N   
2470 C CA  . GLU   A 120 ? 0.1775 0.2047 0.2095 0.0070  0.0038  0.0798  120 GLU   A CA  
2471 C C   . GLU   A 120 ? 0.1612 0.1881 0.1943 -0.0109 0.0070  0.0764  120 GLU   A C   
2472 O O   . GLU   A 120 ? 0.1632 0.1842 0.1986 -0.0114 0.0029  0.0717  120 GLU   A O   
2473 C CB  . GLU   A 120 ? 0.2399 0.2753 0.2629 0.0314  0.0029  0.1374  120 GLU   A CB  
2474 C CG  . GLU   A 120 ? 0.3360 0.3559 0.3827 0.0487  0.0025  0.1324  120 GLU   A CG  
2475 C CD  . GLU   A 120 ? 0.4131 0.4232 0.4966 0.0570  0.0130  0.1126  120 GLU   A CD  
2476 O OE1 . GLU   A 120 ? 0.4449 0.4532 0.5351 0.0569  0.0148  0.1081  120 GLU   A OE1 
2477 O OE2 . GLU   A 120 ? 0.5144 0.5144 0.5496 0.0596  0.0185  0.1060  120 GLU   A OE2 
2484 N N   . VAL   A 121 ? 0.1581 0.1878 0.1754 -0.0117 0.0125  0.0613  121 VAL   A N   
2485 C CA  . VAL   A 121 ? 0.1679 0.1909 0.1563 -0.0076 0.0224  0.0577  121 VAL   A CA  
2486 C C   . VAL   A 121 ? 0.1522 0.1745 0.1476 -0.0123 0.0190  0.0386  121 VAL   A C   
2487 O O   . VAL   A 121 ? 0.1561 0.1820 0.1703 -0.0198 -0.0027 0.0372  121 VAL   A O   
2488 C CB  . VAL   A 121 ? 0.2081 0.2288 0.1835 0.0027  0.0323  0.0665  121 VAL   A CB  
2489 C CG1 . VAL   A 121 ? 0.2137 0.2478 0.1903 0.0129  0.0327  0.0675  121 VAL   A CG1 
2490 C CG2 . VAL   A 121 ? 0.2303 0.2482 0.2313 -0.0064 0.0263  0.0505  121 VAL   A CG2 
2500 N N   . LEU   A 122 ? 0.1443 0.1593 0.1722 -0.0105 0.0186  0.0446  122 LEU   A N   
2501 C CA  . LEU   A 122 ? 0.1515 0.1487 0.1664 -0.0166 0.0325  0.0414  122 LEU   A CA  
2502 C C   . LEU   A 122 ? 0.1454 0.1460 0.1674 -0.0165 0.0119  0.0334  122 LEU   A C   
2503 O O   . LEU   A 122 ? 0.1452 0.1513 0.2015 -0.0196 0.0141  0.0377  122 LEU   A O   
2504 C CB  . LEU   A 122 ? 0.1706 0.1516 0.1979 -0.0032 0.0213  0.0490  122 LEU   A CB  
2505 C CG  . LEU   A 122 ? 0.1743 0.1570 0.1881 -0.0063 0.0236  0.0337  122 LEU   A CG  
2506 C CD1 . LEU   A 122 ? 0.1983 0.1567 0.2054 -0.0123 0.0271  0.0298  122 LEU   A CD1 
2507 C CD2 . LEU   A 122 ? 0.1682 0.1472 0.1855 -0.0087 0.0327  0.0285  122 LEU   A CD2 
2519 N N   . LEU   A 123 ? 0.1412 0.1456 0.1512 -0.0190 0.0030  0.0310  123 LEU   A N   
2520 C CA  . LEU   A 123 ? 0.1421 0.1473 0.1448 -0.0146 0.0167  0.0269  123 LEU   A CA  
2521 C C   . LEU   A 123 ? 0.1328 0.1472 0.1483 -0.0076 0.0133  0.0349  123 LEU   A C   
2522 O O   . LEU   A 123 ? 0.1261 0.1604 0.1531 -0.0252 0.0042  0.0365  123 LEU   A O   
2523 C CB  . LEU   A 123 ? 0.1544 0.1559 0.1625 -0.0162 0.0294  0.0278  123 LEU   A CB  
2524 C CG  . LEU   A 123 ? 0.1531 0.1673 0.1761 -0.0172 0.0322  0.0109  123 LEU   A CG  
2525 C CD1 . LEU   A 123 ? 0.1645 0.1744 0.1924 0.0006  0.0270  0.0056  123 LEU   A CD1 
2526 C CD2 . LEU   A 123 ? 0.1695 0.1713 0.1789 -0.0108 0.0227  0.0029  123 LEU   A CD2 
2538 N N   A ALA   A 124 ? 0.1304 0.1359 0.1530 -0.0078 0.0153  0.0284  124 ALA   A N   
2539 N N   B ALA   A 124 ? 0.1399 0.1406 0.1381 -0.0118 0.0117  0.0275  124 ALA   A N   
2540 C CA  A ALA   A 124 ? 0.1223 0.1311 0.1616 -0.0077 0.0087  0.0325  124 ALA   A CA  
2541 C CA  B ALA   A 124 ? 0.1461 0.1430 0.1350 -0.0189 0.0075  0.0249  124 ALA   A CA  
2542 C C   A ALA   A 124 ? 0.1175 0.1290 0.1651 -0.0076 0.0175  0.0342  124 ALA   A C   
2543 C C   B ALA   A 124 ? 0.1459 0.1434 0.1347 -0.0162 0.0076  0.0207  124 ALA   A C   
2544 O O   A ALA   A 124 ? 0.1218 0.1386 0.1776 -0.0033 0.0147  0.0406  124 ALA   A O   
2545 O O   B ALA   A 124 ? 0.1454 0.1433 0.1349 -0.0125 0.0052  0.0212  124 ALA   A O   
2546 C CB  A ALA   A 124 ? 0.1225 0.1266 0.1903 -0.0062 0.0006  0.0363  124 ALA   A CB  
2547 C CB  B ALA   A 124 ? 0.1503 0.1423 0.1364 -0.0258 0.0075  0.0254  124 ALA   A CB  
2558 N N   A PRO   A 125 ? 0.1173 0.1284 0.1694 -0.0075 0.0095  0.0421  125 PRO   A N   
2559 N N   B PRO   A 125 ? 0.1470 0.1430 0.1322 -0.0127 0.0044  0.0190  125 PRO   A N   
2560 C CA  A PRO   A 125 ? 0.1274 0.1350 0.1744 -0.0043 0.0114  0.0408  125 PRO   A CA  
2561 C CA  B PRO   A 125 ? 0.1481 0.1454 0.1354 -0.0091 0.0035  0.0170  125 PRO   A CA  
2562 C C   A PRO   A 125 ? 0.1183 0.1386 0.1630 -0.0085 0.0110  0.0332  125 PRO   A C   
2563 C C   B PRO   A 125 ? 0.1450 0.1445 0.1370 -0.0072 0.0026  0.0191  125 PRO   A C   
2564 O O   A PRO   A 125 ? 0.1193 0.1375 0.1817 -0.0044 -0.0022 0.0280  125 PRO   A O   
2565 O O   B PRO   A 125 ? 0.1466 0.1458 0.1457 -0.0062 0.0077  0.0200  125 PRO   A O   
2566 C CB  A PRO   A 125 ? 0.1412 0.1298 0.1605 -0.0082 0.0163  0.0351  125 PRO   A CB  
2567 C CB  B PRO   A 125 ? 0.1511 0.1467 0.1325 -0.0101 0.0077  0.0147  125 PRO   A CB  
2568 C CG  A PRO   A 125 ? 0.1416 0.1302 0.1726 -0.0111 0.0142  0.0309  125 PRO   A CG  
2569 C CG  B PRO   A 125 ? 0.1539 0.1462 0.1357 -0.0125 0.0070  0.0170  125 PRO   A CG  
2570 C CD  A PRO   A 125 ? 0.1271 0.1361 0.1684 -0.0172 0.0176  0.0354  125 PRO   A CD  
2571 C CD  B PRO   A 125 ? 0.1502 0.1449 0.1334 -0.0131 0.0078  0.0175  125 PRO   A CD  
2586 N N   A LEU   A 126 ? 0.1165 0.1455 0.1699 0.0012  0.0064  0.0326  126 LEU   A N   
2587 N N   B LEU   A 126 ? 0.1460 0.1402 0.1397 -0.0027 -0.0055 0.0203  126 LEU   A N   
2588 C CA  A LEU   A 126 ? 0.1248 0.1440 0.1699 -0.0039 0.0027  0.0370  126 LEU   A CA  
2589 C CA  B LEU   A 126 ? 0.1429 0.1319 0.1405 0.0007  -0.0064 0.0182  126 LEU   A CA  
2590 C C   A LEU   A 126 ? 0.1326 0.1380 0.1779 0.0023  0.0070  0.0265  126 LEU   A C   
2591 C C   B LEU   A 126 ? 0.1365 0.1240 0.1335 0.0039  -0.0109 0.0190  126 LEU   A C   
2592 O O   A LEU   A 126 ? 0.1427 0.1379 0.1929 0.0104  0.0190  0.0398  126 LEU   A O   
2593 O O   B LEU   A 126 ? 0.1373 0.1181 0.1398 0.0006  -0.0186 0.0261  126 LEU   A O   
2594 C CB  A LEU   A 126 ? 0.1333 0.1520 0.1767 -0.0026 -0.0001 0.0346  126 LEU   A CB  
2595 C CB  B LEU   A 126 ? 0.1459 0.1315 0.1481 0.0004  -0.0053 0.0152  126 LEU   A CB  
2596 C CG  A LEU   A 126 ? 0.1264 0.1737 0.2061 -0.0031 0.0126  0.0365  126 LEU   A CG  
2597 C CG  B LEU   A 126 ? 0.1465 0.1270 0.1537 0.0035  -0.0044 0.0038  126 LEU   A CG  
2598 C CD1 A LEU   A 126 ? 0.1301 0.1988 0.2424 -0.0024 0.0054  0.0371  126 LEU   A CD1 
2599 C CD1 B LEU   A 126 ? 0.1492 0.1263 0.1616 0.0056  -0.0096 -0.0034 126 LEU   A CD1 
2600 C CD2 A LEU   A 126 ? 0.1449 0.1639 0.2102 -0.0174 0.0222  0.0363  126 LEU   A CD2 
2601 C CD2 B LEU   A 126 ? 0.1423 0.1252 0.1528 0.0080  -0.0095 0.0014  126 LEU   A CD2 
2624 N N   A LEU   A 127 ? 0.1276 0.1365 0.1760 0.0046  0.0112  0.0331  127 LEU   A N   
2625 N N   B LEU   A 127 ? 0.1317 0.1260 0.1282 0.0069  -0.0082 0.0297  127 LEU   A N   
2626 C CA  A LEU   A 127 ? 0.1286 0.1394 0.1666 -0.0003 -0.0008 0.0228  127 LEU   A CA  
2627 C CA  B LEU   A 127 ? 0.1282 0.1295 0.1307 0.0098  -0.0031 0.0314  127 LEU   A CA  
2628 C C   A LEU   A 127 ? 0.1259 0.1327 0.1521 0.0001  -0.0052 0.0173  127 LEU   A C   
2629 C C   B LEU   A 127 ? 0.1297 0.1309 0.1384 0.0112  -0.0021 0.0192  127 LEU   A C   
2630 O O   A LEU   A 127 ? 0.1337 0.1389 0.1642 -0.0105 -0.0046 0.0200  127 LEU   A O   
2631 O O   B LEU   A 127 ? 0.1289 0.1322 0.1457 0.0117  0.0063  0.0248  127 LEU   A O   
2632 C CB  A LEU   A 127 ? 0.1322 0.1502 0.1736 0.0085  0.0093  0.0266  127 LEU   A CB  
2633 C CB  B LEU   A 127 ? 0.1266 0.1359 0.1303 0.0051  -0.0023 0.0308  127 LEU   A CB  
2634 C CG  A LEU   A 127 ? 0.1355 0.1581 0.1723 0.0103  -0.0055 0.0319  127 LEU   A CG  
2635 C CG  B LEU   A 127 ? 0.1257 0.1426 0.1206 0.0051  -0.0057 0.0267  127 LEU   A CG  
2636 C CD1 A LEU   A 127 ? 0.1412 0.1565 0.1944 0.0039  -0.0032 0.0355  127 LEU   A CD1 
2637 C CD1 B LEU   A 127 ? 0.1252 0.1449 0.1213 0.0099  -0.0077 0.0259  127 LEU   A CD1 
2638 C CD2 A LEU   A 127 ? 0.1473 0.1649 0.1975 0.0086  -0.0150 0.0251  127 LEU   A CD2 
2639 C CD2 B LEU   A 127 ? 0.1277 0.1439 0.1098 0.0035  -0.0125 0.0181  127 LEU   A CD2 
2662 N N   A SER   A 128 ? 0.1273 0.1313 0.1522 -0.0046 -0.0061 0.0216  128 SER   A N   
2663 N N   B SER   A 128 ? 0.1287 0.1321 0.1414 0.0061  -0.0052 0.0143  128 SER   A N   
2664 C CA  A SER   A 128 ? 0.1406 0.1347 0.1415 -0.0039 -0.0079 0.0232  128 SER   A CA  
2665 C CA  B SER   A 128 ? 0.1306 0.1313 0.1330 -0.0005 -0.0102 0.0115  128 SER   A CA  
2666 C C   A SER   A 128 ? 0.1456 0.1392 0.1509 -0.0000 -0.0085 0.0205  128 SER   A C   
2667 C C   B SER   A 128 ? 0.1282 0.1322 0.1327 -0.0051 -0.0171 0.0129  128 SER   A C   
2668 O O   A SER   A 128 ? 0.1617 0.1543 0.1596 0.0069  -0.0168 0.0096  128 SER   A O   
2669 O O   B SER   A 128 ? 0.1242 0.1326 0.1378 -0.0040 -0.0139 0.0108  128 SER   A O   
2670 C CB  A SER   A 128 ? 0.1407 0.1320 0.1489 -0.0039 -0.0092 0.0296  128 SER   A CB  
2671 C CB  B SER   A 128 ? 0.1333 0.1302 0.1305 -0.0018 -0.0075 0.0140  128 SER   A CB  
2672 O OG  A SER   A 128 ? 0.1465 0.1440 0.1566 -0.0040 -0.0025 0.0160  128 SER   A OG  
2673 O OG  B SER   A 128 ? 0.1360 0.1317 0.1285 -0.0058 -0.0003 0.0281  128 SER   A OG  
2684 N N   A ALA   A 129 ? 0.1409 0.1521 0.1635 -0.0003 -0.0007 0.0264  129 ALA   A N   
2685 N N   B ALA   A 129 ? 0.1309 0.1385 0.1264 -0.0063 -0.0252 0.0123  129 ALA   A N   
2686 C CA  A ALA   A 129 ? 0.1412 0.1555 0.1711 0.0016  0.0015  0.0284  129 ALA   A CA  
2687 C CA  B ALA   A 129 ? 0.1366 0.1432 0.1319 -0.0052 -0.0229 0.0131  129 ALA   A CA  
2688 C C   A ALA   A 129 ? 0.1432 0.1469 0.1510 -0.0044 -0.0034 0.0109  129 ALA   A C   
2689 C C   B ALA   A 129 ? 0.1418 0.1467 0.1318 -0.0018 -0.0170 0.0158  129 ALA   A C   
2690 O O   A ALA   A 129 ? 0.1445 0.1487 0.1608 -0.0086 -0.0032 0.0201  129 ALA   A O   
2691 O O   B ALA   A 129 ? 0.1373 0.1475 0.1296 0.0027  -0.0155 0.0140  129 ALA   A O   
2692 C CB  A ALA   A 129 ? 0.1458 0.1766 0.1981 0.0061  0.0109  0.0409  129 ALA   A CB  
2693 C CB  B ALA   A 129 ? 0.1370 0.1505 0.1310 -0.0051 -0.0249 0.0044  129 ALA   A CB  
2704 N N   A GLY   A 130 ? 0.1420 0.1463 0.1785 -0.0017 0.0075  0.0016  130 GLY   A N   
2705 N N   B GLY   A 130 ? 0.1488 0.1527 0.1261 0.0023  -0.0186 0.0211  130 GLY   A N   
2706 C CA  A GLY   A 130 ? 0.1584 0.1472 0.1928 0.0038  0.0112  -0.0069 130 GLY   A CA  
2707 C CA  B GLY   A 130 ? 0.1525 0.1550 0.1341 0.0068  -0.0164 0.0187  130 GLY   A CA  
2708 C C   A GLY   A 130 ? 0.1582 0.1344 0.1813 0.0106  0.0035  -0.0026 130 GLY   A C   
2709 C C   B GLY   A 130 ? 0.1552 0.1528 0.1345 0.0097  -0.0155 0.0177  130 GLY   A C   
2710 O O   A GLY   A 130 ? 0.1615 0.1360 0.1819 0.0040  -0.0056 0.0010  130 GLY   A O   
2711 O O   B GLY   A 130 ? 0.1583 0.1536 0.1358 0.0164  -0.0163 0.0195  130 GLY   A O   
2718 N N   A ILE   A 131 ? 0.1684 0.1385 0.1640 -0.0012 -0.0049 0.0070  131 ILE   A N   
2719 N N   B ILE   A 131 ? 0.1561 0.1545 0.1342 0.0029  -0.0113 0.0155  131 ILE   A N   
2720 C CA  A ILE   A 131 ? 0.1830 0.1440 0.1583 -0.0100 -0.0204 0.0038  131 ILE   A CA  
2721 C CA  B ILE   A 131 ? 0.1570 0.1548 0.1349 -0.0007 -0.0092 0.0180  131 ILE   A CA  
2722 C C   A ILE   A 131 ? 0.1699 0.1457 0.1473 -0.0149 -0.0175 0.0185  131 ILE   A C   
2723 C C   B ILE   A 131 ? 0.1584 0.1570 0.1380 0.0006  -0.0036 0.0215  131 ILE   A C   
2724 O O   A ILE   A 131 ? 0.1808 0.1491 0.1655 -0.0112 -0.0155 0.0198  131 ILE   A O   
2725 O O   B ILE   A 131 ? 0.1592 0.1600 0.1365 0.0004  0.0055  0.0237  131 ILE   A O   
2726 C CB  A ILE   A 131 ? 0.2093 0.1549 0.1598 -0.0178 -0.0229 -0.0093 131 ILE   A CB  
2727 C CB  B ILE   A 131 ? 0.1599 0.1525 0.1417 -0.0030 -0.0089 0.0095  131 ILE   A CB  
2728 C CG1 A ILE   A 131 ? 0.2242 0.1864 0.1712 -0.0250 -0.0330 -0.0196 131 ILE   A CG1 
2729 C CG1 B ILE   A 131 ? 0.1595 0.1521 0.1408 -0.0034 -0.0083 -0.0002 131 ILE   A CG1 
2730 C CG2 A ILE   A 131 ? 0.2260 0.1440 0.1935 -0.0101 0.0010  -0.0267 131 ILE   A CG2 
2731 C CG2 B ILE   A 131 ? 0.1655 0.1519 0.1449 -0.0054 -0.0003 0.0094  131 ILE   A CG2 
2732 C CD1 A ILE   A 131 ? 0.2313 0.1994 0.2160 -0.0305 -0.0286 -0.0263 131 ILE   A CD1 
2733 C CD1 B ILE   A 131 ? 0.1605 0.1498 0.1457 -0.0027 -0.0050 -0.0111 131 ILE   A CD1 
2756 N N   A PHE   A 132 ? 0.1625 0.1416 0.1430 -0.0033 -0.0172 0.0200  132 PHE   A N   
2757 N N   B PHE   A 132 ? 0.1595 0.1554 0.1403 0.0021  -0.0083 0.0186  132 PHE   A N   
2758 C CA  A PHE   A 132 ? 0.1637 0.1488 0.1404 -0.0025 -0.0072 0.0125  132 PHE   A CA  
2759 C CA  B PHE   A 132 ? 0.1603 0.1541 0.1471 0.0015  -0.0132 0.0204  132 PHE   A CA  
2760 C C   A PHE   A 132 ? 0.1695 0.1609 0.1480 0.0039  -0.0009 0.0126  132 PHE   A C   
2761 C C   B PHE   A 132 ? 0.1625 0.1590 0.1536 0.0052  -0.0128 0.0165  132 PHE   A C   
2762 O O   A PHE   A 132 ? 0.1812 0.1799 0.1464 -0.0043 -0.0005 0.0162  132 PHE   A O   
2763 O O   B PHE   A 132 ? 0.1662 0.1692 0.1533 0.0011  -0.0106 0.0221  132 PHE   A O   
2764 C CB  A PHE   A 132 ? 0.1648 0.1411 0.1383 -0.0017 -0.0092 0.0070  132 PHE   A CB  
2765 C CB  B PHE   A 132 ? 0.1593 0.1513 0.1394 -0.0040 -0.0102 0.0269  132 PHE   A CB  
2766 C CG  A PHE   A 132 ? 0.1663 0.1425 0.1267 0.0035  -0.0205 0.0101  132 PHE   A CG  
2767 C CG  B PHE   A 132 ? 0.1608 0.1531 0.1453 -0.0062 -0.0091 0.0235  132 PHE   A CG  
2768 C CD1 A PHE   A 132 ? 0.1684 0.1584 0.1423 0.0110  -0.0137 -0.0019 132 PHE   A CD1 
2769 C CD1 B PHE   A 132 ? 0.1617 0.1574 0.1484 -0.0043 -0.0051 0.0174  132 PHE   A CD1 
2770 C CD2 A PHE   A 132 ? 0.1703 0.1537 0.1518 0.0101  -0.0154 -0.0006 132 PHE   A CD2 
2771 C CD2 B PHE   A 132 ? 0.1619 0.1570 0.1568 -0.0064 -0.0121 0.0163  132 PHE   A CD2 
2772 C CE1 A PHE   A 132 ? 0.1687 0.1652 0.1590 0.0088  -0.0228 -0.0082 132 PHE   A CE1 
2773 C CE1 B PHE   A 132 ? 0.1641 0.1590 0.1584 -0.0047 -0.0085 0.0111  132 PHE   A CE1 
2774 C CE2 A PHE   A 132 ? 0.1657 0.1651 0.1560 0.0135  -0.0166 -0.0022 132 PHE   A CE2 
2775 C CE2 B PHE   A 132 ? 0.1616 0.1602 0.1651 -0.0056 -0.0117 0.0090  132 PHE   A CE2 
2776 C CZ  A PHE   A 132 ? 0.1630 0.1665 0.1567 0.0012  -0.0303 -0.0005 132 PHE   A CZ  
2777 C CZ  B PHE   A 132 ? 0.1628 0.1608 0.1660 -0.0065 -0.0142 0.0064  132 PHE   A CZ  
2796 N N   A GLY   A 133 ? 0.1745 0.1593 0.1373 0.0020  -0.0309 0.0061  133 GLY   A N   
2797 N N   B GLY   A 133 ? 0.1608 0.1551 0.1536 0.0073  -0.0136 0.0073  133 GLY   A N   
2798 C CA  A GLY   A 133 ? 0.1849 0.1736 0.1577 -0.0074 -0.0373 0.0009  133 GLY   A CA  
2799 C CA  B GLY   A 133 ? 0.1588 0.1546 0.1595 0.0085  -0.0165 0.0014  133 GLY   A CA  
2800 C C   A GLY   A 133 ? 0.1883 0.1835 0.1618 -0.0114 -0.0499 -0.0020 133 GLY   A C   
2801 C C   B GLY   A 133 ? 0.1576 0.1559 0.1646 0.0092  -0.0196 -0.0022 133 GLY   A C   
2802 O O   A GLY   A 133 ? 0.2019 0.2080 0.1791 -0.0167 -0.0530 -0.0204 133 GLY   A O   
2803 O O   B GLY   A 133 ? 0.1552 0.1611 0.1676 0.0120  -0.0147 -0.0052 133 GLY   A O   
2810 N N   A ALA   A 134 ? 0.1830 0.1699 0.1597 -0.0115 -0.0344 -0.0045 134 ALA   A N   
2811 N N   B ALA   A 134 ? 0.1587 0.1521 0.1667 0.0077  -0.0209 -0.0054 134 ALA   A N   
2812 C CA  A ALA   A 134 ? 0.1810 0.1730 0.1884 -0.0102 -0.0314 -0.0062 134 ALA   A CA  
2813 C CA  B ALA   A 134 ? 0.1592 0.1506 0.1720 0.0044  -0.0165 -0.0092 134 ALA   A CA  
2814 C C   A ALA   A 134 ? 0.1792 0.1829 0.1890 -0.0057 -0.0195 0.0118  134 ALA   A C   
2815 C C   B ALA   A 134 ? 0.1602 0.1521 0.1698 0.0040  -0.0131 -0.0094 134 ALA   A C   
2816 O O   A ALA   A 134 ? 0.1910 0.1904 0.2144 -0.0030 0.0071  0.0144  134 ALA   A O   
2817 O O   B ALA   A 134 ? 0.1637 0.1548 0.1820 0.0030  -0.0046 -0.0110 134 ALA   A O   
2818 C CB  A ALA   A 134 ? 0.1918 0.1740 0.2150 -0.0053 -0.0314 -0.0140 134 ALA   A CB  
2819 C CB  B ALA   A 134 ? 0.1606 0.1479 0.1769 0.0048  -0.0155 -0.0148 134 ALA   A CB  
2830 N N   A ASP   A 135 ? 0.1852 0.1908 0.2137 -0.0145 -0.0274 0.0277  135 ASP   A N   
2831 N N   B ASP   A 135 ? 0.1636 0.1539 0.1718 0.0005  -0.0159 -0.0051 135 ASP   A N   
2832 C CA  A ASP   A 135 ? 0.1813 0.2016 0.2400 -0.0246 -0.0393 0.0435  135 ASP   A CA  
2833 C CA  B ASP   A 135 ? 0.1631 0.1567 0.1757 -0.0015 -0.0151 -0.0005 135 ASP   A CA  
2834 C C   A ASP   A 135 ? 0.1714 0.1939 0.2452 -0.0154 -0.0291 0.0557  135 ASP   A C   
2835 C C   B ASP   A 135 ? 0.1629 0.1581 0.1790 0.0021  -0.0120 0.0032  135 ASP   A C   
2836 O O   A ASP   A 135 ? 0.1681 0.1753 0.2493 -0.0195 -0.0329 0.0572  135 ASP   A O   
2837 O O   B ASP   A 135 ? 0.1631 0.1562 0.1827 0.0021  -0.0144 0.0065  135 ASP   A O   
2838 C CB  A ASP   A 135 ? 0.2068 0.2343 0.2817 -0.0455 -0.0497 0.0285  135 ASP   A CB  
2839 C CB  B ASP   A 135 ? 0.1637 0.1608 0.1754 -0.0078 -0.0201 -0.0052 135 ASP   A CB  
2840 C CG  A ASP   A 135 ? 0.2258 0.2658 0.3254 -0.0595 -0.0561 0.0248  135 ASP   A CG  
2841 C CG  B ASP   A 135 ? 0.1628 0.1671 0.1776 -0.0105 -0.0258 -0.0109 135 ASP   A CG  
2842 O OD1 A ASP   A 135 ? 0.2167 0.2766 0.3173 -0.0618 -0.0715 0.0451  135 ASP   A OD1 
2843 O OD1 B ASP   A 135 ? 0.1631 0.1663 0.1874 -0.0103 -0.0242 -0.0175 135 ASP   A OD1 
2844 O OD2 A ASP   A 135 ? 0.2599 0.2874 0.3775 -0.0623 -0.0304 0.0238  135 ASP   A OD2 
2845 O OD2 B ASP   A 135 ? 0.1588 0.1697 0.1748 -0.0132 -0.0301 -0.0120 135 ASP   A OD2 
2854 N N   A PRO   A 136 ? 0.1575 0.2000 0.2438 0.0036  -0.0137 0.0726  136 PRO   A N   
2855 N N   B PRO   A 136 ? 0.1629 0.1619 0.1823 0.0062  -0.0078 0.0076  136 PRO   A N   
2856 C CA  A PRO   A 136 ? 0.1485 0.2044 0.2496 0.0012  -0.0024 0.0661  136 PRO   A CA  
2857 C CA  B PRO   A 136 ? 0.1635 0.1703 0.1838 0.0052  -0.0046 0.0084  136 PRO   A CA  
2858 C C   A PRO   A 136 ? 0.1275 0.1989 0.2485 0.0064  0.0006  0.0590  136 PRO   A C   
2859 C C   B PRO   A 136 ? 0.1635 0.1770 0.1817 0.0035  -0.0030 0.0081  136 PRO   A C   
2860 O O   A PRO   A 136 ? 0.1217 0.1942 0.2535 -0.0005 0.0026  0.0559  136 PRO   A O   
2861 O O   B PRO   A 136 ? 0.1631 0.1724 0.1753 0.0025  -0.0008 0.0032  136 PRO   A O   
2862 C CB  A PRO   A 136 ? 0.1753 0.2107 0.2714 0.0046  0.0046  0.0670  136 PRO   A CB  
2863 C CB  B PRO   A 136 ? 0.1677 0.1698 0.1915 0.0070  -0.0045 0.0091  136 PRO   A CB  
2864 C CG  A PRO   A 136 ? 0.1912 0.2234 0.2977 0.0112  0.0055  0.0525  136 PRO   A CG  
2865 C CG  B PRO   A 136 ? 0.1707 0.1697 0.1995 0.0088  -0.0047 0.0053  136 PRO   A CG  
2866 C CD  A PRO   A 136 ? 0.1735 0.2138 0.2631 0.0150  0.0057  0.0755  136 PRO   A CD  
2867 C CD  B PRO   A 136 ? 0.1651 0.1632 0.1935 0.0087  -0.0038 0.0115  136 PRO   A CD  
2882 N N   A ILE   A 137 ? 0.1290 0.1987 0.2546 0.0025  -0.0084 0.0638  137 ILE   A N   
2883 N N   B ILE   A 137 ? 0.1654 0.1834 0.1907 0.0015  -0.0051 0.0098  137 ILE   A N   
2884 C CA  A ILE   A 137 ? 0.1357 0.2074 0.2640 -0.0093 -0.0225 0.0600  137 ILE   A CA  
2885 C CA  B ILE   A 137 ? 0.1683 0.1915 0.1996 0.0016  -0.0076 0.0126  137 ILE   A CA  
2886 C C   A ILE   A 137 ? 0.1359 0.1991 0.2511 -0.0246 -0.0254 0.0500  137 ILE   A C   
2887 C C   B ILE   A 137 ? 0.1651 0.1940 0.1969 -0.0034 -0.0049 0.0146  137 ILE   A C   
2888 O O   A ILE   A 137 ? 0.1449 0.1899 0.2591 -0.0269 -0.0258 0.0440  137 ILE   A O   
2889 O O   B ILE   A 137 ? 0.1652 0.1945 0.1959 -0.0046 -0.0038 0.0146  137 ILE   A O   
2890 C CB  A ILE   A 137 ? 0.1416 0.2328 0.2897 -0.0124 -0.0386 0.0524  137 ILE   A CB  
2891 C CB  B ILE   A 137 ? 0.1744 0.1971 0.2142 0.0044  -0.0146 0.0122  137 ILE   A CB  
2892 C CG1 A ILE   A 137 ? 0.1533 0.2597 0.3182 -0.0017 -0.0307 0.0564  137 ILE   A CG1 
2893 C CG1 B ILE   A 137 ? 0.1780 0.2030 0.2205 0.0105  -0.0200 0.0164  137 ILE   A CG1 
2894 C CG2 A ILE   A 137 ? 0.1542 0.2337 0.3003 -0.0188 -0.0473 0.0386  137 ILE   A CG2 
2895 C CG2 B ILE   A 137 ? 0.1793 0.1981 0.2187 0.0037  -0.0150 0.0074  137 ILE   A CG2 
2896 C CD1 A ILE   A 137 ? 0.1710 0.2788 0.3407 0.0032  -0.0279 0.0555  137 ILE   A CD1 
2897 C CD1 B ILE   A 137 ? 0.1812 0.2067 0.2265 0.0119  -0.0228 0.0210  137 ILE   A CD1 
2920 N N   A HIS   A 138 ? 0.1326 0.2101 0.2414 -0.0202 -0.0122 0.0346  138 HIS   A N   
2921 N N   B HIS   A 138 ? 0.1615 0.1957 0.1989 -0.0057 -0.0003 0.0139  138 HIS   A N   
2922 C CA  A HIS   A 138 ? 0.1430 0.2086 0.2202 -0.0205 -0.0095 0.0357  138 HIS   A CA  
2923 C CA  B HIS   A 138 ? 0.1580 0.1935 0.1975 -0.0074 0.0002  0.0198  138 HIS   A CA  
2924 C C   A HIS   A 138 ? 0.1368 0.1957 0.2166 -0.0124 -0.0108 0.0461  138 HIS   A C   
2925 C C   B HIS   A 138 ? 0.1455 0.1882 0.2009 -0.0077 -0.0007 0.0341  138 HIS   A C   
2926 O O   A HIS   A 138 ? 0.1529 0.1923 0.2208 -0.0141 -0.0036 0.0378  138 HIS   A O   
2927 O O   B HIS   A 138 ? 0.1491 0.1897 0.1972 -0.0072 0.0030  0.0302  138 HIS   A O   
2928 C CB  A HIS   A 138 ? 0.1604 0.2227 0.2149 -0.0225 -0.0204 0.0200  138 HIS   A CB  
2929 C CB  B HIS   A 138 ? 0.1659 0.1972 0.2000 -0.0065 -0.0021 0.0104  138 HIS   A CB  
2930 C CG  A HIS   A 138 ? 0.1822 0.2335 0.2232 -0.0245 -0.0217 0.0047  138 HIS   A CG  
2931 C CG  B HIS   A 138 ? 0.1738 0.2010 0.2075 -0.0056 -0.0029 0.0010  138 HIS   A CG  
2932 N ND1 A HIS   A 138 ? 0.1923 0.2487 0.2549 -0.0292 -0.0246 -0.0102 138 HIS   A ND1 
2933 N ND1 B HIS   A 138 ? 0.1782 0.2061 0.2165 -0.0058 -0.0028 -0.0048 138 HIS   A ND1 
2934 C CD2 A HIS   A 138 ? 0.1845 0.2330 0.2296 -0.0147 -0.0254 0.0163  138 HIS   A CD2 
2935 C CD2 B HIS   A 138 ? 0.1746 0.2000 0.2122 -0.0032 -0.0052 0.0009  138 HIS   A CD2 
2936 C CE1 A HIS   A 138 ? 0.1970 0.2540 0.2529 -0.0153 -0.0304 -0.0045 138 HIS   A CE1 
2937 C CE1 B HIS   A 138 ? 0.1792 0.2059 0.2166 -0.0039 -0.0057 -0.0041 138 HIS   A CE1 
2938 N NE2 A HIS   A 138 ? 0.1924 0.2466 0.2354 -0.0124 -0.0233 0.0076  138 HIS   A NE2 
2939 N NE2 B HIS   A 138 ? 0.1769 0.2031 0.2149 -0.0035 -0.0058 -0.0017 138 HIS   A NE2 
2954 N N   . SER   A 139 ? 0.1324 0.1815 0.2141 -0.0097 -0.0029 0.0521  139 SER   A N   
2955 C CA  . SER   A 139 ? 0.1277 0.1715 0.2188 -0.0098 -0.0069 0.0532  139 SER   A CA  
2956 C C   . SER   A 139 ? 0.1215 0.1647 0.2233 -0.0117 0.0006  0.0364  139 SER   A C   
2957 O O   . SER   A 139 ? 0.1195 0.1638 0.2201 -0.0160 0.0013  0.0452  139 SER   A O   
2958 C CB  . SER   A 139 ? 0.1316 0.1739 0.2202 -0.0141 -0.0083 0.0529  139 SER   A CB  
2959 O OG  . SER   A 139 ? 0.1367 0.1703 0.2126 -0.0188 -0.0158 0.0566  139 SER   A OG  
2966 N N   . LEU   A 140 ? 0.1187 0.1726 0.2111 -0.0060 -0.0004 0.0495  140 LEU   A N   
2967 C CA  . LEU   A 140 ? 0.1191 0.1694 0.2131 -0.0094 -0.0002 0.0565  140 LEU   A CA  
2968 C C   . LEU   A 140 ? 0.1152 0.1786 0.2102 -0.0154 0.0028  0.0482  140 LEU   A C   
2969 O O   . LEU   A 140 ? 0.1256 0.1716 0.2294 -0.0103 0.0002  0.0447  140 LEU   A O   
2970 C CB  . LEU   A 140 ? 0.1230 0.1749 0.2234 -0.0094 0.0029  0.0539  140 LEU   A CB  
2971 C CG  . LEU   A 140 ? 0.1226 0.1891 0.2167 -0.0178 0.0086  0.0622  140 LEU   A CG  
2972 C CD1 . LEU   A 140 ? 0.1322 0.1947 0.2134 -0.0147 0.0013  0.0602  140 LEU   A CD1 
2973 C CD2 . LEU   A 140 ? 0.1312 0.2072 0.2343 -0.0112 0.0144  0.0627  140 LEU   A CD2 
2985 N N   . ARG   A 141 ? 0.1233 0.1813 0.2121 -0.0168 -0.0049 0.0456  141 ARG   A N   
2986 C CA  . ARG   A 141 ? 0.1425 0.1885 0.2337 -0.0270 -0.0111 0.0252  141 ARG   A CA  
2987 C C   . ARG   A 141 ? 0.1419 0.1713 0.2149 -0.0170 -0.0108 0.0261  141 ARG   A C   
2988 O O   . ARG   A 141 ? 0.1358 0.1665 0.2270 -0.0180 0.0051  0.0230  141 ARG   A O   
2989 C CB  . ARG   A 141 ? 0.1523 0.2156 0.2690 -0.0288 -0.0245 0.0038  141 ARG   A CB  
2990 C CG  . ARG   A 141 ? 0.1867 0.2492 0.3088 -0.0294 -0.0168 -0.0049 141 ARG   A CG  
2991 C CD  . ARG   A 141 ? 0.2101 0.2657 0.3234 -0.0410 -0.0092 -0.0046 141 ARG   A CD  
2992 N NE  . ARG   A 141 ? 0.1982 0.2763 0.3283 -0.0486 -0.0135 0.0027  141 ARG   A NE  
2993 C CZ  . ARG   A 141 ? 0.2033 0.2962 0.3348 -0.0575 -0.0062 0.0057  141 ARG   A CZ  
2994 N NH1 . ARG   A 141 ? 0.1903 0.3032 0.3285 -0.0637 0.0100  -0.0081 141 ARG   A NH1 
2995 N NH2 . ARG   A 141 ? 0.2117 0.3114 0.3582 -0.0497 -0.0295 0.0107  141 ARG   A NH2 
3009 N N   . VAL   A 142 ? 0.1317 0.1637 0.2094 -0.0125 -0.0021 0.0204  142 VAL   A N   
3010 C CA  . VAL   A 142 ? 0.1337 0.1577 0.2157 -0.0166 0.0083  0.0151  142 VAL   A CA  
3011 C C   . VAL   A 142 ? 0.1182 0.1537 0.2113 -0.0189 0.0077  0.0195  142 VAL   A C   
3012 O O   . VAL   A 142 ? 0.1240 0.1543 0.2161 -0.0049 0.0025  0.0246  142 VAL   A O   
3013 C CB  . VAL   A 142 ? 0.1440 0.1681 0.2075 -0.0162 0.0066  0.0196  142 VAL   A CB  
3014 C CG1 . VAL   A 142 ? 0.1447 0.1608 0.1962 -0.0124 0.0137  0.0126  142 VAL   A CG1 
3015 C CG2 . VAL   A 142 ? 0.1551 0.1887 0.2136 -0.0078 0.0017  0.0240  142 VAL   A CG2 
3025 N N   . CYS   A 143 ? 0.1231 0.1518 0.1977 -0.0154 0.0015  0.0212  143 CYS   A N   
3026 C CA  . CYS   A 143 ? 0.1213 0.1465 0.2036 -0.0098 0.0088  0.0238  143 CYS   A CA  
3027 C C   . CYS   A 143 ? 0.1217 0.1460 0.2024 -0.0090 0.0050  0.0315  143 CYS   A C   
3028 O O   . CYS   A 143 ? 0.1241 0.1466 0.2032 -0.0094 0.0046  0.0305  143 CYS   A O   
3029 C CB  . CYS   A 143 ? 0.1363 0.1518 0.2150 -0.0084 0.0187  0.0370  143 CYS   A CB  
3030 S SG  . CYS   A 143 ? 0.1500 0.1586 0.1881 0.0050  0.0153  0.0231  143 CYS   A SG  
3036 N N   . VAL   A 144 ? 0.1195 0.1552 0.2286 -0.0078 0.0065  0.0450  144 VAL   A N   
3037 C CA  . VAL   A 144 ? 0.1261 0.1617 0.2607 -0.0106 0.0218  0.0394  144 VAL   A CA  
3038 C C   . VAL   A 144 ? 0.1319 0.1496 0.2563 -0.0229 -0.0066 0.0295  144 VAL   A C   
3039 O O   . VAL   A 144 ? 0.1495 0.1508 0.2604 -0.0093 -0.0101 0.0373  144 VAL   A O   
3040 C CB  . VAL   A 144 ? 0.1509 0.1914 0.3136 -0.0058 0.0313  0.0447  144 VAL   A CB  
3041 C CG1 . VAL   A 144 ? 0.1658 0.2039 0.3585 -0.0223 0.0069  0.0453  144 VAL   A CG1 
3042 C CG2 . VAL   A 144 ? 0.1359 0.1986 0.3142 -0.0047 0.0400  0.0632  144 VAL   A CG2 
3052 N N   . ASP   A 145 ? 0.1370 0.1493 0.2602 -0.0225 -0.0079 0.0203  145 ASP   A N   
3053 C CA  . ASP   A 145 ? 0.1494 0.1537 0.2635 -0.0218 -0.0076 0.0148  145 ASP   A CA  
3054 C C   . ASP   A 145 ? 0.1516 0.1484 0.2559 -0.0150 0.0013  -0.0019 145 ASP   A C   
3055 O O   . ASP   A 145 ? 0.1668 0.1587 0.2985 -0.0194 -0.0012 -0.0298 145 ASP   A O   
3056 C CB  . ASP   A 145 ? 0.1641 0.1758 0.2742 -0.0291 -0.0223 0.0167  145 ASP   A CB  
3057 C CG  . ASP   A 145 ? 0.1849 0.2176 0.2974 -0.0457 -0.0322 0.0268  145 ASP   A CG  
3058 O OD1 . ASP   A 145 ? 0.1785 0.2293 0.3179 -0.0565 -0.0216 0.0245  145 ASP   A OD1 
3059 O OD2 . ASP   A 145 ? 0.2041 0.2415 0.3017 -0.0559 -0.0497 0.0272  145 ASP   A OD2 
3064 N N   . THR   A 146 ? 0.1336 0.1397 0.2142 -0.0137 0.0045  0.0096  146 THR   A N   
3065 C CA  . THR   A 146 ? 0.1298 0.1370 0.2062 -0.0088 0.0002  0.0083  146 THR   A CA  
3066 C C   . THR   A 146 ? 0.1232 0.1302 0.2194 -0.0035 0.0093  0.0169  146 THR   A C   
3067 O O   . THR   A 146 ? 0.1356 0.1429 0.2230 0.0028  0.0045  0.0161  146 THR   A O   
3068 C CB  . THR   A 146 ? 0.1276 0.1413 0.2023 -0.0078 0.0068  0.0166  146 THR   A CB  
3069 O OG1 . THR   A 146 ? 0.1306 0.1540 0.2059 -0.0034 0.0025  0.0138  146 THR   A OG1 
