data_7HDW
# 
_entry.id   7HDW 
# 
_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   7HDW         pdb_00007hdw 10.2210/pdb7hdw/pdb 
WWPDB D_1001407350 ?            ?                   
# 
_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                        7HDW 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                               18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 
'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                   114.023   1   ?                      ? ? ? 
3 non-polymer syn '(3S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-ol' 218.255   1   ?                      ? ? ? 
4 water       nat water                                                    18.015    413 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                   TFA   
3 '(3S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-ol' A1A85 
4 water                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A85 non-polymer         . '(3S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-ol' ? 'C11 H14 N4 O'   218.255 
ALA   'L-peptide linking' y ALANINE                                                  ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                               ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                          ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                 ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                          ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                  ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                    ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                               ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                  ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                   ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                               ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                            ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                  ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                   ? 'C3 H7 N O3'     105.093 
TFA   non-polymer         . 'trifluoroacetic acid'                                   ? 'C2 H F3 O2'     114.023 
THR   'L-peptide linking' y THREONINE                                                ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                 ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A85 1   202 201  A1A85 LA1 A . 
E 4 HOH   1   301 229  HOH   HOH A . 
E 4 HOH   2   302 196  HOH   HOH A . 
E 4 HOH   3   303 292  HOH   HOH A . 
E 4 HOH   4   304 209  HOH   HOH A . 
E 4 HOH   5   305 1289 HOH   HOH A . 
E 4 HOH   6   306 153  HOH   HOH A . 
E 4 HOH   7   307 1309 HOH   HOH A . 
E 4 HOH   8   308 493  HOH   HOH A . 
E 4 HOH   9   309 1301 HOH   HOH A . 
E 4 HOH   10  310 136  HOH   HOH A . 
E 4 HOH   11  311 952  HOH   HOH A . 
E 4 HOH   12  312 1296 HOH   HOH A . 
E 4 HOH   13  313 625  HOH   HOH A . 
E 4 HOH   14  314 109  HOH   HOH A . 
E 4 HOH   15  315 1295 HOH   HOH A . 
E 4 HOH   16  316 124  HOH   HOH A . 
E 4 HOH   17  317 337  HOH   HOH A . 
E 4 HOH   18  318 57   HOH   HOH A . 
E 4 HOH   19  319 49   HOH   HOH A . 
E 4 HOH   20  320 21   HOH   HOH A . 
E 4 HOH   21  321 247  HOH   HOH A . 
E 4 HOH   22  322 93   HOH   HOH A . 
E 4 HOH   23  323 1290 HOH   HOH A . 
E 4 HOH   24  324 192  HOH   HOH A . 
E 4 HOH   25  325 86   HOH   HOH A . 
E 4 HOH   26  326 35   HOH   HOH A . 
E 4 HOH   27  327 76   HOH   HOH A . 
E 4 HOH   28  328 34   HOH   HOH A . 
E 4 HOH   29  329 393  HOH   HOH A . 
E 4 HOH   30  330 18   HOH   HOH A . 
E 4 HOH   31  331 1310 HOH   HOH A . 
E 4 HOH   32  332 1300 HOH   HOH A . 
E 4 HOH   33  333 236  HOH   HOH A . 
E 4 HOH   34  334 164  HOH   HOH A . 
E 4 HOH   35  335 151  HOH   HOH A . 
E 4 HOH   36  336 469  HOH   HOH A . 
E 4 HOH   37  337 1    HOH   HOH A . 
E 4 HOH   38  338 409  HOH   HOH A . 
E 4 HOH   39  339 661  HOH   HOH A . 
E 4 HOH   40  340 132  HOH   HOH A . 
E 4 HOH   41  341 40   HOH   HOH A . 
E 4 HOH   42  342 1283 HOH   HOH A . 
E 4 HOH   43  343 165  HOH   HOH A . 
E 4 HOH   44  344 1308 HOH   HOH A . 
E 4 HOH   45  345 56   HOH   HOH A . 
E 4 HOH   46  346 169  HOH   HOH A . 
E 4 HOH   47  347 218  HOH   HOH A . 
E 4 HOH   48  348 140  HOH   HOH A . 
E 4 HOH   49  349 42   HOH   HOH A . 
E 4 HOH   50  350 630  HOH   HOH A . 
E 4 HOH   51  351 354  HOH   HOH A . 
E 4 HOH   52  352 320  HOH   HOH A . 
E 4 HOH   53  353 405  HOH   HOH A . 
E 4 HOH   54  354 225  HOH   HOH A . 
E 4 HOH   55  355 92   HOH   HOH A . 
E 4 HOH   56  356 964  HOH   HOH A . 
E 4 HOH   57  357 17   HOH   HOH A . 
E 4 HOH   58  358 102  HOH   HOH A . 
E 4 HOH   59  359 33   HOH   HOH A . 
E 4 HOH   60  360 241  HOH   HOH A . 
E 4 HOH   61  361 2    HOH   HOH A . 
E 4 HOH   62  362 81   HOH   HOH A . 
E 4 HOH   63  363 26   HOH   HOH A . 
E 4 HOH   64  364 461  HOH   HOH A . 
E 4 HOH   65  365 155  HOH   HOH A . 
E 4 HOH   66  366 19   HOH   HOH A . 
E 4 HOH   67  367 662  HOH   HOH A . 
E 4 HOH   68  368 46   HOH   HOH A . 
E 4 HOH   69  369 66   HOH   HOH A . 
E 4 HOH   70  370 62   HOH   HOH A . 
E 4 HOH   71  371 5    HOH   HOH A . 
E 4 HOH   72  372 39   HOH   HOH A . 
E 4 HOH   73  373 154  HOH   HOH A . 
E 4 HOH   74  374 140  HOH   HOH A . 
E 4 HOH   75  375 138  HOH   HOH A . 
E 4 HOH   76  376 939  HOH   HOH A . 
E 4 HOH   77  377 396  HOH   HOH A . 
E 4 HOH   78  378 199  HOH   HOH A . 
E 4 HOH   79  379 27   HOH   HOH A . 
E 4 HOH   80  380 134  HOH   HOH A . 
E 4 HOH   81  381 139  HOH   HOH A . 
E 4 HOH   82  382 333  HOH   HOH A . 
E 4 HOH   83  383 4    HOH   HOH A . 
E 4 HOH   84  384 45   HOH   HOH A . 
E 4 HOH   85  385 78   HOH   HOH A . 
E 4 HOH   86  386 159  HOH   HOH A . 
E 4 HOH   87  387 85   HOH   HOH A . 
E 4 HOH   88  388 351  HOH   HOH A . 
E 4 HOH   89  389 162  HOH   HOH A . 
E 4 HOH   90  390 6    HOH   HOH A . 
E 4 HOH   91  391 186  HOH   HOH A . 
E 4 HOH   92  392 148  HOH   HOH A . 
E 4 HOH   93  393 366  HOH   HOH A . 
E 4 HOH   94  394 278  HOH   HOH A . 
E 4 HOH   95  395 96   HOH   HOH A . 
E 4 HOH   96  396 36   HOH   HOH A . 
E 4 HOH   97  397 74   HOH   HOH A . 
E 4 HOH   98  398 116  HOH   HOH A . 
E 4 HOH   99  399 8    HOH   HOH A . 
E 4 HOH   100 400 12   HOH   HOH A . 
E 4 HOH   101 401 105  HOH   HOH A . 
E 4 HOH   102 402 1094 HOH   HOH A . 
E 4 HOH   103 403 115  HOH   HOH A . 
E 4 HOH   104 404 24   HOH   HOH A . 
E 4 HOH   105 405 25   HOH   HOH A . 
E 4 HOH   106 406 83   HOH   HOH A . 
E 4 HOH   107 407 1315 HOH   HOH A . 
E 4 HOH   108 408 58   HOH   HOH A . 
E 4 HOH   109 409 67   HOH   HOH A . 
E 4 HOH   110 410 195  HOH   HOH A . 
E 4 HOH   111 411 51   HOH   HOH A . 
E 4 HOH   112 412 3    HOH   HOH A . 
E 4 HOH   113 413 1275 HOH   HOH A . 
E 4 HOH   114 414 1279 HOH   HOH A . 
E 4 HOH   115 415 125  HOH   HOH A . 
E 4 HOH   116 416 123  HOH   HOH A . 
E 4 HOH   117 417 397  HOH   HOH A . 
E 4 HOH   118 418 281  HOH   HOH A . 
E 4 HOH   119 419 381  HOH   HOH A . 
E 4 HOH   120 420 7    HOH   HOH A . 
E 4 HOH   121 421 1238 HOH   HOH A . 
E 4 HOH   122 422 68   HOH   HOH A . 
E 4 HOH   123 423 121  HOH   HOH A . 
E 4 HOH   124 424 53   HOH   HOH A . 
E 4 HOH   125 425 95   HOH   HOH A . 
E 4 HOH   126 426 1068 HOH   HOH A . 
E 4 HOH   127 427 1313 HOH   HOH A . 
E 4 HOH   128 428 16   HOH   HOH A . 
E 4 HOH   129 429 303  HOH   HOH A . 
E 4 HOH   130 430 122  HOH   HOH A . 
E 4 HOH   131 431 296  HOH   HOH A . 
E 4 HOH   132 432 4    HOH   HOH A . 
E 4 HOH   133 433 156  HOH   HOH A . 
E 4 HOH   134 434 70   HOH   HOH A . 
E 4 HOH   135 435 944  HOH   HOH A . 
E 4 HOH   136 436 582  HOH   HOH A . 
E 4 HOH   137 437 1222 HOH   HOH A . 
E 4 HOH   138 438 576  HOH   HOH A . 
E 4 HOH   139 439 212  HOH   HOH A . 
E 4 HOH   140 440 80   HOH   HOH A . 
E 4 HOH   141 441 73   HOH   HOH A . 
E 4 HOH   142 442 71   HOH   HOH A . 
E 4 HOH   143 443 94   HOH   HOH A . 
E 4 HOH   144 444 188  HOH   HOH A . 
E 4 HOH   145 445 1189 HOH   HOH A . 
E 4 HOH   146 446 79   HOH   HOH A . 
E 4 HOH   147 447 97   HOH   HOH A . 
E 4 HOH   148 448 104  HOH   HOH A . 
E 4 HOH   149 449 1286 HOH   HOH A . 
E 4 HOH   150 450 1134 HOH   HOH A . 
E 4 HOH   151 451 509  HOH   HOH A . 
E 4 HOH   152 452 107  HOH   HOH A . 
E 4 HOH   153 453 330  HOH   HOH A . 
E 4 HOH   154 454 726  HOH   HOH A . 
E 4 HOH   155 455 1119 HOH   HOH A . 
E 4 HOH   156 456 2    HOH   HOH A . 
E 4 HOH   157 457 163  HOH   HOH A . 
E 4 HOH   158 458 801  HOH   HOH A . 
E 4 HOH   159 459 280  HOH   HOH A . 
E 4 HOH   160 460 342  HOH   HOH A . 
E 4 HOH   161 461 408  HOH   HOH A . 
E 4 HOH   162 462 756  HOH   HOH A . 
E 4 HOH   163 463 556  HOH   HOH A . 
E 4 HOH   164 464 319  HOH   HOH A . 
E 4 HOH   165 465 126  HOH   HOH A . 
E 4 HOH   166 466 370  HOH   HOH A . 
E 4 HOH   167 467 361  HOH   HOH A . 
E 4 HOH   168 468 1307 HOH   HOH A . 
E 4 HOH   169 469 63   HOH   HOH A . 
E 4 HOH   170 470 1276 HOH   HOH A . 
E 4 HOH   171 471 135  HOH   HOH A . 
E 4 HOH   172 472 250  HOH   HOH A . 
E 4 HOH   173 473 1284 HOH   HOH A . 
E 4 HOH   174 474 202  HOH   HOH A . 
E 4 HOH   175 475 1306 HOH   HOH A . 
E 4 HOH   176 476 1287 HOH   HOH A . 
E 4 HOH   177 477 224  HOH   HOH A . 
E 4 HOH   178 478 695  HOH   HOH A . 
E 4 HOH   179 479 674  HOH   HOH A . 
E 4 HOH   180 480 208  HOH   HOH A . 
E 4 HOH   181 481 941  HOH   HOH A . 
E 4 HOH   182 482 315  HOH   HOH A . 
E 4 HOH   183 483 267  HOH   HOH A . 
E 4 HOH   184 484 919  HOH   HOH A . 
E 4 HOH   185 485 152  HOH   HOH A . 
E 4 HOH   186 486 318  HOH   HOH A . 
E 4 HOH   187 487 331  HOH   HOH A . 
E 4 HOH   188 488 1314 HOH   HOH A . 
E 4 HOH   189 489 711  HOH   HOH A . 
E 4 HOH   190 490 309  HOH   HOH A . 
E 4 HOH   191 491 805  HOH   HOH A . 
E 4 HOH   192 492 1299 HOH   HOH A . 
E 4 HOH   193 493 521  HOH   HOH A . 
E 4 HOH   194 494 981  HOH   HOH A . 
E 4 HOH   195 495 263  HOH   HOH A . 
E 4 HOH   196 496 3    HOH   HOH A . 
E 4 HOH   197 497 180  HOH   HOH A . 
E 4 HOH   198 498 1071 HOH   HOH A . 
E 4 HOH   199 499 363  HOH   HOH A . 
E 4 HOH   200 500 313  HOH   HOH A . 
E 4 HOH   201 501 326  HOH   HOH A . 
E 4 HOH   202 502 356  HOH   HOH A . 
E 4 HOH   203 503 371  HOH   HOH A . 
E 4 HOH   204 504 185  HOH   HOH A . 
E 4 HOH   205 505 429  HOH   HOH A . 
E 4 HOH   206 506 70   HOH   HOH A . 
E 4 HOH   207 507 772  HOH   HOH A . 
E 4 HOH   208 508 376  HOH   HOH A . 
E 4 HOH   209 509 1074 HOH   HOH A . 
E 4 HOH   210 510 1292 HOH   HOH A . 
E 4 HOH   211 511 346  HOH   HOH A . 
E 4 HOH   212 512 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 1249 HOH   HOH B . 
F 4 HOH   3   203 549  HOH   HOH B . 
F 4 HOH   4   204 240  HOH   HOH B . 
F 4 HOH   5   205 205  HOH   HOH B . 
F 4 HOH   6   206 358  HOH   HOH B . 
F 4 HOH   7   207 531  HOH   HOH B . 
F 4 HOH   8   208 364  HOH   HOH B . 
F 4 HOH   9   209 353  HOH   HOH B . 
F 4 HOH   10  210 232  HOH   HOH B . 
F 4 HOH   11  211 264  HOH   HOH B . 
F 4 HOH   12  212 758  HOH   HOH B . 
F 4 HOH   13  213 50   HOH   HOH B . 
F 4 HOH   14  214 120  HOH   HOH B . 
F 4 HOH   15  215 398  HOH   HOH B . 
F 4 HOH   16  216 1278 HOH   HOH B . 
F 4 HOH   17  217 452  HOH   HOH B . 
F 4 HOH   18  218 743  HOH   HOH B . 
F 4 HOH   19  219 332  HOH   HOH B . 
F 4 HOH   20  220 172  HOH   HOH B . 
F 4 HOH   21  221 15   HOH   HOH B . 
F 4 HOH   22  222 900  HOH   HOH B . 
F 4 HOH   23  223 75   HOH   HOH B . 
F 4 HOH   24  224 82   HOH   HOH B . 
F 4 HOH   25  225 1140 HOH   HOH B . 
F 4 HOH   26  226 69   HOH   HOH B . 
F 4 HOH   27  227 131  HOH   HOH B . 
F 4 HOH   28  228 166  HOH   HOH B . 
F 4 HOH   29  229 60   HOH   HOH B . 
F 4 HOH   30  230 444  HOH   HOH B . 
F 4 HOH   31  231 54   HOH   HOH B . 
F 4 HOH   32  232 144  HOH   HOH B . 
F 4 HOH   33  233 133  HOH   HOH B . 
F 4 HOH   34  234 300  HOH   HOH B . 
F 4 HOH   35  235 110  HOH   HOH B . 
F 4 HOH   36  236 325  HOH   HOH B . 
F 4 HOH   37  237 1    HOH   HOH B . 
F 4 HOH   38  238 41   HOH   HOH B . 
F 4 HOH   39  239 343  HOH   HOH B . 
F 4 HOH   40  240 52   HOH   HOH B . 
F 4 HOH   41  241 272  HOH   HOH B . 
F 4 HOH   42  242 1312 HOH   HOH B . 
F 4 HOH   43  243 271  HOH   HOH B . 
F 4 HOH   44  244 391  HOH   HOH B . 
F 4 HOH   45  245 14   HOH   HOH B . 
F 4 HOH   46  246 654  HOH   HOH B . 
F 4 HOH   47  247 31   HOH   HOH B . 
F 4 HOH   48  248 128  HOH   HOH B . 
F 4 HOH   49  249 129  HOH   HOH B . 
F 4 HOH   50  250 9    HOH   HOH B . 
F 4 HOH   51  251 276  HOH   HOH B . 
F 4 HOH   52  252 127  HOH   HOH B . 
F 4 HOH   53  253 287  HOH   HOH B . 
F 4 HOH   54  254 723  HOH   HOH B . 
F 4 HOH   55  255 181  HOH   HOH B . 
F 4 HOH   56  256 30   HOH   HOH B . 
F 4 HOH   57  257 72   HOH   HOH B . 
F 4 HOH   58  258 150  HOH   HOH B . 
F 4 HOH   59  259 221  HOH   HOH B . 
F 4 HOH   60  260 10   HOH   HOH B . 
F 4 HOH   61  261 282  HOH   HOH B . 
F 4 HOH   62  262 103  HOH   HOH B . 
F 4 HOH   63  263 252  HOH   HOH B . 
F 4 HOH   64  264 47   HOH   HOH B . 
F 4 HOH   65  265 1277 HOH   HOH B . 
F 4 HOH   66  266 231  HOH   HOH B . 
F 4 HOH   67  267 117  HOH   HOH B . 
F 4 HOH   68  268 242  HOH   HOH B . 
F 4 HOH   69  269 11   HOH   HOH B . 
F 4 HOH   70  270 302  HOH   HOH B . 
F 4 HOH   71  271 147  HOH   HOH B . 
F 4 HOH   72  272 84   HOH   HOH B . 
F 4 HOH   73  273 59   HOH   HOH B . 
F 4 HOH   74  274 77   HOH   HOH B . 
F 4 HOH   75  275 347  HOH   HOH B . 
F 4 HOH   76  276 243  HOH   HOH B . 
F 4 HOH   77  277 175  HOH   HOH B . 
F 4 HOH   78  278 143  HOH   HOH B . 
F 4 HOH   79  279 61   HOH   HOH B . 
F 4 HOH   80  280 20   HOH   HOH B . 
F 4 HOH   81  281 220  HOH   HOH B . 
F 4 HOH   82  282 114  HOH   HOH B . 
F 4 HOH   83  283 43   HOH   HOH B . 
F 4 HOH   84  284 22   HOH   HOH B . 
F 4 HOH   85  285 207  HOH   HOH B . 
F 4 HOH   86  286 89   HOH   HOH B . 
F 4 HOH   87  287 88   HOH   HOH B . 
F 4 HOH   88  288 106  HOH   HOH B . 
F 4 HOH   89  289 1106 HOH   HOH B . 
F 4 HOH   90  290 13   HOH   HOH B . 
F 4 HOH   91  291 99   HOH   HOH B . 
F 4 HOH   92  292 1305 HOH   HOH B . 
F 4 HOH   93  293 235  HOH   HOH B . 
F 4 HOH   94  294 1066 HOH   HOH B . 
F 4 HOH   95  295 960  HOH   HOH B . 
F 4 HOH   96  296 1285 HOH   HOH B . 
F 4 HOH   97  297 160  HOH   HOH B . 
F 4 HOH   98  298 137  HOH   HOH B . 
F 4 HOH   99  299 311  HOH   HOH B . 
F 4 HOH   100 300 170  HOH   HOH B . 
F 4 HOH   101 301 316  HOH   HOH B . 
F 4 HOH   102 302 216  HOH   HOH B . 
F 4 HOH   103 303 215  HOH   HOH B . 
F 4 HOH   104 304 635  HOH   HOH B . 
F 4 HOH   105 305 299  HOH   HOH B . 
F 4 HOH   106 306 416  HOH   HOH B . 
F 4 HOH   107 307 182  HOH   HOH B . 
F 4 HOH   108 308 142  HOH   HOH B . 
F 4 HOH   109 309 112  HOH   HOH B . 
F 4 HOH   110 310 101  HOH   HOH B . 
F 4 HOH   111 311 297  HOH   HOH B . 
F 4 HOH   112 312 23   HOH   HOH B . 
F 4 HOH   113 313 197  HOH   HOH B . 
F 4 HOH   114 314 38   HOH   HOH B . 
F 4 HOH   115 315 37   HOH   HOH B . 
F 4 HOH   116 316 44   HOH   HOH B . 
F 4 HOH   117 317 118  HOH   HOH B . 
F 4 HOH   118 318 32   HOH   HOH B . 
F 4 HOH   119 319 387  HOH   HOH B . 
F 4 HOH   120 320 177  HOH   HOH B . 
F 4 HOH   121 321 91   HOH   HOH B . 
F 4 HOH   122 322 29   HOH   HOH B . 
F 4 HOH   123 323 28   HOH   HOH B . 
F 4 HOH   124 324 1294 HOH   HOH B . 
F 4 HOH   125 325 98   HOH   HOH B . 
F 4 HOH   126 326 100  HOH   HOH B . 
F 4 HOH   127 327 48   HOH   HOH B . 
F 4 HOH   128 328 1274 HOH   HOH B . 
F 4 HOH   129 329 341  HOH   HOH B . 
F 4 HOH   130 330 334  HOH   HOH B . 
F 4 HOH   131 331 55   HOH   HOH B . 
F 4 HOH   132 332 445  HOH   HOH B . 
F 4 HOH   133 333 141  HOH   HOH B . 
F 4 HOH   134 334 704  HOH   HOH B . 
F 4 HOH   135 335 161  HOH   HOH B . 
F 4 HOH   136 336 717  HOH   HOH B . 
F 4 HOH   137 337 1291 HOH   HOH B . 
F 4 HOH   138 338 65   HOH   HOH B . 
F 4 HOH   139 339 178  HOH   HOH B . 
F 4 HOH   140 340 234  HOH   HOH B . 
F 4 HOH   141 341 1126 HOH   HOH B . 
F 4 HOH   142 342 1293 HOH   HOH B . 
F 4 HOH   143 343 619  HOH   HOH B . 
F 4 HOH   144 344 362  HOH   HOH B . 
F 4 HOH   145 345 87   HOH   HOH B . 
F 4 HOH   146 346 1304 HOH   HOH B . 
F 4 HOH   147 347 90   HOH   HOH B . 
F 4 HOH   148 348 339  HOH   HOH B . 
F 4 HOH   149 349 1280 HOH   HOH B . 
F 4 HOH   150 350 623  HOH   HOH B . 
F 4 HOH   151 351 1046 HOH   HOH B . 
F 4 HOH   152 352 191  HOH   HOH B . 
F 4 HOH   153 353 463  HOH   HOH B . 
F 4 HOH   154 354 335  HOH   HOH B . 
F 4 HOH   155 355 1077 HOH   HOH B . 
F 4 HOH   156 356 304  HOH   HOH B . 
F 4 HOH   157 357 203  HOH   HOH B . 
F 4 HOH   158 358 541  HOH   HOH B . 
F 4 HOH   159 359 290  HOH   HOH B . 
F 4 HOH   160 360 718  HOH   HOH B . 
F 4 HOH   161 361 389  HOH   HOH B . 
F 4 HOH   162 362 1072 HOH   HOH B . 
F 4 HOH   163 363 283  HOH   HOH B . 
F 4 HOH   164 364 291  HOH   HOH B . 
F 4 HOH   165 365 479  HOH   HOH B . 
F 4 HOH   166 366 615  HOH   HOH B . 
F 4 HOH   167 367 340  HOH   HOH B . 
F 4 HOH   168 368 1316 HOH   HOH B . 
F 4 HOH   169 369 373  HOH   HOH B . 
F 4 HOH   170 370 898  HOH   HOH B . 
F 4 HOH   171 371 667  HOH   HOH B . 
F 4 HOH   172 372 310  HOH   HOH B . 
F 4 HOH   173 373 431  HOH   HOH B . 
F 4 HOH   174 374 1303 HOH   HOH B . 
F 4 HOH   175 375 190  HOH   HOH B . 
F 4 HOH   176 376 1000 HOH   HOH B . 
F 4 HOH   177 377 418  HOH   HOH B . 
F 4 HOH   178 378 149  HOH   HOH B . 
F 4 HOH   179 379 1173 HOH   HOH B . 
F 4 HOH   180 380 183  HOH   HOH B . 
F 4 HOH   181 381 1163 HOH   HOH B . 
F 4 HOH   182 382 176  HOH   HOH B . 
F 4 HOH   183 383 1311 HOH   HOH B . 
F 4 HOH   184 384 491  HOH   HOH B . 
F 4 HOH   185 385 424  HOH   HOH B . 
F 4 HOH   186 386 1298 HOH   HOH B . 
F 4 HOH   187 387 248  HOH   HOH B . 
F 4 HOH   188 388 265  HOH   HOH B . 
F 4 HOH   189 389 470  HOH   HOH B . 
F 4 HOH   190 390 350  HOH   HOH B . 
F 4 HOH   191 391 184  HOH   HOH B . 
F 4 HOH   192 392 360  HOH   HOH B . 
F 4 HOH   193 393 355  HOH   HOH B . 
F 4 HOH   194 394 410  HOH   HOH B . 
F 4 HOH   195 395 157  HOH   HOH B . 
F 4 HOH   196 396 274  HOH   HOH B . 
F 4 HOH   197 397 566  HOH   HOH B . 
F 4 HOH   198 398 314  HOH   HOH B . 
F 4 HOH   199 399 321  HOH   HOH B . 
F 4 HOH   200 400 792  HOH   HOH B . 
F 4 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HDW 
_cell.length_a           88.728 
_cell.length_b           88.728 
_cell.length_c           39.436 
_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                         7HDW 
_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          7HDW 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.49 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HDW 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.360 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165439 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.052 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.500 
_reflns.B_iso_Wilson_estimate        12.610 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.056 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1045875 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 33854 8078 ? 2.569 ? ? ? 4.200 ? 0.400  ? ? ? ? ? ? 98.800 2.938 1.387 0.292 
1 2 5.480 44.360 ? 7517  1092 ? 0.029 ? ? ? 6.900 ? 54.900 ? ? ? ? ? ? 99.800 0.032 0.012 0.999 
# 
_refine.entry_id                                 7HDW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3600 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4900 
_refine.ls_number_reflns_obs                     164716 
_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                          0.1566 
_refine.ls_R_factor_R_work                       0.1559 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1706 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7944 
_refine.ls_number_reflns_R_work                  156772 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.4777 
_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                            0.1400 
_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                                84.420 
_refine.B_iso_min                                9.320 
_refine.pdbx_overall_phase_error                 22.4300 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.3600 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.number_atoms_solvent             413 
_refine_hist.number_atoms_total               2992 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           19.72 
_refine_hist.pdbx_B_iso_mean_solvent          32.64 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 89.0000  4685 . 0.4913 0.4725 . 253 0.0000 4938 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 99.0000  5127 . 0.4272 0.4611 . 216 0.0000 5343 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5253 . 0.3952 0.3557 . 266 0.0000 5519 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5175 . 0.3587 0.3831 . 271 0.0000 5446 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5195 . 0.3147 0.3201 . 327 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5188 . 0.3057 0.3123 . 247 0.0000 5435 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5253 . 0.2785 0.3397 . 258 0.0000 5511 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5232 . 0.2396 0.2424 . 245 0.0000 5477 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5249 . 0.2335 0.2397 . 279 0.0000 5528 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5183 . 0.2082 0.2163 . 244 0.0000 5427 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5265 . 0.1885 0.2267 . 271 0.0000 5536 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5233 . 0.1838 0.2144 . 261 0.0000 5494 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5161 . 0.1588 0.1900 . 286 0.0000 5447 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5318 . 0.1650 0.1992 . 224 0.0000 5542 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5180 . 0.1587 0.1822 . 261 0.0000 5441 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5240 . 0.1638 0.1846 . 274 0.0000 5514 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5210 . 0.1532 0.1775 . 285 0.0000 5495 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5252 . 0.1414 0.1590 . 278 0.0000 5530 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5247 . 0.1481 0.1743 . 245 0.0000 5492 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5219 . 0.1375 0.1747 . 271 0.0000 5490 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5281 . 0.1355 0.1413 . 247 0.0000 5528 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5222 . 0.1269 0.1359 . 279 0.0000 5501 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5284 . 0.1195 0.1399 . 266 0.0000 5550 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5261 . 0.1264 0.1463 . 255 0.0000 5516 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5275 . 0.1342 0.1456 . 253 0.0000 5528 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5261 . 0.1341 0.1390 . 283 0.0000 5544 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5265 . 0.1361 0.1416 . 285 0.0000 5550 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5285 . 0.1378 0.1455 . 291 0.0000 5576 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5305 . 0.1493 0.1688 . 254 0.0000 5559 . 'X-RAY DIFFRACTION' 
3.1100 44.3600 30 100.0000 5468 . 0.1515 0.1694 . 269 0.0000 5737 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDW 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003646' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDW 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HDW A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDW 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 7HDW SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDW MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDW SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDW MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HDW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    207 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    313 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.80 -132.60 
2 1 SER A 128 ? B 68.04 -1.71   
3 1 HIS B 86  ? ? 57.38 -127.31 
# 
_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 511 ? 6.09 . 
2 1 O ? A HOH 512 ? 7.68 . 
3 1 O ? B HOH 401 ? 6.52 . 
# 
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 
A1A85 N2   N Y N 1   
A1A85 C3   C N N 2   
A1A85 C6   C Y N 3   
A1A85 C9   C Y N 4   
A1A85 C1   C N S 5   
A1A85 C10  C Y N 6   
A1A85 C11  C N N 7   
A1A85 C2   C N N 8   
A1A85 C4   C N N 9   
A1A85 C5   C Y N 10  
A1A85 C7   C Y N 11  
A1A85 C8   C Y N 12  
A1A85 N1   N N N 13  
A1A85 N3   N Y N 14  
A1A85 N4   N Y N 15  
A1A85 O1   O N N 16  
A1A85 H6   H N N 17  
A1A85 H5   H N N 18  
A1A85 H9   H N N 19  
A1A85 H10  H N N 20  
A1A85 H1   H N N 21  
A1A85 H11  H N N 22  
A1A85 H14  H N N 23  
A1A85 H13  H N N 24  
A1A85 H4   H N N 25  
A1A85 H3   H N N 26  
A1A85 H7   H N N 27  
A1A85 H8   H N N 28  
A1A85 H12  H N N 29  
A1A85 H2   H N N 30  
ALA   N    N N N 31  
ALA   CA   C N S 32  
ALA   C    C N N 33  
ALA   O    O N N 34  
ALA   CB   C N N 35  
ALA   OXT  O N N 36  
ALA   H    H N N 37  
ALA   H2   H N N 38  
ALA   HA   H N N 39  
ALA   HB1  H N N 40  
ALA   HB2  H N N 41  
ALA   HB3  H N N 42  
ALA   HXT  H N N 43  
ARG   N    N N N 44  
ARG   CA   C N S 45  
ARG   C    C N N 46  
ARG   O    O N N 47  
ARG   CB   C N N 48  
ARG   CG   C N N 49  
ARG   CD   C N N 50  
ARG   NE   N N N 51  
ARG   CZ   C N N 52  
ARG   NH1  N N N 53  
ARG   NH2  N N N 54  
ARG   OXT  O N N 55  
ARG   H    H N N 56  
ARG   H2   H N N 57  
ARG   HA   H N N 58  
ARG   HB2  H N N 59  
ARG   HB3  H N N 60  
ARG   HG2  H N N 61  
ARG   HG3  H N N 62  
ARG   HD2  H N N 63  
ARG   HD3  H N N 64  
ARG   HE   H N N 65  
ARG   HH11 H N N 66  
ARG   HH12 H N N 67  
ARG   HH21 H N N 68  
ARG   HH22 H N N 69  
ARG   HXT  H N N 70  
ASN   N    N N N 71  
ASN   CA   C N S 72  
ASN   C    C N N 73  
ASN   O    O N N 74  
ASN   CB   C N N 75  
ASN   CG   C N N 76  
ASN   OD1  O N N 77  
ASN   ND2  N N N 78  
ASN   OXT  O N N 79  
ASN   H    H N N 80  
ASN   H2   H N N 81  
ASN   HA   H N N 82  
ASN   HB2  H N N 83  
ASN   HB3  H N N 84  
ASN   HD21 H N N 85  
ASN   HD22 H N N 86  
ASN   HXT  H N N 87  
ASP   N    N N N 88  
ASP   CA   C N S 89  
ASP   C    C N N 90  
ASP   O    O N N 91  
ASP   CB   C N N 92  
ASP   CG   C N N 93  
ASP   OD1  O N N 94  
ASP   OD2  O N N 95  
ASP   OXT  O N N 96  
ASP   H    H N N 97  
ASP   H2   H N N 98  
ASP   HA   H N N 99  
ASP   HB2  H N N 100 
ASP   HB3  H N N 101 
ASP   HD2  H N N 102 
ASP   HXT  H N N 103 
CYS   N    N N N 104 
CYS   CA   C N R 105 
CYS   C    C N N 106 
CYS   O    O N N 107 
CYS   CB   C N N 108 
CYS   SG   S N N 109 
CYS   OXT  O N N 110 
CYS   H    H N N 111 
CYS   H2   H N N 112 
CYS   HA   H N N 113 
CYS   HB2  H N N 114 
CYS   HB3  H N N 115 
CYS   HG   H N N 116 
CYS   HXT  H N N 117 
GLN   N    N N N 118 
GLN   CA   C N S 119 
GLN   C    C N N 120 
GLN   O    O N N 121 
GLN   CB   C N N 122 
GLN   CG   C N N 123 
GLN   CD   C N N 124 
GLN   OE1  O N N 125 
GLN   NE2  N N N 126 
GLN   OXT  O N N 127 
GLN   H    H N N 128 
GLN   H2   H N N 129 
GLN   HA   H N N 130 
GLN   HB2  H N N 131 
GLN   HB3  H N N 132 
GLN   HG2  H N N 133 
GLN   HG3  H N N 134 
GLN   HE21 H N N 135 
GLN   HE22 H N N 136 
GLN   HXT  H N N 137 
GLU   N    N N N 138 
GLU   CA   C N S 139 
GLU   C    C N N 140 
GLU   O    O N N 141 
GLU   CB   C N N 142 
GLU   CG   C N N 143 
GLU   CD   C N N 144 
GLU   OE1  O N N 145 
GLU   OE2  O N N 146 
GLU   OXT  O N N 147 
GLU   H    H N N 148 
GLU   H2   H N N 149 
GLU   HA   H N N 150 
GLU   HB2  H N N 151 
GLU   HB3  H N N 152 
GLU   HG2  H N N 153 
GLU   HG3  H N N 154 
GLU   HE2  H N N 155 
GLU   HXT  H N N 156 
GLY   N    N N N 157 
GLY   CA   C N N 158 
GLY   C    C N N 159 
GLY   O    O N N 160 
GLY   OXT  O N N 161 
GLY   H    H N N 162 
GLY   H2   H N N 163 
GLY   HA2  H N N 164 
GLY   HA3  H N N 165 
GLY   HXT  H N N 166 
HIS   N    N N N 167 
HIS   CA   C N S 168 
HIS   C    C N N 169 
HIS   O    O N N 170 
HIS   CB   C N N 171 
HIS   CG   C Y N 172 
HIS   ND1  N Y N 173 
HIS   CD2  C Y N 174 
HIS   CE1  C Y N 175 
HIS   NE2  N Y N 176 
HIS   OXT  O N N 177 
HIS   H    H N N 178 
HIS   H2   H N N 179 
HIS   HA   H N N 180 
HIS   HB2  H N N 181 
HIS   HB3  H N N 182 
HIS   HD1  H N N 183 
HIS   HD2  H N N 184 
HIS   HE1  H N N 185 
HIS   HE2  H N N 186 
HIS   HXT  H N N 187 
HOH   O    O N N 188 
HOH   H1   H N N 189 
HOH   H2   H N N 190 
ILE   N    N N N 191 
ILE   CA   C N S 192 
ILE   C    C N N 193 
ILE   O    O N N 194 
ILE   CB   C N S 195 
ILE   CG1  C N N 196 
ILE   CG2  C N N 197 
ILE   CD1  C N N 198 
ILE   OXT  O N N 199 
ILE   H    H N N 200 
ILE   H2   H N N 201 
ILE   HA   H N N 202 
ILE   HB   H N N 203 
ILE   HG12 H N N 204 
ILE   HG13 H N N 205 
ILE   HG21 H N N 206 
ILE   HG22 H N N 207 
ILE   HG23 H N N 208 
ILE   HD11 H N N 209 
ILE   HD12 H N N 210 
ILE   HD13 H N N 211 
ILE   HXT  H N N 212 
LEU   N    N N N 213 
LEU   CA   C N S 214 
LEU   C    C N N 215 
LEU   O    O N N 216 
LEU   CB   C N N 217 
LEU   CG   C N N 218 
LEU   CD1  C N N 219 
LEU   CD2  C N N 220 
LEU   OXT  O N N 221 
LEU   H    H N N 222 
LEU   H2   H N N 223 
LEU   HA   H N N 224 
LEU   HB2  H N N 225 
LEU   HB3  H N N 226 
LEU   HG   H N N 227 
LEU   HD11 H N N 228 
LEU   HD12 H N N 229 
LEU   HD13 H N N 230 
LEU   HD21 H N N 231 
LEU   HD22 H N N 232 
LEU   HD23 H N N 233 
LEU   HXT  H N N 234 
LYS   N    N N N 235 
LYS   CA   C N S 236 
LYS   C    C N N 237 
LYS   O    O N N 238 
LYS   CB   C N N 239 
LYS   CG   C N N 240 
LYS   CD   C N N 241 
LYS   CE   C N N 242 
LYS   NZ   N N N 243 
LYS   OXT  O N N 244 
LYS   H    H N N 245 
LYS   H2   H N N 246 
LYS   HA   H N N 247 
LYS   HB2  H N N 248 
LYS   HB3  H N N 249 
LYS   HG2  H N N 250 
LYS   HG3  H N N 251 
LYS   HD2  H N N 252 
LYS   HD3  H N N 253 
LYS   HE2  H N N 254 
LYS   HE3  H N N 255 
LYS   HZ1  H N N 256 
LYS   HZ2  H N N 257 
LYS   HZ3  H N N 258 
LYS   HXT  H N N 259 
MET   N    N N N 260 
MET   CA   C N S 261 
MET   C    C N N 262 
MET   O    O N N 263 
MET   CB   C N N 264 
MET   CG   C N N 265 
MET   SD   S N N 266 
MET   CE   C N N 267 
MET   OXT  O N N 268 
MET   H    H N N 269 
MET   H2   H N N 270 
MET   HA   H N N 271 
MET   HB2  H N N 272 
MET   HB3  H N N 273 
MET   HG2  H N N 274 
MET   HG3  H N N 275 
MET   HE1  H N N 276 
MET   HE2  H N N 277 
MET   HE3  H N N 278 
MET   HXT  H N N 279 
PHE   N    N N N 280 
PHE   CA   C N S 281 
PHE   C    C N N 282 
PHE   O    O N N 283 
PHE   CB   C N N 284 
PHE   CG   C Y N 285 
PHE   CD1  C Y N 286 
PHE   CD2  C Y N 287 
PHE   CE1  C Y N 288 
PHE   CE2  C Y N 289 
PHE   CZ   C Y N 290 
PHE   OXT  O N N 291 
PHE   H    H N N 292 
PHE   H2   H N N 293 
PHE   HA   H N N 294 
PHE   HB2  H N N 295 
PHE   HB3  H N N 296 
PHE   HD1  H N N 297 
PHE   HD2  H N N 298 
PHE   HE1  H N N 299 
PHE   HE2  H N N 300 
PHE   HZ   H N N 301 
PHE   HXT  H N N 302 
PRO   N    N N N 303 
PRO   CA   C N S 304 
PRO   C    C N N 305 
PRO   O    O N N 306 
PRO   CB   C N N 307 
PRO   CG   C N N 308 
PRO   CD   C N N 309 
PRO   OXT  O N N 310 
PRO   H    H N N 311 
PRO   HA   H N N 312 
PRO   HB2  H N N 313 
PRO   HB3  H N N 314 
PRO   HG2  H N N 315 
PRO   HG3  H N N 316 
PRO   HD2  H N N 317 
PRO   HD3  H N N 318 
PRO   HXT  H N N 319 
SER   N    N N N 320 
SER   CA   C N S 321 
SER   C    C N N 322 
SER   O    O N N 323 
SER   CB   C N N 324 
SER   OG   O N N 325 
SER   OXT  O N N 326 
SER   H    H N N 327 
SER   H2   H N N 328 
SER   HA   H N N 329 
SER   HB2  H N N 330 
SER   HB3  H N N 331 
SER   HG   H N N 332 
SER   HXT  H N N 333 
TFA   C1   C N N 334 
TFA   C2   C N N 335 
TFA   O    O N N 336 
TFA   F1   F N N 337 
TFA   F2   F N N 338 
TFA   F3   F N N 339 
TFA   OXT  O N N 340 
TFA   HXT  H N N 341 
THR   N    N N N 342 
THR   CA   C N S 343 
THR   C    C N N 344 
THR   O    O N N 345 
THR   CB   C N R 346 
THR   OG1  O N N 347 
THR   CG2  C N N 348 
THR   OXT  O N N 349 
THR   H    H N N 350 
THR   H2   H N N 351 
THR   HA   H N N 352 
THR   HB   H N N 353 
THR   HG1  H N N 354 
THR   HG21 H N N 355 
THR   HG22 H N N 356 
THR   HG23 H N N 357 
THR   HXT  H N N 358 
TYR   N    N N N 359 
TYR   CA   C N S 360 
TYR   C    C N N 361 
TYR   O    O N N 362 
TYR   CB   C N N 363 
TYR   CG   C Y N 364 
TYR   CD1  C Y N 365 
TYR   CD2  C Y N 366 
TYR   CE1  C Y N 367 
TYR   CE2  C Y N 368 
TYR   CZ   C Y N 369 
TYR   OH   O N N 370 
TYR   OXT  O N N 371 
TYR   H    H N N 372 
TYR   H2   H N N 373 
TYR   HA   H N N 374 
TYR   HB2  H N N 375 
TYR   HB3  H N N 376 
TYR   HD1  H N N 377 
TYR   HD2  H N N 378 
TYR   HE1  H N N 379 
TYR   HE2  H N N 380 
TYR   HH   H N N 381 
TYR   HXT  H N N 382 
VAL   N    N N N 383 
VAL   CA   C N S 384 
VAL   C    C N N 385 
VAL   O    O N N 386 
VAL   CB   C N N 387 
VAL   CG1  C N N 388 
VAL   CG2  C N N 389 
VAL   OXT  O N N 390 
VAL   H    H N N 391 
VAL   H2   H N N 392 
VAL   HA   H N N 393 
VAL   HB   H N N 394 
VAL   HG11 H N N 395 
VAL   HG12 H N N 396 
VAL   HG13 H N N 397 
VAL   HG21 H N N 398 
VAL   HG22 H N N 399 
VAL   HG23 H N N 400 
VAL   HXT  H N N 401 
# 
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 
A1A85 O1  C1   sing N N 1   
A1A85 C2  C1   sing N N 2   
A1A85 C2  C3   sing N N 3   
A1A85 C1  C11  sing N N 4   
A1A85 C3  C4   sing N N 5   
A1A85 C11 N1   sing N N 6   
A1A85 C4  N1   sing N N 7   
A1A85 N1  C5   sing N N 8   
A1A85 C5  N2   doub Y N 9   
A1A85 C5  C8   sing Y N 10  
A1A85 C9  C8   sing Y N 11  
A1A85 C9  C10  doub Y N 12  
A1A85 N2  C6   sing Y N 13  
A1A85 C8  C7   doub Y N 14  
A1A85 C10 N4   sing Y N 15  
A1A85 C6  N3   doub Y N 16  
A1A85 C7  N4   sing Y N 17  
A1A85 C7  N3   sing Y N 18  
A1A85 C3  H6   sing N N 19  
A1A85 C3  H5   sing N N 20  
A1A85 C6  H9   sing N N 21  
A1A85 C9  H10  sing N N 22  
A1A85 C1  H1   sing N N 23  
A1A85 C10 H11  sing N N 24  
A1A85 C11 H14  sing N N 25  
A1A85 C11 H13  sing N N 26  
A1A85 C2  H4   sing N N 27  
A1A85 C2  H3   sing N N 28  
A1A85 C4  H7   sing N N 29  
A1A85 C4  H8   sing N N 30  
A1A85 N4  H12  sing N N 31  
A1A85 O1  H2   sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
TFA   C1  C2   sing N N 322 
TFA   C1  O    doub N N 323 
TFA   C1  OXT  sing N N 324 
TFA   C2  F1   sing N N 325 
TFA   C2  F2   sing N N 326 
TFA   C2  F3   sing N N 327 
TFA   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_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                    7HDW 
_atom_sites.fract_transf_matrix[1][1]   0.011270 
_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]   0.011270 
_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]   0.025358 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.603 -16.139 22.230  0.56 59.73 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.541 -15.805 22.367  0.44 58.59 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.627 -15.069 22.392  0.56 59.20 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.528 -14.772 22.544  0.44 58.05 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.273 -13.717 22.110  0.56 57.12 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.131 -13.397 22.282  0.44 55.93 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.380 -13.441 22.575  0.56 57.69 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.188 -13.064 22.820  0.44 56.47 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 17.981 -15.105 23.794  0.56 60.22 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.892 -14.848 23.946  0.44 59.12 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.948 -13.995 23.939  0.56 60.68 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.809 -13.791 24.095  0.44 59.60 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.347 -16.464 24.051  0.56 60.62 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.326 -16.239 24.200  0.44 59.48 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.919 -15.191 21.745  0.56 71.06 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.821 -14.913 21.899  0.44 69.68 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.667 -14.964 24.465  0.56 72.29 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.574 -14.676 24.615  0.44 70.96 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.438 -14.143 24.751  0.56 72.84 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.314 -13.960 24.911  0.44 71.54 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.404 -13.140 23.988  0.56 72.84 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.223 -12.915 24.134  0.44 71.54 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.356 -14.013 23.171  0.56 72.84 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.213 -13.842 23.331  0.44 71.54 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.884 -16.440 24.904  0.56 72.77 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.850 -16.237 25.045  0.44 71.40 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.717 -16.656 23.339  0.56 72.77 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.719 -16.468 23.479  0.44 71.40 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.042 -17.139 24.070  0.56 72.77 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.056 -16.877 24.233  0.44 71.40 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.581 -12.882 21.337  0.56 53.90 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.457 -12.600 21.454  0.44 52.77 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.021 -11.523 21.050  0.56 50.47 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 18.904 -11.251 21.124  0.44 49.41 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.860 -10.561 21.297  0.56 47.23 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.783 -10.258 21.417  0.44 46.28 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.762 -10.966 21.690  0.56 47.32 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.711 -10.623 21.910  0.44 46.32 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.599 -11.400 19.633  0.56 50.09 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.400 -11.155 19.674  0.44 49.01 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.629 -11.850 18.562  0.56 49.75 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.379 -11.641 18.671  0.44 48.67 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.469 -11.438 18.543  0.56 49.61 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.202 -11.285 18.738  0.44 48.54 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.101 -12.707 17.662  0.56 49.64 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.827 -12.463 17.728  0.44 48.55 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.835 -13.089 20.960  0.56 64.70 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.720 -12.826 21.069  0.44 63.35 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.731 -11.297 21.666  0.56 60.58 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.651 -11.029 21.692  0.44 59.32 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.826 -10.471 19.463  0.56 60.13 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.607 -10.228 19.470  0.44 58.84 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.395 -11.951 19.569  0.56 60.13 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.196 -11.698 19.577  0.44 58.84 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.591 -12.993 17.032  0.56 59.59 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.289 -12.767 17.131  0.44 58.28 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.918 -12.975 17.710  0.56 59.59 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.657 -12.691 17.716  0.44 58.28 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.111 -9.272  21.061  0.56 43.74 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.037 -8.987  21.106  0.44 43.02 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.194 -8.206  21.449  0.56 40.24 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.146 -7.896  21.476  0.44 39.83 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.351 -7.681  20.288  0.56 35.74 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.256 -7.431  20.329  0.44 35.92 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.751 -6.607  20.408  0.56 35.96 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.558 -6.421  20.471  0.44 35.93 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 17.964 -7.054  22.098  0.56 41.01 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 17.945 -6.716  22.034  0.44 40.37 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 18.960 -6.552  21.224  0.56 41.59 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.794 -6.162  21.046  0.44 40.79 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.822 -8.991  20.671  0.56 52.51 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.731 -8.733  20.666  0.44 51.65 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.588 -8.557  22.120  0.56 48.31 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.565 -8.207  22.185  0.44 47.82 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.341 -6.339  22.309  0.56 49.23 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.325 -6.034  22.340  0.44 48.46 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.387 -7.373  22.910  0.56 49.23 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.487 -7.026  22.777  0.44 48.46 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.373 -5.919  21.593  0.56 49.93 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.222 -5.514  21.367  0.44 48.97 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.290 -8.401  19.171  0.56 30.91 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.264 -8.132  19.199  0.44 32.00 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.417 -8.001  18.074  0.56 26.30 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.293 -7.846  18.155  0.44 28.45 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 13.971 -8.349  18.412  0.56 24.69 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 13.904 -8.256  18.633  0.44 27.30 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.673 -9.483  18.799  0.56 25.04 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.751 -9.158  19.460  0.44 27.24 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.836 -8.697  16.783  0.56 23.85 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.637 -8.617  16.880  0.44 26.35 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.108 -8.157  16.194  0.56 22.14 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 16.965 -8.241  16.268  0.44 24.85 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.111 -6.952  15.513  0.56 21.26 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.068 -7.166  15.399  0.44 24.12 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.298 -8.854  16.318  0.56 21.93 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.103 -8.983  16.541  0.44 24.64 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.277 -6.447  14.966  0.56 21.02 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.283 -6.828  14.827  0.44 23.84 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.467 -8.357  15.774  0.56 21.86 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.320 -8.651  15.973  0.44 24.14 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.457 -7.149  15.098  0.56 21.29 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.410 -7.570  15.115  0.44 24.05 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.744 -9.122  19.023  0.56 37.12 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.807 -8.774  19.018  0.44 38.42 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.478 -7.046  17.950  0.56 31.58 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.286 -6.900  17.960  0.44 34.16 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 15.968 -9.642  16.966  0.56 28.65 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.666 -9.563  17.086  0.44 31.64 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.131 -8.585  16.128  0.56 28.65 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 14.949 -8.448  16.219  0.44 31.64 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.316 -6.474  15.424  0.56 25.54 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.312 -6.662  15.201  0.44 28.97 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.310 -9.665  16.774  0.56 26.34 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.049 -9.709  17.118  0.44 29.59 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.264 -5.633  14.512  0.56 25.24 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.341 -6.102  14.247  0.44 28.63 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.263 -8.829  15.864  0.56 26.25 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.080 -9.154  16.167  0.44 28.99 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.241 -6.810  14.731  0.56 25.57 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.227 -7.347  14.730  0.44 28.88 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.071 -7.378  18.253  0.56 23.16 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 12.881 -7.576  18.117  0.44 25.77 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.694 -7.487  18.721  0.56 22.67 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.513 -7.896  18.501  0.44 24.73 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.709 -7.259  17.582  0.56 21.22 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.547 -7.501  17.393  0.44 22.27 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 10.950 -6.441  16.688  0.56 22.21 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.757 -6.518  16.679  0.44 22.73 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.422 -6.467  19.837  0.56 23.78 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.114 -7.214  19.817  0.44 26.35 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.056 -6.480  20.218  0.56 25.76 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 11.739 -7.830  20.929  0.44 27.58 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.242 -6.633  17.859  0.56 27.82 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 12.956 -6.934  17.550  0.44 30.94 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.545 -8.375  19.080  0.56 27.23 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.442 -8.854  18.631  0.44 29.70 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 11.964 -6.696  20.610  0.56 28.56 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 11.387 -6.286  19.788  0.44 31.64 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.664 -5.582  19.517  0.56 28.56 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 10.151 -7.276  19.923  0.44 31.64 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 9.927  -5.907  20.819  0.56 30.94 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 12.572 -7.784  20.857  0.44 33.11 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.596  -7.993  17.624  0.56 19.80 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.476  -8.280  17.265  0.44 19.60 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.502  -7.763  16.703  0.56 18.68 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.442  -8.010  16.287  0.44 17.84 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.715  -8.262  15.295  0.56 17.38 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.701  -8.555  14.901  0.44 16.15 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 7.976  -7.858  14.394  0.56 17.59 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.001  -8.160  13.960  0.44 16.23 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.454  -8.629  18.185  0.56 23.78 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.326  -8.979  17.748  0.44 23.54 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.707  -8.195  17.048  0.56 22.43 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.604  -8.378  16.612  0.44 21.43 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.328  -6.810  16.655  0.56 22.43 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.333  -7.049  16.210  0.44 21.43 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.699  -9.128  15.069  0.56 16.52 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.676  -9.449  14.741  0.44 15.05 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 9.956  -9.647  13.736  0.56 14.85 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.013 -10.000 13.438  0.44 14.06 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.119  -10.890 13.475  0.56 13.54 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.174  -11.231 13.119  0.44 12.80 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.904  -11.715 14.369  0.56 15.49 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 8.895  -12.060 13.990  0.44 12.77 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.439 -9.996  13.553  0.56 15.61 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.498 -10.369 13.378  0.44 14.91 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.337 -8.794  13.361  0.56 16.10 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.411 -9.170  13.250  0.44 15.05 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.611 -7.949  14.421  0.56 16.65 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.744 -8.407  14.359  0.44 15.06 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 12.874 -8.492  12.118  0.56 15.96 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 12.916 -8.792  12.016  0.44 15.35 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.407 -6.841  14.256  0.56 16.81 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.565 -7.299  14.243  0.44 15.74 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.676 -7.382  11.943  0.56 15.88 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.737 -7.694  11.890  0.44 15.83 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 13.937 -6.563  13.018  0.56 16.62 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.058 -6.950  13.004  0.44 16.33 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 14.723 -5.453  12.852  0.56 17.58 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.875 -5.856  12.867  0.44 17.53 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.231 -9.430  15.671  0.56 19.84 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.168 -9.746  15.384  0.44 18.08 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.722  -8.973  13.075  0.56 17.84 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.840  -9.338  12.756  0.44 16.90 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.748 -10.489 14.329  0.56 18.76 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 11.740 -10.844 14.189  0.44 17.91 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.510 -10.547 12.760  0.56 18.76 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.645 -10.938 12.607  0.44 17.91 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.248 -8.138  15.258  0.56 20.00 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.403 -8.641  15.196  0.44 18.09 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.697 -9.050  11.393  0.56 19.17 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.701 -9.294  11.262  0.44 18.44 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.589 -6.289  14.980  0.56 20.20 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.781 -6.796  14.997  0.44 18.91 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.045 -7.193  11.108  0.56 19.07 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.076 -7.456  11.057  0.44 19.02 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 14.854 -5.080  13.596  0.56 21.12 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 15.104 -5.766  12.064  0.44 21.06 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.639  -11.001 12.243  0.56 12.79 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.803  -11.355 11.850  0.44 13.00 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.047  -12.233 11.753  0.56 13.32 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.197  -12.568 11.325  0.44 12.93 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.171  -13.177 11.335  0.56 13.08 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.310  -13.505 10.872  0.44 12.37 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.127 -12.765 10.669  0.56 12.60 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.250 -13.075 10.193  0.44 12.44 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.143  -11.915 10.561  0.56 14.56 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.305  -12.222 10.136  0.44 14.28 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.551  -13.107 9.806   0.56 17.04 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.562  -13.384 9.482   0.44 16.11 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.503  -13.809 10.645  0.56 18.77 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.560  -13.977 10.454  0.44 17.55 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 5.977  -12.670 8.461   0.56 18.60 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 5.873  -12.900 8.227   0.44 17.32 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.648  -10.359 11.661  0.56 15.37 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 8.901  -10.743 11.260  0.44 15.62 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.521  -12.647 12.455  0.56 16.01 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.670  -13.011 12.011  0.44 15.53 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.396  -11.381 10.882  0.56 17.49 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.636  -11.591 10.436  0.44 17.16 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.654  -11.395 9.925   0.56 17.49 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.855  -11.816 9.452   0.44 17.16 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.257  -13.742 9.626   0.56 20.47 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.195  -14.082 9.238   0.44 19.35 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.194  -14.595 10.166  0.56 22.54 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.076  -14.694 10.016  0.44 21.09 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.899  -14.072 11.491  0.56 22.54 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.030  -14.323 11.229  0.44 21.09 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.762  -13.203 10.800  0.56 22.54 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 4.941  -13.281 10.730  0.44 21.09 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.611  -13.450 8.011   0.56 22.34 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.401  -13.641 7.823   0.44 20.80 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.278  -12.017 8.612   0.56 22.34 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.251  -12.197 8.469   0.44 20.80 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.686  -12.282 7.926   0.56 22.34 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 6.545  -12.557 7.619   0.44 20.80 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.061  -14.437 11.739  0.56 13.16 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.208  -14.775 11.260  0.44 11.50 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.044 -15.450 11.379  0.56 12.89 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.214 -15.774 10.927  0.44 12.32 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.700  -15.990 9.998   0.56 12.68 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.864  -16.376 9.574   0.44 12.92 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.582  -16.470 9.777   0.56 13.86 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.804  -16.991 9.422   0.44 14.61 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.037 -16.564 12.423  0.56 12.53 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.259 -16.854 12.009  0.44 12.20 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.107 -17.626 12.248  0.56 13.01 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.273 -17.966 11.781  0.44 13.05 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.151 -18.531 13.473  0.56 13.36 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.328 -18.866 13.011  0.44 14.22 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.157 -19.665 13.317  0.56 13.35 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.338 -19.990 12.866  0.44 14.64 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.557 -19.176 13.175  0.56 13.76 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.714 -19.472 12.683  0.44 14.10 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.417  -14.724 12.223  0.56 15.82 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.551  -15.095 11.722  0.44 13.82 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 10.927 -15.047 11.343  0.56 15.48 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.087 -15.358 10.870  0.44 14.80 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.167 -16.158 13.294  0.56 15.06 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.481 -16.435 12.857  0.44 14.66 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.175  -17.002 12.392  0.56 15.06 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.386  -17.270 12.073  0.44 14.66 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 10.902 -18.169 11.471  0.56 15.64 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 11.008 -18.505 11.018  0.44 15.69 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 11.974 -17.202 12.147  0.56 15.64 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.155 -17.587 11.639  0.44 15.69 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.405 -18.006 14.248  0.56 16.05 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.580 -18.339 13.784  0.44 17.09 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.273 -18.923 13.611  0.56 16.05 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.455 -19.269 13.153  0.44 17.09 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.116 -20.237 14.099  0.56 16.04 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.321 -20.543 13.665  0.44 17.59 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 11.938 -20.176 12.521  0.56 16.04 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 12.107 -20.518 12.088  0.44 17.59 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.069 -19.812 12.819  0.56 16.53 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.289 -20.151 12.630  0.44 16.95 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.582 -18.459 12.649  0.56 16.53 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.763 -18.992 11.937  0.44 16.95 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 13.887 -18.959 13.974  0.56 16.53 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.940 -18.958 13.375  0.44 16.95 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.641 -15.886 9.061   0.56 12.32 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.753 -16.210 8.593   0.44 12.47 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.438 -16.421 7.721   0.56 12.96 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.509 -16.768 7.267   0.44 12.69 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.001 -17.831 7.579   0.56 12.83 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.118 -18.152 7.094   0.44 12.54 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.354 -18.701 6.985   0.56 13.51 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.495 -19.029 6.485   0.44 12.64 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.067 -15.494 6.674   0.56 14.53 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.051 -15.846 6.175   0.44 13.10 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.295 -14.224 6.308   0.56 15.89 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.487 -14.425 6.117   0.44 14.31 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.100 -13.390 5.318   0.56 15.55 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 10.984 -13.738 4.856   0.44 14.12 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 8.917  -14.577 5.735   0.56 16.70 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.954  -14.397 6.197   0.44 15.28 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.407 -15.495 9.172   0.56 14.80 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.503 -15.784 8.673   0.44 14.98 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.486  -16.457 7.542   0.56 15.57 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.558  -16.859 7.144   0.44 15.25 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 11.936 -15.206 7.000   0.56 17.46 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 12.012 -15.773 6.295   0.44 15.74 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.185 -15.994 5.853   0.56 17.46 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 10.870 -16.268 5.319   0.44 15.74 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.161 -13.687 7.106   0.56 19.08 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.830 -13.934 6.875   0.44 17.19 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.600 -12.586 5.099   0.56 18.69 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.626 -12.839 4.826   0.44 16.97 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 11.948 -13.149 5.722   0.56 18.69 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 11.955 -13.708 4.873   0.44 16.97 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.252 -13.913 4.515   0.56 18.69 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 10.686 -14.240 4.080   0.44 16.97 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.570  -13.819 5.242   0.56 20.06 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.654  -13.488 6.047   0.44 18.36 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 9.017  -15.340 5.146   0.56 20.06 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.592  -14.985 5.518   0.44 18.36 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.321  -14.803 6.466   0.56 20.06 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.680  -14.697 7.078   0.44 18.36 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.207 -18.058 8.097   0.56 11.92 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.329 -18.355 7.603   0.44 12.77 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 12.892 -19.344 8.027   0.56 12.68 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 13.011 -19.637 7.512   0.44 13.06 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.630 -19.564 9.342   0.56 12.83 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.775 -19.849 8.810   0.44 13.09 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.506 -18.788 10.296  0.56 12.35 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.652 -19.071 9.761   0.44 13.47 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 13.888 -19.394 6.860   0.56 13.05 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 13.959 -19.699 6.304   0.44 13.91 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 14.930 -18.450 7.100   0.56 12.83 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 15.041 -18.783 6.503   0.44 13.64 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.223 -19.079 5.526   0.56 14.31 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.239 -19.355 5.011   0.44 14.92 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.670 -17.446 8.492   0.56 14.33 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.789 -17.755 8.022   0.44 15.34 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.242 -20.046 7.903   0.56 15.24 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.357 -20.350 7.426   0.44 15.70 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.278 -20.280 6.802   0.56 15.68 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.313 -20.601 6.228   0.44 16.71 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.559 -18.801 7.529   0.56 15.42 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.570 -18.819 5.850   0.44 16.39 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 13.865 -19.183 4.800   0.56 17.20 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 13.784 -19.620 4.254   0.44 17.93 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.485 -19.691 5.375   0.56 17.20 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.393 -19.823 4.971   0.44 17.93 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 12.891 -18.172 5.521   0.56 17.20 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 13.077 -18.400 4.969   0.44 17.93 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.428 -20.629 9.371   0.56 13.68 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.590 -20.908 8.839   0.44 13.97 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.274 -20.912 10.522  0.56 14.76 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.405 -21.172 10.018  0.44 14.76 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.088 -19.693 10.947  0.56 13.80 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.272 -19.973 10.391  0.44 13.08 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.264 -19.447 12.146  0.56 14.51 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.555 -19.767 11.578  0.44 13.69 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.202 -22.076 10.172  0.56 17.49 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.277 -22.410 9.789   0.44 18.03 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.184 -22.396 11.277  0.56 20.47 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.162 -22.719 10.980  0.44 21.11 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.758 -22.988 12.296  0.56 22.10 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.676 -22.606 12.127  0.44 22.44 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.378 -22.076 11.115  0.56 21.90 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.336 -23.083 10.774  0.44 22.07 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.503 -21.181 8.728   0.56 16.44 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.693 -21.479 8.200   0.44 16.78 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.711 -21.169 11.265  0.56 17.73 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 14.828 -21.369 10.772  0.44 17.73 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.657 -22.864 10.019  0.56 21.01 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.705 -23.186 9.624   0.44 21.65 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 16.690 -21.851 9.364   0.56 21.01 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 16.853 -22.266 9.022   0.44 21.65 ?  14  ASP   A HB3  1 
ATOM   371  N N    A ASN   A 1 15  ? 16.582 -18.907 9.984   0.56 12.74 ?  15  ASN   A N    1 
ATOM   372  N N    B ASN   A 1 15  ? 16.690 -19.164 9.407   0.44 12.16 ?  15  ASN   A N    1 
ATOM   373  C CA   A ASN   A 1 15  ? 17.561 -17.868 10.279  0.56 12.43 ?  15  ASN   A CA   1 
ATOM   374  C CA   B ASN   A 1 15  ? 17.683 -18.120 9.649   0.44 11.84 ?  15  ASN   A CA   1 
ATOM   375  C C    A ASN   A 1 15  ? 17.202 -16.479 9.774   0.56 11.86 ?  15  ASN   A C    1 
ATOM   376  C C    B ASN   A 1 15  ? 17.315 -16.735 9.123   0.44 11.80 ?  15  ASN   A C    1 
ATOM   377  O O    A ASN   A 1 15  ? 17.964 -15.545 10.038  0.56 12.23 ?  15  ASN   A O    1 
ATOM   378  O O    B ASN   A 1 15  ? 18.096 -15.797 9.325   0.44 12.10 ?  15  ASN   A O    1 
ATOM   379  C CB   A ASN   A 1 15  ? 18.941 -18.249 9.714   0.56 12.39 ?  15  ASN   A CB   1 
ATOM   380  C CB   B ASN   A 1 15  ? 19.047 -18.535 9.070   0.44 11.10 ?  15  ASN   A CB   1 
ATOM   381  C CG   A ASN   A 1 15  ? 18.938 -18.374 8.201   0.56 12.77 ?  15  ASN   A CG   1 
ATOM   382  C CG   B ASN   A 1 15  ? 19.032 -18.617 7.554   0.44 12.01 ?  15  ASN   A CG   1 
ATOM   383  O OD1  A ASN   A 1 15  ? 18.238 -19.215 7.637   0.56 13.35 ?  15  ASN   A OD1  1 
ATOM   384  O OD1  B ASN   A 1 15  ? 18.329 -19.439 6.971   0.44 12.64 ?  15  ASN   A OD1  1 
ATOM   385  N ND2  A ASN   A 1 15  ? 19.727 -17.532 7.536   0.56 12.71 ?  15  ASN   A ND2  1 
ATOM   386  N ND2  B ASN   A 1 15  ? 19.818 -17.770 6.910   0.44 12.16 ?  15  ASN   A ND2  1 
ATOM   387  H H    A ASN   A 1 15  ? 16.369 -18.957 9.157   0.56 15.31 ?  15  ASN   A H    1 
ATOM   388  H H    B ASN   A 1 15  ? 16.411 -19.214 8.595   0.44 14.61 ?  15  ASN   A H    1 
ATOM   389  H HA   A ASN   A 1 15  ? 17.656 -17.795 11.242  0.56 14.94 ?  15  ASN   A HA   1 
ATOM   390  H HA   B ASN   A 1 15  ? 17.807 -18.053 10.606  0.44 14.23 ?  15  ASN   A HA   1 
ATOM   391  H HB2  A ASN   A 1 15  ? 19.581 -17.555 9.962   0.56 14.90 ?  15  ASN   A HB2  1 
ATOM   392  H HB2  B ASN   A 1 15  ? 19.718 -17.876 9.329   0.44 13.34 ?  15  ASN   A HB2  1 
ATOM   393  H HB3  A ASN   A 1 15  ? 19.209 -19.095 10.090  0.56 14.90 ?  15  ASN   A HB3  1 
ATOM   394  H HB3  B ASN   A 1 15  ? 19.305 -19.409 9.421   0.44 13.34 ?  15  ASN   A HB3  1 
ATOM   395  H HD21 A ASN   A 1 15  ? 19.761 -17.558 6.676   0.56 15.28 ?  15  ASN   A HD21 1 
ATOM   396  H HD21 B ASN   A 1 15  ? 19.844 -17.785 6.050   0.44 14.62 ?  15  ASN   A HD21 1 
ATOM   397  H HD22 A ASN   A 1 15  ? 20.203 -16.953 7.963   0.56 15.28 ?  15  ASN   A HD22 1 
ATOM   398  H HD22 B ASN   A 1 15  ? 20.300 -17.207 7.344   0.44 14.62 ?  15  ASN   A HD22 1 
ATOM   399  N N    A VAL   A 1 16  ? 16.082 -16.304 9.073   0.56 11.68 ?  16  VAL   A N    1 
ATOM   400  N N    B VAL   A 1 16  ? 16.171 -16.574 8.462   0.44 11.64 ?  16  VAL   A N    1 
ATOM   401  C CA   A VAL   A 1 16  ? 15.710 -15.017 8.495   0.56 11.57 ?  16  VAL   A CA   1 
ATOM   402  C CA   B VAL   A 1 16  ? 15.763 -15.301 7.873   0.44 11.26 ?  16  VAL   A CA   1 
ATOM   403  C C    A VAL   A 1 16  ? 14.426 -14.520 9.145   0.56 12.04 ?  16  VAL   A C    1 
ATOM   404  C C    B VAL   A 1 16  ? 14.500 -14.799 8.568   0.44 11.36 ?  16  VAL   A C    1 
ATOM   405  O O    A VAL   A 1 16  ? 13.435 -15.260 9.238   0.56 12.22 ?  16  VAL   A O    1 
ATOM   406  O O    B VAL   A 1 16  ? 13.494 -15.516 8.645   0.44 10.81 ?  16  VAL   A O    1 
ATOM   407  C CB   A VAL   A 1 16  ? 15.572 -15.079 6.962   0.56 11.91 ?  16  VAL   A CB   1 
ATOM   408  C CB   B VAL   A 1 16  ? 15.526 -15.424 6.357   0.44 11.59 ?  16  VAL   A CB   1 
ATOM   409  C CG1  A VAL   A 1 16  ? 15.197 -13.697 6.402   0.56 11.88 ?  16  VAL   A CG1  1 
ATOM   410  C CG1  B VAL   A 1 16  ? 15.049 -14.090 5.785   0.44 12.42 ?  16  VAL   A CG1  1 
ATOM   411  C CG2  A VAL   A 1 16  ? 16.857 -15.605 6.328   0.56 12.72 ?  16  VAL   A CG2  1 
ATOM   412  C CG2  B VAL   A 1 16  ? 16.782 -15.910 5.645   0.44 11.28 ?  16  VAL   A CG2  1 
ATOM   413  H H    A VAL   A 1 16  ? 15.507 -16.927 8.921   0.56 14.04 ?  16  VAL   A H    1 
ATOM   414  H H    B VAL   A 1 16  ? 15.613 -17.216 8.338   0.44 14.00 ?  16  VAL   A H    1 
ATOM   415  H HA   A VAL   A 1 16  ? 16.402 -14.370 8.695   0.56 13.90 ?  16  VAL   A HA   1 
ATOM   416  H HA   B VAL   A 1 16  ? 16.470 -14.654 8.023   0.44 13.54 ?  16  VAL   A HA   1 
ATOM   417  H HB   A VAL   A 1 16  ? 14.856 -15.693 6.737   0.56 14.32 ?  16  VAL   A HB   1 
ATOM   418  H HB   B VAL   A 1 16  ? 14.827 -16.083 6.212   0.44 13.93 ?  16  VAL   A HB   1 
ATOM   419  H HG11 A VAL   A 1 16  ? 15.290 -13.712 5.437   0.56 14.28 ?  16  VAL   A HG11 1 
ATOM   420  H HG11 B VAL   A 1 16  ? 15.056 -14.145 4.820   0.44 14.93 ?  16  VAL   A HG11 1 
ATOM   421  H HG12 A VAL   A 1 16  ? 14.280 -13.494 6.643   0.56 14.28 ?  16  VAL   A HG12 1 
ATOM   422  H HG12 B VAL   A 1 16  ? 14.148 -13.913 6.099   0.44 14.93 ?  16  VAL   A HG12 1 
ATOM   423  H HG13 A VAL   A 1 16  ? 15.795 -13.032 6.780   0.56 14.28 ?  16  VAL   A HG13 1 
ATOM   424  H HG13 B VAL   A 1 16  ? 15.648 -13.389 6.084   0.44 14.93 ?  16  VAL   A HG13 1 
ATOM   425  H HG21 A VAL   A 1 16  ? 16.900 -15.309 5.406   0.56 15.29 ?  16  VAL   A HG21 1 
ATOM   426  H HG21 B VAL   A 1 16  ? 16.804 -15.524 4.758   0.44 13.56 ?  16  VAL   A HG21 1 
ATOM   427  H HG22 A VAL   A 1 16  ? 17.613 -15.267 6.825   0.56 15.29 ?  16  VAL   A HG22 1 
ATOM   428  H HG22 B VAL   A 1 16  ? 17.560 -15.624 6.149   0.44 13.56 ?  16  VAL   A HG22 1 
ATOM   429  H HG23 A VAL   A 1 16  ? 16.847 -16.575 6.365   0.56 15.29 ?  16  VAL   A HG23 1 
ATOM   430  H HG23 B VAL   A 1 16  ? 16.762 -16.878 5.592   0.44 13.56 ?  16  VAL   A HG23 1 
ATOM   431  N N    A TYR   A 1 17  ? 14.449 -13.255 9.567   0.56 12.59 ?  17  TYR   A N    1 
ATOM   432  N N    B TYR   A 1 17  ? 14.545 -13.544 9.016   0.44 11.35 ?  17  TYR   A N    1 
ATOM   433  C CA   A TYR   A 1 17  ? 13.335 -12.573 10.206  0.56 12.12 ?  17  TYR   A CA   1 
ATOM   434  C CA   B TYR   A 1 17  ? 13.470 -12.870 9.730   0.44 11.76 ?  17  TYR   A CA   1 
ATOM   435  C C    A TYR   A 1 17  ? 13.089 -11.262 9.477   0.56 12.68 ?  17  TYR   A C    1 
ATOM   436  C C    B TYR   A 1 17  ? 13.192 -11.537 9.043   0.44 12.30 ?  17  TYR   A C    1 
ATOM   437  O O    A TYR   A 1 17  ? 14.022 -10.675 8.926   0.56 12.17 ?  17  TYR   A O    1 
ATOM   438  O O    B TYR   A 1 17  ? 14.058 -10.987 8.358   0.44 12.13 ?  17  TYR   A O    1 
ATOM   439  C CB   A TYR   A 1 17  ? 13.675 -12.299 11.671  0.56 12.43 ?  17  TYR   A CB   1 
ATOM   440  C CB   B TYR   A 1 17  ? 13.881 -12.611 11.185  0.44 12.40 ?  17  TYR   A CB   1 
ATOM   441  C CG   A TYR   A 1 17  ? 13.856 -13.572 12.459  0.56 12.78 ?  17  TYR   A CG   1 
ATOM   442  C CG   B TYR   A 1 17  ? 14.147 -13.870 11.986  0.44 14.20 ?  17  TYR   A CG   1 
ATOM   443  C CD1  A TYR   A 1 17  ? 15.038 -14.303 12.386  0.56 13.96 ?  17  TYR   A CD1  1 
ATOM   444  C CD1  B TYR   A 1 17  ? 15.366 -14.535 11.900  0.44 15.21 ?  17  TYR   A CD1  1 
ATOM   445  C CD2  A TYR   A 1 17  ? 12.833 -14.058 13.253  0.56 12.96 ?  17  TYR   A CD2  1 
ATOM   446  C CD2  B TYR   A 1 17  ? 13.181 -14.393 12.833  0.44 14.77 ?  17  TYR   A CD2  1 
ATOM   447  C CE1  A TYR   A 1 17  ? 15.195 -15.483 13.088  0.56 14.37 ?  17  TYR   A CE1  1 
ATOM   448  C CE1  B TYR   A 1 17  ? 15.608 -15.694 12.632  0.44 15.88 ?  17  TYR   A CE1  1 
ATOM   449  C CE2  A TYR   A 1 17  ? 12.975 -15.243 13.962  0.56 13.57 ?  17  TYR   A CE2  1 
ATOM   450  C CE2  B TYR   A 1 17  ? 13.414 -15.548 13.568  0.44 15.71 ?  17  TYR   A CE2  1 
ATOM   451  C CZ   A TYR   A 1 17  ? 14.163 -15.947 13.880  0.56 13.69 ?  17  TYR   A CZ   1 
ATOM   452  C CZ   B TYR   A 1 17  ? 14.630 -16.190 13.466  0.44 16.19 ?  17  TYR   A CZ   1 
ATOM   453  O OH   A TYR   A 1 17  ? 14.314 -17.122 14.580  0.56 14.99 ?  17  TYR   A OH   1 
ATOM   454  O OH   B TYR   A 1 17  ? 14.859 -17.335 14.198  0.44 17.27 ?  17  TYR   A OH   1 
ATOM   455  H H    A TYR   A 1 17  ? 15.140 -12.739 9.479   0.56 15.13 ?  17  TYR   A H    1 
ATOM   456  H H    B TYR   A 1 17  ? 15.228 -13.038 8.902   0.44 13.65 ?  17  TYR   A H    1 
ATOM   457  H HA   A TYR   A 1 17  ? 12.534 -13.109 10.150  0.56 14.57 ?  17  TYR   A HA   1 
ATOM   458  H HA   B TYR   A 1 17  ? 12.666 -13.422 9.721   0.44 14.13 ?  17  TYR   A HA   1 
ATOM   459  H HB2  A TYR   A 1 17  ? 14.494 -11.793 11.709  0.56 14.94 ?  17  TYR   A HB2  1 
ATOM   460  H HB2  B TYR   A 1 17  ? 14.692 -12.087 11.192  0.44 14.90 ?  17  TYR   A HB2  1 
ATOM   461  H HB3  A TYR   A 1 17  ? 12.950 -11.793 12.074  0.56 14.94 ?  17  TYR   A HB3  1 
ATOM   462  H HB3  B TYR   A 1 17  ? 13.169 -12.134 11.629  0.44 14.90 ?  17  TYR   A HB3  1 
ATOM   463  H HD1  A TYR   A 1 17  ? 15.730 -13.987 11.848  0.56 16.77 ?  17  TYR   A HD1  1 
ATOM   464  H HD1  B TYR   A 1 17  ? 16.031 -14.206 11.341  0.44 18.28 ?  17  TYR   A HD1  1 
ATOM   465  H HD2  A TYR   A 1 17  ? 12.028 -13.591 13.308  0.56 15.57 ?  17  TYR   A HD2  1 
ATOM   466  H HD2  B TYR   A 1 17  ? 12.358 -13.972 12.910  0.44 17.75 ?  17  TYR   A HD2  1 
ATOM   467  H HE1  A TYR   A 1 17  ? 15.995 -15.954 13.031  0.56 17.26 ?  17  TYR   A HE1  1 
ATOM   468  H HE1  B TYR   A 1 17  ? 16.431 -16.130 12.568  0.44 19.07 ?  17  TYR   A HE1  1 
ATOM   469  H HE2  A TYR   A 1 17  ? 12.280 -15.558 14.498  0.56 16.30 ?  17  TYR   A HE2  1 
ATOM   470  H HE2  B TYR   A 1 17  ? 12.755 -15.889 14.133  0.44 18.87 ?  17  TYR   A HE2  1 
ATOM   471  H HH   A TYR   A 1 17  ? 13.575 -17.368 14.888  0.56 18.01 ?  17  TYR   A HH   1 
ATOM   472  H HH   B TYR   A 1 17  ? 15.617 -17.650 14.012  0.44 20.74 ?  17  TYR   A HH   1 
ATOM   473  N N    A ILE   A 1 18  ? 11.836 -10.793 9.469   0.56 13.14 ?  18  ILE   A N    1 
ATOM   474  N N    B ILE   A 1 18  ? 11.980 -11.005 9.227   0.44 13.13 ?  18  ILE   A N    1 
ATOM   475  C CA   A ILE   A 1 18  ? 11.467 -9.613  8.688   0.56 13.18 ?  18  ILE   A CA   1 
ATOM   476  C CA   B ILE   A 1 18  ? 11.571 -9.811  8.491   0.44 13.99 ?  18  ILE   A CA   1 
ATOM   477  C C    A ILE   A 1 18  ? 10.498 -8.741  9.477   0.56 13.53 ?  18  ILE   A C    1 
ATOM   478  C C    B ILE   A 1 18  ? 10.591 -8.974  9.311   0.44 14.71 ?  18  ILE   A C    1 
ATOM   479  O O    A ILE   A 1 18  ? 9.626  -9.245  10.190  0.56 14.03 ?  18  ILE   A O    1 
ATOM   480  O O    B ILE   A 1 18  ? 9.830  -9.497  10.128  0.44 15.51 ?  18  ILE   A O    1 
ATOM   481  C CB   A ILE   A 1 18  ? 10.919 -10.010 7.300   0.56 13.42 ?  18  ILE   A CB   1 
ATOM   482  C CB   B ILE   A 1 18  ? 11.004 -10.211 7.109   0.44 14.14 ?  18  ILE   A CB   1 
ATOM   483  C CG1  A ILE   A 1 18  ? 10.901 -8.820  6.338   0.56 14.49 ?  18  ILE   A CG1  1 
ATOM   484  C CG1  B ILE   A 1 18  ? 10.916 -9.000  6.190   0.44 14.81 ?  18  ILE   A CG1  1 