3070 C CG2 . THR   A 146 ? 0.1297 0.1411 0.2201 -0.0049 0.0006  0.0168  146 THR   A CG2 
3078 N N   . VAL   A 147 ? 0.1197 0.1409 0.2086 -0.0004 0.0121  0.0217  147 VAL   A N   
3079 C CA  . VAL   A 147 ? 0.1178 0.1382 0.2093 -0.0056 0.0234  0.0233  147 VAL   A CA  
3080 C C   . VAL   A 147 ? 0.1239 0.1351 0.2170 -0.0107 0.0182  0.0269  147 VAL   A C   
3081 O O   . VAL   A 147 ? 0.1256 0.1411 0.2335 -0.0139 0.0152  0.0275  147 VAL   A O   
3082 C CB  . VAL   A 147 ? 0.1339 0.1381 0.2017 -0.0113 0.0227  0.0247  147 VAL   A CB  
3083 C CG1 . VAL   A 147 ? 0.1699 0.1439 0.1996 -0.0100 0.0233  0.0333  147 VAL   A CG1 
3084 C CG2 . VAL   A 147 ? 0.1423 0.1337 0.2007 -0.0094 0.0102  0.0281  147 VAL   A CG2 
3094 N N   . ARG   A 148 ? 0.1253 0.1352 0.2269 -0.0149 0.0147  0.0392  148 ARG   A N   
3095 C CA  . ARG   A 148 ? 0.1311 0.1379 0.2258 -0.0113 0.0011  0.0440  148 ARG   A CA  
3096 C C   . ARG   A 148 ? 0.1382 0.1365 0.2223 -0.0114 0.0086  0.0541  148 ARG   A C   
3097 O O   . ARG   A 148 ? 0.1748 0.1476 0.2369 -0.0203 0.0168  0.0489  148 ARG   A O   
3098 C CB  . ARG   A 148 ? 0.1364 0.1401 0.2382 -0.0023 0.0127  0.0392  148 ARG   A CB  
3099 C CG  . ARG   A 148 ? 0.1575 0.1400 0.2724 -0.0083 0.0321  0.0218  148 ARG   A CG  
3100 C CD  . ARG   A 148 ? 0.1783 0.1423 0.2865 -0.0056 0.0424  0.0439  148 ARG   A CD  
3101 N NE  . ARG   A 148 ? 0.1720 0.1459 0.2836 0.0124  0.0516  0.0565  148 ARG   A NE  
3102 C CZ  . ARG   A 148 ? 0.1666 0.1357 0.2699 0.0059  0.0458  0.0515  148 ARG   A CZ  
3103 N NH1 . ARG   A 148 ? 0.1764 0.1347 0.2845 -0.0063 0.0499  0.0263  148 ARG   A NH1 
3104 N NH2 . ARG   A 148 ? 0.1567 0.1554 0.2767 0.0127  0.0445  0.0550  148 ARG   A NH2 
3118 N N   . THR   A 149 ? 0.1378 0.1454 0.2068 -0.0141 0.0032  0.0417  149 THR   A N   
3119 C CA  . THR   A 149 ? 0.1468 0.1474 0.2091 -0.0124 0.0040  0.0450  149 THR   A CA  
3120 C C   . THR   A 149 ? 0.1439 0.1493 0.2049 -0.0165 0.0143  0.0548  149 THR   A C   
3121 O O   . THR   A 149 ? 0.1399 0.1618 0.2086 -0.0172 0.0109  0.0524  149 THR   A O   
3122 C CB  . THR   A 149 ? 0.1435 0.1641 0.2122 -0.0170 0.0044  0.0414  149 THR   A CB  
3123 O OG1 . THR   A 149 ? 0.1428 0.1571 0.2203 -0.0237 0.0090  0.0336  149 THR   A OG1 
3124 C CG2 . THR   A 149 ? 0.1474 0.1720 0.2289 -0.0046 -0.0025 0.0451  149 THR   A CG2 
3132 N N   . ASN   A 150 ? 0.1482 0.1471 0.2069 -0.0037 0.0043  0.0505  150 ASN   A N   
3133 C CA  . ASN   A 150 ? 0.1613 0.1594 0.2020 -0.0104 0.0158  0.0502  150 ASN   A CA  
3134 C C   . ASN   A 150 ? 0.1381 0.1536 0.2056 -0.0122 0.0092  0.0415  150 ASN   A C   
3135 O O   . ASN   A 150 ? 0.1468 0.1637 0.2484 -0.0146 -0.0105 0.0390  150 ASN   A O   
3136 C CB  . ASN   A 150 ? 0.2031 0.1917 0.2268 -0.0119 0.0393  0.0695  150 ASN   A CB  
3137 C CG  . ASN   A 150 ? 0.2589 0.2227 0.2918 -0.0090 0.0118  0.0811  150 ASN   A CG  
3138 O OD1 . ASN   A 150 ? 0.2868 0.2331 0.3068 -0.0151 0.0088  0.0996  150 ASN   A OD1 
3139 N ND2 . ASN   A 150 ? 0.2872 0.2469 0.3255 -0.0008 0.0005  0.0692  150 ASN   A ND2 
3146 N N   . VAL   A 151 ? 0.1391 0.1444 0.1994 -0.0174 0.0073  0.0444  151 VAL   A N   
3147 C CA  . VAL   A 151 ? 0.1471 0.1445 0.1966 -0.0206 0.0144  0.0483  151 VAL   A CA  
3148 C C   . VAL   A 151 ? 0.1419 0.1351 0.2127 -0.0248 0.0217  0.0508  151 VAL   A C   
3149 O O   . VAL   A 151 ? 0.1490 0.1436 0.2384 -0.0147 0.0200  0.0415  151 VAL   A O   
3150 C CB  . VAL   A 151 ? 0.1683 0.1667 0.1963 -0.0009 0.0167  0.0405  151 VAL   A CB  
3151 C CG1 . VAL   A 151 ? 0.1612 0.1902 0.2293 -0.0055 0.0046  0.0285  151 VAL   A CG1 
3152 C CG2 . VAL   A 151 ? 0.1768 0.1665 0.2043 -0.0016 0.0283  0.0422  151 VAL   A CG2 
3162 N N   . TYR   A 152 ? 0.1370 0.1399 0.2067 -0.0169 0.0187  0.0448  152 TYR   A N   
3163 C CA  . TYR   A 152 ? 0.1389 0.1447 0.1872 -0.0163 0.0169  0.0377  152 TYR   A CA  
3164 C C   . TYR   A 152 ? 0.1356 0.1448 0.1854 -0.0173 0.0228  0.0411  152 TYR   A C   
3165 O O   . TYR   A 152 ? 0.1433 0.1398 0.1845 -0.0235 0.0216  0.0321  152 TYR   A O   
3166 C CB  . TYR   A 152 ? 0.1544 0.1522 0.1910 -0.0062 0.0294  0.0395  152 TYR   A CB  
3167 C CG  . TYR   A 152 ? 0.1663 0.1712 0.1821 -0.0078 0.0338  0.0470  152 TYR   A CG  
3168 C CD1 . TYR   A 152 ? 0.1726 0.1941 0.1997 0.0025  0.0364  0.0555  152 TYR   A CD1 
3169 C CD2 . TYR   A 152 ? 0.1642 0.1816 0.1789 -0.0234 0.0289  0.0403  152 TYR   A CD2 
3170 C CE1 . TYR   A 152 ? 0.1934 0.2030 0.2185 0.0020  0.0130  0.0595  152 TYR   A CE1 
3171 C CE2 . TYR   A 152 ? 0.1828 0.1945 0.1935 -0.0317 0.0242  0.0404  152 TYR   A CE2 
3172 C CZ  . TYR   A 152 ? 0.2028 0.1952 0.1972 -0.0191 0.0146  0.0594  152 TYR   A CZ  
3173 O OH  . TYR   A 152 ? 0.2356 0.2162 0.2224 -0.0123 0.0203  0.0753  152 TYR   A OH  
3183 N N   . LEU   A 153 ? 0.1319 0.1425 0.1878 -0.0178 0.0211  0.0431  153 LEU   A N   
3184 C CA  . LEU   A 153 ? 0.1277 0.1417 0.2075 -0.0077 0.0238  0.0452  153 LEU   A CA  
3185 C C   . LEU   A 153 ? 0.1329 0.1493 0.2138 -0.0056 0.0338  0.0428  153 LEU   A C   
3186 O O   . LEU   A 153 ? 0.1364 0.1595 0.2376 -0.0052 0.0444  0.0463  153 LEU   A O   
3187 C CB  . LEU   A 153 ? 0.1250 0.1454 0.2188 -0.0061 0.0224  0.0417  153 LEU   A CB  
3188 C CG  . LEU   A 153 ? 0.1335 0.1471 0.2081 -0.0126 0.0263  0.0371  153 LEU   A CG  
3189 C CD1 . LEU   A 153 ? 0.1437 0.1498 0.2101 -0.0107 0.0075  0.0350  153 LEU   A CD1 
3190 C CD2 . LEU   A 153 ? 0.1445 0.1492 0.2120 -0.0099 0.0325  0.0133  153 LEU   A CD2 
3202 N N   A ALA   A 154 ? 0.1272 0.1413 0.2237 -0.0042 0.0304  0.0462  154 ALA   A N   
3203 N N   B ALA   A 154 ? 0.1402 0.1546 0.1955 -0.0050 0.0240  0.0383  154 ALA   A N   
3204 C CA  A ALA   A 154 ? 0.1441 0.1441 0.2439 -0.0016 0.0362  0.0416  154 ALA   A CA  
3205 C CA  B ALA   A 154 ? 0.1533 0.1623 0.1862 -0.0016 0.0181  0.0346  154 ALA   A CA  
3206 C C   A ALA   A 154 ? 0.1408 0.1448 0.2453 0.0077  0.0345  0.0548  154 ALA   A C   
3207 C C   B ALA   A 154 ? 0.1609 0.1699 0.1816 -0.0005 0.0123  0.0336  154 ALA   A C   
3208 O O   A ALA   A 154 ? 0.1465 0.1569 0.2488 0.0046  0.0406  0.0609  154 ALA   A O   
3209 O O   B ALA   A 154 ? 0.1632 0.1706 0.1817 -0.0019 0.0104  0.0389  154 ALA   A O   
3210 C CB  A ALA   A 154 ? 0.1617 0.1451 0.2513 0.0102  0.0303  0.0277  154 ALA   A CB  
3211 C CB  B ALA   A 154 ? 0.1581 0.1621 0.1826 0.0021  0.0155  0.0317  154 ALA   A CB  
3222 N N   A VAL   A 155 ? 0.1529 0.1482 0.2419 0.0094  0.0330  0.0744  155 VAL   A N   
3223 N N   B VAL   A 155 ? 0.1690 0.1783 0.1822 0.0009  0.0094  0.0286  155 VAL   A N   
3224 C CA  A VAL   A 155 ? 0.1572 0.1608 0.2598 0.0123  0.0319  0.0774  155 VAL   A CA  
3225 C CA  B VAL   A 155 ? 0.1758 0.1867 0.1834 0.0011  0.0095  0.0289  155 VAL   A CA  
3226 C C   A VAL   A 155 ? 0.1713 0.1726 0.2952 0.0177  0.0318  0.0827  155 VAL   A C   
3227 C C   B VAL   A 155 ? 0.1870 0.1998 0.1921 0.0057  0.0063  0.0276  155 VAL   A C   
3228 O O   A VAL   A 155 ? 0.1674 0.1722 0.2978 0.0271  0.0356  0.0682  155 VAL   A O   
3229 O O   B VAL   A 155 ? 0.1825 0.2002 0.1784 0.0114  -0.0007 0.0275  155 VAL   A O   
3230 C CB  A VAL   A 155 ? 0.1613 0.1696 0.2460 0.0143  0.0243  0.0665  155 VAL   A CB  
3231 C CB  B VAL   A 155 ? 0.1750 0.1857 0.1835 -0.0014 0.0063  0.0252  155 VAL   A CB  
3232 C CG1 A VAL   A 155 ? 0.1779 0.1826 0.2566 0.0138  0.0087  0.0649  155 VAL   A CG1 
3233 C CG1 B VAL   A 155 ? 0.1799 0.1884 0.1872 0.0005  0.0035  0.0235  155 VAL   A CG1 
3234 C CG2 A VAL   A 155 ? 0.1706 0.1827 0.2535 0.0255  0.0172  0.0564  155 VAL   A CG2 
3235 C CG2 B VAL   A 155 ? 0.1721 0.1873 0.1835 -0.0045 0.0066  0.0238  155 VAL   A CG2 
3254 N N   A PHE   A 156 ? 0.1839 0.1766 0.3238 0.0197  0.0326  0.1048  156 PHE   A N   
3255 N N   B PHE   A 156 ? 0.2011 0.2110 0.2159 0.0049  0.0081  0.0283  156 PHE   A N   
3256 C CA  A PHE   A 156 ? 0.2103 0.1795 0.3586 0.0279  0.0352  0.1027  156 PHE   A CA  
3257 C CA  B PHE   A 156 ? 0.2156 0.2205 0.2339 0.0037  0.0100  0.0243  156 PHE   A CA  
3258 C C   A PHE   A 156 ? 0.2115 0.1838 0.3712 0.0400  0.0442  0.1027  156 PHE   A C   
3259 C C   B PHE   A 156 ? 0.2286 0.2312 0.2461 0.0056  0.0134  0.0257  156 PHE   A C   
3260 O O   A PHE   A 156 ? 0.2179 0.1964 0.3939 0.0387  0.0496  0.0807  156 PHE   A O   
3261 O O   B PHE   A 156 ? 0.2297 0.2323 0.2467 0.0060  0.0166  0.0241  156 PHE   A O   
3262 C CB  A PHE   A 156 ? 0.2445 0.1813 0.3596 0.0183  0.0180  0.1202  156 PHE   A CB  
3263 C CB  B PHE   A 156 ? 0.2171 0.2196 0.2385 0.0006  0.0061  0.0176  156 PHE   A CB  
3264 C CG  A PHE   A 156 ? 0.2856 0.1939 0.3794 0.0293  -0.0039 0.1093  156 PHE   A CG  
3265 C CG  B PHE   A 156 ? 0.2197 0.2211 0.2440 0.0005  0.0016  0.0103  156 PHE   A CG  
3266 C CD1 A PHE   A 156 ? 0.3028 0.2069 0.3895 0.0391  -0.0088 0.0851  156 PHE   A CD1 
3267 C CD1 B PHE   A 156 ? 0.2180 0.2221 0.2439 0.0012  -0.0006 0.0084  156 PHE   A CD1 
3268 C CD2 A PHE   A 156 ? 0.3099 0.1997 0.3828 0.0374  -0.0136 0.1229  156 PHE   A CD2 
3269 C CD2 B PHE   A 156 ? 0.2231 0.2231 0.2502 0.0001  -0.0006 0.0082  156 PHE   A CD2 
3270 C CE1 A PHE   A 156 ? 0.3176 0.2140 0.4067 0.0449  -0.0052 0.0769  156 PHE   A CE1 
3271 C CE1 B PHE   A 156 ? 0.2167 0.2232 0.2444 0.0025  -0.0016 0.0050  156 PHE   A CE1 
3272 C CE2 A PHE   A 156 ? 0.3266 0.2121 0.3949 0.0463  -0.0160 0.1025  156 PHE   A CE2 
3273 C CE2 B PHE   A 156 ? 0.2235 0.2243 0.2512 0.0002  -0.0033 0.0047  156 PHE   A CE2 
3274 C CZ  A PHE   A 156 ? 0.3264 0.2161 0.4101 0.0510  -0.0094 0.0741  156 PHE   A CZ  
3275 C CZ  B PHE   A 156 ? 0.2185 0.2231 0.2491 0.0012  -0.0036 0.0030  156 PHE   A CZ  
3294 N N   A ASP   A 157 ? 0.2134 0.1880 0.3469 0.0413  0.0418  0.1243  157 ASP   A N   
3295 N N   B ASP   A 157 ? 0.2417 0.2424 0.2514 0.0058  0.0087  0.0293  157 ASP   A N   
3296 C CA  A ASP   A 157 ? 0.2242 0.2164 0.3511 0.0434  0.0280  0.1336  157 ASP   A CA  
3297 C CA  B ASP   A 157 ? 0.2571 0.2557 0.2597 0.0070  0.0031  0.0307  157 ASP   A CA  
3298 C C   A ASP   A 157 ? 0.2056 0.2301 0.3564 0.0551  0.0441  0.1384  157 ASP   A C   
3299 C C   B ASP   A 157 ? 0.2614 0.2666 0.2648 0.0090  0.0062  0.0293  157 ASP   A C   
3300 O O   A ASP   A 157 ? 0.1897 0.2169 0.3500 0.0561  0.0482  0.1394  157 ASP   A O   
3301 O O   B ASP   A 157 ? 0.2594 0.2667 0.2612 0.0095  0.0055  0.0283  157 ASP   A O   
3302 C CB  A ASP   A 157 ? 0.2502 0.2302 0.3700 0.0470  0.0022  0.1239  157 ASP   A CB  
3303 C CB  B ASP   A 157 ? 0.2678 0.2576 0.2674 0.0077  -0.0044 0.0313  157 ASP   A CB  
3304 C CG  A ASP   A 157 ? 0.2832 0.2405 0.3973 0.0499  -0.0243 0.1141  157 ASP   A CG  
3305 C CG  B ASP   A 157 ? 0.2787 0.2582 0.2743 0.0106  -0.0132 0.0326  157 ASP   A CG  
3306 O OD1 A ASP   A 157 ? 0.3318 0.2522 0.4366 0.0436  -0.0492 0.0956  157 ASP   A OD1 
3307 O OD1 B ASP   A 157 ? 0.2797 0.2547 0.2729 0.0128  -0.0142 0.0378  157 ASP   A OD1 
3308 O OD2 A ASP   A 157 ? 0.2624 0.2397 0.4130 0.0450  -0.0197 0.1320  157 ASP   A OD2 
3309 O OD2 B ASP   A 157 ? 0.2868 0.2613 0.2818 0.0091  -0.0213 0.0302  157 ASP   A OD2 
3318 N N   A LYS   A 158 ? 0.2123 0.2549 0.3851 0.0607  0.0613  0.1262  158 LYS   A N   
3319 N N   B LYS   A 158 ? 0.2680 0.2765 0.2788 0.0095  0.0098  0.0257  158 LYS   A N   
3320 C CA  A LYS   A 158 ? 0.2099 0.2839 0.3949 0.0669  0.0753  0.1216  158 LYS   A CA  
3321 C CA  B LYS   A 158 ? 0.2728 0.2865 0.2920 0.0092  0.0127  0.0225  158 LYS   A CA  
3322 C C   A LYS   A 158 ? 0.1848 0.2964 0.3771 0.0711  0.0670  0.1514  158 LYS   A C   
3323 C C   B LYS   A 158 ? 0.2719 0.2894 0.2919 0.0093  0.0117  0.0279  158 LYS   A C   
3324 O O   A LYS   A 158 ? 0.1794 0.2971 0.3782 0.0603  0.0684  0.1601  158 LYS   A O   
3325 O O   B LYS   A 158 ? 0.2739 0.2917 0.2906 0.0081  0.0114  0.0290  158 LYS   A O   
3326 C CB  A LYS   A 158 ? 0.2335 0.2953 0.4204 0.0709  0.0959  0.1156  158 LYS   A CB  
3327 C CB  B LYS   A 158 ? 0.2786 0.2924 0.3067 0.0084  0.0176  0.0147  158 LYS   A CB  
3328 C CG  A LYS   A 158 ? 0.2563 0.3094 0.4487 0.0735  0.1200  0.1053  158 LYS   A CG  
3329 C CG  B LYS   A 158 ? 0.2841 0.2976 0.3214 0.0076  0.0227  0.0059  158 LYS   A CG  
3330 C CD  A LYS   A 158 ? 0.2722 0.3222 0.4650 0.0659  0.1428  0.1116  158 LYS   A CD  
3331 C CD  B LYS   A 158 ? 0.2881 0.3015 0.3316 0.0065  0.0271  0.0013  158 LYS   A CD  
3332 C CE  A LYS   A 158 ? 0.2799 0.3304 0.4783 0.0571  0.1580  0.1181  158 LYS   A CE  
3333 C CE  B LYS   A 158 ? 0.2891 0.3032 0.3398 0.0062  0.0292  -0.0003 158 LYS   A CE  
3334 N NZ  A LYS   A 158 ? 0.2814 0.3341 0.4797 0.0506  0.1707  0.1269  158 LYS   A NZ  
3335 N NZ  B LYS   A 158 ? 0.2898 0.3047 0.3426 0.0055  0.0310  -0.0021 158 LYS   A NZ  
3362 N N   A ASN   A 159 ? 0.1817 0.3138 0.3932 0.0772  0.0461  0.1482  159 ASN   A N   
3363 N N   B ASN   A 159 ? 0.2693 0.2888 0.2973 0.0091  0.0103  0.0278  159 ASN   A N   
3364 C CA  A ASN   A 159 ? 0.1816 0.3257 0.3896 0.0698  0.0197  0.1648  159 ASN   A CA  
3365 C CA  B ASN   A 159 ? 0.2666 0.2864 0.3003 0.0064  0.0080  0.0281  159 ASN   A CA  
3366 C C   A ASN   A 159 ? 0.1644 0.3237 0.3594 0.0469  0.0160  0.1534  159 ASN   A C   
3367 C C   B ASN   A 159 ? 0.2574 0.2778 0.2789 0.0016  0.0085  0.0295  159 ASN   A C   
3368 O O   A ASN   A 159 ? 0.1515 0.3292 0.3507 0.0482  -0.0036 0.1319  159 ASN   A O   
3369 O O   B ASN   A 159 ? 0.2583 0.2774 0.2770 0.0020  0.0094  0.0283  159 ASN   A O   
3370 C CB  A ASN   A 159 ? 0.2080 0.3394 0.4377 0.0734  0.0130  0.1752  159 ASN   A CB  
3371 C CB  B ASN   A 159 ? 0.2728 0.2921 0.3235 0.0073  0.0070  0.0268  159 ASN   A CB  
3372 C CG  A ASN   A 159 ? 0.2394 0.3572 0.4918 0.0636  0.0208  0.1683  159 ASN   A CG  
3373 C CG  B ASN   A 159 ? 0.2801 0.2964 0.3457 0.0076  0.0051  0.0244  159 ASN   A CG  
3374 O OD1 A ASN   A 159 ? 0.2457 0.3700 0.5146 0.0575  0.0354  0.1624  159 ASN   A OD1 
3375 O OD1 B ASN   A 159 ? 0.2820 0.2965 0.3544 0.0084  0.0043  0.0249  159 ASN   A OD1 
3376 N ND2 A ASN   A 159 ? 0.2626 0.3644 0.5182 0.0586  0.0224  0.1608  159 ASN   A ND2 
3377 N ND2 B ASN   A 159 ? 0.2844 0.3007 0.3557 0.0080  0.0055  0.0221  159 ASN   A ND2 
3390 N N   A LEU   A 160 ? 0.1551 0.3059 0.3422 0.0340  0.0054  0.1604  160 LEU   A N   
3391 N N   B LEU   A 160 ? 0.2457 0.2680 0.2635 -0.0035 0.0073  0.0297  160 LEU   A N   
3392 C CA  A LEU   A 160 ? 0.1528 0.2863 0.3215 0.0205  0.0137  0.1536  160 LEU   A CA  
3393 C CA  B LEU   A 160 ? 0.2351 0.2575 0.2450 -0.0078 0.0079  0.0312  160 LEU   A CA  
3394 C C   A LEU   A 160 ? 0.1395 0.2801 0.3023 0.0137  0.0212  0.1438  160 LEU   A C   
3395 C C   B LEU   A 160 ? 0.2260 0.2527 0.2342 -0.0076 0.0051  0.0324  160 LEU   A C   
3396 O O   A LEU   A 160 ? 0.1381 0.2949 0.3141 0.0122  0.0255  0.1366  160 LEU   A O   
3397 O O   B LEU   A 160 ? 0.2249 0.2560 0.2336 -0.0073 0.0036  0.0354  160 LEU   A O   
3398 C CB  A LEU   A 160 ? 0.1619 0.2766 0.3088 0.0068  0.0191  0.1467  160 LEU   A CB  
3399 C CB  B LEU   A 160 ? 0.2317 0.2524 0.2394 -0.0103 0.0082  0.0308  160 LEU   A CB  
3400 C CG  A LEU   A 160 ? 0.1721 0.2796 0.3102 -0.0121 0.0247  0.1183  160 LEU   A CG  
3401 C CG  B LEU   A 160 ? 0.2288 0.2483 0.2357 -0.0119 0.0072  0.0282  160 LEU   A CG  
3402 C CD1 A LEU   A 160 ? 0.1886 0.2880 0.3117 -0.0171 0.0248  0.1010  160 LEU   A CD1 
3403 C CD1 B LEU   A 160 ? 0.2286 0.2471 0.2350 -0.0120 0.0050  0.0261  160 LEU   A CD1 
3404 C CD2 A LEU   A 160 ? 0.1769 0.2786 0.3118 -0.0155 0.0329  0.1072  160 LEU   A CD2 
3405 C CD2 B LEU   A 160 ? 0.2267 0.2470 0.2354 -0.0112 0.0075  0.0264  160 LEU   A CD2 
3428 N N   A TYR   A 161 ? 0.1389 0.2578 0.2901 0.0145  0.0277  0.1343  161 TYR   A N   
3429 N N   B TYR   A 161 ? 0.2196 0.2440 0.2269 -0.0076 0.0039  0.0293  161 TYR   A N   
3430 C CA  A TYR   A 161 ? 0.1373 0.2428 0.2913 0.0146  0.0280  0.1315  161 TYR   A CA  
3431 C CA  B TYR   A 161 ? 0.2132 0.2376 0.2228 -0.0082 0.0054  0.0313  161 TYR   A CA  
3432 C C   A TYR   A 161 ? 0.1315 0.2557 0.3040 0.0077  0.0212  0.1288  161 TYR   A C   
3433 C C   B TYR   A 161 ? 0.2142 0.2432 0.2266 -0.0092 0.0050  0.0334  161 TYR   A C   
3434 O O   A TYR   A 161 ? 0.1259 0.2588 0.3173 0.0031  0.0223  0.1231  161 TYR   A O   
3435 O O   B TYR   A 161 ? 0.2112 0.2433 0.2233 -0.0104 0.0063  0.0345  161 TYR   A O   
3436 C CB  A TYR   A 161 ? 0.1509 0.2273 0.2942 0.0161  0.0357  0.1035  161 TYR   A CB  
3437 C CB  B TYR   A 161 ? 0.2080 0.2269 0.2176 -0.0082 0.0060  0.0291  161 TYR   A CB  
3438 C CG  A TYR   A 161 ? 0.1510 0.2187 0.2972 0.0166  0.0316  0.0868  161 TYR   A CG  
3439 C CG  B TYR   A 161 ? 0.2019 0.2183 0.2131 -0.0077 0.0055  0.0266  161 TYR   A CG  
3440 C CD1 A TYR   A 161 ? 0.1458 0.2098 0.3035 0.0133  0.0307  0.0809  161 TYR   A CD1 
3441 C CD1 B TYR   A 161 ? 0.1985 0.2136 0.2114 -0.0072 0.0043  0.0254  161 TYR   A CD1 
3442 C CD2 A TYR   A 161 ? 0.1512 0.2257 0.2922 0.0183  0.0259  0.0821  161 TYR   A CD2 
3443 C CD2 B TYR   A 161 ? 0.1990 0.2171 0.2110 -0.0074 0.0048  0.0247  161 TYR   A CD2 
3444 C CE1 A TYR   A 161 ? 0.1525 0.2040 0.2987 0.0125  0.0212  0.0787  161 TYR   A CE1 
3445 C CE1 B TYR   A 161 ? 0.1971 0.2116 0.2100 -0.0063 0.0030  0.0249  161 TYR   A CE1 
3446 C CE2 A TYR   A 161 ? 0.1578 0.2183 0.2939 0.0124  0.0300  0.0903  161 TYR   A CE2 
3447 C CE2 B TYR   A 161 ? 0.1981 0.2141 0.2110 -0.0069 0.0049  0.0253  161 TYR   A CE2 
3448 C CZ  A TYR   A 161 ? 0.1637 0.2077 0.2977 0.0055  0.0227  0.0922  161 TYR   A CZ  
3449 C CZ  B TYR   A 161 ? 0.1977 0.2120 0.2121 -0.0064 0.0041  0.0272  161 TYR   A CZ  
3450 O OH  A TYR   A 161 ? 0.1826 0.2108 0.3151 -0.0058 0.0175  0.0925  161 TYR   A OH  
3451 O OH  B TYR   A 161 ? 0.1995 0.2128 0.2190 -0.0063 0.0044  0.0305  161 TYR   A OH  
3470 N N   A ASP   A 162 ? 0.1292 0.2693 0.3234 0.0137  0.0270  0.1287  162 ASP   A N   
3471 N N   B ASP   A 162 ? 0.2192 0.2491 0.2399 -0.0078 0.0056  0.0336  162 ASP   A N   
3472 C CA  A ASP   A 162 ? 0.1303 0.3002 0.3249 0.0079  0.0321  0.1211  162 ASP   A CA  
3473 C CA  B ASP   A 162 ? 0.2243 0.2584 0.2507 -0.0091 0.0066  0.0354  162 ASP   A CA  
3474 C C   A ASP   A 162 ? 0.1224 0.3104 0.3196 -0.0020 0.0312  0.1354  162 ASP   A C   
3475 C C   B ASP   A 162 ? 0.2299 0.2656 0.2538 -0.0113 0.0060  0.0382  162 ASP   A C   
3476 O O   A ASP   A 162 ? 0.1277 0.3103 0.3522 -0.0042 0.0332  0.1337  162 ASP   A O   
3477 O O   B ASP   A 162 ? 0.2282 0.2632 0.2541 -0.0141 0.0055  0.0391  162 ASP   A O   
3478 C CB  A ASP   A 162 ? 0.1471 0.3167 0.3362 0.0147  0.0440  0.1079  162 ASP   A CB  
3479 C CB  B ASP   A 162 ? 0.2243 0.2613 0.2600 -0.0074 0.0081  0.0336  162 ASP   A CB  
3480 C CG  A ASP   A 162 ? 0.1639 0.3375 0.3587 0.0208  0.0620  0.0896  162 ASP   A CG  
3481 C CG  B ASP   A 162 ? 0.2258 0.2657 0.2702 -0.0052 0.0111  0.0306  162 ASP   A CG  
3482 O OD1 A ASP   A 162 ? 0.1727 0.3528 0.3731 0.0108  0.0550  0.0788  162 ASP   A OD1 
3483 O OD1 B ASP   A 162 ? 0.2252 0.2683 0.2763 -0.0050 0.0100  0.0281  162 ASP   A OD1 
3484 O OD2 A ASP   A 162 ? 0.1807 0.3396 0.3837 0.0366  0.0680  0.0707  162 ASP   A OD2 
3485 O OD2 B ASP   A 162 ? 0.2285 0.2662 0.2744 -0.0034 0.0153  0.0308  162 ASP   A OD2 
3494 N N   A LYS   A 163 ? 0.1407 0.3338 0.3255 -0.0048 -0.0015 0.1332  163 LYS   A N   
3495 N N   B LYS   A 163 ? 0.2388 0.2751 0.2632 -0.0109 0.0041  0.0374  163 LYS   A N   
3496 C CA  A LYS   A 163 ? 0.1526 0.3497 0.3110 -0.0079 -0.0070 0.1267  163 LYS   A CA  
3497 C CA  B LYS   A 163 ? 0.2447 0.2816 0.2703 -0.0104 0.0052  0.0339  163 LYS   A CA  
3498 C C   A LYS   A 163 ? 0.1462 0.3385 0.3044 -0.0144 0.0037  0.1172  163 LYS   A C   
3499 C C   B LYS   A 163 ? 0.2354 0.2748 0.2503 -0.0101 0.0076  0.0341  163 LYS   A C   
3500 O O   A LYS   A 163 ? 0.1384 0.3531 0.3314 -0.0246 0.0028  0.1015  163 LYS   A O   
3501 O O   B LYS   A 163 ? 0.2357 0.2793 0.2512 -0.0101 0.0059  0.0354  163 LYS   A O   
3502 C CB  A LYS   A 163 ? 0.1909 0.3765 0.3405 0.0105  -0.0270 0.1166  163 LYS   A CB  
3503 C CB  B LYS   A 163 ? 0.2593 0.2926 0.3015 -0.0086 0.0039  0.0283  163 LYS   A CB  
3504 C CG  A LYS   A 163 ? 0.2366 0.4019 0.3938 0.0132  -0.0237 0.1045  163 LYS   A CG  
3505 C CG  B LYS   A 163 ? 0.2724 0.3023 0.3365 -0.0092 0.0050  0.0234  163 LYS   A CG  
3506 C CD  A LYS   A 163 ? 0.2820 0.4225 0.4506 0.0148  -0.0203 0.0946  163 LYS   A CD  
3507 C CD  B LYS   A 163 ? 0.2836 0.3112 0.3685 -0.0099 0.0056  0.0199  163 LYS   A CD  
3508 C CE  A LYS   A 163 ? 0.3082 0.4366 0.4993 0.0142  -0.0162 0.0870  163 LYS   A CE  
3509 C CE  B LYS   A 163 ? 0.2924 0.3184 0.3936 -0.0110 0.0064  0.0183  163 LYS   A CE  
3510 N NZ  A LYS   A 163 ? 0.3354 0.4458 0.5261 0.0127  -0.0182 0.0840  163 LYS   A NZ  
3511 N NZ  B LYS   A 163 ? 0.2980 0.3228 0.4078 -0.0111 0.0068  0.0172  163 LYS   A NZ  
3538 N N   A LEU   A 164 ? 0.1297 0.3071 0.2855 -0.0250 -0.0001 0.1126  164 LEU   A N   
3539 N N   B LEU   A 164 ? 0.2239 0.2612 0.2339 -0.0113 0.0076  0.0312  164 LEU   A N   
3540 C CA  A LEU   A 164 ? 0.1316 0.2843 0.2779 -0.0314 0.0076  0.1016  164 LEU   A CA  
3541 C CA  B LEU   A 164 ? 0.2146 0.2497 0.2225 -0.0111 0.0082  0.0289  164 LEU   A CA  
3542 C C   A LEU   A 164 ? 0.1406 0.2810 0.2825 -0.0278 0.0197  0.0956  164 LEU   A C   
3543 C C   B LEU   A 164 ? 0.2098 0.2457 0.2179 -0.0079 0.0107  0.0268  164 LEU   A C   
3544 O O   A LEU   A 164 ? 0.1502 0.2859 0.2779 -0.0310 0.0437  0.0786  164 LEU   A O   
3545 O O   B LEU   A 164 ? 0.2095 0.2467 0.2170 -0.0096 0.0139  0.0237  164 LEU   A O   
3546 C CB  A LEU   A 164 ? 0.1352 0.2699 0.2654 -0.0312 0.0187  0.1027  164 LEU   A CB  
3547 C CB  B LEU   A 164 ? 0.2105 0.2432 0.2187 -0.0122 0.0057  0.0305  164 LEU   A CB  
3548 C CG  A LEU   A 164 ? 0.1419 0.2643 0.2684 -0.0192 0.0148  0.0863  164 LEU   A CG  
3549 C CG  B LEU   A 164 ? 0.2069 0.2375 0.2156 -0.0123 0.0025  0.0306  164 LEU   A CG  
3550 C CD1 A LEU   A 164 ? 0.1361 0.2598 0.2725 -0.0057 0.0084  0.0760  164 LEU   A CD1 
3551 C CD1 B LEU   A 164 ? 0.2021 0.2346 0.2127 -0.0099 -0.0001 0.0338  164 LEU   A CD1 
3552 C CD2 A LEU   A 164 ? 0.1538 0.2641 0.2661 -0.0240 0.0259  0.0807  164 LEU   A CD2 
3553 C CD2 B LEU   A 164 ? 0.2088 0.2351 0.2166 -0.0144 0.0025  0.0280  164 LEU   A CD2 
3576 N N   A VAL   A 165 ? 0.1271 0.2721 0.2789 -0.0260 0.0133  0.0989  165 VAL   A N   
3577 N N   B VAL   A 165 ? 0.2040 0.2410 0.2154 -0.0035 0.0128  0.0263  165 VAL   A N   
3578 C CA  A VAL   A 165 ? 0.1432 0.2706 0.2677 -0.0269 0.0213  0.1037  165 VAL   A CA  
3579 C CA  B VAL   A 165 ? 0.1997 0.2391 0.2130 -0.0004 0.0162  0.0249  165 VAL   A CA  
3580 C C   A VAL   A 165 ? 0.1362 0.2837 0.2699 -0.0168 0.0275  0.1039  165 VAL   A C   
3581 C C   B VAL   A 165 ? 0.2003 0.2456 0.2216 -0.0015 0.0120  0.0257  165 VAL   A C   
3582 O O   A VAL   A 165 ? 0.1318 0.2829 0.2773 -0.0164 0.0228  0.0989  165 VAL   A O   
3583 O O   B VAL   A 165 ? 0.2003 0.2440 0.2208 -0.0031 0.0107  0.0242  165 VAL   A O   
3584 C CB  A VAL   A 165 ? 0.1589 0.2618 0.2726 -0.0302 0.0289  0.0919  165 VAL   A CB  
3585 C CB  B VAL   A 165 ? 0.1940 0.2323 0.2089 0.0034  0.0219  0.0206  165 VAL   A CB  
3586 C CG1 A VAL   A 165 ? 0.1623 0.2665 0.2825 -0.0298 0.0275  0.0733  165 VAL   A CG1 
3587 C CG1 B VAL   A 165 ? 0.1899 0.2309 0.2078 0.0036  0.0241  0.0181  165 VAL   A CG1 
3588 C CG2 A VAL   A 165 ? 0.1772 0.2593 0.2766 -0.0284 0.0263  0.0945  165 VAL   A CG2 
3589 C CG2 B VAL   A 165 ? 0.1957 0.2314 0.2118 0.0040  0.0209  0.0187  165 VAL   A CG2 
3608 N N   A SER   A 166 ? 0.1244 0.2977 0.2878 -0.0145 0.0269  0.1019  166 SER   A N   
3609 N N   B SER   A 166 ? 0.2002 0.2544 0.2359 -0.0034 0.0088  0.0274  166 SER   A N   
3610 C CA  A SER   A 166 ? 0.1316 0.3178 0.3046 -0.0143 0.0158  0.0869  166 SER   A CA  
3611 C CA  B SER   A 166 ? 0.2025 0.2646 0.2457 -0.0061 0.0064  0.0273  166 SER   A CA  
3612 C C   A SER   A 166 ? 0.1357 0.3360 0.3028 -0.0189 0.0006  0.0728  166 SER   A C   
3613 C C   B SER   A 166 ? 0.2000 0.2761 0.2442 -0.0085 0.0037  0.0284  166 SER   A C   
3614 O O   A SER   A 166 ? 0.1572 0.3524 0.3354 -0.0313 0.0012  0.0496  166 SER   A O   
3615 O O   B SER   A 166 ? 0.2008 0.2775 0.2501 -0.0118 0.0048  0.0271  166 SER   A O   
3616 C CB  A SER   A 166 ? 0.1491 0.3269 0.3492 -0.0059 0.0087  0.0727  166 SER   A CB  
3617 C CB  B SER   A 166 ? 0.2095 0.2650 0.2589 -0.0068 0.0076  0.0256  166 SER   A CB  
3618 O OG  A SER   A 166 ? 0.1883 0.3354 0.3881 -0.0087 0.0105  0.0722  166 SER   A OG  
3619 O OG  B SER   A 166 ? 0.2189 0.2668 0.2674 -0.0077 0.0105  0.0263  166 SER   A OG  
3630 N N   A SER   A 167 ? 0.1438 0.3380 0.2704 -0.0051 -0.0088 0.0751  167 SER   A N   
3631 N N   B SER   A 167 ? 0.1977 0.2864 0.2394 -0.0054 0.0009  0.0314  167 SER   A N   
3632 C CA  A SER   A 167 ? 0.1718 0.3421 0.2694 0.0042  -0.0157 0.0570  167 SER   A CA  
3633 C CA  B SER   A 167 ? 0.1947 0.2985 0.2378 0.0000  0.0012  0.0297  167 SER   A CA  
3634 C C   A SER   A 167 ? 0.1795 0.3382 0.2651 0.0132  -0.0018 0.0486  167 SER   A C   
3635 C C   B SER   A 167 ? 0.1854 0.3131 0.2446 0.0079  0.0042  0.0317  167 SER   A C   
3636 O O   A SER   A 167 ? 0.1984 0.3455 0.2801 0.0188  -0.0143 0.0498  167 SER   A O   
3637 O O   B SER   A 167 ? 0.1923 0.3132 0.2474 0.0069  -0.0025 0.0328  167 SER   A O   
3638 C CB  A SER   A 167 ? 0.1838 0.3488 0.2744 0.0069  -0.0143 0.0629  167 SER   A CB  
3639 C CB  B SER   A 167 ? 0.1996 0.2968 0.2314 -0.0024 0.0021  0.0292  167 SER   A CB  
3640 O OG  A SER   A 167 ? 0.1893 0.3517 0.2701 0.0018  0.0054  0.0669  167 SER   A OG  
3641 O OG  B SER   A 167 ? 0.2020 0.2958 0.2253 -0.0040 0.0088  0.0290  167 SER   A OG  
3652 N N   . PHE   A 168 ? 0.1700 0.3298 0.2499 0.0157  0.0074  0.0381  168 PHE   A N   
3653 C CA  . PHE   A 168 ? 0.1689 0.3345 0.2738 0.0121  0.0209  0.0326  168 PHE   A CA  
3654 C C   . PHE   A 168 ? 0.1959 0.3616 0.3174 -0.0049 0.0553  0.0145  168 PHE   A C   
3655 O O   . PHE   A 168 ? 0.2035 0.3571 0.3571 -0.0230 0.0647  0.0226  168 PHE   A O   
3656 C CB  . PHE   A 168 ? 0.1675 0.3128 0.2598 0.0049  0.0008  0.0398  168 PHE   A CB  
3657 C CG  . PHE   A 168 ? 0.1615 0.2958 0.2455 -0.0068 -0.0047 0.0499  168 PHE   A CG  
3658 C CD1 . PHE   A 168 ? 0.1615 0.3026 0.2530 -0.0172 -0.0108 0.0569  168 PHE   A CD1 
3659 C CD2 . PHE   A 168 ? 0.1589 0.2839 0.2401 -0.0061 0.0072  0.0500  168 PHE   A CD2 
3660 C CE1 . PHE   A 168 ? 0.1486 0.3011 0.2498 -0.0186 -0.0144 0.0624  168 PHE   A CE1 
3661 C CE2 . PHE   A 168 ? 0.1638 0.2809 0.2550 -0.0073 0.0105  0.0573  168 PHE   A CE2 
3662 C CZ  . PHE   A 168 ? 0.1546 0.2902 0.2519 -0.0127 0.0027  0.0628  168 PHE   A CZ  
3673 N N   . LEU   A 169 ? 0.2526 0.3940 0.3816 -0.0187 0.0404  -0.0121 169 LEU   A N   
3674 C CA  . LEU   A 169 ? 0.3357 0.4325 0.4732 -0.0191 -0.0022 -0.0328 169 LEU   A CA  