ATOM   485  C CG2  A ILE   A 1 18  ? 9.548  -10.672 7.414   0.56 14.73 ?  18  ILE   A CG2  1 
ATOM   486  C CG2  B ILE   A 1 18  ? 9.656  -10.913 7.258   0.44 14.09 ?  18  ILE   A CG2  1 
ATOM   487  C CD1  A ILE   A 1 18  ? 10.804 -9.230  4.887   0.56 15.85 ?  18  ILE   A CD1  1 
ATOM   488  C CD1  B ILE   A 1 18  ? 10.449 -9.340  4.809   0.44 16.38 ?  18  ILE   A CD1  1 
ATOM   489  H H    A ILE   A 1 18  ? 11.176 -11.139 9.903   0.56 15.79 ?  18  ILE   A H    1 
ATOM   490  H H    B ILE   A 1 18  ? 11.389 -11.325 9.764   0.44 15.78 ?  18  ILE   A H    1 
ATOM   491  H HA   A ILE   A 1 18  ? 12.263 -9.082  8.536   0.56 15.84 ?  18  ILE   A HA   1 
ATOM   492  H HA   B ILE   A 1 18  ? 12.366 -9.274  8.334   0.44 16.81 ?  18  ILE   A HA   1 
ATOM   493  H HB   A ILE   A 1 18  ? 11.525 -10.662 6.927   0.56 16.12 ?  18  ILE   A HB   1 
ATOM   494  H HB   B ILE   A 1 18  ? 11.620 -10.844 6.706   0.44 17.00 ?  18  ILE   A HB   1 
ATOM   495  H HG12 A ILE   A 1 18  ? 10.139 -8.252  6.533   0.56 17.41 ?  18  ILE   A HG12 1 
ATOM   496  H HG12 B ILE   A 1 18  ? 10.296 -8.361  6.568   0.44 17.79 ?  18  ILE   A HG12 1 
ATOM   497  H HG13 A ILE   A 1 18  ? 11.723 -8.310  6.437   0.56 17.41 ?  18  ILE   A HG13 1 
ATOM   498  H HG13 B ILE   A 1 18  ? 11.800 -8.599  6.116   0.44 17.79 ?  18  ILE   A HG13 1 
ATOM   499  H HG21 A ILE   A 1 18  ? 9.308  -11.054 6.552   0.56 17.70 ?  18  ILE   A HG21 1 
ATOM   500  H HG21 B ILE   A 1 18  ? 9.417  -11.324 6.411   0.44 16.94 ?  18  ILE   A HG21 1 
ATOM   501  H HG22 A ILE   A 1 18  ? 9.593  -11.371 8.082   0.56 17.70 ?  18  ILE   A HG22 1 
ATOM   502  H HG22 B ILE   A 1 18  ? 9.725  -11.594 7.945   0.44 16.94 ?  18  ILE   A HG22 1 
ATOM   503  H HG23 A ILE   A 1 18  ? 8.889  -10.007 7.671   0.56 17.70 ?  18  ILE   A HG23 1 
ATOM   504  H HG23 B ILE   A 1 18  ? 8.983  -10.260 7.508   0.44 16.94 ?  18  ILE   A HG23 1 
ATOM   505  H HD11 A ILE   A 1 18  ? 10.815 -8.435  4.327   0.56 19.05 ?  18  ILE   A HD11 1 
ATOM   506  H HD11 B ILE   A 1 18  ? 10.558 -8.560  4.243   0.44 19.67 ?  18  ILE   A HD11 1 
ATOM   507  H HD12 A ILE   A 1 18  ? 11.552 -9.801  4.666   0.56 19.05 ?  18  ILE   A HD12 1 
ATOM   508  H HD12 B ILE   A 1 18  ? 10.983 -10.074 4.470   0.44 19.67 ?  18  ILE   A HD12 1 
ATOM   509  H HD13 A ILE   A 1 18  ? 9.969  -9.711  4.752   0.56 19.05 ?  18  ILE   A HD13 1 
ATOM   510  H HD13 B ILE   A 1 18  ? 9.516  -9.595  4.849   0.44 19.67 ?  18  ILE   A HD13 1 
ATOM   511  N N    A LYS   A 1 19  ? 10.653 -7.421  9.337   0.56 13.65 ?  19  LYS   A N    1 
ATOM   512  N N    B LYS   A 1 19  ? 10.609 -7.657  9.067   0.44 15.19 ?  19  LYS   A N    1 
ATOM   513  C CA   A LYS   A 1 19  ? 9.832  -6.460  10.061  0.56 14.52 ?  19  LYS   A CA   1 
ATOM   514  C CA   B LYS   A 1 19  ? 9.775  -6.686  9.775   0.44 15.30 ?  19  LYS   A CA   1 
ATOM   515  C C    A LYS   A 1 19  ? 9.670  -5.216  9.204   0.56 14.59 ?  19  LYS   A C    1 
ATOM   516  C C    B LYS   A 1 19  ? 9.601  -5.435  8.914   0.44 14.74 ?  19  LYS   A C    1 
ATOM   517  O O    A LYS   A 1 19  ? 10.608 -4.812  8.516   0.56 14.50 ?  19  LYS   A O    1 
ATOM   518  O O    B LYS   A 1 19  ? 10.480 -5.089  8.120   0.44 13.75 ?  19  LYS   A O    1 
ATOM   519  C CB   A LYS   A 1 19  ? 10.535 -6.087  11.370  0.56 15.66 ?  19  LYS   A CB   1 
ATOM   520  C CB   B LYS   A 1 19  ? 10.436 -6.305  11.109  0.44 16.41 ?  19  LYS   A CB   1 
ATOM   521  C CG   A LYS   A 1 19  ? 9.826  -5.085  12.256  0.56 16.82 ?  19  LYS   A CG   1 
ATOM   522  C CG   B LYS   A 1 19  ? 9.643  -5.352  12.012  0.44 17.53 ?  19  LYS   A CG   1 
ATOM   523  C CD   A LYS   A 1 19  ? 10.711 -4.818  13.459  0.56 17.96 ?  19  LYS   A CD   1 
ATOM   524  C CD   B LYS   A 1 19  ? 10.432 -5.066  13.293  0.44 18.40 ?  19  LYS   A CD   1 
ATOM   525  C CE   A LYS   A 1 19  ? 10.069 -3.910  14.479  0.56 18.95 ?  19  LYS   A CE   1 
ATOM   526  C CE   B LYS   A 1 19  ? 9.704  -4.120  14.244  0.44 19.36 ?  19  LYS   A CE   1 
ATOM   527  N NZ   A LYS   A 1 19  ? 10.985 -3.734  15.638  0.56 20.05 ?  19  LYS   A NZ   1 
ATOM   528  N NZ   B LYS   A 1 19  ? 10.552 -3.767  15.425  0.44 20.07 ?  19  LYS   A NZ   1 
ATOM   529  H H    A LYS   A 1 19  ? 11.240 -7.044  8.822   0.56 16.41 ?  19  LYS   A H    1 
ATOM   530  H H    B LYS   A 1 19  ? 11.118 -7.305  8.479   0.44 18.25 ?  19  LYS   A H    1 
ATOM   531  H HA   A LYS   A 1 19  ? 8.957  -6.829  10.258  0.56 17.44 ?  19  LYS   A HA   1 
ATOM   532  H HA   B LYS   A 1 19  ? 8.906  -7.079  9.956   0.44 18.38 ?  19  LYS   A HA   1 
ATOM   533  H HB2  A LYS   A 1 19  ? 10.644 -6.896  11.897  0.56 18.82 ?  19  LYS   A HB2  1 
ATOM   534  H HB2  B LYS   A 1 19  ? 10.592 -7.116  11.617  0.44 19.71 ?  19  LYS   A HB2  1 
ATOM   535  H HB3  A LYS   A 1 19  ? 11.405 -5.719  11.161  0.56 18.82 ?  19  LYS   A HB3  1 
ATOM   536  H HB3  B LYS   A 1 19  ? 11.283 -5.878  10.915  0.44 19.71 ?  19  LYS   A HB3  1 
ATOM   537  H HG2  A LYS   A 1 19  ? 9.689  -4.253  11.775  0.56 20.21 ?  19  LYS   A HG2  1 
ATOM   538  H HG2  B LYS   A 1 19  ? 9.492  -4.511  11.552  0.44 21.06 ?  19  LYS   A HG2  1 
ATOM   539  H HG3  A LYS   A 1 19  ? 8.980  -5.451  12.561  0.56 20.21 ?  19  LYS   A HG3  1 
ATOM   540  H HG3  B LYS   A 1 19  ? 8.797  -5.760  12.259  0.44 21.06 ?  19  LYS   A HG3  1 
ATOM   541  H HD2  A LYS   A 1 19  ? 10.909 -5.663  13.891  0.56 21.58 ?  19  LYS   A HD2  1 
ATOM   542  H HD2  B LYS   A 1 19  ? 10.589 -5.899  13.764  0.44 22.11 ?  19  LYS   A HD2  1 
ATOM   543  H HD3  A LYS   A 1 19  ? 11.532 -4.401  13.154  0.56 21.58 ?  19  LYS   A HD3  1 
ATOM   544  H HD3  B LYS   A 1 19  ? 11.281 -4.656  13.058  0.44 22.11 ?  19  LYS   A HD3  1 
ATOM   545  H HE2  A LYS   A 1 19  ? 9.902  -3.042  14.078  0.56 22.76 ?  19  LYS   A HE2  1 
ATOM   546  H HE2  B LYS   A 1 19  ? 9.484  -3.300  13.777  0.44 23.26 ?  19  LYS   A HE2  1 
ATOM   547  H HE3  A LYS   A 1 19  ? 9.242  -4.308  14.790  0.56 22.76 ?  19  LYS   A HE3  1 
ATOM   548  H HE3  B LYS   A 1 19  ? 8.899  -4.549  14.571  0.44 23.26 ?  19  LYS   A HE3  1 
ATOM   549  H HZ1  A LYS   A 1 19  ? 10.584 -3.255  16.269  0.56 24.08 ?  19  LYS   A HZ1  1 
ATOM   550  H HZ1  B LYS   A 1 19  ? 10.111 -3.216  15.967  0.44 24.10 ?  19  LYS   A HZ1  1 
ATOM   551  H HZ2  A LYS   A 1 19  ? 11.206 -4.529  15.972  0.56 24.08 ?  19  LYS   A HZ2  1 
ATOM   552  H HZ2  B LYS   A 1 19  ? 10.769 -4.504  15.878  0.44 24.10 ?  19  LYS   A HZ2  1 
ATOM   553  H HZ3  A LYS   A 1 19  ? 11.724 -3.314  15.379  0.56 24.08 ?  19  LYS   A HZ3  1 
ATOM   554  H HZ3  B LYS   A 1 19  ? 11.302 -3.366  15.155  0.44 24.10 ?  19  LYS   A HZ3  1 
ATOM   555  N N    A ASN   A 1 20  ? 8.478  -4.620  9.230   0.56 14.95 ?  20  ASN   A N    1 
ATOM   556  N N    B ASN   A 1 20  ? 8.461  -4.753  9.087   0.44 15.38 ?  20  ASN   A N    1 
ATOM   557  C CA   A ASN   A 1 20  ? 8.299  -3.277  8.689   0.56 15.27 ?  20  ASN   A CA   1 
ATOM   558  C CA   B ASN   A 1 20  ? 8.191  -3.467  8.424   0.44 15.59 ?  20  ASN   A CA   1 
ATOM   559  C C    A ASN   A 1 20  ? 8.933  -2.303  9.671   0.56 15.87 ?  20  ASN   A C    1 
ATOM   560  C C    B ASN   A 1 20  ? 8.722  -2.353  9.319   0.44 16.24 ?  20  ASN   A C    1 
ATOM   561  O O    A ASN   A 1 20  ? 8.457  -2.149  10.802  0.56 16.45 ?  20  ASN   A O    1 
ATOM   562  O O    B ASN   A 1 20  ? 8.037  -1.882  10.232  0.44 17.08 ?  20  ASN   A O    1 
ATOM   563  C CB   A ASN   A 1 20  ? 6.813  -2.990  8.486   0.56 15.63 ?  20  ASN   A CB   1 
ATOM   564  C CB   B ASN   A 1 20  ? 6.692  -3.302  8.164   0.44 15.27 ?  20  ASN   A CB   1 
ATOM   565  C CG   A ASN   A 1 20  ? 6.528  -1.540  8.137   0.56 16.36 ?  20  ASN   A CG   1 
ATOM   566  C CG   B ASN   A 1 20  ? 6.327  -1.948  7.526   0.44 14.62 ?  20  ASN   A CG   1 
ATOM   567  O OD1  A ASN   A 1 20  ? 5.533  -0.980  8.595   0.56 19.11 ?  20  ASN   A OD1  1 
ATOM   568  O OD1  B ASN   A 1 20  ? 5.234  -1.406  7.768   0.44 14.55 ?  20  ASN   A OD1  1 
ATOM   569  N ND2  A ASN   A 1 20  ? 7.397  -0.923  7.333   0.56 15.60 ?  20  ASN   A ND2  1 
ATOM   570  N ND2  B ASN   A 1 20  ? 7.222  -1.418  6.692   0.44 14.70 ?  20  ASN   A ND2  1 
ATOM   571  H H    A ASN   A 1 20  ? 7.764  -4.975  9.542   0.56 17.97 ?  20  ASN   A H    1 
ATOM   572  H H    B ASN   A 1 20  ? 7.815  -5.037  9.581   0.44 18.48 ?  20  ASN   A H    1 
ATOM   573  H HA   A ASN   A 1 20  ? 8.749  -3.207  7.834   0.56 18.34 ?  20  ASN   A HA   1 
ATOM   574  H HA   B ASN   A 1 20  ? 8.661  -3.447  7.578   0.44 18.72 ?  20  ASN   A HA   1 
ATOM   575  H HB2  A ASN   A 1 20  ? 6.480  -3.538  7.758   0.56 18.78 ?  20  ASN   A HB2  1 
ATOM   576  H HB2  B ASN   A 1 20  ? 6.398  -3.998  7.566   0.44 18.34 ?  20  ASN   A HB2  1 
ATOM   577  H HB3  A ASN   A 1 20  ? 6.334  -3.197  9.301   0.56 18.78 ?  20  ASN   A HB3  1 
ATOM   578  H HB3  B ASN   A 1 20  ? 6.221  -3.379  9.011   0.44 18.34 ?  20  ASN   A HB3  1 
ATOM   579  H HD21 A ASN   A 1 20  ? 7.273  -0.100  7.109   0.56 18.74 ?  20  ASN   A HD21 1 
ATOM   580  H HD21 B ASN   A 1 20  ? 7.061  -0.667  6.319   0.44 17.66 ?  20  ASN   A HD21 1 
ATOM   581  H HD22 A ASN   A 1 20  ? 8.085  -1.345  7.035   0.56 18.74 ?  20  ASN   A HD22 1 
ATOM   582  H HD22 B ASN   A 1 20  ? 7.964  -1.830  6.532   0.44 17.66 ?  20  ASN   A HD22 1 
ATOM   583  N N    A ALA   A 1 21  ? 10.044 -1.692  9.269   0.56 16.45 ?  21  ALA   A N    1 
ATOM   584  N N    B ALA   A 1 21  ? 9.954  -1.914  9.051   0.44 16.56 ?  21  ALA   A N    1 
ATOM   585  C CA   A ALA   A 1 21  ? 10.769 -0.837  10.193  0.56 16.56 ?  21  ALA   A CA   1 
ATOM   586  C CA   B ALA   A 1 21  ? 10.584 -0.912  9.903   0.44 16.84 ?  21  ALA   A CA   1 
ATOM   587  C C    A ALA   A 1 21  ? 11.716 0.062   9.424   0.56 16.14 ?  21  ALA   A C    1 
ATOM   588  C C    B ALA   A 1 21  ? 11.653 -0.151  9.130   0.44 15.28 ?  21  ALA   A C    1 
ATOM   589  O O    A ALA   A 1 21  ? 12.184 -0.282  8.335   0.56 16.80 ?  21  ALA   A O    1 
ATOM   590  O O    B ALA   A 1 21  ? 12.159 -0.615  8.105   0.44 15.13 ?  21  ALA   A O    1 
ATOM   591  C CB   A ALA   A 1 21  ? 11.552 -1.666  11.212  0.56 17.20 ?  21  ALA   A CB   1 
ATOM   592  C CB   B ALA   A 1 21  ? 11.184 -1.541  11.166  0.44 18.14 ?  21  ALA   A CB   1 
ATOM   593  H H    A ALA   A 1 21  ? 10.398 -1.762  8.485   0.56 19.76 ?  21  ALA   A H    1 
ATOM   594  H H    B ALA   A 1 21  ? 10.439 -2.177  8.388   0.44 19.89 ?  21  ALA   A H    1 
ATOM   595  H HA   A ALA   A 1 21  ? 10.136 -0.276  10.670  0.56 19.90 ?  21  ALA   A HA   1 
ATOM   596  H HA   B ALA   A 1 21  ? 9.905  -0.282  10.185  0.44 20.23 ?  21  ALA   A HA   1 
ATOM   597  H HB1  A ALA   A 1 21  ? 11.958 -1.063  11.848  0.56 20.67 ?  21  ALA   A HB1  1 
ATOM   598  H HB1  B ALA   A 1 21  ? 11.587 -0.843  11.705  0.44 21.79 ?  21  ALA   A HB1  1 
ATOM   599  H HB2  A ALA   A 1 21  ? 10.932 -2.261  11.667  0.56 20.67 ?  21  ALA   A HB2  1 
ATOM   600  H HB2  B ALA   A 1 21  ? 10.479 -1.980  11.672  0.44 21.79 ?  21  ALA   A HB2  1 
ATOM   601  H HB3  A ALA   A 1 21  ? 12.225 -2.181  10.749  0.56 20.67 ?  21  ALA   A HB3  1 
ATOM   602  H HB3  B ALA   A 1 21  ? 11.857 -2.191  10.910  0.44 21.79 ?  21  ALA   A HB3  1 
ATOM   603  N N    A ASP   A 1 22  ? 11.969 1.227   10.011  0.56 16.02 ?  22  ASP   A N    1 
ATOM   604  N N    B ASP   A 1 22  ? 11.977 1.036   9.647   0.44 15.10 ?  22  ASP   A N    1 
ATOM   605  C CA   A ASP   A 1 22  ? 13.009 2.138   9.553   0.56 15.59 ?  22  ASP   A CA   1 
ATOM   606  C CA   B ASP   A 1 22  ? 13.098 1.833   9.162   0.44 14.83 ?  22  ASP   A CA   1 
ATOM   607  C C    A ASP   A 1 22  ? 14.340 1.650   10.115  0.56 14.88 ?  22  ASP   A C    1 
ATOM   608  C C    B ASP   A 1 22  ? 14.377 1.311   9.812   0.44 13.97 ?  22  ASP   A C    1 
ATOM   609  O O    A ASP   A 1 22  ? 14.542 1.650   11.334  0.56 16.04 ?  22  ASP   A O    1 
ATOM   610  O O    B ASP   A 1 22  ? 14.482 1.273   11.043  0.44 14.20 ?  22  ASP   A O    1 
ATOM   611  C CB   A ASP   A 1 22  ? 12.673 3.533   10.069  0.56 17.37 ?  22  ASP   A CB   1 
ATOM   612  C CB   B ASP   A 1 22  ? 12.868 3.297   9.535   0.44 15.98 ?  22  ASP   A CB   1 
ATOM   613  C CG   A ASP   A 1 22  ? 13.669 4.583   9.631   0.56 18.89 ?  22  ASP   A CG   1 
ATOM   614  C CG   B ASP   A 1 22  ? 13.899 4.238   8.925   0.44 17.21 ?  22  ASP   A CG   1 
ATOM   615  O OD1  A ASP   A 1 22  ? 14.787 4.238   9.210   0.56 18.91 ?  22  ASP   A OD1  1 
ATOM   616  O OD1  B ASP   A 1 22  ? 15.013 3.786   8.577   0.44 16.49 ?  22  ASP   A OD1  1 
ATOM   617  O OD2  A ASP   A 1 22  ? 13.327 5.778   9.716   0.56 20.08 -1 22  ASP   A OD2  1 
ATOM   618  O OD2  B ASP   A 1 22  ? 13.593 5.443   8.800   0.44 19.27 -1 22  ASP   A OD2  1 
ATOM   619  H H    A ASP   A 1 22  ? 11.519 1.529   10.683  0.56 19.25 ?  22  ASP   A H    1 
ATOM   620  H H    B ASP   A 1 22  ? 11.541 1.404   10.295  0.44 18.14 ?  22  ASP   A H    1 
ATOM   621  H HA   A ASP   A 1 22  ? 13.046 2.148   8.582   0.56 18.73 ?  22  ASP   A HA   1 
ATOM   622  H HA   B ASP   A 1 22  ? 13.165 1.750   8.198   0.44 17.82 ?  22  ASP   A HA   1 
ATOM   623  H HB2  A ASP   A 1 22  ? 11.801 3.795   9.733   0.56 20.87 ?  22  ASP   A HB2  1 
ATOM   624  H HB2  B ASP   A 1 22  ? 11.989 3.566   9.226   0.44 19.20 ?  22  ASP   A HB2  1 
ATOM   625  H HB3  A ASP   A 1 22  ? 12.658 3.513   11.040  0.56 20.87 ?  22  ASP   A HB3  1 
ATOM   626  H HB3  B ASP   A 1 22  ? 12.922 3.386   10.499  0.44 19.20 ?  22  ASP   A HB3  1 
ATOM   627  N N    A ILE   A 1 23  ? 15.245 1.227   9.226   0.56 14.57 ?  23  ILE   A N    1 
ATOM   628  N N    B ILE   A 1 23  ? 15.338 0.886   8.987   0.44 14.28 ?  23  ILE   A N    1 
ATOM   629  C CA   A ILE   A 1 23  ? 16.492 0.599   9.659   0.56 14.40 ?  23  ILE   A CA   1 
ATOM   630  C CA   B ILE   A 1 23  ? 16.571 0.293   9.501   0.44 13.93 ?  23  ILE   A CA   1 
ATOM   631  C C    A ILE   A 1 23  ? 17.298 1.535   10.551  0.56 14.56 ?  23  ILE   A C    1 
ATOM   632  C C    B ILE   A 1 23  ? 17.316 1.272   10.393  0.44 14.55 ?  23  ILE   A C    1 
ATOM   633  O O    A ILE   A 1 23  ? 17.998 1.083   11.464  0.56 15.57 ?  23  ILE   A O    1 
ATOM   634  O O    B ILE   A 1 23  ? 18.019 0.860   11.324  0.44 15.06 ?  23  ILE   A O    1 
ATOM   635  C CB   A ILE   A 1 23  ? 17.293 0.083   8.442   0.56 14.03 ?  23  ILE   A CB   1 
ATOM   636  C CB   B ILE   A 1 23  ? 17.462 -0.246  8.360   0.44 13.87 ?  23  ILE   A CB   1 
ATOM   637  C CG1  A ILE   A 1 23  ? 18.437 -0.831  8.895   0.56 13.89 ?  23  ILE   A CG1  1 
ATOM   638  C CG1  B ILE   A 1 23  ? 18.515 -1.195  8.937   0.44 13.57 ?  23  ILE   A CG1  1 
ATOM   639  C CG2  A ILE   A 1 23  ? 17.801 1.240   7.593   0.56 14.36 ?  23  ILE   A CG2  1 
ATOM   640  C CG2  B ILE   A 1 23  ? 18.120 0.895   7.591   0.44 14.59 ?  23  ILE   A CG2  1 
ATOM   641  C CD1  A ILE   A 1 23  ? 19.143 -1.544  7.757   0.56 14.63 ?  23  ILE   A CD1  1 
ATOM   642  C CD1  B ILE   A 1 23  ? 19.386 -1.845  7.908   0.44 13.89 ?  23  ILE   A CD1  1 
ATOM   643  H H    A ILE   A 1 23  ? 15.154 1.294   8.376   0.56 17.51 ?  23  ILE   A H    1 
ATOM   644  H H    B ILE   A 1 23  ? 15.298 0.924   8.144   0.44 17.16 ?  23  ILE   A H    1 
ATOM   645  H HA   A ILE   A 1 23  ? 16.264 -0.173  10.199  0.56 17.30 ?  23  ILE   A HA   1 
ATOM   646  H HA   B ILE   A 1 23  ? 16.327 -0.468  10.047  0.44 16.74 ?  23  ILE   A HA   1 
ATOM   647  H HB   A ILE   A 1 23  ? 16.688 -0.446  7.896   0.56 16.85 ?  23  ILE   A HB   1 
ATOM   648  H HB   B ILE   A 1 23  ? 16.905 -0.750  7.743   0.44 16.67 ?  23  ILE   A HB   1 
ATOM   649  H HG12 A ILE   A 1 23  ? 19.093 -0.296  9.367   0.56 16.69 ?  23  ILE   A HG12 1 
ATOM   650  H HG12 B ILE   A 1 23  ? 19.091 -0.696  9.537   0.44 16.30 ?  23  ILE   A HG12 1 
ATOM   651  H HG13 A ILE   A 1 23  ? 18.076 -1.508  9.492   0.56 16.69 ?  23  ILE   A HG13 1 
ATOM   652  H HG13 B ILE   A 1 23  ? 18.065 -1.902  9.428   0.44 16.30 ?  23  ILE   A HG13 1 
ATOM   653  H HG21 A ILE   A 1 23  ? 18.158 0.888   6.762   0.56 17.26 ?  23  ILE   A HG21 1 
ATOM   654  H HG21 B ILE   A 1 23  ? 18.480 0.549   6.757   0.44 17.54 ?  23  ILE   A HG21 1 
ATOM   655  H HG22 A ILE   A 1 23  ? 17.063 1.842   7.405   0.56 17.26 ?  23  ILE   A HG22 1 
ATOM   656  H HG22 B ILE   A 1 23  ? 17.456 1.575   7.407   0.44 17.54 ?  23  ILE   A HG22 1 
ATOM   657  H HG23 A ILE   A 1 23  ? 18.494 1.710   8.079   0.56 17.26 ?  23  ILE   A HG23 1 
ATOM   658  H HG23 B ILE   A 1 23  ? 18.837 1.268   8.128   0.44 17.54 ?  23  ILE   A HG23 1 
ATOM   659  H HD11 A ILE   A 1 23  ? 19.802 -2.151  8.128   0.56 17.58 ?  23  ILE   A HD11 1 
ATOM   660  H HD11 B ILE   A 1 23  ? 19.935 -2.516  8.342   0.44 16.69 ?  23  ILE   A HD11 1 
ATOM   661  H HD12 A ILE   A 1 23  ? 18.489 -2.038  7.240   0.56 17.58 ?  23  ILE   A HD12 1 
ATOM   662  H HD12 B ILE   A 1 23  ? 18.822 -2.257  7.239   0.44 16.69 ?  23  ILE   A HD12 1 
ATOM   663  H HD13 A ILE   A 1 23  ? 19.580 -0.884  7.196   0.56 17.58 ?  23  ILE   A HD13 1 
ATOM   664  H HD13 B ILE   A 1 23  ? 19.947 -1.167  7.501   0.44 16.69 ?  23  ILE   A HD13 1 
ATOM   665  N N    A VAL   A 1 24  ? 17.202 2.847   10.321  0.56 14.79 ?  24  VAL   A N    1 
ATOM   666  N N    B VAL   A 1 24  ? 17.177 2.574   10.132  0.44 15.64 ?  24  VAL   A N    1 
ATOM   667  C CA   A VAL   A 1 24  ? 17.878 3.805   11.195  0.56 16.12 ?  24  VAL   A CA   1 
ATOM   668  C CA   B VAL   A 1 24  ? 17.830 3.575   10.970  0.44 16.96 ?  24  VAL   A CA   1 
ATOM   669  C C    A VAL   A 1 24  ? 17.315 3.723   12.608  0.56 16.62 ?  24  VAL   A C    1 
ATOM   670  C C    B VAL   A 1 24  ? 17.267 3.531   12.384  0.44 18.01 ?  24  VAL   A C    1 
ATOM   671  O O    A VAL   A 1 24  ? 18.061 3.618   13.592  0.56 17.48 ?  24  VAL   A O    1 
ATOM   672  O O    B VAL   A 1 24  ? 18.016 3.568   13.368  0.44 18.96 ?  24  VAL   A O    1 
ATOM   673  C CB   A VAL   A 1 24  ? 17.760 5.228   10.623  0.56 16.52 ?  24  VAL   A CB   1 
ATOM   674  C CB   B VAL   A 1 24  ? 17.691 4.970   10.332  0.44 17.46 ?  24  VAL   A CB   1 
ATOM   675  C CG1  A VAL   A 1 24  ? 18.181 6.263   11.662  0.56 17.06 ?  24  VAL   A CG1  1 
ATOM   676  C CG1  B VAL   A 1 24  ? 18.400 6.015   11.173  0.44 18.63 ?  24  VAL   A CG1  1 
ATOM   677  C CG2  A VAL   A 1 24  ? 18.593 5.360   9.361   0.56 16.89 ?  24  VAL   A CG2  1 
ATOM   678  C CG2  B VAL   A 1 24  ? 18.228 4.956   8.908   0.44 17.04 ?  24  VAL   A CG2  1 
ATOM   679  H H    A VAL   A 1 24  ? 16.757 3.201   9.676   0.56 17.77 ?  24  VAL   A H    1 
ATOM   680  H H    B VAL   A 1 24  ? 16.709 2.897   9.491   0.44 18.79 ?  24  VAL   A H    1 
ATOM   681  H HA   A VAL   A 1 24  ? 18.819 3.580   11.236  0.56 19.37 ?  24  VAL   A HA   1 
ATOM   682  H HA   B VAL   A 1 24  ? 18.774 3.369   11.026  0.44 20.38 ?  24  VAL   A HA   1 
ATOM   683  H HB   A VAL   A 1 24  ? 16.835 5.400   10.386  0.56 19.85 ?  24  VAL   A HB   1 
ATOM   684  H HB   B VAL   A 1 24  ? 16.751 5.208   10.293  0.44 20.97 ?  24  VAL   A HB   1 
ATOM   685  H HG11 A VAL   A 1 24  ? 18.372 7.099   11.211  0.56 20.50 ?  24  VAL   A HG11 1 
ATOM   686  H HG11 B VAL   A 1 24  ? 18.769 6.694   10.589  0.44 22.38 ?  24  VAL   A HG11 1 
ATOM   687  H HG12 A VAL   A 1 24  ? 17.458 6.386   12.295  0.56 20.50 ?  24  VAL   A HG12 1 
ATOM   688  H HG12 B VAL   A 1 24  ? 17.755 6.413   11.777  0.44 22.38 ?  24  VAL   A HG12 1 
ATOM   689  H HG13 A VAL   A 1 24  ? 18.976 5.944   12.118  0.56 20.50 ?  24  VAL   A HG13 1 
ATOM   690  H HG13 B VAL   A 1 24  ? 19.113 5.588   11.675  0.44 22.38 ?  24  VAL   A HG13 1 
ATOM   691  H HG21 A VAL   A 1 24  ? 18.347 6.181   8.902   0.56 20.28 ?  24  VAL   A HG21 1 
ATOM   692  H HG21 B VAL   A 1 24  ? 18.236 5.861   8.564   0.44 20.47 ?  24  VAL   A HG21 1 
ATOM   693  H HG22 A VAL   A 1 24  ? 19.533 5.390   9.603   0.56 20.28 ?  24  VAL   A HG22 1 
ATOM   694  H HG22 B VAL   A 1 24  ? 19.129 4.596   8.915   0.44 20.47 ?  24  VAL   A HG22 1 
ATOM   695  H HG23 A VAL   A 1 24  ? 18.423 4.599   8.783   0.56 20.28 ?  24  VAL   A HG23 1 
ATOM   696  H HG23 B VAL   A 1 24  ? 17.655 4.398   8.358   0.44 20.47 ?  24  VAL   A HG23 1 
ATOM   697  N N    A GLU   A 1 25  ? 15.988 3.800   12.731  0.56 16.92 ?  25  GLU   A N    1 
ATOM   698  N N    B GLU   A 1 25  ? 15.941 3.436   12.510  0.44 18.69 ?  25  GLU   A N    1 
ATOM   699  C CA   A GLU   A 1 25  ? 15.368 3.730   14.049  0.56 18.65 ?  25  GLU   A CA   1 
ATOM   700  C CA   B GLU   A 1 25  ? 15.329 3.377   13.834  0.44 19.83 ?  25  GLU   A CA   1 
ATOM   701  C C    A GLU   A 1 25  ? 15.586 2.365   14.689  0.56 17.32 ?  25  GLU   A C    1 
ATOM   702  C C    B GLU   A 1 25  ? 15.589 2.034   14.506  0.44 18.99 ?  25  GLU   A C    1 
ATOM   703  O O    A GLU   A 1 25  ? 15.796 2.272   15.904  0.56 18.02 ?  25  GLU   A O    1 
ATOM   704  O O    B GLU   A 1 25  ? 15.809 1.974   15.721  0.44 19.73 ?  25  GLU   A O    1 
ATOM   705  C CB   A GLU   A 1 25  ? 13.884 4.088   13.952  0.56 21.21 ?  25  GLU   A CB   1 
ATOM   706  C CB   B GLU   A 1 25  ? 13.832 3.684   13.741  0.44 21.66 ?  25  GLU   A CB   1 
ATOM   707  C CG   A GLU   A 1 25  ? 13.641 5.559   13.615  0.56 24.44 ?  25  GLU   A CG   1 
ATOM   708  C CG   B GLU   A 1 25  ? 13.535 5.086   13.217  0.44 24.65 ?  25  GLU   A CG   1 
ATOM   709  C CD   A GLU   A 1 25  ? 14.412 6.509   14.519  0.56 27.26 ?  25  GLU   A CD   1 
ATOM   710  C CD   B GLU   A 1 25  ? 14.298 6.163   13.956  0.44 27.35 ?  25  GLU   A CD   1 
ATOM   711  O OE1  A GLU   A 1 25  ? 14.382 6.316   15.755  0.56 28.44 ?  25  GLU   A OE1  1 
ATOM   712  O OE1  B GLU   A 1 25  ? 14.489 6.025   15.183  0.44 28.64 ?  25  GLU   A OE1  1 
ATOM   713  O OE2  A GLU   A 1 25  ? 15.067 7.432   13.992  0.56 28.55 -1 25  GLU   A OE2  1 
ATOM   714  O OE2  B GLU   A 1 25  ? 14.723 7.141   13.305  0.44 28.35 -1 25  GLU   A OE2  1 
ATOM   715  H H    A GLU   A 1 25  ? 15.437 3.905   12.075  0.56 20.33 ?  25  GLU   A H    1 
ATOM   716  H H    B GLU   A 1 25  ? 15.386 3.397   11.853  0.44 22.46 ?  25  GLU   A H    1 
ATOM   717  H HA   A GLU   A 1 25  ? 15.795 4.382   14.623  0.56 22.40 ?  25  GLU   A HA   1 
ATOM   718  H HA   B GLU   A 1 25  ? 15.736 4.053   14.390  0.44 23.81 ?  25  GLU   A HA   1 
ATOM   719  H HB2  A GLU   A 1 25  ? 13.471 3.555   13.252  0.56 25.48 ?  25  GLU   A HB2  1 
ATOM   720  H HB2  B GLU   A 1 25  ? 13.413 3.052   13.138  0.44 26.02 ?  25  GLU   A HB2  1 
ATOM   721  H HB3  A GLU   A 1 25  ? 13.455 3.906   14.801  0.56 25.48 ?  25  GLU   A HB3  1 
ATOM   722  H HB3  B GLU   A 1 25  ? 13.438 3.609   14.625  0.44 26.02 ?  25  GLU   A HB3  1 
ATOM   723  H HG2  A GLU   A 1 25  ? 13.919 5.722   12.701  0.56 29.35 ?  25  GLU   A HG2  1 
ATOM   724  H HG2  B GLU   A 1 25  ? 13.792 5.139   12.286  0.44 29.60 ?  25  GLU   A HG2  1 
ATOM   725  H HG3  A GLU   A 1 25  ? 12.695 5.752   13.715  0.56 29.35 ?  25  GLU   A HG3  1 
ATOM   726  H HG3  B GLU   A 1 25  ? 12.589 5.270   13.315  0.44 29.60 ?  25  GLU   A HG3  1 
ATOM   727  N N    A GLU   A 1 26  ? 15.561 1.296   13.887  0.56 17.26 ?  26  GLU   A N    1 
ATOM   728  N N    B GLU   A 1 26  ? 15.588 0.946   13.732  0.44 18.15 ?  26  GLU   A N    1 
ATOM   729  C CA   A GLU   A 1 26  ? 15.863 -0.031  14.418  0.56 16.86 ?  26  GLU   A CA   1 
ATOM   730  C CA   B GLU   A 1 26  ? 15.927 -0.355  14.299  0.44 17.83 ?  26  GLU   A CA   1 
ATOM   731  C C    A GLU   A 1 26  ? 17.279 -0.082  14.979  0.56 16.57 ?  26  GLU   A C    1 
ATOM   732  C C    B GLU   A 1 26  ? 17.347 -0.361  14.846  0.44 17.06 ?  26  GLU   A C    1 
ATOM   733  O O    A GLU   A 1 26  ? 17.495 -0.513  16.118  0.56 16.57 ?  26  GLU   A O    1 
ATOM   734  O O    B GLU   A 1 26  ? 17.624 -0.992  15.872  0.44 16.72 ?  26  GLU   A O    1 
ATOM   735  C CB   A GLU   A 1 26  ? 15.696 -1.091  13.326  0.56 18.35 ?  26  GLU   A CB   1 
ATOM   736  C CB   B GLU   A 1 26  ? 15.760 -1.448  13.243  0.44 18.68 ?  26  GLU   A CB   1 
ATOM   737  C CG   A GLU   A 1 26  ? 14.308 -1.685  13.197  0.56 21.51 ?  26  GLU   A CG   1 
ATOM   738  C CG   B GLU   A 1 26  ? 14.324 -1.801  12.942  0.44 19.82 ?  26  GLU   A CG   1 
ATOM   739  C CD   A GLU   A 1 26  ? 13.932 -2.582  14.371  0.56 23.29 ?  26  GLU   A CD   1 
ATOM   740  C CD   B GLU   A 1 26  ? 13.598 -2.323  14.152  0.44 20.01 ?  26  GLU   A CD   1 
ATOM   741  O OE1  A GLU   A 1 26  ? 14.325 -3.771  14.402  0.56 23.50 ?  26  GLU   A OE1  1 
ATOM   742  O OE1  B GLU   A 1 26  ? 14.141 -3.208  14.846  0.44 20.19 ?  26  GLU   A OE1  1 
ATOM   743  O OE2  A GLU   A 1 26  ? 13.241 -2.087  15.273  0.56 23.74 -1 26  GLU   A OE2  1 
ATOM   744  O OE2  B GLU   A 1 26  ? 12.492 -1.823  14.414  0.44 18.73 -1 26  GLU   A OE2  1 
ATOM   745  H H    A GLU   A 1 26  ? 15.371 1.320   13.046  0.56 20.74 ?  26  GLU   A H    1 
ATOM   746  H H    B GLU   A 1 26  ? 15.398 0.934   12.895  0.44 21.80 ?  26  GLU   A H    1 
ATOM   747  H HA   A GLU   A 1 26  ? 15.242 -0.228  15.133  0.56 20.26 ?  26  GLU   A HA   1 
ATOM   748  H HA   B GLU   A 1 26  ? 15.329 -0.549  15.035  0.44 21.42 ?  26  GLU   A HA   1 
ATOM   749  H HB2  A GLU   A 1 26  ? 15.924 -0.689  12.471  0.56 22.05 ?  26  GLU   A HB2  1 
ATOM   750  H HB2  B GLU   A 1 26  ? 16.168 -1.149  12.413  0.44 22.43 ?  26  GLU   A HB2  1 
ATOM   751  H HB3  A GLU   A 1 26  ? 16.310 -1.816  13.515  0.56 22.05 ?  26  GLU   A HB3  1 
ATOM   752  H HB3  B GLU   A 1 26  ? 16.206 -2.255  13.551  0.44 22.43 ?  26  GLU   A HB3  1 
ATOM   753  H HG2  A GLU   A 1 26  ? 13.671 -0.954  13.137  0.56 25.84 ?  26  GLU   A HG2  1 
ATOM   754  H HG2  B GLU   A 1 26  ? 13.854 -1.007  12.644  0.44 23.80 ?  26  GLU   A HG2  1 
ATOM   755  H HG3  A GLU   A 1 26  ? 14.269 -2.224  12.393  0.56 25.84 ?  26  GLU   A HG3  1 
ATOM   756  H HG3  B GLU   A 1 26  ? 14.293 -2.487  12.262  0.44 23.80 ?  26  GLU   A HG3  1 
ATOM   757  N N    . ALA   A 1 27  ? 18.263 0.345   14.180  1.00 16.10 ?  27  ALA   A N    1 
ATOM   758  C CA   . ALA   A 1 27  ? 19.647 0.342   14.635  1.00 16.58 ?  27  ALA   A CA   1 
ATOM   759  C C    . ALA   A 1 27  ? 19.809 1.153   15.913  1.00 18.46 ?  27  ALA   A C    1 
ATOM   760  O O    . ALA   A 1 27  ? 20.479 0.711   16.854  1.00 18.88 ?  27  ALA   A O    1 
ATOM   761  C CB   . ALA   A 1 27  ? 20.562 0.875   13.532  1.00 15.75 ?  27  ALA   A CB   1 
ATOM   762  H H    A ALA   A 1 27  ? 18.151 0.630   13.373  0.56 19.34 ?  27  ALA   A H    1 
ATOM   763  H H    B ALA   A 1 27  ? 18.107 0.824   13.479  0.44 19.34 ?  27  ALA   A H    1 
ATOM   764  H HA   . ALA   A 1 27  ? 19.910 -0.569  14.821  1.00 19.92 ?  27  ALA   A HA   1 
ATOM   765  H HB1  . ALA   A 1 27  ? 21.480 0.864   13.848  1.00 18.92 ?  27  ALA   A HB1  1 
ATOM   766  H HB2  . ALA   A 1 27  ? 20.481 0.305   12.746  1.00 18.92 ?  27  ALA   A HB2  1 
ATOM   767  H HB3  . ALA   A 1 27  ? 20.301 1.781   13.305  1.00 18.92 ?  27  ALA   A HB3  1 
ATOM   768  N N    A LYS   A 1 28  ? 19.195 2.336   15.982  0.56 20.10 ?  28  LYS   A N    1 
ATOM   769  N N    B LYS   A 1 28  ? 19.196 2.340   15.966  0.44 19.58 ?  28  LYS   A N    1 
ATOM   770  C CA   A LYS   A 1 28  ? 19.356 3.158   17.177  0.56 22.41 ?  28  LYS   A CA   1 
ATOM   771  C CA   B LYS   A 1 28  ? 19.278 3.165   17.167  0.44 21.39 ?  28  LYS   A CA   1 
ATOM   772  C C    A LYS   A 1 28  ? 18.767 2.500   18.416  0.56 23.85 ?  28  LYS   A C    1 
ATOM   773  C C    B LYS   A 1 28  ? 18.727 2.422   18.375  0.44 22.79 ?  28  LYS   A C    1 
ATOM   774  O O    A LYS   A 1 28  ? 19.193 2.817   19.532  0.56 24.88 ?  28  LYS   A O    1 
ATOM   775  O O    B LYS   A 1 28  ? 19.303 2.484   19.467  0.44 23.55 ?  28  LYS   A O    1 
ATOM   776  C CB   A LYS   A 1 28  ? 18.751 4.546   16.969  0.56 24.30 ?  28  LYS   A CB   1 
ATOM   777  C CB   B LYS   A 1 28  ? 18.528 4.484   16.956  0.44 22.60 ?  28  LYS   A CB   1 
ATOM   778  C CG   A LYS   A 1 28  ? 19.623 5.454   16.122  0.56 25.78 ?  28  LYS   A CG   1 
ATOM   779  C CG   B LYS   A 1 28  ? 19.050 5.340   15.812  0.44 23.90 ?  28  LYS   A CG   1 
ATOM   780  C CD   A LYS   A 1 28  ? 19.139 6.893   16.153  0.56 27.42 ?  28  LYS   A CD   1 
ATOM   781  C CD   B LYS   A 1 28  ? 18.373 6.703   15.796  0.44 25.47 ?  28  LYS   A CD   1 
ATOM   782  C CE   A LYS   A 1 28  ? 17.800 7.039   15.459  0.56 28.72 ?  28  LYS   A CE   1 
ATOM   783  C CE   B LYS   A 1 28  ? 18.625 7.443   14.490  0.44 26.48 ?  28  LYS   A CE   1 
ATOM   784  N NZ   A LYS   A 1 28  ? 17.389 8.465   15.368  0.56 29.37 ?  28  LYS   A NZ   1 
ATOM   785  N NZ   B LYS   A 1 28  ? 18.207 8.875   14.559  0.44 27.14 ?  28  LYS   A NZ   1 
ATOM   786  H H    A LYS   A 1 28  ? 18.696 2.674   15.371  0.56 24.14 ?  28  LYS   A H    1 
ATOM   787  H H    B LYS   A 1 28  ? 18.731 2.682   15.331  0.44 23.52 ?  28  LYS   A H    1 
ATOM   788  H HA   A LYS   A 1 28  ? 20.305 3.278   17.337  0.56 26.92 ?  28  LYS   A HA   1 
ATOM   789  H HA   B LYS   A 1 28  ? 20.204 3.376   17.353  0.44 25.69 ?  28  LYS   A HA   1 
ATOM   790  H HB2  A LYS   A 1 28  ? 17.896 4.452   16.524  0.56 29.18 ?  28  LYS   A HB2  1 
ATOM   791  H HB2  B LYS   A 1 28  ? 17.598 4.291   16.767  0.44 27.15 ?  28  LYS   A HB2  1 
ATOM   792  H HB3  A LYS   A 1 28  ? 18.630 4.970   17.834  0.56 29.18 ?  28  LYS   A HB3  1 
ATOM   793  H HB3  B LYS   A 1 28  ? 18.596 5.018   17.762  0.44 27.15 ?  28  LYS   A HB3  1 
ATOM   794  H HG2  A LYS   A 1 28  ? 20.531 5.433   16.462  0.56 30.96 ?  28  LYS   A HG2  1 
ATOM   795  H HG2  B LYS   A 1 28  ? 20.003 5.477   15.920  0.44 28.71 ?  28  LYS   A HG2  1 
ATOM   796  H HG3  A LYS   A 1 28  ? 19.602 5.147   15.202  0.56 30.96 ?  28  LYS   A HG3  1 
ATOM   797  H HG3  B LYS   A 1 28  ? 18.871 4.903   14.967  0.44 28.71 ?  28  LYS   A HG3  1 
ATOM   798  H HD2  A LYS   A 1 28  ? 19.037 7.177   17.075  0.56 32.92 ?  28  LYS   A HD2  1 
ATOM   799  H HD2  B LYS   A 1 28  ? 17.415 6.587   15.898  0.44 30.58 ?  28  LYS   A HD2  1 
ATOM   800  H HD3  A LYS   A 1 28  ? 19.782 7.458   15.696  0.56 32.92 ?  28  LYS   A HD3  1 
ATOM   801  H HD3  B LYS   A 1 28  ? 18.724 7.243   16.521  0.44 30.58 ?  28  LYS   A HD3  1 
ATOM   802  H HE2  A LYS   A 1 28  ? 17.866 6.682   14.559  0.56 34.49 ?  28  LYS   A HE2  1 
ATOM   803  H HE2  B LYS   A 1 28  ? 19.571 7.411   14.280  0.44 31.80 ?  28  LYS   A HE2  1 
ATOM   804  H HE3  A LYS   A 1 28  ? 17.124 6.559   15.962  0.56 34.49 ?  28  LYS   A HE3  1 
ATOM   805  H HE3  B LYS   A 1 28  ? 18.112 7.016   13.786  0.44 31.80 ?  28  LYS   A HE3  1 
ATOM   806  H HZ1  A LYS   A 1 28  ? 16.603 8.529   14.958  0.56 35.26 ?  28  LYS   A HZ1  1 
ATOM   807  H HZ1  B LYS   A 1 28  ? 18.367 9.277   13.781  0.44 32.58 ?  28  LYS   A HZ1  1 
ATOM   808  H HZ2  A LYS   A 1 28  ? 17.320 8.814   16.184  0.56 35.26 ?  28  LYS   A HZ2  1 
ATOM   809  H HZ2  B LYS   A 1 28  ? 17.337 8.930   14.739  0.44 32.58 ?  28  LYS   A HZ2  1 
ATOM   810  H HZ3  A LYS   A 1 28  ? 17.995 8.927   14.907  0.56 35.26 ?  28  LYS   A HZ3  1 
ATOM   811  H HZ3  B LYS   A 1 28  ? 18.662 9.293   15.200  0.44 32.58 ?  28  LYS   A HZ3  1 
ATOM   812  N N    A LYS   A 1 29  ? 17.800 1.596   18.249  0.56 24.52 ?  29  LYS   A N    1 
ATOM   813  N N    B LYS   A 1 29  ? 17.625 1.693   18.193  0.44 23.67 ?  29  LYS   A N    1 
ATOM   814  C CA   A LYS   A 1 29  ? 17.216 0.892   19.388  0.56 25.96 ?  29  LYS   A CA   1 
ATOM   815  C CA   B LYS   A 1 29  ? 16.973 1.023   19.314  0.44 24.97 ?  29  LYS   A CA   1 
ATOM   816  C C    A LYS   A 1 29  ? 18.047 -0.327  19.781  0.56 25.12 ?  29  LYS   A C    1 
ATOM   817  C C    B LYS   A 1 29  ? 17.733 -0.230  19.731  0.44 24.37 ?  29  LYS   A C    1 
ATOM   818  O O    A LYS   A 1 29  ? 18.394 -0.500  20.955  0.56 26.35 ?  29  LYS   A O    1 
ATOM   819  O O    B LYS   A 1 29  ? 17.946 -0.467  20.926  0.44 24.79 ?  29  LYS   A O    1 
ATOM   820  C CB   A LYS   A 1 29  ? 15.784 0.471   19.052  0.56 28.56 ?  29  LYS   A CB   1 
ATOM   821  C CB   B LYS   A 1 29  ? 15.539 0.657   18.933  0.44 27.22 ?  29  LYS   A CB   1 
ATOM   822  C CG   A LYS   A 1 29  ? 15.051 -0.236  20.184  0.56 31.25 ?  29  LYS   A CG   1 
ATOM   823  C CG   B LYS   A 1 29  ? 14.737 0.015   20.055  0.44 29.47 ?  29  LYS   A CG   1 
ATOM   824  C CD   A LYS   A 1 29  ? 14.705 0.728   21.306  0.56 33.54 ?  29  LYS   A CD   1 
ATOM   825  C CD   B LYS   A 1 29  ? 14.473 0.999   21.181  0.44 31.43 ?  29  LYS   A CD   1 
ATOM   826  C CE   A LYS   A 1 29  ? 13.825 0.062   22.353  0.56 35.04 ?  29  LYS   A CE   1 
ATOM   827  C CE   B LYS   A 1 29  ? 13.590 0.386   22.254  0.44 32.79 ?  29  LYS   A CE   1 
ATOM   828  N NZ   A LYS   A 1 29  ? 13.410 1.015   23.418  0.56 35.81 ?  29  LYS   A NZ   1 
ATOM   829  N NZ   B LYS   A 1 29  ? 13.324 1.348   23.356  0.44 33.57 ?  29  LYS   A NZ   1 
ATOM   830  H H    A LYS   A 1 29  ? 17.455 1.388   17.490  0.56 29.45 ?  29  LYS   A H    1 
ATOM   831  H H    B LYS   A 1 29  ? 17.243 1.562   17.432  0.44 28.43 ?  29  LYS   A H    1 
ATOM   832  H HA   A LYS   A 1 29  ? 17.181 1.492   20.148  0.56 31.17 ?  29  LYS   A HA   1 
ATOM   833  H HA   B LYS   A 1 29  ? 16.944 1.626   20.073  0.44 29.98 ?  29  LYS   A HA   1 
ATOM   834  H HB2  A LYS   A 1 29  ? 15.272 1.264   18.825  0.56 34.29 ?  29  LYS   A HB2  1 
ATOM   835  H HB2  B LYS   A 1 29  ? 15.074 1.462   18.665  0.44 32.68 ?  29  LYS   A HB2  1 
ATOM   836  H HB3  A LYS   A 1 29  ? 15.805 -0.133  18.295  0.56 34.29 ?  29  LYS   A HB3  1 
ATOM   837  H HB3  B LYS   A 1 29  ? 15.565 0.028   18.196  0.44 32.68 ?  29  LYS   A HB3  1 
ATOM   838  H HG2  A LYS   A 1 29  ? 14.225 -0.611  19.843  0.56 37.52 ?  29  LYS   A HG2  1 
ATOM   839  H HG2  B LYS   A 1 29  ? 13.883 -0.281  19.705  0.44 35.39 ?  29  LYS   A HG2  1 
ATOM   840  H HG3  A LYS   A 1 29  ? 15.610 -0.941  20.550  0.56 37.52 ?  29  LYS   A HG3  1 
ATOM   841  H HG3  B LYS   A 1 29  ? 15.228 -0.740  20.418  0.44 35.39 ?  29  LYS   A HG3  1 
ATOM   842  H HD2  A LYS   A 1 29  ? 15.521 1.025   21.738  0.56 40.27 ?  29  LYS   A HD2  1 
ATOM   843  H HD2  B LYS   A 1 29  ? 15.315 1.253   21.590  0.44 37.73 ?  29  LYS   A HD2  1 
ATOM   844  H HD3  A LYS   A 1 29  ? 14.223 1.486   20.940  0.56 40.27 ?  29  LYS   A HD3  1 
ATOM   845  H HD3  B LYS   A 1 29  ? 14.023 1.780   20.824  0.44 37.73 ?  29  LYS   A HD3  1 
ATOM   846  H HE2  A LYS   A 1 29  ? 13.025 -0.282  21.925  0.56 42.07 ?  29  LYS   A HE2  1 
ATOM   847  H HE2  B LYS   A 1 29  ? 12.740 0.130   21.861  0.44 39.37 ?  29  LYS   A HE2  1 
ATOM   848  H HE3  A LYS   A 1 29  ? 14.318 -0.662  22.770  0.56 42.07 ?  29  LYS   A HE3  1 
ATOM   849  H HE3  B LYS   A 1 29  ? 14.034 -0.392  22.628  0.44 39.37 ?  29  LYS   A HE3  1 
ATOM   850  H HZ1  A LYS   A 1 29  ? 12.897 0.599   24.015  0.56 42.99 ?  29  LYS   A HZ1  1 
ATOM   851  H HZ1  B LYS   A 1 29  ? 12.806 0.969   23.972  0.44 40.31 ?  29  LYS   A HZ1  1 
ATOM   852  H HZ2  A LYS   A 1 29  ? 14.127 1.342   23.831  0.56 42.99 ?  29  LYS   A HZ2  1 
ATOM   853  H HZ2  B LYS   A 1 29  ? 14.090 1.595   23.735  0.44 40.31 ?  29  LYS   A HZ2  1 
ATOM   854  H HZ3  A LYS   A 1 29  ? 12.949 1.688   23.061  0.56 42.99 ?  29  LYS   A HZ3  1 
ATOM   855  H HZ3  B LYS   A 1 29  ? 12.913 2.070   23.037  0.44 40.31 ?  29  LYS   A HZ3  1 
ATOM   856  N N    A VAL   A 1 30  ? 18.362 -1.187  18.812  0.56 24.29 ?  30  VAL   A N    1 
ATOM   857  N N    B VAL   A 1 30  ? 18.124 -1.055  18.759  0.44 24.14 ?  30  VAL   A N    1 
ATOM   858  C CA   A VAL   A 1 30  ? 19.008 -2.462  19.110  0.56 23.78 ?  30  VAL   A CA   1 
ATOM   859  C CA   B VAL   A 1 30  ? 18.778 -2.320  19.075  0.44 23.76 ?  30  VAL   A CA   1 
ATOM   860  C C    A VAL   A 1 30  ? 20.510 -2.303  19.328  0.56 22.39 ?  30  VAL   A C    1 
ATOM   861  C C    B VAL   A 1 30  ? 20.270 -2.131  19.318  0.44 23.17 ?  30  VAL   A C    1 
ATOM   862  O O    A VAL   A 1 30  ? 21.102 -3.030  20.132  0.56 22.83 ?  30  VAL   A O    1 
ATOM   863  O O    B VAL   A 1 30  ? 20.861 -2.837  20.142  0.44 23.43 ?  30  VAL   A O    1 
ATOM   864  C CB   A VAL   A 1 30  ? 18.710 -3.471  17.985  0.56 24.49 ?  30  VAL   A CB   1 
ATOM   865  C CB   B VAL   A 1 30  ? 18.517 -3.336  17.948  0.44 24.13 ?  30  VAL   A CB   1 
ATOM   866  C CG1  A VAL   A 1 30  ? 19.505 -4.760  18.183  0.56 25.35 ?  30  VAL   A CG1  1 
ATOM   867  C CG1  B VAL   A 1 30  ? 19.280 -4.629  18.200  0.44 24.80 ?  30  VAL   A CG1  1 
ATOM   868  C CG2  A VAL   A 1 30  ? 17.219 -3.764  17.912  0.56 24.77 ?  30  VAL   A CG2  1 
ATOM   869  C CG2  B VAL   A 1 30  ? 17.026 -3.608  17.814  0.44 24.14 ?  30  VAL   A CG2  1 
ATOM   870  H H    A VAL   A 1 30  ? 18.205 -1.058  17.979  0.56 29.17 ?  30  VAL   A H    1 
ATOM   871  H H    B VAL   A 1 30  ? 18.011 -0.912  17.918  0.44 28.99 ?  30  VAL   A H    1 
ATOM   872  H HA   A VAL   A 1 30  ? 18.624 -2.818  19.927  0.56 28.55 ?  30  VAL   A HA   1 
ATOM   873  H HA   B VAL   A 1 30  ? 18.383 -2.675  19.885  0.44 28.53 ?  30  VAL   A HA   1 
ATOM   874  H HB   A VAL   A 1 30  ? 18.982 -3.086  17.137  0.56 29.42 ?  30  VAL   A HB   1 
ATOM   875  H HB   B VAL   A 1 30  ? 18.832 -2.966  17.109  0.44 28.98 ?  30  VAL   A HB   1 
ATOM   876  H HG11 A VAL   A 1 30  ? 19.136 -5.449  17.606  0.56 30.44 ?  30  VAL   A HG11 1 
ATOM   877  H HG11 B VAL   A 1 30  ? 18.890 -5.336  17.661  0.44 29.78 ?  30  VAL   A HG11 1 
ATOM   878  H HG12 A VAL   A 1 30  ? 20.434 -4.604  17.953  0.56 30.44 ?  30  VAL   A HG12 1 
ATOM   879  H HG12 B VAL   A 1 30  ? 20.210 -4.503  17.956  0.44 29.78 ?  30  VAL   A HG12 1 
ATOM   880  H HG13 A VAL   A 1 30  ? 19.433 -5.037  19.110  0.56 30.44 ?  30  VAL   A HG13 1 
ATOM   881  H HG13 B VAL   A 1 30  ? 19.212 -4.855  19.139  0.44 29.78 ?  30  VAL   A HG13 1 
ATOM   882  H HG21 A VAL   A 1 30  ? 17.061 -4.424  17.218  0.56 29.75 ?  30  VAL   A HG21 1 
ATOM   883  H HG21 B VAL   A 1 30  ? 16.889 -4.280  17.128  0.44 28.99 ?  30  VAL   A HG21 1 
ATOM   884  H HG22 A VAL   A 1 30  ? 16.924 -4.109  18.769  0.56 29.75 ?  30  VAL   A HG22 1 
ATOM   885  H HG22 B VAL   A 1 30  ? 16.687 -3.930  18.664  0.44 28.99 ?  30  VAL   A HG22 1 
ATOM   886  H HG23 A VAL   A 1 30  ? 16.747 -2.944  17.703  0.56 29.75 ?  30  VAL   A HG23 1 
ATOM   887  H HG23 B VAL   A 1 30  ? 16.577 -2.786  17.567  0.44 28.99 ?  30  VAL   A HG23 1 
ATOM   888  N N    A LYS   A 1 31  ? 21.148 -1.375  18.622  0.56 21.13 ?  31  LYS   A N    1 
ATOM   889  N N    B LYS   A 1 31  ? 20.895 -1.185  18.625  0.44 22.93 ?  31  LYS   A N    1 
ATOM   890  C CA   A LYS   A 1 31  ? 22.602 -1.270  18.577  0.56 21.70 ?  31  LYS   A CA   1 
ATOM   891  C CA   B LYS   A 1 31  ? 22.346 -1.051  18.592  0.44 23.34 ?  31  LYS   A CA   1 
ATOM   892  C C    A LYS   A 1 31  ? 23.229 -2.626  18.236  0.56 19.05 ?  31  LYS   A C    1 
ATOM   893  C C    B LYS   A 1 31  ? 22.991 -2.407  18.296  0.44 21.29 ?  31  LYS   A C    1 
ATOM   894  O O    A LYS   A 1 31  ? 24.013 -3.170  19.021  0.56 20.08 ?  31  LYS   A O    1 