3675 C C   . LEU   A 169 ? 0.3628 0.4401 0.5154 -0.0194 -0.0152 -0.0285 169 LEU   A C   
3676 O O   . LEU   A 169 ? 0.3777 0.4442 0.5313 -0.0207 -0.0146 -0.0311 169 LEU   A O   
3677 C CB  . LEU   A 169 ? 0.3813 0.4565 0.5106 -0.0202 -0.0251 -0.0496 169 LEU   A CB  
3678 C CG  . LEU   A 169 ? 0.4231 0.4738 0.5407 -0.0230 -0.0392 -0.0675 169 LEU   A CG  
3679 C CD1 . LEU   A 169 ? 0.4391 0.4819 0.5521 -0.0228 -0.0421 -0.0720 169 LEU   A CD1 
3680 C CD2 . LEU   A 169 ? 0.4416 0.4770 0.5466 -0.0244 -0.0416 -0.0737 169 LEU   A CD2 
3681 O OXT . LEU   A 169 ? 0.3591 0.4416 0.5265 -0.0173 -0.0175 -0.0257 169 LEU   A OXT 
3693 N N   A SER   B 1   ? 0.3620 0.3521 0.3760 -0.1170 -0.0802 0.0283  1   SER   B N   
3694 N N   B SER   B 1   ? 0.3576 0.3540 0.3493 -0.0304 -0.0227 0.0098  1   SER   B N   
3695 C CA  A SER   B 1   ? 0.3461 0.3526 0.3677 -0.1238 -0.0913 0.0275  1   SER   B CA  
3696 C CA  B SER   B 1   ? 0.3548 0.3539 0.3453 -0.0307 -0.0223 0.0106  1   SER   B CA  
3697 C C   A SER   B 1   ? 0.3141 0.3527 0.3532 -0.1260 -0.1038 0.0470  1   SER   B C   
3698 C C   B SER   B 1   ? 0.3490 0.3531 0.3477 -0.0301 -0.0240 0.0159  1   SER   B C   
3699 O O   A SER   B 1   ? 0.3201 0.3514 0.3237 -0.1137 -0.1037 0.0480  1   SER   B O   
3700 O O   B SER   B 1   ? 0.3496 0.3519 0.3404 -0.0290 -0.0249 0.0153  1   SER   B O   
3701 C CB  A SER   B 1   ? 0.3599 0.3533 0.3913 -0.1220 -0.0807 0.0063  1   SER   B CB  
3702 C CB  B SER   B 1   ? 0.3571 0.3547 0.3526 -0.0305 -0.0190 0.0052  1   SER   B CB  
3703 O OG  A SER   B 1   ? 0.3774 0.3648 0.4290 -0.1161 -0.0593 -0.0001 1   SER   B OG  
3704 O OG  B SER   B 1   ? 0.3600 0.3570 0.3576 -0.0307 -0.0157 0.0019  1   SER   B OG  
3719 N N   A MET   B 2   ? 0.2918 0.3542 0.3617 -0.1232 -0.0980 0.0848  2   MET   B N   
3720 N N   B MET   B 2   ? 0.3422 0.3519 0.3519 -0.0297 -0.0242 0.0244  2   MET   B N   
3721 C CA  A MET   B 2   ? 0.2784 0.3543 0.3756 -0.1000 -0.0920 0.1083  2   MET   B CA  
3722 C CA  B MET   B 2   ? 0.3325 0.3478 0.3564 -0.0282 -0.0238 0.0316  2   MET   B CA  
3723 C C   A MET   B 2   ? 0.2426 0.3265 0.3444 -0.0815 -0.0915 0.1392  2   MET   B C   
3724 C C   B MET   B 2   ? 0.3078 0.3264 0.3227 -0.0318 -0.0248 0.0401  2   MET   B C   
3725 O O   A MET   B 2   ? 0.2376 0.3377 0.3498 -0.0576 -0.1118 0.1375  2   MET   B O   
3726 O O   B MET   B 2   ? 0.3085 0.3289 0.3244 -0.0301 -0.0231 0.0393  2   MET   B O   
3727 C CB  A MET   B 2   ? 0.3131 0.3903 0.4548 -0.0749 -0.0699 0.0851  2   MET   B CB  
3728 C CB  B MET   B 2   ? 0.3459 0.3632 0.3968 -0.0217 -0.0212 0.0294  2   MET   B CB  
3729 C CG  A MET   B 2   ? 0.3443 0.4212 0.5282 -0.0496 -0.0528 0.0724  2   MET   B CG  
3730 C CG  B MET   B 2   ? 0.3572 0.3764 0.4332 -0.0158 -0.0197 0.0290  2   MET   B CG  
3731 S SD  A MET   B 2   ? 0.3722 0.4511 0.5959 -0.0294 -0.0390 0.0591  2   MET   B SD  
3732 S SD  B MET   B 2   ? 0.3663 0.3874 0.4650 -0.0106 -0.0201 0.0290  2   MET   B SD  
3733 C CE  A MET   B 2   ? 0.3723 0.4579 0.5992 -0.0283 -0.0267 0.0563  2   MET   B CE  
3734 C CE  B MET   B 2   ? 0.3679 0.3893 0.4727 -0.0101 -0.0174 0.0272  2   MET   B CE  
3753 N N   A VAL   B 3   ? 0.2184 0.2876 0.3147 -0.0869 -0.0809 0.1539  3   VAL   B N   
3754 N N   B VAL   B 3   ? 0.2820 0.3016 0.2910 -0.0377 -0.0289 0.0497  3   VAL   B N   
3755 C CA  A VAL   B 3   ? 0.2167 0.2524 0.3019 -0.0788 -0.0742 0.1386  3   VAL   B CA  
3756 C CA  B VAL   B 3   ? 0.2563 0.2760 0.2640 -0.0424 -0.0342 0.0566  3   VAL   B CA  
3757 C C   A VAL   B 3   ? 0.2019 0.2434 0.2571 -0.0684 -0.0711 0.1206  3   VAL   B C   
3758 C C   B VAL   B 3   ? 0.2273 0.2504 0.2369 -0.0500 -0.0463 0.0702  3   VAL   B C   
3759 O O   A VAL   B 3   ? 0.2063 0.2622 0.2697 -0.0643 -0.0789 0.1305  3   VAL   B O   
3760 O O   B VAL   B 3   ? 0.2277 0.2566 0.2307 -0.0466 -0.0444 0.0717  3   VAL   B O   
3761 C CB  A VAL   B 3   ? 0.2387 0.2460 0.3499 -0.0746 -0.0700 0.1197  3   VAL   B CB  
3762 C CB  B VAL   B 3   ? 0.2602 0.2762 0.2699 -0.0409 -0.0292 0.0507  3   VAL   B CB  
3763 C CG1 A VAL   B 3   ? 0.2448 0.2371 0.3710 -0.0765 -0.0734 0.1112  3   VAL   B CG1 
3764 C CG1 B VAL   B 3   ? 0.2618 0.2759 0.2735 -0.0410 -0.0286 0.0468  3   VAL   B CG1 
3765 C CG2 A VAL   B 3   ? 0.2490 0.2562 0.3661 -0.0691 -0.0633 0.1209  3   VAL   B CG2 
3766 C CG2 B VAL   B 3   ? 0.2617 0.2772 0.2719 -0.0395 -0.0272 0.0501  3   VAL   B CG2 
3785 N N   . ASN   B 4   ? 0.1991 0.2190 0.2259 -0.0604 -0.0607 0.0875  4   ASN   B N   
3786 C CA  . ASN   B 4   ? 0.1955 0.2138 0.1958 -0.0618 -0.0528 0.0453  4   ASN   B CA  
3787 C C   . ASN   B 4   ? 0.1963 0.2277 0.1938 -0.0616 -0.0374 0.0331  4   ASN   B C   
3788 O O   . ASN   B 4   ? 0.1960 0.2335 0.2249 -0.0539 -0.0291 0.0198  4   ASN   B O   
3789 C CB  . ASN   B 4   ? 0.1924 0.2106 0.1867 -0.0522 -0.0584 0.0385  4   ASN   B CB  
3790 C CG  . ASN   B 4   ? 0.1882 0.1884 0.1812 -0.0481 -0.0520 0.0294  4   ASN   B CG  
3791 O OD1 . ASN   B 4   ? 0.1914 0.1761 0.1778 -0.0476 -0.0562 0.0282  4   ASN   B OD1 
3792 N ND2 . ASN   B 4   ? 0.2060 0.1965 0.1799 -0.0258 -0.0361 0.0242  4   ASN   B ND2 
3800 N N   . SER   B 5   ? 0.2123 0.2405 0.1998 -0.0618 -0.0211 0.0290  5   SER   B N   
3801 C CA  . SER   B 5   ? 0.2368 0.2733 0.2323 -0.0576 0.0026  0.0269  5   SER   B CA  
3802 C C   . SER   B 5   ? 0.2547 0.2808 0.2630 -0.0762 0.0271  0.0270  5   SER   B C   
3803 O O   . SER   B 5   ? 0.2665 0.2810 0.3288 -0.0674 0.0587  0.0298  5   SER   B O   
3804 C CB  . SER   B 5   ? 0.2462 0.2972 0.2534 -0.0464 0.0050  0.0374  5   SER   B CB  
3805 O OG  . SER   B 5   ? 0.2727 0.3322 0.3071 -0.0319 0.0019  0.0464  5   SER   B OG  
3811 N N   . PHE   B 6   ? 0.2765 0.3047 0.2457 -0.0833 0.0423  0.0349  6   PHE   B N   
3812 C CA  . PHE   B 6   ? 0.2884 0.3106 0.2115 -0.0982 0.0437  0.0203  6   PHE   B CA  
3813 C C   . PHE   B 6   ? 0.3378 0.3397 0.2540 -0.0975 0.0615  -0.0101 6   PHE   B C   
3814 O O   . PHE   B 6   ? 0.3492 0.3663 0.2823 -0.0852 0.0456  -0.0291 6   PHE   B O   
3815 C CB  . PHE   B 6   ? 0.2547 0.2871 0.1900 -0.0909 0.0122  0.0174  6   PHE   B CB  
3816 C CG  . PHE   B 6   ? 0.2225 0.2515 0.1866 -0.0794 -0.0030 0.0090  6   PHE   B CG  
3817 C CD1 . PHE   B 6   ? 0.2226 0.2200 0.1702 -0.0735 -0.0169 0.0083  6   PHE   B CD1 
3818 C CD2 . PHE   B 6   ? 0.2019 0.2452 0.1900 -0.0652 0.0067  0.0334  6   PHE   B CD2 
3819 C CE1 . PHE   B 6   ? 0.2153 0.1960 0.1744 -0.0596 -0.0160 0.0012  6   PHE   B CE1 
3820 C CE2 . PHE   B 6   ? 0.2066 0.2269 0.2115 -0.0478 0.0087  0.0329  6   PHE   B CE2 
3821 C CZ  . PHE   B 6   ? 0.2070 0.2011 0.1972 -0.0477 0.0020  0.0147  6   PHE   B CZ  
3831 N N   . SER   B 7   ? 0.3713 0.3251 0.2638 -0.1175 0.0885  -0.0349 7   SER   B N   
3832 C CA  . SER   B 7   ? 0.4027 0.3390 0.3058 -0.1173 0.1152  -0.0369 7   SER   B CA  
3833 C C   . SER   B 7   ? 0.4067 0.3211 0.2931 -0.1219 0.1337  -0.0512 7   SER   B C   
3834 O O   . SER   B 7   ? 0.4221 0.3197 0.3194 -0.1306 0.1291  -0.0517 7   SER   B O   
3835 C CB  . SER   B 7   ? 0.4243 0.3570 0.3697 -0.1119 0.1275  -0.0360 7   SER   B CB  
3836 O OG  . SER   B 7   ? 0.4445 0.3675 0.4258 -0.1096 0.1322  -0.0271 7   SER   B OG  
3842 N N   . GLY   B 8   ? 0.4000 0.3118 0.2954 -0.1027 0.1337  -0.0665 8   GLY   B N   
3843 C CA  . GLY   B 8   ? 0.3856 0.2948 0.2980 -0.0951 0.1339  -0.0734 8   GLY   B CA  
3844 C C   . GLY   B 8   ? 0.3715 0.2666 0.2937 -0.0957 0.1355  -0.0605 8   GLY   B C   
3845 O O   . GLY   B 8   ? 0.3864 0.2782 0.3285 -0.0888 0.1399  -0.0619 8   GLY   B O   
3849 N N   . TYR   B 9   ? 0.3530 0.2390 0.2647 -0.0842 0.1101  -0.0679 9   TYR   B N   
3850 C CA  . TYR   B 9   ? 0.3348 0.2133 0.2417 -0.0734 0.0718  -0.0543 9   TYR   B CA  
3851 C C   . TYR   B 9   ? 0.3261 0.2092 0.2325 -0.0652 0.0330  -0.0393 9   TYR   B C   
3852 O O   . TYR   B 9   ? 0.3347 0.2305 0.2632 -0.0624 0.0378  -0.0272 9   TYR   B O   
3853 C CB  . TYR   B 9   ? 0.3291 0.1957 0.2386 -0.0630 0.0701  -0.0496 9   TYR   B CB  
3854 C CG  . TYR   B 9   ? 0.3160 0.1750 0.2440 -0.0695 0.0716  -0.0493 9   TYR   B CG  
3855 C CD1 . TYR   B 9   ? 0.3142 0.1785 0.2608 -0.0857 0.0736  -0.0450 9   TYR   B CD1 
3856 C CD2 . TYR   B 9   ? 0.2990 0.1668 0.2393 -0.0623 0.0671  -0.0529 9   TYR   B CD2 
3857 C CE1 . TYR   B 9   ? 0.3047 0.1881 0.2704 -0.0867 0.0736  -0.0595 9   TYR   B CE1 
3858 C CE2 . TYR   B 9   ? 0.2954 0.1703 0.2473 -0.0597 0.0642  -0.0519 9   TYR   B CE2 
3859 C CZ  . TYR   B 9   ? 0.2931 0.1852 0.2626 -0.0743 0.0708  -0.0652 9   TYR   B CZ  
3860 O OH  . TYR   B 9   ? 0.2846 0.1990 0.2778 -0.0790 0.0691  -0.0765 9   TYR   B OH  
3870 N N   . LEU   B 10  ? 0.3073 0.1847 0.2052 -0.0594 0.0151  -0.0388 10  LEU   B N   
3871 C CA  . LEU   B 10  ? 0.2997 0.1848 0.2091 -0.0661 -0.0135 -0.0414 10  LEU   B CA  
3872 C C   . LEU   B 10  ? 0.2747 0.1838 0.2151 -0.0700 -0.0273 -0.0361 10  LEU   B C   
3873 O O   . LEU   B 10  ? 0.2584 0.1813 0.2142 -0.0521 -0.0203 -0.0243 10  LEU   B O   
3874 C CB  . LEU   B 10  ? 0.3140 0.1821 0.2243 -0.0689 -0.0325 -0.0205 10  LEU   B CB  
3875 C CG  . LEU   B 10  ? 0.3290 0.1906 0.2600 -0.0604 -0.0586 -0.0079 10  LEU   B CG  
3876 C CD1 . LEU   B 10  ? 0.3392 0.2050 0.2830 -0.0515 -0.0546 -0.0087 10  LEU   B CD1 
3877 C CD2 . LEU   B 10  ? 0.3360 0.1931 0.2852 -0.0618 -0.0483 0.0137  10  LEU   B CD2 
3889 N N   . LYS   B 11  ? 0.2864 0.2103 0.2161 -0.0665 -0.0320 -0.0282 11  LYS   B N   
3890 C CA  . LYS   B 11  ? 0.3025 0.2415 0.2501 -0.0554 -0.0431 -0.0266 11  LYS   B CA  
3891 C C   . LYS   B 11  ? 0.2845 0.2219 0.2591 -0.0697 -0.0426 -0.0381 11  LYS   B C   
3892 O O   . LYS   B 11  ? 0.3033 0.2395 0.2885 -0.0812 -0.0466 -0.0741 11  LYS   B O   
3893 C CB  . LYS   B 11  ? 0.3364 0.2926 0.3039 -0.0309 -0.0474 -0.0221 11  LYS   B CB  
3894 C CG  . LYS   B 11  ? 0.3693 0.3275 0.3711 -0.0124 -0.0487 -0.0203 11  LYS   B CG  
3895 C CD  . LYS   B 11  ? 0.3925 0.3525 0.4287 -0.0003 -0.0467 -0.0259 11  LYS   B CD  
3896 C CE  . LYS   B 11  ? 0.4075 0.3683 0.4751 0.0057  -0.0397 -0.0257 11  LYS   B CE  
3897 N NZ  . LYS   B 11  ? 0.4151 0.3774 0.5023 0.0082  -0.0376 -0.0212 11  LYS   B NZ  
3911 N N   . LEU   B 12  ? 0.2459 0.1975 0.2517 -0.0638 -0.0402 -0.0425 12  LEU   B N   
3912 C CA  . LEU   B 12  ? 0.2330 0.1815 0.2672 -0.0548 -0.0332 -0.0300 12  LEU   B CA  
3913 C C   . LEU   B 12  ? 0.2205 0.1745 0.2777 -0.0518 -0.0448 -0.0256 12  LEU   B C   
3914 O O   . LEU   B 12  ? 0.2186 0.1730 0.2991 -0.0588 -0.0615 -0.0177 12  LEU   B O   
3915 C CB  . LEU   B 12  ? 0.2366 0.1594 0.2636 -0.0407 -0.0180 -0.0345 12  LEU   B CB  
3916 C CG  . LEU   B 12  ? 0.2379 0.1536 0.2762 -0.0427 -0.0103 -0.0252 12  LEU   B CG  
3917 C CD1 . LEU   B 12  ? 0.2503 0.1496 0.2698 -0.0284 -0.0104 -0.0046 12  LEU   B CD1 
3918 C CD2 . LEU   B 12  ? 0.2456 0.1588 0.2895 -0.0382 -0.0045 -0.0335 12  LEU   B CD2 
3930 N N   . THR   B 13  ? 0.2087 0.1803 0.2731 -0.0499 -0.0377 -0.0381 13  THR   B N   
3931 C CA  . THR   B 13  ? 0.2076 0.1884 0.2658 -0.0576 -0.0471 -0.0255 13  THR   B CA  
3932 C C   . THR   B 13  ? 0.2591 0.2079 0.2826 -0.0627 -0.0659 -0.0217 13  THR   B C   
3933 O O   . THR   B 13  ? 0.2781 0.2035 0.2950 -0.0575 -0.0362 -0.0256 13  THR   B O   
3934 C CB  . THR   B 13  ? 0.1904 0.1905 0.2711 -0.0509 -0.0469 -0.0172 13  THR   B CB  
3935 O OG1 . THR   B 13  ? 0.1821 0.1839 0.2761 -0.0454 -0.0387 -0.0206 13  THR   B OG1 
3936 C CG2 . THR   B 13  ? 0.2012 0.1985 0.2750 -0.0450 -0.0385 -0.0056 13  THR   B CG2 
3944 N N   A ASP   B 14  ? 0.2699 0.2163 0.2949 -0.0767 -0.1121 -0.0078 14  ASP   B N   
3945 N N   B ASP   B 14  ? 0.2664 0.2184 0.2961 -0.0648 -0.0663 -0.0144 14  ASP   B N   
3946 C CA  A ASP   B 14  ? 0.2866 0.2390 0.3260 -0.0712 -0.1112 0.0181  14  ASP   B CA  
3947 C CA  B ASP   B 14  ? 0.2704 0.2283 0.3113 -0.0644 -0.0652 -0.0052 14  ASP   B CA  
3948 C C   A ASP   B 14  ? 0.2731 0.2199 0.2848 -0.0757 -0.0931 0.0207  14  ASP   B C   
3949 C C   B ASP   B 14  ? 0.2538 0.2102 0.2813 -0.0642 -0.0725 0.0024  14  ASP   B C   
3950 O O   A ASP   B 14  ? 0.3040 0.2411 0.2914 -0.0783 -0.0929 0.0310  14  ASP   B O   
3951 O O   B ASP   B 14  ? 0.2611 0.2128 0.2773 -0.0658 -0.0729 0.0004  14  ASP   B O   
3952 C CB  A ASP   B 14  ? 0.3115 0.2824 0.3964 -0.0651 -0.1214 0.0204  14  ASP   B CB  
3953 C CB  B ASP   B 14  ? 0.2877 0.2529 0.3571 -0.0624 -0.0557 -0.0052 14  ASP   B CB  
3954 C CG  A ASP   B 14  ? 0.3424 0.3206 0.4730 -0.0592 -0.1164 0.0074  14  ASP   B CG  
3955 C CG  B ASP   B 14  ? 0.3040 0.2708 0.3957 -0.0567 -0.0463 -0.0071 14  ASP   B CG  
3956 O OD1 A ASP   B 14  ? 0.3637 0.3378 0.4900 -0.0628 -0.1150 -0.0113 14  ASP   B OD1 
3957 O OD1 B ASP   B 14  ? 0.3091 0.2780 0.4086 -0.0549 -0.0424 -0.0106 14  ASP   B OD1 
3958 O OD2 A ASP   B 14  ? 0.3469 0.3378 0.5107 -0.0584 -0.1131 0.0096  14  ASP   B OD2 
3959 O OD2 B ASP   B 14  ? 0.3100 0.2755 0.4120 -0.0556 -0.0438 -0.0058 14  ASP   B OD2 
3968 N N   . ASN   B 15  ? 0.2295 0.1906 0.2595 -0.0594 -0.0818 0.0094  15  ASN   B N   
3969 C CA  . ASN   B 15  ? 0.1861 0.1630 0.2473 -0.0362 -0.0572 0.0064  15  ASN   B CA  
3970 C C   . ASN   B 15  ? 0.1652 0.1521 0.2384 -0.0216 -0.0395 -0.0018 15  ASN   B C   
3971 O O   . ASN   B 15  ? 0.1639 0.1430 0.2521 -0.0249 -0.0494 -0.0136 15  ASN   B O   
3972 C CB  . ASN   B 15  ? 0.1832 0.1571 0.2524 -0.0173 -0.0600 0.0092  15  ASN   B CB  
3973 C CG  . ASN   B 15  ? 0.1659 0.1600 0.2651 -0.0261 -0.0341 0.0080  15  ASN   B CG  
3974 O OD1 . ASN   B 15  ? 0.1669 0.1849 0.2917 -0.0399 -0.0365 0.0163  15  ASN   B OD1 
3975 N ND2 . ASN   B 15  ? 0.1681 0.1341 0.2524 -0.0203 -0.0029 -0.0093 15  ASN   B ND2 
3983 N N   . VAL   B 16  ? 0.1728 0.1411 0.2275 -0.0285 -0.0511 -0.0028 16  VAL   B N   
3984 C CA  . VAL   B 16  ? 0.1691 0.1466 0.2159 -0.0276 -0.0384 -0.0245 16  VAL   B CA  
3985 C C   . VAL   B 16  ? 0.1670 0.1547 0.2125 -0.0364 -0.0368 -0.0161 16  VAL   B C   
3986 O O   . VAL   B 16  ? 0.1789 0.1708 0.2368 -0.0331 -0.0285 -0.0297 16  VAL   B O   
3987 C CB  . VAL   B 16  ? 0.1743 0.1465 0.2259 -0.0137 -0.0218 -0.0127 16  VAL   B CB  
3988 C CG1 . VAL   B 16  ? 0.1825 0.1444 0.2262 -0.0027 -0.0181 -0.0104 16  VAL   B CG1 
3989 C CG2 . VAL   B 16  ? 0.1726 0.1543 0.2508 -0.0120 -0.0100 -0.0100 16  VAL   B CG2 
3999 N N   . TYR   B 17  ? 0.1779 0.1607 0.2134 -0.0343 -0.0237 -0.0108 17  TYR   B N   
4000 C CA  . TYR   B 17  ? 0.1824 0.1788 0.2084 -0.0426 -0.0307 -0.0023 17  TYR   B CA  
4001 C C   . TYR   B 17  ? 0.1771 0.1548 0.2085 -0.0373 -0.0219 -0.0149 17  TYR   B C   
4002 O O   . TYR   B 17  ? 0.1712 0.1632 0.2200 -0.0316 -0.0318 -0.0396 17  TYR   B O   
4003 C CB  . TYR   B 17  ? 0.2120 0.2202 0.2221 -0.0273 -0.0322 0.0270  17  TYR   B CB  
4004 C CG  . TYR   B 17  ? 0.2456 0.2643 0.2621 -0.0163 -0.0372 0.0307  17  TYR   B CG  
4005 C CD1 . TYR   B 17  ? 0.2650 0.2732 0.2797 -0.0129 -0.0472 0.0367  17  TYR   B CD1 
4006 C CD2 . TYR   B 17  ? 0.2656 0.2905 0.2844 -0.0057 -0.0450 0.0248  17  TYR   B CD2 
4007 C CE1 . TYR   B 17  ? 0.2834 0.2929 0.2995 -0.0041 -0.0594 0.0317  17  TYR   B CE1 
4008 C CE2 . TYR   B 17  ? 0.2840 0.3058 0.3067 0.0057  -0.0620 0.0313  17  TYR   B CE2 
4009 C CZ  . TYR   B 17  ? 0.2958 0.3140 0.3104 0.0068  -0.0677 0.0345  17  TYR   B CZ  
4010 O OH  . TYR   B 17  ? 0.3117 0.3463 0.3363 0.0171  -0.0726 0.0338  17  TYR   B OH  
4020 N N   . ILE   B 18  ? 0.1884 0.1500 0.1997 -0.0340 -0.0129 -0.0213 18  ILE   B N   
4021 C CA  . ILE   B 18  ? 0.1915 0.1472 0.1958 -0.0334 -0.0088 -0.0268 18  ILE   B CA  
4022 C C   . ILE   B 18  ? 0.2071 0.1501 0.1925 -0.0437 -0.0069 -0.0312 18  ILE   B C   
4023 O O   . ILE   B 18  ? 0.2282 0.1681 0.2146 -0.0371 0.0045  -0.0451 18  ILE   B O   
4024 C CB  . ILE   B 18  ? 0.1939 0.1512 0.2125 -0.0388 -0.0134 -0.0209 18  ILE   B CB  
4025 C CG1 . ILE   B 18  ? 0.1916 0.1557 0.2211 -0.0381 -0.0032 -0.0088 18  ILE   B CG1 
4026 C CG2 . ILE   B 18  ? 0.1939 0.1553 0.2148 -0.0379 -0.0153 -0.0181 18  ILE   B CG2 
4027 C CD1 . ILE   B 18  ? 0.1968 0.1816 0.2410 -0.0387 -0.0192 0.0119  18  ILE   B CD1 
4039 N N   . LYS   B 19  ? 0.2126 0.1539 0.2150 -0.0315 0.0273  -0.0367 19  LYS   B N   
4040 C CA  . LYS   B 19  ? 0.2157 0.1560 0.2281 -0.0342 0.0292  -0.0418 19  LYS   B CA  
4041 C C   . LYS   B 19  ? 0.1943 0.1601 0.2345 -0.0274 0.0339  -0.0535 19  LYS   B C   
4042 O O   . LYS   B 19  ? 0.1882 0.1610 0.2246 -0.0206 0.0207  -0.0493 19  LYS   B O   
4043 C CB  . LYS   B 19  ? 0.2440 0.1761 0.2427 -0.0304 0.0338  -0.0299 19  LYS   B CB  
4044 C CG  . LYS   B 19  ? 0.2699 0.1956 0.2547 -0.0375 0.0441  -0.0332 19  LYS   B CG  
4045 C CD  . LYS   B 19  ? 0.2989 0.2297 0.2685 -0.0428 0.0516  -0.0273 19  LYS   B CD  
4046 C CE  . LYS   B 19  ? 0.3249 0.2599 0.2864 -0.0479 0.0459  -0.0265 19  LYS   B CE  
4047 N NZ  . LYS   B 19  ? 0.3420 0.2765 0.2953 -0.0554 0.0535  -0.0241 19  LYS   B NZ  
4061 N N   . ASN   B 20  ? 0.1911 0.1665 0.2746 -0.0250 0.0387  -0.0618 20  ASN   B N   
4062 C CA  . ASN   B 20  ? 0.1920 0.1794 0.2963 -0.0118 0.0464  -0.0714 20  ASN   B CA  
4063 C C   . ASN   B 20  ? 0.1909 0.1981 0.2917 -0.0193 0.0513  -0.0856 20  ASN   B C   
4064 O O   . ASN   B 20  ? 0.2109 0.2336 0.3122 -0.0282 0.0486  -0.0874 20  ASN   B O   
4065 C CB  . ASN   B 20  ? 0.2203 0.1788 0.3242 0.0066  0.0351  -0.0704 20  ASN   B CB  
4066 C CG  . ASN   B 20  ? 0.2479 0.1902 0.3391 0.0341  0.0313  -0.0823 20  ASN   B CG  
4067 O OD1 . ASN   B 20  ? 0.2750 0.2184 0.3621 0.0468  0.0280  -0.0807 20  ASN   B OD1 
4068 N ND2 . ASN   B 20  ? 0.2407 0.1938 0.3315 0.0371  0.0190  -0.0857 20  ASN   B ND2 
4075 N N   . ALA   B 21  ? 0.1955 0.1885 0.2859 -0.0285 0.0497  -0.0698 21  ALA   B N   
4076 C CA  . ALA   B 21  ? 0.2002 0.1932 0.3027 -0.0396 0.0413  -0.0555 21  ALA   B CA  
4077 C C   . ALA   B 21  ? 0.2046 0.1691 0.2913 -0.0239 0.0420  -0.0367 21  ALA   B C   
4078 O O   . ALA   B 21  ? 0.2102 0.1552 0.2858 -0.0300 0.0368  -0.0291 21  ALA   B O   
4079 C CB  . ALA   B 21  ? 0.2140 0.2210 0.3104 -0.0536 0.0337  -0.0401 21  ALA   B CB  
4085 N N   . ASP   B 22  ? 0.1982 0.1570 0.2854 -0.0239 0.0381  -0.0309 22  ASP   B N   
4086 C CA  . ASP   B 22  ? 0.1852 0.1508 0.2720 -0.0132 0.0297  -0.0242 22  ASP   B CA  
4087 C C   . ASP   B 22  ? 0.1795 0.1449 0.2397 -0.0162 0.0218  -0.0125 22  ASP   B C   
4088 O O   . ASP   B 22  ? 0.1836 0.1498 0.2428 -0.0129 0.0145  -0.0091 22  ASP   B O   
4089 C CB  . ASP   B 22  ? 0.1946 0.1550 0.3118 -0.0083 0.0269  -0.0108 22  ASP   B CB  
4090 C CG  . ASP   B 22  ? 0.1951 0.1747 0.3496 -0.0057 0.0030  -0.0121 22  ASP   B CG  
4091 O OD1 . ASP   B 22  ? 0.2065 0.1726 0.3458 -0.0048 -0.0201 -0.0125 22  ASP   B OD1 
4092 O OD2 . ASP   B 22  ? 0.2025 0.2066 0.3971 0.0028  -0.0178 -0.0249 22  ASP   B OD2 
4097 N N   . ILE   B 23  ? 0.1796 0.1409 0.2123 -0.0107 0.0114  0.0114  23  ILE   B N   
4098 C CA  . ILE   B 23  ? 0.1715 0.1392 0.1987 -0.0096 0.0034  0.0027  23  ILE   B CA  
4099 C C   . ILE   B 23  ? 0.1638 0.1404 0.2007 -0.0049 -0.0081 -0.0030 23  ILE   B C   
4100 O O   . ILE   B 23  ? 0.1520 0.1386 0.1930 -0.0090 -0.0081 0.0054  23  ILE   B O   
4101 C CB  . ILE   B 23  ? 0.1670 0.1482 0.2042 -0.0190 0.0005  0.0116  23  ILE   B CB  
4102 C CG1 . ILE   B 23  ? 0.1681 0.1542 0.2142 -0.0153 0.0068  0.0281  23  ILE   B CG1 
4103 C CG2 . ILE   B 23  ? 0.1776 0.1700 0.2181 -0.0150 0.0002  0.0074  23  ILE   B CG2 
4104 C CD1 . ILE   B 23  ? 0.1760 0.1654 0.2151 -0.0093 0.0064  0.0228  23  ILE   B CD1 
4116 N N   . VAL   B 24  ? 0.1668 0.1404 0.2061 -0.0051 -0.0109 -0.0036 24  VAL   B N   
4117 C CA  . VAL   B 24  ? 0.1597 0.1456 0.2366 -0.0024 -0.0192 -0.0074 24  VAL   B CA  
4118 C C   . VAL   B 24  ? 0.1583 0.1489 0.2386 -0.0116 -0.0128 -0.0003 24  VAL   B C   
4119 O O   . VAL   B 24  ? 0.1582 0.1584 0.2494 -0.0183 -0.0074 0.0119  24  VAL   B O   
4120 C CB  . VAL   B 24  ? 0.1727 0.1602 0.2386 0.0037  -0.0204 -0.0031 24  VAL   B CB  
4121 C CG1 . VAL   B 24  ? 0.1723 0.1624 0.2507 -0.0024 -0.0211 -0.0033 24  VAL   B CG1 
4122 C CG2 . VAL   B 24  ? 0.1813 0.1903 0.2325 0.0085  -0.0259 -0.0107 24  VAL   B CG2 
4132 N N   . GLU   B 25  ? 0.1802 0.1671 0.2321 -0.0099 -0.0055 -0.0020 25  GLU   B N   
4133 C CA  . GLU   B 25  ? 0.1892 0.1907 0.2444 -0.0029 0.0108  -0.0079 25  GLU   B CA  
4134 C C   . GLU   B 25  ? 0.1831 0.1882 0.2136 -0.0105 0.0141  -0.0005 25  GLU   B C   
4135 O O   . GLU   B 25  ? 0.1837 0.2003 0.2300 -0.0104 0.0210  0.0030  25  GLU   B O   
4136 C CB  . GLU   B 25  ? 0.2223 0.2219 0.3122 0.0233  0.0343  -0.0194 25  GLU   B CB  
4137 C CG  . GLU   B 25  ? 0.2658 0.2722 0.4143 0.0302  0.0224  -0.0141 25  GLU   B CG  
4138 C CD  . GLU   B 25  ? 0.3193 0.3341 0.4971 0.0238  0.0160  -0.0129 25  GLU   B CD  
4139 O OE1 . GLU   B 25  ? 0.3247 0.3579 0.5267 0.0286  0.0246  -0.0124 25  GLU   B OE1 
4140 O OE2 . GLU   B 25  ? 0.3231 0.3493 0.5313 0.0207  0.0109  -0.0179 25  GLU   B OE2 
4147 N N   . GLU   B 26  ? 0.1803 0.1773 0.1937 -0.0212 0.0103  -0.0049 26  GLU   B N   
4148 C CA  . GLU   B 26  ? 0.1788 0.1861 0.2009 -0.0309 -0.0018 -0.0016 26  GLU   B CA  
4149 C C   . GLU   B 26  ? 0.1698 0.1741 0.1988 -0.0193 0.0037  0.0094  26  GLU   B C   
4150 O O   . GLU   B 26  ? 0.1904 0.1937 0.2005 -0.0220 0.0006  0.0206  26  GLU   B O   
4151 C CB  . GLU   B 26  ? 0.2060 0.2078 0.2199 -0.0440 -0.0024 0.0079  26  GLU   B CB  
4152 C CG  . GLU   B 26  ? 0.2509 0.2477 0.2763 -0.0527 0.0108  -0.0145 26  GLU   B CG  
4153 C CD  . GLU   B 26  ? 0.2798 0.2704 0.2929 -0.0743 0.0296  -0.0484 26  GLU   B CD  
4154 O OE1 . GLU   B 26  ? 0.3098 0.2544 0.3028 -0.0886 0.0629  -0.0437 26  GLU   B OE1 
4155 O OE2 . GLU   B 26  ? 0.2751 0.3117 0.3358 -0.0642 0.0274  -0.0390 26  GLU   B OE2 
4162 N N   . ALA   B 27  ? 0.1488 0.1577 0.1999 -0.0215 0.0115  0.0097  27  ALA   B N   
4163 C CA  . ALA   B 27  ? 0.1531 0.1626 0.2074 -0.0136 0.0065  0.0247  27  ALA   B CA  
4164 C C   . ALA   B 27  ? 0.1587 0.1665 0.2332 -0.0140 0.0212  0.0334  27  ALA   B C   
4165 O O   . ALA   B 27  ? 0.1680 0.1761 0.2474 -0.0052 0.0188  0.0405  27  ALA   B O   
4166 C CB  . ALA   B 27  ? 0.1712 0.1458 0.2155 -0.0200 -0.0017 0.0190  27  ALA   B CB  
4172 N N   . LYS   B 28  ? 0.1526 0.1853 0.2735 -0.0163 0.0269  0.0516  28  LYS   B N   
4173 C CA  . LYS   B 28  ? 0.1714 0.2249 0.2978 -0.0035 0.0560  0.0744  28  LYS   B CA  
4174 C C   . LYS   B 28  ? 0.1939 0.2396 0.2838 0.0036  0.0622  0.0705  28  LYS   B C   
4175 O O   . LYS   B 28  ? 0.2178 0.2444 0.2936 -0.0008 0.0649  0.0655  28  LYS   B O   
4176 C CB  . LYS   B 28  ? 0.1902 0.2584 0.3336 0.0081  0.0732  0.0934  28  LYS   B CB  
4177 C CG  . LYS   B 28  ? 0.2124 0.3006 0.3655 0.0137  0.0821  0.1008  28  LYS   B CG  
4178 C CD  . LYS   B 28  ? 0.2564 0.3495 0.4195 0.0209  0.0912  0.1006  28  LYS   B CD  
4179 C CE  . LYS   B 28  ? 0.2891 0.3804 0.4619 0.0332  0.0891  0.1014  28  LYS   B CE  
4180 N NZ  . LYS   B 28  ? 0.3400 0.4002 0.4917 0.0424  0.0860  0.1038  28  LYS   B NZ  
4194 N N   . LYS   B 29  ? 0.2119 0.2656 0.2815 0.0248  0.0610  0.0572  29  LYS   B N   
4195 C CA  . LYS   B 29  ? 0.2561 0.3007 0.3075 0.0261  0.0631  0.0474  29  LYS   B CA  
4196 C C   . LYS   B 29  ? 0.2546 0.3022 0.2697 0.0229  0.0535  0.0581  29  LYS   B C   
4197 O O   . LYS   B 29  ? 0.2810 0.3222 0.2848 0.0266  0.0488  0.0665  29  LYS   B O   
4198 C CB  . LYS   B 29  ? 0.3105 0.3385 0.3879 0.0233  0.0594  0.0368  29  LYS   B CB  
4199 C CG  . LYS   B 29  ? 0.3537 0.3698 0.4698 0.0189  0.0590  0.0379  29  LYS   B CG  
4200 C CD  . LYS   B 29  ? 0.3863 0.3912 0.5379 0.0139  0.0655  0.0332  29  LYS   B CD  
4201 C CE  . LYS   B 29  ? 0.4115 0.4076 0.5859 0.0101  0.0712  0.0291  29  LYS   B CE  
4202 N NZ  . LYS   B 29  ? 0.4280 0.4202 0.6098 0.0096  0.0727  0.0274  29  LYS   B NZ  
4216 N N   . VAL   B 30  ? 0.2196 0.2830 0.2478 0.0090  0.0469  0.0577  30  VAL   B N   
4217 C CA  . VAL   B 30  ? 0.2019 0.2701 0.2762 -0.0065 0.0056  0.0665  30  VAL   B CA  
4218 C C   . VAL   B 30  ? 0.1766 0.2608 0.2539 -0.0096 0.0075  0.0867  30  VAL   B C   
4219 O O   . VAL   B 30  ? 0.1911 0.2796 0.2660 0.0002  0.0130  0.1001  30  VAL   B O   
4220 C CB  . VAL   B 30  ? 0.2106 0.2677 0.3114 -0.0229 -0.0208 0.0657  30  VAL   B CB  
4221 C CG1 . VAL   B 30  ? 0.2145 0.2805 0.3108 -0.0239 -0.0164 0.0669  30  VAL   B CG1 
4222 C CG2 . VAL   B 30  ? 0.2184 0.2607 0.3205 -0.0375 -0.0333 0.0557  30  VAL   B CG2 
4232 N N   . LYS   B 31  ? 0.1654 0.2255 0.2812 -0.0220 -0.0008 0.0897  31  LYS   B N   
4233 C CA  . LYS   B 31  ? 0.1612 0.2179 0.3072 -0.0366 -0.0054 0.0896  31  LYS   B CA  
4234 C C   . LYS   B 31  ? 0.1624 0.1786 0.2726 -0.0382 -0.0220 0.0725  31  LYS   B C   
4235 O O   . LYS   B 31  ? 0.1703 0.1976 0.2805 -0.0296 -0.0188 0.0889  31  LYS   B O   
4236 C CB  . LYS   B 31  ? 0.1801 0.2614 0.3574 -0.0344 0.0207  0.0978  31  LYS   B CB  
4237 C CG  . LYS   B 31  ? 0.2201 0.3006 0.4013 -0.0362 0.0354  0.0871  31  LYS   B CG  
4238 C CD  . LYS   B 31  ? 0.2610 0.3408 0.4464 -0.0315 0.0293  0.0754  31  LYS   B CD  
4239 C CE  . LYS   B 31  ? 0.2826 0.3647 0.4885 -0.0244 0.0164  0.0620  31  LYS   B CE  
4240 N NZ  . LYS   B 31  ? 0.3169 0.3769 0.5097 -0.0133 0.0039  0.0484  31  LYS   B NZ  
4254 N N   . PRO   B 32  ? 0.1747 0.1489 0.2275 -0.0323 -0.0389 0.0423  32  PRO   B N   
4255 C CA  . PRO   B 32  ? 0.1797 0.1500 0.1880 -0.0314 -0.0430 0.0250  32  PRO   B CA  
4256 C C   . PRO   B 32  ? 0.1864 0.1423 0.1918 -0.0389 -0.0558 0.0313  32  PRO   B C   
4257 O O   . PRO   B 32  ? 0.2022 0.1472 0.2292 -0.0434 -0.0694 0.0372  32  PRO   B O   
4258 C CB  . PRO   B 32  ? 0.1980 0.1407 0.1752 -0.0309 -0.0341 0.0114  32  PRO   B CB  
4259 C CG  . PRO   B 32  ? 0.2163 0.1334 0.1802 -0.0273 -0.0504 0.0191  32  PRO   B CG  
4260 C CD  . PRO   B 32  ? 0.2010 0.1401 0.2103 -0.0208 -0.0539 0.0261  32  PRO   B CD  
4268 N N   . THR   B 33  ? 0.1878 0.1341 0.1863 -0.0314 -0.0508 0.0221  33  THR   B N   
4269 C CA  . THR   B 33  ? 0.1945 0.1384 0.1787 -0.0352 -0.0564 0.0316  33  THR   B CA  
4270 C C   . THR   B 33  ? 0.2010 0.1328 0.1725 -0.0312 -0.0548 0.0219  33  THR   B C   
4271 O O   . THR   B 33  ? 0.2220 0.1358 0.1756 -0.0453 -0.0565 0.0187  33  THR   B O   
4272 C CB  . THR   B 33  ? 0.2029 0.1459 0.1920 -0.0168 -0.0544 0.0362  33  THR   B CB  
4273 O OG1 . THR   B 33  ? 0.1898 0.1617 0.1865 -0.0211 -0.0502 0.0387  33  THR   B OG1 
4274 C CG2 . THR   B 33  ? 0.2268 0.1535 0.2248 -0.0093 -0.0576 0.0294  33  THR   B CG2 
4282 N N   . VAL   B 34  ? 0.1788 0.1281 0.1667 -0.0332 -0.0487 0.0163  34  VAL   B N   
4283 C CA  . VAL   B 34  ? 0.1690 0.1304 0.1633 -0.0276 -0.0333 0.0113  34  VAL   B CA  
4284 C C   . VAL   B 34  ? 0.1539 0.1211 0.1400 -0.0255 -0.0161 0.0057  34  VAL   B C   