ATOM   895  O O    B LYS   A 1 31  ? 23.759 -2.928  19.110  0.44 22.01 ?  31  LYS   A O    1 
ATOM   896  C CB   A LYS   A 1 31  ? 23.178 -0.710  19.870  0.56 25.95 ?  31  LYS   A CB   1 
ATOM   897  C CB   B LYS   A 1 31  ? 22.894 -0.455  19.881  0.44 26.46 ?  31  LYS   A CB   1 
ATOM   898  C CG   A LYS   A 1 31  ? 22.509 0.566   20.353  0.56 30.54 ?  31  LYS   A CG   1 
ATOM   899  C CG   B LYS   A 1 31  ? 22.203 0.824   20.310  0.44 29.92 ?  31  LYS   A CG   1 
ATOM   900  C CD   A LYS   A 1 31  ? 23.531 1.610   20.781  0.56 34.12 ?  31  LYS   A CD   1 
ATOM   901  C CD   B LYS   A 1 31  ? 23.212 1.856   20.777  0.44 32.74 ?  31  LYS   A CD   1 
ATOM   902  C CE   A LYS   A 1 31  ? 22.902 2.673   21.672  0.56 36.68 ?  31  LYS   A CE   1 
ATOM   903  C CE   B LYS   A 1 31  ? 22.552 2.946   21.599  0.44 34.85 ?  31  LYS   A CE   1 
ATOM   904  N NZ   A LYS   A 1 31  ? 21.708 3.317   21.057  0.56 37.96 ?  31  LYS   A NZ   1 
ATOM   905  N NZ   B LYS   A 1 31  ? 21.309 3.471   20.969  0.44 36.03 ?  31  LYS   A NZ   1 
ATOM   906  H H    A LYS   A 1 31  ? 20.746 -0.786  18.142  0.56 25.38 ?  31  LYS   A H    1 
ATOM   907  H H    B LYS   A 1 31  ? 20.484 -0.598  18.153  0.44 27.54 ?  31  LYS   A H    1 
ATOM   908  H HA   A LYS   A 1 31  ? 22.837 -0.657  17.867  0.56 26.06 ?  31  LYS   A HA   1 
ATOM   909  H HA   B LYS   A 1 31  ? 22.575 -0.449  17.873  0.44 28.03 ?  31  LYS   A HA   1 
ATOM   910  H HB2  A LYS   A 1 31  ? 23.086 -1.377  20.565  0.56 31.16 ?  31  LYS   A HB2  1 
ATOM   911  H HB2  B LYS   A 1 31  ? 22.788 -1.101  20.593  0.44 31.77 ?  31  LYS   A HB2  1 
ATOM   912  H HB3  A LYS   A 1 31  ? 24.119 -0.513  19.727  0.56 31.16 ?  31  LYS   A HB3  1 
ATOM   913  H HB3  B LYS   A 1 31  ? 23.837 -0.256  19.754  0.44 31.77 ?  31  LYS   A HB3  1 
ATOM   914  H HG2  A LYS   A 1 31  ? 21.975 0.941   19.636  0.56 36.67 ?  31  LYS   A HG2  1 
ATOM   915  H HG2  B LYS   A 1 31  ? 21.713 1.194   19.559  0.44 35.93 ?  31  LYS   A HG2  1 
ATOM   916  H HG3  A LYS   A 1 31  ? 21.947 0.363   21.118  0.56 36.67 ?  31  LYS   A HG3  1 
ATOM   917  H HG3  B LYS   A 1 31  ? 21.600 0.632   21.045  0.44 35.93 ?  31  LYS   A HG3  1 
ATOM   918  H HD2  A LYS   A 1 31  ? 24.243 1.178   21.279  0.56 40.97 ?  31  LYS   A HD2  1 
ATOM   919  H HD2  B LYS   A 1 31  ? 23.882 1.420   21.328  0.44 39.31 ?  31  LYS   A HD2  1 
ATOM   920  H HD3  A LYS   A 1 31  ? 23.891 2.047   19.992  0.56 40.97 ?  31  LYS   A HD3  1 
ATOM   921  H HD3  B LYS   A 1 31  ? 23.630 2.266   20.003  0.44 39.31 ?  31  LYS   A HD3  1 
ATOM   922  H HE2  A LYS   A 1 31  ? 22.624 2.261   22.505  0.56 44.03 ?  31  LYS   A HE2  1 
ATOM   923  H HE2  B LYS   A 1 31  ? 22.324 2.587   22.469  0.44 41.84 ?  31  LYS   A HE2  1 
ATOM   924  H HE3  A LYS   A 1 31  ? 23.558 3.365   21.848  0.56 44.03 ?  31  LYS   A HE3  1 
ATOM   925  H HE3  B LYS   A 1 31  ? 23.172 3.683   21.697  0.44 41.84 ?  31  LYS   A HE3  1 
ATOM   926  H HZ1  A LYS   A 1 31  ? 21.385 3.943   21.602  0.56 45.57 ?  31  LYS   A HZ1  1 
ATOM   927  H HZ1  B LYS   A 1 31  ? 20.992 4.152   21.445  0.44 43.26 ?  31  LYS   A HZ1  1 
ATOM   928  H HZ2  A LYS   A 1 31  ? 21.930 3.696   20.283  0.56 45.57 ?  31  LYS   A HZ2  1 
ATOM   929  H HZ2  B LYS   A 1 31  ? 21.483 3.751   20.143  0.44 43.26 ?  31  LYS   A HZ2  1 
ATOM   930  H HZ3  A LYS   A 1 31  ? 21.075 2.709   20.910  0.56 45.57 ?  31  LYS   A HZ3  1 
ATOM   931  H HZ3  B LYS   A 1 31  ? 20.691 2.831   20.933  0.44 43.26 ?  31  LYS   A HZ3  1 
ATOM   932  N N    A PRO   A 1 32  ? 22.912 -3.183  17.071  0.56 17.57 ?  32  PRO   A N    1 
ATOM   933  N N    B PRO   A 1 32  ? 22.699 -2.995  17.139  0.44 19.15 ?  32  PRO   A N    1 
ATOM   934  C CA   A PRO   A 1 32  ? 23.383 -4.529  16.737  0.56 18.00 ?  32  PRO   A CA   1 
ATOM   935  C CA   B PRO   A 1 32  ? 23.185 -4.346  16.849  0.44 18.30 ?  32  PRO   A CA   1 
ATOM   936  C C    A PRO   A 1 32  ? 24.883 -4.554  16.513  0.56 17.97 ?  32  PRO   A C    1 
ATOM   937  C C    B PRO   A 1 32  ? 24.693 -4.351  16.657  0.44 17.70 ?  32  PRO   A C    1 
ATOM   938  O O    A PRO   A 1 32  ? 25.522 -3.532  16.252  0.56 17.72 ?  32  PRO   A O    1 
ATOM   939  O O    B PRO   A 1 32  ? 25.347 -3.311  16.570  0.44 17.45 ?  32  PRO   A O    1 
ATOM   940  C CB   A PRO   A 1 32  ? 22.653 -4.834  15.428  0.56 17.49 ?  32  PRO   A CB   1 
ATOM   941  C CB   B PRO   A 1 32  ? 22.465 -4.693  15.544  0.44 17.80 ?  32  PRO   A CB   1 
ATOM   942  C CG   A PRO   A 1 32  ? 22.479 -3.490  14.796  0.56 16.85 ?  32  PRO   A CG   1 
ATOM   943  C CG   B PRO   A 1 32  ? 22.303 -3.373  14.865  0.44 17.77 ?  32  PRO   A CG   1 
ATOM   944  C CD   A PRO   A 1 32  ? 22.194 -2.562  15.945  0.56 16.87 ?  32  PRO   A CD   1 
ATOM   945  C CD   B PRO   A 1 32  ? 22.012 -2.400  15.979  0.44 18.12 ?  32  PRO   A CD   1 
ATOM   946  H HA   A PRO   A 1 32  ? 23.130 -5.168  17.424  0.56 21.62 ?  32  PRO   A HA   1 
ATOM   947  H HA   B PRO   A 1 32  ? 22.931 -4.968  17.547  0.44 21.98 ?  32  PRO   A HA   1 
ATOM   948  H HB2  A PRO   A 1 32  ? 23.203 -5.414  14.873  0.56 21.01 ?  32  PRO   A HB2  1 
ATOM   949  H HB2  B PRO   A 1 32  ? 23.009 -5.294  15.012  0.44 21.39 ?  32  PRO   A HB2  1 
ATOM   950  H HB3  A PRO   A 1 32  ? 21.797 -5.250  15.617  0.56 21.01 ?  32  PRO   A HB3  1 
ATOM   951  H HB3  B PRO   A 1 32  ? 21.599 -5.091  15.738  0.44 21.39 ?  32  PRO   A HB3  1 
ATOM   952  H HG2  A PRO   A 1 32  ? 23.295 -3.239  14.339  0.56 20.24 ?  32  PRO   A HG2  1 
ATOM   953  H HG2  B PRO   A 1 32  ? 23.125 -3.140  14.407  0.44 21.35 ?  32  PRO   A HG2  1 
ATOM   954  H HG3  A PRO   A 1 32  ? 21.731 -3.519  14.178  0.56 20.24 ?  32  PRO   A HG3  1 
ATOM   955  H HG3  B PRO   A 1 32  ? 21.561 -3.416  14.240  0.44 21.35 ?  32  PRO   A HG3  1 
ATOM   956  H HD2  A PRO   A 1 32  ? 22.553 -1.681  15.752  0.56 20.27 ?  32  PRO   A HD2  1 
ATOM   957  H HD2  B PRO   A 1 32  ? 22.388 -1.531  15.766  0.44 21.76 ?  32  PRO   A HD2  1 
ATOM   958  H HD3  A PRO   A 1 32  ? 21.243 -2.530  16.120  0.56 20.27 ?  32  PRO   A HD3  1 
ATOM   959  H HD3  B PRO   A 1 32  ? 21.057 -2.348  16.136  0.44 21.76 ?  32  PRO   A HD3  1 
ATOM   960  N N    A THR   A 1 33  ? 25.441 -5.764  16.585  0.56 17.74 ?  33  THR   A N    1 
ATOM   961  N N    B THR   A 1 33  ? 25.243 -5.564  16.584  0.44 17.94 ?  33  THR   A N    1 
ATOM   962  C CA   A THR   A 1 33  ? 26.854 -5.936  16.272  0.56 17.83 ?  33  THR   A CA   1 
ATOM   963  C CA   B THR   A 1 33  ? 26.669 -5.712  16.316  0.44 17.74 ?  33  THR   A CA   1 
ATOM   964  C C    A THR   A 1 33  ? 27.151 -5.483  14.847  0.56 16.58 ?  33  THR   A C    1 
ATOM   965  C C    B THR   A 1 33  ? 27.006 -5.269  14.896  0.44 16.14 ?  33  THR   A C    1 
ATOM   966  O O    A THR   A 1 33  ? 28.211 -4.900  14.584  0.56 16.37 ?  33  THR   A O    1 
ATOM   967  O O    B THR   A 1 33  ? 27.981 -4.540  14.676  0.44 15.62 ?  33  THR   A O    1 
ATOM   968  C CB   A THR   A 1 33  ? 27.260 -7.397  16.481  0.56 19.99 ?  33  THR   A CB   1 
ATOM   969  C CB   B THR   A 1 33  ? 27.087 -7.165  16.535  0.44 19.37 ?  33  THR   A CB   1 
ATOM   970  O OG1  A THR   A 1 33  ? 26.992 -7.783  17.835  0.56 21.41 ?  33  THR   A OG1  1 
ATOM   971  O OG1  B THR   A 1 33  ? 26.754 -7.565  17.870  0.44 20.52 ?  33  THR   A OG1  1 
ATOM   972  C CG2  A THR   A 1 33  ? 28.737 -7.597  16.199  0.56 20.80 ?  33  THR   A CG2  1 
ATOM   973  C CG2  B THR   A 1 33  ? 28.584 -7.329  16.316  0.44 19.94 ?  33  THR   A CG2  1 
ATOM   974  H H    A THR   A 1 33  ? 25.028 -6.488  16.790  0.56 21.31 ?  33  THR   A H    1 
ATOM   975  H H    B THR   A 1 33  ? 24.817 -6.303  16.686  0.44 21.55 ?  33  THR   A H    1 
ATOM   976  H HA   A THR   A 1 33  ? 27.382 -5.389  16.874  0.56 21.42 ?  33  THR   A HA   1 
ATOM   977  H HA   B THR   A 1 33  ? 27.166 -5.156  16.936  0.44 21.31 ?  33  THR   A HA   1 
ATOM   978  H HB   A THR   A 1 33  ? 26.748 -7.963  15.881  0.56 24.01 ?  33  THR   A HB   1 
ATOM   979  H HB   B THR   A 1 33  ? 26.617 -7.735  15.902  0.44 23.26 ?  33  THR   A HB   1 
ATOM   980  H HG1  A THR   A 1 33  ? 27.422 -7.291  18.365  0.56 25.71 ?  33  THR   A HG1  1 
ATOM   981  H HG1  B THR   A 1 33  ? 27.155 -7.075  18.422  0.44 24.65 ?  33  THR   A HG1  1 
ATOM   982  H HG21 A THR   A 1 33  ? 29.012 -8.478  16.500  0.56 24.98 ?  33  THR   A HG21 1 
ATOM   983  H HG21 B THR   A 1 33  ? 28.870 -8.203  16.626  0.44 23.95 ?  33  THR   A HG21 1 
ATOM   984  H HG22 A THR   A 1 33  ? 28.909 -7.522  15.250  0.56 24.98 ?  33  THR   A HG22 1 
ATOM   985  H HG22 B THR   A 1 33  ? 28.797 -7.246  15.373  0.44 23.95 ?  33  THR   A HG22 1 
ATOM   986  H HG23 A THR   A 1 33  ? 29.257 -6.929  16.672  0.56 24.98 ?  33  THR   A HG23 1 
ATOM   987  H HG23 B THR   A 1 33  ? 29.067 -6.648  16.810  0.44 23.95 ?  33  THR   A HG23 1 
ATOM   988  N N    . VAL   A 1 34  ? 26.217 -5.715  13.920  1.00 15.36 ?  34  VAL   A N    1 
ATOM   989  C CA   . VAL   A 1 34  ? 26.412 -5.384  12.511  1.00 14.15 ?  34  VAL   A CA   1 
ATOM   990  C C    . VAL   A 1 34  ? 25.112 -4.823  11.943  1.00 13.72 ?  34  VAL   A C    1 
ATOM   991  O O    . VAL   A 1 34  ? 24.070 -5.493  11.975  1.00 14.58 ?  34  VAL   A O    1 
ATOM   992  C CB   . VAL   A 1 34  ? 26.851 -6.604  11.679  1.00 14.91 ?  34  VAL   A CB   1 
ATOM   993  C CG1  . VAL   A 1 34  ? 27.010 -6.213  10.216  1.00 15.17 ?  34  VAL   A CG1  1 
ATOM   994  C CG2  . VAL   A 1 34  ? 28.136 -7.227  12.227  1.00 16.24 ?  34  VAL   A CG2  1 
ATOM   995  H H    A VAL   A 1 34  ? 25.452 -6.065  14.092  0.56 18.45 ?  34  VAL   A H    1 
ATOM   996  H H    B VAL   A 1 34  ? 25.546 -6.233  14.057  0.44 18.45 ?  34  VAL   A H    1 
ATOM   997  H HA   . VAL   A 1 34  ? 27.096 -4.701  12.430  1.00 17.00 ?  34  VAL   A HA   1 
ATOM   998  H HB   . VAL   A 1 34  ? 26.153 -7.279  11.736  1.00 17.91 ?  34  VAL   A HB   1 
ATOM   999  H HG11 . VAL   A 1 34  ? 27.505 -6.912  9.759   1.00 18.23 ?  34  VAL   A HG11 1 
ATOM   1000 H HG12 . VAL   A 1 34  ? 26.130 -6.120  9.814   1.00 18.23 ?  34  VAL   A HG12 1 
ATOM   1001 H HG13 . VAL   A 1 34  ? 27.492 -5.377  10.163  1.00 18.23 ?  34  VAL   A HG13 1 
ATOM   1002 H HG21 . VAL   A 1 34  ? 28.403 -7.959  11.647  1.00 19.51 ?  34  VAL   A HG21 1 
ATOM   1003 H HG22 . VAL   A 1 34  ? 28.830 -6.552  12.248  1.00 19.51 ?  34  VAL   A HG22 1 
ATOM   1004 H HG23 . VAL   A 1 34  ? 27.972 -7.562  13.124  1.00 19.51 ?  34  VAL   A HG23 1 
ATOM   1005 N N    . VAL   A 1 35  ? 25.183 -3.621  11.380  1.00 13.22 ?  35  VAL   A N    1 
ATOM   1006 C CA   . VAL   A 1 35  ? 24.153 -3.112  10.484  1.00 12.85 ?  35  VAL   A CA   1 
ATOM   1007 C C    . VAL   A 1 35  ? 24.710 -3.114  9.066   1.00 12.05 ?  35  VAL   A C    1 
ATOM   1008 O O    . VAL   A 1 35  ? 25.855 -2.703  8.840   1.00 12.69 ?  35  VAL   A O    1 
ATOM   1009 C CB   . VAL   A 1 35  ? 23.619 -1.721  10.897  1.00 13.39 ?  35  VAL   A CB   1 
ATOM   1010 C CG1  . VAL   A 1 35  ? 24.697 -0.632  10.788  1.00 13.48 ?  35  VAL   A CG1  1 
ATOM   1011 C CG2  . VAL   A 1 35  ? 22.392 -1.359  10.052  1.00 13.89 ?  35  VAL   A CG2  1 
ATOM   1012 H H    . VAL   A 1 35  ? 25.827 -3.067  11.501  1.00 15.88 ?  35  VAL   A H    1 
ATOM   1013 H HA   . VAL   A 1 35  ? 23.396 -3.724  10.502  1.00 15.45 ?  35  VAL   A HA   1 
ATOM   1014 H HB   . VAL   A 1 35  ? 23.324 -1.760  11.818  1.00 16.09 ?  35  VAL   A HB   1 
ATOM   1015 H HG11 . VAL   A 1 35  ? 24.343 0.193   11.152  1.00 16.20 ?  35  VAL   A HG11 1 
ATOM   1016 H HG12 . VAL   A 1 35  ? 25.471 -0.916  11.294  1.00 16.20 ?  35  VAL   A HG12 1 
ATOM   1017 H HG13 . VAL   A 1 35  ? 24.930 -0.512  9.856   1.00 16.20 ?  35  VAL   A HG13 1 
ATOM   1018 H HG21 . VAL   A 1 35  ? 22.027 -0.522  10.367  1.00 16.69 ?  35  VAL   A HG21 1 
ATOM   1019 H HG22 . VAL   A 1 35  ? 22.665 -1.275  9.122   1.00 16.69 ?  35  VAL   A HG22 1 
ATOM   1020 H HG23 . VAL   A 1 35  ? 21.732 -2.066  10.136  1.00 16.69 ?  35  VAL   A HG23 1 
ATOM   1021 N N    . VAL   A 1 36  ? 23.901 -3.578  8.113   1.00 11.04 ?  36  VAL   A N    1 
ATOM   1022 C CA   . VAL   A 1 36  ? 24.279 -3.592  6.705   1.00 11.06 ?  36  VAL   A CA   1 
ATOM   1023 C C    . VAL   A 1 36  ? 23.825 -2.301  6.040   1.00 11.63 ?  36  VAL   A C    1 
ATOM   1024 O O    . VAL   A 1 36  ? 22.665 -1.887  6.179   1.00 11.98 ?  36  VAL   A O    1 
ATOM   1025 C CB   . VAL   A 1 36  ? 23.678 -4.808  5.984   1.00 10.73 ?  36  VAL   A CB   1 
ATOM   1026 C CG1  . VAL   A 1 36  ? 23.933 -4.739  4.507   1.00 11.67 ?  36  VAL   A CG1  1 
ATOM   1027 C CG2  . VAL   A 1 36  ? 24.231 -6.090  6.566   1.00 11.83 ?  36  VAL   A CG2  1 
ATOM   1028 H H    . VAL   A 1 36  ? 23.106 -3.888  8.259   1.00 13.26 ?  36  VAL   A H    1 
ATOM   1029 H HA   . VAL   A 1 36  ? 25.244 -3.651  6.637   1.00 13.29 ?  36  VAL   A HA   1 
ATOM   1030 H HB   . VAL   A 1 36  ? 22.713 -4.807  6.124   1.00 12.90 ?  36  VAL   A HB   1 
ATOM   1031 H HG11 . VAL   A 1 36  ? 23.786 -5.616  4.120   1.00 14.03 ?  36  VAL   A HG11 1 
ATOM   1032 H HG12 . VAL   A 1 36  ? 23.324 -4.098  4.103   1.00 14.03 ?  36  VAL   A HG12 1 
ATOM   1033 H HG13 . VAL   A 1 36  ? 24.850 -4.463  4.358   1.00 14.03 ?  36  VAL   A HG13 1 
ATOM   1034 H HG21 . VAL   A 1 36  ? 23.842 -6.845  6.093   1.00 14.21 ?  36  VAL   A HG21 1 
ATOM   1035 H HG22 . VAL   A 1 36  ? 25.194 -6.094  6.458   1.00 14.21 ?  36  VAL   A HG22 1 
ATOM   1036 H HG23 . VAL   A 1 36  ? 24.002 -6.140  7.508   1.00 14.21 ?  36  VAL   A HG23 1 
ATOM   1037 N N    . ASN   A 1 37  ? 24.749 -1.673  5.310   1.00 10.53 ?  37  ASN   A N    1 
ATOM   1038 C CA   . ASN   A 1 37  ? 24.429 -0.555  4.434   1.00 10.19 ?  37  ASN   A CA   1 
ATOM   1039 C C    . ASN   A 1 37  ? 24.316 -1.031  2.995   1.00 10.37 ?  37  ASN   A C    1 
ATOM   1040 O O    . ASN   A 1 37  ? 25.112 -1.859  2.534   1.00 10.88 ?  37  ASN   A O    1 
ATOM   1041 C CB   . ASN   A 1 37  ? 25.497 0.535   4.525   1.00 10.47 ?  37  ASN   A CB   1 
ATOM   1042 C CG   . ASN   A 1 37  ? 25.183 1.721   3.657   1.00 10.87 ?  37  ASN   A CG   1 
ATOM   1043 O OD1  . ASN   A 1 37  ? 24.009 2.056   3.461   1.00 11.34 ?  37  ASN   A OD1  1 
ATOM   1044 N ND2  . ASN   A 1 37  ? 26.218 2.372   3.139   1.00 11.38 ?  37  ASN   A ND2  1 
ATOM   1045 H H    . ASN   A 1 37  ? 25.588 -1.873  5.315   1.00 12.66 ?  37  ASN   A H    1 
ATOM   1046 H HA   . ASN   A 1 37  ? 23.583 -0.166  4.698   1.00 12.25 ?  37  ASN   A HA   1 
ATOM   1047 H HB2  . ASN   A 1 37  ? 25.563 0.845   5.440   1.00 12.59 ?  37  ASN   A HB2  1 
ATOM   1048 H HB3  . ASN   A 1 37  ? 26.352 0.169   4.236   1.00 12.59 ?  37  ASN   A HB3  1 
ATOM   1049 H HD21 . ASN   A 1 37  ? 26.086 3.057   2.631   1.00 13.68 ?  37  ASN   A HD21 1 
ATOM   1050 H HD22 . ASN   A 1 37  ? 27.018 2.114   3.295   1.00 13.68 ?  37  ASN   A HD22 1 
ATOM   1051 N N    A ALA   A 1 38  ? 23.295 -0.506  2.306   0.56 10.41 ?  38  ALA   A N    1 
ATOM   1052 N N    B ALA   A 1 38  ? 23.307 -0.539  2.278   0.44 11.20 ?  38  ALA   A N    1 
ATOM   1053 C CA   A ALA   A 1 38  ? 23.111 -0.637  0.860   0.56 10.46 ?  38  ALA   A CA   1 
ATOM   1054 C CA   B ALA   A 1 38  ? 23.194 -0.838  0.849   0.44 11.83 ?  38  ALA   A CA   1 
ATOM   1055 C C    A ALA   A 1 38  ? 24.032 0.373   0.172   0.56 10.61 ?  38  ALA   A C    1 
ATOM   1056 C C    B ALA   A 1 38  ? 23.978 0.224   0.085   0.44 12.03 ?  38  ALA   A C    1 
ATOM   1057 O O    A ALA   A 1 38  ? 23.626 1.461   -0.247  0.56 10.06 ?  38  ALA   A O    1 
ATOM   1058 O O    B ALA   A 1 38  ? 23.444 1.259   -0.321  0.44 12.25 ?  38  ALA   A O    1 
ATOM   1059 C CB   A ALA   A 1 38  ? 21.648 -0.402  0.488   0.56 11.25 ?  38  ALA   A CB   1 
ATOM   1060 C CB   B ALA   A 1 38  ? 21.739 -0.923  0.407   0.44 12.72 ?  38  ALA   A CB   1 
ATOM   1061 H H    A ALA   A 1 38  ? 22.680 -0.032  2.672   0.56 12.51 ?  38  ALA   A H    1 
ATOM   1062 H H    B ALA   A 1 38  ? 22.684 -0.034  2.591   0.44 13.46 ?  38  ALA   A H    1 
ATOM   1063 H HA   A ALA   A 1 38  ? 23.365 -1.527  0.577   0.56 12.58 ?  38  ALA   A HA   1 
ATOM   1064 H HA   B ALA   A 1 38  ? 23.612 -1.694  0.673   0.44 14.22 ?  38  ALA   A HA   1 
ATOM   1065 H HB1  A ALA   A 1 38  ? 21.540 -0.524  -0.470  0.56 13.52 ?  38  ALA   A HB1  1 
ATOM   1066 H HB1  B ALA   A 1 38  ? 21.710 -1.328  -0.475  0.44 15.28 ?  38  ALA   A HB1  1 
ATOM   1067 H HB2  A ALA   A 1 38  ? 21.096 -1.040  0.965   0.56 13.52 ?  38  ALA   A HB2  1 
ATOM   1068 H HB2  B ALA   A 1 38  ? 21.250 -1.472  1.037   0.44 15.28 ?  38  ALA   A HB2  1 
ATOM   1069 H HB3  A ALA   A 1 38  ? 21.399 0.502   0.734   0.56 13.52 ?  38  ALA   A HB3  1 
ATOM   1070 H HB3  B ALA   A 1 38  ? 21.367 -0.033  0.375   0.44 15.28 ?  38  ALA   A HB3  1 
ATOM   1071 N N    A ALA   A 1 39  ? 25.303 -0.002  0.061   0.56 10.51 ?  39  ALA   A N    1 
ATOM   1072 N N    B ALA   A 1 39  ? 25.265 -0.042  -0.113  0.44 11.63 ?  39  ALA   A N    1 
ATOM   1073 C CA   A ALA   A 1 39  ? 26.362 0.866   -0.425  0.56 10.41 ?  39  ALA   A CA   1 
ATOM   1074 C CA   B ALA   A 1 39  ? 26.204 0.941   -0.628  0.44 11.40 ?  39  ALA   A CA   1 
ATOM   1075 C C    A ALA   A 1 39  ? 26.480 0.818   -1.943  0.56 10.71 ?  39  ALA   A C    1 
ATOM   1076 C C    B ALA   A 1 39  ? 26.381 0.814   -2.137  0.44 10.83 ?  39  ALA   A C    1 
ATOM   1077 O O    A ALA   A 1 39  ? 25.963 -0.083  -2.612  0.56 11.48 ?  39  ALA   A O    1 
ATOM   1078 O O    B ALA   A 1 39  ? 25.996 -0.174  -2.767  0.44 11.27 ?  39  ALA   A O    1 
ATOM   1079 C CB   A ALA   A 1 39  ? 27.694 0.449   0.208   0.56 10.99 ?  39  ALA   A CB   1 
ATOM   1080 C CB   B ALA   A 1 39  ? 27.555 0.781   0.074   0.44 12.63 ?  39  ALA   A CB   1 
ATOM   1081 H H    A ALA   A 1 39  ? 25.583 -0.790  0.270   0.56 12.64 ?  39  ALA   A H    1 
ATOM   1082 H H    B ALA   A 1 39  ? 25.623 -0.811  0.058   0.44 13.98 ?  39  ALA   A H    1 
ATOM   1083 H HA   A ALA   A 1 39  ? 26.175 1.780   -0.167  0.56 12.51 ?  39  ALA   A HA   1 
ATOM   1084 H HA   B ALA   A 1 39  ? 25.864 1.825   -0.420  0.44 13.70 ?  39  ALA   A HA   1 
ATOM   1085 H HB1  A ALA   A 1 39  ? 28.396 1.037   -0.121  0.56 13.21 ?  39  ALA   A HB1  1 
ATOM   1086 H HB1  B ALA   A 1 39  ? 28.166 1.446   -0.280  0.44 15.18 ?  39  ALA   A HB1  1 
ATOM   1087 H HB2  A ALA   A 1 39  ? 27.622 0.534   1.173   0.56 13.21 ?  39  ALA   A HB2  1 
ATOM   1088 H HB2  B ALA   A 1 39  ? 27.436 0.917   1.029   0.44 15.18 ?  39  ALA   A HB2  1 
ATOM   1089 H HB3  A ALA   A 1 39  ? 27.888 -0.466  -0.033  0.56 13.21 ?  39  ALA   A HB3  1 
ATOM   1090 H HB3  B ALA   A 1 39  ? 27.894 -0.109  -0.095  0.44 15.18 ?  39  ALA   A HB3  1 
ATOM   1091 N N    A ASN   A 1 40  ? 27.197 1.806   -2.482  0.56 10.96 ?  40  ASN   A N    1 
ATOM   1092 N N    B ASN   A 1 40  ? 26.987 1.847   -2.714  0.44 10.95 ?  40  ASN   A N    1 
ATOM   1093 C CA   A ASN   A 1 40  ? 27.742 1.749   -3.835  0.56 11.11 ?  40  ASN   A CA   1 
ATOM   1094 C CA   B ASN   A 1 40  ? 27.566 1.776   -4.046  0.44 11.23 ?  40  ASN   A CA   1 
ATOM   1095 C C    A ASN   A 1 40  ? 29.265 1.612   -3.778  0.56 10.85 ?  40  ASN   A C    1 
ATOM   1096 C C    B ASN   A 1 40  ? 29.087 1.642   -3.925  0.44 11.16 ?  40  ASN   A C    1 
ATOM   1097 O O    A ASN   A 1 40  ? 29.876 1.722   -2.712  0.56 10.69 ?  40  ASN   A O    1 
ATOM   1098 O O    B ASN   A 1 40  ? 29.653 1.721   -2.833  0.44 11.29 ?  40  ASN   A O    1 
ATOM   1099 C CB   A ASN   A 1 40  ? 27.283 2.937   -4.702  0.56 12.03 ?  40  ASN   A CB   1 
ATOM   1100 C CB   B ASN   A 1 40  ? 27.167 2.991   -4.895  0.44 11.23 ?  40  ASN   A CB   1 
ATOM   1101 C CG   A ASN   A 1 40  ? 27.603 4.285   -4.088  0.56 13.26 ?  40  ASN   A CG   1 
ATOM   1102 C CG   B ASN   A 1 40  ? 27.556 4.305   -4.260  0.44 11.76 ?  40  ASN   A CG   1 
ATOM   1103 O OD1  A ASN   A 1 40  ? 28.731 4.535   -3.656  0.56 12.69 ?  40  ASN   A OD1  1 
ATOM   1104 O OD1  B ASN   A 1 40  ? 28.739 4.585   -4.066  0.44 11.46 ?  40  ASN   A OD1  1 
ATOM   1105 N ND2  A ASN   A 1 40  ? 26.605 5.171   -4.057  0.56 14.45 ?  40  ASN   A ND2  1 
ATOM   1106 N ND2  B ASN   A 1 40  ? 26.561 5.126   -3.940  0.44 13.16 ?  40  ASN   A ND2  1 
ATOM   1107 H H    A ASN   A 1 40  ? 27.391 2.537   -2.074  0.56 13.17 ?  40  ASN   A H    1 
ATOM   1108 H H    B ASN   A 1 40  ? 27.077 2.613   -2.340  0.44 13.16 ?  40  ASN   A H    1 
ATOM   1109 H HA   A ASN   A 1 40  ? 27.408 0.951   -4.264  0.56 13.35 ?  40  ASN   A HA   1 
ATOM   1110 H HA   B ASN   A 1 40  ? 27.226 0.975   -4.491  0.44 13.49 ?  40  ASN   A HA   1 
ATOM   1111 H HB2  A ASN   A 1 40  ? 27.724 2.884   -5.574  0.56 14.46 ?  40  ASN   A HB2  1 
ATOM   1112 H HB2  B ASN   A 1 40  ? 27.612 2.929   -5.750  0.44 13.50 ?  40  ASN   A HB2  1 
ATOM   1113 H HB3  A ASN   A 1 40  ? 26.323 2.887   -4.826  0.56 14.46 ?  40  ASN   A HB3  1 
ATOM   1114 H HB3  B ASN   A 1 40  ? 26.204 2.985   -5.016  0.44 13.50 ?  40  ASN   A HB3  1 
ATOM   1115 H HD21 A ASN   A 1 40  ? 26.736 5.958   -3.733  0.56 17.37 ?  40  ASN   A HD21 1 
ATOM   1116 H HD21 B ASN   A 1 40  ? 26.733 5.882   -3.566  0.44 15.81 ?  40  ASN   A HD21 1 
ATOM   1117 H HD22 A ASN   A 1 40  ? 25.828 4.954   -4.356  0.56 17.37 ?  40  ASN   A HD22 1 
ATOM   1118 H HD22 B ASN   A 1 40  ? 25.747 4.901   -4.099  0.44 15.81 ?  40  ASN   A HD22 1 
ATOM   1119 N N    A VAL   A 1 41  ? 29.869 1.327   -4.938  0.56 11.38 ?  41  VAL   A N    1 
ATOM   1120 N N    B VAL   A 1 41  ? 29.748 1.426   -5.065  0.44 11.00 ?  41  VAL   A N    1 
ATOM   1121 C CA   A VAL   A 1 41  ? 31.303 1.040   -4.984  0.56 12.15 ?  41  VAL   A CA   1 
ATOM   1122 C CA   B VAL   A 1 41  ? 31.168 1.066   -5.042  0.44 12.07 ?  41  VAL   A CA   1 
ATOM   1123 C C    A VAL   A 1 41  ? 32.136 2.217   -4.515  0.56 12.24 ?  41  VAL   A C    1 
ATOM   1124 C C    B VAL   A 1 41  ? 32.065 2.191   -4.534  0.44 12.31 ?  41  VAL   A C    1 
ATOM   1125 O O    A VAL   A 1 41  ? 33.284 2.028   -4.096  0.56 12.60 ?  41  VAL   A O    1 
ATOM   1126 O O    B VAL   A 1 41  ? 33.191 1.927   -4.096  0.44 12.84 ?  41  VAL   A O    1 
ATOM   1127 C CB   A VAL   A 1 41  ? 31.777 0.575   -6.384  0.56 13.09 ?  41  VAL   A CB   1 
ATOM   1128 C CB   B VAL   A 1 41  ? 31.654 0.564   -6.417  0.44 13.25 ?  41  VAL   A CB   1 
ATOM   1129 C CG1  A VAL   A 1 41  ? 31.121 -0.746  -6.782  0.56 13.29 ?  41  VAL   A CG1  1 
ATOM   1130 C CG1  B VAL   A 1 41  ? 30.846 -0.649  -6.872  0.44 14.35 ?  41  VAL   A CG1  1 
ATOM   1131 C CG2  A VAL   A 1 41  ? 31.555 1.654   -7.438  0.56 14.35 ?  41  VAL   A CG2  1 
ATOM   1132 C CG2  B VAL   A 1 41  ? 31.625 1.677   -7.458  0.44 13.99 ?  41  VAL   A CG2  1 
ATOM   1133 H H    A VAL   A 1 41  ? 29.477 1.280   -5.698  0.56 13.68 ?  41  VAL   A H    1 
ATOM   1134 H H    B VAL   A 1 41  ? 29.393 1.465   -5.845  0.44 13.22 ?  41  VAL   A H    1 
ATOM   1135 H HA   A VAL   A 1 41  ? 31.487 0.307   -4.375  0.56 14.61 ?  41  VAL   A HA   1 
ATOM   1136 H HA   B VAL   A 1 41  ? 31.273 0.328   -4.425  0.44 14.51 ?  41  VAL   A HA   1 
ATOM   1137 H HB   A VAL   A 1 41  ? 32.733 0.409   -6.344  0.56 15.73 ?  41  VAL   A HB   1 
ATOM   1138 H HB   B VAL   A 1 41  ? 32.573 0.276   -6.326  0.44 15.92 ?  41  VAL   A HB   1 
ATOM   1139 H HG11 A VAL   A 1 41  ? 31.452 -1.016  -7.654  0.56 15.97 ?  41  VAL   A HG11 1 
ATOM   1140 H HG11 B VAL   A 1 41  ? 31.141 -0.910  -7.759  0.44 17.24 ?  41  VAL   A HG11 1 
ATOM   1141 H HG12 A VAL   A 1 41  ? 31.338 -1.420  -6.122  0.56 15.97 ?  41  VAL   A HG12 1 
ATOM   1142 H HG12 B VAL   A 1 41  ? 30.989 -1.376  -6.248  0.44 17.24 ?  41  VAL   A HG12 1 
ATOM   1143 H HG13 A VAL   A 1 41  ? 30.158 -0.619  -6.822  0.56 15.97 ?  41  VAL   A HG13 1 
ATOM   1144 H HG13 B VAL   A 1 41  ? 29.905 -0.416  -6.896  0.44 17.24 ?  41  VAL   A HG13 1 
ATOM   1145 H HG21 A VAL   A 1 41  ? 31.779 1.296   -8.313  0.56 17.24 ?  41  VAL   A HG21 1 
ATOM   1146 H HG21 B VAL   A 1 41  ? 31.800 1.296   -8.334  0.44 16.81 ?  41  VAL   A HG21 1 
ATOM   1147 H HG22 A VAL   A 1 41  ? 30.628 1.930   -7.422  0.56 17.24 ?  41  VAL   A HG22 1 
ATOM   1148 H HG22 B VAL   A 1 41  ? 30.752 2.098   -7.449  0.44 16.81 ?  41  VAL   A HG22 1 
ATOM   1149 H HG23 A VAL   A 1 41  ? 32.130 2.413   -7.240  0.56 17.24 ?  41  VAL   A HG23 1 
ATOM   1150 H HG23 B VAL   A 1 41  ? 32.309 2.331   -7.242  0.44 16.81 ?  41  VAL   A HG23 1 
ATOM   1151 N N    . TYR   A 1 42  ? 31.599 3.437   -4.595  1.00 11.72 ?  42  TYR   A N    1 
ATOM   1152 C CA   . TYR   A 1 42  ? 32.338 4.619   -4.172  1.00 12.18 ?  42  TYR   A CA   1 
ATOM   1153 C C    . TYR   A 1 42  ? 32.083 4.989   -2.724  1.00 12.01 ?  42  TYR   A C    1 
ATOM   1154 O O    . TYR   A 1 42  ? 32.642 5.981   -2.240  1.00 12.20 ?  42  TYR   A O    1 
ATOM   1155 C CB   . TYR   A 1 42  ? 31.986 5.810   -5.082  1.00 12.28 ?  42  TYR   A CB   1 
ATOM   1156 C CG   . TYR   A 1 42  ? 32.176 5.498   -6.547  1.00 12.91 ?  42  TYR   A CG   1 
ATOM   1157 C CD1  . TYR   A 1 42  ? 33.440 5.296   -7.074  1.00 14.11 ?  42  TYR   A CD1  1 
ATOM   1158 C CD2  . TYR   A 1 42  ? 31.085 5.372   -7.400  1.00 14.81 ?  42  TYR   A CD2  1 
ATOM   1159 C CE1  . TYR   A 1 42  ? 33.614 4.980   -8.410  1.00 14.72 ?  42  TYR   A CE1  1 
ATOM   1160 C CE2  . TYR   A 1 42  ? 31.255 5.077   -8.742  1.00 16.04 ?  42  TYR   A CE2  1 
ATOM   1161 C CZ   . TYR   A 1 42  ? 32.523 4.876   -9.239  1.00 15.63 ?  42  TYR   A CZ   1 
ATOM   1162 O OH   . TYR   A 1 42  ? 32.702 4.572   -10.563 1.00 17.65 ?  42  TYR   A OH   1 
ATOM   1163 H H    A TYR   A 1 42  ? 30.811 3.599   -4.892  0.56 14.09 ?  42  TYR   A H    1 
ATOM   1164 H H    B TYR   A 1 42  ? 30.817 3.625   -4.894  0.44 14.09 ?  42  TYR   A H    1 
ATOM   1165 H HA   . TYR   A 1 42  ? 33.287 4.451   -4.274  1.00 14.64 ?  42  TYR   A HA   1 
ATOM   1166 H HB2  . TYR   A 1 42  ? 31.051 6.048   -4.942  1.00 14.76 ?  42  TYR   A HB2  1 
ATOM   1167 H HB3  . TYR   A 1 42  ? 32.554 6.561   -4.859  1.00 14.76 ?  42  TYR   A HB3  1 
ATOM   1168 H HD1  . TYR   A 1 42  ? 34.180 5.357   -6.517  1.00 16.95 ?  42  TYR   A HD1  1 
ATOM   1169 H HD2  . TYR   A 1 42  ? 30.224 5.506   -7.065  1.00 17.79 ?  42  TYR   A HD2  1 
ATOM   1170 H HE1  . TYR   A 1 42  ? 34.470 4.852   -8.749  1.00 17.69 ?  42  TYR   A HE1  1 
ATOM   1171 H HE2  . TYR   A 1 42  ? 30.514 5.001   -9.302  1.00 19.27 ?  42  TYR   A HE2  1 
ATOM   1172 H HH   . TYR   A 1 42  ? 33.527 4.476   -10.724 1.00 21.20 ?  42  TYR   A HH   1 
ATOM   1173 N N    . LEU   A 1 43  ? 31.222 4.241   -2.039  1.00 11.43 ?  43  LEU   A N    1 
ATOM   1174 C CA   . LEU   A 1 43  ? 30.778 4.582   -0.689  1.00 10.84 ?  43  LEU   A CA   1 
ATOM   1175 C C    . LEU   A 1 43  ? 30.299 6.030   -0.602  1.00 11.08 ?  43  LEU   A C    1 
ATOM   1176 O O    . LEU   A 1 43  ? 30.554 6.734   0.378   1.00 12.19 ?  43  LEU   A O    1 
ATOM   1177 C CB   . LEU   A 1 43  ? 31.827 4.278   0.378   1.00 12.07 ?  43  LEU   A CB   1 
ATOM   1178 C CG   . LEU   A 1 43  ? 32.319 2.826   0.473   1.00 12.49 ?  43  LEU   A CG   1 
ATOM   1179 C CD1  . LEU   A 1 43  ? 33.357 2.708   1.567   1.00 13.12 ?  43  LEU   A CD1  1 
ATOM   1180 C CD2  . LEU   A 1 43  ? 31.161 1.852   0.724   1.00 13.15 ?  43  LEU   A CD2  1 
ATOM   1181 H H    . LEU   A 1 43  ? 30.872 3.506   -2.335  1.00 13.74 ?  43  LEU   A H    1 
ATOM   1182 H HA   . LEU   A 1 43  ? 30.007 4.025   -0.482  1.00 13.04 ?  43  LEU   A HA   1 
ATOM   1183 H HB2  . LEU   A 1 43  ? 32.601 4.836   0.213   1.00 14.51 ?  43  LEU   A HB2  1 
ATOM   1184 H HB3  . LEU   A 1 43  ? 31.449 4.506   1.246   1.00 14.51 ?  43  LEU   A HB3  1 
ATOM   1185 H HG   . LEU   A 1 43  ? 32.741 2.583   -0.365  1.00 15.01 ?  43  LEU   A HG   1 
ATOM   1186 H HD11 . LEU   A 1 43  ? 33.662 1.787   1.614   1.00 15.77 ?  43  LEU   A HD11 1 
ATOM   1187 H HD12 . LEU   A 1 43  ? 34.103 3.292   1.360   1.00 15.77 ?  43  LEU   A HD12 1 
ATOM   1188 H HD13 . LEU   A 1 43  ? 32.958 2.967   2.412   1.00 15.77 ?  43  LEU   A HD13 1 
ATOM   1189 H HD21 . LEU   A 1 43  ? 31.527 0.967   0.880   1.00 15.80 ?  43  LEU   A HD21 1 
ATOM   1190 H HD22 . LEU   A 1 43  ? 30.668 2.149   1.504   1.00 15.80 ?  43  LEU   A HD22 1 
ATOM   1191 H HD23 . LEU   A 1 43  ? 30.586 1.844   -0.053  1.00 15.80 ?  43  LEU   A HD23 1 
ATOM   1192 N N    A LYS   A 1 44  ? 29.582 6.471   -1.635  0.56 11.10 ?  44  LYS   A N    1 
ATOM   1193 N N    B LYS   A 1 44  ? 29.591 6.473   -1.639  0.44 11.77 ?  44  LYS   A N    1 
ATOM   1194 C CA   A LYS   A 1 44  ? 28.944 7.785   -1.636  0.56 11.59 ?  44  LYS   A CA   1 
ATOM   1195 C CA   B LYS   A 1 44  ? 28.937 7.777   -1.637  0.44 12.93 ?  44  LYS   A CA   1 
ATOM   1196 C C    A LYS   A 1 44  ? 27.512 7.610   -1.146  0.56 11.00 ?  44  LYS   A C    1 
ATOM   1197 C C    B LYS   A 1 44  ? 27.506 7.583   -1.154  0.44 12.56 ?  44  LYS   A C    1 
ATOM   1198 O O    A LYS   A 1 44  ? 26.654 7.086   -1.865  0.56 11.96 ?  44  LYS   A O    1 
ATOM   1199 O O    B LYS   A 1 44  ? 26.660 7.052   -1.883  0.44 13.01 ?  44  LYS   A O    1 
ATOM   1200 C CB   A LYS   A 1 44  ? 29.003 8.409   -3.026  0.56 14.04 ?  44  LYS   A CB   1 
ATOM   1201 C CB   B LYS   A 1 44  ? 28.978 8.402   -3.027  0.44 15.19 ?  44  LYS   A CB   1 
ATOM   1202 C CG   A LYS   A 1 44  ? 30.396 8.836   -3.450  0.56 17.00 ?  44  LYS   A CG   1 
ATOM   1203 C CG   B LYS   A 1 44  ? 30.343 8.931   -3.425  0.44 17.67 ?  44  LYS   A CG   1 
ATOM   1204 C CD   A LYS   A 1 44  ? 31.050 9.774   -2.439  0.56 21.23 ?  44  LYS   A CD   1 
ATOM   1205 C CD   B LYS   A 1 44  ? 30.913 9.875   -2.371  0.44 20.99 ?  44  LYS   A CD   1 
ATOM   1206 C CE   A LYS   A 1 44  ? 32.412 10.241  -2.915  0.56 24.10 ?  44  LYS   A CE   1 
ATOM   1207 C CE   B LYS   A 1 44  ? 32.178 10.554  -2.862  0.44 23.16 ?  44  LYS   A CE   1 
ATOM   1208 N NZ   A LYS   A 1 44  ? 33.179 10.883  -1.816  0.56 25.69 ?  44  LYS   A NZ   1 
ATOM   1209 N NZ   B LYS   A 1 44  ? 33.021 11.040  -1.736  0.44 24.76 ?  44  LYS   A NZ   1 
ATOM   1210 H H    A LYS   A 1 44  ? 29.448 6.020   -2.356  0.56 13.35 ?  44  LYS   A H    1 
ATOM   1211 H H    B LYS   A 1 44  ? 29.476 6.028   -2.368  0.44 14.15 ?  44  LYS   A H    1 
ATOM   1212 H HA   A LYS   A 1 44  ? 29.394 8.365   -1.005  0.56 13.93 ?  44  LYS   A HA   1 
ATOM   1213 H HA   B LYS   A 1 44  ? 29.380 8.360   -1.003  0.44 15.54 ?  44  LYS   A HA   1 
ATOM   1214 H HB2  A LYS   A 1 44  ? 28.682 7.767   -3.675  0.56 16.87 ?  44  LYS   A HB2  1 
ATOM   1215 H HB2  B LYS   A 1 44  ? 28.717 7.734   -3.680  0.44 18.25 ?  44  LYS   A HB2  1 
ATOM   1216 H HB3  A LYS   A 1 44  ? 28.439 9.201   -3.039  0.56 16.87 ?  44  LYS   A HB3  1 
ATOM   1217 H HB3  B LYS   A 1 44  ? 28.354 9.147   -3.054  0.44 18.25 ?  44  LYS   A HB3  1 
ATOM   1218 H HG2  A LYS   A 1 44  ? 30.958 8.050   -3.537  0.56 20.43 ?  44  LYS   A HG2  1 
ATOM   1219 H HG2  B LYS   A 1 44  ? 30.955 8.186   -3.530  0.44 21.23 ?  44  LYS   A HG2  1 
ATOM   1220 H HG3  A LYS   A 1 44  ? 30.344 9.303   -4.300  0.56 20.43 ?  44  LYS   A HG3  1 
ATOM   1221 H HG3  B LYS   A 1 44  ? 30.266 9.422   -4.259  0.44 21.23 ?  44  LYS   A HG3  1 
ATOM   1222 H HD2  A LYS   A 1 44  ? 30.479 10.549  -2.307  0.56 25.50 ?  44  LYS   A HD2  1 
ATOM   1223 H HD2  B LYS   A 1 44  ? 30.251 10.553  -2.158  0.44 25.21 ?  44  LYS   A HD2  1 
ATOM   1224 H HD3  A LYS   A 1 44  ? 31.177 9.305   -1.598  0.56 25.50 ?  44  LYS   A HD3  1 
ATOM   1225 H HD3  B LYS   A 1 44  ? 31.139 9.365   -1.575  0.44 25.21 ?  44  LYS   A HD3  1 
ATOM   1226 H HE2  A LYS   A 1 44  ? 32.918 9.477   -3.233  0.56 28.94 ?  44  LYS   A HE2  1 
ATOM   1227 H HE2  B LYS   A 1 44  ? 32.697 9.916   -3.378  0.44 27.82 ?  44  LYS   A HE2  1 
ATOM   1228 H HE3  A LYS   A 1 44  ? 32.295 10.888  -3.627  0.56 28.94 ?  44  LYS   A HE3  1 
ATOM   1229 H HE3  B LYS   A 1 44  ? 31.936 11.312  -3.412  0.44 27.82 ?  44  LYS   A HE3  1 
ATOM   1230 H HZ1  A LYS   A 1 44  ? 33.971 11.152  -2.115  0.56 30.85 ?  44  LYS   A HZ1  1 
ATOM   1231 H HZ1  B LYS   A 1 44  ? 33.755 11.431  -2.055  0.44 29.73 ?  44  LYS   A HZ1  1 
ATOM   1232 H HZ2  A LYS   A 1 44  ? 32.730 11.591  -1.509  0.56 30.85 ?  44  LYS   A HZ2  1 
ATOM   1233 H HZ2  B LYS   A 1 44  ? 32.568 11.628  -1.248  0.44 29.73 ?  44  LYS   A HZ2  1 
ATOM   1234 H HZ3  A LYS   A 1 44  ? 33.297 10.307  -1.150  0.56 30.85 ?  44  LYS   A HZ3  1 
ATOM   1235 H HZ3  B LYS   A 1 44  ? 33.261 10.357  -1.217  0.44 29.73 ?  44  LYS   A HZ3  1 
ATOM   1236 N N    A HIS   A 1 45  ? 27.265 8.023   0.093   0.56 10.45 ?  45  HIS   A N    1 
ATOM   1237 N N    B HIS   A 1 45  ? 27.242 7.994   0.082   0.44 12.29 ?  45  HIS   A N    1 
ATOM   1238 C CA   A HIS   A 1 45  ? 26.039 7.668   0.810   0.56 10.74 ?  45  HIS   A CA   1 
ATOM   1239 C CA   B HIS   A 1 45  ? 25.979 7.703   0.758   0.44 12.65 ?  45  HIS   A CA   1 
ATOM   1240 C C    A HIS   A 1 45  ? 24.990 8.767   0.630   0.56 11.34 ?  45  HIS   A C    1 
ATOM   1241 C C    B HIS   A 1 45  ? 25.039 8.886   0.560   0.44 13.33 ?  45  HIS   A C    1 
ATOM   1242 O O    A HIS   A 1 45  ? 24.635 9.507   1.550   0.56 12.46 ?  45  HIS   A O    1 
ATOM   1243 O O    B HIS   A 1 45  ? 24.941 9.780   1.401   0.44 14.28 ?  45  HIS   A O    1 
ATOM   1244 C CB   A HIS   A 1 45  ? 26.358 7.422   2.276   0.56 10.44 ?  45  HIS   A CB   1 
ATOM   1245 C CB   B HIS   A 1 45  ? 26.229 7.434   2.231   0.44 12.18 ?  45  HIS   A CB   1 
ATOM   1246 C CG   A HIS   A 1 45  ? 27.459 6.428   2.493   0.56 10.64 ?  45  HIS   A CG   1 
ATOM   1247 C CG   B HIS   A 1 45  ? 27.349 6.476   2.482   0.44 11.49 ?  45  HIS   A CG   1 
ATOM   1248 N ND1  A HIS   A 1 45  ? 27.426 5.140   1.996   0.56 11.67 ?  45  HIS   A ND1  1 
ATOM   1249 N ND1  B HIS   A 1 45  ? 27.373 5.197   1.965   0.44 11.45 ?  45  HIS   A ND1  1 
ATOM   1250 C CD2  A HIS   A 1 45  ? 28.640 6.556   3.143   0.56 11.08 ?  45  HIS   A CD2  1 
ATOM   1251 C CD2  B HIS   A 1 45  ? 28.497 6.623   3.185   0.44 11.22 ?  45  HIS   A CD2  1 
ATOM   1252 C CE1  A HIS   A 1 45  ? 28.540 4.519   2.342   0.56 11.51 ?  45  HIS   A CE1  1 
ATOM   1253 C CE1  B HIS   A 1 45  ? 28.486 4.598   2.348   0.44 10.89 ?  45  HIS   A CE1  1 
ATOM   1254 N NE2  A HIS   A 1 45  ? 29.292 5.355   3.037   0.56 11.66 ?  45  HIS   A NE2  1 
ATOM   1255 N NE2  B HIS   A 1 45  ? 29.185 5.441   3.089   0.44 11.27 ?  45  HIS   A NE2  1 
ATOM   1256 H H    A HIS   A 1 45  ? 27.798 8.524   0.547   0.56 12.56 ?  45  HIS   A H    1 
ATOM   1257 H H    B HIS   A 1 45  ? 27.789 8.460   0.561   0.44 14.77 ?  45  HIS   A H    1 
ATOM   1258 H HA   A HIS   A 1 45  ? 25.683 6.848   0.438   0.56 12.91 ?  45  HIS   A HA   1 
ATOM   1259 H HA   B HIS   A 1 45  ? 25.575 6.916   0.364   0.44 15.20 ?  45  HIS   A HA   1 
ATOM   1260 H HB2  A HIS   A 1 45  ? 26.623 8.258   2.686   0.56 12.55 ?  45  HIS   A HB2  1 
ATOM   1261 H HB2  B HIS   A 1 45  ? 26.447 8.269   2.672   0.44 14.64 ?  45  HIS   A HB2  1 
ATOM   1262 H HB3  A HIS   A 1 45  ? 25.561 7.078   2.715   0.56 12.55 ?  45  HIS   A HB3  1 
ATOM   1263 H HB3  B HIS   A 1 45  ? 25.422 7.058   2.621   0.44 14.64 ?  45  HIS   A HB3  1 
ATOM   1264 H HD2  A HIS   A 1 45  ? 28.954 7.318   3.577   0.56 13.32 ?  45  HIS   A HD2  1 
ATOM   1265 H HD2  B HIS   A 1 45  ? 28.769 7.386   3.644   0.44 13.49 ?  45  HIS   A HD2  1 
ATOM   1266 H HE1  A HIS   A 1 45  ? 28.753 3.636   2.139   0.56 13.83 ?  45  HIS   A HE1  1 
ATOM   1267 H HE1  B HIS   A 1 45  ? 28.730 3.725   2.139   0.44 13.09 ?  45  HIS   A HE1  1 
ATOM   1268 H HE2  A HIS   A 1 45  ? 30.065 5.173   3.369   0.56 14.02 ?  45  HIS   A HE2  1 
ATOM   1269 H HE2  B HIS   A 1 45  ? 29.947 5.274   3.448   0.44 13.55 ?  45  HIS   A HE2  1 
ATOM   1270 N N    A GLY   A 1 46  ? 24.465 8.836   -0.588  0.56 12.72 ?  46  GLY   A N    1 
ATOM   1271 N N    B GLY   A 1 46  ? 24.334 8.882   -0.563  0.44 14.11 ?  46  GLY   A N    1 
ATOM   1272 C CA   A GLY   A 1 46  ? 23.661 9.980   -0.983  0.56 13.76 ?  46  GLY   A CA   1 
ATOM   1273 C CA   B GLY   A 1 46  ? 23.478 10.002  -0.892  0.44 14.00 ?  46  GLY   A CA   1 
ATOM   1274 C C    A GLY   A 1 46  ? 22.165 9.850   -0.802  0.56 13.84 ?  46  GLY   A C    1 
ATOM   1275 C C    B GLY   A 1 46  ? 22.032 9.816   -0.475  0.44 13.02 ?  46  GLY   A C    1 
ATOM   1276 O O    A GLY   A 1 46  ? 21.481 10.849  -0.546  0.56 13.90 ?  46  GLY   A O    1 
ATOM   1277 O O    B GLY   A 1 46  ? 21.411 10.737  0.068   0.44 12.97 ?  46  GLY   A O    1 
ATOM   1278 H H    A GLY   A 1 46  ? 24.544 8.232   -1.194  0.56 15.29 ?  46  GLY   A H    1 
ATOM   1279 H H    B GLY   A 1 46  ? 24.342 8.243   -1.141  0.44 16.95 ?  46  GLY   A H    1 
ATOM   1280 H HA2  A GLY   A 1 46  ? 23.946 10.752  -0.475  0.56 16.53 ?  46  GLY   A HA2  1 
ATOM   1281 H HA2  B GLY   A 1 46  ? 23.822 10.798  -0.455  0.44 16.83 ?  46  GLY   A HA2  1 
ATOM   1282 H HA3  A GLY   A 1 46  ? 23.814 10.159  -1.919  0.56 16.53 ?  46  GLY   A HA3  1 
ATOM   1283 H HA3  B GLY   A 1 46  ? 23.515 10.146  -1.848  0.44 16.83 ?  46  GLY   A HA3  1 
ATOM   1284 N N    A GLY   A 1 47  ? 21.641 8.641   -0.960  0.56 14.00 ?  47  GLY   A N    1 
ATOM   1285 N N    B GLY   A 1 47  ? 21.482 8.634   -0.730  0.44 13.07 ?  47  GLY   A N    1 
ATOM   1286 C CA   A GLY   A 1 47  ? 20.206 8.445   -0.935  0.56 13.61 ?  47  GLY   A CA   1 
ATOM   1287 C CA   B GLY   A 1 47  ? 20.074 8.403   -0.474  0.44 13.41 ?  47  GLY   A CA   1 
ATOM   1288 C C    A GLY   A 1 47  ? 19.893 7.016   -0.554  0.56 12.99 ?  47  GLY   A C    1 
ATOM   1289 C C    B GLY   A 1 47  ? 19.730 6.992   -0.052  0.44 12.32 ?  47  GLY   A C    1 
ATOM   1290 O O    A GLY   A 1 47  ? 20.785 6.194   -0.335  0.56 12.36 ?  47  GLY   A O    1 
ATOM   1291 O O    B GLY   A 1 47  ? 20.623 6.172   0.194   0.44 11.63 ?  47  GLY   A O    1 
ATOM   1292 H H    A GLY   A 1 47  ? 22.092 7.917   -1.078  0.56 16.82 ?  47  GLY   A H    1 
ATOM   1293 H H    B GLY   A 1 47  ? 21.906 7.960   -1.058  0.44 15.71 ?  47  GLY   A H    1 
ATOM   1294 H HA2  A GLY   A 1 47  ? 19.791 9.044   -0.289  0.56 16.36 ?  47  GLY   A HA2  1 
ATOM   1295 H HA2  B GLY   A 1 47  ? 19.783 8.992   0.231   0.44 16.11 ?  47  GLY   A HA2  1 
ATOM   1296 H HA3  A GLY   A 1 47  ? 19.833 8.623   -1.813  0.56 16.36 ?  47  GLY   A HA3  1 
ATOM   1297 H HA3  B GLY   A 1 47  ? 19.569 8.609   -1.275  0.44 16.11 ?  47  GLY   A HA3  1 
ATOM   1298 N N    A GLY   A 1 48  ? 18.601 6.720   -0.491  0.56 12.65 ?  48  GLY   A N    1 
ATOM   1299 N N    B GLY   A 1 48  ? 18.434 6.697   0.032   0.44 12.63 ?  48  GLY   A N    1 
ATOM   1300 C CA   A GLY   A 1 48  ? 18.176 5.404   -0.077  0.56 12.35 ?  48  GLY   A CA   1 
ATOM   1301 C CA   B GLY   A 1 48  ? 18.030 5.382   0.470   0.44 12.39 ?  48  GLY   A CA   1 
ATOM   1302 C C    A GLY   A 1 48  ? 18.628 5.095   1.336   0.56 11.04 ?  48  GLY   A C    1 
ATOM   1303 C C    B GLY   A 1 48  ? 18.556 5.098   1.864   0.44 11.98 ?  48  GLY   A C    1 
ATOM   1304 O O    A GLY   A 1 48  ? 18.786 5.984   2.182   0.56 11.53 ?  48  GLY   A O    1 