4285 O O   . VAL   B 34  ? 0.1721 0.1244 0.1449 -0.0241 -0.0275 0.0022  34  VAL   B O   
4286 C CB  . VAL   B 34  ? 0.1737 0.1317 0.1897 -0.0108 -0.0271 0.0051  34  VAL   B CB  
4287 C CG1 . VAL   B 34  ? 0.1708 0.1475 0.1947 -0.0073 -0.0135 0.0004  34  VAL   B CG1 
4288 C CG2 . VAL   B 34  ? 0.1783 0.1389 0.2137 -0.0108 -0.0237 0.0097  34  VAL   B CG2 
4298 N N   . VAL   B 35  ? 0.1422 0.1208 0.1302 -0.0257 -0.0108 0.0106  35  VAL   B N   
4299 C CA  . VAL   B 35  ? 0.1374 0.1225 0.1337 -0.0223 -0.0118 0.0112  35  VAL   B CA  
4300 C C   . VAL   B 35  ? 0.1298 0.1166 0.1379 -0.0214 -0.0154 0.0104  35  VAL   B C   
4301 O O   . VAL   B 35  ? 0.1348 0.1173 0.1425 -0.0247 -0.0068 -0.0043 35  VAL   B O   
4302 C CB  . VAL   B 35  ? 0.1375 0.1395 0.1489 -0.0200 0.0020  0.0108  35  VAL   B CB  
4303 C CG1 . VAL   B 35  ? 0.1321 0.1470 0.1779 -0.0218 0.0019  0.0022  35  VAL   B CG1 
4304 C CG2 . VAL   B 35  ? 0.1391 0.1459 0.1666 -0.0090 0.0000  0.0021  35  VAL   B CG2 
4314 N N   . VAL   B 36  ? 0.1353 0.1152 0.1314 -0.0181 -0.0128 0.0064  36  VAL   B N   
4315 C CA  . VAL   B 36  ? 0.1268 0.1127 0.1410 -0.0137 -0.0112 0.0016  36  VAL   B CA  
4316 C C   . VAL   B 36  ? 0.1245 0.1166 0.1305 -0.0122 -0.0046 0.0036  36  VAL   B C   
4317 O O   . VAL   B 36  ? 0.1337 0.1266 0.1467 -0.0101 -0.0022 -0.0061 36  VAL   B O   
4318 C CB  . VAL   B 36  ? 0.1283 0.1193 0.1519 -0.0136 -0.0057 0.0005  36  VAL   B CB  
4319 C CG1 . VAL   B 36  ? 0.1269 0.1361 0.1734 -0.0151 -0.0074 0.0020  36  VAL   B CG1 
4320 C CG2 . VAL   B 36  ? 0.1285 0.1292 0.1691 -0.0133 -0.0099 0.0075  36  VAL   B CG2 
4330 N N   . ASN   B 37  ? 0.1256 0.1256 0.1277 -0.0038 -0.0052 0.0051  37  ASN   B N   
4331 C CA  . ASN   B 37  ? 0.1244 0.1231 0.1485 0.0042  -0.0157 0.0102  37  ASN   B CA  
4332 C C   . ASN   B 37  ? 0.1239 0.1220 0.1501 0.0020  -0.0065 0.0064  37  ASN   B C   
4333 O O   . ASN   B 37  ? 0.1372 0.1316 0.1442 0.0018  0.0006  0.0047  37  ASN   B O   
4334 C CB  . ASN   B 37  ? 0.1312 0.1307 0.1470 0.0011  -0.0172 0.0036  37  ASN   B CB  
4335 C CG  . ASN   B 37  ? 0.1322 0.1262 0.1580 -0.0004 -0.0113 -0.0001 37  ASN   B CG  
4336 O OD1 . ASN   B 37  ? 0.1405 0.1333 0.1580 0.0051  -0.0124 0.0022  37  ASN   B OD1 
4337 N ND2 . ASN   B 37  ? 0.1367 0.1238 0.1546 -0.0013 -0.0196 0.0092  37  ASN   B ND2 
4344 N N   . ALA   B 38  ? 0.1363 0.1200 0.1470 0.0053  -0.0006 0.0038  38  ALA   B N   
4345 C CA  . ALA   B 38  ? 0.1433 0.1231 0.1569 -0.0010 0.0037  0.0093  38  ALA   B CA  
4346 C C   . ALA   B 38  ? 0.1383 0.1215 0.1646 -0.0049 -0.0025 0.0045  38  ALA   B C   
4347 O O   . ALA   B 38  ? 0.1480 0.1359 0.1645 0.0084  -0.0070 0.0064  38  ALA   B O   
4348 C CB  . ALA   B 38  ? 0.1747 0.1270 0.1692 -0.0088 0.0131  0.0086  38  ALA   B CB  
4354 N N   . ALA   B 39  ? 0.1440 0.1249 0.1503 0.0016  -0.0040 0.0061  39  ALA   B N   
4355 C CA  . ALA   B 39  ? 0.1518 0.1309 0.1417 0.0045  -0.0086 0.0095  39  ALA   B CA  
4356 C C   . ALA   B 39  ? 0.1506 0.1434 0.1320 0.0033  -0.0094 0.0045  39  ALA   B C   
4357 O O   . ALA   B 39  ? 0.1562 0.1473 0.1543 -0.0003 -0.0052 0.0128  39  ALA   B O   
4358 C CB  . ALA   B 39  ? 0.1493 0.1343 0.1699 -0.0034 0.0019  0.0045  39  ALA   B CB  
4364 N N   . ASN   B 40  ? 0.1523 0.1629 0.1435 -0.0053 0.0009  -0.0068 40  ASN   B N   
4365 C CA  . ASN   B 40  ? 0.1543 0.1668 0.1563 0.0005  -0.0015 -0.0105 40  ASN   B CA  
4366 C C   . ASN   B 40  ? 0.1588 0.1637 0.1457 0.0074  -0.0032 -0.0025 40  ASN   B C   
4367 O O   . ASN   B 40  ? 0.1600 0.1547 0.1513 0.0084  -0.0101 0.0013  40  ASN   B O   
4368 C CB  . ASN   B 40  ? 0.1693 0.1654 0.1744 0.0111  -0.0123 0.0095  40  ASN   B CB  
4369 C CG  . ASN   B 40  ? 0.1750 0.1720 0.2055 0.0072  -0.0237 0.0203  40  ASN   B CG  
4370 O OD1 . ASN   B 40  ? 0.1783 0.1661 0.2760 0.0053  -0.0323 0.0223  40  ASN   B OD1 
4371 N ND2 . ASN   B 40  ? 0.1760 0.1755 0.2066 0.0029  -0.0182 0.0187  40  ASN   B ND2 
4378 N N   . VAL   B 41  ? 0.1701 0.1659 0.1512 0.0103  0.0073  -0.0012 41  VAL   B N   
4379 C CA  . VAL   B 41  ? 0.1774 0.1803 0.1546 0.0105  0.0054  -0.0087 41  VAL   B CA  
4380 C C   . VAL   B 41  ? 0.1780 0.1796 0.1435 0.0160  -0.0032 -0.0092 41  VAL   B C   
4381 O O   . VAL   B 41  ? 0.1778 0.1775 0.1462 0.0154  -0.0141 -0.0172 41  VAL   B O   
4382 C CB  . VAL   B 41  ? 0.1913 0.1986 0.1710 0.0015  0.0186  -0.0218 41  VAL   B CB  
4383 C CG1 . VAL   B 41  ? 0.1856 0.2090 0.1902 0.0008  0.0336  -0.0282 41  VAL   B CG1 
4384 C CG2 . VAL   B 41  ? 0.2033 0.2164 0.1832 -0.0038 0.0231  -0.0189 41  VAL   B CG2 
4394 N N   . TYR   B 42  ? 0.1879 0.1809 0.1419 0.0188  -0.0170 0.0089  42  TYR   B N   
4395 C CA  . TYR   B 42  ? 0.1932 0.1888 0.1574 0.0151  -0.0305 -0.0122 42  TYR   B CA  
4396 C C   . TYR   B 42  ? 0.1731 0.1665 0.1684 0.0204  -0.0286 -0.0149 42  TYR   B C   
4397 O O   . TYR   B 42  ? 0.1783 0.1729 0.1974 0.0135  -0.0331 -0.0181 42  TYR   B O   
4398 C CB  . TYR   B 42  ? 0.2189 0.2191 0.1810 0.0105  -0.0369 0.0049  42  TYR   B CB  
4399 C CG  . TYR   B 42  ? 0.2210 0.2359 0.1723 0.0001  -0.0354 0.0141  42  TYR   B CG  
4400 C CD1 . TYR   B 42  ? 0.2175 0.2315 0.1477 -0.0100 -0.0135 -0.0037 42  TYR   B CD1 
4401 C CD2 . TYR   B 42  ? 0.2370 0.2441 0.2065 0.0051  -0.0192 0.0141  42  TYR   B CD2 
4402 C CE1 . TYR   B 42  ? 0.2274 0.2403 0.1724 -0.0014 -0.0113 -0.0002 42  TYR   B CE1 
4403 C CE2 . TYR   B 42  ? 0.2435 0.2523 0.1965 0.0123  0.0024  0.0262  42  TYR   B CE2 
4404 C CZ  . TYR   B 42  ? 0.2513 0.2630 0.1937 0.0203  0.0091  0.0089  42  TYR   B CZ  
4405 O OH  . TYR   B 42  ? 0.2860 0.3008 0.2473 0.0361  0.0230  0.0205  42  TYR   B OH  
4415 N N   . LEU   B 43  ? 0.1576 0.1481 0.1581 0.0107  -0.0168 -0.0139 43  LEU   B N   
4416 C CA  . LEU   B 43  ? 0.1598 0.1506 0.1524 0.0069  -0.0042 -0.0045 43  LEU   B CA  
4417 C C   . LEU   B 43  ? 0.1651 0.1532 0.1520 0.0035  -0.0124 0.0024  43  LEU   B C   
4418 O O   . LEU   B 43  ? 0.1595 0.1552 0.1793 0.0052  -0.0208 0.0098  43  LEU   B O   
4419 C CB  . LEU   B 43  ? 0.1610 0.1461 0.1612 0.0016  -0.0231 -0.0063 43  LEU   B CB  
4420 C CG  . LEU   B 43  ? 0.1688 0.1440 0.1537 0.0011  -0.0297 -0.0047 43  LEU   B CG  
4421 C CD1 . LEU   B 43  ? 0.1735 0.1484 0.1920 -0.0037 -0.0385 -0.0003 43  LEU   B CD1 
4422 C CD2 . LEU   B 43  ? 0.1631 0.1402 0.1638 0.0001  -0.0237 -0.0060 43  LEU   B CD2 
4434 N N   . LYS   B 44  ? 0.1569 0.1455 0.1632 0.0085  -0.0029 -0.0061 44  LYS   B N   
4435 C CA  . LYS   B 44  ? 0.1729 0.1567 0.1635 0.0090  -0.0127 0.0097  44  LYS   B CA  
4436 C C   . LYS   B 44  ? 0.1594 0.1543 0.1633 0.0125  -0.0092 -0.0008 44  LYS   B C   
4437 O O   . LYS   B 44  ? 0.1847 0.1521 0.1955 0.0055  -0.0055 0.0005  44  LYS   B O   
4438 C CB  . LYS   B 44  ? 0.2058 0.1772 0.1718 0.0184  -0.0293 0.0074  44  LYS   B CB  
4439 C CG  . LYS   B 44  ? 0.2430 0.2060 0.2091 0.0152  -0.0571 0.0073  44  LYS   B CG  
4440 C CD  . LYS   B 44  ? 0.2794 0.2354 0.2747 -0.0002 -0.0641 0.0069  44  LYS   B CD  
4441 C CE  . LYS   B 44  ? 0.3104 0.2657 0.3229 -0.0084 -0.0637 0.0126  44  LYS   B CE  
4442 N NZ  . LYS   B 44  ? 0.3280 0.2777 0.3470 -0.0068 -0.0643 0.0272  44  LYS   B NZ  
4456 N N   . HIS   B 45  ? 0.1537 0.1585 0.1472 0.0049  -0.0169 0.0094  45  HIS   B N   
4457 C CA  . HIS   B 45  ? 0.1619 0.1525 0.1551 0.0109  -0.0100 0.0005  45  HIS   B CA  
4458 C C   . HIS   B 45  ? 0.1872 0.1742 0.1939 0.0139  -0.0174 -0.0057 45  HIS   B C   
4459 O O   . HIS   B 45  ? 0.1961 0.2004 0.2400 0.0402  0.0066  0.0047  45  HIS   B O   
4460 C CB  . HIS   B 45  ? 0.1546 0.1579 0.1674 0.0011  -0.0072 -0.0028 45  HIS   B CB  
4461 C CG  . HIS   B 45  ? 0.1560 0.1512 0.1562 -0.0053 -0.0089 0.0050  45  HIS   B CG  
4462 N ND1 . HIS   B 45  ? 0.1584 0.1470 0.1677 0.0003  -0.0204 -0.0060 45  HIS   B ND1 
4463 C CD2 . HIS   B 45  ? 0.1665 0.1523 0.1838 -0.0098 -0.0153 0.0058  45  HIS   B CD2 
4464 C CE1 . HIS   B 45  ? 0.1701 0.1306 0.1695 -0.0024 -0.0271 -0.0063 45  HIS   B CE1 
4465 N NE2 . HIS   B 45  ? 0.1760 0.1453 0.1690 -0.0034 -0.0199 -0.0014 45  HIS   B NE2 
4473 N N   A GLY   B 46  ? 0.1882 0.1649 0.2205 0.0158  -0.0386 0.0004  46  GLY   B N   
4474 N N   B GLY   B 46  ? 0.1927 0.1844 0.2078 0.0151  -0.0220 0.0001  46  GLY   B N   
4475 C CA  A GLY   B 46  ? 0.1994 0.1803 0.2518 0.0142  -0.0525 0.0028  46  GLY   B CA  
4476 C CA  B GLY   B 46  ? 0.1979 0.1957 0.2249 0.0134  -0.0251 0.0053  46  GLY   B CA  
4477 C C   A GLY   B 46  ? 0.2001 0.2017 0.2942 0.0215  -0.0443 0.0039  46  GLY   B C   
4478 C C   B GLY   B 46  ? 0.2002 0.2057 0.2491 0.0115  -0.0240 0.0078  46  GLY   B C   
4479 O O   A GLY   B 46  ? 0.2131 0.2231 0.3813 0.0258  -0.0092 -0.0221 46  GLY   B O   
4480 O O   B GLY   B 46  ? 0.2043 0.2114 0.2557 0.0118  -0.0205 0.0120  46  GLY   B O   
4487 N N   . GLY   B 47  ? 0.1993 0.2104 0.2732 0.0064  -0.0200 0.0041  47  GLY   B N   
4488 C CA  . GLY   B 47  ? 0.1894 0.1776 0.2399 -0.0025 -0.0185 0.0082  47  GLY   B CA  
4489 C C   . GLY   B 47  ? 0.1730 0.1567 0.2075 -0.0008 -0.0024 0.0162  47  GLY   B C   
4490 O O   . GLY   B 47  ? 0.1864 0.1435 0.2026 0.0043  -0.0114 0.0166  47  GLY   B O   
4495 N N   . GLY   B 48  ? 0.1563 0.1520 0.2057 0.0028  -0.0093 0.0204  48  GLY   B N   
4496 C CA  . GLY   B 48  ? 0.1539 0.1461 0.2015 -0.0051 -0.0059 0.0154  48  GLY   B CA  
4497 C C   . GLY   B 48  ? 0.1455 0.1394 0.1895 -0.0005 0.0032  0.0061  48  GLY   B C   
4498 O O   . GLY   B 48  ? 0.1414 0.1494 0.2047 0.0040  -0.0115 0.0140  48  GLY   B O   
4502 N N   . VAL   B 49  ? 0.1456 0.1424 0.1830 0.0095  0.0030  0.0039  49  VAL   B N   
4503 C CA  . VAL   B 49  ? 0.1531 0.1502 0.1791 0.0122  -0.0166 -0.0058 49  VAL   B CA  
4504 C C   . VAL   B 49  ? 0.1468 0.1427 0.1563 0.0144  -0.0057 0.0018  49  VAL   B C   
4505 O O   . VAL   B 49  ? 0.1526 0.1498 0.1642 0.0058  -0.0033 0.0044  49  VAL   B O   
4506 C CB  . VAL   B 49  ? 0.1572 0.1684 0.1985 0.0015  -0.0259 0.0057  49  VAL   B CB  
4507 C CG1 . VAL   B 49  ? 0.1570 0.1806 0.1902 0.0062  -0.0300 -0.0053 49  VAL   B CG1 
4508 C CG2 . VAL   B 49  ? 0.1750 0.1848 0.2270 -0.0080 -0.0417 0.0046  49  VAL   B CG2 
4518 N N   . ALA   B 50  ? 0.1416 0.1357 0.1701 0.0046  -0.0043 0.0039  50  ALA   B N   
4519 C CA  . ALA   B 50  ? 0.1361 0.1305 0.1664 0.0074  -0.0065 0.0055  50  ALA   B CA  
4520 C C   . ALA   B 50  ? 0.1482 0.1357 0.1617 0.0067  -0.0022 0.0044  50  ALA   B C   
4521 O O   . ALA   B 50  ? 0.1462 0.1372 0.1511 0.0069  -0.0056 0.0030  50  ALA   B O   
4522 C CB  . ALA   B 50  ? 0.1479 0.1334 0.1662 0.0033  0.0035  0.0093  50  ALA   B CB  
4528 N N   . GLY   B 51  ? 0.1396 0.1474 0.1783 0.0129  -0.0128 0.0115  51  GLY   B N   
4529 C CA  . GLY   B 51  ? 0.1445 0.1545 0.2025 0.0168  -0.0132 0.0097  51  GLY   B CA  
4530 C C   . GLY   B 51  ? 0.1448 0.1492 0.1953 0.0206  -0.0071 0.0063  51  GLY   B C   
4531 O O   . GLY   B 51  ? 0.1467 0.1611 0.2143 0.0155  -0.0132 0.0015  51  GLY   B O   
4535 N N   . ALA   B 52  ? 0.1404 0.1430 0.1900 0.0181  -0.0060 0.0154  52  ALA   B N   
4536 C CA  . ALA   B 52  ? 0.1496 0.1504 0.1919 0.0195  0.0045  0.0079  52  ALA   B CA  
4537 C C   . ALA   B 52  ? 0.1399 0.1527 0.1743 0.0111  -0.0016 0.0059  52  ALA   B C   
4538 O O   . ALA   B 52  ? 0.1443 0.1574 0.1899 0.0131  0.0077  0.0037  52  ALA   B O   
4539 C CB  . ALA   B 52  ? 0.1681 0.1518 0.1922 0.0047  0.0050  0.0042  52  ALA   B CB  
4545 N N   . LEU   B 53  ? 0.1317 0.1478 0.1714 0.0132  0.0001  0.0044  53  LEU   B N   
4546 C CA  . LEU   B 53  ? 0.1353 0.1538 0.1771 0.0102  -0.0029 0.0066  53  LEU   B CA  
4547 C C   . LEU   B 53  ? 0.1459 0.1424 0.1743 0.0132  0.0063  0.0111  53  LEU   B C   
4548 O O   . LEU   B 53  ? 0.1473 0.1544 0.1806 0.0022  0.0044  0.0201  53  LEU   B O   
4549 C CB  . LEU   B 53  ? 0.1330 0.1583 0.1798 0.0085  0.0003  0.0217  53  LEU   B CB  
4550 C CG  . LEU   B 53  ? 0.1321 0.1721 0.1726 0.0020  0.0019  0.0294  53  LEU   B CG  
4551 C CD1 . LEU   B 53  ? 0.1434 0.1938 0.2048 0.0114  -0.0036 0.0096  53  LEU   B CD1 
4552 C CD2 . LEU   B 53  ? 0.1558 0.1999 0.2054 -0.0076 -0.0049 -0.0024 53  LEU   B CD2 
4564 N N   . ASN   B 54  ? 0.1457 0.1318 0.1667 0.0062  0.0051  0.0091  54  ASN   B N   
4565 C CA  . ASN   B 54  ? 0.1488 0.1484 0.1833 0.0035  -0.0027 0.0016  54  ASN   B CA  
4566 C C   . ASN   B 54  ? 0.1384 0.1488 0.1939 0.0049  -0.0002 0.0046  54  ASN   B C   
4567 O O   . ASN   B 54  ? 0.1396 0.1549 0.2004 -0.0000 0.0023  0.0013  54  ASN   B O   
4568 C CB  . ASN   B 54  ? 0.1498 0.1601 0.1970 0.0083  0.0115  0.0099  54  ASN   B CB  
4569 C CG  . ASN   B 54  ? 0.1424 0.1711 0.1884 0.0063  0.0025  0.0042  54  ASN   B CG  
4570 O OD1 . ASN   B 54  ? 0.1444 0.1684 0.2051 -0.0015 -0.0165 -0.0139 54  ASN   B OD1 
4571 N ND2 . ASN   B 54  ? 0.1536 0.1920 0.2123 0.0021  -0.0269 0.0192  54  ASN   B ND2 
4578 N N   . LYS   B 55  ? 0.1378 0.1585 0.2095 0.0073  0.0029  0.0065  55  LYS   B N   
4579 C CA  . LYS   B 55  ? 0.1432 0.1711 0.2296 0.0178  -0.0009 0.0069  55  LYS   B CA  
4580 C C   . LYS   B 55  ? 0.1385 0.1691 0.2204 0.0128  0.0082  0.0046  55  LYS   B C   
4581 O O   . LYS   B 55  ? 0.1381 0.1869 0.2357 0.0098  0.0085  0.0009  55  LYS   B O   
4582 C CB  . LYS   B 55  ? 0.1553 0.1820 0.2619 0.0212  0.0070  0.0119  55  LYS   B CB  
4583 C CG  . LYS   B 55  ? 0.1946 0.2143 0.3302 0.0283  0.0153  0.0197  55  LYS   B CG  
4584 C CD  . LYS   B 55  ? 0.2352 0.2405 0.3950 0.0411  0.0270  0.0329  55  LYS   B CD  
4585 C CE  . LYS   B 55  ? 0.2652 0.2652 0.4495 0.0448  0.0428  0.0352  55  LYS   B CE  
4586 N NZ  . LYS   B 55  ? 0.2775 0.2842 0.4793 0.0465  0.0296  0.0433  55  LYS   B NZ  
4600 N N   . ALA   B 56  ? 0.1397 0.1739 0.2030 0.0116  0.0020  0.0022  56  ALA   B N   
4601 C CA  . ALA   B 56  ? 0.1488 0.1916 0.2054 0.0067  0.0044  0.0005  56  ALA   B CA  
4602 C C   . ALA   B 56  ? 0.1521 0.1862 0.1967 0.0044  0.0116  0.0041  56  ALA   B C   
4603 O O   . ALA   B 56  ? 0.1679 0.1995 0.2193 0.0093  0.0358  0.0094  56  ALA   B O   
4604 C CB  . ALA   B 56  ? 0.1595 0.2198 0.2015 -0.0054 -0.0003 -0.0111 56  ALA   B CB  
4610 N N   . THR   B 57  ? 0.1426 0.1770 0.2010 0.0035  0.0183  0.0079  57  THR   B N   
4611 C CA  . THR   B 57  ? 0.1514 0.1761 0.1980 0.0038  0.0277  0.0110  57  THR   B CA  
4612 C C   . THR   B 57  ? 0.1522 0.1858 0.2214 0.0012  0.0241  0.0070  57  THR   B C   
4613 O O   . THR   B 57  ? 0.1597 0.1877 0.2273 -0.0160 0.0182  0.0120  57  THR   B O   
4614 C CB  . THR   B 57  ? 0.1578 0.1600 0.1852 0.0021  0.0212  0.0177  57  THR   B CB  
4615 O OG1 . THR   B 57  ? 0.1584 0.1534 0.2082 -0.0007 0.0217  0.0095  57  THR   B OG1 
4616 C CG2 . THR   B 57  ? 0.1527 0.1657 0.1877 -0.0038 0.0153  0.0164  57  THR   B CG2 
4624 N N   . ASN   B 58  ? 0.1381 0.2050 0.2386 -0.0113 0.0076  -0.0092 58  ASN   B N   
4625 C CA  . ASN   B 58  ? 0.1658 0.2537 0.2781 -0.0214 0.0323  0.0004  58  ASN   B CA  
4626 C C   . ASN   B 58  ? 0.1458 0.2277 0.2392 -0.0183 0.0036  0.0092  58  ASN   B C   
4627 O O   . ASN   B 58  ? 0.1511 0.2352 0.2504 -0.0240 0.0042  -0.0025 58  ASN   B O   
4628 C CB  . ASN   B 58  ? 0.2470 0.3341 0.4083 -0.0389 0.0726  0.0081  58  ASN   B CB  
4629 C CG  . ASN   B 58  ? 0.3730 0.4144 0.5499 -0.0429 0.0834  0.0261  58  ASN   B CG  
4630 O OD1 . ASN   B 58  ? 0.4001 0.4429 0.6042 -0.0418 0.0828  0.0297  58  ASN   B OD1 
4631 N ND2 . ASN   B 58  ? 0.5215 0.5215 0.6035 -0.0464 0.0871  0.0323  58  ASN   B ND2 
4638 N N   . ASN   B 59  ? 0.1414 0.2056 0.2171 -0.0151 0.0016  0.0150  59  ASN   B N   
4639 C CA  . ASN   B 59  ? 0.1444 0.2044 0.2059 -0.0104 -0.0132 0.0237  59  ASN   B CA  
4640 C C   . ASN   B 59  ? 0.1449 0.1917 0.2047 -0.0142 -0.0156 0.0047  59  ASN   B C   
4641 O O   . ASN   B 59  ? 0.1460 0.1923 0.2061 -0.0141 -0.0116 0.0007  59  ASN   B O   
4642 C CB  . ASN   B 59  ? 0.1561 0.2222 0.2312 -0.0002 -0.0240 0.0189  59  ASN   B CB  
4643 C CG  . ASN   B 59  ? 0.1639 0.2402 0.2462 0.0000  -0.0350 0.0144  59  ASN   B CG  
4644 O OD1 . ASN   B 59  ? 0.1680 0.2455 0.2501 0.0023  -0.0281 0.0246  59  ASN   B OD1 
4645 N ND2 . ASN   B 59  ? 0.1741 0.2522 0.2608 -0.0036 -0.0430 0.0131  59  ASN   B ND2 
4652 N N   . ALA   B 60  ? 0.1497 0.1795 0.2158 -0.0099 -0.0030 0.0064  60  ALA   B N   
4653 C CA  . ALA   B 60  ? 0.1538 0.1721 0.2048 -0.0187 -0.0027 0.0096  60  ALA   B CA  
4654 C C   . ALA   B 60  ? 0.1516 0.1618 0.1823 -0.0117 -0.0077 0.0112  60  ALA   B C   
4655 O O   . ALA   B 60  ? 0.1602 0.1642 0.1952 -0.0189 0.0003  0.0038  60  ALA   B O   
4656 C CB  . ALA   B 60  ? 0.1670 0.1714 0.2326 -0.0198 0.0082  0.0164  60  ALA   B CB  
4662 N N   . MET   B 61  ? 0.1421 0.1549 0.1874 -0.0083 0.0008  0.0111  61  MET   B N   
4663 C CA  . MET   B 61  ? 0.1370 0.1508 0.1802 -0.0090 -0.0116 0.0074  61  MET   B CA  
4664 C C   . MET   B 61  ? 0.1471 0.1473 0.1848 -0.0084 -0.0161 0.0135  61  MET   B C   
4665 O O   . MET   B 61  ? 0.1499 0.1456 0.1669 -0.0031 -0.0065 -0.0060 61  MET   B O   
4666 C CB  . MET   B 61  ? 0.1309 0.1529 0.1903 -0.0029 -0.0076 -0.0002 61  MET   B CB  
4667 C CG  . MET   B 61  ? 0.1407 0.1547 0.1731 -0.0059 -0.0080 0.0088  61  MET   B CG  
4668 S SD  . MET   B 61  ? 0.1419 0.1512 0.1970 -0.0027 -0.0050 -0.0050 61  MET   B SD  
4669 C CE  . MET   B 61  ? 0.1499 0.1804 0.2139 -0.0046 0.0081  -0.0283 61  MET   B CE  
4679 N N   . GLN   B 62  ? 0.1489 0.1522 0.1778 -0.0041 -0.0217 0.0160  62  GLN   B N   
4680 C CA  . GLN   B 62  ? 0.1456 0.1548 0.1800 0.0005  -0.0197 0.0051  62  GLN   B CA  
4681 C C   . GLN   B 62  ? 0.1489 0.1616 0.1897 -0.0031 -0.0184 0.0011  62  GLN   B C   
4682 O O   . GLN   B 62  ? 0.1610 0.1648 0.1859 -0.0047 -0.0305 -0.0118 62  GLN   B O   
4683 C CB  . GLN   B 62  ? 0.1498 0.1618 0.1861 -0.0022 -0.0125 0.0067  62  GLN   B CB  
4684 C CG  . GLN   B 62  ? 0.1503 0.1687 0.1947 0.0020  -0.0234 0.0013  62  GLN   B CG  
4685 C CD  . GLN   B 62  ? 0.1508 0.1658 0.1797 0.0042  -0.0344 0.0078  62  GLN   B CD  
4686 O OE1 . GLN   B 62  ? 0.1569 0.1622 0.1946 0.0007  -0.0354 -0.0034 62  GLN   B OE1 
4687 N NE2 . GLN   B 62  ? 0.1565 0.1731 0.1913 0.0058  -0.0282 -0.0031 62  GLN   B NE2 
4696 N N   . VAL   B 63  ? 0.1460 0.1672 0.1939 -0.0052 -0.0220 -0.0071 63  VAL   B N   
4697 C CA  . VAL   B 63  ? 0.1600 0.1676 0.2177 -0.0138 -0.0347 -0.0103 63  VAL   B CA  
4698 C C   . VAL   B 63  ? 0.1675 0.1543 0.2001 -0.0203 -0.0399 -0.0185 63  VAL   B C   
4699 O O   . VAL   B 63  ? 0.1765 0.1599 0.2217 -0.0182 -0.0534 -0.0145 63  VAL   B O   
4700 C CB  . VAL   B 63  ? 0.1601 0.1883 0.2531 -0.0204 -0.0336 -0.0096 63  VAL   B CB  
4701 C CG1 . VAL   B 63  ? 0.1693 0.1926 0.2662 -0.0264 -0.0269 -0.0104 63  VAL   B CG1 
4702 C CG2 . VAL   B 63  ? 0.1583 0.2093 0.2594 -0.0122 -0.0314 -0.0117 63  VAL   B CG2 
4712 N N   . GLU   B 64  ? 0.1661 0.1473 0.1977 -0.0086 -0.0352 -0.0112 64  GLU   B N   
4713 C CA  . GLU   B 64  ? 0.1599 0.1420 0.1917 -0.0135 -0.0369 -0.0060 64  GLU   B CA  
4714 C C   . GLU   B 64  ? 0.1524 0.1461 0.1818 -0.0081 -0.0319 -0.0098 64  GLU   B C   
4715 O O   . GLU   B 64  ? 0.1652 0.1554 0.1746 -0.0116 -0.0309 -0.0085 64  GLU   B O   
4716 C CB  . GLU   B 64  ? 0.1564 0.1534 0.1893 -0.0142 -0.0276 -0.0027 64  GLU   B CB  
4717 C CG  . GLU   B 64  ? 0.1651 0.1565 0.1836 -0.0258 -0.0296 -0.0074 64  GLU   B CG  
4718 C CD  . GLU   B 64  ? 0.1686 0.1652 0.1927 -0.0321 -0.0339 0.0008  64  GLU   B CD  
4719 O OE1 . GLU   B 64  ? 0.1740 0.1843 0.1988 -0.0329 -0.0259 -0.0185 64  GLU   B OE1 
4720 O OE2 . GLU   B 64  ? 0.1902 0.1757 0.2003 -0.0288 -0.0506 -0.0070 64  GLU   B OE2 
4727 N N   . SER   B 65  ? 0.1532 0.1412 0.1867 -0.0121 -0.0212 -0.0095 65  SER   B N   
4728 C CA  . SER   B 65  ? 0.1526 0.1414 0.1911 -0.0075 -0.0276 -0.0127 65  SER   B CA  
4729 C C   . SER   B 65  ? 0.1581 0.1415 0.1771 -0.0011 -0.0371 -0.0174 65  SER   B C   
4730 O O   . SER   B 65  ? 0.1645 0.1544 0.1788 0.0016  -0.0320 -0.0236 65  SER   B O   
4731 C CB  . SER   B 65  ? 0.1604 0.1486 0.1817 -0.0098 -0.0211 -0.0118 65  SER   B CB  
4732 O OG  . SER   B 65  ? 0.1568 0.1475 0.1804 -0.0056 -0.0149 -0.0253 65  SER   B OG  
4738 N N   . ASP   B 66  ? 0.1715 0.1478 0.1732 -0.0035 -0.0344 -0.0214 66  ASP   B N   
4739 C CA  . ASP   B 66  ? 0.1751 0.1565 0.1768 -0.0029 -0.0344 -0.0163 66  ASP   B CA  
4740 C C   . ASP   B 66  ? 0.1714 0.1609 0.1780 -0.0063 -0.0286 -0.0173 66  ASP   B C   
4741 O O   . ASP   B 66  ? 0.1755 0.1734 0.1890 0.0057  -0.0281 -0.0283 66  ASP   B O   
4742 C CB  . ASP   B 66  ? 0.1900 0.1687 0.2025 0.0061  -0.0415 -0.0162 66  ASP   B CB  
4743 C CG  . ASP   B 66  ? 0.2202 0.1885 0.2209 0.0142  -0.0503 0.0039  66  ASP   B CG  
4744 O OD1 . ASP   B 66  ? 0.2462 0.1845 0.2306 0.0087  -0.0490 0.0075  66  ASP   B OD1 
4745 O OD2 . ASP   B 66  ? 0.2348 0.2136 0.2787 0.0345  -0.0546 0.0018  66  ASP   B OD2 
4750 N N   . ASP   B 67  ? 0.1725 0.1551 0.1715 -0.0089 -0.0287 -0.0164 67  ASP   B N   
4751 C CA  . ASP   B 67  ? 0.1847 0.1524 0.1836 -0.0112 -0.0247 -0.0120 67  ASP   B CA  
4752 C C   . ASP   B 67  ? 0.1823 0.1505 0.1889 0.0008  -0.0241 -0.0136 67  ASP   B C   
4753 O O   . ASP   B 67  ? 0.1875 0.1622 0.1984 0.0016  -0.0227 -0.0222 67  ASP   B O   
4754 C CB  . ASP   B 67  ? 0.2037 0.1610 0.2085 -0.0145 -0.0371 -0.0131 67  ASP   B CB  
4755 C CG  . ASP   B 67  ? 0.2424 0.1694 0.2199 -0.0087 -0.0657 -0.0168 67  ASP   B CG  
4756 O OD1 . ASP   B 67  ? 0.2734 0.1757 0.2369 -0.0119 -0.0721 -0.0108 67  ASP   B OD1 
4757 O OD2 . ASP   B 67  ? 0.2611 0.1753 0.2398 0.0072  -0.0666 -0.0123 67  ASP   B OD2 
4762 N N   . TYR   B 68  ? 0.1735 0.1533 0.1889 0.0003  -0.0394 -0.0257 68  TYR   B N   
4763 C CA  . TYR   B 68  ? 0.1721 0.1703 0.2002 0.0038  -0.0417 -0.0320 68  TYR   B CA  
4764 C C   . TYR   B 68  ? 0.1631 0.1692 0.1855 0.0041  -0.0401 -0.0373 68  TYR   B C   
4765 O O   . TYR   B 68  ? 0.1730 0.1769 0.2021 0.0082  -0.0354 -0.0517 68  TYR   B O   
4766 C CB  . TYR   B 68  ? 0.1772 0.1893 0.2045 0.0092  -0.0487 -0.0417 68  TYR   B CB  
4767 C CG  . TYR   B 68  ? 0.1879 0.2063 0.2145 0.0141  -0.0393 -0.0637 68  TYR   B CG  
4768 C CD1 . TYR   B 68  ? 0.1896 0.2089 0.2381 -0.0040 -0.0331 -0.0817 68  TYR   B CD1 
4769 C CD2 . TYR   B 68  ? 0.1930 0.2274 0.2301 0.0229  -0.0494 -0.0610 68  TYR   B CD2 
4770 C CE1 . TYR   B 68  ? 0.1940 0.2291 0.2578 -0.0001 -0.0250 -0.0836 68  TYR   B CE1 
4771 C CE2 . TYR   B 68  ? 0.1952 0.2337 0.2538 0.0202  -0.0366 -0.0743 68  TYR   B CE2 
4772 C CZ  . TYR   B 68  ? 0.1895 0.2343 0.2614 0.0064  -0.0363 -0.0828 68  TYR   B CZ  
4773 O OH  . TYR   B 68  ? 0.1884 0.2522 0.2878 0.0046  -0.0341 -0.0588 68  TYR   B OH  
4783 N N   . ILE   B 69  ? 0.1649 0.1598 0.1951 0.0020  -0.0376 -0.0356 69  ILE   B N   
4784 C CA  . ILE   B 69  ? 0.1710 0.1637 0.1992 -0.0030 -0.0290 -0.0387 69  ILE   B CA  
4785 C C   . ILE   B 69  ? 0.1744 0.1643 0.1895 0.0066  -0.0388 -0.0293 69  ILE   B C   
4786 O O   . ILE   B 69  ? 0.1750 0.1763 0.1831 0.0019  -0.0217 -0.0298 69  ILE   B O   
4787 C CB  . ILE   B 69  ? 0.1774 0.1699 0.2177 -0.0083 0.0035  -0.0292 69  ILE   B CB  
4788 C CG1 . ILE   B 69  ? 0.1792 0.1742 0.2336 -0.0052 0.0084  -0.0328 69  ILE   B CG1 
4789 C CG2 . ILE   B 69  ? 0.1932 0.1843 0.2343 -0.0050 0.0013  -0.0200 69  ILE   B CG2 
4790 C CD1 . ILE   B 69  ? 0.1779 0.1816 0.2428 -0.0162 -0.0001 -0.0381 69  ILE   B CD1 
4802 N N   . ALA   B 70  ? 0.1729 0.1638 0.1886 0.0085  -0.0458 -0.0244 70  ALA   B N   
4803 C CA  . ALA   B 70  ? 0.1768 0.1684 0.1812 0.0058  -0.0511 -0.0252 70  ALA   B CA  
4804 C C   . ALA   B 70  ? 0.1840 0.1603 0.1997 0.0016  -0.0519 -0.0307 70  ALA   B C   
4805 O O   . ALA   B 70  ? 0.1948 0.1631 0.1924 0.0031  -0.0467 -0.0298 70  ALA   B O   
4806 C CB  . ALA   B 70  ? 0.1781 0.1862 0.1828 0.0010  -0.0472 -0.0198 70  ALA   B CB  
4812 N N   . THR   B 71  ? 0.1911 0.1610 0.2033 0.0071  -0.0604 -0.0352 71  THR   B N   
4813 C CA  . THR   B 71  ? 0.2030 0.1702 0.2213 0.0088  -0.0720 -0.0332 71  THR   B CA  
4814 C C   . THR   B 71  ? 0.1981 0.1743 0.2363 0.0262  -0.0679 -0.0541 71  THR   B C   
4815 O O   . THR   B 71  ? 0.2076 0.1805 0.2753 0.0266  -0.0604 -0.0676 71  THR   B O   
4816 C CB  . THR   B 71  ? 0.2261 0.1957 0.2348 -0.0011 -0.0840 -0.0120 71  THR   B CB  
4817 O OG1 . THR   B 71  ? 0.2407 0.2236 0.2739 -0.0181 -0.0766 0.0111  71  THR   B OG1 
4818 C CG2 . THR   B 71  ? 0.2455 0.1925 0.2534 0.0043  -0.0674 0.0023  71  THR   B CG2 
4826 N N   . ASN   B 72  ? 0.1834 0.1805 0.2287 0.0174  -0.0648 -0.0726 72  ASN   B N   
4827 C CA  . ASN   B 72  ? 0.1857 0.1963 0.2267 0.0158  -0.0502 -0.0738 72  ASN   B CA  
4828 C C   . ASN   B 72  ? 0.1835 0.2072 0.2386 0.0022  -0.0265 -0.0657 72  ASN   B C   
4829 O O   . ASN   B 72  ? 0.1865 0.2218 0.2675 0.0077  -0.0135 -0.0720 72  ASN   B O   
4830 C CB  . ASN   B 72  ? 0.1947 0.2043 0.2398 0.0165  -0.0616 -0.0635 72  ASN   B CB  
4831 C CG  . ASN   B 72  ? 0.2105 0.2199 0.2510 0.0322  -0.0646 -0.0365 72  ASN   B CG  
4832 O OD1 . ASN   B 72  ? 0.2279 0.2376 0.2532 0.0195  -0.0458 -0.0366 72  ASN   B OD1 
4833 N ND2 . ASN   B 72  ? 0.2261 0.2261 0.2851 0.0459  -0.0531 -0.0001 72  ASN   B ND2 
4840 N N   . GLY   B 73  ? 0.1836 0.2041 0.2198 -0.0055 -0.0274 -0.0604 73  GLY   B N   
4841 C CA  . GLY   B 73  ? 0.1762 0.2126 0.1896 -0.0056 -0.0230 -0.0452 73  GLY   B CA  
4842 C C   . GLY   B 73  ? 0.1738 0.2090 0.1506 0.0022  -0.0242 -0.0429 73  GLY   B C   
4843 O O   . GLY   B 73  ? 0.1686 0.1992 0.1733 0.0089  -0.0209 -0.0356 73  GLY   B O   
4847 N N   . PRO   B 74  ? 0.1797 0.2208 0.1548 0.0027  -0.0260 -0.0377 74  PRO   B N   
4848 C CA  . PRO   B 74  ? 0.1704 0.2154 0.1562 0.0077  -0.0206 -0.0288 74  PRO   B CA  
4849 C C   . PRO   B 74  ? 0.1556 0.1983 0.1546 0.0076  -0.0233 -0.0258 74  PRO   B C   
4850 O O   . PRO   B 74  ? 0.1587 0.2027 0.1999 0.0114  -0.0177 -0.0358 74  PRO   B O   
4851 C CB  . PRO   B 74  ? 0.1929 0.2398 0.1583 0.0082  -0.0193 -0.0239 74  PRO   B CB  
4852 C CG  . PRO   B 74  ? 0.2089 0.2508 0.1931 0.0081  -0.0149 -0.0170 74  PRO   B CG  
4853 C CD  . PRO   B 74  ? 0.2025 0.2401 0.1873 0.0094  -0.0186 -0.0257 74  PRO   B CD  
4861 N N   . LEU   B 75  ? 0.1594 0.1833 0.1455 0.0101  -0.0225 -0.0252 75  LEU   B N   
4862 C CA  . LEU   B 75  ? 0.1593 0.1840 0.1467 0.0066  -0.0184 -0.0077 75  LEU   B CA  
4863 C C   . LEU   B 75  ? 0.1659 0.1955 0.1499 0.0059  -0.0107 -0.0068 75  LEU   B C   
4864 O O   . LEU   B 75  ? 0.1836 0.2086 0.1570 -0.0001 -0.0123 0.0065  75  LEU   B O   
4865 C CB  . LEU   B 75  ? 0.1644 0.1816 0.1309 -0.0052 -0.0244 0.0109  75  LEU   B CB  
4866 C CG  . LEU   B 75  ? 0.1961 0.1982 0.1512 -0.0339 -0.0188 0.0057  75  LEU   B CG  