ATOM   1305 O O    B GLY   A 1 48  ? 18.711 5.989   2.712   0.44 11.84 ?  48  GLY   A O    1 
ATOM   1306 H H    A GLY   A 1 48  ? 17.966 7.260   -0.670  0.56 15.20 ?  48  GLY   A H    1 
ATOM   1307 H H    B GLY   A 1 48  ? 17.776 7.231   -0.149  0.44 15.18 ?  48  GLY   A H    1 
ATOM   1308 H HA2  A GLY   A 1 48  ? 17.208 5.346   -0.109  0.56 14.84 ?  48  GLY   A HA2  1 
ATOM   1309 H HA2  B GLY   A 1 48  ? 17.059 5.306   0.466   0.44 14.90 ?  48  GLY   A HA2  1 
ATOM   1310 H HA3  A GLY   A 1 48  ? 18.550 4.732   -0.664  0.56 14.84 ?  48  GLY   A HA3  1 
ATOM   1311 H HA3  B GLY   A 1 48  ? 18.383 4.708   -0.147  0.44 14.90 ?  48  GLY   A HA3  1 
ATOM   1312 N N    A VAL   A 1 49  ? 18.845 3.803   1.595   0.56 10.77 ?  49  VAL   A N    1 
ATOM   1313 N N    B VAL   A 1 49  ? 18.837 3.818   2.102   0.44 11.48 ?  49  VAL   A N    1 
ATOM   1314 C CA   A VAL   A 1 49  ? 19.329 3.369   2.904   0.56 11.12 ?  49  VAL   A CA   1 
ATOM   1315 C CA   B VAL   A 1 49  ? 19.386 3.396   3.389   0.44 12.32 ?  49  VAL   A CA   1 
ATOM   1316 C C    A VAL   A 1 49  ? 20.622 4.083   3.258   0.56 9.83  ?  49  VAL   A C    1 
ATOM   1317 C C    B VAL   A 1 49  ? 20.715 4.084   3.667   0.44 11.35 ?  49  VAL   A C    1 
ATOM   1318 O O    A VAL   A 1 49  ? 20.805 4.518   4.396   0.56 9.75  ?  49  VAL   A O    1 
ATOM   1319 O O    B VAL   A 1 49  ? 20.989 4.493   4.803   0.44 11.14 ?  49  VAL   A O    1 
ATOM   1320 C CB   A VAL   A 1 49  ? 19.510 1.839   2.948   0.56 12.16 ?  49  VAL   A CB   1 
ATOM   1321 C CB   B VAL   A 1 49  ? 19.502 1.860   3.433   0.44 14.72 ?  49  VAL   A CB   1 
ATOM   1322 C CG1  A VAL   A 1 49  ? 20.295 1.432   4.181   0.56 13.39 ?  49  VAL   A CG1  1 
ATOM   1323 C CG1  B VAL   A 1 49  ? 19.821 1.339   2.063   0.44 16.73 ?  49  VAL   A CG1  1 
ATOM   1324 C CG2  A VAL   A 1 49  ? 18.170 1.139   2.981   0.56 12.95 ?  49  VAL   A CG2  1 
ATOM   1325 C CG2  B VAL   A 1 49  ? 20.565 1.401   4.432   0.44 14.52 ?  49  VAL   A CG2  1 
ATOM   1326 H H    A VAL   A 1 49  ? 18.726 3.164   1.037   0.56 12.95 ?  49  VAL   A H    1 
ATOM   1327 H H    B VAL   A 1 49  ? 18.703 3.187   1.524   0.44 13.79 ?  49  VAL   A H    1 
ATOM   1328 H HA   A VAL   A 1 49  ? 18.670 3.601   3.579   0.56 13.37 ?  49  VAL   A HA   1 
ATOM   1329 H HA   B VAL   A 1 49  ? 18.773 3.660   4.084   0.44 14.81 ?  49  VAL   A HA   1 
ATOM   1330 H HB   A VAL   A 1 49  ? 19.997 1.544   2.162   0.56 14.62 ?  49  VAL   A HB   1 
ATOM   1331 H HB   B VAL   A 1 49  ? 18.649 1.483   3.708   0.44 17.69 ?  49  VAL   A HB   1 
ATOM   1332 H HG11 A VAL   A 1 49  ? 20.142 0.493   4.354   0.56 16.09 ?  49  VAL   A HG11 1 
ATOM   1333 H HG11 B VAL   A 1 49  ? 20.209 0.467   2.157   0.44 20.09 ?  49  VAL   A HG11 1 
ATOM   1334 H HG12 A VAL   A 1 49  ? 21.238 1.593   4.027   0.56 16.09 ?  49  VAL   A HG12 1 
ATOM   1335 H HG12 B VAL   A 1 49  ? 18.999 1.282   1.545   0.44 20.09 ?  49  VAL   A HG12 1 
ATOM   1336 H HG13 A VAL   A 1 49  ? 19.985 1.960   4.936   0.56 16.09 ?  49  VAL   A HG13 1 
ATOM   1337 H HG13 B VAL   A 1 49  ? 20.447 1.944   1.636   0.44 20.09 ?  49  VAL   A HG13 1 
ATOM   1338 H HG21 A VAL   A 1 49  ? 18.313 0.181   2.968   0.56 15.57 ?  49  VAL   A HG21 1 
ATOM   1339 H HG21 B VAL   A 1 49  ? 20.440 0.455   4.605   0.44 17.45 ?  49  VAL   A HG21 1 
ATOM   1340 H HG22 A VAL   A 1 49  ? 17.703 1.394   3.793   0.56 15.57 ?  49  VAL   A HG22 1 
ATOM   1341 H HG22 B VAL   A 1 49  ? 21.444 1.551   4.049   0.44 17.45 ?  49  VAL   A HG22 1 
ATOM   1342 H HG23 A VAL   A 1 49  ? 17.657 1.409   2.205   0.56 15.57 ?  49  VAL   A HG23 1 
ATOM   1343 H HG23 B VAL   A 1 49  ? 20.464 1.903   5.253   0.44 17.45 ?  49  VAL   A HG23 1 
ATOM   1344 N N    A ALA   A 1 50  ? 21.556 4.154   2.306   0.56 9.69  ?  50  ALA   A N    1 
ATOM   1345 N N    B ALA   A 1 50  ? 21.570 4.200   2.645   0.44 11.16 ?  50  ALA   A N    1 
ATOM   1346 C CA   A ALA   A 1 50  ? 22.873 4.710   2.592   0.56 10.72 ?  50  ALA   A CA   1 
ATOM   1347 C CA   B ALA   A 1 50  ? 22.894 4.776   2.854   0.44 10.35 ?  50  ALA   A CA   1 
ATOM   1348 C C    A ALA   A 1 50  ? 22.779 6.170   2.999   0.56 10.01 ?  50  ALA   A C    1 
ATOM   1349 C C    B ALA   A 1 50  ? 22.791 6.230   3.288   0.44 9.57  ?  50  ALA   A C    1 
ATOM   1350 O O    A ALA   A 1 50  ? 23.441 6.599   3.945   0.56 10.48 ?  50  ALA   A O    1 
ATOM   1351 O O    B ALA   A 1 50  ? 23.359 6.625   4.313   0.44 9.32  ?  50  ALA   A O    1 
ATOM   1352 C CB   A ALA   A 1 50  ? 23.769 4.568   1.365   0.56 11.12 ?  50  ALA   A CB   1 
ATOM   1353 C CB   B ALA   A 1 50  ? 23.737 4.639   1.581   0.44 10.12 ?  50  ALA   A CB   1 
ATOM   1354 H H    A ALA   A 1 50  ? 21.453 3.879   1.505   0.56 11.65 ?  50  ALA   A H    1 
ATOM   1355 H H    B ALA   A 1 50  ? 21.408 3.960   1.826   0.44 13.41 ?  50  ALA   A H    1 
ATOM   1356 H HA   A ALA   A 1 50  ? 23.278 4.223   3.328   0.56 12.88 ?  50  ALA   A HA   1 
ATOM   1357 H HA   B ALA   A 1 50  ? 23.345 4.295   3.556   0.44 12.44 ?  50  ALA   A HA   1 
ATOM   1358 H HB1  A ALA   A 1 50  ? 24.638 4.948   1.567   0.56 13.36 ?  50  ALA   A HB1  1 
ATOM   1359 H HB1  B ALA   A 1 50  ? 24.617 5.024   1.735   0.44 12.16 ?  50  ALA   A HB1  1 
ATOM   1360 H HB2  A ALA   A 1 50  ? 23.856 3.630   1.149   0.56 13.36 ?  50  ALA   A HB2  1 
ATOM   1361 H HB2  B ALA   A 1 50  ? 23.830 3.696   1.358   0.44 12.16 ?  50  ALA   A HB2  1 
ATOM   1362 H HB3  A ALA   A 1 50  ? 23.361 5.047   0.627   0.56 13.36 ?  50  ALA   A HB3  1 
ATOM   1363 H HB3  B ALA   A 1 50  ? 23.300 5.105   0.850   0.44 12.16 ?  50  ALA   A HB3  1 
ATOM   1364 N N    A GLY   A 1 51  ? 21.974 6.955   2.286   0.56 10.54 ?  51  GLY   A N    1 
ATOM   1365 N N    B GLY   A 1 51  ? 22.042 7.035   2.530   0.44 10.96 ?  51  GLY   A N    1 
ATOM   1366 C CA   A GLY   A 1 51  ? 21.794 8.343   2.672   0.56 11.58 ?  51  GLY   A CA   1 
ATOM   1367 C CA   B GLY   A 1 51  ? 21.890 8.432   2.894   0.44 10.74 ?  51  GLY   A CA   1 
ATOM   1368 C C    A GLY   A 1 51  ? 21.206 8.483   4.060   0.56 11.32 ?  51  GLY   A C    1 
ATOM   1369 C C    B GLY   A 1 51  ? 21.257 8.592   4.261   0.44 10.78 ?  51  GLY   A C    1 
ATOM   1370 O O    A GLY   A 1 51  ? 21.601 9.365   4.825   0.56 12.01 ?  51  GLY   A O    1 
ATOM   1371 O O    B GLY   A 1 51  ? 21.622 9.488   5.027   0.44 11.38 ?  51  GLY   A O    1 
ATOM   1372 H H    A GLY   A 1 51  ? 21.543 6.716   1.590   0.56 12.67 ?  51  GLY   A H    1 
ATOM   1373 H H    B GLY   A 1 51  ? 21.612 6.796   1.813   0.44 13.18 ?  51  GLY   A H    1 
ATOM   1374 H HA2  A GLY   A 1 51  ? 22.648 8.802   2.661   0.56 13.92 ?  51  GLY   A HA2  1 
ATOM   1375 H HA2  B GLY   A 1 51  ? 22.760 8.860   2.894   0.44 12.91 ?  51  GLY   A HA2  1 
ATOM   1376 H HA3  A GLY   A 1 51  ? 21.198 8.783   2.049   0.56 13.92 ?  51  GLY   A HA3  1 
ATOM   1377 H HA3  B GLY   A 1 51  ? 21.332 8.879   2.230   0.44 12.91 ?  51  GLY   A HA3  1 
ATOM   1378 N N    A ALA   A 1 52  ? 20.242 7.623   4.398   0.56 11.68 ?  52  ALA   A N    1 
ATOM   1379 N N    B ALA   A 1 52  ? 20.297 7.723   4.586   0.44 10.80 ?  52  ALA   A N    1 
ATOM   1380 C CA   A ALA   A 1 52  ? 19.606 7.678   5.710   0.56 12.50 ?  52  ALA   A CA   1 
ATOM   1381 C CA   B ALA   A 1 52  ? 19.628 7.811   5.879   0.44 11.39 ?  52  ALA   A CA   1 
ATOM   1382 C C    A ALA   A 1 52  ? 20.577 7.296   6.821   0.56 12.29 ?  52  ALA   A C    1 
ATOM   1383 C C    B ALA   A 1 52  ? 20.540 7.365   7.020   0.44 10.52 ?  52  ALA   A C    1 
ATOM   1384 O O    A ALA   A 1 52  ? 20.656 7.979   7.845   0.56 13.21 ?  52  ALA   A O    1 
ATOM   1385 O O    B ALA   A 1 52  ? 20.579 8.008   8.075   0.44 10.88 ?  52  ALA   A O    1 
ATOM   1386 C CB   A ALA   A 1 52  ? 18.375 6.768   5.731   0.56 13.41 ?  52  ALA   A CB   1 
ATOM   1387 C CB   B ALA   A 1 52  ? 18.330 7.005   5.852   0.44 12.11 ?  52  ALA   A CB   1 
ATOM   1388 H H    A ALA   A 1 52  ? 19.951 6.998   3.895   0.56 14.04 ?  52  ALA   A H    1 
ATOM   1389 H H    B ALA   A 1 52  ? 20.027 7.080   4.074   0.44 12.99 ?  52  ALA   A H    1 
ATOM   1390 H HA   A ALA   A 1 52  ? 19.307 8.581   5.886   0.56 15.03 ?  52  ALA   A HA   1 
ATOM   1391 H HA   B ALA   A 1 52  ? 19.394 8.736   6.028   0.44 13.69 ?  52  ALA   A HA   1 
ATOM   1392 H HB1  A ALA   A 1 52  ? 17.958 6.812   6.608   0.56 16.11 ?  52  ALA   A HB1  1 
ATOM   1393 H HB1  B ALA   A 1 52  ? 17.883 7.106   6.705   0.44 14.56 ?  52  ALA   A HB1  1 
ATOM   1394 H HB2  A ALA   A 1 52  ? 17.750 7.072   5.054   0.56 16.11 ?  52  ALA   A HB2  1 
ATOM   1395 H HB2  B ALA   A 1 52  ? 17.763 7.342   5.139   0.44 14.56 ?  52  ALA   A HB2  1 
ATOM   1396 H HB3  A ALA   A 1 52  ? 18.649 5.857   5.542   0.56 16.11 ?  52  ALA   A HB3  1 
ATOM   1397 H HB3  B ALA   A 1 52  ? 18.538 6.071   5.691   0.44 14.56 ?  52  ALA   A HB3  1 
ATOM   1398 N N    A LEU   A 1 53  ? 21.313 6.193   6.653   0.56 11.62 ?  53  LEU   A N    1 
ATOM   1399 N N    B LEU   A 1 53  ? 21.266 6.255   6.845   0.44 10.40 ?  53  LEU   A N    1 
ATOM   1400 C CA   A LEU   A 1 53  ? 22.258 5.784   7.691   0.56 12.36 ?  53  LEU   A CA   1 
ATOM   1401 C CA   B LEU   A 1 53  ? 22.257 5.866   7.849   0.44 10.58 ?  53  LEU   A CA   1 
ATOM   1402 C C    A LEU   A 1 53  ? 23.319 6.849   7.905   0.56 11.68 ?  53  LEU   A C    1 
ATOM   1403 C C    B LEU   A 1 53  ? 23.289 6.969   8.035   0.44 10.42 ?  53  LEU   A C    1 
ATOM   1404 O O    A LEU   A 1 53  ? 23.686 7.152   9.043   0.56 11.87 ?  53  LEU   A O    1 
ATOM   1405 O O    B LEU   A 1 53  ? 23.553 7.410   9.158   0.44 11.15 ?  53  LEU   A O    1 
ATOM   1406 C CB   A LEU   A 1 53  ? 22.917 4.450   7.328   0.56 13.29 ?  53  LEU   A CB   1 
ATOM   1407 C CB   B LEU   A 1 53  ? 22.953 4.555   7.457   0.44 10.62 ?  53  LEU   A CB   1 
ATOM   1408 C CG   A LEU   A 1 53  ? 21.974 3.245   7.348   0.56 13.48 ?  53  LEU   A CG   1 
ATOM   1409 C CG   B LEU   A 1 53  ? 22.206 3.216   7.557   0.44 10.88 ?  53  LEU   A CG   1 
ATOM   1410 C CD1  A LEU   A 1 53  ? 22.679 2.026   6.795   0.56 13.01 ?  53  LEU   A CD1  1 
ATOM   1411 C CD1  B LEU   A 1 53  ? 23.052 2.112   6.940   0.44 11.95 ?  53  LEU   A CD1  1 
ATOM   1412 C CD2  A LEU   A 1 53  ? 21.469 2.981   8.759   0.56 14.40 ?  53  LEU   A CD2  1 
ATOM   1413 C CD2  B LEU   A 1 53  ? 21.867 2.861   8.991   0.44 10.73 ?  53  LEU   A CD2  1 
ATOM   1414 H H    A LEU   A 1 53  ? 21.288 5.677   5.969   0.56 13.96 ?  53  LEU   A H    1 
ATOM   1415 H H    B LEU   A 1 53  ? 21.200 5.720   6.172   0.44 12.50 ?  53  LEU   A H    1 
ATOM   1416 H HA   A LEU   A 1 53  ? 21.784 5.658   8.530   0.56 14.85 ?  53  LEU   A HA   1 
ATOM   1417 H HA   B LEU   A 1 53  ? 21.809 5.725   8.694   0.44 12.72 ?  53  LEU   A HA   1 
ATOM   1418 H HB2  A LEU   A 1 53  ? 23.285 4.517   6.431   0.56 15.97 ?  53  LEU   A HB2  1 
ATOM   1419 H HB2  B LEU   A 1 53  ? 23.232 4.641   6.531   0.44 12.76 ?  53  LEU   A HB2  1 
ATOM   1420 H HB3  A LEU   A 1 53  ? 23.635 4.269   7.958   0.56 15.97 ?  53  LEU   A HB3  1 
ATOM   1421 H HB3  B LEU   A 1 53  ? 23.740 4.468   8.012   0.44 12.76 ?  53  LEU   A HB3  1 
ATOM   1422 H HG   A LEU   A 1 53  ? 21.208 3.434   6.783   0.56 16.20 ?  53  LEU   A HG   1 
ATOM   1423 H HG   B LEU   A 1 53  ? 21.381 3.271   7.051   0.44 13.08 ?  53  LEU   A HG   1 
ATOM   1424 H HD11 A LEU   A 1 53  ? 22.068 1.274   6.814   0.56 15.63 ?  53  LEU   A HD11 1 
ATOM   1425 H HD11 B LEU   A 1 53  ? 22.575 1.269   7.012   0.44 14.36 ?  53  LEU   A HD11 1 
ATOM   1426 H HD12 A LEU   A 1 53  ? 22.954 2.208   5.884   0.56 15.63 ?  53  LEU   A HD12 1 
ATOM   1427 H HD12 B LEU   A 1 53  ? 23.216 2.319   6.007   0.44 14.36 ?  53  LEU   A HD12 1 
ATOM   1428 H HD13 A LEU   A 1 53  ? 23.456 1.837   7.345   0.56 15.63 ?  53  LEU   A HD13 1 
ATOM   1429 H HD13 B LEU   A 1 53  ? 23.895 2.054   7.419   0.44 14.36 ?  53  LEU   A HD13 1 
ATOM   1430 H HD21 A LEU   A 1 53  ? 21.008 2.131   8.777   0.56 17.30 ?  53  LEU   A HD21 1 
ATOM   1431 H HD21 B LEU   A 1 53  ? 21.415 2.003   9.006   0.44 12.90 ?  53  LEU   A HD21 1 
ATOM   1432 H HD22 A LEU   A 1 53  ? 22.228 2.960   9.365   0.56 17.30 ?  53  LEU   A HD22 1 
ATOM   1433 H HD22 B LEU   A 1 53  ? 22.684 2.817   9.508   0.44 12.90 ?  53  LEU   A HD22 1 
ATOM   1434 H HD23 A LEU   A 1 53  ? 20.862 3.693   9.019   0.56 17.30 ?  53  LEU   A HD23 1 
ATOM   1435 H HD23 B LEU   A 1 53  ? 21.282 3.548   9.351   0.44 12.90 ?  53  LEU   A HD23 1 
ATOM   1436 N N    A ASN   A 1 54  ? 23.822 7.429   6.822   0.56 11.31 ?  54  ASN   A N    1 
ATOM   1437 N N    B ASN   A 1 54  ? 23.877 7.433   6.934   0.44 10.95 ?  54  ASN   A N    1 
ATOM   1438 C CA   A ASN   A 1 54  ? 24.872 8.419   6.974   0.56 11.33 ?  54  ASN   A CA   1 
ATOM   1439 C CA   B ASN   A 1 54  ? 24.916 8.443   7.045   0.44 11.35 ?  54  ASN   A CA   1 
ATOM   1440 C C    A ASN   A 1 54  ? 24.367 9.645   7.728   0.56 11.18 ?  54  ASN   A C    1 
ATOM   1441 C C    B ASN   A 1 54  ? 24.394 9.707   7.714   0.44 11.48 ?  54  ASN   A C    1 
ATOM   1442 O O    A ASN   A 1 54  ? 25.044 10.151  8.631   0.56 11.61 ?  54  ASN   A O    1 
ATOM   1443 O O    B ASN   A 1 54  ? 25.097 10.318  8.529   0.44 12.02 ?  54  ASN   A O    1 
ATOM   1444 C CB   A ASN   A 1 54  ? 25.428 8.802   5.614   0.56 11.53 ?  54  ASN   A CB   1 
ATOM   1445 C CB   B ASN   A 1 54  ? 25.497 8.765   5.678   0.44 11.22 ?  54  ASN   A CB   1 
ATOM   1446 C CG   A ASN   A 1 54  ? 26.482 9.862   5.727   0.56 11.83 ?  54  ASN   A CG   1 
ATOM   1447 C CG   B ASN   A 1 54  ? 26.478 9.902   5.749   0.44 11.23 ?  54  ASN   A CG   1 
ATOM   1448 O OD1  A ASN   A 1 54  ? 27.510 9.655   6.379   0.56 12.25 ?  54  ASN   A OD1  1 
ATOM   1449 O OD1  B ASN   A 1 54  ? 27.468 9.831   6.485   0.44 10.75 ?  54  ASN   A OD1  1 
ATOM   1450 N ND2  A ASN   A 1 54  ? 26.240 11.012  5.118   0.56 12.22 ?  54  ASN   A ND2  1 
ATOM   1451 N ND2  B ASN   A 1 54  ? 26.212 10.968  5.005   0.44 12.15 ?  54  ASN   A ND2  1 
ATOM   1452 H H    A ASN   A 1 54  ? 23.569 7.273   6.018   0.56 13.59 ?  54  ASN   A H    1 
ATOM   1453 H H    B ASN   A 1 54  ? 23.694 7.186   6.130   0.44 13.16 ?  54  ASN   A H    1 
ATOM   1454 H HA   A ASN   A 1 54  ? 25.590 8.033   7.493   0.56 13.62 ?  54  ASN   A HA   1 
ATOM   1455 H HA   B ASN   A 1 54  ? 25.631 8.096   7.596   0.44 13.64 ?  54  ASN   A HA   1 
ATOM   1456 H HB2  A ASN   A 1 54  ? 25.824 8.017   5.202   0.56 13.86 ?  54  ASN   A HB2  1 
ATOM   1457 H HB2  B ASN   A 1 54  ? 25.961 7.983   5.337   0.44 13.48 ?  54  ASN   A HB2  1 
ATOM   1458 H HB3  A ASN   A 1 54  ? 24.710 9.144   5.058   0.56 13.86 ?  54  ASN   A HB3  1 
ATOM   1459 H HB3  B ASN   A 1 54  ? 24.781 9.019   5.075   0.44 13.48 ?  54  ASN   A HB3  1 
ATOM   1460 H HD21 A ASN   A 1 54  ? 26.815 11.649  5.157   0.56 14.69 ?  54  ASN   A HD21 1 
ATOM   1461 H HD21 B ASN   A 1 54  ? 26.744 11.643  5.015   0.44 14.60 ?  54  ASN   A HD21 1 
ATOM   1462 H HD22 A ASN   A 1 54  ? 25.512 11.116  4.672   0.56 14.69 ?  54  ASN   A HD22 1 
ATOM   1463 H HD22 B ASN   A 1 54  ? 25.511 10.980  4.508   0.44 14.60 ?  54  ASN   A HD22 1 
ATOM   1464 N N    . LYS   A 1 55  ? 23.170 10.128  7.378   1.00 11.50 ?  55  LYS   A N    1 
ATOM   1465 C CA   . LYS   A 1 55  ? 22.600 11.296  8.036   1.00 12.68 ?  55  LYS   A CA   1 
ATOM   1466 C C    . LYS   A 1 55  ? 22.498 11.067  9.538   1.00 12.47 ?  55  LYS   A C    1 
ATOM   1467 O O    . LYS   A 1 55  ? 22.780 11.970  10.338  1.00 13.08 ?  55  LYS   A O    1 
ATOM   1468 C CB   . LYS   A 1 55  ? 21.233 11.586  7.416   1.00 13.97 ?  55  LYS   A CB   1 
ATOM   1469 C CG   . LYS   A 1 55  ? 20.495 12.773  8.000   1.00 15.83 ?  55  LYS   A CG   1 
ATOM   1470 C CD   . LYS   A 1 55  ? 19.152 12.967  7.292   1.00 18.54 ?  55  LYS   A CD   1 
ATOM   1471 C CE   . LYS   A 1 55  ? 18.319 14.074  7.913   1.00 20.83 ?  55  LYS   A CE   1 
ATOM   1472 N NZ   . LYS   A 1 55  ? 16.958 14.149  7.302   1.00 22.54 ?  55  LYS   A NZ   1 
ATOM   1473 H H    A LYS   A 1 55  ? 22.663 9.784   6.771   0.56 13.82 ?  55  LYS   A H    1 
ATOM   1474 H H    B LYS   A 1 55  ? 22.657 9.753   6.795   0.44 13.82 ?  55  LYS   A H    1 
ATOM   1475 H HA   . LYS   A 1 55  ? 23.173 12.060  7.884   1.00 15.24 ?  55  LYS   A HA   1 
ATOM   1476 H HB2  . LYS   A 1 55  ? 21.353 11.760  6.470   1.00 16.79 ?  55  LYS   A HB2  1 
ATOM   1477 H HB3  . LYS   A 1 55  ? 20.666 10.809  7.535   1.00 16.79 ?  55  LYS   A HB3  1 
ATOM   1478 H HG2  . LYS   A 1 55  ? 20.319 12.622  8.942   1.00 19.02 ?  55  LYS   A HG2  1 
ATOM   1479 H HG3  . LYS   A 1 55  ? 21.021 13.579  7.878   1.00 19.02 ?  55  LYS   A HG3  1 
ATOM   1480 H HD2  . LYS   A 1 55  ? 19.315 13.194  6.361   1.00 22.27 ?  55  LYS   A HD2  1 
ATOM   1481 H HD3  . LYS   A 1 55  ? 18.644 12.141  7.345   1.00 22.27 ?  55  LYS   A HD3  1 
ATOM   1482 H HE2  . LYS   A 1 55  ? 18.220 13.906  8.862   1.00 25.02 ?  55  LYS   A HE2  1 
ATOM   1483 H HE3  . LYS   A 1 55  ? 18.765 14.926  7.769   1.00 25.02 ?  55  LYS   A HE3  1 
ATOM   1484 H HZ1  . LYS   A 1 55  ? 16.395 14.550  7.864   1.00 27.07 ?  55  LYS   A HZ1  1 
ATOM   1485 H HZ2  . LYS   A 1 55  ? 16.987 14.619  6.545   1.00 27.07 ?  55  LYS   A HZ2  1 
ATOM   1486 H HZ3  . LYS   A 1 55  ? 16.656 13.332  7.126   1.00 27.07 ?  55  LYS   A HZ3  1 
ATOM   1487 N N    . ALA   A 1 56  ? 22.097 9.857   9.940   1.00 12.79 ?  56  ALA   A N    1 
ATOM   1488 C CA   . ALA   A 1 56  ? 21.968 9.533   11.354  1.00 13.56 ?  56  ALA   A CA   1 
ATOM   1489 C C    . ALA   A 1 56  ? 23.305 9.558   12.082  1.00 13.72 ?  56  ALA   A C    1 
ATOM   1490 O O    . ALA   A 1 56  ? 23.322 9.738   13.302  1.00 14.66 ?  56  ALA   A O    1 
ATOM   1491 C CB   . ALA   A 1 56  ? 21.269 8.179   11.528  1.00 14.35 ?  56  ALA   A CB   1 
ATOM   1492 H H    . ALA   A 1 56  ? 21.896 9.211   9.408   1.00 15.37 ?  56  ALA   A H    1 
ATOM   1493 H HA   . ALA   A 1 56  ? 21.412 10.195  11.772  1.00 16.29 ?  56  ALA   A HA   1 
ATOM   1494 H HB1  . ALA   A 1 56  ? 21.197 7.975   12.475  1.00 17.24 ?  56  ALA   A HB1  1 
ATOM   1495 H HB2  . ALA   A 1 56  ? 20.380 8.232   11.137  1.00 17.24 ?  56  ALA   A HB2  1 
ATOM   1496 H HB3  . ALA   A 1 56  ? 21.782 7.487   11.080  1.00 17.24 ?  56  ALA   A HB3  1 
ATOM   1497 N N    . THR   A 1 57  ? 24.419 9.367   11.371  1.00 12.40 ?  57  THR   A N    1 
ATOM   1498 C CA   . THR   A 1 57  ? 25.754 9.493   11.960  1.00 13.10 ?  57  THR   A CA   1 
ATOM   1499 C C    . THR   A 1 57  ? 26.313 10.907  11.876  1.00 13.09 ?  57  THR   A C    1 
ATOM   1500 O O    . THR   A 1 57  ? 27.500 11.107  12.159  1.00 13.51 ?  57  THR   A O    1 
ATOM   1501 C CB   . THR   A 1 57  ? 26.771 8.544   11.302  1.00 12.69 ?  57  THR   A CB   1 
ATOM   1502 O OG1  . THR   A 1 57  ? 27.154 9.040   10.006  1.00 12.43 ?  57  THR   A OG1  1 
ATOM   1503 C CG2  . THR   A 1 57  ? 26.248 7.114   11.211  1.00 12.70 ?  57  THR   A CG2  1 
ATOM   1504 H H    . THR   A 1 57  ? 24.434 9.147   10.537  1.00 14.91 ?  57  THR   A H    1 
ATOM   1505 H HA   . THR   A 1 57  ? 25.698 9.241   12.901  1.00 15.74 ?  57  THR   A HA   1 
ATOM   1506 H HB   . THR   A 1 57  ? 27.568 8.518   11.862  1.00 15.25 ?  57  THR   A HB   1 
ATOM   1507 H HG1  . THR   A 1 57  ? 26.469 9.096   9.515   1.00 14.94 ?  57  THR   A HG1  1 
ATOM   1508 H HG21 . THR   A 1 57  ? 26.927 6.527   10.844  1.00 15.26 ?  57  THR   A HG21 1 
ATOM   1509 H HG22 . THR   A 1 57  ? 25.999 6.790   12.094  1.00 15.26 ?  57  THR   A HG22 1 
ATOM   1510 H HG23 . THR   A 1 57  ? 25.464 7.081   10.639  1.00 15.26 ?  57  THR   A HG23 1 
ATOM   1511 N N    . ASN   A 1 58  ? 25.505 11.885  11.477  1.00 13.65 ?  58  ASN   A N    1 
ATOM   1512 C CA   . ASN   A 1 58  ? 25.988 13.259  11.388  1.00 14.68 ?  58  ASN   A CA   1 
ATOM   1513 C C    . ASN   A 1 58  ? 27.131 13.380  10.373  1.00 13.46 ?  58  ASN   A C    1 
ATOM   1514 O O    . ASN   A 1 58  ? 28.026 14.209  10.527  1.00 14.11 ?  58  ASN   A O    1 
ATOM   1515 C CB   . ASN   A 1 58  ? 26.382 13.772  12.790  1.00 17.17 ?  58  ASN   A CB   1 
ATOM   1516 C CG   . ASN   A 1 58  ? 26.810 15.231  12.813  1.00 20.37 ?  58  ASN   A CG   1 
ATOM   1517 O OD1  . ASN   A 1 58  ? 26.184 16.078  12.185  1.00 21.68 ?  58  ASN   A OD1  1 
ATOM   1518 N ND2  . ASN   A 1 58  ? 27.872 15.534  13.576  1.00 21.13 ?  58  ASN   A ND2  1 
ATOM   1519 H H    . ASN   A 1 58  ? 24.683 11.774  11.246  1.00 16.41 ?  58  ASN   A H    1 
ATOM   1520 H HA   . ASN   A 1 58  ? 25.258 13.811  11.076  1.00 17.63 ?  58  ASN   A HA   1 
ATOM   1521 H HB2  . ASN   A 1 58  ? 25.616 13.676  13.389  1.00 20.62 ?  58  ASN   A HB2  1 
ATOM   1522 H HB3  . ASN   A 1 58  ? 27.121 13.247  13.131  1.00 20.62 ?  58  ASN   A HB3  1 
ATOM   1523 H HD21 . ASN   A 1 58  ? 28.150 16.350  13.631  1.00 25.38 ?  58  ASN   A HD21 1 
ATOM   1524 H HD22 . ASN   A 1 58  ? 28.280 14.915  14.010  1.00 25.38 ?  58  ASN   A HD22 1 
ATOM   1525 N N    . ASN   A 1 59  ? 27.100 12.562  9.317   1.00 12.42 ?  59  ASN   A N    1 
ATOM   1526 C CA   . ASN   A 1 59  ? 28.087 12.525  8.224   1.00 12.09 ?  59  ASN   A CA   1 
ATOM   1527 C C    . ASN   A 1 59  ? 29.402 11.843  8.620   1.00 12.10 ?  59  ASN   A C    1 
ATOM   1528 O O    . ASN   A 1 59  ? 30.323 11.797  7.796   1.00 11.73 ?  59  ASN   A O    1 
ATOM   1529 C CB   . ASN   A 1 59  ? 28.382 13.909  7.610   1.00 12.35 ?  59  ASN   A CB   1 
ATOM   1530 C CG   . ASN   A 1 59  ? 28.741 13.838  6.140   1.00 12.62 ?  59  ASN   A CG   1 
ATOM   1531 O OD1  . ASN   A 1 59  ? 28.032 13.218  5.347   1.00 12.48 ?  59  ASN   A OD1  1 
ATOM   1532 N ND2  . ASN   A 1 59  ? 29.850 14.484  5.762   1.00 13.82 ?  59  ASN   A ND2  1 
ATOM   1533 H H    . ASN   A 1 59  ? 26.475 11.978  9.202   1.00 14.92 ?  59  ASN   A H    1 
ATOM   1534 H HA   . ASN   A 1 59  ? 27.707 11.994  7.515   1.00 14.53 ?  59  ASN   A HA   1 
ATOM   1535 H HB2  . ASN   A 1 59  ? 27.598 14.472  7.692   1.00 14.84 ?  59  ASN   A HB2  1 
ATOM   1536 H HB3  . ASN   A 1 59  ? 29.131 14.315  8.075   1.00 14.84 ?  59  ASN   A HB3  1 
ATOM   1537 H HD21 . ASN   A 1 59  ? 30.097 14.476  4.938   1.00 16.61 ?  59  ASN   A HD21 1 
ATOM   1538 H HD22 . ASN   A 1 59  ? 30.323 14.910  6.344   1.00 16.61 ?  59  ASN   A HD22 1 
ATOM   1539 N N    . ALA   A 1 60  ? 29.517 11.299  9.831   1.00 12.44 ?  60  ALA   A N    1 
ATOM   1540 C CA   . ALA   A 1 60  ? 30.754 10.618  10.192  1.00 12.06 ?  60  ALA   A CA   1 
ATOM   1541 C C    . ALA   A 1 60  ? 30.979 9.380   9.331   1.00 12.25 ?  60  ALA   A C    1 
ATOM   1542 O O    . ALA   A 1 60  ? 32.121 9.054   8.997   1.00 12.20 ?  60  ALA   A O    1 
ATOM   1543 C CB   . ALA   A 1 60  ? 30.749 10.270  11.673  1.00 12.37 ?  60  ALA   A CB   1 
ATOM   1544 H H    . ALA   A 1 60  ? 28.912 11.306  10.442  1.00 14.95 ?  60  ALA   A H    1 
ATOM   1545 H HA   . ALA   A 1 60  ? 31.496 11.227  10.033  1.00 14.49 ?  60  ALA   A HA   1 
ATOM   1546 H HB1  . ALA   A 1 60  ? 31.578 9.822   11.896  1.00 14.87 ?  60  ALA   A HB1  1 
ATOM   1547 H HB2  . ALA   A 1 60  ? 30.666 11.089  12.190  1.00 14.87 ?  60  ALA   A HB2  1 
ATOM   1548 H HB3  . ALA   A 1 60  ? 29.995 9.688   11.857  1.00 14.87 ?  60  ALA   A HB3  1 
ATOM   1549 N N    . MET   A 1 61  ? 29.909 8.686   8.950   1.00 11.56 ?  61  MET   A N    1 
ATOM   1550 C CA   . MET   A 1 61  ? 30.046 7.547   8.045   1.00 11.55 ?  61  MET   A CA   1 
ATOM   1551 C C    . MET   A 1 61  ? 30.685 7.967   6.723   1.00 11.59 ?  61  MET   A C    1 
ATOM   1552 O O    . MET   A 1 61  ? 31.578 7.281   6.206   1.00 11.69 ?  61  MET   A O    1 
ATOM   1553 C CB   . MET   A 1 61  ? 28.683 6.885   7.827   1.00 11.71 ?  61  MET   A CB   1 
ATOM   1554 C CG   . MET   A 1 61  ? 28.694 5.725   6.846   1.00 11.87 ?  61  MET   A CG   1 
ATOM   1555 S SD   . MET   A 1 61  ? 27.070 4.979   6.652   1.00 13.14 ?  61  MET   A SD   1 
ATOM   1556 C CE   . MET   A 1 61  ? 26.953 4.102   8.217   1.00 14.73 ?  61  MET   A CE   1 
ATOM   1557 H H    . MET   A 1 61  ? 29.101 8.853   9.190   1.00 13.89 ?  61  MET   A H    1 
ATOM   1558 H HA   . MET   A 1 61  ? 30.620 6.888   8.466   1.00 13.88 ?  61  MET   A HA   1 
ATOM   1559 H HB2  . MET   A 1 61  ? 28.361 6.551   8.676   1.00 14.07 ?  61  MET   A HB2  1 
ATOM   1560 H HB3  . MET   A 1 61  ? 28.066 7.552   7.483   1.00 14.07 ?  61  MET   A HB3  1 
ATOM   1561 H HG2  . MET   A 1 61  ? 28.975 6.040   5.973   1.00 14.27 ?  61  MET   A HG2  1 
ATOM   1562 H HG3  . MET   A 1 61  ? 29.301 5.042   7.167   1.00 14.27 ?  61  MET   A HG3  1 
ATOM   1563 H HE1  . MET   A 1 61  ? 26.124 3.601   8.241   1.00 17.70 ?  61  MET   A HE1  1 
ATOM   1564 H HE2  . MET   A 1 61  ? 27.708 3.503   8.302   1.00 17.70 ?  61  MET   A HE2  1 
ATOM   1565 H HE3  . MET   A 1 61  ? 26.964 4.749   8.947   1.00 17.70 ?  61  MET   A HE3  1 
ATOM   1566 N N    . GLN   A 1 62  ? 30.253 9.099   6.165   1.00 11.82 ?  62  GLN   A N    1 
ATOM   1567 C CA   . GLN   A 1 62  ? 30.819 9.560   4.901   1.00 11.72 ?  62  GLN   A CA   1 
ATOM   1568 C C    . GLN   A 1 62  ? 32.289 9.937   5.046   1.00 11.46 ?  62  GLN   A C    1 
ATOM   1569 O O    . GLN   A 1 62  ? 33.100 9.619   4.168   1.00 11.62 ?  62  GLN   A O    1 
ATOM   1570 C CB   . GLN   A 1 62  ? 30.029 10.744  4.355   1.00 11.86 ?  62  GLN   A CB   1 
ATOM   1571 C CG   . GLN   A 1 62  ? 30.403 11.099  2.930   1.00 11.90 ?  62  GLN   A CG   1 
ATOM   1572 C CD   . GLN   A 1 62  ? 30.082 9.964   1.981   1.00 11.80 ?  62  GLN   A CD   1 
ATOM   1573 O OE1  . GLN   A 1 62  ? 28.906 9.664   1.758   1.00 12.61 ?  62  GLN   A OE1  1 
ATOM   1574 N NE2  . GLN   A 1 62  ? 31.111 9.290   1.464   1.00 12.50 ?  62  GLN   A NE2  1 
ATOM   1575 H H    . GLN   A 1 62  ? 29.639 9.603   6.492   1.00 14.21 ?  62  GLN   A H    1 
ATOM   1576 H HA   . GLN   A 1 62  ? 30.767 8.838   4.260   1.00 14.08 ?  62  GLN   A HA   1 
ATOM   1577 H HB2  . GLN   A 1 62  ? 29.085 10.529  4.381   1.00 14.25 ?  62  GLN   A HB2  1 
ATOM   1578 H HB3  . GLN   A 1 62  ? 30.205 11.522  4.913   1.00 14.25 ?  62  GLN   A HB3  1 
ATOM   1579 H HG2  . GLN   A 1 62  ? 29.889 11.870  2.650   1.00 14.30 ?  62  GLN   A HG2  1 
ATOM   1580 H HG3  . GLN   A 1 62  ? 31.349 11.281  2.879   1.00 14.30 ?  62  GLN   A HG3  1 
ATOM   1581 H HE21 . GLN   A 1 62  ? 31.920 9.514   1.663   1.00 15.02 ?  62  GLN   A HE21 1 
ATOM   1582 H HE22 . GLN   A 1 62  ? 30.972 8.628   0.930   1.00 15.02 ?  62  GLN   A HE22 1 
ATOM   1583 N N    . VAL   A 1 63  ? 32.648 10.620  6.138   1.00 12.32 ?  63  VAL   A N    1 
ATOM   1584 C CA   . VAL   A 1 63  ? 34.042 11.007  6.359   1.00 13.11 ?  63  VAL   A CA   1 
ATOM   1585 C C    . VAL   A 1 63  ? 34.933 9.770   6.440   1.00 12.18 ?  63  VAL   A C    1 
ATOM   1586 O O    . VAL   A 1 63  ? 35.985 9.690   5.791   1.00 12.73 ?  63  VAL   A O    1 
ATOM   1587 C CB   . VAL   A 1 63  ? 34.149 11.882  7.618   1.00 14.45 ?  63  VAL   A CB   1 
ATOM   1588 C CG1  . VAL   A 1 63  ? 35.594 12.132  7.984   1.00 16.25 ?  63  VAL   A CG1  1 
ATOM   1589 C CG2  . VAL   A 1 63  ? 33.429 13.207  7.391   1.00 14.89 ?  63  VAL   A CG2  1 
ATOM   1590 H H    . VAL   A 1 63  ? 32.104 10.879  6.758   1.00 14.80 ?  63  VAL   A H    1 
ATOM   1591 H HA   . VAL   A 1 63  ? 34.339 11.538  5.606   1.00 15.75 ?  63  VAL   A HA   1 
ATOM   1592 H HB   . VAL   A 1 63  ? 33.724 11.433  8.364   1.00 17.36 ?  63  VAL   A HB   1 
ATOM   1593 H HG11 . VAL   A 1 63  ? 35.638 12.874  8.609   1.00 19.53 ?  63  VAL   A HG11 1 
ATOM   1594 H HG12 . VAL   A 1 63  ? 35.961 11.335  8.393   1.00 19.53 ?  63  VAL   A HG12 1 
ATOM   1595 H HG13 . VAL   A 1 63  ? 36.088 12.353  7.179   1.00 19.53 ?  63  VAL   A HG13 1 
ATOM   1596 H HG21 . VAL   A 1 63  ? 33.519 13.758  8.185   1.00 17.89 ?  63  VAL   A HG21 1 
ATOM   1597 H HG22 . VAL   A 1 63  ? 33.830 13.658  6.630   1.00 17.89 ?  63  VAL   A HG22 1 
ATOM   1598 H HG23 . VAL   A 1 63  ? 32.493 13.030  7.215   1.00 17.89 ?  63  VAL   A HG23 1 
ATOM   1599 N N    . GLU   A 1 64  ? 34.501 8.768   7.212   1.00 11.80 ?  64  GLU   A N    1 
ATOM   1600 C CA   . GLU   A 1 64  ? 35.256 7.525   7.309   1.00 12.42 ?  64  GLU   A CA   1 
ATOM   1601 C C    . GLU   A 1 64  ? 35.346 6.839   5.953   1.00 12.03 ?  64  GLU   A C    1 
ATOM   1602 O O    . GLU   A 1 64  ? 36.397 6.289   5.584   1.00 12.24 ?  64  GLU   A O    1 
ATOM   1603 C CB   . GLU   A 1 64  ? 34.566 6.610   8.328   1.00 13.08 ?  64  GLU   A CB   1 
ATOM   1604 C CG   . GLU   A 1 64  ? 35.213 5.260   8.476   1.00 14.21 ?  64  GLU   A CG   1 
ATOM   1605 C CD   . GLU   A 1 64  ? 34.333 4.274   9.212   1.00 14.84 ?  64  GLU   A CD   1 
ATOM   1606 O OE1  . GLU   A 1 64  ? 33.093 4.364   9.084   1.00 15.13 ?  64  GLU   A OE1  1 
ATOM   1607 O OE2  . GLU   A 1 64  ? 34.879 3.385   9.898   1.00 14.77 -1 64  GLU   A OE2  1 
ATOM   1608 H H    . GLU   A 1 64  ? 33.771 8.783   7.675   1.00 14.19 ?  64  GLU   A H    1 
ATOM   1609 H HA   . GLU   A 1 64  ? 36.149 7.718   7.629   1.00 14.93 ?  64  GLU   A HA   1 
ATOM   1610 H HB2  . GLU   A 1 64  ? 34.584 7.044   9.204   1.00 15.72 ?  64  GLU   A HB2  1 
ATOM   1611 H HB3  . GLU   A 1 64  ? 33.642 6.480   8.057   1.00 15.72 ?  64  GLU   A HB3  1 
ATOM   1612 H HG2  . GLU   A 1 64  ? 35.399 4.893   7.595   1.00 17.07 ?  64  GLU   A HG2  1 
ATOM   1613 H HG3  . GLU   A 1 64  ? 36.031 5.357   8.976   1.00 17.07 ?  64  GLU   A HG3  1 
ATOM   1614 N N    . SER   A 1 65  ? 34.235 6.833   5.217   1.00 11.44 ?  65  SER   A N    1 
ATOM   1615 C CA   . SER   A 1 65  ? 34.187 6.172   3.921   1.00 11.72 ?  65  SER   A CA   1 
ATOM   1616 C C    . SER   A 1 65  ? 35.124 6.828   2.916   1.00 11.88 ?  65  SER   A C    1 
ATOM   1617 O O    . SER   A 1 65  ? 35.765 6.141   2.117   1.00 12.75 ?  65  SER   A O    1 
ATOM   1618 C CB   . SER   A 1 65  ? 32.757 6.180   3.381   1.00 12.36 ?  65  SER   A CB   1 
ATOM   1619 O OG   . SER   A 1 65  ? 31.891 5.358   4.160   1.00 11.79 ?  65  SER   A OG   1 
ATOM   1620 H H    . SER   A 1 65  ? 33.497 7.215   5.447   1.00 13.75 ?  65  SER   A H    1 
ATOM   1621 H HA   . SER   A 1 65  ? 34.463 5.250   4.028   1.00 14.09 ?  65  SER   A HA   1 
ATOM   1622 H HB2  . SER   A 1 65  ? 32.421 7.090   3.395   1.00 14.86 ?  65  SER   A HB2  1 
ATOM   1623 H HB3  . SER   A 1 65  ? 32.767 5.848   2.470   1.00 14.86 ?  65  SER   A HB3  1 
ATOM   1624 H HG   . SER   A 1 65  ? 31.874 5.636   4.957   1.00 14.17 ?  65  SER   A HG   1 
ATOM   1625 N N    . ASP   A 1 66  ? 35.193 8.160   2.913   1.00 11.53 ?  66  ASP   A N    1 
ATOM   1626 C CA   . ASP   A 1 66  ? 36.066 8.840   1.964   1.00 12.92 ?  66  ASP   A CA   1 
ATOM   1627 C C    . ASP   A 1 66  ? 37.525 8.496   2.224   1.00 13.18 ?  66  ASP   A C    1 
ATOM   1628 O O    . ASP   A 1 66  ? 38.308 8.320   1.283   1.00 13.70 ?  66  ASP   A O    1 
ATOM   1629 C CB   . ASP   A 1 66  ? 35.853 10.352  2.042   1.00 14.22 ?  66  ASP   A CB   1 
ATOM   1630 C CG   . ASP   A 1 66  ? 34.514 10.811  1.449   1.00 16.04 ?  66  ASP   A CG   1 
ATOM   1631 O OD1  . ASP   A 1 66  ? 33.808 10.020  0.783   1.00 16.32 ?  66  ASP   A OD1  1 
ATOM   1632 O OD2  . ASP   A 1 66  ? 34.204 12.012  1.616   1.00 19.07 -1 66  ASP   A OD2  1 
ATOM   1633 H H    . ASP   A 1 66  ? 34.754 8.683   3.443   1.00 13.86 ?  66  ASP   A H    1 
ATOM   1634 H HA   . ASP   A 1 66  ? 35.842 8.553   1.067   1.00 15.52 ?  66  ASP   A HA   1 
ATOM   1635 H HB2  . ASP   A 1 66  ? 35.876 10.628  2.970   1.00 17.08 ?  66  ASP   A HB2  1 
ATOM   1636 H HB3  . ASP   A 1 66  ? 36.563 10.795  1.547   1.00 17.08 ?  66  ASP   A HB3  1 
ATOM   1637 N N    . ASP   A 1 67  ? 37.907 8.383   3.496   1.00 13.28 ?  67  ASP   A N    1 
ATOM   1638 C CA   . ASP   A 1 67  ? 39.261 7.938   3.811   1.00 13.93 ?  67  ASP   A CA   1 
ATOM   1639 C C    . ASP   A 1 67  ? 39.490 6.502   3.347   1.00 13.75 ?  67  ASP   A C    1 
ATOM   1640 O O    . ASP   A 1 67  ? 40.557 6.179   2.811   1.00 14.10 ?  67  ASP   A O    1 
ATOM   1641 C CB   . ASP   A 1 67  ? 39.524 8.084   5.309   1.00 14.97 ?  67  ASP   A CB   1 
ATOM   1642 C CG   . ASP   A 1 67  ? 40.817 7.423   5.737   1.00 16.49 ?  67  ASP   A CG   1 
ATOM   1643 O OD1  . ASP   A 1 67  ? 41.891 8.060   5.612   1.00 19.33 ?  67  ASP   A OD1  1 
ATOM   1644 O OD2  . ASP   A 1 67  ? 40.765 6.259   6.194   1.00 16.10 -1 67  ASP   A OD2  1 
ATOM   1645 H H    . ASP   A 1 67  ? 37.416 8.556   4.177   1.00 15.96 ?  67  ASP   A H    1 
ATOM   1646 H HA   . ASP   A 1 67  ? 39.896 8.505   3.344   1.00 16.74 ?  67  ASP   A HA   1 
ATOM   1647 H HB2  . ASP   A 1 67  ? 39.580 9.022   5.530   1.00 17.99 ?  67  ASP   A HB2  1 
ATOM   1648 H HB3  . ASP   A 1 67  ? 38.799 7.664   5.798   1.00 17.99 ?  67  ASP   A HB3  1 
ATOM   1649 N N    . TYR   A 1 68  ? 38.495 5.623   3.533   1.00 13.54 ?  68  TYR   A N    1 
ATOM   1650 C CA   . TYR   A 1 68  ? 38.615 4.241   3.060   1.00 13.73 ?  68  TYR   A CA   1 
ATOM   1651 C C    . TYR   A 1 68  ? 38.866 4.189   1.553   1.00 13.47 ?  68  TYR   A C    1 
ATOM   1652 O O    . TYR   A 1 68  ? 39.752 3.459   1.079   1.00 13.74 ?  68  TYR   A O    1 
ATOM   1653 C CB   . TYR   A 1 68  ? 37.364 3.419   3.430   1.00 14.06 ?  68  TYR   A CB   1 
ATOM   1654 C CG   . TYR   A 1 68  ? 37.398 2.028   2.810   1.00 15.29 ?  68  TYR   A CG   1 
ATOM   1655 C CD1  . TYR   A 1 68  ? 36.939 1.823   1.512   1.00 16.68 ?  68  TYR   A CD1  1 
ATOM   1656 C CD2  . TYR   A 1 68  ? 37.930 0.948   3.490   1.00 17.02 ?  68  TYR   A CD2  1 
ATOM   1657 C CE1  . TYR   A 1 68  ? 37.005 0.605   0.905   1.00 18.44 ?  68  TYR   A CE1  1 
ATOM   1658 C CE2  . TYR   A 1 68  ? 38.001 -0.313  2.880   1.00 18.10 ?  68  TYR   A CE2  1 
ATOM   1659 C CZ   . TYR   A 1 68  ? 37.539 -0.464  1.588   1.00 19.04 ?  68  TYR   A CZ   1 
ATOM   1660 O OH   . TYR   A 1 68  ? 37.615 -1.688  0.968   1.00 21.11 ?  68  TYR   A OH   1 
ATOM   1661 H H    . TYR   A 1 68  ? 37.750 5.801   3.927   1.00 16.26 ?  68  TYR   A H    1 
ATOM   1662 H HA   . TYR   A 1 68  ? 39.373 3.829   3.496   1.00 16.50 ?  68  TYR   A HA   1 
ATOM   1663 H HB2  . TYR   A 1 68  ? 37.319 3.317   4.394   1.00 16.89 ?  68  TYR   A HB2  1 
ATOM   1664 H HB3  . TYR   A 1 68  ? 36.569 3.876   3.106   1.00 16.89 ?  68  TYR   A HB3  1 
ATOM   1665 H HD1  . TYR   A 1 68  ? 36.590 2.550   1.039   1.00 20.03 ?  68  TYR   A HD1  1 
ATOM   1666 H HD2  . TYR   A 1 68  ? 38.260 1.058   4.349   1.00 20.44 ?  68  TYR   A HD2  1 
ATOM   1667 H HE1  . TYR   A 1 68  ? 36.685 0.496   0.039   1.00 22.15 ?  68  TYR   A HE1  1 
ATOM   1668 H HE2  . TYR   A 1 68  ? 38.358 -1.042  3.330   1.00 21.74 ?  68  TYR   A HE2  1 
ATOM   1669 H HH   . TYR   A 1 68  ? 37.939 -2.253  1.493   1.00 25.36 ?  68  TYR   A HH   1 
ATOM   1670 N N    . ILE   A 1 69  ? 38.081 4.946   0.778   1.00 12.50 ?  69  ILE   A N    1 
ATOM   1671 C CA   . ILE   A 1 69  ? 38.221 4.927   -0.676  1.00 12.72 ?  69  ILE   A CA   1 
ATOM   1672 C C    . ILE   A 1 69  ? 39.554 5.538   -1.098  1.00 12.66 ?  69  ILE   A C    1 
ATOM   1673 O O    . ILE   A 1 69  ? 40.202 5.060   -2.034  1.00 12.85 ?  69  ILE   A O    1 
ATOM   1674 C CB   . ILE   A 1 69  ? 37.022 5.624   -1.354  1.00 13.77 ?  69  ILE   A CB   1 
ATOM   1675 C CG1  . ILE   A 1 69  ? 35.706 4.891   -1.068  1.00 14.28 ?  69  ILE   A CG1  1 
ATOM   1676 C CG2  . ILE   A 1 69  ? 37.254 5.772   -2.865  1.00 15.72 ?  69  ILE   A CG2  1 
ATOM   1677 C CD1  . ILE   A 1 69  ? 35.560 3.594   -1.824  1.00 15.47 ?  69  ILE   A CD1  1 
ATOM   1678 H H    . ILE   A 1 69  ? 37.467 5.480   1.068   1.00 15.02 ?  69  ILE   A H    1 
ATOM   1679 H HA   . ILE   A 1 69  ? 38.223 4.007   -0.969  1.00 15.28 ?  69  ILE   A HA   1 
ATOM   1680 H HB   . ILE   A 1 69  ? 36.945 6.513   -0.984  1.00 16.55 ?  69  ILE   A HB   1 
ATOM   1681 H HG12 . ILE   A 1 69  ? 35.664 4.687   -0.119  1.00 17.16 ?  69  ILE   A HG12 1 
ATOM   1682 H HG13 . ILE   A 1 69  ? 34.966 5.466   -1.313  1.00 17.16 ?  69  ILE   A HG13 1 
ATOM   1683 H HG21 . ILE   A 1 69  ? 36.407 5.977   -3.298  1.00 18.88 ?  69  ILE   A HG21 1 
ATOM   1684 H HG22 . ILE   A 1 69  ? 37.883 6.496   -3.021  1.00 18.88 ?  69  ILE   A HG22 1 
ATOM   1685 H HG23 . ILE   A 1 69  ? 37.609 4.942   -3.218  1.00 18.88 ?  69  ILE   A HG23 1 
ATOM   1686 H HD11 . ILE   A 1 69  ? 34.782 3.122   -1.481  1.00 18.59 ?  69  ILE   A HD11 1 
ATOM   1687 H HD12 . ILE   A 1 69  ? 35.432 3.790   -2.765  1.00 18.59 ?  69  ILE   A HD12 1 
ATOM   1688 H HD13 . ILE   A 1 69  ? 36.353 3.058   -1.697  1.00 18.59 ?  69  ILE   A HD13 1 
ATOM   1689 N N    . ALA   A 1 70  ? 39.969 6.619   -0.440  1.00 13.27 ?  70  ALA   A N    1 
ATOM   1690 C CA   . ALA   A 1 70  ? 41.248 7.231   -0.784  1.00 14.01 ?  70  ALA   A CA   1 
ATOM   1691 C C    . ALA   A 1 70  ? 42.402 6.255   -0.608  1.00 14.30 ?  70  ALA   A C    1 
ATOM   1692 O O    . ALA   A 1 70  ? 43.390 6.323   -1.344  1.00 16.49 ?  70  ALA   A O    1 
ATOM   1693 C CB   . ALA   A 1 70  ? 41.486 8.487   0.059   1.00 15.04 ?  70  ALA   A CB   1 
ATOM   1694 H H    . ALA   A 1 70  ? 39.538 7.014   0.186   1.00 15.95 ?  70  ALA   A H    1 
ATOM   1695 H HA   . ALA   A 1 70  ? 41.233 7.505   -1.719  1.00 16.84 ?  70  ALA   A HA   1 
ATOM   1696 H HB1  . ALA   A 1 70  ? 42.345 8.873   -0.184  1.00 18.07 ?  70  ALA   A HB1  1 
ATOM   1697 H HB2  . ALA   A 1 70  ? 40.777 9.122   -0.114  1.00 18.07 ?  70  ALA   A HB2  1 
ATOM   1698 H HB3  . ALA   A 1 70  ? 41.491 8.237   0.995   1.00 18.07 ?  70  ALA   A HB3  1 
ATOM   1699 N N    . THR   A 1 71  ? 42.295 5.347   0.354   1.00 13.67 ?  71  THR   A N    1 
ATOM   1700 C CA   . THR   A 1 71  ? 43.344 4.371   0.613   1.00 15.74 ?  71  THR   A CA   1 
ATOM   1701 C C    . THR   A 1 71  ? 43.229 3.139   -0.273  1.00 16.20 ?  71  THR   A C    1 
ATOM   1702 O O    . THR   A 1 71  ? 44.246 2.628   -0.764  1.00 18.52 ?  71  THR   A O    1 
ATOM   1703 C CB   . THR   A 1 71  ? 43.261 3.932   2.073   1.00 18.25 ?  71  THR   A CB   1 
ATOM   1704 O OG1  . THR   A 1 71  ? 43.473 5.067   2.920   1.00 19.72 ?  71  THR   A OG1  1 
ATOM   1705 C CG2  . THR   A 1 71  ? 44.283 2.851   2.385   1.00 19.71 ?  71  THR   A CG2  1 
ATOM   1706 H H    . THR   A 1 71  ? 41.613 5.269   0.871   1.00 16.43 ?  71  THR   A H    1 
ATOM   1707 H HA   . THR   A 1 71  ? 44.213 4.776   0.460   1.00 18.92 ?  71  THR   A HA   1 
ATOM   1708 H HB   . THR   A 1 71  ? 42.375 3.563   2.237   1.00 21.92 ?  71  THR   A HB   1 
ATOM   1709 H HG1  . THR   A 1 71  ? 42.875 5.639   2.770   1.00 23.69 ?  71  THR   A HG1  1 
ATOM   1710 H HG21 . THR   A 1 71  ? 44.386 2.764   3.346   1.00 23.68 ?  71  THR   A HG21 1 
ATOM   1711 H HG22 . THR   A 1 71  ? 43.998 1.997   2.022   1.00 23.68 ?  71  THR   A HG22 1 
ATOM   1712 H HG23 . THR   A 1 71  ? 45.143 3.086   2.000   1.00 23.68 ?  71  THR   A HG23 1 
ATOM   1713 N N    . ASN   A 1 72  ? 42.008 2.641   -0.479  1.00 14.58 ?  72  ASN   A N    1 
ATOM   1714 C CA   . ASN   A 1 72  ? 41.795 1.315   -1.043  1.00 15.46 ?  72  ASN   A CA   1 
ATOM   1715 C C    . ASN   A 1 72  ? 41.180 1.303   -2.430  1.00 15.47 ?  72  ASN   A C    1 
ATOM   1716 O O    . ASN   A 1 72  ? 41.180 0.242   -3.074  1.00 16.62 ?  72  ASN   A O    1 
ATOM   1717 C CB   . ASN   A 1 72  ? 40.905 0.493   -0.108  1.00 16.49 ?  72  ASN   A CB   1 
ATOM   1718 C CG   . ASN   A 1 72  ? 41.515 0.337   1.255   1.00 17.91 ?  72  ASN   A CG   1 
ATOM   1719 O OD1  . ASN   A 1 72  ? 41.054 0.912   2.234   1.00 20.01 ?  72  ASN   A OD1  1 
ATOM   1720 N ND2  . ASN   A 1 72  ? 42.577 -0.427  1.323   1.00 18.23 ?  72  ASN   A ND2  1 
ATOM   1721 H H    . ASN   A 1 72  ? 41.276 3.058   -0.289  1.00 17.52 ?  72  ASN   A H    1 
ATOM   1722 H HA   . ASN   A 1 72  ? 42.651 0.869   -1.106  1.00 18.58 ?  72  ASN   A HA   1 
ATOM   1723 H HB2  . ASN   A 1 72  ? 40.048 0.934   -0.011  1.00 19.81 ?  72  ASN   A HB2  1 
ATOM   1724 H HB3  . ASN   A 1 72  ? 40.784 -0.394  -0.486  1.00 19.81 ?  72  ASN   A HB3  1 
ATOM   1725 H HD21 . ASN   A 1 72  ? 42.975 -0.545  2.079   1.00 21.90 ?  72  ASN   A HD21 1 
ATOM   1726 H HD22 . ASN   A 1 72  ? 42.886 -0.806  0.615   1.00 21.90 ?  72  ASN   A HD22 1 
ATOM   1727 N N    . GLY   A 1 73  ? 40.633 2.418   -2.895  1.00 14.87 ?  73  GLY   A N    1 
ATOM   1728 C CA   . GLY   A 1 73  ? 39.907 2.417   -4.138  1.00 14.48 ?  73  GLY   A CA   1 
ATOM   1729 C C    . GLY   A 1 73  ? 38.514 1.847   -3.964  1.00 13.90 ?  73  GLY   A C    1 
ATOM   1730 O O    . GLY   A 1 73  ? 38.120 1.411   -2.876  1.00 14.02 ?  73  GLY   A O    1 
ATOM   1731 H H    . GLY   A 1 73  ? 40.684 3.194   -2.515  1.00 17.87 ?  73  GLY   A H    1 
ATOM   1732 H HA2  . GLY   A 1 73  ? 39.835 3.334   -4.467  1.00 17.40 ?  73  GLY   A HA2  1 
ATOM   1733 H HA3  . GLY   A 1 73  ? 40.384 1.894   -4.798  1.00 17.40 ?  73  GLY   A HA3  1 
ATOM   1734 N N    . PRO   A 1 74  ? 37.741 1.856   -5.046  1.00 14.41 ?  74  PRO   A N    1 
ATOM   1735 C CA   . PRO   A 1 74  ? 36.341 1.429   -4.965  1.00 14.86 ?  74  PRO   A CA   1 
ATOM   1736 C C    . PRO   A 1 74  ? 36.189 -0.053  -4.652  1.00 14.05 ?  74  PRO   A C    1 
ATOM   1737 O O    . PRO   A 1 74  ? 37.058 -0.883  -4.933  1.00 14.64 ?  74  PRO   A O    1 
ATOM   1738 C CB   . PRO   A 1 74  ? 35.798 1.728   -6.366  1.00 16.14 ?  74  PRO   A CB   1 
ATOM   1739 C CG   . PRO   A 1 74  ? 36.744 2.696   -6.971  1.00 18.98 ?  74  PRO   A CG   1 
ATOM   1740 C CD   . PRO   A 1 74  ? 38.081 2.388   -6.376  1.00 16.46 ?  74  PRO   A CD   1 
ATOM   1741 H HA   . PRO   A 1 74  ? 35.863 1.956   -4.304  1.00 17.85 ?  74  PRO   A HA   1 
ATOM   1742 H HB2  . PRO   A 1 74  ? 35.766 0.908   -6.880  1.00 19.39 ?  74  PRO   A HB2  1 
ATOM   1743 H HB3  . PRO   A 1 74  ? 34.910 2.117   -6.289  1.00 19.39 ?  74  PRO   A HB3  1 
ATOM   1744 H HG2  . PRO   A 1 74  ? 36.764 2.576   -7.932  1.00 22.80 ?  74  PRO   A HG2  1 
ATOM   1745 H HG3  . PRO   A 1 74  ? 36.474 3.601   -6.745  1.00 22.80 ?  74  PRO   A HG3  1 
ATOM   1746 H HD2  . PRO   A 1 74  ? 38.543 1.717   -6.906  1.00 19.77 ?  74  PRO   A HD2  1 
ATOM   1747 H HD3  . PRO   A 1 74  ? 38.608 3.201   -6.301  1.00 19.77 ?  74  PRO   A HD3  1 
ATOM   1748 N N    . LEU   A 1 75  ? 35.031 -0.378  -4.083  1.00 12.87 ?  75  LEU   A N    1 
ATOM   1749 C CA   . LEU   A 1 75  ? 34.641 -1.769  -3.938  1.00 12.74 ?  75  LEU   A CA   1 
ATOM   1750 C C    . LEU   A 1 75  ? 34.256 -2.338  -5.300  1.00 13.41 ?  75  LEU   A C    1 
ATOM   1751 O O    . LEU   A 1 75  ? 34.121 -1.614  -6.288  1.00 14.30 ?  75  LEU   A O    1 
ATOM   1752 C CB   . LEU   A 1 75  ? 33.451 -1.892  -2.986  1.00 13.19 ?  75  LEU   A CB   1 
ATOM   1753 C CG   . LEU   A 1 75  ? 33.659 -1.485  -1.533  1.00 14.51 ?  75  LEU   A CG   1 
ATOM   1754 C CD1  . LEU   A 1 75  ? 32.378 -1.692  -0.736  1.00 16.62 ?  75  LEU   A CD1  1 
ATOM   1755 C CD2  . LEU   A 1 75  ? 34.796 -2.210  -0.876  1.00 17.73 ?  75  LEU   A CD2  1 
ATOM   1756 H H    . LEU   A 1 75  ? 34.456 0.188   -3.782  1.00 15.46 ?  75  LEU   A H    1 
ATOM   1757 H HA   . LEU   A 1 75  ? 35.383 -2.279  -3.594  1.00 15.31 ?  75  LEU   A HA   1 
ATOM   1758 H HB2  . LEU   A 1 75  ? 32.731 -1.352  -3.334  1.00 15.85 ?  75  LEU   A HB2  1 
ATOM   1759 H HB3  . LEU   A 1 75  ? 33.177 -2.825  -2.981  1.00 15.85 ?  75  LEU   A HB3  1 
ATOM   1760 H HG   . LEU   A 1 75  ? 33.873 -0.537  -1.509  1.00 17.44 ?  75  LEU   A HG   1 
ATOM   1761 H HD11 . LEU   A 1 75  ? 32.531 -1.419  0.183   1.00 19.97 ?  75  LEU   A HD11 1 
ATOM   1762 H HD12 . LEU   A 1 75  ? 31.677 -1.146  -1.129  1.00 19.97 ?  75  LEU   A HD12 1 
ATOM   1763 H HD13 . LEU   A 1 75  ? 32.132 -2.625  -0.771  1.00 19.97 ?  75  LEU   A HD13 1 
ATOM   1764 H HD21 . LEU   A 1 75  ? 34.852 -1.938  0.056   1.00 21.30 ?  75  LEU   A HD21 1 
ATOM   1765 H HD22 . LEU   A 1 75  ? 34.644 -3.163  -0.934  1.00 21.30 ?  75  LEU   A HD22 1 
ATOM   1766 H HD23 . LEU   A 1 75  ? 35.629 -1.980  -1.329  1.00 21.30 ?  75  LEU   A HD23 1 
ATOM   1767 N N    . LYS   A 1 76  ? 34.086 -3.659  -5.334  1.00 13.74 ?  76  LYS   A N    1 
ATOM   1768 C CA   . LYS   A 1 76  ? 33.488 -4.376  -6.454  1.00 14.29 ?  76  LYS   A CA   1 
ATOM   1769 C C    . LYS   A 1 76  ? 31.977 -4.445  -6.267  1.00 13.12 ?  76  LYS   A C    1 
ATOM   1770 O O    . LYS   A 1 76  ? 31.489 -4.554  -5.145  1.00 12.70 ?  76  LYS   A O    1 
ATOM   1771 C CB   . LYS   A 1 76  ? 34.021 -5.817  -6.496  1.00 15.62 ?  76  LYS   A CB   1 
ATOM   1772 C CG   . LYS   A 1 76  ? 35.522 -5.922  -6.705  1.00 17.00 ?  76  LYS   A CG   1 
ATOM   1773 C CD   . LYS   A 1 76  ? 36.033 -7.328  -6.468  1.00 18.16 ?  76  LYS   A CD   1 
ATOM   1774 C CE   . LYS   A 1 76  ? 37.531 -7.404  -6.676  1.00 20.51 ?  76  LYS   A CE   1 
ATOM   1775 N NZ   . LYS   A 1 76  ? 38.070 -8.747  -6.380  1.00 21.32 ?  76  LYS   A NZ   1 
ATOM   1776 H H    . LYS   A 1 76  ? 34.322 -4.183  -4.693  1.00 16.51 ?  76  LYS   A H    1 
ATOM   1777 H HA   . LYS   A 1 76  ? 33.694 -3.933  -7.294  1.00 17.17 ?  76  LYS   A HA   1 
ATOM   1778 H HB2  . LYS   A 1 76  ? 33.810 -6.249  -5.653  1.00 18.76 ?  76  LYS   A HB2  1 
ATOM   1779 H HB3  . LYS   A 1 76  ? 33.589 -6.288  -7.224  1.00 18.76 ?  76  LYS   A HB3  1 
ATOM   1780 H HG2  . LYS   A 1 76  ? 35.738 -5.672  -7.617  1.00 20.43 ?  76  LYS   A HG2  1 
ATOM   1781 H HG3  . LYS   A 1 76  ? 35.977 -5.330  -6.082  1.00 20.43 ?  76  LYS   A HG3  1 
ATOM   1782 H HD2  . LYS   A 1 76  ? 35.834 -7.595  -5.556  1.00 21.82 ?  76  LYS   A HD2  1 
ATOM   1783 H HD3  . LYS   A 1 76  ? 35.604 -7.936  -7.095  1.00 21.82 ?  76  LYS   A HD3  1 
ATOM   1784 H HE2  . LYS   A 1 76  ? 37.734 -7.198  -7.600  1.00 24.63 ?  76  LYS   A HE2  1 
ATOM   1785 H HE3  . LYS   A 1 76  ? 37.965 -6.774  -6.085  1.00 24.63 ?  76  LYS   A HE3  1 
ATOM   1786 H HZ1  . LYS   A 1 76  ? 38.951 -8.766  -6.512  1.00 25.61 ?  76  LYS   A HZ1  1 
ATOM   1787 H HZ2  . LYS   A 1 76  ? 37.903 -8.972  -5.533  1.00 25.61 ?  76  LYS   A HZ2  1 
ATOM   1788 H HZ3  . LYS   A 1 76  ? 37.692 -9.359  -6.913  1.00 25.61 ?  76  LYS   A HZ3  1 
ATOM   1789 N N    . VAL   A 1 77  ? 31.230 -4.417  -7.376  1.00 13.46 ?  77  VAL   A N    1 
ATOM   1790 C CA   . VAL   A 1 77  ? 29.824 -4.799  -7.288  1.00 13.00 ?  77  VAL   A CA   1 
ATOM   1791 C C    . VAL   A 1 77  ? 29.758 -6.255  -6.843  1.00 12.71 ?  77  VAL   A C    1 
ATOM   1792 O O    . VAL   A 1 77  ? 30.412 -7.131  -7.423  1.00 13.42 ?  77  VAL   A O    1 
ATOM   1793 C CB   . VAL   A 1 77  ? 29.097 -4.582  -8.622  1.00 14.34 ?  77  VAL   A CB   1 
ATOM   1794 C CG1  . VAL   A 1 77  ? 27.635 -5.006  -8.508  1.00 15.25 ?  77  VAL   A CG1  1 
ATOM   1795 C CG2  . VAL   A 1 77  ? 29.210 -3.128  -9.061  1.00 16.10 ?  77  VAL   A CG2  1 
ATOM   1796 H H    . VAL   A 1 77  ? 31.507 -4.187  -8.157  1.00 16.17 ?  77  VAL   A H    1 
ATOM   1797 H HA   . VAL   A 1 77  ? 29.390 -4.251  -6.612  1.00 15.63 ?  77  VAL   A HA   1 
ATOM   1798 H HB   . VAL   A 1 77  ? 29.518 -5.130  -9.300  1.00 17.23 ?  77  VAL   A HB   1 
ATOM   1799 H HG11 . VAL   A 1 77  ? 27.160 -4.697  -9.292  1.00 18.32 ?  77  VAL   A HG11 1 
ATOM   1800 H HG12 . VAL   A 1 77  ? 27.592 -5.972  -8.451  1.00 18.32 ?  77  VAL   A HG12 1 
ATOM   1801 H HG13 . VAL   A 1 77  ? 27.256 -4.607  -7.710  1.00 18.32 ?  77  VAL   A HG13 1 
ATOM   1802 H HG21 . VAL   A 1 77  ? 28.690 -3.002  -9.869  1.00 19.34 ?  77  VAL   A HG21 1 
ATOM   1803 H HG22 . VAL   A 1 77  ? 28.872 -2.557  -8.354  1.00 19.34 ?  77  VAL   A HG22 1 
ATOM   1804 H HG23 . VAL   A 1 77  ? 30.144 -2.921  -9.234  1.00 19.34 ?  77  VAL   A HG23 1 
ATOM   1805 N N    . GLY   A 1 78  ? 28.974 -6.517  -5.798  1.00 12.19 ?  78  GLY   A N    1 
ATOM   1806 C CA   . GLY   A 1 78  ? 28.946 -7.804  -5.141  1.00 12.52 ?  78  GLY   A CA   1 
ATOM   1807 C C    . GLY   A 1 78  ? 29.850 -7.891  -3.934  1.00 12.01 ?  78  GLY   A C    1 
ATOM   1808 O O    . GLY   A 1 78  ? 29.790 -8.897  -3.207  1.00 12.98 ?  78  GLY   A O    1 
ATOM   1809 H H    . GLY   A 1 78  ? 28.424 -5.939  -5.457  1.00 14.65 ?  78  GLY   A H    1 
ATOM   1810 H HA2  . GLY   A 1 78  ? 28.038 -7.994  -4.858  1.00 15.04 ?  78  GLY   A HA2  1 
ATOM   1811 H HA3  . GLY   A 1 78  ? 29.216 -8.485  -5.774  1.00 15.04 ?  78  GLY   A HA3  1 
ATOM   1812 N N    . GLY   A 1 79  ? 30.704 -6.883  -3.710  1.00 11.89 ?  79  GLY   A N    1 
ATOM   1813 C CA   . GLY   A 1 79  ? 31.654 -6.899  -2.622  1.00 12.16 ?  79  GLY   A CA   1 
ATOM   1814 C C    . GLY   A 1 79  ? 31.196 -6.105  -1.406  1.00 11.31 ?  79  GLY   A C    1 
ATOM   1815 O O    . GLY   A 1 79  ? 30.084 -5.586  -1.343  1.00 12.37 ?  79  GLY   A O    1 
ATOM   1816 H H    . GLY   A 1 79  ? 30.745 -6.166  -4.191  1.00 14.28 ?  79  GLY   A H    1 
ATOM   1817 H HA2  . GLY   A 1 79  ? 31.810 -7.819  -2.352  1.00 14.62 ?  79  GLY   A HA2  1 
ATOM   1818 H HA3  . GLY   A 1 79  ? 32.500 -6.532  -2.934  1.00 14.62 ?  79  GLY   A HA3  1 
ATOM   1819 N N    . SER   A 1 80  ? 32.093 -6.021  -0.424  1.00 12.39 ?  80  SER   A N    1 
ATOM   1820 C CA   . SER   A 1 80  ? 31.764 -5.379  0.838   1.00 12.21 ?  80  SER   A CA   1 
ATOM   1821 C C    . SER   A 1 80  ? 33.031 -4.927  1.545   1.00 12.01 ?  80  SER   A C    1 
ATOM   1822 O O    . SER   A 1 80  ? 34.142 -5.364  1.229   1.00 13.54 ?  80  SER   A O    1 
ATOM   1823 C CB   . SER   A 1 80  ? 30.989 -6.332  1.754   1.00 13.27 ?  80  SER   A CB   1 
ATOM   1824 O OG   . SER   A 1 80  ? 31.812 -7.390  2.228   1.00 14.84 ?  80  SER   A OG   1 
ATOM   1825 H H    . SER   A 1 80  ? 32.903 -6.324  -0.470  1.00 14.89 ?  80  SER   A H    1 
ATOM   1826 H HA   . SER   A 1 80  ? 31.216 -4.600  0.649   1.00 14.67 ?  80  SER   A HA   1 
ATOM   1827 H HB2  . SER   A 1 80  ? 30.655 -5.829  2.512   1.00 15.94 ?  80  SER   A HB2  1 
ATOM   1828 H HB3  . SER   A 1 80  ? 30.245 -6.707  1.255   1.00 15.94 ?  80  SER   A HB3  1 
ATOM   1829 H HG   . SER   A 1 80  ? 32.103 -7.835  1.575   1.00 17.83 ?  80  SER   A HG   1 
ATOM   1830 N N    . CYS   A 1 81  ? 32.835 -4.081  2.550   1.00 11.57 ?  81  CYS   A N    1 
ATOM   1831 C CA   . CYS   A 1 81  ? 33.877 -3.792  3.524   1.00 12.30 ?  81  CYS   A CA   1 
ATOM   1832 C C    . CYS   A 1 81  ? 33.229 -3.558  4.882   1.00 12.33 ?  81  CYS   A C    1 
ATOM   1833 O O    . CYS   A 1 81  ? 32.065 -3.151  4.972   1.00 13.06 ?  81  CYS   A O    1 
ATOM   1834 C CB   . CYS   A 1 81  ? 34.756 -2.600  3.118   1.00 13.03 ?  81  CYS   A CB   1 
ATOM   1835 S SG   . CYS   A 1 81  ? 33.863 -1.030  3.103   1.00 13.03 ?  81  CYS   A SG   1 
ATOM   1836 H H    . CYS   A 1 81  ? 32.096 -3.662  2.699   1.00 13.91 ?  81  CYS   A H    1 
ATOM   1837 H HA   . CYS   A 1 81  ? 34.456 -4.568  3.599   1.00 14.79 ?  81  CYS   A HA   1 
ATOM   1838 H HB2  . CYS   A 1 81  ? 35.494 -2.524  3.751   1.00 15.65 ?  81  CYS   A HB2  1 
ATOM   1839 H HB3  . CYS   A 1 81  ? 35.110 -2.755  2.226   1.00 15.65 ?  81  CYS   A HB3  1 
ATOM   1840 H HG   . CYS   A 1 81  ? 34.615 -0.151  2.785   1.00 15.65 ?  81  CYS   A HG   1 
ATOM   1841 N N    . VAL   A 1 82  ? 34.000 -3.816  5.937   1.00 12.55 ?  82  VAL   A N    1 
ATOM   1842 C CA   . VAL   A 1 82  ? 33.575 -3.577  7.308   1.00 12.70 ?  82  VAL   A CA   1 
ATOM   1843 C C    . VAL   A 1 82  ? 34.165 -2.261  7.783   1.00 12.89 ?  82  VAL   A C    1 
ATOM   1844 O O    . VAL   A 1 82  ? 35.390 -2.090  7.776   1.00 13.66 ?  82  VAL   A O    1 
ATOM   1845 C CB   . VAL   A 1 82  ? 34.002 -4.717  8.242   1.00 14.29 ?  82  VAL   A CB   1 
ATOM   1846 C CG1  . VAL   A 1 82  ? 33.540 -4.443  9.660   1.00 16.36 ?  82  VAL   A CG1  1 
ATOM   1847 C CG2  . VAL   A 1 82  ? 33.464 -6.046  7.746   1.00 15.71 ?  82  VAL   A CG2  1 
ATOM   1848 H H    . VAL   A 1 82  ? 34.800 -4.147  5.879   1.00 15.08 ?  82  VAL   A H    1 
ATOM   1849 H HA   . VAL   A 1 82  ? 32.607 -3.499  7.330   1.00 15.27 ?  82  VAL   A HA   1 
ATOM   1850 H HB   . VAL   A 1 82  ? 34.970 -4.762  8.248   1.00 17.17 ?  82  VAL   A HB   1 
ATOM   1851 H HG11 . VAL   A 1 82  ? 33.646 -5.247  10.185  1.00 19.66 ?  82  VAL   A HG11 1 
ATOM   1852 H HG12 . VAL   A 1 82  ? 34.077 -3.726  10.040  1.00 19.66 ?  82  VAL   A HG12 1 
ATOM   1853 H HG13 . VAL   A 1 82  ? 32.605 -4.177  9.643   1.00 19.66 ?  82  VAL   A HG13 1 
ATOM   1854 H HG21 . VAL   A 1 82  ? 33.701 -6.736  8.382   1.00 18.87 ?  82  VAL   A HG21 1 
ATOM   1855 H HG22 . VAL   A 1 82  ? 32.500 -5.986  7.661   1.00 18.87 ?  82  VAL   A HG22 1 
ATOM   1856 H HG23 . VAL   A 1 82  ? 33.860 -6.244  6.881   1.00 18.87 ?  82  VAL   A HG23 1 
ATOM   1857 N N    . LEU   A 1 83  ? 33.306 -1.334  8.196   1.00 12.42 ?  83  LEU   A N    1 
ATOM   1858 C CA   . LEU   A 1 83  ? 33.731 -0.066  8.772   1.00 12.14 ?  83  LEU   A CA   1 
ATOM   1859 C C    . LEU   A 1 83  ? 33.009 0.118   10.104  1.00 12.56 ?  83  LEU   A C    1 
ATOM   1860 O O    . LEU   A 1 83  ? 32.278 -0.768  10.566  1.00 13.07 ?  83  LEU   A O    1 
ATOM   1861 C CB   . LEU   A 1 83  ? 33.485 1.085   7.787   1.00 13.24 ?  83  LEU   A CB   1 
ATOM   1862 C CG   . LEU   A 1 83  ? 34.392 1.070   6.554   1.00 13.79 ?  83  LEU   A CG   1 
ATOM   1863 C CD1  . LEU   A 1 83  ? 33.976 2.141   5.561   1.00 14.77 ?  83  LEU   A CD1  1 
ATOM   1864 C CD2  . LEU   A 1 83  ? 35.861 1.268   6.950   1.00 14.65 ?  83  LEU   A CD2  1 
ATOM   1865 H H    . LEU   A 1 83  ? 32.453 -1.417  8.150   1.00 14.92 ?  83  LEU   A H    1 
ATOM   1866 H HA   . LEU   A 1 83  ? 34.681 -0.097  8.953   1.00 14.59 ?  83  LEU   A HA   1 
ATOM   1867 H HB2  . LEU   A 1 83  ? 32.568 1.041   7.469   1.00 15.91 ?  83  LEU   A HB2  1 
ATOM   1868 H HB3  . LEU   A 1 83  ? 33.628 1.931   8.241   1.00 15.91 ?  83  LEU   A HB3  1 
ATOM   1869 H HG   . LEU   A 1 83  ? 34.318 0.209   6.115   1.00 16.57 ?  83  LEU   A HG   1 
ATOM   1870 H HD11 . LEU   A 1 83  ? 34.567 2.103   4.791   1.00 17.75 ?  83  LEU   A HD11 1 
ATOM   1871 H HD12 . LEU   A 1 83  ? 33.063 1.975   5.288   1.00 17.75 ?  83  LEU   A HD12 1 
ATOM   1872 H HD13 . LEU   A 1 83  ? 34.046 3.009   5.988   1.00 17.75 ?  83  LEU   A HD13 1 
ATOM   1873 H HD21 . LEU   A 1 83  ? 36.388 1.437   6.150   1.00 17.60 ?  83  LEU   A HD21 1 
ATOM   1874 H HD22 . LEU   A 1 83  ? 35.930 2.025   7.554   1.00 17.60 ?  83  LEU   A HD22 1 
ATOM   1875 H HD23 . LEU   A 1 83  ? 36.186 0.465   7.390   1.00 17.60 ?  83  LEU   A HD23 1 
ATOM   1876 N N    . SER   A 1 84  ? 33.208 1.273   10.729  1.00 13.25 ?  84  SER   A N    1 
ATOM   1877 C CA   . SER   A 1 84  ? 32.560 1.533   12.004  1.00 13.59 ?  84  SER   A CA   1 
ATOM   1878 C C    . SER   A 1 84  ? 31.045 1.626   11.846  1.00 12.95 ?  84  SER   A C    1 
ATOM   1879 O O    . SER   A 1 84  ? 30.531 2.077   10.826  1.00 12.79 ?  84  SER   A O    1 
ATOM   1880 C CB   . SER   A 1 84  ? 33.058 2.858   12.572  1.00 14.60 ?  84  SER   A CB   1 
ATOM   1881 O OG   . SER   A 1 84  ? 32.446 3.125   13.812  1.00 15.70 ?  84  SER   A OG   1 
ATOM   1882 H H    . SER   A 1 84  ? 33.704 1.921   10.434  1.00 15.92 ?  84  SER   A H    1 
ATOM   1883 H HA   . SER   A 1 84  ? 32.780 0.823   12.628  1.00 16.33 ?  84  SER   A HA   1 
ATOM   1884 H HB2  . SER   A 1 84  ? 34.021 2.815   12.694  1.00 17.54 ?  84  SER   A HB2  1 
ATOM   1885 H HB3  . SER   A 1 84  ? 32.837 3.572   11.952  1.00 17.54 ?  84  SER   A HB3  1 
ATOM   1886 H HG   . SER   A 1 84  ? 32.728 3.857   14.121  1.00 18.87 ?  84  SER   A HG   1 
ATOM   1887 N N    . GLY   A 1 85  ? 30.336 1.228   12.895  1.00 14.04 ?  85  GLY   A N    1 
ATOM   1888 C CA   . GLY   A 1 85  ? 28.911 1.453   12.988  1.00 14.67 ?  85  GLY   A CA   1 
ATOM   1889 C C    . GLY   A 1 85  ? 28.536 2.773   13.620  1.00 14.27 ?  85  GLY   A C    1 
ATOM   1890 O O    . GLY   A 1 85  ? 27.344 3.087   13.714  1.00 15.57 ?  85  GLY   A O    1 
ATOM   1891 H H    . GLY   A 1 85  ? 30.666 0.812   13.575  1.00 16.87 ?  85  GLY   A H    1 
ATOM   1892 H HA2  . GLY   A 1 85  ? 28.528 1.427   12.098  1.00 17.62 ?  85  GLY   A HA2  1 
ATOM   1893 H HA3  . GLY   A 1 85  ? 28.509 0.742   13.510  1.00 17.62 ?  85  GLY   A HA3  1 
ATOM   1894 N N    . HIS   A 1 86  ? 29.522 3.549   14.068  1.00 13.96 ?  86  HIS   A N    1 
ATOM   1895 C CA   . HIS   A 1 86  ? 29.299 4.890   14.621  1.00 14.43 ?  86  HIS   A CA   1 
ATOM   1896 C C    . HIS   A 1 86  ? 28.302 4.776   15.767  1.00 15.29 ?  86  HIS   A C    1 
ATOM   1897 O O    . HIS   A 1 86  ? 28.475 3.897   16.625  1.00 16.58 ?  86  HIS   A O    1 
ATOM   1898 C CB   . HIS   A 1 86  ? 28.931 5.850   13.501  1.00 14.38 ?  86  HIS   A CB   1 
ATOM   1899 C CG   . HIS   A 1 86  ? 30.000 5.948   12.473  1.00 14.33 ?  86  HIS   A CG   1 
ATOM   1900 N ND1  . HIS   A 1 86  ? 31.093 6.779   12.612  1.00 16.02 ?  86  HIS   A ND1  1 
ATOM   1901 C CD2  . HIS   A 1 86  ? 30.192 5.256   11.327  1.00 14.11 ?  86  HIS   A CD2  1 
ATOM   1902 C CE1  . HIS   A 1 86  ? 31.893 6.614   11.574  1.00 15.38 ?  86  HIS   A CE1  1 
ATOM   1903 N NE2  . HIS   A 1 86  ? 31.376 5.688   10.787  1.00 14.59 ?  86  HIS   A NE2  1 
ATOM   1904 H H    . HIS   A 1 86  ? 30.346 3.319   14.069  1.00 16.77 ?  86  HIS   A H    1 
ATOM   1905 H HA   . HIS   A 1 86  ? 30.134 5.207   14.995  1.00 17.33 ?  86  HIS   A HA   1 
ATOM   1906 H HB2  . HIS   A 1 86  ? 28.119 5.544   13.063  1.00 17.28 ?  86  HIS   A HB2  1 
ATOM   1907 H HB3  . HIS   A 1 86  ? 28.791 6.741   13.866  1.00 17.28 ?  86  HIS   A HB3  1 
ATOM   1908 H HD2  . HIS   A 1 86  ? 29.632 4.601   10.965  1.00 16.95 ?  86  HIS   A HD2  1 
ATOM   1909 H HE1  . HIS   A 1 86  ? 32.690 7.068   11.416  1.00 18.48 ?  86  HIS   A HE1  1 
ATOM   1910 H HE2  . HIS   A 1 86  ? 31.720 5.413   10.035  1.00 17.53 ?  86  HIS   A HE2  1 
ATOM   1911 N N    . ASN   A 1 87  ? 27.281 5.621   15.821  1.00 16.42 ?  87  ASN   A N    1 
ATOM   1912 C CA   . ASN   A 1 87  ? 26.300 5.614   16.890  1.00 17.52 ?  87  ASN   A CA   1 
ATOM   1913 C C    . ASN   A 1 87  ? 25.167 4.629   16.653  1.00 18.42 ?  87  ASN   A C    1 
ATOM   1914 O O    . ASN   A 1 87  ? 24.232 4.585   17.454  1.00 20.91 ?  87  ASN   A O    1 
ATOM   1915 C CB   . ASN   A 1 87  ? 25.702 7.020   17.046  1.00 18.35 ?  87  ASN   A CB   1 
ATOM   1916 C CG   . ASN   A 1 87  ? 25.199 7.592   15.724  1.00 19.17 ?  87  ASN   A CG   1 
ATOM   1917 O OD1  . ASN   A 1 87  ? 25.843 7.455   14.686  1.00 19.51 ?  87  ASN   A OD1  1 
ATOM   1918 N ND2  . ASN   A 1 87  ? 24.043 8.233   15.761  1.00 20.85 ?  87  ASN   A ND2  1 
ATOM   1919 H H    . ASN   A 1 87  ? 27.130 6.226   15.230  1.00 19.73 ?  87  ASN   A H    1 
ATOM   1920 H HA   . ASN   A 1 87  ? 26.726 5.375   17.731  1.00 21.04 ?  87  ASN   A HA   1 
ATOM   1921 H HB2  . ASN   A 1 87  ? 24.950 6.980   17.665  1.00 22.04 ?  87  ASN   A HB2  1 
ATOM   1922 H HB3  . ASN   A 1 87  ? 26.382 7.615   17.394  1.00 22.04 ?  87  ASN   A HB3  1 
ATOM   1923 H HD21 . ASN   A 1 87  ? 23.721 8.567   15.039  1.00 25.04 ?  87  ASN   A HD21 1 
ATOM   1924 H HD22 . ASN   A 1 87  ? 23.620 8.317   16.504  1.00 25.04 ?  87  ASN   A HD22 1 
ATOM   1925 N N    A LEU   A 1 88  ? 25.236 3.834   15.588  0.56 16.84 ?  88  LEU   A N    1 
ATOM   1926 N N    B LEU   A 1 88  ? 25.230 3.828   15.591  0.44 17.28 ?  88  LEU   A N    1 
ATOM   1927 C CA   A LEU   A 1 88  ? 24.131 2.973   15.186  0.56 16.49 ?  88  LEU   A CA   1 
ATOM   1928 C CA   B LEU   A 1 88  ? 24.114 2.977   15.200  0.44 17.06 ?  88  LEU   A CA   1 
ATOM   1929 C C    A LEU   A 1 88  ? 24.348 1.504   15.514  0.56 16.38 ?  88  LEU   A C    1 
ATOM   1930 C C    B LEU   A 1 88  ? 24.345 1.493   15.440  0.44 16.61 ?  88  LEU   A C    1 
ATOM   1931 O O    A LEU   A 1 88  ? 23.374 0.783   15.765  0.56 17.45 ?  88  LEU   A O    1 
ATOM   1932 O O    B LEU   A 1 88  ? 23.367 0.743   15.543  0.44 17.30 ?  88  LEU   A O    1 
ATOM   1933 C CB   A LEU   A 1 88  ? 23.909 3.096   13.677  0.56 16.64 ?  88  LEU   A CB   1 
ATOM   1934 C CB   B LEU   A 1 88  ? 23.807 3.176   13.711  0.44 17.70 ?  88  LEU   A CB   1 
ATOM   1935 C CG   A LEU   A 1 88  ? 23.631 4.494   13.125  0.56 17.61 ?  88  LEU   A CG   1 
ATOM   1936 C CG   B LEU   A 1 88  ? 23.497 4.614   13.289  0.44 18.43 ?  88  LEU   A CG   1 
ATOM   1937 C CD1  A LEU   A 1 88  ? 23.508 4.432   11.613  0.56 18.79 ?  88  LEU   A CD1  1 
ATOM   1938 C CD1  B LEU   A 1 88  ? 23.350 4.715   11.779  0.44 19.16 ?  88  LEU   A CD1  1 
ATOM   1939 C CD2  A LEU   A 1 88  ? 22.376 5.086   13.750  0.56 19.01 ?  88  LEU   A CD2  1 
ATOM   1940 C CD2  B LEU   A 1 88  ? 22.243 5.122   13.989  0.44 19.02 ?  88  LEU   A CD2  1 
ATOM   1941 H H    A LEU   A 1 88  ? 25.933 3.767   15.087  0.56 20.23 ?  88  LEU   A H    1 
ATOM   1942 H H    B LEU   A 1 88  ? 25.921 3.755   15.086  0.44 20.75 ?  88  LEU   A H    1 
ATOM   1943 H HA   A LEU   A 1 88  ? 23.325 3.263   15.632  0.56 19.81 ?  88  LEU   A HA   1 
ATOM   1944 H HA   B LEU   A 1 88  ? 23.328 3.243   15.701  0.44 20.49 ?  88  LEU   A HA   1 
ATOM   1945 H HB2  A LEU   A 1 88  ? 24.697 2.769   13.223  0.56 19.99 ?  88  LEU   A HB2  1 
ATOM   1946 H HB2  B LEU   A 1 88  ? 24.575 2.883   13.199  0.44 21.26 ?  88  LEU   A HB2  1 
ATOM   1947 H HB3  A LEU   A 1 88  ? 23.147 2.547   13.439  0.56 19.99 ?  88  LEU   A HB3  1 
ATOM   1948 H HB3  B LEU   A 1 88  ? 23.037 2.633   13.484  0.44 21.26 ?  88  LEU   A HB3  1 
ATOM   1949 H HG   A LEU   A 1 88  ? 24.375 5.078   13.340  0.56 21.15 ?  88  LEU   A HG   1 
ATOM   1950 H HG   B LEU   A 1 88  ? 24.234 5.185   13.553  0.44 22.14 ?  88  LEU   A HG   1 
ATOM   1951 H HD11 A LEU   A 1 88  ? 23.357 5.328   11.270  0.56 22.57 ?  88  LEU   A HD11 1 
ATOM   1952 H HD11 B LEU   A 1 88  ? 23.164 5.636   11.539  0.44 23.01 ?  88  LEU   A HD11 1 
ATOM   1953 H HD12 A LEU   A 1 88  ? 24.328 4.070   11.245  0.56 22.57 ?  88  LEU   A HD12 1 
ATOM   1954 H HD12 B LEU   A 1 88  ? 24.177 4.425   11.362  0.44 23.01 ?  88  LEU   A HD12 1 
ATOM   1955 H HD13 A LEU   A 1 88  ? 22.759 3.860   11.383  0.56 22.57 ?  88  LEU   A HD13 1 
ATOM   1956 H HD13 B LEU   A 1 88  ? 22.619 4.144   11.493  0.44 23.01 ?  88  LEU   A HD13 1 
ATOM   1957 H HD21 A LEU   A 1 88  ? 22.179 5.936   13.323  0.56 22.83 ?  88  LEU   A HD21 1 
ATOM   1958 H HD21 B LEU   A 1 88  ? 22.009 5.989   13.622  0.44 22.85 ?  88  LEU   A HD21 1 
ATOM   1959 H HD22 A LEU   A 1 88  ? 21.638 4.471   13.618  0.56 22.83 ?  88  LEU   A HD22 1 
ATOM   1960 H HD22 B LEU   A 1 88  ? 21.521 4.492   13.838  0.44 22.85 ?  88  LEU   A HD22 1 
ATOM   1961 H HD23 A LEU   A 1 88  ? 22.530 5.221   14.698  0.56 22.83 ?  88  LEU   A HD23 1 
ATOM   1962 H HD23 B LEU   A 1 88  ? 22.422 5.201   14.938  0.44 22.85 ?  88  LEU   A HD23 1 
ATOM   1963 N N    . ALA   A 1 89  ? 25.597 1.053   15.511  1.00 15.86 ?  89  ALA   A N    1 
ATOM   1964 C CA   . ALA   A 1 89  ? 25.932 -0.356  15.637  1.00 15.39 ?  89  ALA   A CA   1 
ATOM   1965 C C    . ALA   A 1 89  ? 27.414 -0.421  15.968  1.00 16.01 ?  89  ALA   A C    1 
ATOM   1966 O O    . ALA   A 1 89  ? 28.132 0.575   15.855  1.00 16.60 ?  89  ALA   A O    1 
ATOM   1967 C CB   . ALA   A 1 89  ? 25.671 -1.079  14.319  1.00 14.86 ?  89  ALA   A CB   1 
ATOM   1968 H H    A ALA   A 1 89  ? 26.287 1.565   15.439  0.56 19.05 ?  89  ALA   A H    1 
ATOM   1969 H H    B ALA   A 1 89  ? 26.286 1.570   15.469  0.44 19.05 ?  89  ALA   A H    1 
ATOM   1970 H HA   . ALA   A 1 89  ? 25.415 -0.764  16.350  1.00 18.49 ?  89  ALA   A HA   1 
ATOM   1971 H HB1  . ALA   A 1 89  ? 25.921 -2.011  14.421  1.00 17.85 ?  89  ALA   A HB1  1 
ATOM   1972 H HB2  . ALA   A 1 89  ? 24.733 -1.008  14.097  1.00 17.85 ?  89  ALA   A HB2  1 
ATOM   1973 H HB3  . ALA   A 1 89  ? 26.211 -0.668  13.625  1.00 17.85 ?  89  ALA   A HB3  1 
ATOM   1974 N N    . LYS   A 1 90  ? 27.885 -1.601  16.360  1.00 16.88 ?  90  LYS   A N    1 
ATOM   1975 C CA   . LYS   A 1 90  ? 29.328 -1.756  16.515  1.00 17.67 ?  90  LYS   A CA   1 
ATOM   1976 C C    . LYS   A 1 90  ? 30.033 -1.569  15.176  1.00 16.41 ?  90  LYS   A C    1 
ATOM   1977 O O    . LYS   A 1 90  ? 30.983 -0.773  15.058  1.00 17.53 ?  90  LYS   A O    1 
ATOM   1978 C CB   . LYS   A 1 90  ? 29.659 -3.117  17.128  1.00 19.88 ?  90  LYS   A CB   1 
ATOM   1979 C CG   . LYS   A 1 90  ? 31.137 -3.285  17.462  1.00 24.93 ?  90  LYS   A CG   1 
ATOM   1980 C CD   . LYS   A 1 90  ? 31.375 -4.482  18.372  1.00 29.43 ?  90  LYS   A CD   1 
ATOM   1981 C CE   . LYS   A 1 90  ? 32.796 -4.497  18.922  1.00 32.73 ?  90  LYS   A CE   1 
ATOM   1982 N NZ   . LYS   A 1 90  ? 33.805 -4.965  17.928  1.00 36.39 ?  90  LYS   A NZ   1 
ATOM   1983 H H    . LYS   A 1 90  ? 27.411 -2.288  16.546  1.00 20.27 ?  90  LYS   A H    1 
ATOM   1984 H HA   . LYS   A 1 90  ? 29.658 -1.071  17.118  1.00 21.23 ?  90  LYS   A HA   1 
ATOM   1985 H HB2  . LYS   A 1 90  ? 29.150 -3.223  17.950  1.00 23.87 ?  90  LYS   A HB2  1 
ATOM   1986 H HB3  . LYS   A 1 90  ? 29.411 -3.814  16.500  1.00 23.87 ?  90  LYS   A HB3  1 
ATOM   1987 H HG2  . LYS   A 1 90  ? 31.636 -3.423  16.643  1.00 29.94 ?  90  LYS   A HG2  1 
ATOM   1988 H HG3  . LYS   A 1 90  ? 31.452 -2.491  17.919  1.00 29.94 ?  90  LYS   A HG3  1 
ATOM   1989 H HD2  . LYS   A 1 90  ? 30.759 -4.443  19.123  1.00 35.34 ?  90  LYS   A HD2  1 
ATOM   1990 H HD3  . LYS   A 1 90  ? 31.234 -5.301  17.869  1.00 35.34 ?  90  LYS   A HD3  1 
ATOM   1991 H HE2  . LYS   A 1 90  ? 33.038 -3.597  19.192  1.00 39.30 ?  90  LYS   A HE2  1 
ATOM   1992 H HE3  . LYS   A 1 90  ? 32.832 -5.092  19.687  1.00 39.30 ?  90  LYS   A HE3  1 
ATOM   1993 H HZ1  . LYS   A 1 90  ? 33.600 -5.785  17.649  1.00 43.69 ?  90  LYS   A HZ1  1 
ATOM   1994 H HZ2  . LYS   A 1 90  ? 33.822 -4.416  17.229  1.00 43.69 ?  90  LYS   A HZ2  1 
ATOM   1995 H HZ3  . LYS   A 1 90  ? 34.614 -4.982  18.302  1.00 43.69 ?  90  LYS   A HZ3  1 
ATOM   1996 N N    . HIS   A 1 91  ? 29.566 -2.284  14.152  1.00 14.70 ?  91  HIS   A N    1 
ATOM   1997 C CA   . HIS   A 1 91  ? 30.152 -2.290  12.825  1.00 13.76 ?  91  HIS   A CA   1 
ATOM   1998 C C    . HIS   A 1 91  ? 29.080 -2.013  11.788  1.00 12.59 ?  91  HIS   A C    1 
ATOM   1999 O O    . HIS   A 1 91  ? 27.912 -2.360  11.974  1.00 13.76 ?  91  HIS   A O    1 
ATOM   2000 C CB   . HIS   A 1 91  ? 30.742 -3.662  12.478  1.00 16.08 ?  91  HIS   A CB   1 
ATOM   2001 C CG   . HIS   A 1 91  ? 31.741 -4.163  13.469  1.00 20.62 ?  91  HIS   A CG   1 
ATOM   2002 N ND1  . HIS   A 1 91  ? 33.010 -3.634  13.579  1.00 22.57 ?  91  HIS   A ND1  1 
ATOM   2003 C CD2  . HIS   A 1 91  ? 31.664 -5.149  14.393  1.00 22.49 ?  91  HIS   A CD2  1 
ATOM   2004 C CE1  . HIS   A 1 91  ? 33.671 -4.273  14.529  1.00 23.79 ?  91  HIS   A CE1  1 
ATOM   2005 N NE2  . HIS   A 1 91  ? 32.877 -5.199  15.038  1.00 23.82 ?  91  HIS   A NE2  1 
ATOM   2006 H H    . HIS   A 1 91  ? 28.875 -2.807  14.215  1.00 17.66 ?  91  HIS   A H    1 
ATOM   2007 H HA   . HIS   A 1 91  ? 30.849 -1.623  12.761  1.00 16.54 ?  91  HIS   A HA   1 
ATOM   2008 H HB2  . HIS   A 1 91  ? 30.024 -4.315  12.436  1.00 19.32 ?  91  HIS   A HB2  1 
ATOM   2009 H HB3  . HIS   A 1 91  ? 31.185 -3.607  11.616  1.00 19.32 ?  91  HIS   A HB3  1 
ATOM   2010 H HD1  . HIS   A 1 91  ? 33.327 -2.991  13.099  1.00 27.10 ?  91  HIS   A HD1  1 
ATOM   2011 H HD2  . HIS   A 1 91  ? 30.935 -5.692  14.565  1.00 27.01 ?  91  HIS   A HD2  1 
ATOM   2012 H HE1  . HIS   A 1 91  ? 34.551 -4.096  14.792  1.00 28.57 ?  91  HIS   A HE1  1 
ATOM   2013 N N    . CYS   A 1 92  ? 29.488 -1.413  10.678  1.00 12.47 ?  92  CYS   A N    1 
ATOM   2014 C CA   . CYS   A 1 92  ? 28.665 -1.341  9.481   1.00 12.24 ?  92  CYS   A CA   1 
ATOM   2015 C C    . CYS   A 1 92  ? 29.318 -2.170  8.385   1.00 12.21 ?  92  CYS   A C    1 
ATOM   2016 O O    . CYS   A 1 92  ? 30.476 -1.919  8.018   1.00 12.53 ?  92  CYS   A O    1 
ATOM   2017 C CB   . CYS   A 1 92  ? 28.467 0.098   9.007   1.00 12.37 ?  92  CYS   A CB   1 
ATOM   2018 S SG   . CYS   A 1 92  ? 27.452 0.206   7.497   1.00 12.00 ?  92  CYS   A SG   1 
ATOM   2019 H H    . CYS   A 1 92  ? 30.255 -1.024  10.601  1.00 14.99 ?  92  CYS   A H    1 
ATOM   2020 H HA   . CYS   A 1 92  ? 27.795 -1.718  9.672   1.00 14.71 ?  92  CYS   A HA   1 
ATOM   2021 H HB2  . CYS   A 1 92  ? 28.015 0.607   9.702   1.00 14.86 ?  92  CYS   A HB2  1 
ATOM   2022 H HB3  . CYS   A 1 92  ? 29.330 0.496   8.816   1.00 14.86 ?  92  CYS   A HB3  1 
ATOM   2023 H HG   . CYS   A 1 92  ? 27.331 1.358   7.195   1.00 14.42 ?  92  CYS   A HG   1 
ATOM   2024 N N    . LEU   A 1 93  ? 28.580 -3.151  7.876   1.00 11.93 ?  93  LEU   A N    1 
ATOM   2025 C CA   . LEU   A 1 93  ? 28.989 -3.904  6.700   1.00 11.68 ?  93  LEU   A CA   1 
ATOM   2026 C C    . LEU   A 1 93  ? 28.404 -3.215  5.470   1.00 10.99 ?  93  LEU   A C    1 
ATOM   2027 O O    . LEU   A 1 93  ? 27.192 -3.275  5.236   1.00 11.02 ?  93  LEU   A O    1 
ATOM   2028 C CB   . LEU   A 1 93  ? 28.512 -5.351  6.817   1.00 12.20 ?  93  LEU   A CB   1 
ATOM   2029 C CG   . LEU   A 1 93  ? 28.907 -6.250  5.649   1.00 13.11 ?  93  LEU   A CG   1 
ATOM   2030 C CD1  . LEU   A 1 93  ? 30.413 -6.525  5.626   1.00 13.84 ?  93  LEU   A CD1  1 
ATOM   2031 C CD2  . LEU   A 1 93  ? 28.117 -7.560  5.698   1.00 13.75 ?  93  LEU   A CD2  1 
ATOM   2032 H H    . LEU   A 1 93  ? 27.823 -3.394  8.209   1.00 14.34 ?  93  LEU   A H    1 
ATOM   2033 H HA   . LEU   A 1 93  ? 29.952 -3.895  6.636   1.00 14.04 ?  93  LEU   A HA   1 
ATOM   2034 H HB2  . LEU   A 1 93  ? 28.894 -5.733  7.629   1.00 14.66 ?  93  LEU   A HB2  1 
ATOM   2035 H HB3  . LEU   A 1 93  ? 27.548 -5.357  6.882   1.00 14.66 ?  93  LEU   A HB3  1 
ATOM   2036 H HG   . LEU   A 1 93  ? 28.686 -5.803  4.826   1.00 15.76 ?  93  LEU   A HG   1 
ATOM   2037 H HD11 . LEU   A 1 93  ? 30.615 -7.126  4.895   1.00 16.63 ?  93  LEU   A HD11 1 
ATOM   2038 H HD12 . LEU   A 1 93  ? 30.888 -5.687  5.511   1.00 16.63 ?  93  LEU   A HD12 1 
ATOM   2039 H HD13 . LEU   A 1 93  ? 30.675 -6.935  6.471   1.00 16.63 ?  93  LEU   A HD13 1 
ATOM   2040 H HD21 . LEU   A 1 93  ? 28.385 -8.116  4.950   1.00 16.52 ?  93  LEU   A HD21 1 
ATOM   2041 H HD22 . LEU   A 1 93  ? 28.301 -8.014  6.533   1.00 16.52 ?  93  LEU   A HD22 1 
ATOM   2042 H HD23 . LEU   A 1 93  ? 27.170 -7.355  5.634   1.00 16.52 ?  93  LEU   A HD23 1 
ATOM   2043 N N    . HIS   A 1 94  ? 29.258 -2.529  4.708   1.00 10.61 ?  94  HIS   A N    1 
ATOM   2044 C CA   . HIS   A 1 94  ? 28.836 -1.868  3.480   1.00 10.82 ?  94  HIS   A CA   1 
ATOM   2045 C C    . HIS   A 1 94  ? 28.856 -2.898  2.366   1.00 10.81 ?  94  HIS   A C    1 
ATOM   2046 O O    . HIS   A 1 94  ? 29.925 -3.417  2.037   1.00 12.30 ?  94  HIS   A O    1 
ATOM   2047 C CB   . HIS   A 1 94  ? 29.790 -0.716  3.150   1.00 10.85 ?  94  HIS   A CB   1 
ATOM   2048 C CG   . HIS   A 1 94  ? 29.777 0.377   4.165   1.00 10.66 ?  94  HIS   A CG   1 
ATOM   2049 N ND1  . HIS   A 1 94  ? 28.906 1.445   4.100   1.00 11.09 ?  94  HIS   A ND1  1 
ATOM   2050 C CD2  . HIS   A 1 94  ? 30.519 0.554   5.280   1.00 11.75 ?  94  HIS   A CD2  1 
ATOM   2051 C CE1  . HIS   A 1 94  ? 29.120 2.234   5.137   1.00 11.47 ?  94  HIS   A CE1  1 
ATOM   2052 N NE2  . HIS   A 1 94  ? 30.088 1.710   5.872   1.00 11.83 ?  94  HIS   A NE2  1 
ATOM   2053 H H    . HIS   A 1 94  ? 30.098 -2.435  4.882   1.00 12.76 ?  94  HIS   A H    1 
ATOM   2054 H HA   . HIS   A 1 94  ? 27.934 -1.519  3.580   1.00 13.01 ?  94  HIS   A HA   1 
ATOM   2055 H HB2  . HIS   A 1 94  ? 30.691 -1.056  3.099   1.00 13.04 ?  94  HIS   A HB2  1 
ATOM   2056 H HB3  . HIS   A 1 94  ? 29.529 -0.326  2.300   1.00 13.04 ?  94  HIS   A HB3  1 
ATOM   2057 H HD2  . HIS   A 1 94  ? 31.192 -0.000  5.591   1.00 14.12 ?  94  HIS   A HD2  1 
ATOM   2058 H HE1  . HIS   A 1 94  ? 28.655 3.023   5.321   1.00 13.79 ?  94  HIS   A HE1  1 
ATOM   2059 H HE2  . HIS   A 1 94  ? 30.406 2.061   6.590   1.00 14.22 ?  94  HIS   A HE2  1 
ATOM   2060 N N    . VAL   A 1 95  ? 27.692 -3.214  1.805   1.00 10.42 ?  95  VAL   A N    1 
ATOM   2061 C CA   . VAL   A 1 95  ? 27.556 -4.261  0.795   1.00 11.03 ?  95  VAL   A CA   1 
ATOM   2062 C C    . VAL   A 1 95  ? 27.018 -3.633  -0.480  1.00 10.74 ?  95  VAL   A C    1 
ATOM   2063 O O    . VAL   A 1 95  ? 26.016 -2.906  -0.436  1.00 11.08 ?  95  VAL   A O    1 
ATOM   2064 C CB   . VAL   A 1 95  ? 26.626 -5.400  1.249   1.00 11.29 ?  95  VAL   A CB   1 
ATOM   2065 C CG1  . VAL   A 1 95  ? 26.522 -6.445  0.140   1.00 12.33 ?  95  VAL   A CG1  1 
ATOM   2066 C CG2  . VAL   A 1 95  ? 27.132 -6.015  2.541   1.00 11.78 ?  95  VAL   A CG2  1 
ATOM   2067 H H    . VAL   A 1 95  ? 26.948 -2.832  1.995   1.00 12.53 ?  95  VAL   A H    1 
ATOM   2068 H HA   . VAL   A 1 95  ? 28.424 -4.641  0.597   1.00 13.26 ?  95  VAL   A HA   1 
ATOM   2069 H HB   . VAL   A 1 95  ? 25.741 -5.049  1.409   1.00 13.57 ?  95  VAL   A HB   1 
ATOM   2070 H HG11 . VAL   A 1 95  ? 26.146 -7.263  0.505   1.00 14.82 ?  95  VAL   A HG11 1 
ATOM   2071 H HG12 . VAL   A 1 95  ? 25.946 -6.110  -0.566  1.00 14.82 ?  95  VAL   A HG12 1 
ATOM   2072 H HG13 . VAL   A 1 95  ? 27.408 -6.626  -0.216  1.00 14.82 ?  95  VAL   A HG13 1 
ATOM   2073 H HG21 . VAL   A 1 95  ? 26.572 -6.777  2.771   1.00 14.16 ?  95  VAL   A HG21 1 
ATOM   2074 H HG22 . VAL   A 1 95  ? 28.048 -6.308  2.418   1.00 14.16 ?  95  VAL   A HG22 1 
ATOM   2075 H HG23 . VAL   A 1 95  ? 27.086 -5.350  3.244   1.00 14.16 ?  95  VAL   A HG23 1 
ATOM   2076 N N    . VAL   A 1 96  ? 27.656 -3.926  -1.613  1.00 10.62 ?  96  VAL   A N    1 
ATOM   2077 C CA   . VAL   A 1 96  ? 27.255 -3.384  -2.904  1.00 10.89 ?  96  VAL   A CA   1 
ATOM   2078 C C    . VAL   A 1 96  ? 26.455 -4.434  -3.668  1.00 11.51 ?  96  VAL   A C    1 
ATOM   2079 O O    . VAL   A 1 96  ? 27.015 -5.383  -4.222  1.00 12.19 ?  96  VAL   A O    1 
ATOM   2080 C CB   . VAL   A 1 96  ? 28.449 -2.906  -3.727  1.00 11.67 ?  96  VAL   A CB   1 
ATOM   2081 C CG1  . VAL   A 1 96  ? 27.944 -2.264  -5.005  1.00 12.31 ?  96  VAL   A CG1  1 
ATOM   2082 C CG2  . VAL   A 1 96  ? 29.301 -1.934  -2.935  1.00 12.09 ?  96  VAL   A CG2  1 
ATOM   2083 H H    . VAL   A 1 96  ? 28.350 -4.446  -1.655  1.00 12.76 ?  96  VAL   A H    1 
ATOM   2084 H HA   . VAL   A 1 96  ? 26.680 -2.622  -2.755  1.00 13.09 ?  96  VAL   A HA   1 
ATOM   2085 H HB   . VAL   A 1 96  ? 29.003 -3.660  -3.971  1.00 14.03 ?  96  VAL   A HB   1 
ATOM   2086 H HG11 . VAL   A 1 96  ? 28.673 -1.776  -5.422  1.00 14.79 ?  96  VAL   A HG11 1 
ATOM   2087 H HG12 . VAL   A 1 96  ? 27.623 -2.953  -5.603  1.00 14.79 ?  96  VAL   A HG12 1 
ATOM   2088 H HG13 . VAL   A 1 96  ? 27.224 -1.649  -4.786  1.00 14.79 ?  96  VAL   A HG13 1 
ATOM   2089 H HG21 . VAL   A 1 96  ? 30.003 -1.582  -3.505  1.00 14.53 ?  96  VAL   A HG21 1 
ATOM   2090 H HG22 . VAL   A 1 96  ? 28.739 -1.202  -2.620  1.00 14.53 ?  96  VAL   A HG22 1 
ATOM   2091 H HG23 . VAL   A 1 96  ? 29.689 -2.396  -2.177  1.00 14.53 ?  96  VAL   A HG23 1 
ATOM   2092 N N    A GLY   A 1 97  ? 25.136 -4.275  -3.690  0.56 11.39 ?  97  GLY   A N    1 
ATOM   2093 N N    B GLY   A 1 97  ? 25.140 -4.254  -3.736  0.44 11.48 ?  97  GLY   A N    1 
ATOM   2094 C CA   A GLY   A 1 97  ? 24.314 -5.013  -4.610  0.56 12.21 ?  97  GLY   A CA   1 
ATOM   2095 C CA   B GLY   A 1 97  ? 24.335 -5.033  -4.640  0.44 12.16 ?  97  GLY   A CA   1 
ATOM   2096 C C    A GLY   A 1 97  ? 24.296 -4.317  -5.954  0.56 11.91 ?  97  GLY   A C    1 
ATOM   2097 C C    B GLY   A 1 97  ? 24.404 -4.462  -6.042  0.44 12.21 ?  97  GLY   A C    1 
ATOM   2098 O O    A GLY   A 1 97  ? 24.546 -3.110  -6.051  0.56 12.16 ?  97  GLY   A O    1 
ATOM   2099 O O    B GLY   A 1 97  ? 24.756 -3.293  -6.241  0.44 13.14 ?  97  GLY   A O    1 
ATOM   2100 H H    A GLY   A 1 97  ? 24.703 -3.736  -3.174  0.56 13.69 ?  97  GLY   A H    1 
ATOM   2101 H H    B GLY   A 1 97  ? 24.700 -3.683  -3.263  0.44 13.79 ?  97  GLY   A H    1 
ATOM   2102 H HA2  A GLY   A 1 97  ? 24.676 -5.904  -4.717  0.56 14.67 ?  97  GLY   A HA2  1 
ATOM   2103 H HA2  B GLY   A 1 97  ? 24.663 -5.944  -4.652  0.44 14.62 ?  97  GLY   A HA2  1 
ATOM   2104 H HA3  A GLY   A 1 97  ? 23.411 -5.073  -4.266  0.56 14.67 ?  97  GLY   A HA3  1 
ATOM   2105 H HA3  B GLY   A 1 97  ? 23.415 -5.032  -4.343  0.44 14.62 ?  97  GLY   A HA3  1 
ATOM   2106 N N    A PRO   A 1 98  ? 23.996 -5.056  -7.019  0.56 12.09 ?  98  PRO   A N    1 
ATOM   2107 N N    B PRO   A 1 98  ? 24.070 -5.270  -7.046  0.44 12.63 ?  98  PRO   A N    1 
ATOM   2108 C CA   A PRO   A 1 98  ? 23.882 -4.421  -8.337  0.56 12.79 ?  98  PRO   A CA   1 
ATOM   2109 C CA   B PRO   A 1 98  ? 24.043 -4.756  -8.420  0.44 13.43 ?  98  PRO   A CA   1 
ATOM   2110 C C    A PRO   A 1 98  ? 22.756 -3.398  -8.364  0.56 12.47 ?  98  PRO   A C    1 
ATOM   2111 C C    B PRO   A 1 98  ? 22.946 -3.721  -8.621  0.44 13.35 ?  98  PRO   A C    1 
ATOM   2112 O O    A PRO   A 1 98  ? 21.690 -3.598  -7.778  0.56 12.06 ?  98  PRO   A O    1 
ATOM   2113 O O    B PRO   A 1 98  ? 21.828 -3.856  -8.117  0.44 13.28 ?  98  PRO   A O    1 
ATOM   2114 C CB   A PRO   A 1 98  ? 23.594 -5.600  -9.275  0.56 13.01 ?  98  PRO   A CB   1 
ATOM   2115 C CB   B PRO   A 1 98  ? 23.789 -6.009  -9.268  0.44 13.81 ?  98  PRO   A CB   1 
ATOM   2116 C CG   A PRO   A 1 98  ? 22.970 -6.631  -8.396  0.56 12.78 ?  98  PRO   A CG   1 
ATOM   2117 C CG   B PRO   A 1 98  ? 23.161 -6.988  -8.328  0.44 14.13 ?  98  PRO   A CG   1 
ATOM   2118 C CD   A PRO   A 1 98  ? 23.678 -6.493  -7.068  0.56 12.38 ?  98  PRO   A CD   1 
ATOM   2119 C CD   B PRO   A 1 98  ? 23.783 -6.712  -6.987  0.44 13.10 ?  98  PRO   A CD   1 
ATOM   2120 H HA   A PRO   A 1 98  ? 24.716 -4.000  -8.585  0.56 15.37 ?  98  PRO   A HA   1 
ATOM   2121 H HA   B PRO   A 1 98  ? 24.899 -4.369  -8.656  0.44 16.14 ?  98  PRO   A HA   1 
ATOM   2122 H HB2  A PRO   A 1 98  ? 22.979 -5.329  -9.969  0.56 15.64 ?  98  PRO   A HB2  1 
ATOM   2123 H HB2  B PRO   A 1 98  ? 23.183 -5.793  -9.994  0.44 16.59 ?  98  PRO   A HB2  1 
ATOM   2124 H HB3  A PRO   A 1 98  ? 24.424 -5.931  -9.652  0.56 15.64 ?  98  PRO   A HB3  1 