4867 C CD1 . LEU   B 75  ? 0.2315 0.2154 0.1667 -0.0480 0.0012  -0.0011 75  LEU   B CD1 
4868 C CD2 . LEU   B 75  ? 0.2306 0.2203 0.2197 -0.0257 -0.0085 0.0121  75  LEU   B CD2 
4880 N N   . LYS   B 76  ? 0.1654 0.2182 0.1694 0.0029  -0.0046 0.0019  76  LYS   B N   
4881 C CA  . LYS   B 76  ? 0.1722 0.2269 0.2053 -0.0071 0.0166  0.0015  76  LYS   B CA  
4882 C C   . LYS   B 76  ? 0.1629 0.2101 0.1723 0.0021  0.0106  0.0199  76  LYS   B C   
4883 O O   . LYS   B 76  ? 0.1671 0.1906 0.1767 -0.0030 0.0060  0.0235  76  LYS   B O   
4884 C CB  . LYS   B 76  ? 0.1870 0.2372 0.2728 -0.0176 0.0376  -0.0277 76  LYS   B CB  
4885 C CG  . LYS   B 76  ? 0.2031 0.2553 0.3173 -0.0064 0.0249  -0.0317 76  LYS   B CG  
4886 C CD  . LYS   B 76  ? 0.2077 0.2616 0.3551 0.0021  0.0127  -0.0484 76  LYS   B CD  
4887 C CE  . LYS   B 76  ? 0.2163 0.2786 0.3956 0.0106  0.0065  -0.0561 76  LYS   B CE  
4888 N NZ  . LYS   B 76  ? 0.2176 0.2834 0.4222 0.0117  -0.0148 -0.0729 76  LYS   B NZ  
4902 N N   . VAL   B 77  ? 0.1807 0.2201 0.1709 0.0171  0.0133  0.0262  77  VAL   B N   
4903 C CA  . VAL   B 77  ? 0.1755 0.2068 0.1866 0.0208  0.0255  0.0526  77  VAL   B CA  
4904 C C   . VAL   B 77  ? 0.1648 0.1860 0.1896 0.0228  0.0315  0.0384  77  VAL   B C   
4905 O O   . VAL   B 77  ? 0.1684 0.1796 0.1844 0.0295  0.0324  0.0264  77  VAL   B O   
4906 C CB  . VAL   B 77  ? 0.1830 0.2132 0.2218 0.0235  0.0392  0.0601  77  VAL   B CB  
4907 C CG1 . VAL   B 77  ? 0.1884 0.1990 0.2512 0.0154  0.0385  0.0707  77  VAL   B CG1 
4908 C CG2 . VAL   B 77  ? 0.2009 0.2424 0.2415 0.0206  0.0201  0.0615  77  VAL   B CG2 
4918 N N   . GLY   B 78  ? 0.1615 0.1732 0.1868 0.0164  0.0230  0.0298  78  GLY   B N   
4919 C CA  . GLY   B 78  ? 0.1549 0.1653 0.1805 0.0147  0.0242  0.0218  78  GLY   B CA  
4920 C C   . GLY   B 78  ? 0.1489 0.1583 0.1695 0.0122  0.0179  0.0236  78  GLY   B C   
4921 O O   . GLY   B 78  ? 0.1517 0.1546 0.1877 0.0210  0.0220  0.0297  78  GLY   B O   
4925 N N   . GLY   B 79  ? 0.1465 0.1631 0.1678 0.0108  0.0172  0.0128  79  GLY   B N   
4926 C CA  . GLY   B 79  ? 0.1472 0.1530 0.1632 0.0112  0.0112  0.0148  79  GLY   B CA  
4927 C C   . GLY   B 79  ? 0.1358 0.1501 0.1725 0.0114  0.0126  0.0049  79  GLY   B C   
4928 O O   . GLY   B 79  ? 0.1441 0.1462 0.1825 0.0109  0.0226  0.0195  79  GLY   B O   
4932 N N   . SER   B 80  ? 0.1343 0.1390 0.1790 0.0051  0.0211  0.0068  80  SER   B N   
4933 C CA  . SER   B 80  ? 0.1367 0.1355 0.1738 0.0045  0.0005  0.0057  80  SER   B CA  
4934 C C   . SER   B 80  ? 0.1404 0.1375 0.1613 0.0082  -0.0055 -0.0002 80  SER   B C   
4935 O O   . SER   B 80  ? 0.1507 0.1385 0.2015 0.0088  0.0052  -0.0042 80  SER   B O   
4936 C CB  . SER   B 80  ? 0.1388 0.1478 0.1838 -0.0059 -0.0022 0.0096  80  SER   B CB  
4937 O OG  . SER   B 80  ? 0.1470 0.1599 0.2008 -0.0017 -0.0160 0.0176  80  SER   B OG  
4943 N N   . CYS   B 81  ? 0.1380 0.1224 0.1628 0.0015  -0.0001 -0.0066 81  CYS   B N   
4944 C CA  . CYS   B 81  ? 0.1415 0.1251 0.1675 0.0033  -0.0101 -0.0064 81  CYS   B CA  
4945 C C   . CYS   B 81  ? 0.1388 0.1201 0.1492 -0.0018 -0.0106 -0.0034 81  CYS   B C   
4946 O O   . CYS   B 81  ? 0.1636 0.1226 0.1615 0.0048  -0.0025 -0.0059 81  CYS   B O   
4947 C CB  . CYS   B 81  ? 0.1617 0.1332 0.1655 -0.0061 -0.0086 -0.0042 81  CYS   B CB  
4948 S SG  . CYS   B 81  ? 0.1577 0.1517 0.1819 -0.0044 -0.0254 -0.0096 81  CYS   B SG  
4954 N N   . VAL   B 82  ? 0.1439 0.1211 0.1638 0.0002  -0.0107 -0.0038 82  VAL   B N   
4955 C CA  . VAL   B 82  ? 0.1449 0.1270 0.1619 -0.0046 -0.0106 -0.0026 82  VAL   B CA  
4956 C C   . VAL   B 82  ? 0.1559 0.1173 0.1774 -0.0031 -0.0144 -0.0050 82  VAL   B C   
4957 O O   . VAL   B 82  ? 0.1662 0.1193 0.1967 -0.0050 -0.0148 -0.0145 82  VAL   B O   
4958 C CB  . VAL   B 82  ? 0.1547 0.1469 0.1775 0.0001  -0.0151 0.0110  82  VAL   B CB  
4959 C CG1 . VAL   B 82  ? 0.1768 0.1732 0.1807 0.0056  -0.0143 0.0271  82  VAL   B CG1 
4960 C CG2 . VAL   B 82  ? 0.1649 0.1659 0.1896 -0.0056 -0.0273 0.0185  82  VAL   B CG2 
4970 N N   . LEU   B 83  ? 0.1427 0.1196 0.1756 -0.0138 -0.0204 -0.0106 83  LEU   B N   
4971 C CA  . LEU   B 83  ? 0.1448 0.1245 0.1606 -0.0133 -0.0177 -0.0050 83  LEU   B CA  
4972 C C   . LEU   B 83  ? 0.1415 0.1284 0.1540 -0.0140 -0.0196 -0.0034 83  LEU   B C   
4973 O O   . LEU   B 83  ? 0.1450 0.1342 0.1369 -0.0205 -0.0138 0.0052  83  LEU   B O   
4974 C CB  . LEU   B 83  ? 0.1528 0.1428 0.1609 -0.0158 -0.0288 -0.0153 83  LEU   B CB  
4975 C CG  . LEU   B 83  ? 0.1700 0.1592 0.1696 -0.0111 -0.0131 -0.0175 83  LEU   B CG  
4976 C CD1 . LEU   B 83  ? 0.1798 0.1691 0.1751 -0.0071 -0.0267 -0.0066 83  LEU   B CD1 
4977 C CD2 . LEU   B 83  ? 0.1923 0.1653 0.1885 -0.0060 -0.0098 -0.0396 83  LEU   B CD2 
4989 N N   . SER   B 84  ? 0.1524 0.1384 0.1829 -0.0212 -0.0160 -0.0021 84  SER   B N   
4990 C CA  . SER   B 84  ? 0.1507 0.1564 0.1737 -0.0273 -0.0157 0.0135  84  SER   B CA  
4991 C C   . SER   B 84  ? 0.1441 0.1686 0.1436 -0.0195 -0.0152 0.0156  84  SER   B C   
4992 O O   . SER   B 84  ? 0.1565 0.1511 0.1398 -0.0205 -0.0141 0.0001  84  SER   B O   
4993 C CB  . SER   B 84  ? 0.1705 0.1633 0.2173 -0.0294 0.0072  0.0240  84  SER   B CB  
4994 O OG  . SER   B 84  ? 0.1717 0.1763 0.2638 -0.0426 0.0117  0.0318  84  SER   B OG  
5000 N N   . GLY   B 85  ? 0.1461 0.1923 0.1458 -0.0241 -0.0165 0.0215  85  GLY   B N   
5001 C CA  . GLY   B 85  ? 0.1490 0.1985 0.1614 -0.0313 -0.0004 -0.0080 85  GLY   B CA  
5002 C C   . GLY   B 85  ? 0.1499 0.1779 0.1565 -0.0375 -0.0033 0.0043  85  GLY   B C   
5003 O O   . GLY   B 85  ? 0.1582 0.1773 0.1606 -0.0517 0.0135  -0.0107 85  GLY   B O   
5007 N N   . HIS   B 86  ? 0.1507 0.1601 0.1768 -0.0333 -0.0166 0.0102  86  HIS   B N   
5008 C CA  . HIS   B 86  ? 0.1471 0.1598 0.1797 -0.0307 -0.0164 0.0165  86  HIS   B CA  
5009 C C   . HIS   B 86  ? 0.1490 0.1710 0.1644 -0.0414 -0.0064 0.0342  86  HIS   B C   
5010 O O   . HIS   B 86  ? 0.1654 0.1838 0.1689 -0.0317 0.0055  0.0348  86  HIS   B O   
5011 C CB  . HIS   B 86  ? 0.1626 0.1620 0.1878 -0.0199 -0.0262 0.0103  86  HIS   B CB  
5012 C CG  . HIS   B 86  ? 0.1611 0.1678 0.1771 -0.0108 -0.0300 0.0129  86  HIS   B CG  
5013 N ND1 . HIS   B 86  ? 0.1727 0.1929 0.1941 -0.0202 -0.0355 -0.0006 86  HIS   B ND1 
5014 C CD2 . HIS   B 86  ? 0.1628 0.1762 0.1860 -0.0082 -0.0255 0.0056  86  HIS   B CD2 
5015 C CE1 . HIS   B 86  ? 0.1731 0.1964 0.1826 -0.0150 -0.0140 -0.0141 86  HIS   B CE1 
5016 N NE2 . HIS   B 86  ? 0.1715 0.1863 0.1737 -0.0059 -0.0129 0.0017  86  HIS   B NE2 
5024 N N   . ASN   B 87  ? 0.1511 0.1803 0.1708 -0.0282 -0.0018 0.0296  87  ASN   B N   
5025 C CA  . ASN   B 87  ? 0.1576 0.1940 0.1794 -0.0297 0.0258  0.0172  87  ASN   B CA  
5026 C C   . ASN   B 87  ? 0.1699 0.1792 0.1636 -0.0208 0.0302  0.0080  87  ASN   B C   
5027 O O   . ASN   B 87  ? 0.1919 0.1878 0.2001 -0.0202 0.0484  0.0072  87  ASN   B O   
5028 C CB  . ASN   B 87  ? 0.1594 0.2304 0.2085 -0.0253 0.0309  0.0089  87  ASN   B CB  
5029 C CG  . ASN   B 87  ? 0.1662 0.2458 0.2166 0.0033  0.0422  0.0353  87  ASN   B CG  
5030 O OD1 . ASN   B 87  ? 0.1647 0.2341 0.2064 0.0117  0.0466  0.0596  87  ASN   B OD1 
5031 N ND2 . ASN   B 87  ? 0.2025 0.2533 0.2380 0.0010  0.0432  0.0209  87  ASN   B ND2 
5038 N N   . LEU   B 88  ? 0.1586 0.1684 0.1585 -0.0260 0.0126  0.0113  88  LEU   B N   
5039 C CA  . LEU   B 88  ? 0.1702 0.1580 0.1668 -0.0330 0.0057  0.0007  88  LEU   B CA  
5040 C C   . LEU   B 88  ? 0.1749 0.1503 0.1642 -0.0359 -0.0024 0.0009  88  LEU   B C   
5041 O O   . LEU   B 88  ? 0.2032 0.1650 0.1946 -0.0186 -0.0264 -0.0099 88  LEU   B O   
5042 C CB  . LEU   B 88  ? 0.1837 0.1596 0.1830 -0.0396 -0.0054 0.0103  88  LEU   B CB  
5043 C CG  . LEU   B 88  ? 0.2182 0.1928 0.2016 -0.0384 -0.0183 0.0348  88  LEU   B CG  
5044 C CD1 . LEU   B 88  ? 0.2293 0.2289 0.2053 -0.0498 -0.0110 0.0525  88  LEU   B CD1 
5045 C CD2 . LEU   B 88  ? 0.2482 0.2150 0.2500 -0.0005 -0.0489 0.0110  88  LEU   B CD2 
5057 N N   . ALA   B 89  ? 0.1628 0.1502 0.1534 -0.0362 0.0145  0.0036  89  ALA   B N   
5058 C CA  . ALA   B 89  ? 0.1615 0.1496 0.1336 -0.0327 0.0061  0.0147  89  ALA   B CA  
5059 C C   . ALA   B 89  ? 0.1654 0.1472 0.1341 -0.0394 0.0146  0.0102  89  ALA   B C   
5060 O O   . ALA   B 89  ? 0.1483 0.1595 0.1759 -0.0376 0.0152  -0.0259 89  ALA   B O   
5061 C CB  . ALA   B 89  ? 0.1553 0.1516 0.1482 -0.0350 0.0082  0.0170  89  ALA   B CB  
5067 N N   . LYS   B 90  ? 0.1959 0.1384 0.1548 -0.0465 -0.0091 0.0168  90  LYS   B N   
5068 C CA  . LYS   B 90  ? 0.2109 0.1368 0.1424 -0.0432 -0.0096 0.0194  90  LYS   B CA  
5069 C C   . LYS   B 90  ? 0.1978 0.1252 0.1663 -0.0406 -0.0112 0.0025  90  LYS   B C   
5070 O O   . LYS   B 90  ? 0.2067 0.1464 0.1760 -0.0574 0.0012  0.0048  90  LYS   B O   
5071 C CB  . LYS   B 90  ? 0.2326 0.1399 0.1777 -0.0321 -0.0104 0.0232  90  LYS   B CB  
5072 C CG  . LYS   B 90  ? 0.2348 0.1564 0.1843 -0.0162 0.0187  0.0205  90  LYS   B CG  
5073 C CD  . LYS   B 90  ? 0.2605 0.1788 0.2278 -0.0083 0.0419  0.0092  90  LYS   B CD  
5074 C CE  . LYS   B 90  ? 0.2733 0.2019 0.2772 -0.0196 0.0483  -0.0011 90  LYS   B CE  
5075 N NZ  . LYS   B 90  ? 0.2767 0.2005 0.2791 -0.0325 0.0569  -0.0069 90  LYS   B NZ  
5089 N N   . HIS   B 91  ? 0.1715 0.1237 0.1399 -0.0346 -0.0099 0.0102  91  HIS   B N   
5090 C CA  . HIS   B 91  ? 0.1548 0.1280 0.1567 -0.0308 -0.0136 0.0004  91  HIS   B CA  
5091 C C   . HIS   B 91  ? 0.1444 0.1293 0.1400 -0.0298 -0.0084 0.0036  91  HIS   B C   
5092 O O   . HIS   B 91  ? 0.1573 0.1300 0.1371 -0.0262 -0.0174 0.0006  91  HIS   B O   
5093 C CB  . HIS   B 91  ? 0.1744 0.1291 0.1947 -0.0115 -0.0064 0.0091  91  HIS   B CB  
5094 C CG  . HIS   B 91  ? 0.2161 0.1458 0.2595 0.0018  0.0213  0.0211  91  HIS   B CG  
5095 N ND1 . HIS   B 91  ? 0.2472 0.1525 0.3159 0.0008  0.0312  0.0083  91  HIS   B ND1 
5096 C CD2 . HIS   B 91  ? 0.2299 0.1772 0.2991 0.0154  0.0014  0.0567  91  HIS   B CD2 
5097 C CE1 . HIS   B 91  ? 0.2506 0.1640 0.3342 0.0136  0.0265  0.0170  91  HIS   B CE1 
5098 N NE2 . HIS   B 91  ? 0.2416 0.1801 0.3299 0.0282  0.0188  0.0568  91  HIS   B NE2 
5106 N N   . CYS   B 92  ? 0.1394 0.1266 0.1439 -0.0251 -0.0163 0.0017  92  CYS   B N   
5107 C CA  . CYS   B 92  ? 0.1382 0.1212 0.1439 -0.0211 -0.0029 0.0025  92  CYS   B CA  
5108 C C   . CYS   B 92  ? 0.1314 0.1115 0.1459 -0.0104 -0.0063 0.0028  92  CYS   B C   
5109 O O   . CYS   B 92  ? 0.1438 0.1208 0.1564 -0.0115 -0.0058 -0.0013 92  CYS   B O   
5110 C CB  . CYS   B 92  ? 0.1425 0.1349 0.1403 -0.0121 -0.0050 0.0028  92  CYS   B CB  
5111 S SG  . CYS   B 92  ? 0.1402 0.1347 0.1478 -0.0110 -0.0117 0.0064  92  CYS   B SG  
5117 N N   . LEU   B 93  ? 0.1250 0.1202 0.1375 -0.0127 -0.0064 -0.0040 93  LEU   B N   
5118 C CA  . LEU   B 93  ? 0.1282 0.1206 0.1449 -0.0048 -0.0068 0.0031  93  LEU   B CA  
5119 C C   . LEU   B 93  ? 0.1238 0.1165 0.1346 -0.0037 -0.0033 0.0052  93  LEU   B C   
5120 O O   . LEU   B 93  ? 0.1307 0.1233 0.1385 -0.0072 -0.0052 0.0028  93  LEU   B O   
5121 C CB  . LEU   B 93  ? 0.1282 0.1226 0.1624 -0.0007 -0.0083 0.0030  93  LEU   B CB  
5122 C CG  . LEU   B 93  ? 0.1290 0.1369 0.1703 0.0016  -0.0050 0.0168  93  LEU   B CG  
5123 C CD1 . LEU   B 93  ? 0.1390 0.1437 0.1682 0.0082  -0.0029 0.0019  93  LEU   B CD1 
5124 C CD2 . LEU   B 93  ? 0.1259 0.1397 0.1708 -0.0025 -0.0164 0.0060  93  LEU   B CD2 
5136 N N   . HIS   B 94  ? 0.1328 0.1130 0.1286 -0.0054 -0.0118 0.0058  94  HIS   B N   
5137 C CA  . HIS   B 94  ? 0.1336 0.1162 0.1397 -0.0040 -0.0049 0.0033  94  HIS   B CA  
5138 C C   . HIS   B 94  ? 0.1223 0.1231 0.1572 -0.0007 -0.0022 0.0040  94  HIS   B C   
5139 O O   . HIS   B 94  ? 0.1260 0.1340 0.1954 -0.0046 0.0132  -0.0113 94  HIS   B O   
5140 C CB  . HIS   B 94  ? 0.1296 0.1213 0.1519 -0.0010 -0.0119 0.0055  94  HIS   B CB  
5141 C CG  . HIS   B 94  ? 0.1306 0.1175 0.1464 -0.0029 -0.0244 0.0077  94  HIS   B CG  
5142 N ND1 . HIS   B 94  ? 0.1348 0.1320 0.1414 -0.0103 -0.0206 0.0011  94  HIS   B ND1 
5143 C CD2 . HIS   B 94  ? 0.1340 0.1211 0.1496 -0.0006 -0.0182 -0.0008 94  HIS   B CD2 
5144 C CE1 . HIS   B 94  ? 0.1406 0.1280 0.1400 -0.0127 -0.0204 0.0007  94  HIS   B CE1 
5145 N NE2 . HIS   B 94  ? 0.1384 0.1268 0.1479 -0.0134 -0.0145 0.0027  94  HIS   B NE2 
5153 N N   . VAL   B 95  ? 0.1197 0.1199 0.1502 0.0004  -0.0027 0.0042  95  VAL   B N   
5154 C CA  . VAL   B 95  ? 0.1239 0.1288 0.1431 -0.0024 0.0040  0.0176  95  VAL   B CA  
5155 C C   . VAL   B 95  ? 0.1260 0.1233 0.1592 -0.0047 0.0190  0.0125  95  VAL   B C   
5156 O O   . VAL   B 95  ? 0.1385 0.1231 0.1763 0.0074  0.0058  0.0150  95  VAL   B O   
5157 C CB  . VAL   B 95  ? 0.1307 0.1281 0.1608 -0.0042 -0.0061 0.0080  95  VAL   B CB  
5158 C CG1 . VAL   B 95  ? 0.1353 0.1442 0.1816 -0.0067 -0.0010 0.0126  95  VAL   B CG1 
5159 C CG2 . VAL   B 95  ? 0.1321 0.1253 0.1551 0.0017  -0.0083 0.0056  95  VAL   B CG2 
5169 N N   . VAL   B 96  ? 0.1383 0.1309 0.1632 0.0059  0.0109  0.0187  96  VAL   B N   
5170 C CA  . VAL   B 96  ? 0.1479 0.1366 0.1534 0.0094  0.0091  0.0192  96  VAL   B CA  
5171 C C   . VAL   B 96  ? 0.1518 0.1439 0.1765 0.0074  0.0125  0.0202  96  VAL   B C   
5172 O O   . VAL   B 96  ? 0.1511 0.1482 0.1953 0.0040  0.0214  0.0039  96  VAL   B O   
5173 C CB  . VAL   B 96  ? 0.1512 0.1575 0.1662 0.0046  0.0112  0.0091  96  VAL   B CB  
5174 C CG1 . VAL   B 96  ? 0.1544 0.1716 0.1778 0.0124  0.0150  0.0045  96  VAL   B CG1 
5175 C CG2 . VAL   B 96  ? 0.1584 0.1648 0.1724 0.0078  0.0115  -0.0027 96  VAL   B CG2 
5185 N N   . GLY   B 97  ? 0.1572 0.1422 0.1663 0.0041  0.0089  0.0265  97  GLY   B N   
5186 C CA  . GLY   B 97  ? 0.1687 0.1460 0.1694 0.0065  0.0105  0.0270  97  GLY   B CA  
5187 C C   . GLY   B 97  ? 0.1864 0.1551 0.1728 0.0108  0.0086  0.0205  97  GLY   B C   
5188 O O   . GLY   B 97  ? 0.1990 0.1621 0.1679 0.0036  0.0008  0.0170  97  GLY   B O   
5192 N N   . PRO   B 98  ? 0.1964 0.1601 0.1850 0.0094  0.0321  0.0346  98  PRO   B N   
5193 C CA  . PRO   B 98  ? 0.2067 0.1745 0.1918 0.0132  0.0328  0.0294  98  PRO   B CA  
5194 C C   . PRO   B 98  ? 0.2178 0.1731 0.1631 0.0294  0.0338  0.0474  98  PRO   B C   
5195 O O   . PRO   B 98  ? 0.2126 0.1729 0.1895 0.0256  0.0426  0.0434  98  PRO   B O   
5196 C CB  . PRO   B 98  ? 0.1910 0.1760 0.2189 0.0049  0.0469  0.0242  98  PRO   B CB  
5197 C CG  . PRO   B 98  ? 0.1849 0.1718 0.2085 0.0109  0.0350  0.0272  98  PRO   B CG  
5198 C CD  . PRO   B 98  ? 0.1722 0.1634 0.1946 0.0118  0.0311  0.0318  98  PRO   B CD  
5206 N N   . ASN   B 99  ? 0.2264 0.1869 0.1791 0.0468  0.0380  0.0303  99  ASN   B N   
5207 C CA  . ASN   B 99  ? 0.2431 0.1966 0.1875 0.0503  0.0345  0.0485  99  ASN   B CA  
5208 C C   . ASN   B 99  ? 0.2677 0.2281 0.2064 0.0460  0.0483  0.0703  99  ASN   B C   
5209 O O   . ASN   B 99  ? 0.2783 0.2342 0.2197 0.0407  0.0341  0.0685  99  ASN   B O   
5210 C CB  . ASN   B 99  ? 0.2557 0.1951 0.1934 0.0486  0.0255  0.0444  99  ASN   B CB  
5211 C CG  . ASN   B 99  ? 0.2578 0.2050 0.2142 0.0439  0.0078  0.0440  99  ASN   B CG  
5212 O OD1 . ASN   B 99  ? 0.2588 0.2070 0.2476 0.0496  -0.0007 0.0421  99  ASN   B OD1 
5213 N ND2 . ASN   B 99  ? 0.2563 0.2070 0.2253 0.0457  -0.0178 0.0393  99  ASN   B ND2 
5220 N N   A VAL   B 100 ? 0.2826 0.2426 0.2412 0.0305  0.0521  0.0912  100 VAL   B N   
5221 N N   B VAL   B 100 ? 0.2903 0.2469 0.2401 0.0413  0.0374  0.0776  100 VAL   B N   
5222 C CA  A VAL   B 100 ? 0.3101 0.2617 0.2978 0.0244  0.0509  0.0953  100 VAL   B CA  
5223 C CA  B VAL   B 100 ? 0.3150 0.2641 0.2764 0.0359  0.0276  0.0807  100 VAL   B CA  
5224 C C   A VAL   B 100 ? 0.3328 0.2708 0.2837 0.0323  0.0503  0.1131  100 VAL   B C   
5225 C C   B VAL   B 100 ? 0.3333 0.2714 0.2778 0.0382  0.0277  0.1017  100 VAL   B C   
5226 O O   A VAL   B 100 ? 0.3409 0.2853 0.2875 0.0249  0.0636  0.1031  100 VAL   B O   
5227 O O   B VAL   B 100 ? 0.3354 0.2771 0.2801 0.0335  0.0283  0.0986  100 VAL   B O   
5228 C CB  A VAL   B 100 ? 0.3217 0.2809 0.3718 0.0005  0.0437  0.0978  100 VAL   B CB  
5229 C CB  B VAL   B 100 ? 0.3208 0.2741 0.3105 0.0251  0.0197  0.0698  100 VAL   B CB  
5230 C CG1 A VAL   B 100 ? 0.3271 0.2890 0.3944 -0.0090 0.0452  0.0993  100 VAL   B CG1 
5231 C CG1 B VAL   B 100 ? 0.3251 0.2799 0.3210 0.0215  0.0179  0.0671  100 VAL   B CG1 
5232 C CG2 A VAL   B 100 ? 0.3242 0.2859 0.3889 -0.0043 0.0462  0.1075  100 VAL   B CG2 
5233 C CG2 B VAL   B 100 ? 0.3198 0.2750 0.3197 0.0218  0.0181  0.0681  100 VAL   B CG2 
5252 N N   . ASN   B 101 ? 0.3478 0.2731 0.2753 0.0462  0.0289  0.1214  101 ASN   B N   
5253 C CA  . ASN   B 101 ? 0.3868 0.2926 0.3049 0.0567  0.0064  0.1309  101 ASN   B CA  
5254 C C   . ASN   B 101 ? 0.4291 0.3329 0.3015 0.0566  -0.0091 0.1412  101 ASN   B C   
5255 O O   . ASN   B 101 ? 0.4344 0.3482 0.3292 0.0615  -0.0063 0.1108  101 ASN   B O   
5256 C CB  . ASN   B 101 ? 0.3847 0.2794 0.3202 0.0557  0.0103  0.1126  101 ASN   B CB  
5257 C CG  . ASN   B 101 ? 0.3813 0.2713 0.3253 0.0482  0.0145  0.1086  101 ASN   B CG  
5258 O OD1 . ASN   B 101 ? 0.3855 0.2738 0.3559 0.0371  0.0314  0.1033  101 ASN   B OD1 
5259 N ND2 . ASN   B 101 ? 0.3754 0.2668 0.3237 0.0495  0.0083  0.0951  101 ASN   B ND2 
5267 N N   . LYS   B 102 ? 0.4629 0.3668 0.3184 0.0438  -0.0051 0.1335  102 LYS   B N   
5268 C CA  . LYS   B 102 ? 0.4946 0.4089 0.3561 0.0300  0.0060  0.1064  102 LYS   B CA  
5269 C C   . LYS   B 102 ? 0.4900 0.4072 0.3340 0.0311  0.0158  0.1099  102 LYS   B C   
5270 O O   . LYS   B 102 ? 0.5000 0.4107 0.3426 0.0310  0.0028  0.1079  102 LYS   B O   
5271 C CB  . LYS   B 102 ? 0.5270 0.4489 0.4155 0.0190  0.0147  0.0666  102 LYS   B CB  
5272 C CG  . LYS   B 102 ? 0.5536 0.4818 0.4895 0.0122  0.0227  0.0252  102 LYS   B CG  
5273 C CD  . LYS   B 102 ? 0.5741 0.5071 0.5537 0.0061  0.0315  -0.0069 102 LYS   B CD  
5274 C CE  . LYS   B 102 ? 0.5879 0.5262 0.6101 -0.0005 0.0393  -0.0284 102 LYS   B CE  
5275 N NZ  . LYS   B 102 ? 0.5956 0.5384 0.6421 -0.0045 0.0433  -0.0404 102 LYS   B NZ  
5289 N N   . GLY   B 103 ? 0.4713 0.3983 0.3192 0.0303  0.0351  0.1093  103 GLY   B N   
5290 C CA  . GLY   B 103 ? 0.4505 0.3875 0.3253 0.0271  0.0561  0.0950  103 GLY   B CA  
5291 C C   . GLY   B 103 ? 0.4235 0.3706 0.3178 0.0173  0.0750  0.0740  103 GLY   B C   
5292 O O   . GLY   B 103 ? 0.4301 0.3762 0.3226 0.0125  0.0792  0.0724  103 GLY   B O   
5296 N N   A GLU   B 104 ? 0.3986 0.3506 0.2916 0.0157  0.0934  0.0591  104 GLU   B N   
5297 N N   B GLU   B 104 ? 0.4133 0.3662 0.3217 0.0138  0.0616  0.0572  104 GLU   B N   
5298 C CA  A GLU   B 104 ? 0.3770 0.3331 0.2684 0.0193  0.0978  0.0460  104 GLU   B CA  
5299 C CA  B GLU   B 104 ? 0.4026 0.3609 0.3223 0.0102  0.0499  0.0398  104 GLU   B CA  
5300 C C   A GLU   B 104 ? 0.3820 0.3377 0.2825 0.0078  0.1212  0.0417  104 GLU   B C   
5301 C C   B GLU   B 104 ? 0.4009 0.3593 0.3317 0.0037  0.0558  0.0323  104 GLU   B C   
5302 O O   A GLU   B 104 ? 0.3826 0.3364 0.3113 0.0057  0.1238  0.0306  104 GLU   B O   
5303 O O   B GLU   B 104 ? 0.4009 0.3602 0.3372 0.0028  0.0542  0.0294  104 GLU   B O   
5304 C CB  A GLU   B 104 ? 0.3579 0.3104 0.2558 0.0353  0.0662  0.0221  104 GLU   B CB  
5305 C CB  B GLU   B 104 ? 0.3940 0.3560 0.3119 0.0123  0.0345  0.0289  104 GLU   B CB  
5306 C CG  A GLU   B 104 ? 0.3414 0.2940 0.2428 0.0479  0.0226  -0.0103 104 GLU   B CG  
5307 C CG  B GLU   B 104 ? 0.3853 0.3507 0.3019 0.0135  0.0195  0.0167  104 GLU   B CG  
5308 C CD  A GLU   B 104 ? 0.3240 0.2727 0.2230 0.0565  -0.0047 -0.0234 104 GLU   B CD  
5309 C CD  B GLU   B 104 ? 0.3768 0.3441 0.2935 0.0140  0.0086  0.0078  104 GLU   B CD  
5310 O OE1 A GLU   B 104 ? 0.2980 0.2500 0.1930 0.0663  0.0090  -0.0147 104 GLU   B OE1 
5311 O OE1 B GLU   B 104 ? 0.3731 0.3408 0.2870 0.0134  0.0078  0.0071  104 GLU   B OE1 
5312 O OE2 A GLU   B 104 ? 0.3320 0.2835 0.2362 0.0488  -0.0343 -0.0377 104 GLU   B OE2 
5313 O OE2 B GLU   B 104 ? 0.3743 0.3428 0.2952 0.0148  0.0017  0.0022  104 GLU   B OE2 
5326 N N   A ASP   B 105 ? 0.3835 0.3461 0.2814 -0.0018 0.1448  0.0502  105 ASP   B N   
5327 N N   B ASP   B 105 ? 0.3985 0.3561 0.3392 -0.0024 0.0662  0.0292  105 ASP   B N   
5328 C CA  A ASP   B 105 ? 0.3860 0.3523 0.3074 -0.0080 0.1622  0.0381  105 ASP   B CA  
5329 C CA  B ASP   B 105 ? 0.3950 0.3503 0.3454 -0.0081 0.0777  0.0244  105 ASP   B CA  
5330 C C   A ASP   B 105 ? 0.3710 0.3218 0.2844 -0.0166 0.1549  0.0328  105 ASP   B C   
5331 C C   B ASP   B 105 ? 0.3841 0.3293 0.3252 -0.0141 0.0999  0.0261  105 ASP   B C   
5332 O O   A ASP   B 105 ? 0.3519 0.3081 0.2755 -0.0168 0.1669  0.0326  105 ASP   B O   
5333 O O   B ASP   B 105 ? 0.3846 0.3310 0.3239 -0.0142 0.1032  0.0259  105 ASP   B O   
5334 C CB  A ASP   B 105 ? 0.3991 0.3817 0.3724 0.0024  0.1709  0.0186  105 ASP   B CB  
5335 C CB  B ASP   B 105 ? 0.4002 0.3622 0.3749 -0.0065 0.0662  0.0171  105 ASP   B CB  
5336 C CG  A ASP   B 105 ? 0.4044 0.3994 0.4372 0.0069  0.1846  0.0063  105 ASP   B CG  
5337 C CG  B ASP   B 105 ? 0.4030 0.3696 0.3992 -0.0060 0.0566  0.0123  105 ASP   B CG  
5338 O OD1 A ASP   B 105 ? 0.3995 0.4059 0.4425 -0.0037 0.2037  0.0166  105 ASP   B OD1 
5339 O OD1 B ASP   B 105 ? 0.4018 0.3701 0.4070 -0.0074 0.0540  0.0123  105 ASP   B OD1 
5340 O OD2 A ASP   B 105 ? 0.4097 0.4063 0.4831 0.0166  0.1767  -0.0091 105 ASP   B OD2 
5341 O OD2 B ASP   B 105 ? 0.4053 0.3743 0.4104 -0.0055 0.0536  0.0099  105 ASP   B OD2 
5350 N N   . ILE   B 106 ? 0.3689 0.3027 0.3106 -0.0188 0.1210  0.0294  106 ILE   B N   
5351 C CA  . ILE   B 106 ? 0.3436 0.2619 0.3196 -0.0305 0.1289  0.0256  106 ILE   B CA  
5352 C C   . ILE   B 106 ? 0.3037 0.2571 0.3037 -0.0229 0.1255  0.0004  106 ILE   B C   
5353 O O   . ILE   B 106 ? 0.2912 0.2240 0.2987 -0.0232 0.1176  -0.0059 106 ILE   B O   
5354 C CB  . ILE   B 106 ? 0.3616 0.2473 0.3390 -0.0407 0.1269  0.0398  106 ILE   B CB  
5355 C CG1 . ILE   B 106 ? 0.3706 0.2482 0.3474 -0.0280 0.1194  0.0353  106 ILE   B CG1 
5356 C CG2 . ILE   B 106 ? 0.3670 0.2496 0.3675 -0.0511 0.1334  0.0467  106 ILE   B CG2 
5357 C CD1 . ILE   B 106 ? 0.3766 0.2543 0.3460 -0.0141 0.1180  0.0388  106 ILE   B CD1 
5370 N N   A GLN   B 107 ? 0.2935 0.2778 0.3200 -0.0248 0.1235  -0.0042 107 GLN   B N   
5371 N N   B GLN   B 107 ? 0.3026 0.2759 0.3121 -0.0189 0.1043  -0.0007 107 GLN   B N   
5372 C CA  A GLN   B 107 ? 0.2820 0.2960 0.3349 -0.0259 0.1184  -0.0006 107 GLN   B CA  
5373 C CA  B GLN   B 107 ? 0.2963 0.2894 0.3243 -0.0124 0.0815  0.0001  107 GLN   B CA  
5374 C C   A GLN   B 107 ? 0.2548 0.2714 0.3117 -0.0139 0.0874  -0.0062 107 GLN   B C   
5375 C C   B GLN   B 107 ? 0.2672 0.2723 0.2952 -0.0036 0.0753  -0.0030 107 GLN   B C   
5376 O O   A GLN   B 107 ? 0.2489 0.2740 0.3491 -0.0068 0.0611  -0.0201 107 GLN   B O   
5377 O O   B GLN   B 107 ? 0.2698 0.2771 0.2977 -0.0021 0.0694  -0.0054 107 GLN   B O   
5378 C CB  A GLN   B 107 ? 0.3148 0.3403 0.4004 -0.0283 0.1080  0.0051  107 GLN   B CB  
5379 C CB  B GLN   B 107 ? 0.3181 0.3158 0.3695 -0.0123 0.0645  0.0012  107 GLN   B CB  
5380 C CG  A GLN   B 107 ? 0.3517 0.3800 0.4712 -0.0198 0.0787  0.0072  107 GLN   B CG  
5381 C CG  B GLN   B 107 ? 0.3376 0.3374 0.4154 -0.0097 0.0467  0.0021  107 GLN   B CG  
5382 C CD  A GLN   B 107 ? 0.3789 0.4078 0.5257 -0.0154 0.0609  0.0134  107 GLN   B CD  
5383 C CD  B GLN   B 107 ? 0.3529 0.3534 0.4509 -0.0089 0.0324  0.0041  107 GLN   B CD  
5384 O OE1 A GLN   B 107 ? 0.3866 0.4239 0.5486 -0.0077 0.0615  0.0130  107 GLN   B OE1 
5385 O OE1 B GLN   B 107 ? 0.3607 0.3616 0.4647 -0.0077 0.0294  0.0043  107 GLN   B OE1 
5386 N NE2 A GLN   B 107 ? 0.3922 0.4135 0.5457 -0.0149 0.0516  0.0195  107 GLN   B NE2 
5387 N NE2 B GLN   B 107 ? 0.3562 0.3559 0.4649 -0.0089 0.0268  0.0057  107 GLN   B NE2 
5404 N N   . LEU   B 108 ? 0.2342 0.2487 0.2716 0.0067  0.0750  -0.0048 108 LEU   B N   
5405 C CA  . LEU   B 108 ? 0.2121 0.2200 0.2466 0.0232  0.0549  0.0099  108 LEU   B CA  
5406 C C   . LEU   B 108 ? 0.1857 0.1853 0.2374 0.0194  0.0363  0.0225  108 LEU   B C   
5407 O O   . LEU   B 108 ? 0.1853 0.1706 0.2414 0.0205  0.0348  0.0191  108 LEU   B O   
5408 C CB  . LEU   B 108 ? 0.2296 0.2408 0.2303 0.0210  0.0542  0.0141  108 LEU   B CB  
5409 C CG  . LEU   B 108 ? 0.2464 0.2687 0.2339 0.0243  0.0483  -0.0067 108 LEU   B CG  
5410 C CD1 . LEU   B 108 ? 0.2583 0.2842 0.2237 0.0132  0.0465  -0.0027 108 LEU   B CD1 
5411 C CD2 . LEU   B 108 ? 0.2611 0.2778 0.2441 0.0335  0.0366  -0.0165 108 LEU   B CD2 
5424 N N   . LEU   B 109 ? 0.1716 0.1676 0.2389 0.0121  0.0352  0.0151  109 LEU   B N   
5425 C CA  . LEU   B 109 ? 0.1567 0.1392 0.2429 0.0107  0.0327  0.0267  109 LEU   B CA  
5426 C C   . LEU   B 109 ? 0.1448 0.1306 0.2460 0.0082  0.0363  0.0210  109 LEU   B C   
5427 O O   . LEU   B 109 ? 0.1403 0.1302 0.2382 0.0048  0.0319  0.0311  109 LEU   B O   
5428 C CB  . LEU   B 109 ? 0.1643 0.1358 0.2467 0.0052  0.0234  0.0345  109 LEU   B CB  
5429 C CG  . LEU   B 109 ? 0.1639 0.1371 0.2332 0.0048  0.0189  0.0225  109 LEU   B CG  
5430 C CD1 . LEU   B 109 ? 0.1598 0.1487 0.2328 0.0151  0.0240  0.0265  109 LEU   B CD1 
5431 C CD2 . LEU   B 109 ? 0.1707 0.1388 0.2501 0.0085  0.0201  0.0238  109 LEU   B CD2 
5443 N N   . LYS   B 110 ? 0.1412 0.1331 0.2388 0.0021  0.0363  0.0248  110 LYS   B N   
5444 C CA  . LYS   B 110 ? 0.1383 0.1299 0.2306 0.0018  0.0253  0.0118  110 LYS   B CA  
5445 C C   . LYS   B 110 ? 0.1367 0.1266 0.2266 0.0016  0.0301  0.0159  110 LYS   B C   
5446 O O   . LYS   B 110 ? 0.1313 0.1308 0.2154 -0.0042 0.0208  0.0090  110 LYS   B O   
5447 C CB  . LYS   B 110 ? 0.1407 0.1311 0.2552 -0.0067 0.0285  0.0096  110 LYS   B CB  
5448 C CG  . LYS   B 110 ? 0.1390 0.1271 0.2636 -0.0024 0.0072  0.0210  110 LYS   B CG  
5449 C CD  . LYS   B 110 ? 0.1510 0.1305 0.2714 -0.0081 0.0135  0.0174  110 LYS   B CD  
5450 C CE  . LYS   B 110 ? 0.1527 0.1432 0.2898 -0.0061 0.0103  0.0146  110 LYS   B CE  
5451 N NZ  . LYS   B 110 ? 0.1532 0.1608 0.2779 0.0019  0.0021  0.0010  110 LYS   B NZ  
5465 N N   . SER   B 111 ? 0.1440 0.1306 0.2266 -0.0013 0.0297  0.0175  111 SER   B N   
5466 C CA  . SER   B 111 ? 0.1490 0.1432 0.2048 0.0021  0.0156  0.0202  111 SER   B CA  
5467 C C   . SER   B 111 ? 0.1385 0.1349 0.2040 -0.0024 0.0082  0.0148  111 SER   B C   
5468 O O   . SER   B 111 ? 0.1336 0.1403 0.2220 -0.0013 0.0076  0.0164  111 SER   B O   
5469 C CB  . SER   B 111 ? 0.1600 0.1571 0.2173 0.0055  0.0296  0.0353  111 SER   B CB  
5470 O OG  . SER   B 111 ? 0.1821 0.1921 0.2378 0.0121  0.0432  0.0356  111 SER   B OG  
5476 N N   . ALA   B 112 ? 0.1316 0.1390 0.2208 0.0059  0.0229  0.0151  112 ALA   B N   
5477 C CA  . ALA   B 112 ? 0.1318 0.1373 0.2085 0.0062  0.0081  0.0085  112 ALA   B CA  