ATOM   2125 H HB3  B PRO   A 1 98  ? 24.630 -6.348  -9.607  0.44 16.59 ?  98  PRO   A HB3  1 
ATOM   2126 H HG2  A PRO   A 1 98  ? 22.024 -6.452  -8.296  0.56 15.36 ?  98  PRO   A HG2  1 
ATOM   2127 H HG2  B PRO   A 1 98  ? 22.203 -6.841  -8.295  0.44 16.98 ?  98  PRO   A HG2  1 
ATOM   2128 H HG3  A PRO   A 1 98  ? 23.118 -7.516  -8.766  0.56 15.36 ?  98  PRO   A HG3  1 
ATOM   2129 H HG3  B PRO   A 1 98  ? 23.361 -7.891  -8.616  0.44 16.98 ?  98  PRO   A HG3  1 
ATOM   2130 H HD2  A PRO   A 1 98  ? 23.086 -6.741  -6.334  0.56 14.88 ?  98  PRO   A HD2  1 
ATOM   2131 H HD2  B PRO   A 1 98  ? 23.154 -6.904  -6.272  0.44 15.75 ?  98  PRO   A HD2  1 
ATOM   2132 H HD3  A PRO   A 1 98  ? 24.496 -7.017  -7.052  0.56 14.88 ?  98  PRO   A HD3  1 
ATOM   2133 H HD3  B PRO   A 1 98  ? 24.606 -7.216  -6.880  0.44 15.75 ?  98  PRO   A HD3  1 
ATOM   2134 N N    A ASN   A 1 99  ? 23.011 -2.286  -9.047  0.56 12.32 ?  99  ASN   A N    1 
ATOM   2135 N N    B ASN   A 1 99  ? 23.282 -2.674  -9.367  0.44 13.74 ?  99  ASN   A N    1 
ATOM   2136 C CA   A ASN   A 1 99  ? 22.028 -1.226  -9.243  0.56 13.08 ?  99  ASN   A CA   1 
ATOM   2137 C CA   B ASN   A 1 99  ? 22.344 -1.616  -9.720  0.44 14.90 ?  99  ASN   A CA   1 
ATOM   2138 C C    A ASN   A 1 99  ? 21.463 -1.355  -10.652 0.56 13.98 ?  99  ASN   A C    1 
ATOM   2139 C C    B ASN   A 1 99  ? 21.775 -1.954  -11.092 0.44 15.72 ?  99  ASN   A C    1 
ATOM   2140 O O    A ASN   A 1 99  ? 22.135 -1.013  -11.632 0.56 15.30 ?  99  ASN   A O    1 
ATOM   2141 O O    B ASN   A 1 99  ? 22.463 -1.816  -12.110 0.44 15.40 ?  99  ASN   A O    1 
ATOM   2142 C CB   A ASN   A 1 99  ? 22.672 0.142   -9.037  0.56 12.73 ?  99  ASN   A CB   1 
ATOM   2143 C CB   B ASN   A 1 99  ? 23.058 -0.268  -9.745  0.44 16.59 ?  99  ASN   A CB   1 
ATOM   2144 C CG   A ASN   A 1 99  ? 21.661 1.282   -9.050  0.56 13.13 ?  99  ASN   A CG   1 
ATOM   2145 C CG   B ASN   A 1 99  ? 22.120 0.888   -10.018 0.44 18.19 ?  99  ASN   A CG   1 
ATOM   2146 O OD1  A ASN   A 1 99  ? 20.676 1.252   -9.786  0.56 14.48 ?  99  ASN   A OD1  1 
ATOM   2147 O OD1  B ASN   A 1 99  ? 21.015 0.703   -10.525 0.44 18.37 ?  99  ASN   A OD1  1 
ATOM   2148 N ND2  A ASN   A 1 99  ? 21.905 2.291   -8.231  0.56 13.36 ?  99  ASN   A ND2  1 
ATOM   2149 N ND2  B ASN   A 1 99  ? 22.567 2.098   -9.695  0.44 19.67 ?  99  ASN   A ND2  1 
ATOM   2150 H H    A ASN   A 1 99  ? 23.774 -2.114  -9.400  0.56 14.81 ?  99  ASN   A H    1 
ATOM   2151 H H    B ASN   A 1 99  ? 24.072 -2.550  -9.682  0.44 16.51 ?  99  ASN   A H    1 
ATOM   2152 H HA   A ASN   A 1 99  ? 21.303 -1.331  -8.601  0.56 15.72 ?  99  ASN   A HA   1 
ATOM   2153 H HA   B ASN   A 1 99  ? 21.619 -1.582  -9.070  0.44 17.91 ?  99  ASN   A HA   1 
ATOM   2154 H HB2  A ASN   A 1 99  ? 23.130 0.151   -8.184  0.56 15.30 ?  99  ASN   A HB2  1 
ATOM   2155 H HB2  B ASN   A 1 99  ? 23.481 -0.120  -8.884  0.44 19.93 ?  99  ASN   A HB2  1 
ATOM   2156 H HB3  A ASN   A 1 99  ? 23.307 0.297   -9.756  0.56 15.30 ?  99  ASN   A HB3  1 
ATOM   2157 H HB3  B ASN   A 1 99  ? 23.726 -0.281  -10.444 0.44 19.93 ?  99  ASN   A HB3  1 
ATOM   2158 H HD21 A ASN   A 1 99  ? 21.365 2.959   -8.195  0.56 16.05 ?  99  ASN   A HD21 1 
ATOM   2159 H HD21 B ASN   A 1 99  ? 22.073 2.792   -9.825  0.44 23.63 ?  99  ASN   A HD21 1 
ATOM   2160 H HD22 A ASN   A 1 99  ? 22.604 2.278   -7.728  0.56 16.05 ?  99  ASN   A HD22 1 
ATOM   2161 H HD22 B ASN   A 1 99  ? 23.353 2.192   -9.355  0.44 23.63 ?  99  ASN   A HD22 1 
ATOM   2162 N N    A VAL   A 1 100 ? 20.223 -1.851  -10.742 0.56 15.37 ?  100 VAL   A N    1 
ATOM   2163 N N    B VAL   A 1 100 ? 20.519 -2.406  -11.110 0.44 17.61 ?  100 VAL   A N    1 
ATOM   2164 C CA   A VAL   A 1 100 ? 19.582 -2.080  -12.036 0.56 16.91 ?  100 VAL   A CA   1 
ATOM   2165 C CA   B VAL   A 1 100 ? 19.870 -2.795  -12.358 0.44 19.77 ?  100 VAL   A CA   1 
ATOM   2166 C C    A VAL   A 1 100 ? 19.476 -0.783  -12.821 0.56 16.93 ?  100 VAL   A C    1 
ATOM   2167 C C    B VAL   A 1 100 ? 19.783 -1.621  -13.317 0.44 20.01 ?  100 VAL   A C    1 
ATOM   2168 O O    A VAL   A 1 100 ? 19.584 -0.779  -14.053 0.56 17.88 ?  100 VAL   A O    1 
ATOM   2169 O O    B VAL   A 1 100 ? 19.797 -1.806  -14.543 0.44 19.96 ?  100 VAL   A O    1 
ATOM   2170 C CB   A VAL   A 1 100 ? 18.210 -2.766  -11.840 0.56 18.71 ?  100 VAL   A CB   1 
ATOM   2171 C CB   B VAL   A 1 100 ? 18.476 -3.378  -12.061 0.44 21.16 ?  100 VAL   A CB   1 
ATOM   2172 C CG1  A VAL   A 1 100 ? 17.483 -2.934  -13.171 0.56 19.39 ?  100 VAL   A CG1  1 
ATOM   2173 C CG1  B VAL   A 1 100 ? 17.690 -3.560  -13.352 0.44 21.61 ?  100 VAL   A CG1  1 
ATOM   2174 C CG2  A VAL   A 1 100 ? 18.392 -4.118  -11.162 0.56 18.86 ?  100 VAL   A CG2  1 
ATOM   2175 C CG2  B VAL   A 1 100 ? 18.611 -4.688  -11.316 0.44 21.45 ?  100 VAL   A CG2  1 
ATOM   2176 H H    A VAL   A 1 100 ? 19.727 -2.062  -10.065 0.56 18.47 ?  100 VAL   A H    1 
ATOM   2177 H H    B VAL   A 1 100 ? 20.027 -2.500  -10.407 0.44 21.15 ?  100 VAL   A H    1 
ATOM   2178 H HA   A VAL   A 1 100 ? 20.131 -2.689  -12.551 0.56 20.31 ?  100 VAL   A HA   1 
ATOM   2179 H HA   B VAL   A 1 100 ? 20.400 -3.489  -12.777 0.44 23.75 ?  100 VAL   A HA   1 
ATOM   2180 H HB   A VAL   A 1 100 ? 17.654 -2.221  -11.263 0.56 22.47 ?  100 VAL   A HB   1 
ATOM   2181 H HB   B VAL   A 1 100 ? 17.988 -2.753  -11.499 0.44 25.42 ?  100 VAL   A HB   1 
ATOM   2182 H HG11 A VAL   A 1 100 ? 16.729 -3.537  -13.049 0.56 23.29 ?  100 VAL   A HG11 1 
ATOM   2183 H HG11 B VAL   A 1 100 ? 16.938 -4.145  -13.180 0.44 25.95 ?  100 VAL   A HG11 1 
ATOM   2184 H HG12 A VAL   A 1 100 ? 17.165 -2.070  -13.471 0.56 23.29 ?  100 VAL   A HG12 1 
ATOM   2185 H HG12 B VAL   A 1 100 ? 17.369 -2.694  -13.657 0.44 25.95 ?  100 VAL   A HG12 1 
ATOM   2186 H HG13 A VAL   A 1 100 ? 18.097 -3.309  -13.822 0.56 23.29 ?  100 VAL   A HG13 1 
ATOM   2187 H HG13 B VAL   A 1 100 ? 18.270 -3.952  -14.023 0.44 25.95 ?  100 VAL   A HG13 1 
ATOM   2188 H HG21 A VAL   A 1 100 ? 17.531 -4.564  -11.098 0.56 22.65 ?  100 VAL   A HG21 1 
ATOM   2189 H HG21 B VAL   A 1 100 ? 17.726 -5.042  -11.145 0.44 25.76 ?  100 VAL   A HG21 1 
ATOM   2190 H HG22 A VAL   A 1 100 ? 19.002 -4.659  -11.690 0.56 22.65 ?  100 VAL   A HG22 1 
ATOM   2191 H HG22 B VAL   A 1 100 ? 19.118 -5.307  -11.861 0.44 25.76 ?  100 VAL   A HG22 1 
ATOM   2192 H HG23 A VAL   A 1 100 ? 18.758 -3.983  -10.274 0.56 22.65 ?  100 VAL   A HG23 1 
ATOM   2193 H HG23 B VAL   A 1 100 ? 19.072 -4.526  -10.479 0.44 25.76 ?  100 VAL   A HG23 1 
ATOM   2194 N N    A ASN   A 1 101 ? 19.260 0.335   -12.136 0.56 17.12 ?  101 ASN   A N    1 
ATOM   2195 N N    B ASN   A 1 101 ? 19.654 -0.404  -12.787 0.44 21.09 ?  101 ASN   A N    1 
ATOM   2196 C CA   A ASN   A 1 101 ? 19.168 1.614   -12.825 0.56 18.05 ?  101 ASN   A CA   1 
ATOM   2197 C CA   B ASN   A 1 101 ? 19.581 0.776   -13.638 0.44 22.68 ?  101 ASN   A CA   1 
ATOM   2198 C C    A ASN   A 1 101 ? 20.512 2.087   -13.373 0.56 19.74 ?  101 ASN   A C    1 
ATOM   2199 C C    B ASN   A 1 101 ? 20.915 1.104   -14.294 0.44 24.36 ?  101 ASN   A C    1 
ATOM   2200 O O    A ASN   A 1 101 ? 20.548 3.130   -14.040 0.56 21.61 ?  101 ASN   A O    1 
ATOM   2201 O O    B ASN   A 1 101 ? 20.933 1.854   -15.276 0.44 24.75 ?  101 ASN   A O    1 
ATOM   2202 C CB   A ASN   A 1 101 ? 18.522 2.646   -11.902 0.56 17.09 ?  101 ASN   A CB   1 
ATOM   2203 C CB   B ASN   A 1 101 ? 19.070 1.970   -12.829 0.44 22.95 ?  101 ASN   A CB   1 
ATOM   2204 C CG   A ASN   A 1 101 ? 17.134 2.215   -11.445 0.56 16.60 ?  101 ASN   A CG   1 
ATOM   2205 C CG   B ASN   A 1 101 ? 17.761 1.676   -12.127 0.44 23.47 ?  101 ASN   A CG   1 
ATOM   2206 O OD1  A ASN   A 1 101 ? 16.356 1.672   -12.229 0.56 16.79 ?  101 ASN   A OD1  1 
ATOM   2207 O OD1  B ASN   A 1 101 ? 16.911 0.953   -12.647 0.44 24.31 ?  101 ASN   A OD1  1 
ATOM   2208 N ND2  A ASN   A 1 101 ? 16.832 2.424   -10.170 0.56 17.41 ?  101 ASN   A ND2  1 
ATOM   2209 N ND2  B ASN   A 1 101 ? 17.598 2.228   -10.931 0.44 23.60 ?  101 ASN   A ND2  1 
ATOM   2210 H H    A ASN   A 1 101 ? 19.158 0.375   -11.287 0.56 20.57 ?  101 ASN   A H    1 
ATOM   2211 H H    B ASN   A 1 101 ? 19.585 -0.239  -11.943 0.44 25.33 ?  101 ASN   A H    1 
ATOM   2212 H HA   A ASN   A 1 101 ? 18.582 1.505   -13.587 0.56 21.68 ?  101 ASN   A HA   1 
ATOM   2213 H HA   B ASN   A 1 101 ? 18.945 0.611   -14.346 0.44 27.24 ?  101 ASN   A HA   1 
ATOM   2214 H HB2  A ASN   A 1 101 ? 19.077 2.765   -11.118 0.56 20.53 ?  101 ASN   A HB2  1 
ATOM   2215 H HB2  B ASN   A 1 101 ? 19.725 2.203   -12.153 0.44 27.56 ?  101 ASN   A HB2  1 
ATOM   2216 H HB3  A ASN   A 1 101 ? 18.436 3.487   -12.382 0.56 20.53 ?  101 ASN   A HB3  1 
ATOM   2217 H HB3  B ASN   A 1 101 ? 18.926 2.721   -13.426 0.44 27.56 ?  101 ASN   A HB3  1 
ATOM   2218 H HD21 A ASN   A 1 101 ? 16.059 2.194   -9.870  0.56 20.91 ?  101 ASN   A HD21 1 
ATOM   2219 H HD21 B ASN   A 1 101 ? 16.872 2.091   -10.491 0.44 28.34 ?  101 ASN   A HD21 1 
ATOM   2220 H HD22 A ASN   A 1 101 ? 17.402 2.801   -9.650  0.56 20.91 ?  101 ASN   A HD22 1 
ATOM   2221 H HD22 B ASN   A 1 101 ? 18.216 2.726   -10.600 0.44 28.34 ?  101 ASN   A HD22 1 
ATOM   2222 N N    A LYS   A 1 102 ? 21.597 1.342   -13.127 0.56 21.09 ?  102 LYS   A N    1 
ATOM   2223 N N    B LYS   A 1 102 ? 22.023 0.564   -13.781 0.44 26.21 ?  102 LYS   A N    1 
ATOM   2224 C CA   A LYS   A 1 102 ? 22.882 1.545   -13.787 0.56 22.33 ?  102 LYS   A CA   1 
ATOM   2225 C CA   B LYS   A 1 102 ? 23.347 0.783   -14.355 0.44 27.52 ?  102 LYS   A CA   1 
ATOM   2226 C C    A LYS   A 1 102 ? 23.203 0.454   -14.800 0.56 23.34 ?  102 LYS   A C    1 
ATOM   2227 C C    B LYS   A 1 102 ? 23.812 -0.378  -15.231 0.44 26.68 ?  102 LYS   A C    1 
ATOM   2228 O O    A LYS   A 1 102 ? 24.266 0.512   -15.427 0.56 24.14 ?  102 LYS   A O    1 
ATOM   2229 O O    B LYS   A 1 102 ? 25.003 -0.466  -15.550 0.44 26.93 ?  102 LYS   A O    1 
ATOM   2230 C CB   A LYS   A 1 102 ? 24.018 1.590   -12.758 0.56 23.29 ?  102 LYS   A CB   1 
ATOM   2231 C CB   B LYS   A 1 102 ? 24.378 1.068   -13.258 0.44 29.34 ?  102 LYS   A CB   1 
ATOM   2232 C CG   A LYS   A 1 102 ? 23.909 2.684   -11.724 0.56 23.40 ?  102 LYS   A CG   1 
ATOM   2233 C CG   B LYS   A 1 102 ? 24.555 2.548   -12.948 0.44 30.96 ?  102 LYS   A CG   1 
ATOM   2234 C CD   A LYS   A 1 102 ? 25.080 2.613   -10.755 0.56 24.19 ?  102 LYS   A CD   1 
ATOM   2235 C CD   B LYS   A 1 102 ? 25.412 2.780   -11.708 0.44 32.25 ?  102 LYS   A CD   1 
ATOM   2236 C CE   A LYS   A 1 102 ? 25.011 3.705   -9.705  0.56 24.68 ?  102 LYS   A CE   1 
ATOM   2237 C CE   B LYS   A 1 102 ? 25.432 4.259   -11.340 0.44 33.45 ?  102 LYS   A CE   1 
ATOM   2238 N NZ   A LYS   A 1 102 ? 26.109 3.570   -8.704  0.56 24.89 ?  102 LYS   A NZ   1 
ATOM   2239 N NZ   B LYS   A 1 102 ? 26.262 4.560   -10.136 0.44 34.12 ?  102 LYS   A NZ   1 
ATOM   2240 H H    A LYS   A 1 102 ? 21.609 0.682   -12.571 0.56 25.33 ?  102 LYS   A H    1 
ATOM   2241 H H    B LYS   A 1 102 ? 22.029 0.065   -13.077 0.44 31.47 ?  102 LYS   A H    1 
ATOM   2242 H HA   A LYS   A 1 102 ? 22.867 2.386   -14.258 0.56 26.81 ?  102 LYS   A HA   1 
ATOM   2243 H HA   B LYS   A 1 102 ? 23.304 1.572   -14.913 0.44 33.05 ?  102 LYS   A HA   1 
ATOM   2244 H HB2  A LYS   A 1 102 ? 24.040 0.741   -12.287 0.56 27.97 ?  102 LYS   A HB2  1 
ATOM   2245 H HB2  B LYS   A 1 102 ? 24.101 0.628   -12.441 0.44 35.23 ?  102 LYS   A HB2  1 
ATOM   2246 H HB3  A LYS   A 1 102 ? 24.856 1.716   -13.233 0.56 27.97 ?  102 LYS   A HB3  1 
ATOM   2247 H HB3  B LYS   A 1 102 ? 25.242 0.723   -13.538 0.44 35.23 ?  102 LYS   A HB3  1 
ATOM   2248 H HG2  A LYS   A 1 102 ? 23.924 3.547   -12.166 0.56 28.11 ?  102 LYS   A HG2  1 
ATOM   2249 H HG2  B LYS   A 1 102 ? 24.994 2.981   -13.699 0.44 37.17 ?  102 LYS   A HG2  1 
ATOM   2250 H HG3  A LYS   A 1 102 ? 23.086 2.573   -11.223 0.56 28.11 ?  102 LYS   A HG3  1 
ATOM   2251 H HG3  B LYS   A 1 102 ? 23.687 2.948   -12.793 0.44 37.17 ?  102 LYS   A HG3  1 
ATOM   2252 H HD2  A LYS   A 1 102 ? 25.069 1.754   -10.304 0.56 29.05 ?  102 LYS   A HD2  1 
ATOM   2253 H HD2  B LYS   A 1 102 ? 25.041 2.282   -10.961 0.44 38.72 ?  102 LYS   A HD2  1 
ATOM   2254 H HD3  A LYS   A 1 102 ? 25.909 2.717   -11.250 0.56 29.05 ?  102 LYS   A HD3  1 
ATOM   2255 H HD3  B LYS   A 1 102 ? 26.323 2.494   -11.883 0.44 38.72 ?  102 LYS   A HD3  1 
ATOM   2256 H HE2  A LYS   A 1 102 ? 25.098 4.569   -10.138 0.56 29.63 ?  102 LYS   A HE2  1 
ATOM   2257 H HE2  B LYS   A 1 102 ? 25.795 4.763   -12.085 0.44 40.16 ?  102 LYS   A HE2  1 
ATOM   2258 H HE3  A LYS   A 1 102 ? 24.163 3.645   -9.239  0.56 29.63 ?  102 LYS   A HE3  1 
ATOM   2259 H HE3  B LYS   A 1 102 ? 24.525 4.548   -11.155 0.44 40.16 ?  102 LYS   A HE3  1 
ATOM   2260 H HZ1  A LYS   A 1 102 ? 26.050 4.217   -8.099  0.56 29.89 ?  102 LYS   A HZ1  1 
ATOM   2261 H HZ1  B LYS   A 1 102 ? 26.241 5.434   -9.963  0.44 40.96 ?  102 LYS   A HZ1  1 
ATOM   2262 H HZ2  A LYS   A 1 102 ? 26.049 2.782   -8.293  0.56 29.89 ?  102 LYS   A HZ2  1 
ATOM   2263 H HZ2  B LYS   A 1 102 ? 25.947 4.119   -9.430  0.44 40.96 ?  102 LYS   A HZ2  1 
ATOM   2264 H HZ3  A LYS   A 1 102 ? 26.899 3.622   -9.111  0.56 29.89 ?  102 LYS   A HZ3  1 
ATOM   2265 H HZ3  B LYS   A 1 102 ? 27.105 4.314   -10.277 0.44 40.96 ?  102 LYS   A HZ3  1 
ATOM   2266 N N    A GLY   A 1 103 ? 22.337 -0.548  -14.956 0.56 24.46 ?  103 GLY   A N    1 
ATOM   2267 N N    B GLY   A 1 103 ? 22.907 -1.266  -15.631 0.44 25.95 ?  103 GLY   A N    1 
ATOM   2268 C CA   A GLY   A 1 103 ? 22.568 -1.633  -15.894 0.56 25.48 ?  103 GLY   A CA   1 
ATOM   2269 C CA   B GLY   A 1 103 ? 23.319 -2.378  -16.463 0.44 25.44 ?  103 GLY   A CA   1 
ATOM   2270 C C    A GLY   A 1 103 ? 23.413 -2.772  -15.371 0.56 26.57 ?  103 GLY   A C    1 
ATOM   2271 C C    B GLY   A 1 103 ? 24.066 -3.466  -15.731 0.44 24.72 ?  103 GLY   A C    1 
ATOM   2272 O O    A GLY   A 1 103 ? 23.927 -3.560  -16.171 0.56 27.79 ?  103 GLY   A O    1 
ATOM   2273 O O    B GLY   A 1 103 ? 24.647 -4.346  -16.376 0.44 24.96 ?  103 GLY   A O    1 
ATOM   2274 H H    A GLY   A 1 103 ? 21.604 -0.628  -14.524 0.56 29.37 ?  103 GLY   A H    1 
ATOM   2275 H H    B GLY   A 1 103 ? 22.068 -1.252  -15.427 0.44 31.16 ?  103 GLY   A H    1 
ATOM   2276 H HA2  A GLY   A 1 103 ? 21.708 -1.991  -16.186 0.56 30.60 ?  103 GLY   A HA2  1 
ATOM   2277 H HA2  B GLY   A 1 103 ? 22.539 -2.780  -16.863 0.44 30.55 ?  103 GLY   A HA2  1 
ATOM   2278 H HA3  A GLY   A 1 103 ? 23.024 -1.291  -16.675 0.56 30.60 ?  103 GLY   A HA3  1 
ATOM   2279 H HA3  B GLY   A 1 103 ? 23.883 -2.029  -17.179 0.44 30.55 ?  103 GLY   A HA3  1 
ATOM   2280 N N    A GLU   A 1 104 ? 23.575 -2.890  -14.056 0.56 25.84 ?  104 GLU   A N    1 
ATOM   2281 N N    B GLU   A 1 104 ? 24.052 -3.446  -14.402 0.44 23.29 ?  104 GLU   A N    1 
ATOM   2282 C CA   A GLU   A 1 104 ? 24.453 -3.900  -13.482 0.56 25.39 ?  104 GLU   A CA   1 
ATOM   2283 C CA   B GLU   A 1 104 ? 24.864 -4.367  -13.621 0.44 22.16 ?  104 GLU   A CA   1 
ATOM   2284 C C    A GLU   A 1 104 ? 23.757 -5.257  -13.384 0.56 26.04 ?  104 GLU   A C    1 
ATOM   2285 C C    B GLU   A 1 104 ? 24.175 -5.722  -13.478 0.44 21.70 ?  104 GLU   A C    1 
ATOM   2286 O O    A GLU   A 1 104 ? 22.531 -5.350  -13.268 0.56 26.12 ?  104 GLU   A O    1 
ATOM   2287 O O    B GLU   A 1 104 ? 22.958 -5.810  -13.287 0.44 21.76 ?  104 GLU   A O    1 
ATOM   2288 C CB   A GLU   A 1 104 ? 24.969 -3.424  -12.121 0.56 23.79 ?  104 GLU   A CB   1 
ATOM   2289 C CB   B GLU   A 1 104 ? 25.190 -3.746  -12.260 0.44 22.09 ?  104 GLU   A CB   1 
ATOM   2290 C CG   A GLU   A 1 104 ? 25.782 -2.132  -12.261 0.56 22.58 ?  104 GLU   A CG   1 
ATOM   2291 C CG   B GLU   A 1 104 ? 26.058 -2.486  -12.387 0.44 22.44 ?  104 GLU   A CG   1 
ATOM   2292 C CD   A GLU   A 1 104 ? 26.250 -1.521  -10.953 0.56 21.09 ?  104 GLU   A CD   1 
ATOM   2293 C CD   B GLU   A 1 104 ? 26.219 -1.707  -11.091 0.44 22.98 ?  104 GLU   A CD   1 
ATOM   2294 O OE1  A GLU   A 1 104 ? 25.645 -1.780  -9.893  0.56 19.05 ?  104 GLU   A OE1  1 
ATOM   2295 O OE1  B GLU   A 1 104 ? 25.803 -2.197  -10.023 0.44 23.01 ?  104 GLU   A OE1  1 
ATOM   2296 O OE2  A GLU   A 1 104 ? 27.233 -0.743  -11.011 0.56 22.17 -1 104 GLU   A OE2  1 
ATOM   2297 O OE2  B GLU   A 1 104 ? 26.760 -0.579  -11.156 0.44 23.43 -1 104 GLU   A OE2  1 
ATOM   2298 H H    A GLU   A 1 104 ? 23.196 -2.387  -13.475 0.56 31.03 ?  104 GLU   A H    1 
ATOM   2299 H H    B GLU   A 1 104 ? 23.577 -2.899  -13.936 0.44 27.97 ?  104 GLU   A H    1 
ATOM   2300 H HA   A GLU   A 1 104 ? 25.218 -4.009  -14.063 0.56 30.50 ?  104 GLU   A HA   1 
ATOM   2301 H HA   B GLU   A 1 104 ? 25.704 -4.504  -14.085 0.44 26.62 ?  104 GLU   A HA   1 
ATOM   2302 H HB2  A GLU   A 1 104 ? 24.215 -3.252  -11.534 0.56 28.57 ?  104 GLU   A HB2  1 
ATOM   2303 H HB2  B GLU   A 1 104 ? 24.367 -3.498  -11.815 0.44 26.53 ?  104 GLU   A HB2  1 
ATOM   2304 H HB3  A GLU   A 1 104 ? 25.542 -4.107  -11.738 0.56 28.57 ?  104 GLU   A HB3  1 
ATOM   2305 H HB3  B GLU   A 1 104 ? 25.679 -4.392  -11.729 0.44 26.53 ?  104 GLU   A HB3  1 
ATOM   2306 H HG2  A GLU   A 1 104 ? 26.570 -2.321  -12.790 0.56 27.12 ?  104 GLU   A HG2  1 
ATOM   2307 H HG2  B GLU   A 1 104 ? 26.941 -2.741  -12.699 0.44 26.95 ?  104 GLU   A HG2  1 
ATOM   2308 H HG3  A GLU   A 1 104 ? 25.234 -1.471  -12.713 0.56 27.12 ?  104 GLU   A HG3  1 
ATOM   2309 H HG3  B GLU   A 1 104 ? 25.648 -1.882  -13.026 0.44 26.95 ?  104 GLU   A HG3  1 
ATOM   2310 N N    A ASP   A 1 105 ? 24.566 -6.317  -13.436 0.56 26.57 ?  105 ASP   A N    1 
ATOM   2311 N N    B ASP   A 1 105 ? 24.978 -6.778  -13.579 0.44 22.02 ?  105 ASP   A N    1 
ATOM   2312 C CA   A ASP   A 1 105 ? 24.064 -7.680  -13.581 0.56 27.31 ?  105 ASP   A CA   1 
ATOM   2313 C CA   B ASP   A 1 105 ? 24.484 -8.149  -13.645 0.44 22.80 ?  105 ASP   A CA   1 
ATOM   2314 C C    A ASP   A 1 105 ? 23.410 -8.155  -12.286 0.56 25.37 ?  105 ASP   A C    1 
ATOM   2315 C C    B ASP   A 1 105 ? 23.719 -8.517  -12.380 0.44 22.16 ?  105 ASP   A C    1 
ATOM   2316 O O    A ASP   A 1 105 ? 24.063 -8.223  -11.241 0.56 24.26 ?  105 ASP   A O    1 
ATOM   2317 O O    B ASP   A 1 105 ? 24.286 -8.545  -11.285 0.44 20.38 ?  105 ASP   A O    1 
ATOM   2318 C CB   A ASP   A 1 105 ? 25.224 -8.600  -13.956 0.56 29.80 ?  105 ASP   A CB   1 
ATOM   2319 C CB   B ASP   A 1 105 ? 25.689 -9.073  -13.818 0.44 24.35 ?  105 ASP   A CB   1 
ATOM   2320 C CG   A ASP   A 1 105 ? 24.781 -10.025 -14.192 0.56 32.15 ?  105 ASP   A CG   1 
ATOM   2321 C CG   B ASP   A 1 105 ? 25.306 -10.528 -13.986 0.44 25.63 ?  105 ASP   A CG   1 
ATOM   2322 O OD1  A ASP   A 1 105 ? 23.558 -10.255 -14.294 0.56 32.68 ?  105 ASP   A OD1  1 
ATOM   2323 O OD1  B ASP   A 1 105 ? 24.099 -10.839 -14.042 0.44 25.73 ?  105 ASP   A OD1  1 
ATOM   2324 O OD2  A ASP   A 1 105 ? 25.655 -10.914 -14.276 0.56 33.44 -1 105 ASP   A OD2  1 
ATOM   2325 O OD2  B ASP   A 1 105 ? 26.233 -11.367 -14.053 0.44 26.24 -1 105 ASP   A OD2  1 
ATOM   2326 H H    A ASP   A 1 105 ? 25.424 -6.272  -13.390 0.56 31.91 ?  105 ASP   A H    1 
ATOM   2327 H H    B ASP   A 1 105 ? 25.829 -6.713  -13.621 0.44 26.45 ?  105 ASP   A H    1 
ATOM   2328 H HA   A ASP   A 1 105 ? 23.406 -7.718  -14.293 0.56 32.79 ?  105 ASP   A HA   1 
ATOM   2329 H HA   B ASP   A 1 105 ? 23.892 -8.247  -14.407 0.44 27.38 ?  105 ASP   A HA   1 
ATOM   2330 H HB2  A ASP   A 1 105 ? 25.636 -8.282  -14.777 0.56 35.78 ?  105 ASP   A HB2  1 
ATOM   2331 H HB2  B ASP   A 1 105 ? 26.193 -8.786  -14.596 0.44 29.25 ?  105 ASP   A HB2  1 
ATOM   2332 H HB3  A ASP   A 1 105 ? 25.882 -8.597  -13.240 0.56 35.78 ?  105 ASP   A HB3  1 
ATOM   2333 H HB3  B ASP   A 1 105 ? 26.241 -9.018  -13.025 0.44 29.25 ?  105 ASP   A HB3  1 
ATOM   2334 N N    A ILE   A 1 106 ? 22.126 -8.518  -12.364 0.56 24.48 ?  106 ILE   A N    1 
ATOM   2335 N N    B ILE   A 1 106 ? 22.429 -8.824  -12.534 0.44 23.30 ?  106 ILE   A N    1 
ATOM   2336 C CA   A ILE   A 1 106 ? 21.384 -8.956  -11.186 0.56 23.39 ?  106 ILE   A CA   1 
ATOM   2337 C CA   B ILE   A 1 106 ? 21.622 -9.193  -11.378 0.44 24.36 ?  106 ILE   A CA   1 
ATOM   2338 C C    A ILE   A 1 106 ? 21.944 -10.247 -10.604 0.56 22.39 ?  106 ILE   A C    1 
ATOM   2339 C C    B ILE   A 1 106 ? 22.105 -10.490 -10.750 0.44 24.41 ?  106 ILE   A C    1 
ATOM   2340 O O    A ILE   A 1 106 ? 21.732 -10.527 -9.420  0.56 21.63 ?  106 ILE   A O    1 
ATOM   2341 O O    B ILE   A 1 106 ? 21.839 -10.737 -9.569  0.44 24.26 ?  106 ILE   A O    1 
ATOM   2342 C CB   A ILE   A 1 106 ? 19.878 -9.078  -11.515 0.56 24.52 ?  106 ILE   A CB   1 
ATOM   2343 C CB   B ILE   A 1 106 ? 20.122 -9.251  -11.735 0.44 25.79 ?  106 ILE   A CB   1 
ATOM   2344 C CG1  A ILE   A 1 106 ? 19.041 -9.186  -10.238 0.56 24.63 ?  106 ILE   A CG1  1 
ATOM   2345 C CG1  B ILE   A 1 106 ? 19.269 -9.069  -10.480 0.44 26.80 ?  106 ILE   A CG1  1 
ATOM   2346 C CG2  A ILE   A 1 106 ? 19.619 -10.289 -12.387 0.56 25.35 ?  106 ILE   A CG2  1 
ATOM   2347 C CG2  B ILE   A 1 106 ? 19.781 -10.580 -12.363 0.44 26.18 ?  106 ILE   A CG2  1 
ATOM   2348 C CD1  A ILE   A 1 106 ? 19.099 -7.961  -9.358  0.56 24.72 ?  106 ILE   A CD1  1 
ATOM   2349 C CD1  B ILE   A 1 106 ? 19.555 -7.794  -9.723  0.44 27.43 ?  106 ILE   A CD1  1 
ATOM   2350 H H    A ILE   A 1 106 ? 21.666 -8.514  -13.087 0.56 29.40 ?  106 ILE   A H    1 
ATOM   2351 H H    B ILE   A 1 106 ? 22.010 -8.812  -13.281 0.44 27.98 ?  106 ILE   A H    1 
ATOM   2352 H HA   A ILE   A 1 106 ? 21.482 -8.278  -10.502 0.56 28.09 ?  106 ILE   A HA   1 
ATOM   2353 H HA   B ILE   A 1 106 ? 21.747 -8.506  -10.713 0.44 29.26 ?  106 ILE   A HA   1 
ATOM   2354 H HB   A ILE   A 1 106 ? 19.604 -8.284  -11.998 0.56 29.45 ?  106 ILE   A HB   1 
ATOM   2355 H HB   B ILE   A 1 106 ? 19.919 -8.538  -12.364 0.44 30.97 ?  106 ILE   A HB   1 
ATOM   2356 H HG12 A ILE   A 1 106 ? 18.114 -9.323  -10.486 0.56 29.58 ?  106 ILE   A HG12 1 
ATOM   2357 H HG12 B ILE   A 1 106 ? 18.335 -9.055  -10.737 0.44 32.18 ?  106 ILE   A HG12 1 
ATOM   2358 H HG13 A ILE   A 1 106 ? 19.355 -9.940  -9.717  0.56 29.58 ?  106 ILE   A HG13 1 
ATOM   2359 H HG13 B ILE   A 1 106 ? 19.435 -9.812  -9.880  0.44 32.18 ?  106 ILE   A HG13 1 
ATOM   2360 H HG21 A ILE   A 1 106 ? 18.733 -10.212 -12.772 0.56 30.45 ?  106 ILE   A HG21 1 
ATOM   2361 H HG21 B ILE   A 1 106 ? 18.941 -10.494 -12.835 0.44 31.43 ?  106 ILE   A HG21 1 
ATOM   2362 H HG22 A ILE   A 1 106 ? 20.287 -10.318 -13.087 0.56 30.45 ?  106 ILE   A HG22 1 
ATOM   2363 H HG22 B ILE   A 1 106 ? 20.487 -10.825 -12.977 0.44 31.43 ?  106 ILE   A HG22 1 
ATOM   2364 H HG23 A ILE   A 1 106 ? 19.675 -11.088 -11.840 0.56 30.45 ?  106 ILE   A HG23 1 
ATOM   2365 H HG23 B ILE   A 1 106 ? 19.702 -11.247 -11.662 0.44 31.43 ?  106 ILE   A HG23 1 
ATOM   2366 H HD11 A ILE   A 1 106 ? 18.386 -8.009  -8.703  0.56 29.69 ?  106 ILE   A HD11 1 
ATOM   2367 H HD11 B ILE   A 1 106 ? 18.769 -7.547  -9.218  0.44 32.94 ?  106 ILE   A HD11 1 
ATOM   2368 H HD12 A ILE   A 1 106 ? 19.959 -7.934  -8.906  0.56 29.69 ?  106 ILE   A HD12 1 
ATOM   2369 H HD12 B ILE   A 1 106 ? 20.302 -7.946  -9.121  0.44 32.94 ?  106 ILE   A HD12 1 
ATOM   2370 H HD13 A ILE   A 1 106 ? 18.990 -7.169  -9.908  0.56 29.69 ?  106 ILE   A HD13 1 
ATOM   2371 H HD13 B ILE   A 1 106 ? 19.777 -7.095  -10.357 0.44 32.94 ?  106 ILE   A HD13 1 
ATOM   2372 N N    A GLN   A 1 107 ? 22.680 -11.031 -11.400 0.56 23.42 ?  107 GLN   A N    1 
ATOM   2373 N N    B GLN   A 1 107 ? 22.816 -11.329 -11.510 0.44 24.80 ?  107 GLN   A N    1 
ATOM   2374 C CA   A GLN   A 1 107 ? 23.255 -12.274 -10.890 0.56 25.28 ?  107 GLN   A CA   1 
ATOM   2375 C CA   B GLN   A 1 107 ? 23.473 -12.486 -10.917 0.44 26.12 ?  107 GLN   A CA   1 
ATOM   2376 C C    A GLN   A 1 107 ? 24.236 -12.009 -9.754  0.56 23.53 ?  107 GLN   A C    1 
ATOM   2377 C C    B GLN   A 1 107 ? 24.403 -12.085 -9.780  0.44 23.84 ?  107 GLN   A C    1 
ATOM   2378 O O    A GLN   A 1 107 ? 24.430 -12.863 -8.882  0.56 24.52 ?  107 GLN   A O    1 
ATOM   2379 O O    B GLN   A 1 107 ? 24.719 -12.921 -8.927  0.44 24.65 ?  107 GLN   A O    1 
ATOM   2380 C CB   A GLN   A 1 107 ? 23.930 -13.046 -12.030 0.56 28.97 ?  107 GLN   A CB   1 
ATOM   2381 C CB   B GLN   A 1 107 ? 24.262 -13.251 -11.986 0.44 29.40 ?  107 GLN   A CB   1 
ATOM   2382 C CG   A GLN   A 1 107 ? 23.027 -13.266 -13.237 0.56 32.94 ?  107 GLN   A CG   1 
ATOM   2383 C CG   B GLN   A 1 107 ? 23.409 -13.807 -13.117 0.44 32.76 ?  107 GLN   A CG   1 
ATOM   2384 C CD   A GLN   A 1 107 ? 21.753 -14.015 -12.888 0.56 36.03 ?  107 GLN   A CD   1 
ATOM   2385 C CD   B GLN   A 1 107 ? 22.447 -14.880 -12.648 0.44 35.52 ?  107 GLN   A CD   1 
ATOM   2386 O OE1  A GLN   A 1 107 ? 21.787 -15.029 -12.189 0.56 37.43 ?  107 GLN   A OE1  1 
ATOM   2387 O OE1  B GLN   A 1 107 ? 22.743 -15.634 -11.720 0.44 36.62 ?  107 GLN   A OE1  1 
ATOM   2388 N NE2  A GLN   A 1 107 ? 20.619 -13.514 -13.368 0.56 37.08 ?  107 GLN   A NE2  1 
ATOM   2389 N NE2  B GLN   A 1 107 ? 21.283 -14.951 -13.286 0.44 36.65 ?  107 GLN   A NE2  1 
ATOM   2390 H H    A GLN   A 1 107 ? 22.875 -10.857 -12.218 0.56 28.13 ?  107 GLN   A H    1 
ATOM   2391 H H    B GLN   A 1 107 ? 22.933 -11.251 -12.358 0.44 29.78 ?  107 GLN   A H    1 
ATOM   2392 H HA   A GLN   A 1 107 ? 22.549 -12.829 -10.542 0.56 30.36 ?  107 GLN   A HA   1 
ATOM   2393 H HA   B GLN   A 1 107 ? 22.801 -13.087 -10.558 0.44 31.37 ?  107 GLN   A HA   1 
ATOM   2394 H HB2  A GLN   A 1 107 ? 24.710 -12.556 -12.334 0.56 34.79 ?  107 GLN   A HB2  1 
ATOM   2395 H HB2  B GLN   A 1 107 ? 24.918 -12.656 -12.381 0.44 35.30 ?  107 GLN   A HB2  1 
ATOM   2396 H HB3  A GLN   A 1 107 ? 24.199 -13.922 -11.707 0.56 34.79 ?  107 GLN   A HB3  1 
ATOM   2397 H HB3  B GLN   A 1 107 ? 24.713 -14.002 -11.568 0.44 35.30 ?  107 GLN   A HB3  1 
ATOM   2398 H HG2  A GLN   A 1 107 ? 22.777 -12.406 -13.608 0.56 39.55 ?  107 GLN   A HG2  1 
ATOM   2399 H HG2  B GLN   A 1 107 ? 22.888 -13.087 -13.506 0.44 39.33 ?  107 GLN   A HG2  1 
ATOM   2400 H HG3  A GLN   A 1 107 ? 23.509 -13.784 -13.902 0.56 39.55 ?  107 GLN   A HG3  1 
ATOM   2401 H HG3  B GLN   A 1 107 ? 23.988 -14.198 -13.792 0.44 39.33 ?  107 GLN   A HG3  1 
ATOM   2402 H HE21 A GLN   A 1 107 ? 20.633 -12.802 -13.850 0.56 44.51 ?  107 GLN   A HE21 1 
ATOM   2403 H HE21 B GLN   A 1 107 ? 21.111 -14.405 -13.929 0.44 44.00 ?  107 GLN   A HE21 1 
ATOM   2404 H HE22 A GLN   A 1 107 ? 19.871 -13.903 -13.197 0.56 44.51 ?  107 GLN   A HE22 1 
ATOM   2405 H HE22 B GLN   A 1 107 ? 20.702 -15.542 -13.057 0.44 44.00 ?  107 GLN   A HE22 1 
ATOM   2406 N N    . LEU   A 1 108 ? 24.842 -10.824 -9.737  1.00 20.78 ?  108 LEU   A N    1 
ATOM   2407 C CA   . LEU   A 1 108 ? 25.739 -10.403 -8.671  1.00 17.35 ?  108 LEU   A CA   1 
ATOM   2408 C C    . LEU   A 1 108 ? 25.020 -10.215 -7.343  1.00 14.99 ?  108 LEU   A C    1 
ATOM   2409 O O    . LEU   A 1 108 ? 25.688 -10.043 -6.324  1.00 15.51 ?  108 LEU   A O    1 
ATOM   2410 C CB   . LEU   A 1 108 ? 26.477 -9.117  -9.068  1.00 17.76 ?  108 LEU   A CB   1 
ATOM   2411 C CG   . LEU   A 1 108 ? 27.481 -9.316  -10.205 1.00 19.55 ?  108 LEU   A CG   1 
ATOM   2412 C CD1  . LEU   A 1 108 ? 27.969 -7.976  -10.743 1.00 20.41 ?  108 LEU   A CD1  1 
ATOM   2413 C CD2  . LEU   A 1 108 ? 28.661 -10.161 -9.745  1.00 21.53 ?  108 LEU   A CD2  1 
ATOM   2414 H H    A LEU   A 1 108 ? 24.749 -10.236 -10.351 0.56 24.96 ?  108 LEU   A H    1 
ATOM   2415 H H    B LEU   A 1 108 ? 24.646 -10.216 -10.304 0.44 24.96 ?  108 LEU   A H    1 
ATOM   2416 H HA   . LEU   A 1 108 ? 26.406 -11.094 -8.536  1.00 20.84 ?  108 LEU   A HA   1 
ATOM   2417 H HB2  . LEU   A 1 108 ? 25.825 -8.462  -9.361  1.00 21.34 ?  108 LEU   A HB2  1 
ATOM   2418 H HB3  . LEU   A 1 108 ? 26.960 -8.784  -8.299  1.00 21.34 ?  108 LEU   A HB3  1 
ATOM   2419 H HG   . LEU   A 1 108 ? 27.048 -9.789  -10.933 1.00 23.49 ?  108 LEU   A HG   1 
ATOM   2420 H HD11 . LEU   A 1 108 ? 28.590 -8.136  -11.477 1.00 24.51 ?  108 LEU   A HD11 1 
ATOM   2421 H HD12 . LEU   A 1 108 ? 27.211 -7.467  -11.062 1.00 24.51 ?  108 LEU   A HD12 1 
ATOM   2422 H HD13 . LEU   A 1 108 ? 28.421 -7.494  -10.034 1.00 24.51 ?  108 LEU   A HD13 1 
ATOM   2423 H HD21 . LEU   A 1 108 ? 29.355 -10.126 -10.419 1.00 25.86 ?  108 LEU   A HD21 1 
ATOM   2424 H HD22 . LEU   A 1 108 ? 28.993 -9.803  -8.906  1.00 25.86 ?  108 LEU   A HD22 1 
ATOM   2425 H HD23 . LEU   A 1 108 ? 28.364 -11.075 -9.619  1.00 25.86 ?  108 LEU   A HD23 1 
ATOM   2426 N N    . LEU   A 1 109 ? 23.684 -10.277 -7.317  1.00 14.29 ?  109 LEU   A N    1 
ATOM   2427 C CA   . LEU   A 1 109 ? 22.972 -10.142 -6.052  1.00 13.44 ?  109 LEU   A CA   1 
ATOM   2428 C C    . LEU   A 1 109 ? 23.301 -11.293 -5.106  1.00 13.21 ?  109 LEU   A C    1 
ATOM   2429 O O    . LEU   A 1 109 ? 23.445 -11.095 -3.895  1.00 13.89 ?  109 LEU   A O    1 
ATOM   2430 C CB   . LEU   A 1 109 ? 21.469 -10.063 -6.319  1.00 14.64 ?  109 LEU   A CB   1 
ATOM   2431 C CG   . LEU   A 1 109 ? 20.564 -9.772  -5.121  1.00 14.65 ?  109 LEU   A CG   1 
ATOM   2432 C CD1  . LEU   A 1 109 ? 21.024 -8.516  -4.406  1.00 15.07 ?  109 LEU   A CD1  1 
ATOM   2433 C CD2  . LEU   A 1 109 ? 19.117 -9.623  -5.571  1.00 16.29 ?  109 LEU   A CD2  1 
ATOM   2434 H H    . LEU   A 1 109 ? 23.181 -10.394 -8.003  1.00 17.17 ?  109 LEU   A H    1 
ATOM   2435 H HA   . LEU   A 1 109 ? 23.248 -9.313  -5.627  1.00 16.15 ?  109 LEU   A HA   1 
ATOM   2436 H HB2  . LEU   A 1 109 ? 21.313 -9.361  -6.969  1.00 17.59 ?  109 LEU   A HB2  1 
ATOM   2437 H HB3  . LEU   A 1 109 ? 21.183 -10.911 -6.689  1.00 17.59 ?  109 LEU   A HB3  1 
ATOM   2438 H HG   . LEU   A 1 109 ? 20.610 -10.509 -4.495  1.00 17.60 ?  109 LEU   A HG   1 
ATOM   2439 H HD11 . LEU   A 1 109 ? 20.336 -8.224  -3.792  1.00 18.11 ?  109 LEU   A HD11 1 
ATOM   2440 H HD12 . LEU   A 1 109 ? 21.844 -8.708  -3.921  1.00 18.11 ?  109 LEU   A HD12 1 
ATOM   2441 H HD13 . LEU   A 1 109 ? 21.192 -7.820  -5.067  1.00 18.11 ?  109 LEU   A HD13 1 
ATOM   2442 H HD21 . LEU   A 1 109 ? 18.573 -9.335  -4.819  1.00 19.57 ?  109 LEU   A HD21 1 
ATOM   2443 H HD22 . LEU   A 1 109 ? 19.066 -8.962  -6.281  1.00 19.57 ?  109 LEU   A HD22 1 
ATOM   2444 H HD23 . LEU   A 1 109 ? 18.793 -10.479 -5.900  1.00 19.57 ?  109 LEU   A HD23 1 
ATOM   2445 N N    . LYS   A 1 110 ? 23.436 -12.506 -5.637  1.00 13.72 ?  110 LYS   A N    1 
ATOM   2446 C CA   . LYS   A 1 110 ? 23.802 -13.621 -4.770  1.00 13.90 ?  110 LYS   A CA   1 
ATOM   2447 C C    . LYS   A 1 110 ? 25.181 -13.400 -4.159  1.00 13.45 ?  110 LYS   A C    1 
ATOM   2448 O O    . LYS   A 1 110 ? 25.371 -13.601 -2.957  1.00 13.68 ?  110 LYS   A O    1 
ATOM   2449 C CB   . LYS   A 1 110 ? 23.735 -14.945 -5.530  1.00 14.76 ?  110 LYS   A CB   1 
ATOM   2450 C CG   . LYS   A 1 110 ? 23.898 -16.159 -4.612  1.00 15.39 ?  110 LYS   A CG   1 
ATOM   2451 C CD   . LYS   A 1 110 ? 23.697 -17.479 -5.342  1.00 15.42 ?  110 LYS   A CD   1 
ATOM   2452 C CE   . LYS   A 1 110 ? 23.805 -18.667 -4.400  1.00 16.02 ?  110 LYS   A CE   1 
ATOM   2453 N NZ   . LYS   A 1 110 ? 22.637 -18.788 -3.487  1.00 16.40 ?  110 LYS   A NZ   1 
ATOM   2454 H H    . LYS   A 1 110 ? 23.322 -12.704 -6.461  1.00 16.48 ?  110 LYS   A H    1 
ATOM   2455 H HA   . LYS   A 1 110 ? 23.163 -13.671 -4.040  1.00 16.70 ?  110 LYS   A HA   1 
ATOM   2456 H HB2  . LYS   A 1 110 ? 22.875 -15.016 -5.969  1.00 17.74 ?  110 LYS   A HB2  1 
ATOM   2457 H HB3  . LYS   A 1 110 ? 24.450 -14.972 -6.183  1.00 17.74 ?  110 LYS   A HB3  1 
ATOM   2458 H HG2  . LYS   A 1 110 ? 24.788 -16.155 -4.230  1.00 18.50 ?  110 LYS   A HG2  1 
ATOM   2459 H HG3  . LYS   A 1 110 ? 23.235 -16.107 -3.902  1.00 18.50 ?  110 LYS   A HG3  1 
ATOM   2460 H HD2  . LYS   A 1 110 ? 22.818 -17.492 -5.743  1.00 18.53 ?  110 LYS   A HD2  1 
ATOM   2461 H HD3  . LYS   A 1 110 ? 24.383 -17.569 -6.022  1.00 18.53 ?  110 LYS   A HD3  1 
ATOM   2462 H HE2  . LYS   A 1 110 ? 23.864 -19.483 -4.924  1.00 19.25 ?  110 LYS   A HE2  1 
ATOM   2463 H HE3  . LYS   A 1 110 ? 24.605 -18.570 -3.854  1.00 19.25 ?  110 LYS   A HE3  1 
ATOM   2464 H HZ1  . LYS   A 1 110 ? 22.737 -19.490 -2.954  1.00 19.70 ?  110 LYS   A HZ1  1 
ATOM   2465 H HZ2  . LYS   A 1 110 ? 22.568 -18.052 -2.988  1.00 19.70 ?  110 LYS   A HZ2  1 
ATOM   2466 H HZ3  . LYS   A 1 110 ? 21.892 -18.884 -3.963  1.00 19.70 ?  110 LYS   A HZ3  1 
ATOM   2467 N N    . SER   A 1 111 ? 26.146 -12.959 -4.973  1.00 13.14 ?  111 SER   A N    1 
ATOM   2468 C CA   . SER   A 1 111 ? 27.476 -12.651 -4.455  1.00 13.25 ?  111 SER   A CA   1 
ATOM   2469 C C    . SER   A 1 111 ? 27.409 -11.600 -3.352  1.00 12.80 ?  111 SER   A C    1 
ATOM   2470 O O    . SER   A 1 111 ? 28.103 -11.704 -2.335  1.00 13.50 ?  111 SER   A O    1 
ATOM   2471 C CB   . SER   A 1 111 ? 28.366 -12.164 -5.600  1.00 14.89 ?  111 SER   A CB   1 
ATOM   2472 O OG   . SER   A 1 111 ? 28.464 -13.159 -6.610  1.00 16.37 ?  111 SER   A OG   1 
ATOM   2473 H H    . SER   A 1 111 ? 26.049 -12.833 -5.817  1.00 15.79 ?  111 SER   A H    1 
ATOM   2474 H HA   . SER   A 1 111 ? 27.869 -13.459 -4.088  1.00 15.93 ?  111 SER   A HA   1 
ATOM   2475 H HB2  . SER   A 1 111 ? 27.972 -11.369 -5.990  1.00 17.90 ?  111 SER   A HB2  1 
ATOM   2476 H HB3  . SER   A 1 111 ? 29.247 -11.970 -5.256  1.00 17.90 ?  111 SER   A HB3  1 
ATOM   2477 H HG   . SER   A 1 111 ? 28.964 -12.884 -7.239  1.00 19.66 ?  111 SER   A HG   1 
ATOM   2478 N N    . ALA   A 1 112 ? 26.567 -10.582 -3.532  1.00 12.88 ?  112 ALA   A N    1 
ATOM   2479 C CA   . ALA   A 1 112 ? 26.426 -9.549  -2.509  1.00 12.61 ?  112 ALA   A CA   1 
ATOM   2480 C C    . ALA   A 1 112 ? 25.930 -10.143 -1.193  1.00 12.86 ?  112 ALA   A C    1 
ATOM   2481 O O    . ALA   A 1 112 ? 26.469 -9.849  -0.121  1.00 12.61 ?  112 ALA   A O    1 
ATOM   2482 C CB   . ALA   A 1 112 ? 25.465 -8.464  -3.000  1.00 13.23 ?  112 ALA   A CB   1 
ATOM   2483 H H    . ALA   A 1 112 ? 26.076 -10.464 -4.226  1.00 15.47 ?  112 ALA   A H    1 
ATOM   2484 H HA   . ALA   A 1 112 ? 27.290 -9.131  -2.349  1.00 15.15 ?  112 ALA   A HA   1 
ATOM   2485 H HB1  . ALA   A 1 112 ? 25.398 -7.767  -2.323  1.00 15.90 ?  112 ALA   A HB1  1 
ATOM   2486 H HB2  . ALA   A 1 112 ? 25.808 -8.083  -3.824  1.00 15.90 ?  112 ALA   A HB2  1 
ATOM   2487 H HB3  . ALA   A 1 112 ? 24.593 -8.857  -3.154  1.00 15.90 ?  112 ALA   A HB3  1 
ATOM   2488 N N    . TYR   A 1 113 ? 24.882 -10.976 -1.250  1.00 12.90 ?  113 TYR   A N    1 
ATOM   2489 C CA   . TYR   A 1 113 ? 24.368 -11.583 -0.025  1.00 12.71 ?  113 TYR   A CA   1 
ATOM   2490 C C    . TYR   A 1 113 ? 25.370 -12.537 0.630   1.00 12.40 ?  113 TYR   A C    1 
ATOM   2491 O O    . TYR   A 1 113 ? 25.330 -12.716 1.851   1.00 12.93 ?  113 TYR   A O    1 
ATOM   2492 C CB   . TYR   A 1 113 ? 23.050 -12.307 -0.299  1.00 13.13 ?  113 TYR   A CB   1 
ATOM   2493 C CG   . TYR   A 1 113 ? 21.836 -11.404 -0.238  1.00 12.81 ?  113 TYR   A CG   1 
ATOM   2494 C CD1  . TYR   A 1 113 ? 21.459 -10.794 0.952   1.00 12.95 ?  113 TYR   A CD1  1 
ATOM   2495 C CD2  . TYR   A 1 113 ? 21.044 -11.191 -1.361  1.00 13.04 ?  113 TYR   A CD2  1 
ATOM   2496 C CE1  . TYR   A 1 113 ? 20.339 -9.993  1.018   1.00 13.15 ?  113 TYR   A CE1  1 
ATOM   2497 C CE2  . TYR   A 1 113 ? 19.896 -10.389 -1.297  1.00 13.40 ?  113 TYR   A CE2  1 
ATOM   2498 C CZ   . TYR   A 1 113 ? 19.563 -9.800  -0.102  1.00 13.09 ?  113 TYR   A CZ   1 
ATOM   2499 O OH   . TYR   A 1 113 ? 18.439 -9.002  0.000   1.00 13.93 ?  113 TYR   A OH   1 
ATOM   2500 H H    . TYR   A 1 113 ? 24.474 -11.202 -1.972  1.00 15.50 ?  113 TYR   A H    1 
ATOM   2501 H HA   . TYR   A 1 113 ? 24.190 -10.883 0.610   1.00 15.28 ?  113 TYR   A HA   1 
ATOM   2502 H HB2  . TYR   A 1 113 ? 23.081 -12.696 -1.186  1.00 15.78 ?  113 TYR   A HB2  1 
ATOM   2503 H HB3  . TYR   A 1 113 ? 22.934 -13.007 0.363   1.00 15.78 ?  113 TYR   A HB3  1 
ATOM   2504 H HD1  . TYR   A 1 113 ? 21.977 -10.933 1.720   1.00 15.56 ?  113 TYR   A HD1  1 
ATOM   2505 H HD2  . TYR   A 1 113 ? 21.267 -11.604 -2.162  1.00 15.67 ?  113 TYR   A HD2  1 
ATOM   2506 H HE1  . TYR   A 1 113 ? 20.104 -9.598  1.827   1.00 15.80 ?  113 TYR   A HE1  1 
ATOM   2507 H HE2  . TYR   A 1 113 ? 19.368 -10.249 -2.049  1.00 16.10 ?  113 TYR   A HE2  1 
ATOM   2508 H HH   . TYR   A 1 113 ? 18.061 -8.969  -0.750  1.00 16.74 ?  113 TYR   A HH   1 
ATOM   2509 N N    . GLU   A 1 114 ? 26.273 -13.152 -0.144  1.00 12.73 ?  114 GLU   A N    1 
ATOM   2510 C CA   . GLU   A 1 114 ? 27.262 -14.047 0.460   1.00 13.24 ?  114 GLU   A CA   1 
ATOM   2511 C C    . GLU   A 1 114 ? 28.102 -13.329 1.513   1.00 12.84 ?  114 GLU   A C    1 
ATOM   2512 O O    . GLU   A 1 114 ? 28.578 -13.961 2.465   1.00 12.86 ?  114 GLU   A O    1 
ATOM   2513 C CB   . GLU   A 1 114 ? 28.140 -14.698 -0.621  1.00 13.10 ?  114 GLU   A CB   1 
ATOM   2514 C CG   . GLU   A 1 114 ? 27.382 -15.746 -1.417  1.00 13.77 ?  114 GLU   A CG   1 
ATOM   2515 C CD   . GLU   A 1 114 ? 28.113 -16.280 -2.642  1.00 14.27 ?  114 GLU   A CD   1 
ATOM   2516 O OE1  . GLU   A 1 114 ? 29.066 -15.648 -3.133  1.00 14.32 ?  114 GLU   A OE1  1 
ATOM   2517 O OE2  . GLU   A 1 114 ? 27.683 -17.345 -3.141  1.00 15.43 -1 114 GLU   A OE2  1 
ATOM   2518 H H    . GLU   A 1 114 ? 26.339 -13.061 -1.000  1.00 15.30 ?  114 GLU   A H    1 
ATOM   2519 H HA   . GLU   A 1 114 ? 26.792 -14.760 0.907   1.00 15.91 ?  114 GLU   A HA   1 
ATOM   2520 H HB2  . GLU   A 1 114 ? 28.448 -14.015 -1.243  1.00 15.74 ?  114 GLU   A HB2  1 
ATOM   2521 H HB3  . GLU   A 1 114 ? 28.901 -15.130 -0.203  1.00 15.74 ?  114 GLU   A HB3  1 
ATOM   2522 H HG2  . GLU   A 1 114 ? 27.206 -16.506 -0.842  1.00 16.55 ?  114 GLU   A HG2  1 
ATOM   2523 H HG3  . GLU   A 1 114 ? 26.542 -15.365 -1.718  1.00 16.55 ?  114 GLU   A HG3  1 
ATOM   2524 N N    . ASN   A 1 115 ? 28.283 -12.014 1.377   1.00 12.74 ?  115 ASN   A N    1 
ATOM   2525 C CA   . ASN   A 1 115 ? 29.047 -11.285 2.383   1.00 13.34 ?  115 ASN   A CA   1 
ATOM   2526 C C    . ASN   A 1 115 ? 28.421 -11.414 3.766   1.00 12.95 ?  115 ASN   A C    1 
ATOM   2527 O O    . ASN   A 1 115 ? 29.132 -11.346 4.776   1.00 12.94 ?  115 ASN   A O    1 
ATOM   2528 C CB   . ASN   A 1 115 ? 29.156 -9.813  2.000   1.00 13.11 ?  115 ASN   A CB   1 
ATOM   2529 C CG   . ASN   A 1 115 ? 29.964 -9.601  0.746   1.00 13.54 ?  115 ASN   A CG   1 
ATOM   2530 O OD1  . ASN   A 1 115 ? 31.185 -9.706  0.777   1.00 16.36 ?  115 ASN   A OD1  1 
ATOM   2531 N ND2  . ASN   A 1 115 ? 29.302 -9.301  -0.360  1.00 13.22 ?  115 ASN   A ND2  1 
ATOM   2532 H H    . ASN   A 1 115 ? 27.977 -11.532 0.734   1.00 15.31 ?  115 ASN   A H    1 
ATOM   2533 H HA   . ASN   A 1 115 ? 29.941 -11.652 2.428   1.00 16.02 ?  115 ASN   A HA   1 
ATOM   2534 H HB2  . ASN   A 1 115 ? 28.261 -9.458  1.858   1.00 15.75 ?  115 ASN   A HB2  1 