5478 C C   . ALA   B 112 ? 0.1258 0.1282 0.1944 0.0043  0.0071  0.0045  112 ALA   B C   
5479 O O   . ALA   B 112 ? 0.1254 0.1304 0.2051 -0.0043 0.0043  0.0025  112 ALA   B O   
5480 C CB  . ALA   B 112 ? 0.1326 0.1438 0.2234 0.0066  0.0080  0.0155  112 ALA   B CB  
5486 N N   . TYR   B 113 ? 0.1267 0.1180 0.2008 -0.0011 0.0102  0.0092  113 TYR   B N   
5487 C CA  . TYR   B 113 ? 0.1234 0.1201 0.2039 -0.0038 0.0141  0.0042  113 TYR   B CA  
5488 C C   . TYR   B 113 ? 0.1190 0.1116 0.2047 -0.0048 0.0069  0.0092  113 TYR   B C   
5489 O O   . TYR   B 113 ? 0.1239 0.1208 0.1930 -0.0034 -0.0000 0.0026  113 TYR   B O   
5490 C CB  . TYR   B 113 ? 0.1288 0.1139 0.2060 -0.0025 0.0195  0.0114  113 TYR   B CB  
5491 C CG  . TYR   B 113 ? 0.1266 0.1134 0.2191 -0.0043 0.0096  0.0119  113 TYR   B CG  
5492 C CD1 . TYR   B 113 ? 0.1317 0.1190 0.2230 -0.0036 0.0174  0.0197  113 TYR   B CD1 
5493 C CD2 . TYR   B 113 ? 0.1338 0.1196 0.2227 -0.0033 0.0112  0.0081  113 TYR   B CD2 
5494 C CE1 . TYR   B 113 ? 0.1266 0.1267 0.2143 -0.0070 0.0176  0.0090  113 TYR   B CE1 
5495 C CE2 . TYR   B 113 ? 0.1360 0.1181 0.2354 -0.0031 0.0075  0.0114  113 TYR   B CE2 
5496 C CZ  . TYR   B 113 ? 0.1304 0.1232 0.2326 0.0016  0.0045  0.0056  113 TYR   B CZ  
5497 O OH  . TYR   B 113 ? 0.1420 0.1145 0.2541 0.0089  0.0198  0.0043  113 TYR   B OH  
5507 N N   . GLU   B 114 ? 0.1220 0.1109 0.2115 -0.0005 0.0109  0.0065  114 GLU   B N   
5508 C CA  . GLU   B 114 ? 0.1225 0.1080 0.2086 0.0030  0.0136  0.0066  114 GLU   B CA  
5509 C C   . GLU   B 114 ? 0.1244 0.1100 0.2034 0.0026  0.0133  0.0011  114 GLU   B C   
5510 O O   . GLU   B 114 ? 0.1209 0.1131 0.2104 0.0008  0.0030  0.0095  114 GLU   B O   
5511 C CB  . GLU   B 114 ? 0.1238 0.1166 0.2213 -0.0001 0.0126  0.0083  114 GLU   B CB  
5512 C CG  . GLU   B 114 ? 0.1258 0.1185 0.2233 -0.0031 0.0110  0.0110  114 GLU   B CG  
5513 C CD  . GLU   B 114 ? 0.1236 0.1200 0.2233 -0.0054 0.0104  0.0089  114 GLU   B CD  
5514 O OE1 . GLU   B 114 ? 0.1244 0.1432 0.2239 -0.0076 0.0164  0.0126  114 GLU   B OE1 
5515 O OE2 . GLU   B 114 ? 0.1247 0.1394 0.2316 -0.0151 0.0189  0.0067  114 GLU   B OE2 
5522 N N   . ASN   B 115 ? 0.1257 0.1099 0.1984 0.0013  0.0006  0.0023  115 ASN   B N   
5523 C CA  . ASN   B 115 ? 0.1241 0.1169 0.1921 -0.0054 0.0077  0.0090  115 ASN   B CA  
5524 C C   . ASN   B 115 ? 0.1111 0.1145 0.1946 -0.0109 0.0017  -0.0006 115 ASN   B C   
5525 O O   . ASN   B 115 ? 0.1265 0.1173 0.1902 -0.0155 0.0016  0.0002  115 ASN   B O   
5526 C CB  . ASN   B 115 ? 0.1351 0.1267 0.1866 -0.0076 0.0068  0.0043  115 ASN   B CB  
5527 C CG  . ASN   B 115 ? 0.1475 0.1316 0.1940 0.0027  0.0015  -0.0015 115 ASN   B CG  
5528 O OD1 . ASN   B 115 ? 0.1902 0.1463 0.2042 -0.0050 0.0150  -0.0167 115 ASN   B OD1 
5529 N ND2 . ASN   B 115 ? 0.1429 0.1387 0.1988 -0.0055 0.0066  0.0049  115 ASN   B ND2 
5536 N N   . PHE   B 116 ? 0.1214 0.1151 0.1813 -0.0038 -0.0019 0.0016  116 PHE   B N   
5537 C CA  . PHE   B 116 ? 0.1269 0.1186 0.1852 -0.0085 -0.0016 0.0078  116 PHE   B CA  
5538 C C   . PHE   B 116 ? 0.1287 0.1071 0.1777 -0.0126 -0.0019 0.0136  116 PHE   B C   
5539 O O   . PHE   B 116 ? 0.1334 0.1151 0.1764 -0.0043 -0.0070 0.0032  116 PHE   B O   
5540 C CB  . PHE   B 116 ? 0.1218 0.1196 0.1737 -0.0033 -0.0132 0.0052  116 PHE   B CB  
5541 C CG  . PHE   B 116 ? 0.1165 0.1169 0.1827 -0.0037 -0.0044 0.0024  116 PHE   B CG  
5542 C CD1 . PHE   B 116 ? 0.1263 0.1232 0.1998 -0.0018 0.0008  0.0046  116 PHE   B CD1 
5543 C CD2 . PHE   B 116 ? 0.1247 0.1271 0.1722 -0.0039 -0.0053 -0.0021 116 PHE   B CD2 
5544 C CE1 . PHE   B 116 ? 0.1303 0.1271 0.1924 -0.0024 -0.0138 0.0062  116 PHE   B CE1 
5545 C CE2 . PHE   B 116 ? 0.1228 0.1324 0.1830 -0.0025 0.0007  0.0036  116 PHE   B CE2 
5546 C CZ  . PHE   B 116 ? 0.1176 0.1287 0.1921 -0.0009 -0.0128 0.0046  116 PHE   B CZ  
5556 N N   . ASN   B 117 ? 0.1227 0.1136 0.1894 -0.0020 -0.0058 0.0090  117 ASN   B N   
5557 C CA  . ASN   B 117 ? 0.1263 0.1185 0.1969 -0.0006 0.0003  0.0031  117 ASN   B CA  
5558 C C   . ASN   B 117 ? 0.1311 0.1154 0.2069 0.0032  -0.0059 0.0061  117 ASN   B C   
5559 O O   . ASN   B 117 ? 0.1416 0.1216 0.2332 -0.0006 -0.0272 0.0081  117 ASN   B O   
5560 C CB  . ASN   B 117 ? 0.1269 0.1229 0.2092 0.0019  -0.0022 0.0032  117 ASN   B CB  
5561 C CG  . ASN   B 117 ? 0.1246 0.1234 0.2098 0.0014  0.0010  -0.0061 117 ASN   B CG  
5562 O OD1 . ASN   B 117 ? 0.1482 0.1224 0.2264 -0.0099 0.0075  -0.0039 117 ASN   B OD1 
5563 N ND2 . ASN   B 117 ? 0.1264 0.1259 0.2086 -0.0010 0.0040  0.0017  117 ASN   B ND2 
5570 N N   . GLN   B 118 ? 0.1283 0.1107 0.2011 -0.0066 -0.0150 -0.0004 118 GLN   B N   
5571 C CA  . GLN   B 118 ? 0.1294 0.1202 0.2139 0.0007  -0.0182 0.0010  118 GLN   B CA  
5572 C C   . GLN   B 118 ? 0.1392 0.1161 0.2233 -0.0026 -0.0081 0.0022  118 GLN   B C   
5573 O O   . GLN   B 118 ? 0.1620 0.1119 0.2506 -0.0097 0.0056  0.0002  118 GLN   B O   
5574 C CB  . GLN   B 118 ? 0.1374 0.1205 0.2316 0.0012  -0.0199 0.0001  118 GLN   B CB  
5575 C CG  . GLN   B 118 ? 0.1483 0.1251 0.2232 0.0041  -0.0068 -0.0044 118 GLN   B CG  
5576 C CD  . GLN   B 118 ? 0.1504 0.1228 0.2127 -0.0004 -0.0104 -0.0077 118 GLN   B CD  
5577 O OE1 . GLN   B 118 ? 0.1641 0.1239 0.2284 0.0017  0.0081  0.0066  118 GLN   B OE1 
5578 N NE2 . GLN   B 118 ? 0.1609 0.1219 0.2430 -0.0014 -0.0197 0.0039  118 GLN   B NE2 
5587 N N   . HIS   B 119 ? 0.1439 0.1160 0.1798 -0.0081 -0.0089 0.0081  119 HIS   B N   
5588 C CA  . HIS   B 119 ? 0.1527 0.1279 0.1791 -0.0020 -0.0187 0.0035  119 HIS   B CA  
5589 C C   . HIS   B 119 ? 0.1487 0.1286 0.1759 -0.0082 -0.0234 0.0105  119 HIS   B C   
5590 O O   . HIS   B 119 ? 0.1605 0.1329 0.1873 -0.0245 -0.0177 0.0123  119 HIS   B O   
5591 C CB  . HIS   B 119 ? 0.1511 0.1420 0.1920 -0.0040 -0.0185 0.0026  119 HIS   B CB  
5592 C CG  . HIS   B 119 ? 0.1578 0.1657 0.2044 0.0067  -0.0305 -0.0189 119 HIS   B CG  
5593 N ND1 . HIS   B 119 ? 0.1724 0.1852 0.2265 0.0036  -0.0455 -0.0362 119 HIS   B ND1 
5594 C CD2 . HIS   B 119 ? 0.1775 0.1875 0.2030 0.0363  -0.0516 -0.0245 119 HIS   B CD2 
5595 C CE1 . HIS   B 119 ? 0.1955 0.1967 0.2352 0.0195  -0.0510 -0.0501 119 HIS   B CE1 
5596 N NE2 . HIS   B 119 ? 0.1959 0.2076 0.2200 0.0350  -0.0519 -0.0439 119 HIS   B NE2 
5604 N N   . GLU   B 120 ? 0.1725 0.1321 0.1786 -0.0096 -0.0329 0.0123  120 GLU   B N   
5605 C CA  . GLU   B 120 ? 0.1954 0.1437 0.1892 -0.0046 -0.0448 0.0226  120 GLU   B CA  
5606 C C   . GLU   B 120 ? 0.1753 0.1364 0.1781 -0.0155 -0.0294 0.0247  120 GLU   B C   
5607 O O   . GLU   B 120 ? 0.1701 0.1481 0.1806 -0.0167 -0.0333 0.0176  120 GLU   B O   
5608 C CB  . GLU   B 120 ? 0.2552 0.1719 0.2544 0.0136  -0.0707 0.0471  120 GLU   B CB  
5609 C CG  . GLU   B 120 ? 0.3121 0.2355 0.3508 0.0271  -0.0930 0.0745  120 GLU   B CG  
5610 C CD  . GLU   B 120 ? 0.3553 0.3085 0.4582 0.0287  -0.0979 0.0854  120 GLU   B CD  
5611 O OE1 . GLU   B 120 ? 0.3840 0.3290 0.4957 0.0209  -0.0898 0.0961  120 GLU   B OE1 
5612 O OE2 . GLU   B 120 ? 0.3853 0.3532 0.5149 0.0275  -0.0952 0.0768  120 GLU   B OE2 
5619 N N   . VAL   B 121 ? 0.1650 0.1326 0.1848 -0.0191 -0.0246 0.0221  121 VAL   B N   
5620 C CA  . VAL   B 121 ? 0.1603 0.1429 0.1695 -0.0165 -0.0189 0.0215  121 VAL   B CA  
5621 C C   . VAL   B 121 ? 0.1534 0.1361 0.1673 -0.0237 -0.0171 0.0172  121 VAL   B C   
5622 O O   . VAL   B 121 ? 0.1646 0.1324 0.1815 -0.0283 -0.0235 0.0141  121 VAL   B O   
5623 C CB  . VAL   B 121 ? 0.1838 0.1813 0.1725 -0.0039 -0.0253 0.0219  121 VAL   B CB  
5624 C CG1 . VAL   B 121 ? 0.1898 0.1862 0.1975 -0.0136 -0.0028 0.0197  121 VAL   B CG1 
5625 C CG2 . VAL   B 121 ? 0.2116 0.2045 0.1832 0.0050  -0.0293 0.0119  121 VAL   B CG2 
5635 N N   . LEU   B 122 ? 0.1465 0.1310 0.1518 -0.0202 -0.0257 0.0091  122 LEU   B N   
5636 C CA  . LEU   B 122 ? 0.1353 0.1390 0.1480 -0.0206 -0.0145 0.0110  122 LEU   B CA  
5637 C C   . LEU   B 122 ? 0.1383 0.1207 0.1537 -0.0263 -0.0151 0.0106  122 LEU   B C   
5638 O O   . LEU   B 122 ? 0.1555 0.1238 0.1809 -0.0333 -0.0279 0.0040  122 LEU   B O   
5639 C CB  . LEU   B 122 ? 0.1615 0.1462 0.1842 -0.0051 -0.0166 0.0164  122 LEU   B CB  
5640 C CG  . LEU   B 122 ? 0.1506 0.1563 0.1845 -0.0175 0.0007  0.0083  122 LEU   B CG  
5641 C CD1 . LEU   B 122 ? 0.1583 0.1832 0.2023 -0.0199 -0.0121 0.0114  122 LEU   B CD1 
5642 C CD2 . LEU   B 122 ? 0.1494 0.1552 0.1792 -0.0142 0.0075  -0.0048 122 LEU   B CD2 
5654 N N   . LEU   B 123 ? 0.1409 0.1174 0.1520 -0.0222 -0.0123 0.0061  123 LEU   B N   
5655 C CA  . LEU   B 123 ? 0.1457 0.1199 0.1517 -0.0229 -0.0165 0.0034  123 LEU   B CA  
5656 C C   . LEU   B 123 ? 0.1443 0.1157 0.1549 -0.0240 -0.0190 0.0028  123 LEU   B C   
5657 O O   . LEU   B 123 ? 0.1501 0.1185 0.1522 -0.0300 -0.0166 -0.0007 123 LEU   B O   
5658 C CB  . LEU   B 123 ? 0.1471 0.1268 0.1658 -0.0231 -0.0119 0.0005  123 LEU   B CB  
5659 C CG  . LEU   B 123 ? 0.1451 0.1288 0.1747 -0.0164 -0.0078 0.0077  123 LEU   B CG  
5660 C CD1 . LEU   B 123 ? 0.1600 0.1342 0.1776 -0.0174 -0.0027 -0.0064 123 LEU   B CD1 
5661 C CD2 . LEU   B 123 ? 0.1520 0.1386 0.1892 -0.0202 0.0055  0.0177  123 LEU   B CD2 
5673 N N   . ALA   B 124 ? 0.1407 0.1142 0.1569 -0.0168 -0.0101 -0.0033 124 ALA   B N   
5674 C CA  . ALA   B 124 ? 0.1324 0.1163 0.1688 -0.0120 -0.0102 -0.0043 124 ALA   B CA  
5675 C C   . ALA   B 124 ? 0.1253 0.1156 0.1681 -0.0124 -0.0085 0.0045  124 ALA   B C   
5676 O O   . ALA   B 124 ? 0.1416 0.1166 0.1717 -0.0114 -0.0130 0.0026  124 ALA   B O   
5677 C CB  . ALA   B 124 ? 0.1334 0.1250 0.1720 -0.0079 0.0037  -0.0050 124 ALA   B CB  
5683 N N   . PRO   B 125 ? 0.1398 0.1177 0.1594 -0.0133 -0.0109 0.0160  125 PRO   B N   
5684 C CA  . PRO   B 125 ? 0.1439 0.1271 0.1777 -0.0142 -0.0110 0.0192  125 PRO   B CA  
5685 C C   . PRO   B 125 ? 0.1321 0.1226 0.1921 -0.0154 -0.0069 0.0050  125 PRO   B C   
5686 O O   . PRO   B 125 ? 0.1385 0.1218 0.2067 -0.0104 -0.0015 0.0140  125 PRO   B O   
5687 C CB  . PRO   B 125 ? 0.1446 0.1490 0.1902 -0.0235 -0.0165 0.0337  125 PRO   B CB  
5688 C CG  . PRO   B 125 ? 0.1583 0.1512 0.1778 -0.0299 -0.0201 0.0175  125 PRO   B CG  
5689 C CD  . PRO   B 125 ? 0.1532 0.1305 0.1622 -0.0311 -0.0116 0.0077  125 PRO   B CD  
5697 N N   . LEU   B 126 ? 0.1415 0.1152 0.2044 -0.0190 0.0134  0.0113  126 LEU   B N   
5698 C CA  . LEU   B 126 ? 0.1464 0.1275 0.2143 -0.0103 0.0169  0.0143  126 LEU   B CA  
5699 C C   . LEU   B 126 ? 0.1441 0.1370 0.2134 0.0011  0.0186  0.0129  126 LEU   B C   
5700 O O   . LEU   B 126 ? 0.1638 0.1593 0.2345 0.0159  0.0000  -0.0000 126 LEU   B O   
5701 C CB  . LEU   B 126 ? 0.1699 0.1302 0.2396 -0.0122 0.0262  0.0111  126 LEU   B CB  
5702 C CG  . LEU   B 126 ? 0.1827 0.1383 0.2492 -0.0206 0.0230  -0.0081 126 LEU   B CG  
5703 C CD1 . LEU   B 126 ? 0.1991 0.1458 0.3066 -0.0214 0.0233  -0.0085 126 LEU   B CD1 
5704 C CD2 . LEU   B 126 ? 0.1815 0.1539 0.2402 -0.0355 0.0118  -0.0056 126 LEU   B CD2 
5716 N N   . LEU   B 127 ? 0.1401 0.1245 0.2176 0.0033  0.0293  0.0093  127 LEU   B N   
5717 C CA  . LEU   B 127 ? 0.1351 0.1303 0.2275 -0.0024 0.0305  0.0235  127 LEU   B CA  
5718 C C   . LEU   B 127 ? 0.1377 0.1226 0.2262 0.0005  0.0119  0.0166  127 LEU   B C   
5719 O O   . LEU   B 127 ? 0.1405 0.1290 0.2297 -0.0142 0.0075  0.0196  127 LEU   B O   
5720 C CB  . LEU   B 127 ? 0.1537 0.1309 0.2381 -0.0076 0.0174  0.0307  127 LEU   B CB  
5721 C CG  . LEU   B 127 ? 0.1618 0.1324 0.2460 0.0005  0.0188  0.0264  127 LEU   B CG  
5722 C CD1 . LEU   B 127 ? 0.1662 0.1376 0.2397 0.0047  0.0135  0.0099  127 LEU   B CD1 
5723 C CD2 . LEU   B 127 ? 0.1670 0.1423 0.2579 -0.0105 0.0241  0.0317  127 LEU   B CD2 
5735 N N   . SER   B 128 ? 0.1419 0.1233 0.2197 0.0014  0.0024  0.0128  128 SER   B N   
5736 C CA  . SER   B 128 ? 0.1551 0.1333 0.2214 0.0062  -0.0065 0.0214  128 SER   B CA  
5737 C C   . SER   B 128 ? 0.1656 0.1348 0.2508 0.0098  -0.0202 0.0118  128 SER   B C   
5738 O O   . SER   B 128 ? 0.1829 0.1369 0.2809 0.0025  -0.0199 0.0286  128 SER   B O   
5739 C CB  . SER   B 128 ? 0.1657 0.1385 0.2218 0.0091  0.0036  0.0250  128 SER   B CB  
5740 O OG  . SER   B 128 ? 0.1695 0.1536 0.2228 0.0116  0.0146  0.0355  128 SER   B OG  
5746 N N   . ALA   B 129 ? 0.1747 0.1453 0.2584 0.0261  -0.0102 -0.0046 129 ALA   B N   
5747 C CA  . ALA   B 129 ? 0.1919 0.1521 0.2796 0.0278  -0.0106 -0.0087 129 ALA   B CA  
5748 C C   . ALA   B 129 ? 0.1827 0.1418 0.2634 0.0169  0.0091  0.0096  129 ALA   B C   
5749 O O   . ALA   B 129 ? 0.1702 0.1462 0.2711 0.0185  0.0004  0.0164  129 ALA   B O   
5750 C CB  . ALA   B 129 ? 0.2193 0.1744 0.3150 0.0287  0.0013  -0.0176 129 ALA   B CB  
5756 N N   . GLY   B 130 ? 0.1821 0.1385 0.2554 0.0241  0.0135  0.0059  130 GLY   B N   
5757 C CA  . GLY   B 130 ? 0.1843 0.1493 0.2771 0.0212  0.0341  -0.0071 130 GLY   B CA  
5758 C C   . GLY   B 130 ? 0.1886 0.1541 0.2687 0.0164  0.0170  0.0069  130 GLY   B C   
5759 O O   . GLY   B 130 ? 0.2035 0.1620 0.2746 0.0204  0.0042  0.0154  130 GLY   B O   
5763 N N   . ILE   B 131 ? 0.1817 0.1707 0.2746 0.0304  0.0118  0.0044  131 ILE   B N   
5764 C CA  . ILE   B 131 ? 0.1955 0.1889 0.2695 0.0241  0.0027  0.0195  131 ILE   B CA  
5765 C C   . ILE   B 131 ? 0.2048 0.1806 0.2310 0.0159  -0.0001 0.0224  131 ILE   B C   
5766 O O   . ILE   B 131 ? 0.2315 0.1898 0.2346 0.0204  -0.0157 0.0182  131 ILE   B O   
5767 C CB  . ILE   B 131 ? 0.1945 0.2190 0.3075 0.0176  -0.0036 0.0231  131 ILE   B CB  
5768 C CG1 . ILE   B 131 ? 0.2105 0.2360 0.3104 -0.0057 0.0066  0.0221  131 ILE   B CG1 
5769 C CG2 . ILE   B 131 ? 0.1901 0.2390 0.3286 0.0244  -0.0090 0.0134  131 ILE   B CG2 
5770 C CD1 . ILE   B 131 ? 0.2295 0.2535 0.3235 -0.0255 -0.0074 0.0223  131 ILE   B CD1 
5782 N N   . PHE   B 132 ? 0.1891 0.1668 0.2179 0.0098  0.0160  0.0266  132 PHE   B N   
5783 C CA  . PHE   B 132 ? 0.1979 0.1631 0.2282 0.0076  0.0377  0.0211  132 PHE   B CA  
5784 C C   . PHE   B 132 ? 0.2130 0.1746 0.2469 0.0110  0.0454  0.0170  132 PHE   B C   
5785 O O   . PHE   B 132 ? 0.2380 0.1990 0.2661 0.0096  0.0567  0.0251  132 PHE   B O   
5786 C CB  . PHE   B 132 ? 0.1799 0.1628 0.2043 0.0103  0.0467  0.0214  132 PHE   B CB  
5787 C CG  . PHE   B 132 ? 0.1796 0.1719 0.2149 0.0150  0.0347  0.0168  132 PHE   B CG  
5788 C CD1 . PHE   B 132 ? 0.1865 0.1724 0.2458 0.0141  0.0333  0.0119  132 PHE   B CD1 
5789 C CD2 . PHE   B 132 ? 0.1817 0.1754 0.1911 0.0233  0.0325  0.0278  132 PHE   B CD2 
5790 C CE1 . PHE   B 132 ? 0.1914 0.1769 0.2520 0.0066  0.0188  0.0176  132 PHE   B CE1 
5791 C CE2 . PHE   B 132 ? 0.1869 0.1805 0.2006 0.0190  0.0212  0.0261  132 PHE   B CE2 
5792 C CZ  . PHE   B 132 ? 0.1925 0.1793 0.2397 0.0111  0.0004  0.0362  132 PHE   B CZ  
5802 N N   . GLY   B 133 ? 0.2137 0.1628 0.2425 0.0105  0.0306  0.0348  133 GLY   B N   
5803 C CA  . GLY   B 133 ? 0.2220 0.1759 0.2597 -0.0099 0.0212  0.0377  133 GLY   B CA  
5804 C C   . GLY   B 133 ? 0.2317 0.1812 0.2587 -0.0237 0.0277  0.0463  133 GLY   B C   
5805 O O   . GLY   B 133 ? 0.2524 0.1976 0.2962 -0.0354 0.0306  0.0577  133 GLY   B O   
5809 N N   . ALA   B 134 ? 0.2166 0.1803 0.2426 -0.0235 0.0235  0.0290  134 ALA   B N   
5810 C CA  . ALA   B 134 ? 0.2118 0.1754 0.2559 -0.0193 0.0295  0.0131  134 ALA   B CA  
5811 C C   . ALA   B 134 ? 0.2176 0.1659 0.2622 -0.0144 0.0346  0.0251  134 ALA   B C   
5812 O O   . ALA   B 134 ? 0.2232 0.1861 0.2804 -0.0034 0.0271  0.0177  134 ALA   B O   
5813 C CB  . ALA   B 134 ? 0.2121 0.1804 0.2710 -0.0119 0.0227  -0.0052 134 ALA   B CB  
5819 N N   . ASP   B 135 ? 0.2296 0.1595 0.2579 -0.0178 0.0199  0.0294  135 ASP   B N   
5820 C CA  . ASP   B 135 ? 0.2440 0.1539 0.2795 -0.0145 0.0012  0.0384  135 ASP   B CA  
5821 C C   . ASP   B 135 ? 0.2208 0.1527 0.2641 -0.0063 0.0036  0.0355  135 ASP   B C   
5822 O O   . ASP   B 135 ? 0.2122 0.1496 0.2723 -0.0062 0.0081  0.0341  135 ASP   B O   
5823 C CB  . ASP   B 135 ? 0.2768 0.1646 0.3038 -0.0331 0.0010  0.0395  135 ASP   B CB  
5824 C CG  . ASP   B 135 ? 0.3093 0.1696 0.3424 -0.0537 -0.0057 0.0282  135 ASP   B CG  
5825 O OD1 . ASP   B 135 ? 0.3231 0.1578 0.3449 -0.0421 -0.0178 0.0330  135 ASP   B OD1 
5826 O OD2 . ASP   B 135 ? 0.3328 0.2071 0.3984 -0.0665 -0.0037 0.0091  135 ASP   B OD2 
5831 N N   . PRO   B 136 ? 0.2155 0.1543 0.2759 0.0163  -0.0126 0.0279  136 PRO   B N   
5832 C CA  . PRO   B 136 ? 0.1955 0.1468 0.2826 0.0131  -0.0073 0.0094  136 PRO   B CA  
5833 C C   . PRO   B 136 ? 0.1759 0.1359 0.2871 0.0126  -0.0035 0.0044  136 PRO   B C   
5834 O O   . PRO   B 136 ? 0.1600 0.1306 0.2841 0.0070  -0.0010 0.0132  136 PRO   B O   
5835 C CB  . PRO   B 136 ? 0.2045 0.1730 0.2863 0.0247  -0.0131 -0.0054 136 PRO   B CB  
5836 C CG  . PRO   B 136 ? 0.2207 0.1798 0.3035 0.0303  -0.0085 -0.0060 136 PRO   B CG  
5837 C CD  . PRO   B 136 ? 0.2248 0.1714 0.2954 0.0361  -0.0109 0.0067  136 PRO   B CD  
5845 N N   . ILE   B 137 ? 0.1880 0.1283 0.3030 0.0087  -0.0079 0.0025  137 ILE   B N   
5846 C CA  . ILE   B 137 ? 0.1972 0.1237 0.3089 -0.0038 -0.0033 -0.0001 137 ILE   B CA  
5847 C C   . ILE   B 137 ? 0.1869 0.1329 0.2950 -0.0110 -0.0029 0.0099  137 ILE   B C   
5848 O O   . ILE   B 137 ? 0.1761 0.1311 0.2867 -0.0130 -0.0008 0.0078  137 ILE   B O   
5849 C CB  . ILE   B 137 ? 0.2275 0.1349 0.3449 -0.0059 -0.0045 0.0007  137 ILE   B CB  
5850 C CG1 . ILE   B 137 ? 0.2493 0.1512 0.3867 0.0050  0.0029  -0.0064 137 ILE   B CG1 
5851 C CG2 . ILE   B 137 ? 0.2361 0.1411 0.3553 -0.0336 -0.0096 0.0092  137 ILE   B CG2 
5852 C CD1 . ILE   B 137 ? 0.2698 0.1943 0.4173 0.0205  -0.0011 0.0036  137 ILE   B CD1 
5864 N N   . HIS   B 138 ? 0.1923 0.1286 0.2885 -0.0098 0.0077  0.0089  138 HIS   B N   
5865 C CA  . HIS   B 138 ? 0.2030 0.1408 0.2856 -0.0071 0.0260  0.0202  138 HIS   B CA  
5866 C C   . HIS   B 138 ? 0.1837 0.1377 0.2732 -0.0055 0.0254  0.0234  138 HIS   B C   
5867 O O   . HIS   B 138 ? 0.1721 0.1406 0.2931 -0.0009 0.0343  0.0312  138 HIS   B O   
5868 C CB  . HIS   B 138 ? 0.2289 0.1508 0.2902 -0.0146 0.0390  0.0156  138 HIS   B CB  
5869 C CG  . HIS   B 138 ? 0.2426 0.1670 0.2919 -0.0157 0.0608  0.0350  138 HIS   B CG  
5870 N ND1 . HIS   B 138 ? 0.2479 0.1822 0.3198 -0.0101 0.0664  0.0295  138 HIS   B ND1 
5871 C CD2 . HIS   B 138 ? 0.2540 0.1761 0.2888 -0.0131 0.0661  0.0265  138 HIS   B CD2 
5872 C CE1 . HIS   B 138 ? 0.2504 0.1852 0.3115 -0.0089 0.0663  0.0342  138 HIS   B CE1 
5873 N NE2 . HIS   B 138 ? 0.2575 0.1709 0.2958 -0.0017 0.0694  0.0243  138 HIS   B NE2 
5881 N N   . SER   B 139 ? 0.1783 0.1246 0.2606 0.0034  0.0212  0.0189  139 SER   B N   
5882 C CA  . SER   B 139 ? 0.1731 0.1200 0.2502 0.0003  0.0204  0.0060  139 SER   B CA  
5883 C C   . SER   B 139 ? 0.1502 0.1137 0.2523 -0.0018 0.0178  0.0015  139 SER   B C   
5884 O O   . SER   B 139 ? 0.1530 0.1167 0.2604 0.0001  0.0087  0.0124  139 SER   B O   
5885 C CB  . SER   B 139 ? 0.1771 0.1233 0.2545 -0.0003 0.0093  0.0031  139 SER   B CB  
5886 O OG  . SER   B 139 ? 0.1778 0.1239 0.2691 -0.0041 -0.0133 0.0157  139 SER   B OG  
5892 N N   . LEU   B 140 ? 0.1521 0.1112 0.2496 -0.0072 0.0162  0.0002  140 LEU   B N   
5893 C CA  . LEU   B 140 ? 0.1499 0.1123 0.2549 -0.0048 0.0087  -0.0015 140 LEU   B CA  
5894 C C   . LEU   B 140 ? 0.1474 0.1113 0.2704 -0.0035 0.0019  -0.0049 140 LEU   B C   
5895 O O   . LEU   B 140 ? 0.1420 0.1233 0.2567 -0.0052 0.0004  0.0020  140 LEU   B O   
5896 C CB  . LEU   B 140 ? 0.1486 0.1087 0.2738 -0.0089 0.0168  -0.0109 140 LEU   B CB  
5897 C CG  . LEU   B 140 ? 0.1561 0.1148 0.2612 -0.0146 0.0094  0.0012  140 LEU   B CG  
5898 C CD1 . LEU   B 140 ? 0.1664 0.1261 0.2712 -0.0184 0.0116  -0.0016 140 LEU   B CD1 
5899 C CD2 . LEU   B 140 ? 0.1700 0.1284 0.2689 -0.0080 0.0009  -0.0125 140 LEU   B CD2 
5911 N N   . ARG   B 141 ? 0.1374 0.1140 0.2785 -0.0082 0.0130  0.0003  141 ARG   B N   
5912 C CA  . ARG   B 141 ? 0.1400 0.1162 0.3053 -0.0106 0.0196  -0.0016 141 ARG   B CA  
5913 C C   . ARG   B 141 ? 0.1343 0.1196 0.3024 -0.0179 0.0102  -0.0003 141 ARG   B C   
5914 O O   . ARG   B 141 ? 0.1397 0.1257 0.2914 -0.0143 0.0035  -0.0070 141 ARG   B O   
5915 C CB  . ARG   B 141 ? 0.1588 0.1246 0.3312 -0.0195 0.0301  -0.0001 141 ARG   B CB  
5916 C CG  . ARG   B 141 ? 0.1919 0.1506 0.3470 -0.0165 0.0363  0.0037  141 ARG   B CG  
5917 C CD  . ARG   B 141 ? 0.2312 0.1783 0.3473 -0.0086 0.0145  -0.0110 141 ARG   B CD  
5918 N NE  . ARG   B 141 ? 0.2525 0.1780 0.3351 -0.0324 0.0139  -0.0146 141 ARG   B NE  
5919 C CZ  . ARG   B 141 ? 0.2676 0.1688 0.3234 -0.0286 0.0269  -0.0205 141 ARG   B CZ  
5920 N NH1 . ARG   B 141 ? 0.2760 0.1590 0.3154 -0.0313 0.0256  -0.0248 141 ARG   B NH1 
5921 N NH2 . ARG   B 141 ? 0.2788 0.1820 0.3330 -0.0137 0.0217  -0.0076 141 ARG   B NH2 
5935 N N   . VAL   B 142 ? 0.1404 0.1184 0.2865 -0.0135 0.0149  -0.0056 142 VAL   B N   
5936 C CA  . VAL   B 142 ? 0.1374 0.1191 0.2703 -0.0079 0.0107  -0.0040 142 VAL   B CA  
5937 C C   . VAL   B 142 ? 0.1345 0.1138 0.2738 -0.0061 0.0089  -0.0061 142 VAL   B C   
5938 O O   . VAL   B 142 ? 0.1437 0.1137 0.2844 -0.0011 0.0142  -0.0022 142 VAL   B O   
5939 C CB  . VAL   B 142 ? 0.1477 0.1296 0.2698 -0.0019 0.0181  0.0071  142 VAL   B CB  
5940 C CG1 . VAL   B 142 ? 0.1510 0.1237 0.2707 0.0060  0.0202  0.0094  142 VAL   B CG1 
5941 C CG2 . VAL   B 142 ? 0.1723 0.1328 0.2778 -0.0008 0.0208  0.0137  142 VAL   B CG2 
5951 N N   . CYS   B 143 ? 0.1310 0.1153 0.2532 -0.0021 0.0066  0.0067  143 CYS   B N   
5952 C CA  . CYS   B 143 ? 0.1285 0.1158 0.2542 -0.0053 0.0021  0.0041  143 CYS   B CA  
5953 C C   . CYS   B 143 ? 0.1247 0.1176 0.2565 -0.0071 0.0098  0.0030  143 CYS   B C   
5954 O O   . CYS   B 143 ? 0.1350 0.1213 0.2591 -0.0076 0.0029  0.0023  143 CYS   B O   
5955 C CB  . CYS   B 143 ? 0.1361 0.1225 0.2573 -0.0101 0.0046  -0.0054 143 CYS   B CB  
5956 S SG  . CYS   B 143 ? 0.1384 0.1439 0.2290 -0.0054 0.0034  0.0025  143 CYS   B SG  
5962 N N   . VAL   B 144 ? 0.1326 0.1197 0.2704 -0.0045 0.0041  -0.0107 144 VAL   B N   
5963 C CA  . VAL   B 144 ? 0.1386 0.1288 0.2908 -0.0187 -0.0085 -0.0127 144 VAL   B CA  
5964 C C   . VAL   B 144 ? 0.1404 0.1334 0.2879 -0.0107 -0.0095 0.0016  144 VAL   B C   
5965 O O   . VAL   B 144 ? 0.1458 0.1558 0.3110 -0.0040 -0.0073 0.0203  144 VAL   B O   
5966 C CB  . VAL   B 144 ? 0.1676 0.1470 0.3430 -0.0159 -0.0215 -0.0281 144 VAL   B CB  
5967 C CG1 . VAL   B 144 ? 0.1896 0.1931 0.3690 -0.0143 -0.0263 -0.0298 144 VAL   B CG1 
5968 C CG2 . VAL   B 144 ? 0.1880 0.1497 0.3294 -0.0010 -0.0435 -0.0358 144 VAL   B CG2 
5978 N N   . ASP   B 145 ? 0.1437 0.1271 0.2958 -0.0082 -0.0094 -0.0130 145 ASP   B N   
5979 C CA  . ASP   B 145 ? 0.1399 0.1291 0.3174 -0.0083 0.0018  -0.0091 145 ASP   B CA  
5980 C C   . ASP   B 145 ? 0.1321 0.1354 0.3050 -0.0109 0.0056  -0.0073 145 ASP   B C   
5981 O O   . ASP   B 145 ? 0.1370 0.1502 0.3605 -0.0107 0.0078  -0.0210 145 ASP   B O   
5982 C CB  . ASP   B 145 ? 0.1534 0.1377 0.3557 -0.0140 0.0136  0.0044  145 ASP   B CB  
5983 C CG  . ASP   B 145 ? 0.1662 0.1418 0.3954 -0.0272 0.0222  -0.0045 145 ASP   B CG  
5984 O OD1 . ASP   B 145 ? 0.1715 0.1468 0.4096 -0.0257 -0.0166 -0.0183 145 ASP   B OD1 
5985 O OD2 . ASP   B 145 ? 0.1991 0.1513 0.4371 -0.0312 0.0509  0.0002  145 ASP   B OD2 
5990 N N   . THR   B 146 ? 0.1273 0.1289 0.2632 -0.0068 0.0027  0.0024  146 THR   B N   
5991 C CA  . THR   B 146 ? 0.1329 0.1210 0.2436 -0.0080 0.0062  -0.0001 146 THR   B CA  
5992 C C   . THR   B 146 ? 0.1352 0.1180 0.2382 -0.0069 0.0013  0.0027  146 THR   B C   
5993 O O   . THR   B 146 ? 0.1375 0.1196 0.2521 -0.0055 -0.0000 0.0042  146 THR   B O   
5994 C CB  . THR   B 146 ? 0.1415 0.1238 0.2517 -0.0057 0.0134  0.0032  146 THR   B CB  
5995 O OG1 . THR   B 146 ? 0.1442 0.1222 0.2530 -0.0037 0.0160  0.0152  146 THR   B OG1 
5996 C CG2 . THR   B 146 ? 0.1495 0.1284 0.2432 -0.0059 0.0100  0.0007  146 THR   B CG2 
6004 N N   . VAL   B 147 ? 0.1384 0.1194 0.2229 -0.0015 0.0136  0.0024  147 VAL   B N   
6005 C CA  . VAL   B 147 ? 0.1340 0.1157 0.2215 -0.0112 -0.0015 0.0015  147 VAL   B CA  
6006 C C   . VAL   B 147 ? 0.1293 0.1185 0.2422 -0.0187 -0.0058 -0.0049 147 VAL   B C   
6007 O O   . VAL   B 147 ? 0.1450 0.1308 0.2501 -0.0201 -0.0320 -0.0094 147 VAL   B O   
6008 C CB  . VAL   B 147 ? 0.1379 0.1312 0.2128 -0.0082 -0.0057 0.0036  147 VAL   B CB  
6009 C CG1 . VAL   B 147 ? 0.1381 0.1452 0.2041 -0.0090 -0.0046 0.0033  147 VAL   B CG1 
6010 C CG2 . VAL   B 147 ? 0.1396 0.1262 0.2206 -0.0060 -0.0103 0.0070  147 VAL   B CG2 
6020 N N   . ARG   B 148 ? 0.1339 0.1243 0.2318 -0.0105 -0.0186 -0.0103 148 ARG   B N   
6021 C CA  . ARG   B 148 ? 0.1397 0.1331 0.2298 -0.0100 -0.0271 -0.0095 148 ARG   B CA  
6022 C C   . ARG   B 148 ? 0.1444 0.1398 0.2165 -0.0092 -0.0294 -0.0047 148 ARG   B C   
6023 O O   . ARG   B 148 ? 0.1667 0.1675 0.2168 -0.0254 -0.0356 0.0050  148 ARG   B O   
6024 C CB  . ARG   B 148 ? 0.1420 0.1420 0.2289 -0.0032 -0.0247 -0.0195 148 ARG   B CB  
6025 C CG  . ARG   B 148 ? 0.1426 0.1602 0.2434 -0.0136 -0.0276 -0.0310 148 ARG   B CG  
6026 C CD  . ARG   B 148 ? 0.1474 0.1758 0.2513 0.0033  -0.0216 -0.0340 148 ARG   B CD  
6027 N NE  . ARG   B 148 ? 0.1527 0.1713 0.2473 0.0197  -0.0311 -0.0315 148 ARG   B NE  
6028 C CZ  . ARG   B 148 ? 0.1455 0.1643 0.2310 0.0114  -0.0232 -0.0196 148 ARG   B CZ  
6029 N NH1 . ARG   B 148 ? 0.1348 0.1717 0.2214 -0.0008 -0.0044 -0.0175 148 ARG   B NH1 
6030 N NH2 . ARG   B 148 ? 0.1680 0.1495 0.2263 0.0149  -0.0178 -0.0126 148 ARG   B NH2 
6044 N N   . THR   B 149 ? 0.1516 0.1349 0.2050 -0.0107 -0.0294 0.0071  149 THR   B N   
6045 C CA  . THR   B 149 ? 0.1567 0.1353 0.1981 -0.0139 -0.0253 0.0068  149 THR   B CA  
6046 C C   . THR   B 149 ? 0.1544 0.1330 0.1886 -0.0179 -0.0330 0.0017  149 THR   B C   
6047 O O   . THR   B 149 ? 0.1590 0.1357 0.2083 -0.0224 -0.0146 0.0049  149 THR   B O   
6048 C CB  . THR   B 149 ? 0.1607 0.1340 0.2025 -0.0180 -0.0322 -0.0005 149 THR   B CB  
6049 O OG1 . THR   B 149 ? 0.1603 0.1411 0.1957 -0.0261 -0.0305 0.0012  149 THR   B OG1 
6050 C CG2 . THR   B 149 ? 0.1662 0.1366 0.2274 -0.0070 -0.0204 0.0026  149 THR   B CG2 
6058 N N   . ASN   B 150 ? 0.1625 0.1311 0.1912 -0.0185 -0.0393 0.0001  150 ASN   B N   
6059 C CA  . ASN   B 150 ? 0.1700 0.1456 0.1918 -0.0175 -0.0283 -0.0027 150 ASN   B CA  
6060 C C   . ASN   B 150 ? 0.1563 0.1374 0.2019 -0.0148 -0.0253 0.0010  150 ASN   B C   
6061 O O   . ASN   B 150 ? 0.1692 0.1360 0.2189 -0.0249 -0.0474 0.0011  150 ASN   B O   
6062 C CB  . ASN   B 150 ? 0.1923 0.1781 0.2069 -0.0242 -0.0382 0.0077  150 ASN   B CB  
6063 C CG  . ASN   B 150 ? 0.2165 0.2237 0.2295 -0.0178 -0.0411 0.0218  150 ASN   B CG  
6064 O OD1 . ASN   B 150 ? 0.2247 0.2443 0.2503 -0.0300 -0.0572 0.0172  150 ASN   B OD1 
6065 N ND2 . ASN   B 150 ? 0.2284 0.2433 0.2677 -0.0078 -0.0434 0.0547  150 ASN   B ND2 
6072 N N   . VAL   B 151 ? 0.1449 0.1366 0.1911 -0.0192 -0.0286 0.0032  151 VAL   B N   
6073 C CA  . VAL   B 151 ? 0.1433 0.1439 0.1907 -0.0218 -0.0178 -0.0035 151 VAL   B CA  
6074 C C   . VAL   B 151 ? 0.1521 0.1349 0.1843 -0.0250 -0.0254 -0.0060 151 VAL   B C   
6075 O O   . VAL   B 151 ? 0.1622 0.1399 0.2061 -0.0232 -0.0151 -0.0120 151 VAL   B O   
6076 C CB  . VAL   B 151 ? 0.1692 0.1548 0.2018 -0.0063 -0.0157 -0.0043 151 VAL   B CB  
6077 C CG1 . VAL   B 151 ? 0.1764 0.1565 0.2328 -0.0109 -0.0051 -0.0173 151 VAL   B CG1 
6078 C CG2 . VAL   B 151 ? 0.1869 0.1672 0.1994 0.0014  -0.0220 -0.0009 151 VAL   B CG2 
6088 N N   . TYR   B 152 ? 0.1511 0.1234 0.1808 -0.0197 -0.0213 0.0006  152 TYR   B N   
6089 C CA  . TYR   B 152 ? 0.1550 0.1333 0.1800 -0.0251 -0.0117 -0.0097 152 TYR   B CA  
6090 C C   . TYR   B 152 ? 0.1501 0.1233 0.1737 -0.0173 -0.0142 -0.0118 152 TYR   B C   
6091 O O   . TYR   B 152 ? 0.1523 0.1271 0.1710 -0.0240 -0.0098 -0.0073 152 TYR   B O   
6092 C CB  . TYR   B 152 ? 0.1660 0.1521 0.1809 -0.0279 -0.0150 0.0065  152 TYR   B CB  
6093 C CG  . TYR   B 152 ? 0.1858 0.1584 0.1818 -0.0377 -0.0150 -0.0005 152 TYR   B CG  
6094 C CD1 . TYR   B 152 ? 0.1932 0.1723 0.1736 -0.0294 -0.0233 0.0049  152 TYR   B CD1 
6095 C CD2 . TYR   B 152 ? 0.2093 0.1768 0.1849 -0.0376 -0.0101 -0.0029 152 TYR   B CD2 
6096 C CE1 . TYR   B 152 ? 0.2039 0.1874 0.1868 -0.0302 -0.0336 0.0225  152 TYR   B CE1 
6097 C CE2 . TYR   B 152 ? 0.2184 0.1957 0.1903 -0.0417 -0.0186 0.0010  152 TYR   B CE2 
6098 C CZ  . TYR   B 152 ? 0.2175 0.2077 0.1747 -0.0373 -0.0474 0.0192  152 TYR   B CZ  
6099 O OH  . TYR   B 152 ? 0.2432 0.2466 0.2075 -0.0230 -0.0476 0.0169  152 TYR   B OH  
6109 N N   . LEU   B 153 ? 0.1483 0.1255 0.1719 -0.0248 -0.0151 -0.0058 153 LEU   B N   
6110 C CA  . LEU   B 153 ? 0.1541 0.1243 0.1686 -0.0185 -0.0028 -0.0154 153 LEU   B CA  
6111 C C   . LEU   B 153 ? 0.1535 0.1229 0.1934 -0.0213 -0.0075 -0.0149 153 LEU   B C   
6112 O O   . LEU   B 153 ? 0.1604 0.1428 0.2042 -0.0126 -0.0125 -0.0344 153 LEU   B O   
6113 C CB  . LEU   B 153 ? 0.1561 0.1165 0.1948 -0.0227 -0.0007 -0.0061 153 LEU   B CB  
6114 C CG  . LEU   B 153 ? 0.1489 0.1270 0.2207 -0.0225 -0.0007 -0.0045 153 LEU   B CG  
6115 C CD1 . LEU   B 153 ? 0.1520 0.1432 0.2147 -0.0273 0.0086  0.0030  153 LEU   B CD1 
6116 C CD2 . LEU   B 153 ? 0.1532 0.1389 0.2177 -0.0270 0.0130  -0.0005 153 LEU   B CD2 
6128 N N   . ALA   B 154 ? 0.1457 0.1240 0.1909 -0.0063 -0.0104 -0.0129 154 ALA   B N   
6129 C CA  . ALA   B 154 ? 0.1573 0.1327 0.2171 -0.0042 -0.0139 -0.0224 154 ALA   B CA  
6130 C C   . ALA   B 154 ? 0.1681 0.1359 0.2192 -0.0025 -0.0226 -0.0342 154 ALA   B C   
6131 O O   . ALA   B 154 ? 0.2019 0.1361 0.2407 0.0045  -0.0127 -0.0158 154 ALA   B O   
6132 C CB  . ALA   B 154 ? 0.1529 0.1539 0.2343 -0.0048 -0.0071 -0.0331 154 ALA   B CB  
6138 N N   . VAL   B 155 ? 0.1398 0.1272 0.2348 -0.0069 -0.0047 -0.0248 155 VAL   B N   
6139 C CA  . VAL   B 155 ? 0.1363 0.1254 0.2453 -0.0043 -0.0104 -0.0129 155 VAL   B CA  
6140 C C   . VAL   B 155 ? 0.1372 0.1285 0.2332 -0.0013 -0.0112 -0.0210 155 VAL   B C   
6141 O O   . VAL   B 155 ? 0.1588 0.1493 0.2606 0.0045  -0.0088 -0.0432 155 VAL   B O   
6142 C CB  . VAL   B 155 ? 0.1446 0.1445 0.2681 -0.0041 -0.0119 -0.0003 155 VAL   B CB  
6143 C CG1 . VAL   B 155 ? 0.1503 0.1477 0.2667 -0.0103 -0.0168 0.0024  155 VAL   B CG1 
6144 C CG2 . VAL   B 155 ? 0.1351 0.1581 0.3010 -0.0116 -0.0131 0.0246  155 VAL   B CG2 
6154 N N   . PHE   B 156 ? 0.1288 0.1407 0.2475 0.0050  -0.0021 -0.0178 156 PHE   B N   
6155 C CA  . PHE   B 156 ? 0.1362 0.1481 0.2784 0.0052  -0.0037 -0.0142 156 PHE   B CA  
6156 C C   . PHE   B 156 ? 0.1308 0.1581 0.3134 0.0113  -0.0103 -0.0353 156 PHE   B C   
6157 O O   . PHE   B 156 ? 0.1573 0.1803 0.3338 0.0235  0.0005  -0.0443 156 PHE   B O   
6158 C CB  . PHE   B 156 ? 0.1433 0.1454 0.2903 0.0038  -0.0158 -0.0140 156 PHE   B CB  
6159 C CG  . PHE   B 156 ? 0.1439 0.1534 0.2896 -0.0006 -0.0172 0.0004  156 PHE   B CG  
6160 C CD1 . PHE   B 156 ? 0.1476 0.1789 0.3196 0.0051  -0.0018 0.0339  156 PHE   B CD1 
6161 C CD2 . PHE   B 156 ? 0.1549 0.1633 0.2858 0.0095  -0.0246 0.0069  156 PHE   B CD2 
6162 C CE1 . PHE   B 156 ? 0.1525 0.1980 0.3323 0.0040  -0.0072 0.0402  156 PHE   B CE1 
6163 C CE2 . PHE   B 156 ? 0.1615 0.1872 0.3099 0.0120  -0.0144 0.0157  156 PHE   B CE2 
6164 C CZ  . PHE   B 156 ? 0.1517 0.1980 0.3326 0.0141  -0.0196 0.0276  156 PHE   B CZ  
6174 N N   . ASP   B 157 ? 0.1328 0.1446 0.3339 0.0133  -0.0137 -0.0204 157 ASP   B N   
6175 C CA  . ASP   B 157 ? 0.1437 0.1540 0.3580 0.0069  -0.0137 -0.0284 157 ASP   B CA  
6176 C C   . ASP   B 157 ? 0.1473 0.1477 0.3610 0.0088  -0.0127 -0.0428 157 ASP   B C   
6177 O O   . ASP   B 157 ? 0.1368 0.1465 0.3591 0.0053  -0.0138 -0.0372 157 ASP   B O   
6178 C CB  . ASP   B 157 ? 0.1698 0.1766 0.3673 0.0046  -0.0383 -0.0183 157 ASP   B CB  
6179 C CG  . ASP   B 157 ? 0.2141 0.1821 0.3890 0.0031  -0.0246 -0.0170 157 ASP   B CG  
6180 O OD1 . ASP   B 157 ? 0.2209 0.1787 0.4054 0.0048  -0.0183 -0.0046 157 ASP   B OD1 
6181 O OD2 . ASP   B 157 ? 0.2580 0.2006 0.4244 -0.0013 0.0008  -0.0162 157 ASP   B OD2 
6186 N N   . LYS   B 158 ? 0.1511 0.1720 0.3658 0.0079  0.0005  -0.0651 158 LYS   B N   
6187 C CA  . LYS   B 158 ? 0.1700 0.1904 0.3802 0.0024  0.0104  -0.0809 158 LYS   B CA  
6188 C C   . LYS   B 158 ? 0.1696 0.1771 0.3893 0.0040  -0.0032 -0.0758 158 LYS   B C   
6189 O O   . LYS   B 158 ? 0.1737 0.1695 0.4009 -0.0048 -0.0087 -0.0867 158 LYS   B O   
6190 C CB  . LYS   B 158 ? 0.1947 0.2241 0.3823 0.0047  0.0181  -0.1044 158 LYS   B CB  
6191 C CG  . LYS   B 158 ? 0.2336 0.2585 0.3937 0.0137  0.0204  -0.1128 158 LYS   B CG  
6192 C CD  . LYS   B 158 ? 0.2619 0.3015 0.4051 0.0156  0.0302  -0.1065 158 LYS   B CD  
6193 C CE  . LYS   B 158 ? 0.2812 0.3323 0.4264 0.0162  0.0273  -0.0947 158 LYS   B CE  
6194 N NZ  . LYS   B 158 ? 0.2768 0.3404 0.4279 0.0149  0.0308  -0.0897 158 LYS   B NZ  
6208 N N   . ASN   B 159 ? 0.1693 0.1662 0.4038 0.0041  -0.0074 -0.0606 159 ASN   B N   
6209 C CA  . ASN   B 159 ? 0.1790 0.1629 0.4117 0.0152  -0.0251 -0.0453 159 ASN   B CA  
6210 C C   . ASN   B 159 ? 0.1644 0.1477 0.4087 0.0054  -0.0357 -0.0349 159 ASN   B C   
6211 O O   . ASN   B 159 ? 0.1684 0.1388 0.4269 -0.0060 -0.0437 -0.0235 159 ASN   B O   
6212 C CB  . ASN   B 159 ? 0.1967 0.1767 0.4352 0.0254  -0.0418 -0.0336 159 ASN   B CB  
6213 C CG  . ASN   B 159 ? 0.2254 0.1909 0.4527 0.0297  -0.0517 -0.0498 159 ASN   B CG  
6214 O OD1 . ASN   B 159 ? 0.2425 0.2034 0.4623 0.0359  -0.0547 -0.0664 159 ASN   B OD1 
6215 N ND2 . ASN   B 159 ? 0.2288 0.1983 0.4767 0.0351  -0.0476 -0.0399 159 ASN   B ND2 
6222 N N   . LEU   B 160 ? 0.1516 0.1435 0.3897 0.0042  -0.0416 -0.0318 160 LEU   B N   
6223 C CA  . LEU   B 160 ? 0.1495 0.1463 0.3562 0.0040  -0.0384 -0.0152 160 LEU   B CA  
6224 C C   . LEU   B 160 ? 0.1471 0.1321 0.3476 -0.0072 -0.0308 -0.0266 160 LEU   B C   
6225 O O   . LEU   B 160 ? 0.1388 0.1388 0.3441 -0.0077 -0.0248 -0.0125 160 LEU   B O   
6226 C CB  . LEU   B 160 ? 0.1484 0.1547 0.3404 0.0034  -0.0417 -0.0061 160 LEU   B CB  
6227 C CG  . LEU   B 160 ? 0.1514 0.1715 0.3077 0.0090  -0.0373 -0.0003 160 LEU   B CG  
6228 C CD1 . LEU   B 160 ? 0.1601 0.1880 0.2986 0.0009  -0.0289 -0.0080 160 LEU   B CD1 
6229 C CD2 . LEU   B 160 ? 0.1582 0.1777 0.3104 0.0128  -0.0295 -0.0209 160 LEU   B CD2 
6241 N N   . TYR   B 161 ? 0.1455 0.1420 0.3455 -0.0140 -0.0071 -0.0374 161 TYR   B N   
6242 C CA  . TYR   B 161 ? 0.1598 0.1442 0.3251 -0.0207 0.0096  -0.0524 161 TYR   B CA  
6243 C C   . TYR   B 161 ? 0.1617 0.1420 0.3182 -0.0112 0.0102  -0.0424 161 TYR   B C   
6244 O O   . TYR   B 161 ? 0.1636 0.1392 0.3125 -0.0134 0.0060  -0.0430 161 TYR   B O   
6245 C CB  . TYR   B 161 ? 0.1727 0.1570 0.3159 -0.0281 0.0287  -0.0565 161 TYR   B CB  
6246 C CG  . TYR   B 161 ? 0.1941 0.1571 0.3081 -0.0320 0.0387  -0.0605 161 TYR   B CG  
6247 C CD1 . TYR   B 161 ? 0.1981 0.1506 0.2986 -0.0443 0.0341  -0.0620 161 TYR   B CD1 
6248 C CD2 . TYR   B 161 ? 0.2170 0.1662 0.3020 -0.0302 0.0360  -0.0538 161 TYR   B CD2 
6249 C CE1 . TYR   B 161 ? 0.2176 0.1730 0.3082 -0.0439 0.0324  -0.0550 161 TYR   B CE1 
6250 C CE2 . TYR   B 161 ? 0.2344 0.1834 0.3036 -0.0327 0.0328  -0.0504 161 TYR   B CE2 
6251 C CZ  . TYR   B 161 ? 0.2347 0.1914 0.3058 -0.0450 0.0276  -0.0428 161 TYR   B CZ  
6252 O OH  . TYR   B 161 ? 0.2639 0.2187 0.3278 -0.0489 0.0301  -0.0404 161 TYR   B OH  
6262 N N   . ASP   B 162 ? 0.1672 0.1391 0.3363 -0.0109 0.0006  -0.0478 162 ASP   B N   
6263 C CA  . ASP   B 162 ? 0.1780 0.1468 0.3354 -0.0056 -0.0049 -0.0521 162 ASP   B CA  
6264 C C   . ASP   B 162 ? 0.1702 0.1380 0.3298 -0.0114 0.0011  -0.0459 162 ASP   B C   
6265 O O   . ASP   B 162 ? 0.1760 0.1499 0.3271 -0.0203 -0.0107 -0.0307 162 ASP   B O   
6266 C CB  . ASP   B 162 ? 0.1976 0.1647 0.3643 0.0025  -0.0143 -0.0669 162 ASP   B CB  
6267 C CG  . ASP   B 162 ? 0.1985 0.1952 0.3846 0.0059  -0.0109 -0.0777 162 ASP   B CG  
6268 O OD1 . ASP   B 162 ? 0.1943 0.2166 0.3704 0.0014  0.0080  -0.0790 162 ASP   B OD1 
6269 O OD2 . ASP   B 162 ? 0.2108 0.2152 0.4207 0.0190  -0.0010 -0.0788 162 ASP   B OD2 
6274 N N   . LYS   B 163 ? 0.1641 0.1272 0.3290 -0.0131 -0.0165 -0.0299 163 LYS   B N   
6275 C CA  . LYS   B 163 ? 0.1731 0.1467 0.3329 -0.0225 -0.0155 -0.0096 163 LYS   B CA  
6276 C C   . LYS   B 163 ? 0.1476 0.1439 0.3229 -0.0188 -0.0212 -0.0012 163 LYS   B C   
6277 O O   . LYS   B 163 ? 0.1491 0.1547 0.3300 -0.0213 -0.0165 0.0016  163 LYS   B O   
6278 C CB  . LYS   B 163 ? 0.2125 0.1841 0.3765 -0.0214 -0.0201 0.0013  163 LYS   B CB  
6279 C CG  . LYS   B 163 ? 0.2922 0.2675 0.4412 -0.0314 -0.0092 0.0065  163 LYS   B CG  
6280 C CD  . LYS   B 163 ? 0.3603 0.3410 0.5091 -0.0440 -0.0113 0.0022  163 LYS   B CD  
6281 C CE  . LYS   B 163 ? 0.4081 0.3975 0.5580 -0.0533 -0.0120 0.0070  163 LYS   B CE  
6282 N NZ  . LYS   B 163 ? 0.4637 0.4637 0.5874 -0.0586 -0.0124 0.0061  163 LYS   B NZ  
6296 N N   . LEU   B 164 ? 0.1381 0.1274 0.3091 -0.0106 -0.0152 -0.0004 164 LEU   B N   
6297 C CA  . LEU   B 164 ? 0.1414 0.1248 0.2909 -0.0116 -0.0242 0.0006  164 LEU   B CA  
6298 C C   . LEU   B 164 ? 0.1492 0.1294 0.2844 -0.0089 -0.0298 -0.0007 164 LEU   B C   
6299 O O   . LEU   B 164 ? 0.1542 0.1503 0.2973 -0.0137 -0.0280 -0.0015 164 LEU   B O   
6300 C CB  . LEU   B 164 ? 0.1423 0.1264 0.2766 -0.0066 -0.0215 -0.0028 164 LEU   B CB  
6301 C CG  . LEU   B 164 ? 0.1471 0.1435 0.2820 -0.0140 -0.0138 0.0044  164 LEU   B CG  
6302 C CD1 . LEU   B 164 ? 0.1544 0.1452 0.2776 -0.0192 -0.0236 -0.0030 164 LEU   B CD1 
6303 C CD2 . LEU   B 164 ? 0.1597 0.1765 0.2893 -0.0066 0.0096  -0.0171 164 LEU   B CD2 
6315 N N   . VAL   B 165 ? 0.1762 0.1504 0.2968 -0.0210 -0.0339 -0.0089 165 VAL   B N   
6316 C CA  . VAL   B 165 ? 0.2165 0.1572 0.2970 -0.0360 -0.0514 -0.0089 165 VAL   B CA  
6317 C C   . VAL   B 165 ? 0.2474 0.1627 0.3272 -0.0455 -0.0738 -0.0138 165 VAL   B C   
6318 O O   . VAL   B 165 ? 0.2661 0.1752 0.3331 -0.0493 -0.0720 -0.0088 165 VAL   B O   
6319 C CB  . VAL   B 165 ? 0.2365 0.1736 0.2969 -0.0169 -0.0178 -0.0156 165 VAL   B CB  
6320 C CG1 . VAL   B 165 ? 0.2529 0.1785 0.3198 -0.0194 0.0027  -0.0110 165 VAL   B CG1 
6321 C CG2 . VAL   B 165 ? 0.2282 0.1776 0.2949 -0.0157 -0.0047 -0.0125 165 VAL   B CG2 
6331 N N   . SER   B 166 ? 0.2567 0.1482 0.3600 -0.0425 -0.0850 -0.0316 166 SER   B N   
6332 C CA  . SER   B 166 ? 0.2477 0.1504 0.3985 -0.0399 -0.0713 -0.0392 166 SER   B CA  
6333 C C   . SER   B 166 ? 0.2330 0.1586 0.4131 -0.0372 -0.0686 -0.0135 166 SER   B C   
6334 O O   . SER   B 166 ? 0.2357 0.1764 0.4422 -0.0463 -0.0878 -0.0361 166 SER   B O   
6335 C CB  . SER   B 166 ? 0.2444 0.1566 0.4200 -0.0319 -0.0627 -0.0511 166 SER   B CB  
6336 O OG  . SER   B 166 ? 0.2297 0.1622 0.4419 -0.0236 -0.0638 -0.0307 166 SER   B OG  
6342 N N   . SER   B 167 ? 0.2087 0.1512 0.3835 -0.0338 -0.0809 0.0201  167 SER   B N   
6343 C CA  . SER   B 167 ? 0.1978 0.1570 0.3643 -0.0294 -0.0575 0.0229  167 SER   B CA  
6344 C C   . SER   B 167 ? 0.1927 0.1730 0.3492 -0.0422 -0.0550 0.0370  167 SER   B C   
6345 O O   . SER   B 167 ? 0.1988 0.1833 0.3469 -0.0457 -0.0454 0.0302  167 SER   B O   
6346 C CB  . SER   B 167 ? 0.1867 0.1633 0.3593 -0.0235 -0.0302 0.0151  167 SER   B CB  
6347 O OG  . SER   B 167 ? 0.1778 0.1753 0.3507 -0.0150 -0.0139 0.0191  167 SER   B OG  
6353 N N   . PHE   B 168 ? 0.1954 0.1705 0.3487 -0.0456 -0.0348 0.0537  168 PHE   B N   
6354 C CA  . PHE   B 168 ? 0.2026 0.1712 0.3305 -0.0449 -0.0338 0.0386  168 PHE   B CA  
6355 C C   . PHE   B 168 ? 0.1729 0.1631 0.2764 -0.0292 -0.0208 0.0140  168 PHE   B C   
6356 O O   . PHE   B 168 ? 0.1994 0.1516 0.2851 -0.0011 -0.0174 -0.0012 168 PHE   B O   
6357 C CB  . PHE   B 168 ? 0.2228 0.1749 0.3372 -0.0543 -0.0536 0.0530  168 PHE   B CB  
6358 C CG  . PHE   B 168 ? 0.2480 0.1616 0.3227 -0.0612 -0.0590 0.0289  168 PHE   B CG  
6359 C CD1 . PHE   B 168 ? 0.2794 0.1660 0.3288 -0.0614 -0.0593 0.0255  168 PHE   B CD1 
6360 C CD2 . PHE   B 168 ? 0.2328 0.1538 0.3172 -0.0546 -0.0571 0.0331  168 PHE   B CD2 
6361 C CE1 . PHE   B 168 ? 0.2891 0.1788 0.3138 -0.0446 -0.0468 0.0329  168 PHE   B CE1 
6362 C CE2 . PHE   B 168 ? 0.2570 0.1609 0.3136 -0.0418 -0.0599 0.0187  168 PHE   B CE2 
6363 C CZ  . PHE   B 168 ? 0.2744 0.1625 0.3129 -0.0337 -0.0571 0.0320  168 PHE   B CZ  
6373 N N   . LEU   B 169 ? 0.1764 0.1774 0.2786 -0.0118 -0.0063 0.0096  169 LEU   B N   
6374 C CA  . LEU   B 169 ? 0.1991 0.2028 0.3057 -0.0172 0.0011  -0.0180 169 LEU   B CA  
6375 C C   . LEU   B 169 ? 0.2277 0.2238 0.3529 -0.0012 -0.0066 -0.0518 169 LEU   B C   
6376 O O   . LEU   B 169 ? 0.2543 0.2408 0.4026 0.0023  -0.0072 -0.0710 169 LEU   B O   
6377 C CB  . LEU   B 169 ? 0.2210 0.2435 0.3120 -0.0256 -0.0067 0.0089  169 LEU   B CB  
6378 C CG  . LEU   B 169 ? 0.2650 0.2842 0.3524 -0.0107 -0.0064 0.0099  169 LEU   B CG  
6379 C CD1 . LEU   B 169 ? 0.2883 0.3026 0.3566 -0.0121 -0.0101 0.0208  169 LEU   B CD1 
6380 C CD2 . LEU   B 169 ? 0.2634 0.2938 0.3572 0.0092  0.0074  -0.0026 169 LEU   B CD2 
6381 O OXT . LEU   B 169 ? 0.2500 0.2407 0.3548 0.0228  0.0024  -0.0573 169 LEU   B OXT 
6393 N N2  B A1A6Q C .   ? 0.1254 0.1812 0.1503 0.0125  0.0013  -0.0160 201 A1A6Q A N2  
6394 C C3  B A1A6Q C .   ? 0.1561 0.1974 0.1849 -0.0014 -0.0113 0.0066  201 A1A6Q A C3  
6395 C C6  B A1A6Q C .   ? 0.1203 0.1791 0.1437 0.0089  0.0074  -0.0066 201 A1A6Q A C6  
6396 C C9  B A1A6Q C .   ? 0.0783 0.1690 0.1272 -0.0169 0.0142  0.0185  201 A1A6Q A C9  
6397 C C1  B A1A6Q C .   ? 0.1620 0.1893 0.1859 -0.0019 -0.0082 0.0012  201 A1A6Q A C1  
6398 C C10 B A1A6Q C .   ? 0.0545 0.1509 0.1024 -0.0295 0.0014  0.0284  201 A1A6Q A C10 
6399 C C2  B A1A6Q C .   ? 0.1620 0.1961 0.1890 -0.0042 -0.0063 0.0087  201 A1A6Q A C2  
6400 C C4  B A1A6Q C .   ? 0.1517 0.1921 0.1699 0.0020  -0.0077 0.0033  201 A1A6Q A C4  
6401 C C5  B A1A6Q C .   ? 0.1181 0.1805 0.1431 0.0082  0.0041  -0.0006 201 A1A6Q A C5  
6402 C C7  B A1A6Q C .   ? 0.0992 0.1662 0.1256 -0.0034 0.0091  0.0130  201 A1A6Q A C7  
6403 C C8  B A1A6Q C .   ? 0.0985 0.1728 0.1296 -0.0019 0.0143  0.0046  201 A1A6Q A C8  
6404 N N1  B A1A6Q C .   ? 0.1325 0.1858 0.1504 0.0093  -0.0036 0.0046  201 A1A6Q A N1  
6405 N N3  B A1A6Q C .   ? 0.1108 0.1720 0.1332 -0.0018 0.0180  0.0034  201 A1A6Q A N3  
6406 N N4  B A1A6Q C .   ? 0.0826 0.1546 0.1125 -0.0076 -0.0064 0.0337  201 A1A6Q A N4  
6407 O O1  B A1A6Q C .   ? 0.1679 0.1848 0.1920 0.0013  -0.0060 -0.0073 201 A1A6Q A O1  
6408 O O2  B A1A6Q C .   ? 0.1599 0.2006 0.1912 -0.0052 -0.0080 0.0139  201 A1A6Q A O2  
6421 O O   . HOH   D .   ? 0.2109 0.1755 0.2521 0.0224  -0.0316 -0.0020 301 HOH   A O   
6422 O O   . HOH   D .   ? 0.3235 0.2322 0.3957 -0.0056 -0.0258 0.0549  302 HOH   A O   
6423 O O   . HOH   D .   ? 0.2999 0.6842 0.5636 -0.0225 -0.0812 0.2197  303 HOH   A O   
6424 O O   . HOH   D .   ? 0.5553 0.5741 0.4007 0.1633  -0.0776 -0.0708 304 HOH   A O   
6425 O O   . HOH   D .   ? 0.5624 0.4478 0.3813 0.1698  -0.1201 0.0541  305 HOH   A O   
6426 O O   . HOH   D .   ? 0.3991 0.6992 0.4666 -0.1097 0.0596  0.0297  306 HOH   A O   
6427 O O   . HOH   D .   ? 0.2683 0.5477 0.5593 0.1112  0.0429  0.1125  307 HOH   A O   
6428 O O   . HOH   D .   ? 0.2412 0.4994 0.4167 -0.0036 -0.0491 0.1174  308 HOH   A O   
6429 O O   . HOH   D .   ? 0.4095 0.3398 0.4716 0.0086  0.1096  -0.0342 309 HOH   A O   
6430 O O   . HOH   D .   ? 0.4674 0.2934 0.4524 -0.0295 0.1166  0.0807  310 HOH   A O   
6431 O O   . HOH   D .   ? 0.5257 0.4391 0.4393 -0.1839 -0.0861 0.2203  311 HOH   A O   
6432 O O   . HOH   D .   ? 0.6850 0.4946 0.4276 -0.1281 0.0290  0.1742  312 HOH   A O   
6433 O O   B HOH   D .   ? 0.2338 0.1820 0.1305 -0.0443 0.0071  -0.0241 313 HOH   A O   
6434 O O   . HOH   D .   ? 0.1512 0.3928 0.2827 -0.0141 0.0094  0.0979  314 HOH   A O   
6435 O O   . HOH   D .   ? 0.3624 0.4571 0.4870 0.1775  0.0170  0.0793  315 HOH   A O   
6436 O O   . HOH   D .   ? 0.2219 0.1740 0.3119 0.0288  -0.0919 -0.0625 316 HOH   A O   
6437 O O   . HOH   D .   ? 0.3385 0.3321 0.3389 -0.0189 0.1400  0.0203  317 HOH   A O   
6438 O O   . HOH   D .   ? 0.5034 0.5814 0.4647 -0.1316 -0.0996 -0.0690 318 HOH   A O   
6439 O O   . HOH   D .   ? 0.2109 0.1769 0.3652 -0.0367 -0.0016 -0.0213 319 HOH   A O   
6440 O O   . HOH   D .   ? 0.2770 0.2719 0.2693 -0.0742 0.0236  0.0620  320 HOH   A O   
6441 O O   . HOH   D .   ? 0.3277 0.2928 0.1772 -0.0357 0.0494  0.0246  321 HOH   A O   
6442 O O   . HOH   D .   ? 0.1721 0.3058 0.3226 0.0254  -0.0166 -0.0264 322 HOH   A O   
6443 O O   . HOH   D .   ? 0.1761 0.3563 0.4182 -0.0271 0.0270  -0.1164 323 HOH   A O   
6444 O O   . HOH   D .   ? 0.5684 0.4348 0.5142 0.0719  -0.0591 0.0483  324 HOH   A O   
6445 O O   . HOH   D .   ? 0.5222 0.2919 0.3231 -0.1359 0.0607  0.0372  325 HOH   A O   
6446 O O   . HOH   D .   ? 0.2514 0.2336 0.3087 -0.0237 0.0490  0.0652  326 HOH   A O   
6447 O O   . HOH   D .   ? 0.3292 0.4369 0.2769 -0.0100 0.0598  0.0367  327 HOH   A O   
6448 O O   . HOH   D .   ? 0.2667 0.4398 0.5294 -0.0119 0.1224  0.2023  328 HOH   A O   
6449 O O   . HOH   D .   ? 0.6789 0.3995 0.4136 -0.1049 0.1216  0.1391  329 HOH   A O   
6450 O O   . HOH   D .   ? 0.1469 0.1521 0.2475 -0.0182 0.0113  0.0084  330 HOH   A O   
6451 O O   . HOH   D .   ? 0.3520 0.5930 0.3909 -0.0781 -0.0050 0.1016  331 HOH   A O   
6452 O O   . HOH   D .   ? 0.2658 0.2233 0.4100 -0.0235 -0.0944 0.0834  332 HOH   A O   
6453 O O   . HOH   D .   ? 0.7591 0.3833 0.5592 -0.0983 -0.1313 0.0772  333 HOH   A O   
6454 O O   . HOH   D .   ? 0.4004 0.5139 0.4998 0.0422  0.0463  0.1217  334 HOH   A O   
6455 O O   . HOH   D .   ? 0.6372 0.4845 0.4912 0.0838  0.2316  -0.1170 335 HOH   A O   
6456 O O   . HOH   D .   ? 0.2313 0.4249 0.3762 -0.0058 -0.0458 0.1555  336 HOH   A O   
6457 O O   . HOH   D .   ? 0.2407 0.2335 0.3042 0.0485  0.0212  0.0535  337 HOH   A O   
6458 O O   . HOH   D .   ? 0.2454 0.2115 0.2778 0.0050  -0.0176 0.0627  338 HOH   A O   
6459 O O   . HOH   D .   ? 0.2737 0.4109 0.4087 -0.0396 -0.0638 -0.0146 339 HOH   A O   
6460 O O   . HOH   D .   ? 0.6635 0.5583 0.3400 -0.0398 -0.0446 0.1216  340 HOH   A O   
6461 O O   . HOH   D .   ? 0.4388 0.3254 0.3297 -0.0707 -0.0902 -0.0266 341 HOH   A O   
6462 O O   . HOH   D .   ? 0.3943 0.2196 0.4354 0.0449  -0.1177 0.0524  342 HOH   A O   
6463 O O   . HOH   D .   ? 0.4806 0.1973 0.4922 0.0478  0.0155  0.0157  343 HOH   A O   
6464 O O   . HOH   D .   ? 0.4558 0.5369 0.2703 -0.1114 0.0971  0.0730  344 HOH   A O   
6465 O O   . HOH   D .   ? 0.2472 0.3911 0.3607 0.0875  -0.0629 -0.0152 345 HOH   A O   
6466 O O   B HOH   D .   ? 0.1531 0.1501 0.1556 0.0182  0.0145  0.0457  346 HOH   A O   
6467 O O   . HOH   D .   ? 0.1745 0.1701 0.2333 0.0102  -0.0235 0.0293  347 HOH   A O   
6468 O O   A HOH   D .   ? 0.3333 0.1518 0.2086 0.0494  0.0324  0.0282  348 HOH   A O   
6469 O O   . HOH   D .   ? 0.5413 0.5022 0.4752 -0.0552 -0.0536 -0.0151 349 HOH   A O   
6470 O O   . HOH   D .   ? 0.4449 0.4839 0.4872 0.1547  0.1131  -0.0656 350 HOH   A O   
6471 O O   . HOH   D .   ? 0.2452 0.4283 0.3330 -0.0449 0.0351  0.0140  351 HOH   A O   
6472 O O   . HOH   D .   ? 0.2681 0.1982 0.2665 -0.0365 0.0084  -0.0069 352 HOH   A O   
6473 O O   . HOH   D .   ? 0.1422 0.2185 0.2415 0.0050  -0.0071 0.0584  353 HOH   A O   
6474 O O   . HOH   D .   ? 0.1836 0.2089 0.3952 0.0239  0.0869  -0.0040 354 HOH   A O   
6475 O O   . HOH   D .   ? 0.5908 0.3877 0.2996 0.0199  0.0277  0.1267  355 HOH   A O   
6476 O O   . HOH   D .   ? 0.2119 0.1732 0.2997 -0.0022 -0.0617 -0.0210 356 HOH   A O   
6477 O O   . HOH   D .   ? 0.1454 0.1932 0.2747 0.0162  -0.0074 0.0042  357 HOH   A O   
6478 O O   . HOH   D .   ? 0.3484 0.4373 0.4043 0.1718  0.0536  0.0341  358 HOH   A O   
6479 O O   . HOH   D .   ? 0.1309 0.1308 0.1385 -0.0018 0.0087  0.0060  359 HOH   A O   
6480 O O   . HOH   D .   ? 0.1878 0.2187 0.2525 -0.0045 -0.0067 0.0783  360 HOH   A O   
6481 O O   . HOH   D .   ? 0.3471 0.3035 0.3715 -0.1037 -0.0257 -0.0093 361 HOH   A O   
6482 O O   . HOH   D .   ? 0.3100 0.3464 0.2241 -0.0877 -0.0187 -0.0633 362 HOH   A O   
6483 O O   A HOH   D .   ? 0.2146 0.4031 0.2877 0.0904  0.0287  -0.0012 363 HOH   A O   
6484 O O   . HOH   D .   ? 0.3836 0.2172 0.4318 -0.0982 0.0713  0.0310  364 HOH   A O   
6485 O O   . HOH   D .   ? 0.1573 0.1344 0.2461 -0.0101 0.0221  -0.0103 365 HOH   A O   
6486 O O   . HOH   D .   ? 0.3839 0.6394 0.5070 -0.0544 -0.1208 0.0162  366 HOH   A O   
6487 O O   A HOH   D .   ? 0.1576 0.2955 0.2609 0.0581  0.0439  0.0898  367 HOH   A O   
6488 O O   A HOH   D .   ? 0.1495 0.1643 0.2167 0.0101  -0.0249 -0.0286 368 HOH   A O   
6489 O O   . HOH   D .   ? 0.1459 0.1535 0.1654 -0.0074 -0.0176 -0.0003 369 HOH   A O   
6490 O O   . HOH   D .   ? 0.3314 0.2278 0.4533 -0.0651 0.0003  0.0067  370 HOH   A O   
6491 O O   . HOH   D .   ? 0.1855 0.1960 0.2588 -0.0372 0.0058  0.0350  371 HOH   A O   
6492 O O   B HOH   D .   ? 0.1475 0.1918 0.1552 0.0153  -0.0217 0.0232  372 HOH   A O   
6493 O O   . HOH   D .   ? 0.4636 0.2545 0.4007 -0.1347 0.1742  -0.0769 373 HOH   A O   
6494 O O   . HOH   D .   ? 0.3111 0.3413 0.4783 -0.0591 -0.0997 -0.0657 374 HOH   A O   
6495 O O   . HOH   D .   ? 0.1689 0.1671 0.2417 -0.0193 0.0141  0.0367  375 HOH   A O   
6496 O O   . HOH   D .   ? 0.2109 0.1849 0.1920 -0.0020 -0.0015 0.0204  376 HOH   A O   
6497 O O   . HOH   D .   ? 0.3789 0.2073 0.2526 0.1099  0.0580  0.0205  377 HOH   A O   
6498 O O   . HOH   D .   ? 0.3164 0.2438 0.3581 -0.0118 -0.0373 0.0914  378 HOH   A O   
6499 O O   . HOH   D .   ? 0.1981 0.2150 0.2240 -0.0266 -0.0362 0.0406  379 HOH   A O   
6500 O O   B HOH   D .   ? 0.1778 0.1946 0.1848 0.0080  -0.0144 -0.0143 380 HOH   A O   
6501 O O   . HOH   D .   ? 0.1882 0.2429 0.3862 0.0235  0.0811  -0.0524 381 HOH   A O   
6502 O O   . HOH   D .   ? 0.2758 0.4172 0.2970 0.0484  0.0732  0.1653  382 HOH   A O   
6503 O O   . HOH   D .   ? 0.2988 0.3582 0.3707 -0.0192 -0.0119 0.0612  383 HOH   A O   
6504 O O   . HOH   D .   ? 0.6140 0.4585 0.5423 -0.1411 0.0326  0.0928  384 HOH   A O   
6505 O O   B HOH   D .   ? 0.1686 0.1556 0.0596 0.0124  0.0076  0.0192  385 HOH   A O   
6506 O O   . HOH   D .   ? 0.2614 0.2647 0.3821 -0.0634 0.0897  -0.0016 386 HOH   A O   
6507 O O   . HOH   D .   ? 0.4179 0.3916 0.4730 0.1372  0.1137  -0.0845 387 HOH   A O   
6508 O O   . HOH   D .   ? 0.2964 0.3160 0.2060 0.0366  0.0621  0.0051  388 HOH   A O   
6509 O O   . HOH   D .   ? 0.4666 0.5044 0.5165 -0.1069 -0.0309 0.0982  389 HOH   A O   
6510 O O   . HOH   D .   ? 0.1433 0.1703 0.1950 0.0103  -0.0267 -0.0234 390 HOH   A O   
6511 O O   . HOH   D .   ? 0.2632 0.1925 0.1935 -0.0581 0.0310  0.0245  391 HOH   A O   
6512 O O   . HOH   D .   ? 0.2183 0.2002 0.2888 -0.0018 -0.0449 0.0344  392 HOH   A O   
6513 O O   . HOH   D .   ? 0.1739 0.2171 0.1946 -0.0059 0.0083  0.0627  393 HOH   A O   
6514 O O   . HOH   D .   ? 0.4879 0.2807 0.4185 0.0854  -0.0222 -0.0533 394 HOH   A O   
6515 O O   . HOH   D .   ? 0.3043 0.5785 0.3937 0.0908  0.0872  -0.0850 395 HOH   A O   
6516 O O   . HOH   D .   ? 0.2630 0.3117 0.3154 -0.0105 0.0968  -0.0120 396 HOH   A O   
6517 O O   . HOH   D .   ? 0.1652 0.1704 0.2976 0.0190  -0.0295 0.0357  397 HOH   A O   
6518 O O   . HOH   D .   ? 0.1672 0.2645 0.3498 -0.0080 0.0662  0.0815  398 HOH   A O   
6519 O O   A HOH   D .   ? 0.1536 0.1498 0.1490 -0.0005 -0.0194 0.0003  399 HOH   A O   
6520 O O   . HOH   D .   ? 0.2505 0.4100 0.3836 -0.0260 0.1067  -0.0828 400 HOH   A O   
6521 O O   . HOH   D .   ? 0.2850 0.2990 0.2412 -0.0732 -0.0802 0.0338  401 HOH   A O   
6522 O O   . HOH   D .   ? 0.1785 0.1817 0.3951 0.0320  0.1047  0.0948  402 HOH   A O   
6523 O O   . HOH   D .   ? 0.2276 0.1662 0.2864 0.0021  -0.0341 0.0040  403 HOH   A O   
6524 O O   . HOH   D .   ? 0.2423 0.1730 0.2772 -0.0068 0.0005  0.0270  404 HOH   A O   
6525 O O   . HOH   D .   ? 0.3272 0.4408 0.3288 0.1477  -0.0714 -0.1347 405 HOH   A O   
6526 O O   B HOH   D .   ? 0.1610 0.3341 0.3712 -0.0708 0.0347  -0.0423 406 HOH   A O   
6527 O O   . HOH   D .   ? 0.1368 0.1404 0.1934 0.0037  -0.0144 0.0079  407 HOH   A O   
6528 O O   . HOH   D .   ? 0.1753 0.1381 0.1744 -0.0215 0.0095  0.0036  408 HOH   A O   
6529 O O   A HOH   D .   ? 0.2840 0.2181 0.4112 -0.0332 0.0965  0.0123  409 HOH   A O   
6530 O O   . HOH   D .   ? 0.1912 0.2515 0.3445 -0.0014 -0.0180 0.0110  410 HOH   A O   
6531 O O   . HOH   D .   ? 0.5396 0.4531 0.1990 0.0075  0.0803  0.0750  411 HOH   A O   
6532 O O   . HOH   D .   ? 0.2558 0.2180 0.2717 -0.0572 -0.0049 0.0678  412 HOH   A O   
6533 O O   . HOH   D .   ? 0.6067 0.6220 0.5783 -0.0922 0.0593  0.0320  413 HOH   A O   
6534 O O   . HOH   D .   ? 0.5028 0.6224 0.5285 0.0439  0.0077  0.0290  414 HOH   A O   
6535 O O   . HOH   D .   ? 0.2945 0.3887 0.6467 -0.0270 0.0935  -0.0561 415 HOH   A O   
6536 O O   . HOH   D .   ? 0.3538 0.3073 0.5050 0.0805  0.0773  0.0157  416 HOH   A O   
6537 O O   . HOH   D .   ? 0.2137 0.2299 0.3841 0.0232  -0.0508 -0.0491 417 HOH   A O   
6538 O O   . HOH   D .   ? 0.2323 0.2744 0.3166 0.0002  -0.0070 -0.0563 418 HOH   A O   
6539 O O   . HOH   D .   ? 0.3874 0.3274 0.2656 -0.0106 -0.1181 0.0254  419 HOH   A O   
6540 O O   . HOH   D .   ? 0.4465 0.6073 0.3516 -0.0764 -0.0360 0.1525  420 HOH   A O   
6541 O O   . HOH   D .   ? 0.1500 0.1723 0.3066 -0.0038 -0.0006 0.0215  421 HOH   A O   
6542 O O   . HOH   D .   ? 0.2943 0.3705 0.4852 -0.0163 0.0915  0.0016  422 HOH   A O   