ATOM   2535 H HB3  . ASN   A 1 115 ? 29.586 -9.330  2.725   1.00 15.75 ?  115 ASN   A HB3  1 
ATOM   2536 H HD21 . ASN   A 1 115 ? 29.723 -9.170  -1.097  1.00 15.88 ?  115 ASN   A HD21 1 
ATOM   2537 H HD22 . ASN   A 1 115 ? 28.438 -9.257  -0.347  1.00 15.88 ?  115 ASN   A HD22 1 
ATOM   2538 N N    . PHE   A 1 116 ? 27.092 -11.586 3.837   1.00 13.07 ?  116 PHE   A N    1 
ATOM   2539 C CA   . PHE   A 1 116 ? 26.432 -11.680 5.136   1.00 12.91 ?  116 PHE   A CA   1 
ATOM   2540 C C    . PHE   A 1 116 ? 26.908 -12.906 5.915   1.00 12.98 ?  116 PHE   A C    1 
ATOM   2541 O O    . PHE   A 1 116 ? 26.834 -12.924 7.147   1.00 13.44 ?  116 PHE   A O    1 
ATOM   2542 C CB   . PHE   A 1 116 ? 24.905 -11.814 4.982   1.00 13.18 ?  116 PHE   A CB   1 
ATOM   2543 C CG   . PHE   A 1 116 ? 24.155 -10.567 4.521   1.00 12.69 ?  116 PHE   A CG   1 
ATOM   2544 C CD1  . PHE   A 1 116 ? 24.738 -9.541  3.786   1.00 12.75 ?  116 PHE   A CD1  1 
ATOM   2545 C CD2  . PHE   A 1 116 ? 22.799 -10.459 4.829   1.00 13.07 ?  116 PHE   A CD2  1 
ATOM   2546 C CE1  . PHE   A 1 116 ? 23.975 -8.460  3.363   1.00 13.09 ?  116 PHE   A CE1  1 
ATOM   2547 C CE2  . PHE   A 1 116 ? 22.043 -9.370  4.425   1.00 13.56 ?  116 PHE   A CE2  1 
ATOM   2548 C CZ   . PHE   A 1 116 ? 22.624 -8.376  3.688   1.00 12.85 ?  116 PHE   A CZ   1 
ATOM   2549 H H    . PHE   A 1 116 ? 26.562 -11.638 3.159   1.00 15.70 ?  116 PHE   A H    1 
ATOM   2550 H HA   . PHE   A 1 116 ? 26.615 -10.888 5.660   1.00 15.51 ?  116 PHE   A HA   1 
ATOM   2551 H HB2  . PHE   A 1 116 ? 24.724 -12.516 4.332   1.00 15.84 ?  116 PHE   A HB2  1 
ATOM   2552 H HB3  . PHE   A 1 116 ? 24.533 -12.077 5.840   1.00 15.84 ?  116 PHE   A HB3  1 
ATOM   2553 H HD1  . PHE   A 1 116 ? 25.633 -9.602  3.556   1.00 15.32 ?  116 PHE   A HD1  1 
ATOM   2554 H HD2  . PHE   A 1 116 ? 22.387 -11.144 5.318   1.00 15.71 ?  116 PHE   A HD2  1 
ATOM   2555 H HE1  . PHE   A 1 116 ? 24.376 -7.774  2.879   1.00 15.73 ?  116 PHE   A HE1  1 
ATOM   2556 H HE2  . PHE   A 1 116 ? 21.136 -9.325  4.646   1.00 16.30 ?  116 PHE   A HE2  1 
ATOM   2557 H HZ   . PHE   A 1 116 ? 22.123 -7.635  3.425   1.00 15.45 ?  116 PHE   A HZ   1 
ATOM   2558 N N    . ASN   A 1 117 ? 27.361 -13.953 5.218   1.00 12.95 ?  117 ASN   A N    1 
ATOM   2559 C CA   . ASN   A 1 117 ? 27.724 -15.194 5.895   1.00 13.91 ?  117 ASN   A CA   1 
ATOM   2560 C C    . ASN   A 1 117 ? 28.978 -15.077 6.740   1.00 14.39 ?  117 ASN   A C    1 
ATOM   2561 O O    . ASN   A 1 117 ? 29.265 -15.997 7.514   1.00 14.89 ?  117 ASN   A O    1 
ATOM   2562 C CB   . ASN   A 1 117 ? 27.851 -16.325 4.879   1.00 13.82 ?  117 ASN   A CB   1 
ATOM   2563 C CG   . ASN   A 1 117 ? 26.501 -16.715 4.325   1.00 13.75 ?  117 ASN   A CG   1 
ATOM   2564 O OD1  . ASN   A 1 117 ? 25.515 -16.730 5.059   1.00 14.85 ?  117 ASN   A OD1  1 
ATOM   2565 N ND2  . ASN   A 1 117 ? 26.439 -16.984 3.037   1.00 13.63 ?  117 ASN   A ND2  1 
ATOM   2566 H H    . ASN   A 1 117 ? 27.448 -13.972 4.358   1.00 15.56 ?  117 ASN   A H    1 
ATOM   2567 H HA   . ASN   A 1 117 ? 26.997 -15.431 6.491   1.00 16.71 ?  117 ASN   A HA   1 
ATOM   2568 H HB2  . ASN   A 1 117 ? 28.408 -16.030 4.139   1.00 16.60 ?  117 ASN   A HB2  1 
ATOM   2569 H HB3  . ASN   A 1 117 ? 28.238 -17.098 5.307   1.00 16.60 ?  117 ASN   A HB3  1 
ATOM   2570 H HD21 . ASN   A 1 117 ? 25.695 -17.208 2.684   1.00 16.38 ?  117 ASN   A HD21 1 
ATOM   2571 H HD22 . ASN   A 1 117 ? 27.159 -16.959 2.562   1.00 16.38 ?  117 ASN   A HD22 1 
ATOM   2572 N N    . GLN   A 1 118 ? 29.713 -13.970 6.630   1.00 14.17 ?  118 GLN   A N    1 
ATOM   2573 C CA   . GLN   A 1 118 ? 30.877 -13.745 7.471   1.00 14.88 ?  118 GLN   A CA   1 
ATOM   2574 C C    . GLN   A 1 118 ? 30.526 -13.164 8.834   1.00 15.30 ?  118 GLN   A C    1 
ATOM   2575 O O    . GLN   A 1 118 ? 31.447 -12.868 9.607   1.00 16.02 ?  118 GLN   A O    1 
ATOM   2576 C CB   . GLN   A 1 118 ? 31.888 -12.846 6.751   1.00 15.40 ?  118 GLN   A CB   1 
ATOM   2577 C CG   . GLN   A 1 118 ? 32.351 -13.411 5.425   1.00 15.45 ?  118 GLN   A CG   1 
ATOM   2578 C CD   . GLN   A 1 118 ? 33.198 -14.662 5.595   1.00 15.63 ?  118 GLN   A CD   1 
ATOM   2579 O OE1  . GLN   A 1 118 ? 34.066 -14.728 6.473   1.00 16.07 ?  118 GLN   A OE1  1 
ATOM   2580 N NE2  . GLN   A 1 118 ? 32.954 -15.661 4.752   1.00 15.50 ?  118 GLN   A NE2  1 
ATOM   2581 H H    . GLN   A 1 118 ? 29.545 -13.325 6.083   1.00 17.02 ?  118 GLN   A H    1 
ATOM   2582 H HA   . GLN   A 1 118 ? 31.305 -14.604 7.627   1.00 17.87 ?  118 GLN   A HA   1 
ATOM   2583 H HB2  . GLN   A 1 118 ? 31.476 -11.985 6.587   1.00 18.50 ?  118 GLN   A HB2  1 
ATOM   2584 H HB3  . GLN   A 1 118 ? 32.666 -12.738 7.322   1.00 18.50 ?  118 GLN   A HB3  1 
ATOM   2585 H HG2  . GLN   A 1 118 ? 31.576 -13.642 4.886   1.00 18.56 ?  118 GLN   A HG2  1 
ATOM   2586 H HG3  . GLN   A 1 118 ? 32.888 -12.748 4.967   1.00 18.56 ?  118 GLN   A HG3  1 
ATOM   2587 H HE21 . GLN   A 1 118 ? 32.338 -15.576 4.152   1.00 18.62 ?  118 GLN   A HE21 1 
ATOM   2588 H HE22 . GLN   A 1 118 ? 33.400 -16.391 4.806   1.00 18.62 ?  118 GLN   A HE22 1 
ATOM   2589 N N    . HIS   A 1 119 ? 29.236 -12.995 9.139   1.00 14.63 ?  119 HIS   A N    1 
ATOM   2590 C CA   . HIS   A 1 119 ? 28.781 -12.385 10.382  1.00 14.91 ?  119 HIS   A CA   1 
ATOM   2591 C C    . HIS   A 1 119 ? 27.641 -13.206 10.955  1.00 15.48 ?  119 HIS   A C    1 
ATOM   2592 O O    . HIS   A 1 119 ? 26.705 -13.555 10.233  1.00 15.74 ?  119 HIS   A O    1 
ATOM   2593 C CB   . HIS   A 1 119 ? 28.328 -10.955 10.098  1.00 14.87 ?  119 HIS   A CB   1 
ATOM   2594 C CG   . HIS   A 1 119 ? 29.415 -10.148 9.481   1.00 16.07 ?  119 HIS   A CG   1 
ATOM   2595 N ND1  . HIS   A 1 119 ? 30.387 -9.528  10.233  1.00 18.14 ?  119 HIS   A ND1  1 
ATOM   2596 C CD2  . HIS   A 1 119 ? 29.752 -9.954  8.186   1.00 16.62 ?  119 HIS   A CD2  1 
ATOM   2597 C CE1  . HIS   A 1 119 ? 31.255 -8.946  9.424   1.00 18.04 ?  119 HIS   A CE1  1 
ATOM   2598 N NE2  . HIS   A 1 119 ? 30.899 -9.197  8.177   1.00 18.30 ?  119 HIS   A NE2  1 
ATOM   2599 H H    . HIS   A 1 119 ? 28.584 -13.243 8.625   1.00 17.57 ?  119 HIS   A H    1 
ATOM   2600 H HA   . HIS   A 1 119 ? 29.506 -12.366 11.020  1.00 17.91 ?  119 HIS   A HA   1 
ATOM   2601 H HB2  . HIS   A 1 119 ? 27.574 -10.976 9.485   1.00 17.86 ?  119 HIS   A HB2  1 
ATOM   2602 H HB3  . HIS   A 1 119 ? 28.068 -10.535 10.932  1.00 17.86 ?  119 HIS   A HB3  1 
ATOM   2603 H HD2  . HIS   A 1 119 ? 29.294 -10.271 7.439   1.00 19.96 ?  119 HIS   A HD2  1 
ATOM   2604 H HE1  . HIS   A 1 119 ? 31.986 -8.437  9.687   1.00 21.67 ?  119 HIS   A HE1  1 
ATOM   2605 H HE2  . HIS   A 1 119 ? 31.301 -8.906  7.473   1.00 21.98 ?  119 HIS   A HE2  1 
ATOM   2606 N N    A GLU   A 1 120 ? 27.731 -13.534 12.245  0.56 15.52 ?  120 GLU   A N    1 
ATOM   2607 N N    B GLU   A 1 120 ? 27.704 -13.463 12.264  0.44 16.69 ?  120 GLU   A N    1 
ATOM   2608 C CA   A GLU   A 1 120 ? 26.770 -14.472 12.825  0.56 17.19 ?  120 GLU   A CA   1 
ATOM   2609 C CA   B GLU   A 1 120 ? 26.740 -14.365 12.892  0.44 18.86 ?  120 GLU   A CA   1 
ATOM   2610 C C    A GLU   A 1 120 ? 25.354 -13.907 12.881  0.56 16.16 ?  120 GLU   A C    1 
ATOM   2611 C C    B GLU   A 1 120 ? 25.331 -13.777 12.927  0.44 18.22 ?  120 GLU   A C    1 
ATOM   2612 O O    A GLU   A 1 120 ? 24.382 -14.673 12.791  0.56 15.84 ?  120 GLU   A O    1 
ATOM   2613 O O    B GLU   A 1 120 ? 24.349 -14.508 12.746  0.44 18.64 ?  120 GLU   A O    1 
ATOM   2614 C CB   A GLU   A 1 120 ? 27.221 -14.894 14.224  0.56 21.19 ?  120 GLU   A CB   1 
ATOM   2615 C CB   B GLU   A 1 120 ? 27.208 -14.743 14.299  0.44 22.51 ?  120 GLU   A CB   1 
ATOM   2616 C CG   A GLU   A 1 120 ? 28.434 -15.812 14.227  0.56 26.03 ?  120 GLU   A CG   1 
ATOM   2617 C CG   B GLU   A 1 120 ? 28.394 -15.696 14.323  0.44 26.68 ?  120 GLU   A CG   1 
ATOM   2618 C CD   A GLU   A 1 120 ? 28.632 -16.521 15.550  0.56 30.30 ?  120 GLU   A CD   1 
ATOM   2619 C CD   B GLU   A 1 120 ? 28.498 -16.458 15.628  0.44 30.40 ?  120 GLU   A CD   1 
ATOM   2620 O OE1  A GLU   A 1 120 ? 28.250 -15.952 16.595  0.56 32.88 ?  120 GLU   A OE1  1 
ATOM   2621 O OE1  B GLU   A 1 120 ? 28.102 -15.902 16.675  0.44 32.15 ?  120 GLU   A OE1  1 
ATOM   2622 O OE2  A GLU   A 1 120 ? 29.170 -17.649 15.544  0.56 32.53 -1 120 GLU   A OE2  1 
ATOM   2623 O OE2  B GLU   A 1 120 ? 28.966 -17.616 15.606  0.44 32.57 -1 120 GLU   A OE2  1 
ATOM   2624 H H    A GLU   A 1 120 ? 28.330 -13.240 12.788  0.56 18.65 ?  120 GLU   A H    1 
ATOM   2625 H H    B GLU   A 1 120 ? 28.292 -13.132 12.799  0.44 20.05 ?  120 GLU   A H    1 
ATOM   2626 H HA   A GLU   A 1 120 ? 26.756 -15.272 12.276  0.56 20.65 ?  120 GLU   A HA   1 
ATOM   2627 H HA   B GLU   A 1 120 ? 26.702 -15.179 12.373  0.44 22.66 ?  120 GLU   A HA   1 
ATOM   2628 H HB2  A GLU   A 1 120 ? 27.450 -14.105 14.737  0.56 25.45 ?  120 GLU   A HB2  1 
ATOM   2629 H HB2  B GLU   A 1 120 ? 27.470 -13.941 14.775  0.44 27.03 ?  120 GLU   A HB2  1 
ATOM   2630 H HB3  A GLU   A 1 120 ? 26.493 -15.368 14.659  0.56 25.45 ?  120 GLU   A HB3  1 
ATOM   2631 H HB3  B GLU   A 1 120 ? 26.477 -15.178 14.767  0.44 27.03 ?  120 GLU   A HB3  1 
ATOM   2632 H HG2  A GLU   A 1 120 ? 28.330 -16.479 13.531  0.56 31.26 ?  120 GLU   A HG2  1 
ATOM   2633 H HG2  B GLU   A 1 120 ? 28.305 -16.338 13.600  0.44 32.04 ?  120 GLU   A HG2  1 
ATOM   2634 H HG3  A GLU   A 1 120 ? 29.231 -15.287 14.071  0.56 31.26 ?  120 GLU   A HG3  1 
ATOM   2635 H HG3  B GLU   A 1 120 ? 29.215 -15.190 14.217  0.44 32.04 ?  120 GLU   A HG3  1 
ATOM   2636 N N    A VAL   A 1 121 ? 25.219 -12.598 13.082  0.56 15.49 ?  121 VAL   A N    1 
ATOM   2637 N N    B VAL   A 1 121 ? 25.202 -12.474 13.176  0.44 17.28 ?  121 VAL   A N    1 
ATOM   2638 C CA   A VAL   A 1 121 ? 23.931 -11.918 13.161  0.56 15.13 ?  121 VAL   A CA   1 
ATOM   2639 C CA   B VAL   A 1 121 ? 23.897 -11.826 13.299  0.44 16.57 ?  121 VAL   A CA   1 
ATOM   2640 C C    A VAL   A 1 121 ? 24.071 -10.562 12.476  0.56 14.17 ?  121 VAL   A C    1 
ATOM   2641 C C    B VAL   A 1 121 ? 23.975 -10.447 12.661  0.44 14.56 ?  121 VAL   A C    1 
ATOM   2642 O O    A VAL   A 1 121 ? 25.102 -9.896  12.609  0.56 15.08 ?  121 VAL   A O    1 
ATOM   2643 O O    B VAL   A 1 121 ? 24.873 -9.664  12.987  0.44 12.92 ?  121 VAL   A O    1 
ATOM   2644 C CB   A VAL   A 1 121 ? 23.488 -11.717 14.629  0.56 17.55 ?  121 VAL   A CB   1 
ATOM   2645 C CB   B VAL   A 1 121 ? 23.441 -11.702 14.768  0.44 18.72 ?  121 VAL   A CB   1 
ATOM   2646 C CG1  A VAL   A 1 121 ? 22.093 -11.103 14.699  0.56 18.37 ?  121 VAL   A CG1  1 
ATOM   2647 C CG1  B VAL   A 1 121 ? 22.089 -11.006 14.846  0.44 19.25 ?  121 VAL   A CG1  1 
ATOM   2648 C CG2  A VAL   A 1 121 ? 23.514 -13.021 15.402  0.56 18.87 ?  121 VAL   A CG2  1 
ATOM   2649 C CG2  B VAL   A 1 121 ? 23.361 -13.062 15.436  0.44 19.84 ?  121 VAL   A CG2  1 
ATOM   2650 H H    A VAL   A 1 121 ? 25.885 -12.072 13.197  0.56 18.62 ?  121 VAL   A H    1 
ATOM   2651 H H    B VAL   A 1 121 ? 25.867 -11.932 13.272  0.44 20.75 ?  121 VAL   A H    1 
ATOM   2652 H HA   A VAL   A 1 121 ? 23.256 -12.451 12.704  0.56 18.17 ?  121 VAL   A HA   1 
ATOM   2653 H HA   B VAL   A 1 121 ? 23.238 -12.343 12.820  0.44 19.90 ?  121 VAL   A HA   1 
ATOM   2654 H HB   A VAL   A 1 121 ? 24.102 -11.105 15.061  0.56 21.09 ?  121 VAL   A HB   1 
ATOM   2655 H HB   B VAL   A 1 121 ? 24.080 -11.162 15.258  0.44 22.48 ?  121 VAL   A HB   1 
ATOM   2656 H HG11 A VAL   A 1 121 ? 21.803 -11.078 15.627  0.56 22.07 ?  121 VAL   A HG11 1 
ATOM   2657 H HG11 B VAL   A 1 121 ? 21.721 -11.131 15.736  0.44 23.12 ?  121 VAL   A HG11 1 
ATOM   2658 H HG12 A VAL   A 1 121 ? 22.121 -10.203 14.340  0.56 22.07 ?  121 VAL   A HG12 1 
ATOM   2659 H HG12 B VAL   A 1 121 ? 22.203 -10.061 14.666  0.44 23.12 ?  121 VAL   A HG12 1 
ATOM   2660 H HG13 A VAL   A 1 121 ? 21.479 -11.648 14.181  0.56 22.07 ?  121 VAL   A HG13 1 
ATOM   2661 H HG13 B VAL   A 1 121 ? 21.493 -11.400 14.188  0.44 23.12 ?  121 VAL   A HG13 1 
ATOM   2662 H HG21 A VAL   A 1 121 ? 23.154 -12.867 16.294  0.56 22.67 ?  121 VAL   A HG21 1 
ATOM   2663 H HG21 B VAL   A 1 121 ? 23.019 -12.951 16.340  0.44 23.84 ?  121 VAL   A HG21 1 
ATOM   2664 H HG22 A VAL   A 1 121 ? 22.965 -13.675 14.939  0.56 22.67 ?  121 VAL   A HG22 1 
ATOM   2665 H HG22 B VAL   A 1 121 ? 22.762 -13.630 14.927  0.44 23.84 ?  121 VAL   A HG22 1 
ATOM   2666 H HG23 A VAL   A 1 121 ? 24.425 -13.336 15.465  0.56 22.67 ?  121 VAL   A HG23 1 
ATOM   2667 H HG23 B VAL   A 1 121 ? 24.246 -13.453 15.465  0.44 23.84 ?  121 VAL   A HG23 1 
ATOM   2668 N N    . LEU   A 1 122 ? 23.018 -10.135 11.780  1.00 13.64 ?  122 LEU   A N    1 
ATOM   2669 C CA   . LEU   A 1 122 ? 23.016 -8.846  11.093  1.00 13.34 ?  122 LEU   A CA   1 
ATOM   2670 C C    . LEU   A 1 122 ? 21.621 -8.243  11.039  1.00 13.46 ?  122 LEU   A C    1 
ATOM   2671 O O    . LEU   A 1 122 ? 20.629 -8.959  10.887  1.00 14.33 ?  122 LEU   A O    1 
ATOM   2672 C CB   . LEU   A 1 122 ? 23.461 -8.962  9.631   1.00 15.34 ?  122 LEU   A CB   1 
ATOM   2673 C CG   . LEU   A 1 122 ? 24.673 -9.808  9.272   1.00 15.13 ?  122 LEU   A CG   1 
ATOM   2674 C CD1  . LEU   A 1 122 ? 24.268 -11.256 9.033   1.00 15.35 ?  122 LEU   A CD1  1 
ATOM   2675 C CD2  . LEU   A 1 122 ? 25.372 -9.226  8.045   1.00 14.74 ?  122 LEU   A CD2  1 
ATOM   2676 H H    A LEU   A 1 122 ? 22.276 -10.569 11.701  0.56 16.39 ?  122 LEU   A H    1 
ATOM   2677 H H    B LEU   A 1 122 ? 22.362 -10.653 11.566  0.44 16.39 ?  122 LEU   A H    1 
ATOM   2678 H HA   . LEU   A 1 122 ? 23.607 -8.226  11.550  1.00 16.03 ?  122 LEU   A HA   1 
ATOM   2679 H HB2  . LEU   A 1 122 ? 22.728 -9.325  9.125   1.00 18.43 ?  122 LEU   A HB2  1 
ATOM   2680 H HB3  . LEU   A 1 122 ? 23.662 -8.071  9.313   1.00 18.43 ?  122 LEU   A HB3  1 
ATOM   2681 H HG   . LEU   A 1 122 ? 25.317 -9.799  10.000  1.00 18.18 ?  122 LEU   A HG   1 
ATOM   2682 H HD11 . LEU   A 1 122 ? 25.051 -11.781 8.796   1.00 18.44 ?  122 LEU   A HD11 1 
ATOM   2683 H HD12 . LEU   A 1 122 ? 23.870 -11.610 9.843   1.00 18.44 ?  122 LEU   A HD12 1 
ATOM   2684 H HD13 . LEU   A 1 122 ? 23.621 -11.289 8.308   1.00 18.44 ?  122 LEU   A HD13 1 
ATOM   2685 H HD21 . LEU   A 1 122 ? 26.122 -9.799  7.792   1.00 17.71 ?  122 LEU   A HD21 1 
ATOM   2686 H HD22 . LEU   A 1 122 ? 24.742 -9.179  7.308   1.00 17.71 ?  122 LEU   A HD22 1 
ATOM   2687 H HD23 . LEU   A 1 122 ? 25.703 -8.338  8.254   1.00 17.71 ?  122 LEU   A HD23 1 
ATOM   2688 N N    A LEU   A 1 123 ? 21.564 -6.915  11.099  0.56 13.32 ?  123 LEU   A N    1 
ATOM   2689 N N    B LEU   A 1 123 ? 21.565 -6.921  11.206  0.44 13.22 ?  123 LEU   A N    1 
ATOM   2690 C CA   A LEU   A 1 123 ? 20.400 -6.137  10.683  0.56 12.77 ?  123 LEU   A CA   1 
ATOM   2691 C CA   B LEU   A 1 123 ? 20.391 -6.111  10.903  0.44 12.73 ?  123 LEU   A CA   1 
ATOM   2692 C C    A LEU   A 1 123 ? 20.661 -5.652  9.264   0.56 12.22 ?  123 LEU   A C    1 
ATOM   2693 C C    B LEU   A 1 123 ? 20.616 -5.527  9.517   0.44 12.05 ?  123 LEU   A C    1 
ATOM   2694 O O    A LEU   A 1 123 ? 21.744 -5.129  8.989   0.56 12.28 ?  123 LEU   A O    1 
ATOM   2695 O O    B LEU   A 1 123 ? 21.616 -4.835  9.301   0.44 11.90 ?  123 LEU   A O    1 
ATOM   2696 C CB   A LEU   A 1 123 ? 20.232 -4.938  11.618  0.56 13.26 ?  123 LEU   A CB   1 
ATOM   2697 C CB   B LEU   A 1 123 ? 20.247 -4.985  11.929  0.44 13.30 ?  123 LEU   A CB   1 
ATOM   2698 C CG   A LEU   A 1 123 ? 19.182 -3.875  11.290  0.56 13.86 ?  123 LEU   A CG   1 
ATOM   2699 C CG   B LEU   A 1 123 ? 19.218 -3.898  11.599  0.44 13.62 ?  123 LEU   A CG   1 
ATOM   2700 C CD1  A LEU   A 1 123 ? 17.778 -4.463  11.287  0.56 14.47 ?  123 LEU   A CD1  1 
ATOM   2701 C CD1  B LEU   A 1 123 ? 17.809 -4.481  11.517  0.44 14.50 ?  123 LEU   A CD1  1 
ATOM   2702 C CD2  A LEU   A 1 123 ? 19.280 -2.705  12.273  0.56 13.69 ?  123 LEU   A CD2  1 
ATOM   2703 C CD2  B LEU   A 1 123 ? 19.285 -2.767  12.617  0.44 14.93 ?  123 LEU   A CD2  1 
ATOM   2704 H H    A LEU   A 1 123 ? 22.214 -6.430  11.391  0.56 16.01 ?  123 LEU   A H    1 
ATOM   2705 H H    B LEU   A 1 123 ? 22.229 -6.453  11.495  0.44 15.89 ?  123 LEU   A H    1 
ATOM   2706 H HA   A LEU   A 1 123 ? 19.602 -6.692  10.706  0.56 15.34 ?  123 LEU   A HA   1 
ATOM   2707 H HA   B LEU   A 1 123 ? 19.592 -6.647  10.895  0.44 15.30 ?  123 LEU   A HA   1 
ATOM   2708 H HB2  A LEU   A 1 123 ? 20.014 -5.280  12.496  0.56 15.93 ?  123 LEU   A HB2  1 
ATOM   2709 H HB2  B LEU   A 1 123 ? 19.985 -5.376  12.776  0.44 15.98 ?  123 LEU   A HB2  1 
ATOM   2710 H HB3  A LEU   A 1 123 ? 21.085 -4.483  11.659  0.56 15.93 ?  123 LEU   A HB3  1 
ATOM   2711 H HB3  B LEU   A 1 123 ? 21.106 -4.542  12.030  0.44 15.98 ?  123 LEU   A HB3  1 
ATOM   2712 H HG   A LEU   A 1 123 ? 19.357 -3.521  10.403  0.56 16.66 ?  123 LEU   A HG   1 
ATOM   2713 H HG   B LEU   A 1 123 ? 19.427 -3.511  10.733  0.44 16.37 ?  123 LEU   A HG   1 
ATOM   2714 H HD11 A LEU   A 1 123 ? 17.142 -3.759  11.086  0.56 17.39 ?  123 LEU   A HD11 1 
ATOM   2715 H HD11 B LEU   A 1 123 ? 17.174 -3.760  11.382  0.44 17.42 ?  123 LEU   A HD11 1 
ATOM   2716 H HD12 A LEU   A 1 123 ? 17.730 -5.158  10.614  0.56 17.39 ?  123 LEU   A HD12 1 
ATOM   2717 H HD12 B LEU   A 1 123 ? 17.767 -5.100  10.771  0.44 17.42 ?  123 LEU   A HD12 1 
ATOM   2718 H HD13 A LEU   A 1 123 ? 17.593 -4.836  12.164  0.56 17.39 ?  123 LEU   A HD13 1 
ATOM   2719 H HD13 B LEU   A 1 123 ? 17.611 -4.945  12.345  0.44 17.42 ?  123 LEU   A HD13 1 
ATOM   2720 H HD21 A LEU   A 1 123 ? 18.608 -2.044  12.051  0.56 16.45 ?  123 LEU   A HD21 1 
ATOM   2721 H HD21 B LEU   A 1 123 ? 18.623 -2.097  12.388  0.44 17.93 ?  123 LEU   A HD21 1 
ATOM   2722 H HD22 A LEU   A 1 123 ? 19.127 -3.040  13.175  0.56 16.45 ?  123 LEU   A HD22 1 
ATOM   2723 H HD22 B LEU   A 1 123 ? 19.101 -3.130  13.497  0.44 17.93 ?  123 LEU   A HD22 1 
ATOM   2724 H HD23 A LEU   A 1 123 ? 20.165 -2.313  12.215  0.56 16.45 ?  123 LEU   A HD23 1 
ATOM   2725 H HD23 B LEU   A 1 123 ? 20.173 -2.379  12.596  0.44 17.93 ?  123 LEU   A HD23 1 
ATOM   2726 N N    A ALA   A 1 124 ? 19.688 -5.808  8.365   0.56 11.73 ?  124 ALA   A N    1 
ATOM   2727 N N    B ALA   A 1 124 ? 19.716 -5.803  8.580   0.44 11.77 ?  124 ALA   A N    1 
ATOM   2728 C CA   A ALA   A 1 124 ? 20.001 -5.592  6.959   0.56 11.46 ?  124 ALA   A CA   1 
ATOM   2729 C CA   B ALA   A 1 124 ? 19.970 -5.460  7.191   0.44 11.05 ?  124 ALA   A CA   1 
ATOM   2730 C C    A ALA   A 1 124 ? 18.781 -5.174  6.151   0.56 10.98 ?  124 ALA   A C    1 
ATOM   2731 C C    B ALA   A 1 124 ? 18.725 -4.956  6.484   0.44 10.80 ?  124 ALA   A C    1 
ATOM   2732 O O    A ALA   A 1 124 ? 17.648 -5.548  6.482   0.56 11.18 ?  124 ALA   A O    1 
ATOM   2733 O O    B ALA   A 1 124 ? 17.596 -5.266  6.882   0.44 10.69 ?  124 ALA   A O    1 
ATOM   2734 C CB   A ALA   A 1 124 ? 20.623 -6.854  6.343   0.56 12.42 ?  124 ALA   A CB   1 
ATOM   2735 C CB   B ALA   A 1 124 ? 20.505 -6.662  6.405   0.44 11.00 ?  124 ALA   A CB   1 
ATOM   2736 H H    A ALA   A 1 124 ? 18.870 -6.023  8.540   0.56 14.10 ?  124 ALA   A H    1 
ATOM   2737 H H    B ALA   A 1 124 ? 18.961 -6.187  8.717   0.44 14.15 ?  124 ALA   A H    1 
ATOM   2738 H HA   A ALA   A 1 124 ? 20.664 -4.884  6.912   0.56 13.77 ?  124 ALA   A HA   1 
ATOM   2739 H HA   B ALA   A 1 124 ? 20.646 -4.760  7.161   0.44 13.28 ?  124 ALA   A HA   1 
ATOM   2740 H HB1  A ALA   A 1 124 ? 20.834 -6.684  5.413   0.56 14.93 ?  124 ALA   A HB1  1 
ATOM   2741 H HB1  B ALA   A 1 124 ? 20.663 -6.396  5.484   0.44 13.23 ?  124 ALA   A HB1  1 
ATOM   2742 H HB2  A ALA   A 1 124 ? 21.442 -7.077  6.827   0.56 14.93 ?  124 ALA   A HB2  1 
ATOM   2743 H HB2  B ALA   A 1 124 ? 21.335 -6.956  6.810   0.44 13.23 ?  124 ALA   A HB2  1 
ATOM   2744 H HB3  A ALA   A 1 124 ? 19.995 -7.587  6.415   0.56 14.93 ?  124 ALA   A HB3  1 
ATOM   2745 H HB3  B ALA   A 1 124 ? 19.848 -7.372  6.436   0.44 13.23 ?  124 ALA   A HB3  1 
ATOM   2746 N N    A PRO   A 1 125 ? 18.990 -4.432  5.071   0.56 10.30 ?  125 PRO   A N    1 
ATOM   2747 N N    B PRO   A 1 125 ? 18.910 -4.193  5.412   0.44 10.36 ?  125 PRO   A N    1 
ATOM   2748 C CA   A PRO   A 1 125 ? 17.925 -4.168  4.107   0.56 10.68 ?  125 PRO   A CA   1 
ATOM   2749 C CA   B PRO   A 1 125 ? 17.845 -3.945  4.444   0.44 11.93 ?  125 PRO   A CA   1 
ATOM   2750 C C    A PRO   A 1 125 ? 17.956 -5.223  3.008   0.56 10.07 ?  125 PRO   A C    1 
ATOM   2751 C C    B PRO   A 1 125 ? 17.890 -5.012  3.354   0.44 12.01 ?  125 PRO   A C    1 
ATOM   2752 O O    A PRO   A 1 125 ? 18.920 -5.976  2.864   0.56 10.90 ?  125 PRO   A O    1 
ATOM   2753 O O    B PRO   A 1 125 ? 18.817 -5.823  3.284   0.44 11.82 ?  125 PRO   A O    1 
ATOM   2754 C CB   A PRO   A 1 125 ? 18.367 -2.823  3.530   0.56 11.20 ?  125 PRO   A CB   1 
ATOM   2755 C CB   B PRO   A 1 125 ? 18.271 -2.590  3.863   0.44 11.77 ?  125 PRO   A CB   1 
ATOM   2756 C CG   A PRO   A 1 125 ? 19.871 -2.985  3.439   0.56 10.77 ?  125 PRO   A CG   1 
ATOM   2757 C CG   B PRO   A 1 125 ? 19.781 -2.702  3.814   0.44 11.80 ?  125 PRO   A CG   1 
ATOM   2758 C CD   A PRO   A 1 125 ? 20.264 -3.820  4.649   0.56 9.86  ?  125 PRO   A CD   1 
ATOM   2759 C CD   B PRO   A 1 125 ? 20.166 -3.514  5.028   0.44 11.39 ?  125 PRO   A CD   1 
ATOM   2760 H HA   A PRO   A 1 125 ? 17.047 -4.121  4.529   0.56 12.83 ?  125 PRO   A HA   1 
ATOM   2761 H HA   B PRO   A 1 125 ? 16.968 -3.895  4.852   0.44 14.34 ?  125 PRO   A HA   1 
ATOM   2762 H HB2  A PRO   A 1 125 ? 17.964 -2.697  2.659   0.56 13.47 ?  125 PRO   A HB2  1 
ATOM   2763 H HB2  B PRO   A 1 125 ? 17.901 -2.469  2.972   0.44 14.14 ?  125 PRO   A HB2  1 
ATOM   2764 H HB3  A PRO   A 1 125 ? 18.120 -2.116  4.143   0.56 13.47 ?  125 PRO   A HB3  1 
ATOM   2765 H HB3  B PRO   A 1 125 ? 17.994 -1.870  4.454   0.44 14.14 ?  125 PRO   A HB3  1 
ATOM   2766 H HG2  A PRO   A 1 125 ? 20.097 -3.443  2.613   0.56 12.94 ?  125 PRO   A HG2  1 
ATOM   2767 H HG2  B PRO   A 1 125 ? 20.053 -3.157  2.998   0.44 14.18 ?  125 PRO   A HG2  1 
ATOM   2768 H HG3  A PRO   A 1 125 ? 20.287 -2.110  3.470   0.56 12.94 ?  125 PRO   A HG3  1 
ATOM   2769 H HG3  B PRO   A 1 125 ? 20.182 -1.816  3.854   0.44 14.18 ?  125 PRO   A HG3  1 
ATOM   2770 H HD2  A PRO   A 1 125 ? 20.907 -4.500  4.399   0.56 11.86 ?  125 PRO   A HD2  1 
ATOM   2771 H HD2  B PRO   A 1 125 ? 20.853 -4.158  4.790   0.44 13.70 ?  125 PRO   A HD2  1 
ATOM   2772 H HD3  A PRO   A 1 125 ? 20.604 -3.249  5.356   0.56 11.86 ?  125 PRO   A HD3  1 
ATOM   2773 H HD3  B PRO   A 1 125 ? 20.465 -2.927  5.737   0.44 13.70 ?  125 PRO   A HD3  1 
ATOM   2774 N N    A LEU   A 1 126 ? 16.899 -5.237  2.202   0.56 10.72 ?  126 LEU   A N    1 
ATOM   2775 N N    B LEU   A 1 126 ? 16.868 -4.992  2.496   0.44 13.17 ?  126 LEU   A N    1 
ATOM   2776 C CA   A LEU   A 1 126 ? 16.907 -6.057  0.997   0.56 11.26 ?  126 LEU   A CA   1 
ATOM   2777 C CA   B LEU   A 1 126 ? 16.915 -5.764  1.258   0.44 13.86 ?  126 LEU   A CA   1 
ATOM   2778 C C    A LEU   A 1 126 ? 17.838 -5.430  -0.030  0.56 11.38 ?  126 LEU   A C    1 
ATOM   2779 C C    B LEU   A 1 126 ? 17.910 -5.127  0.297   0.44 14.05 ?  126 LEU   A C    1 
ATOM   2780 O O    A LEU   A 1 126 ? 17.595 -4.324  -0.530  0.56 10.86 ?  126 LEU   A O    1 
ATOM   2781 O O    B LEU   A 1 126 ? 17.885 -3.915  0.088   0.44 15.82 ?  126 LEU   A O    1 
ATOM   2782 C CB   A LEU   A 1 126 ? 15.500 -6.228  0.442   0.56 12.14 ?  126 LEU   A CB   1 
ATOM   2783 C CB   B LEU   A 1 126 ? 15.539 -5.784  0.591   0.44 14.97 ?  126 LEU   A CB   1 
ATOM   2784 C CG   A LEU   A 1 126 ? 14.625 -7.160  1.279   0.56 12.87 ?  126 LEU   A CG   1 
ATOM   2785 C CG   B LEU   A 1 126 ? 14.468 -6.774  1.053   0.44 16.02 ?  126 LEU   A CG   1 
ATOM   2786 C CD1  A LEU   A 1 126 ? 13.195 -7.039  0.806   0.56 13.09 ?  126 LEU   A CD1  1 
ATOM   2787 C CD1  B LEU   A 1 126 ? 13.202 -6.590  0.222   0.44 16.37 ?  126 LEU   A CD1  1 
ATOM   2788 C CD2  A LEU   A 1 126 ? 15.113 -8.601  1.201   0.56 13.31 ?  126 LEU   A CD2  1 
ATOM   2789 C CD2  B LEU   A 1 126 ? 14.954 -8.205  0.952   0.44 16.06 ?  126 LEU   A CD2  1 
ATOM   2790 H H    A LEU   A 1 126 ? 16.178 -4.774  2.317   0.56 12.89 ?  126 LEU   A H    1 
ATOM   2791 H H    B LEU   A 1 126 ? 16.140 -4.542  2.607   0.44 15.82 ?  126 LEU   A H    1 
ATOM   2792 H HA   A LEU   A 1 126 ? 17.252 -6.933  1.214   0.56 13.54 ?  126 LEU   A HA   1 
ATOM   2793 H HA   B LEU   A 1 126 ? 17.195 -6.669  1.444   0.44 16.66 ?  126 LEU   A HA   1 
ATOM   2794 H HB2  A LEU   A 1 126 ? 15.062 -5.362  0.409   0.56 14.59 ?  126 LEU   A HB2  1 
ATOM   2795 H HB2  B LEU   A 1 126 ? 15.154 -4.899  0.691   0.44 17.99 ?  126 LEU   A HB2  1 
ATOM   2796 H HB3  A LEU   A 1 126 ? 15.555 -6.600  -0.455  0.56 14.59 ?  126 LEU   A HB3  1 
ATOM   2797 H HB3  B LEU   A 1 126 ? 15.678 -5.955  -0.354  0.44 17.99 ?  126 LEU   A HB3  1 
ATOM   2798 H HG   A LEU   A 1 126 ? 14.658 -6.883  2.207   0.56 15.46 ?  126 LEU   A HG   1 
ATOM   2799 H HG   B LEU   A 1 126 ? 14.242 -6.593  1.978   0.44 19.25 ?  126 LEU   A HG   1 
ATOM   2800 H HD11 A LEU   A 1 126 ? 12.638 -7.641  1.327   0.56 15.73 ?  126 LEU   A HD11 1 
ATOM   2801 H HD11 B LEU   A 1 126 ? 12.529 -7.221  0.523   0.44 19.66 ?  126 LEU   A HD11 1 
ATOM   2802 H HD12 A LEU   A 1 126 ? 12.900 -6.126  0.927   0.56 15.73 ?  126 LEU   A HD12 1 
ATOM   2803 H HD12 B LEU   A 1 126 ? 12.877 -5.682  0.331   0.44 19.66 ?  126 LEU   A HD12 1 
ATOM   2804 H HD13 A LEU   A 1 126 ? 13.152 -7.283  -0.133  0.56 15.73 ?  126 LEU   A HD13 1 
ATOM   2805 H HD13 B LEU   A 1 126 ? 13.410 -6.754  -0.714  0.44 19.66 ?  126 LEU   A HD13 1 
ATOM   2806 H HD21 A LEU   A 1 126 ? 14.445 -9.186  1.586   0.56 16.00 ?  126 LEU   A HD21 1 
ATOM   2807 H HD21 B LEU   A 1 126 ? 14.216 -8.803  1.142   0.44 19.30 ?  126 LEU   A HD21 1 
ATOM   2808 H HD22 A LEU   A 1 126 ? 15.266 -8.833  0.272   0.56 16.00 ?  126 LEU   A HD22 1 
ATOM   2809 H HD22 B LEU   A 1 126 ? 15.285 -8.360  0.053   0.44 19.30 ?  126 LEU   A HD22 1 
ATOM   2810 H HD23 A LEU   A 1 126 ? 15.946 -8.679  1.699   0.56 16.00 ?  126 LEU   A HD23 1 
ATOM   2811 H HD23 B LEU   A 1 126 ? 15.666 -8.339  1.595   0.44 19.30 ?  126 LEU   A HD23 1 
ATOM   2812 N N    A LEU   A 1 127 ? 18.913 -6.146  -0.340  0.56 11.80 ?  127 LEU   A N    1 
ATOM   2813 N N    B LEU   A 1 127 ? 18.778 -5.935  -0.304  0.44 13.10 ?  127 LEU   A N    1 
ATOM   2814 C CA   A LEU   A 1 127 ? 19.916 -5.642  -1.258  0.56 11.74 ?  127 LEU   A CA   1 
ATOM   2815 C CA   B LEU   A 1 127 ? 19.774 -5.418  -1.233  0.44 12.86 ?  127 LEU   A CA   1 
ATOM   2816 C C    A LEU   A 1 127 ? 19.304 -5.436  -2.633  0.56 11.61 ?  127 LEU   A C    1 
ATOM   2817 C C    B LEU   A 1 127 ? 19.213 -5.344  -2.651  0.44 12.55 ?  127 LEU   A C    1 
ATOM   2818 O O    A LEU   A 1 127 ? 18.495 -6.239  -3.109  0.56 12.11 ?  127 LEU   A O    1 
ATOM   2819 O O    B LEU   A 1 127 ? 18.353 -6.135  -3.051  0.44 12.53 ?  127 LEU   A O    1 
ATOM   2820 C CB   A LEU   A 1 127 ? 21.076 -6.632  -1.346  0.56 12.23 ?  127 LEU   A CB   1 
ATOM   2821 C CB   B LEU   A 1 127 ? 21.043 -6.280  -1.213  0.44 13.16 ?  127 LEU   A CB   1 
ATOM   2822 C CG   A LEU   A 1 127 ? 21.861 -6.873  -0.057  0.56 12.51 ?  127 LEU   A CG   1 
ATOM   2823 C CG   B LEU   A 1 127 ? 21.848 -6.294  0.096   0.44 13.38 ?  127 LEU   A CG   1 
ATOM   2824 C CD1  A LEU   A 1 127 ? 22.962 -7.877  -0.318  0.56 12.95 ?  127 LEU   A CD1  1 
ATOM   2825 C CD1  B LEU   A 1 127 ? 23.012 -7.285  0.031   0.44 14.15 ?  127 LEU   A CD1  1 
ATOM   2826 C CD2  A LEU   A 1 127 ? 22.456 -5.577  0.453   0.56 13.50 ?  127 LEU   A CD2  1 
ATOM   2827 C CD2  B LEU   A 1 127 ? 22.362 -4.903  0.464   0.44 14.07 ?  127 LEU   A CD2  1 
ATOM   2828 H H    A LEU   A 1 127 ? 19.071 -6.936  -0.035  0.56 14.18 ?  127 LEU   A H    1 
ATOM   2829 H H    B LEU   A 1 127 ? 18.808 -6.786  -0.184  0.44 15.74 ?  127 LEU   A H    1 
ATOM   2830 H HA   A LEU   A 1 127 ? 20.253 -4.795  -0.938  0.56 14.12 ?  127 LEU   A HA   1 
ATOM   2831 H HA   B LEU   A 1 127 ? 20.022 -4.523  -0.958  0.44 15.45 ?  127 LEU   A HA   1 
ATOM   2832 H HB2  A LEU   A 1 127 ? 20.723 -7.491  -1.631  0.56 14.69 ?  127 LEU   A HB2  1 
ATOM   2833 H HB2  B LEU   A 1 127 ? 20.791 -7.197  -1.405  0.44 15.82 ?  127 LEU   A HB2  1 
ATOM   2834 H HB3  A LEU   A 1 127 ? 21.705 -6.308  -2.006  0.56 14.69 ?  127 LEU   A HB3  1 
ATOM   2835 H HB3  B LEU   A 1 127 ? 21.635 -5.959  -1.913  0.44 15.82 ?  127 LEU   A HB3  1 
ATOM   2836 H HG   A LEU   A 1 127 ? 21.268 -7.236  0.624   0.56 15.03 ?  127 LEU   A HG   1 
ATOM   2837 H HG   B LEU   A 1 127 ? 21.265 -6.584  0.810   0.44 16.08 ?  127 LEU   A HG   1 
ATOM   2838 H HD11 A LEU   A 1 127 ? 23.423 -8.065  0.515   0.56 15.56 ?  127 LEU   A HD11 1 
ATOM   2839 H HD11 B LEU   A 1 127 ? 23.520 -7.231  0.858   0.44 17.00 ?  127 LEU   A HD11 1 
ATOM   2840 H HD12 A LEU   A 1 127 ? 22.573 -8.692  -0.672  0.56 15.56 ?  127 LEU   A HD12 1 
ATOM   2841 H HD12 B LEU   A 1 127 ? 22.659 -8.182  -0.080  0.44 17.00 ?  127 LEU   A HD12 1 
ATOM   2842 H HD13 A LEU   A 1 127 ? 23.583 -7.501  -0.961  0.56 15.56 ?  127 LEU   A HD13 1 
ATOM   2843 H HD13 B LEU   A 1 127 ? 23.583 -7.059  -0.720  0.44 17.00 ?  127 LEU   A HD13 1 
ATOM   2844 H HD21 A LEU   A 1 127 ? 23.071 -5.776  1.173   0.56 16.22 ?  127 LEU   A HD21 1 
ATOM   2845 H HD21 B LEU   A 1 127 ? 22.941 -4.976  1.240   0.44 16.91 ?  127 LEU   A HD21 1 
ATOM   2846 H HD22 A LEU   A 1 127 ? 22.929 -5.146  -0.278  0.56 16.22 ?  127 LEU   A HD22 1 
ATOM   2847 H HD22 B LEU   A 1 127 ? 22.861 -4.541  -0.286  0.44 16.91 ?  127 LEU   A HD22 1 
ATOM   2848 H HD23 A LEU   A 1 127 ? 21.742 -5.005  0.768   0.56 16.22 ?  127 LEU   A HD23 1 
ATOM   2849 H HD23 B LEU   A 1 127 ? 21.607 -4.331  0.667   0.44 16.91 ?  127 LEU   A HD23 1 
ATOM   2850 N N    A SER   A 1 128 ? 19.698 -4.343  -3.269  0.56 11.84 ?  128 SER   A N    1 
ATOM   2851 N N    B SER   A 1 128 ? 19.707 -4.364  -3.404  0.44 12.71 ?  128 SER   A N    1 
ATOM   2852 C CA   A SER   A 1 128 ? 19.287 -3.957  -4.607  0.56 12.01 ?  128 SER   A CA   1 
ATOM   2853 C CA   B SER   A 1 128 ? 19.404 -4.105  -4.809  0.44 12.49 ?  128 SER   A CA   1 
ATOM   2854 C C    A SER   A 1 128 ? 17.823 -3.537  -4.684  0.56 11.79 ?  128 SER   A C    1 
ATOM   2855 C C    B SER   A 1 128 ? 17.972 -3.639  -5.064  0.44 12.74 ?  128 SER   A C    1 
ATOM   2856 O O    A SER   A 1 128 ? 17.346 -3.248  -5.782  0.56 12.81 ?  128 SER   A O    1 
ATOM   2857 O O    B SER   A 1 128 ? 17.632 -3.357  -6.218  0.44 12.93 ?  128 SER   A O    1 
ATOM   2858 C CB   A SER   A 1 128 ? 19.633 -5.008  -5.673  0.56 12.29 ?  128 SER   A CB   1 
ATOM   2859 C CB   B SER   A 1 128 ? 19.769 -5.272  -5.739  0.44 12.47 ?  128 SER   A CB   1 
ATOM   2860 O OG   A SER   A 1 128 ? 21.044 -5.194  -5.748  0.56 12.81 ?  128 SER   A OG   1 
ATOM   2861 O OG   B SER   A 1 128 ? 21.173 -5.485  -5.757  0.44 12.44 ?  128 SER   A OG   1 
ATOM   2862 H H    A SER   A 1 128 ? 20.242 -3.774  -2.919  0.56 14.23 ?  128 SER   A H    1 
ATOM   2863 H H    B SER   A 1 128 ? 20.273 -3.795  -3.093  0.44 15.28 ?  128 SER   A H    1 
ATOM   2864 H HA   A SER   A 1 128 ? 19.794 -3.173  -4.834  0.56 14.44 ?  128 SER   A HA   1 
ATOM   2865 H HA   B SER   A 1 128 ? 19.960 -3.365  -5.077  0.44 15.01 ?  128 SER   A HA   1 
ATOM   2866 H HB2  A SER   A 1 128 ? 19.209 -5.850  -5.446  0.56 14.77 ?  128 SER   A HB2  1 
ATOM   2867 H HB2  B SER   A 1 128 ? 19.321 -6.073  -5.430  0.44 14.98 ?  128 SER   A HB2  1 
ATOM   2868 H HB3  A SER   A 1 128 ? 19.313 -4.698  -6.536  0.56 14.77 ?  128 SER   A HB3  1 
ATOM   2869 H HB3  B SER   A 1 128 ? 19.482 -5.052  -6.640  0.44 14.98 ?  128 SER   A HB3  1 
ATOM   2870 H HG   A SER   A 1 128 ? 21.417 -4.467  -5.933  0.56 15.39 ?  128 SER   A HG   1 
ATOM   2871 H HG   B SER   A 1 128 ? 21.559 -4.773  -5.979  0.44 14.95 ?  128 SER   A HG   1 
ATOM   2872 N N    A ALA   A 1 129 ? 17.106 -3.477  -3.560  0.56 11.97 ?  129 ALA   A N    1 
ATOM   2873 N N    B ALA   A 1 129 ? 17.130 -3.541  -4.038  0.44 12.96 ?  129 ALA   A N    1 
ATOM   2874 C CA   A ALA   A 1 129 ? 15.727 -3.014  -3.543  0.56 11.18 ?  129 ALA   A CA   1 
ATOM   2875 C CA   B ALA   A 1 129 ? 15.774 -3.040  -4.206  0.44 12.91 ?  129 ALA   A CA   1 
ATOM   2876 C C    A ALA   A 1 129 ? 15.692 -1.486  -3.511  0.56 10.97 ?  129 ALA   A C    1 
ATOM   2877 C C    B ALA   A 1 129 ? 15.784 -1.506  -4.174  0.44 13.89 ?  129 ALA   A C    1 
ATOM   2878 O O    A ALA   A 1 129 ? 16.724 -0.806  -3.531  0.56 11.73 ?  129 ALA   A O    1 
ATOM   2879 O O    B ALA   A 1 129 ? 16.837 -0.862  -4.141  0.44 13.55 ?  129 ALA   A O    1 
ATOM   2880 C CB   A ALA   A 1 129 ? 14.980 -3.612  -2.348  0.56 11.97 ?  129 ALA   A CB   1 
ATOM   2881 C CB   B ALA   A 1 129 ? 14.848 -3.671  -3.161  0.44 12.88 ?  129 ALA   A CB   1 
ATOM   2882 H H    A ALA   A 1 129 ? 17.399 -3.709  -2.783  0.56 14.38 ?  129 ALA   A H    1 
ATOM   2883 H H    B ALA   A 1 129 ? 17.320 -3.765  -3.226  0.44 15.57 ?  129 ALA   A H    1 
ATOM   2884 H HA   A ALA   A 1 129 ? 15.277 -3.316  -4.347  0.56 13.44 ?  129 ALA   A HA   1 
ATOM   2885 H HA   B ALA   A 1 129 ? 15.444 -3.313  -5.075  0.44 15.52 ?  129 ALA   A HA   1 
ATOM   2886 H HB1  A ALA   A 1 129 ? 14.058 -3.298  -2.355  0.56 14.38 ?  129 ALA   A HB1  1 
ATOM   2887 H HB1  B ALA   A 1 129 ? 13.945 -3.335  -3.288  0.44 15.48 ?  129 ALA   A HB1  1 
ATOM   2888 H HB2  A ALA   A 1 129 ? 14.996 -4.580  -2.406  0.56 14.38 ?  129 ALA   A HB2  1 
ATOM   2889 H HB2  B ALA   A 1 129 ? 14.852 -4.639  -3.272  0.44 15.48 ?  129 ALA   A HB2  1 
ATOM   2890 H HB3  A ALA   A 1 129 ? 15.413 -3.326  -1.524  0.56 14.38 ?  129 ALA   A HB3  1 
ATOM   2891 H HB3  B ALA   A 1 129 ? 15.163 -3.444  -2.273  0.44 15.48 ?  129 ALA   A HB3  1 
ATOM   2892 N N    A GLY   A 1 130 ? 14.485 -0.934  -3.462  0.56 10.88 ?  130 GLY   A N    1 
ATOM   2893 N N    B GLY   A 1 130 ? 14.599 -0.907  -4.208  0.44 14.75 ?  130 GLY   A N    1 
ATOM   2894 C CA   A GLY   A 1 130 ? 14.354 0.512   -3.415  0.56 11.28 ?  130 GLY   A CA   1 
ATOM   2895 C CA   B GLY   A 1 130 ? 14.521 0.544   -4.204  0.44 15.53 ?  130 GLY   A CA   1 
ATOM   2896 C C    A GLY   A 1 130 ? 14.968 1.146   -4.647  0.56 10.51 ?  130 GLY   A C    1 
ATOM   2897 C C    B GLY   A 1 130 ? 15.205 1.146   -5.412  0.44 15.79 ?  130 GLY   A C    1 
ATOM   2898 O O    A GLY   A 1 130 ? 14.749 0.698   -5.775  0.56 10.86 ?  130 GLY   A O    1 
ATOM   2899 O O    B GLY   A 1 130 ? 15.014 0.701   -6.551  0.44 15.70 ?  130 GLY   A O    1 
ATOM   2900 H H    A GLY   A 1 130 ? 13.735 -1.373  -3.455  0.56 13.08 ?  130 GLY   A H    1 
ATOM   2901 H H    B GLY   A 1 130 ? 13.842 -1.309  -4.237  0.44 17.72 ?  130 GLY   A H    1 
ATOM   2902 H HA2  A GLY   A 1 130 ? 13.412 0.749   -3.363  0.56 13.56 ?  130 GLY   A HA2  1 
ATOM   2903 H HA2  B GLY   A 1 130 ? 13.595 0.818   -4.213  0.44 18.66 ?  130 GLY   A HA2  1 
ATOM   2904 H HA3  A GLY   A 1 130 ? 14.804 0.850   -2.630  0.56 13.56 ?  130 GLY   A HA3  1 
ATOM   2905 H HA3  B GLY   A 1 130 ? 14.947 0.896   -3.413  0.44 18.66 ?  130 GLY   A HA3  1 
ATOM   2906 N N    A ILE   A 1 131 ? 15.742 2.216   -4.430  0.56 11.26 ?  131 ILE   A N    1 
ATOM   2907 N N    B ILE   A 1 131 ? 16.018 2.177   -5.160  0.44 16.53 ?  131 ILE   A N    1 
ATOM   2908 C CA   A ILE   A 1 131 ? 16.298 2.990   -5.538  0.56 11.70 ?  131 ILE   A CA   1 
ATOM   2909 C CA   B ILE   A 1 131 ? 16.661 2.919   -6.241  0.44 16.95 ?  131 ILE   A CA   1 
ATOM   2910 C C    A ILE   A 1 131 ? 17.360 2.235   -6.328  0.56 10.80 ?  131 ILE   A C    1 
ATOM   2911 C C    B ILE   A 1 131 ? 17.697 2.107   -6.997  0.44 16.74 ?  131 ILE   A C    1 
ATOM   2912 O O    A ILE   A 1 131 ? 17.806 2.735   -7.367  0.56 11.24 ?  131 ILE   A O    1 
ATOM   2913 O O    B ILE   A 1 131 ? 18.158 2.561   -8.050  0.44 17.41 ?  131 ILE   A O    1 
ATOM   2914 C CB   A ILE   A 1 131 ? 16.820 4.371   -5.079  0.56 13.44 ?  131 ILE   A CB   1 
ATOM   2915 C CB   B ILE   A 1 131 ? 17.239 4.276   -5.780  0.44 18.06 ?  131 ILE   A CB   1 
ATOM   2916 C CG1  A ILE   A 1 131 ? 18.045 4.231   -4.168  0.56 15.25 ?  131 ILE   A CG1  1 
ATOM   2917 C CG1  B ILE   A 1 131 ? 18.418 4.092   -4.821  0.44 18.91 ?  131 ILE   A CG1  1 
ATOM   2918 C CG2  A ILE   A 1 131 ? 15.708 5.157   -4.389  0.56 14.52 ?  131 ILE   A CG2  1 
ATOM   2919 C CG2  B ILE   A 1 131 ? 16.150 5.114   -5.131  0.44 18.46 ?  131 ILE   A CG2  1 
ATOM   2920 C CD1  A ILE   A 1 131 ? 18.668 5.565   -3.771  0.56 16.73 ?  131 ILE   A CD1  1 
ATOM   2921 C CD1  B ILE   A 1 131 ? 19.061 5.407   -4.415  0.44 19.42 ?  131 ILE   A CD1  1 
ATOM   2922 H H    A ILE   A 1 131 ? 15.931 2.522   -3.649  0.56 13.54 ?  131 ILE   A H    1 
ATOM   2923 H H    B ILE   A 1 131 ? 16.208 2.466   -4.375  0.44 19.86 ?  131 ILE   A H    1 
ATOM   2924 H HA   A ILE   A 1 131 ? 15.567 3.169   -6.156  0.56 14.07 ?  131 ILE   A HA   1 
ATOM   2925 H HA   B ILE   A 1 131 ? 15.984 3.120   -6.892  0.44 20.36 ?  131 ILE   A HA   1 
ATOM   2926 H HB   A ILE   A 1 131 ? 17.079 4.865   -5.870  0.56 16.15 ?  131 ILE   A HB   1 
ATOM   2927 H HB   B ILE   A 1 131 ? 17.558 4.749   -6.565  0.44 21.69 ?  131 ILE   A HB   1 
ATOM   2928 H HG12 A ILE   A 1 131 ? 17.777 3.767   -3.359  0.56 18.33 ?  131 ILE   A HG12 1 
ATOM   2929 H HG12 B ILE   A 1 131 ? 18.102 3.653   -4.017  0.44 22.72 ?  131 ILE   A HG12 1 
ATOM   2930 H HG13 A ILE   A 1 131 ? 18.720 3.714   -4.635  0.56 18.33 ?  131 ILE   A HG13 1 
ATOM   2931 H HG13 B ILE   A 1 131 ? 19.098 3.552   -5.251  0.44 22.72 ?  131 ILE   A HG13 1 
ATOM   2932 H HG21 A ILE   A 1 131 ? 16.002 6.070   -4.255  0.56 17.45 ?  131 ILE   A HG21 1 
ATOM   2933 H HG21 B ILE   A 1 131 ? 16.479 6.014   -4.999  0.44 22.18 ?  131 ILE   A HG21 1 
ATOM   2934 H HG22 A ILE   A 1 131 ? 14.915 5.143   -4.948  0.56 17.45 ?  131 ILE   A HG22 1 
ATOM   2935 H HG22 B ILE   A 1 131 ? 15.376 5.129   -5.716  0.44 22.18 ?  131 ILE   A HG22 1 
ATOM   2936 H HG23 A ILE   A 1 131 ? 15.513 4.742   -3.533  0.56 17.45 ?  131 ILE   A HG23 1 
ATOM   2937 H HG23 B ILE   A 1 131 ? 15.913 4.715   -4.281  0.44 22.18 ?  131 ILE   A HG23 1 
ATOM   2938 H HD11 A ILE   A 1 131 ? 19.496 5.392   -3.299  0.56 20.09 ?  131 ILE   A HD11 1 
ATOM   2939 H HD11 B ILE   A 1 131 ? 19.888 5.222   -3.948  0.44 23.32 ?  131 ILE   A HD11 1 
ATOM   2940 H HD12 A ILE   A 1 131 ? 18.842 6.080   -4.573  0.56 20.09 ?  131 ILE   A HD12 1 
ATOM   2941 H HD12 B ILE   A 1 131 ? 19.238 5.930   -5.213  0.44 23.32 ?  131 ILE   A HD12 1 
ATOM   2942 H HD13 A ILE   A 1 131 ? 18.050 6.041   -3.197  0.56 20.09 ?  131 ILE   A HD13 1 
ATOM   2943 H HD13 B ILE   A 1 131 ? 18.452 5.891   -3.834  0.44 23.32 ?  131 ILE   A HD13 1 
ATOM   2944 N N    A PHE   A 1 132 ? 17.782 1.047   -5.875  0.56 10.41 ?  132 PHE   A N    1 
ATOM   2945 N N    B PHE   A 1 132 