6543 O O   . HOH   D .   ? 0.2009 0.1697 0.1612 -0.0034 0.0156  0.0178  423 HOH   A O   
6544 O O   . HOH   D .   ? 0.1994 0.2729 0.2530 -0.0048 -0.0468 0.0370  424 HOH   A O   
6545 O O   . HOH   D .   ? 0.3247 0.1284 0.2287 0.0001  -0.0431 0.0125  425 HOH   A O   
6546 O O   . HOH   D .   ? 0.2601 0.6026 0.1814 -0.0477 0.0474  -0.0061 426 HOH   A O   
6547 O O   . HOH   D .   ? 0.5388 0.4663 0.5486 -0.0886 -0.0549 -0.1263 427 HOH   A O   
6548 O O   . HOH   D .   ? 0.2309 0.4160 0.2768 0.1584  0.0011  0.0265  428 HOH   A O   
6549 O O   . HOH   D .   ? 0.1599 0.2087 0.3200 -0.0206 0.0022  0.0620  429 HOH   A O   
6550 O O   . HOH   D .   ? 0.6539 0.3949 0.4873 0.1689  -0.0728 0.1395  430 HOH   A O   
6551 O O   . HOH   D .   ? 0.4879 0.4425 0.3708 -0.0033 -0.1423 0.0321  431 HOH   A O   
6552 O O   . HOH   D .   ? 0.4573 0.2243 0.5220 -0.0869 -0.2209 0.1080  432 HOH   A O   
6553 O O   . HOH   D .   ? 0.5453 0.7012 0.4164 0.0628  0.2371  -0.0800 433 HOH   A O   
6554 O O   . HOH   D .   ? 0.4970 0.5900 0.6061 -0.1660 0.0093  -0.1016 434 HOH   A O   
6555 O O   . HOH   D .   ? 0.3705 0.2629 0.2686 -0.0218 -0.0241 0.0215  435 HOH   A O   
6556 O O   A HOH   D .   ? 0.2569 0.2078 0.3122 0.0338  0.0559  0.0903  436 HOH   A O   
6557 O O   A HOH   D .   ? 0.1754 0.1379 0.1621 -0.0066 -0.0183 -0.0105 437 HOH   A O   
6558 O O   . HOH   D .   ? 0.3613 0.2624 0.1828 -0.0848 0.0424  0.0490  438 HOH   A O   
6559 O O   . HOH   D .   ? 0.2686 0.1688 0.2816 0.0001  0.0151  0.0124  439 HOH   A O   
6560 O O   . HOH   D .   ? 0.1806 0.2149 0.4918 -0.0183 -0.0680 0.0468  440 HOH   A O   
6561 O O   . HOH   D .   ? 0.6368 0.6729 0.5733 0.0660  -0.1249 0.0396  441 HOH   A O   
6562 O O   . HOH   D .   ? 0.8354 0.8744 0.6729 -0.0007 0.0280  -0.0612 442 HOH   A O   
6563 O O   . HOH   D .   ? 0.6629 0.7075 0.4264 0.1928  -0.1174 0.1871  443 HOH   A O   
6564 O O   . HOH   D .   ? 0.5206 0.3397 0.6363 0.0718  -0.0279 -0.1105 444 HOH   A O   
6565 O O   . HOH   D .   ? 0.4840 0.4436 0.4841 0.0139  0.0383  0.1927  445 HOH   A O   
6566 O O   . HOH   D .   ? 0.3448 0.2974 0.3406 0.1612  -0.0387 -0.0344 446 HOH   A O   
6567 O O   B HOH   D .   ? 0.1836 0.1243 0.1747 -0.0143 0.0237  0.0249  447 HOH   A O   
6568 O O   . HOH   D .   ? 0.2935 0.2891 0.4923 -0.0066 0.1108  -0.0870 448 HOH   A O   
6569 O O   B HOH   D .   ? 0.1968 0.2313 0.2089 0.0158  0.0225  -0.0002 449 HOH   A O   
6570 O O   . HOH   D .   ? 0.2370 0.2035 0.2765 0.0137  0.0274  0.0200  450 HOH   A O   
6571 O O   . HOH   D .   ? 0.4566 0.4008 0.4742 -0.1299 -0.1045 -0.1126 451 HOH   A O   
6572 O O   . HOH   D .   ? 0.5927 0.4931 0.6913 0.0332  -0.1325 0.1467  452 HOH   A O   
6573 O O   . HOH   D .   ? 0.2186 0.2675 0.2585 0.0115  -0.0135 -0.0605 453 HOH   A O   
6574 O O   B HOH   D .   ? 0.0817 0.1792 0.1655 -0.0280 0.0274  0.0538  454 HOH   A O   
6575 O O   A HOH   D .   ? 0.2948 0.1834 0.4046 0.0218  0.0752  0.1024  455 HOH   A O   
6576 O O   . HOH   D .   ? 0.5969 0.3447 0.4297 -0.0184 0.0446  0.0943  456 HOH   A O   
6577 O O   . HOH   D .   ? 0.5024 0.4550 0.4508 0.0140  -0.0006 0.1148  457 HOH   A O   
6578 O O   B HOH   D .   ? 0.1156 0.1925 0.1358 0.0199  0.0351  0.0197  458 HOH   A O   
6579 O O   . HOH   D .   ? 0.4633 0.3523 0.4841 0.0274  0.0455  0.0617  459 HOH   A O   
6580 O O   . HOH   D .   ? 0.2680 0.3165 0.3608 0.0819  -0.0045 0.0575  460 HOH   A O   
6581 O O   . HOH   D .   ? 0.6460 0.5483 0.4510 -0.0567 0.1262  0.0707  461 HOH   A O   
6582 O O   . HOH   D .   ? 0.3072 0.2622 0.3342 -0.0643 0.0075  -0.0455 462 HOH   A O   
6583 O O   . HOH   D .   ? 0.6951 0.7800 0.4946 0.0604  -0.0127 -0.0192 463 HOH   A O   
6584 O O   . HOH   D .   ? 0.6728 0.5175 0.5139 0.0548  0.1787  0.2019  464 HOH   A O   
6585 O O   . HOH   D .   ? 0.3010 0.5328 0.5024 -0.1671 0.0670  -0.1688 465 HOH   A O   
6586 O O   . HOH   D .   ? 0.4102 0.4773 0.4624 0.1044  -0.0209 0.1389  466 HOH   A O   
6587 O O   . HOH   D .   ? 0.2863 0.4007 0.4369 -0.0314 -0.0257 -0.0259 467 HOH   A O   
6588 O O   . HOH   D .   ? 0.2662 0.1769 0.2560 0.0208  -0.0851 -0.0217 468 HOH   A O   
6589 O O   . HOH   D .   ? 0.4091 0.6202 0.3599 -0.0786 -0.0692 0.2181  469 HOH   A O   
6590 O O   . HOH   D .   ? 0.2800 0.2434 0.5143 0.0434  -0.1224 -0.0390 470 HOH   A O   
6591 O O   . HOH   D .   ? 0.2482 0.2603 0.3441 -0.0764 0.0381  -0.0309 471 HOH   A O   
6592 O O   . HOH   D .   ? 0.2873 0.4061 0.5252 0.0620  0.0065  -0.1798 472 HOH   A O   
6593 O O   . HOH   D .   ? 0.5715 0.4714 0.4527 0.0457  0.1418  0.0727  473 HOH   A O   
6594 O O   . HOH   D .   ? 0.6051 0.3046 0.7055 0.0761  0.0618  0.1982  474 HOH   A O   
6595 O O   . HOH   D .   ? 0.4060 0.5284 0.3799 0.0347  -0.0553 -0.0560 475 HOH   A O   
6596 O O   . HOH   D .   ? 0.3431 0.2455 0.3886 -0.0025 0.0785  0.0028  476 HOH   A O   
6597 O O   . HOH   D .   ? 0.5049 0.5498 0.5899 -0.1750 -0.1233 0.0817  477 HOH   A O   
6598 O O   . HOH   D .   ? 0.4794 0.4816 0.4801 -0.2154 -0.0714 -0.0218 478 HOH   A O   
6599 O O   . HOH   D .   ? 0.5333 0.5171 0.4685 0.0984  -0.1021 -0.1105 479 HOH   A O   
6600 O O   . HOH   D .   ? 0.4271 0.4488 0.3380 -0.0624 -0.0386 -0.0200 480 HOH   A O   
6601 O O   . HOH   D .   ? 0.2323 0.2209 0.2655 0.0146  -0.0075 -0.0171 481 HOH   A O   
6602 O O   . HOH   D .   ? 0.6672 0.4834 0.5974 -0.0450 0.0554  -0.0701 482 HOH   A O   
6603 O O   . HOH   D .   ? 0.7310 0.3816 0.3328 -0.0365 -0.1245 0.0073  483 HOH   A O   
6604 O O   . HOH   D .   ? 0.5258 0.4093 0.4111 0.0625  0.0088  -0.1292 484 HOH   A O   
6605 O O   . HOH   D .   ? 0.4204 0.4961 0.2819 -0.0350 0.0055  0.0299  485 HOH   A O   
6606 O O   . HOH   D .   ? 0.4175 0.2609 0.3472 -0.0659 -0.1191 0.0762  486 HOH   A O   
6607 O O   . HOH   D .   ? 0.5786 0.4111 0.4186 -0.0239 0.1605  -0.0080 487 HOH   A O   
6608 O O   B HOH   D .   ? 0.3086 0.2590 0.1927 0.0342  0.0213  0.0648  488 HOH   A O   
6609 O O   . HOH   D .   ? 0.2980 0.4983 0.3633 0.1143  0.1133  0.2287  489 HOH   A O   
6610 O O   . HOH   D .   ? 0.2980 0.4731 0.4401 0.0430  0.1280  0.1059  490 HOH   A O   
6611 O O   . HOH   D .   ? 0.5609 0.6636 0.4221 -0.1119 0.1153  0.1273  491 HOH   A O   
6612 O O   . HOH   D .   ? 0.5273 0.5839 0.4158 0.1569  -0.1502 0.0109  492 HOH   A O   
6613 O O   . HOH   D .   ? 0.4965 0.5266 0.6438 0.0725  0.0873  -0.1069 493 HOH   A O   
6614 O O   . HOH   D .   ? 0.3707 0.3520 0.2740 -0.0514 0.0987  -0.0283 494 HOH   A O   
6615 O O   . HOH   D .   ? 0.5365 0.5358 0.5325 -0.0145 -0.1166 0.0648  495 HOH   A O   
6616 O O   B HOH   D .   ? 0.2328 0.1671 0.2295 -0.0120 0.0488  -0.0096 496 HOH   A O   
6617 O O   . HOH   D .   ? 0.6027 0.5248 0.4429 -0.0837 -0.0964 -0.0704 497 HOH   A O   
6618 O O   . HOH   D .   ? 0.2567 0.2697 0.6084 0.0020  -0.1075 0.0363  498 HOH   A O   
6619 O O   . HOH   D .   ? 0.4889 0.3376 0.4590 -0.0310 0.2303  0.0315  499 HOH   A O   
6620 O O   . HOH   D .   ? 0.2916 0.2143 0.5621 0.0075  0.0487  0.0806  500 HOH   A O   
6621 O O   . HOH   D .   ? 0.6313 0.2549 0.4233 -0.0643 0.0632  0.0566  501 HOH   A O   
6622 O O   . HOH   D .   ? 0.3809 0.2876 0.4422 -0.0787 0.0471  0.0716  502 HOH   A O   
6623 O O   . HOH   D .   ? 0.2599 0.2860 0.4712 -0.0147 0.1053  -0.0436 503 HOH   A O   
6624 O O   . HOH   D .   ? 0.3868 0.7885 0.5278 -0.1064 -0.0032 0.2023  504 HOH   A O   
6625 O O   . HOH   D .   ? 0.2239 0.3217 0.3588 0.0514  -0.0570 0.0638  505 HOH   A O   
6626 O O   B HOH   D .   ? 0.1676 0.2836 0.2486 0.0225  0.0239  0.0477  506 HOH   A O   
6627 O O   . HOH   D .   ? 0.4619 0.2429 0.4230 -0.1424 0.0109  0.0354  507 HOH   A O   
6628 O O   . HOH   D .   ? 0.3097 0.4206 0.4006 0.0523  -0.0354 0.0329  508 HOH   A O   
6629 O O   . HOH   D .   ? 0.5352 0.5934 0.4650 0.0726  -0.0699 0.0507  509 HOH   A O   
6630 O O   . HOH   D .   ? 0.6050 0.4132 0.5196 -0.0609 -0.0259 0.0947  510 HOH   A O   
6631 O O   . HOH   D .   ? 0.2948 0.4721 0.3377 -0.0603 -0.0244 -0.0892 511 HOH   A O   
6632 O O   . HOH   D .   ? 0.4676 0.6858 0.4761 0.2709  -0.0180 0.1498  512 HOH   A O   
6633 O O   . HOH   D .   ? 0.3177 0.2390 0.4354 0.0102  0.0429  0.0624  513 HOH   A O   
6634 O O   . HOH   D .   ? 0.4674 0.5162 0.4184 -0.0247 -0.0210 -0.1288 514 HOH   A O   
6635 O O   A HOH   D .   ? 0.3600 0.7340 0.3569 0.0284  0.1247  0.0271  515 HOH   A O   
6636 O O   . HOH   D .   ? 0.2838 0.6463 0.3866 0.0424  0.0377  -0.0289 516 HOH   A O   
6637 O O   . HOH   D .   ? 0.4314 0.4789 0.4048 0.1658  -0.0169 0.0734  517 HOH   A O   
6638 O O   . HOH   D .   ? 0.4646 0.5994 0.5091 -0.0500 -0.0941 0.0092  518 HOH   A O   
6639 O O   . HOH   D .   ? 0.2976 0.3703 0.5249 -0.0000 -0.0887 0.1881  519 HOH   A O   
6640 O O   . HOH   E .   ? 0.2323 0.2084 0.3348 0.0286  0.0769  0.0380  201 HOH   B O   
6641 O O   . HOH   E .   ? 0.4557 0.4545 0.2902 0.0216  -0.0624 -0.1510 202 HOH   B O   
6642 O O   . HOH   E .   ? 0.4727 0.3406 0.3748 -0.0291 -0.0171 -0.1249 203 HOH   B O   
6643 O O   . HOH   E .   ? 0.3255 0.5507 0.4889 -0.0108 0.1702  -0.1939 204 HOH   B O   
6644 O O   . HOH   E .   ? 0.3682 0.6913 0.3740 0.0874  0.0116  0.2313  205 HOH   B O   
6645 O O   . HOH   E .   ? 0.6251 0.4502 0.4876 0.0668  0.1294  0.0165  206 HOH   B O   
6646 O O   . HOH   E .   ? 0.6286 0.6049 0.5914 0.1835  0.0272  -0.0043 207 HOH   B O   
6647 O O   . HOH   E .   ? 0.4533 0.5593 0.4029 0.2595  -0.1313 -0.0207 208 HOH   B O   
6648 O O   . HOH   E .   ? 0.3825 0.3049 0.6174 -0.0522 0.0897  -0.0281 209 HOH   B O   
6649 O O   . HOH   E .   ? 0.4919 0.4073 0.6339 0.0279  -0.1018 0.2531  210 HOH   B O   
6650 O O   . HOH   E .   ? 0.4269 0.4155 0.3838 -0.0108 -0.1016 0.0637  211 HOH   B O   
6651 O O   . HOH   E .   ? 0.3113 0.1949 0.5314 0.0162  0.1818  0.0869  212 HOH   B O   
6652 O O   . HOH   E .   ? 0.2855 0.2909 0.6352 0.0781  -0.1220 0.0425  213 HOH   B O   
6653 O O   . HOH   E .   ? 0.4136 0.4822 0.4043 0.2064  -0.0279 0.0516  214 HOH   B O   
6654 O O   . HOH   E .   ? 0.3941 0.4440 0.5217 -0.1186 0.0091  -0.1213 215 HOH   B O   
6655 O O   . HOH   E .   ? 0.1585 0.1826 0.2855 -0.0198 -0.0038 0.0037  216 HOH   B O   
6656 O O   . HOH   E .   ? 0.3778 0.4188 0.5057 -0.1588 -0.0023 0.0686  217 HOH   B O   
6657 O O   . HOH   E .   ? 0.1790 0.2338 0.3080 0.0050  0.0266  -0.0209 218 HOH   B O   
6658 O O   . HOH   E .   ? 0.4081 0.4772 0.4097 0.0357  0.0748  -0.1252 219 HOH   B O   
6659 O O   . HOH   E .   ? 0.3785 0.5203 0.4677 0.2375  0.0182  -0.0547 220 HOH   B O   
6660 O O   . HOH   E .   ? 0.2798 0.4259 0.4319 0.0348  -0.0813 0.0267  221 HOH   B O   
6661 O O   . HOH   E .   ? 0.5766 0.3161 0.4084 -0.1823 0.0547  0.0285  222 HOH   B O   
6662 O O   . HOH   E .   ? 0.4846 0.2017 0.3664 -0.0163 -0.1115 0.0108  223 HOH   B O   
6663 O O   . HOH   E .   ? 0.5753 0.5623 0.3297 0.0976  0.0068  0.0220  224 HOH   B O   
6664 O O   . HOH   E .   ? 0.2583 0.1829 0.2779 -0.0329 0.1062  -0.0022 225 HOH   B O   
6665 O O   . HOH   E .   ? 0.2653 0.3738 0.3516 -0.0886 0.0518  -0.0593 226 HOH   B O   
6666 O O   . HOH   E .   ? 0.4415 0.4337 0.6204 -0.0526 -0.1506 -0.0897 227 HOH   B O   
6667 O O   . HOH   E .   ? 0.4385 0.6732 0.3733 0.2493  -0.0048 -0.0425 228 HOH   B O   
6668 O O   . HOH   E .   ? 0.1714 0.1980 0.3151 -0.0092 0.0107  0.0084  229 HOH   B O   
6669 O O   . HOH   E .   ? 0.2674 0.2468 0.3236 0.0315  0.0291  -0.0784 230 HOH   B O   
6670 O O   . HOH   E .   ? 0.6622 0.4245 0.5055 0.1665  -0.0065 -0.1337 231 HOH   B O   
6671 O O   . HOH   E .   ? 0.3880 0.3475 0.5490 0.0488  0.0274  -0.0077 232 HOH   B O   
6672 O O   . HOH   E .   ? 0.2185 0.2277 0.3875 -0.0385 -0.0044 -0.0541 233 HOH   B O   
6673 O O   . HOH   E .   ? 0.3807 0.2561 0.4224 0.0719  -0.0257 -0.0848 234 HOH   B O   
6674 O O   . HOH   E .   ? 0.3927 0.3462 0.2293 0.0400  0.0688  0.0473  235 HOH   B O   
6675 O O   . HOH   E .   ? 0.3667 0.2391 0.4034 0.0524  -0.0994 -0.1035 236 HOH   B O   
6676 O O   . HOH   E .   ? 0.2089 0.1286 0.3420 0.0123  -0.0559 -0.0162 237 HOH   B O   
6677 O O   . HOH   E .   ? 0.2184 0.2348 0.3081 -0.0454 0.0059  -0.0266 238 HOH   B O   
6678 O O   . HOH   E .   ? 0.2246 0.1964 0.2278 -0.0315 -0.0487 0.0098  239 HOH   B O   
6679 O O   . HOH   E .   ? 0.1471 0.1467 0.1755 -0.0147 -0.0078 0.0003  240 HOH   B O   
6680 O O   . HOH   E .   ? 0.4692 0.3085 0.4073 -0.2185 0.0030  0.0113  241 HOH   B O   
6681 O O   . HOH   E .   ? 0.1455 0.1317 0.1728 -0.0041 -0.0085 0.0124  242 HOH   B O   
6682 O O   . HOH   E .   ? 0.3480 0.1789 0.2180 0.0100  -0.0615 -0.0018 243 HOH   B O   
6683 O O   . HOH   E .   ? 0.3221 0.1693 0.5966 -0.0138 -0.1255 -0.0351 244 HOH   B O   
6684 O O   . HOH   E .   ? 0.2177 0.3819 0.2950 -0.0344 -0.0522 -0.0561 245 HOH   B O   
6685 O O   . HOH   E .   ? 0.3426 0.2450 0.3245 -0.0479 0.0294  -0.0647 246 HOH   B O   
6686 O O   . HOH   E .   ? 0.3197 0.2334 0.4113 -0.0037 0.1373  0.0084  247 HOH   B O   
6687 O O   . HOH   E .   ? 0.2000 0.4275 0.2614 -0.0320 -0.0168 0.0747  248 HOH   B O   
6688 O O   . HOH   E .   ? 0.1569 0.1504 0.2770 -0.0094 0.0027  -0.0049 249 HOH   B O   
6689 O O   . HOH   E .   ? 0.3420 0.3522 0.2307 0.0350  0.0658  0.0243  250 HOH   B O   
6690 O O   . HOH   E .   ? 0.1654 0.1621 0.3293 -0.0201 -0.0158 0.0145  251 HOH   B O   
6691 O O   . HOH   E .   ? 0.4370 0.3630 0.3903 -0.0859 0.0711  -0.1040 252 HOH   B O   
6692 O O   . HOH   E .   ? 0.2123 0.1446 0.2225 -0.0277 -0.0415 0.0262  253 HOH   B O   
6693 O O   . HOH   E .   ? 0.2332 0.2089 0.2098 0.0109  0.0013  0.0024  254 HOH   B O   
6694 O O   . HOH   E .   ? 0.2832 0.2410 0.3218 0.0864  0.0948  0.0085  255 HOH   B O   
6695 O O   . HOH   E .   ? 0.3022 0.4067 0.3428 -0.1077 -0.0232 -0.0500 256 HOH   B O   
6696 O O   . HOH   E .   ? 0.5262 0.3232 0.2658 0.0073  0.0840  -0.0386 257 HOH   B O   
6697 O O   . HOH   E .   ? 0.1364 0.1655 0.2356 -0.0027 0.0087  0.0175  258 HOH   B O   
6698 O O   . HOH   E .   ? 0.3014 0.4798 0.5584 -0.0103 0.0452  -0.1321 259 HOH   B O   
6699 O O   . HOH   E .   ? 0.2271 0.3001 0.2220 -0.0416 0.0200  0.0427  260 HOH   B O   
6700 O O   . HOH   E .   ? 0.1949 0.1506 0.2507 -0.0218 -0.0068 0.0064  261 HOH   B O   
6701 O O   . HOH   E .   ? 0.2463 0.2015 0.2515 0.0822  -0.0792 -0.0557 262 HOH   B O   
6702 O O   . HOH   E .   ? 0.2279 0.3925 0.5312 0.1169  -0.0499 -0.0755 263 HOH   B O   
6703 O O   . HOH   E .   ? 0.1846 0.2720 0.2775 0.0390  0.0477  0.1005  264 HOH   B O   
6704 O O   . HOH   E .   ? 0.2544 0.2100 0.3020 -0.0613 0.0068  -0.0021 265 HOH   B O   
6705 O O   . HOH   E .   ? 0.3220 0.5012 0.3643 -0.0345 -0.0940 0.1244  266 HOH   B O   
6706 O O   . HOH   E .   ? 0.2235 0.2161 0.2278 0.0127  0.0078  0.0111  267 HOH   B O   
6707 O O   . HOH   E .   ? 0.4469 0.3642 0.2926 0.0435  -0.0080 -0.1023 268 HOH   B O   
6708 O O   . HOH   E .   ? 0.4092 0.3563 0.4658 -0.0178 -0.1308 -0.0988 269 HOH   B O   
6709 O O   . HOH   E .   ? 0.2536 0.3188 0.5189 -0.0335 0.0159  -0.1002 270 HOH   B O   
6710 O O   . HOH   E .   ? 0.2068 0.4250 0.4931 -0.0464 -0.0408 -0.1368 271 HOH   B O   
6711 O O   . HOH   E .   ? 0.2614 0.2931 0.2523 -0.0351 -0.0839 0.0199  272 HOH   B O   
6712 O O   . HOH   E .   ? 0.2483 0.3171 0.2451 0.1007  -0.0231 -0.0261 273 HOH   B O   
6713 O O   . HOH   E .   ? 0.2020 0.1993 0.3966 -0.0041 -0.0463 -0.0286 274 HOH   B O   
6714 O O   . HOH   E .   ? 0.3923 0.4839 0.5477 -0.0036 -0.1510 -0.0092 275 HOH   B O   
6715 O O   . HOH   E .   ? 0.1822 0.1825 0.1823 -0.0370 -0.0428 0.0073  276 HOH   B O   
6716 O O   . HOH   E .   ? 0.2583 0.2098 0.4738 0.0114  0.0332  0.0281  277 HOH   B O   
6717 O O   . HOH   E .   ? 0.3519 0.3633 0.4597 0.1309  -0.0714 -0.0904 278 HOH   B O   
6718 O O   . HOH   E .   ? 0.1773 0.1365 0.4308 -0.0126 -0.0291 -0.0004 279 HOH   B O   
6719 O O   . HOH   E .   ? 0.2432 0.2499 0.2519 -0.0407 -0.0625 -0.0288 280 HOH   B O   
6720 O O   . HOH   E .   ? 0.1553 0.1629 0.3542 -0.0175 0.0104  0.0083  281 HOH   B O   
6721 O O   . HOH   E .   ? 0.2516 0.3941 0.3954 0.0355  0.1115  0.0141  282 HOH   B O   
6722 O O   . HOH   E .   ? 0.1636 0.1499 0.1906 0.0055  0.0019  0.0007  283 HOH   B O   
6723 O O   . HOH   E .   ? 0.2530 0.3649 0.3420 -0.0933 0.0644  -0.1323 284 HOH   B O   
6724 O O   . HOH   E .   ? 0.2473 0.2610 0.2957 0.0097  -0.0815 0.0216  285 HOH   B O   
6725 O O   . HOH   E .   ? 0.2819 0.4551 0.4926 -0.0971 -0.1190 0.1248  286 HOH   B O   
6726 O O   . HOH   E .   ? 0.1628 0.2065 0.1727 -0.0041 -0.0221 0.0075  287 HOH   B O   
6727 O O   . HOH   E .   ? 0.1716 0.3147 0.4560 0.0175  0.0061  -0.1163 288 HOH   B O   
6728 O O   . HOH   E .   ? 0.3525 0.3400 0.4037 -0.1254 0.1442  -0.0532 289 HOH   B O   
6729 O O   . HOH   E .   ? 0.3666 0.2079 0.4051 -0.0870 -0.1978 0.0731  290 HOH   B O   
6730 O O   . HOH   E .   ? 0.2950 0.6592 0.7089 0.1390  -0.0749 -0.1098 291 HOH   B O   
6731 O O   . HOH   E .   ? 0.3320 0.2882 0.3015 -0.0239 0.0076  -0.1251 292 HOH   B O   
6732 O O   . HOH   E .   ? 0.2636 0.6897 0.2619 0.0796  -0.0316 -0.0553 293 HOH   B O   
6733 O O   . HOH   E .   ? 0.3054 0.2669 0.5027 -0.0206 -0.0466 0.0972  294 HOH   B O   
6734 O O   . HOH   E .   ? 0.1725 0.1899 0.3053 0.0143  -0.0166 0.0020  295 HOH   B O   
6735 O O   . HOH   E .   ? 0.2167 0.1593 0.2839 -0.0252 -0.0304 -0.0008 296 HOH   B O   
6736 O O   . HOH   E .   ? 0.5293 0.5719 0.2613 -0.0095 -0.0277 0.1133  297 HOH   B O   
6737 O O   . HOH   E .   ? 0.4644 0.3833 0.2578 0.1357  -0.0916 0.0406  298 HOH   B O   
6738 O O   . HOH   E .   ? 0.1903 0.1597 0.2543 0.0086  0.0121  0.0173  299 HOH   B O   
6739 O O   . HOH   E .   ? 0.4791 0.4296 0.5873 0.0599  0.0003  0.0756  300 HOH   B O   
6740 O O   . HOH   E .   ? 0.2010 0.2778 0.5672 0.0413  -0.0554 -0.1222 301 HOH   B O   
6741 O O   . HOH   E .   ? 0.3536 0.2620 0.2384 0.0211  -0.0756 -0.0177 302 HOH   B O   
6742 O O   . HOH   E .   ? 0.3691 0.6806 0.3179 0.0846  -0.0881 0.1021  303 HOH   B O   
6743 O O   . HOH   E .   ? 0.4419 0.3339 0.5028 -0.0974 -0.0008 0.1162  304 HOH   B O   
6744 O O   . HOH   E .   ? 0.5700 0.3891 0.3326 0.2639  0.1170  0.0812  305 HOH   B O   
6745 O O   . HOH   E .   ? 0.4430 0.4596 0.2357 0.0151  0.0756  0.0727  306 HOH   B O   
6746 O O   . HOH   E .   ? 0.1644 0.1835 0.3086 -0.0250 -0.0072 0.0157  307 HOH   B O   
6747 O O   . HOH   E .   ? 0.4920 0.4467 0.2586 0.1581  -0.0797 -0.0350 308 HOH   B O   
6748 O O   . HOH   E .   ? 0.3305 0.1909 0.3607 0.0714  0.1091  0.0481  309 HOH   B O   
6749 O O   . HOH   E .   ? 0.1669 0.1469 0.3153 0.0056  -0.0049 0.0039  310 HOH   B O   
6750 O O   . HOH   E .   ? 0.6357 0.4656 0.4917 0.1262  0.0748  -0.0107 311 HOH   B O   
6751 O O   . HOH   E .   ? 0.2346 0.3030 0.4684 -0.0261 -0.0335 -0.0010 312 HOH   B O   
6752 O O   . HOH   E .   ? 0.4873 0.2837 0.2540 -0.1789 0.0701  -0.0169 313 HOH   B O   
6753 O O   . HOH   E .   ? 0.2008 0.1603 0.3410 0.0299  -0.0841 -0.0041 314 HOH   B O   
6754 O O   . HOH   E .   ? 0.2394 0.1471 0.2844 -0.0224 -0.0209 0.0282  315 HOH   B O   
6755 O O   . HOH   E .   ? 0.2969 0.3066 0.3600 -0.0514 0.0983  -0.0852 316 HOH   B O   
6756 O O   . HOH   E .   ? 0.6172 0.5593 0.4817 0.2652  0.0024  0.0186  317 HOH   B O   
6757 O O   . HOH   E .   ? 0.4129 0.2289 0.2928 0.1481  0.1087  0.0308  318 HOH   B O   
6758 O O   . HOH   E .   ? 0.2174 0.1947 0.2001 -0.0071 0.0151  0.0161  319 HOH   B O   
6759 O O   . HOH   E .   ? 0.1860 0.2936 0.3349 0.0365  -0.0211 -0.0693 320 HOH   B O   
6760 O O   . HOH   E .   ? 0.2801 0.2157 0.2697 0.0121  -0.0202 0.0306  321 HOH   B O   
6761 O O   . HOH   E .   ? 0.4609 0.4337 0.2920 0.0353  -0.0356 -0.0646 322 HOH   B O   
6762 O O   . HOH   E .   ? 0.1706 0.2845 0.2538 -0.0140 -0.0263 0.0711  323 HOH   B O   
6763 O O   . HOH   E .   ? 0.1587 0.1619 0.3136 -0.0113 -0.0165 -0.0205 324 HOH   B O   
6764 O O   . HOH   E .   ? 0.4998 0.2514 0.2991 0.0401  0.0394  0.0789  325 HOH   B O   
6765 O O   . HOH   E .   ? 0.5648 0.5357 0.5288 -0.1049 -0.0341 0.1212  326 HOH   B O   
6766 O O   . HOH   E .   ? 0.4335 0.3230 0.5147 0.1061  0.1990  0.1711  327 HOH   B O   
6767 O O   . HOH   E .   ? 0.3400 0.4157 0.7193 -0.0316 -0.0923 0.2262  328 HOH   B O   
6768 O O   . HOH   E .   ? 0.2229 0.5867 0.5165 -0.0429 -0.0074 0.0232  329 HOH   B O   
6769 O O   . HOH   E .   ? 0.1948 0.2126 0.3048 0.0365  0.0467  0.0271  330 HOH   B O   
6770 O O   . HOH   E .   ? 0.8116 0.2080 0.2930 0.0107  -0.0794 0.0104  331 HOH   B O   
6771 O O   . HOH   E .   ? 0.6526 0.3256 0.3648 -0.0138 0.1256  0.1101  332 HOH   B O   
6772 O O   . HOH   E .   ? 0.2715 0.3396 0.4471 -0.0648 -0.1374 0.1310  333 HOH   B O   
6773 O O   . HOH   E .   ? 0.2770 0.2039 0.4914 0.0008  -0.0039 0.0380  334 HOH   B O   
6774 O O   . HOH   E .   ? 0.5664 0.5363 0.6095 0.0811  -0.0874 0.2306  335 HOH   B O   
6775 O O   . HOH   E .   ? 0.5254 0.3515 0.4114 0.0396  0.0530  -0.1396 336 HOH   B O   
6776 O O   . HOH   E .   ? 0.5013 0.5441 0.3475 -0.0117 -0.0961 0.0716  337 HOH   B O   
6777 O O   . HOH   E .   ? 0.1779 0.1463 0.2477 0.0075  -0.0250 0.0091  338 HOH   B O   
6778 O O   . HOH   E .   ? 0.5746 0.5005 0.5961 -0.0925 -0.0566 -0.1145 339 HOH   B O   
6779 O O   . HOH   E .   ? 0.2260 0.2348 0.5549 -0.0447 0.0162  0.1397  340 HOH   B O   
6780 O O   . HOH   E .   ? 0.5095 0.3539 0.3339 0.0539  -0.1221 -0.0671 341 HOH   B O   
6781 O O   . HOH   E .   ? 0.4564 0.6448 0.3500 0.0054  -0.0510 0.1339  342 HOH   B O   
6782 O O   . HOH   E .   ? 0.3741 0.6008 0.3739 -0.0500 -0.1038 -0.0653 343 HOH   B O   
6783 O O   . HOH   E .   ? 0.1880 0.5651 0.5957 -0.0191 -0.0533 0.0245  344 HOH   B O   
6784 O O   . HOH   E .   ? 0.6404 0.6165 0.3140 -0.0460 -0.1012 0.0933  345 HOH   B O   
6785 O O   . HOH   E .   ? 0.2152 0.1977 0.3187 -0.0008 0.0717  -0.0019 346 HOH   B O   
6786 O O   . HOH   E .   ? 0.4547 0.5297 0.4811 -0.0085 -0.0905 0.0624  347 HOH   B O   
6787 O O   . HOH   E .   ? 0.2404 0.5801 0.3672 0.1600  -0.0503 -0.1378 348 HOH   B O   
6788 O O   . HOH   E .   ? 0.2765 0.2239 0.4763 -0.0207 -0.0978 -0.0545 349 HOH   B O   
6789 O O   . HOH   E .   ? 0.2209 0.4042 0.5234 0.0376  0.0171  0.0262  350 HOH   B O   
6790 O O   . HOH   E .   ? 0.5136 0.5532 0.5120 -0.1326 0.0704  0.0992  351 HOH   B O   
6791 O O   . HOH   E .   ? 0.3646 0.2170 0.3344 -0.0525 -0.0025 -0.0634 352 HOH   B O   
6792 O O   . HOH   E .   ? 0.4301 0.5630 0.5818 0.0186  0.0265  -0.0758 353 HOH   B O   
6793 O O   . HOH   E .   ? 0.3031 0.1862 0.4181 0.0472  -0.1236 -0.0518 354 HOH   B O   
6794 O O   . HOH   E .   ? 0.3533 0.4268 0.4863 -0.1588 -0.0269 0.0233  355 HOH   B O   
6795 O O   . HOH   E .   ? 0.3830 0.2831 0.4060 -0.1112 -0.0241 -0.0454 356 HOH   B O   
6796 O O   . HOH   E .   ? 0.4476 0.2794 0.5426 -0.0986 0.1252  0.0481  357 HOH   B O   
6797 O O   . HOH   E .   ? 0.4905 0.3502 0.4352 0.0553  0.1147  -0.0376 358 HOH   B O   
6798 O O   . HOH   E .   ? 0.4714 0.5444 0.5002 0.1666  -0.1235 0.1211  359 HOH   B O   
6799 O O   . HOH   E .   ? 0.4740 0.3336 0.4928 0.0376  -0.1646 -0.0104 360 HOH   B O   
6800 O O   . HOH   E .   ? 0.4935 0.4311 0.5200 -0.0108 0.0110  0.0293  361 HOH   B O   
6801 O O   . HOH   E .   ? 0.4861 0.3855 0.6173 0.0760  0.0861  0.1225  362 HOH   B O   
6802 O O   . HOH   E .   ? 0.4229 0.6178 0.3105 0.1796  -0.0104 0.0537  363 HOH   B O   
6803 O O   . HOH   E .   ? 0.2065 0.3487 0.6557 -0.0595 -0.0611 -0.0782 364 HOH   B O   
6804 O O   . HOH   E .   ? 0.6392 0.2172 0.3719 -0.0034 -0.0185 0.0689  365 HOH   B O   
6805 O O   . HOH   E .   ? 0.6002 0.2956 0.5145 -0.1361 -0.0135 0.0063  366 HOH   B O   
6806 O O   . HOH   E .   ? 0.6116 0.4051 0.4416 0.0830  0.0968  0.0535  367 HOH   B O   
6807 O O   . HOH   E .   ? 0.5747 0.5240 0.3489 0.1225  -0.1477 0.0566  368 HOH   B O   
6808 O O   . HOH   E .   ? 0.5469 0.3814 0.4606 0.0896  -0.1564 -0.0176 369 HOH   B O   
6809 O O   . HOH   E .   ? 0.4570 0.5155 0.5462 0.2633  0.0766  0.1072  370 HOH   B O   
6810 O O   . HOH   E .   ? 0.6336 0.4331 0.3048 -0.1029 -0.1132 -0.0752 371 HOH   B O   
6811 O O   . HOH   E .   ? 0.8237 0.7767 0.5600 0.2085  -0.1124 0.1067  372 HOH   B O   
6812 O O   . HOH   E .   ? 0.3806 0.3235 0.4293 0.0633  -0.1444 -0.0211 373 HOH   B O   
6813 O O   . HOH   E .   ? 0.4929 0.5588 0.4352 -0.0278 -0.0444 -0.1055 374 HOH   B O   
6814 O O   . HOH   E .   ? 0.5035 0.6878 0.5573 0.1458  0.0299  0.2648  375 HOH   B O   
6815 O O   . HOH   E .   ? 0.4269 0.4661 0.4594 -0.0876 -0.0692 0.0328  376 HOH   B O   
6816 O O   . HOH   E .   ? 0.2435 0.3984 0.4659 0.0277  -0.0794 -0.0529 377 HOH   B O   
6817 O O   . HOH   E .   ? 0.3426 0.4208 0.2355 0.0343  0.0297  0.0086  378 HOH   B O   
6818 O O   . HOH   E .   ? 0.6746 0.3485 0.5010 -0.0807 -0.0222 -0.0140 379 HOH   B O   
6819 O O   . HOH   E .   ? 0.4826 0.6884 0.4297 -0.1322 0.0137  -0.1406 380 HOH   B O   
6820 O O   . HOH   E .   ? 0.3520 0.4708 0.4942 0.1246  -0.0248 0.0172  381 HOH   B O   
6821 O O   . HOH   E .   ? 0.3022 0.2608 0.3488 0.0012  0.0303  0.0475  382 HOH   B O   
6822 O O   . HOH   E .   ? 0.4138 0.7628 0.5448 0.0857  0.1878  0.1001  383 HOH   B O   
6823 O O   . HOH   E .   ? 0.5170 0.6707 0.6316 0.0442  0.1922  0.1328  384 HOH   B O   
6824 O O   . HOH   E .   ? 0.5041 0.4365 0.4690 -0.0428 -0.0376 -0.0590 385 HOH   B O   
6825 O O   . HOH   E .   ? 0.6798 0.4061 0.4333 0.0507  0.1024  -0.1120 386 HOH   B O   
6826 O O   . HOH   E .   ? 0.6703 0.5940 0.4610 0.2009  -0.0019 0.0460  387 HOH   B O   
6827 O O   . HOH   E .   ? 0.2453 0.4288 0.3919 -0.0814 -0.1100 -0.0345 388 HOH   B O   
6828 O O   . HOH   E .   ? 0.4637 0.3616 0.3095 -0.0147 0.0316  -0.0244 389 HOH   B O   
6829 O O   . HOH   E .   ? 0.5655 0.4191 0.4979 -0.0776 0.0314  -0.0105 390 HOH   B O   
6830 O O   . HOH   E .   ? 0.3871 0.2156 0.3358 0.0661  -0.0290 0.0124  391 HOH   B O   
6831 O O   . HOH   E .   ? 0.4739 0.4143 0.3979 0.0141  0.0158  0.0371  392 HOH   B O   
6832 O O   . HOH   E .   ? 0.4548 0.2248 0.4939 -0.0497 0.0338  0.0468  393 HOH   B O   
6833 O O   . HOH   E .   ? 0.2525 0.5016 0.6337 -0.1335 -0.0649 -0.0182 394 HOH   B O   
6834 O O   . HOH   E .   ? 0.4787 0.5746 0.3782 0.1277  -0.0167 -0.1015 395 HOH   B O   
6835 O O   . HOH   E .   ? 0.4078 0.3971 0.4410 0.0062  0.0889  0.0809  396 HOH   B O   
6836 O O   . HOH   E .   ? 0.3198 0.3784 0.3982 0.0375  0.0161  -0.0792 397 HOH   B O   
6837 O O   . HOH   E .   ? 0.2282 0.2833 0.5858 -0.0676 -0.0900 0.0178  398 HOH   B O   
6838 O O   . HOH   E .   ? 0.5805 0.6161 0.6841 0.1245  -0.1146 0.1720  399 HOH   B O   
6839 O O   . HOH   E .   ? 0.5781 0.4092 0.3076 -0.2152 -0.0187 0.0943  400 HOH   B O   
6840 O O   . HOH   E .   ? 0.5855 0.5966 0.3847 0.1570  -0.0467 -0.0006 401 HOH   B O   
# 
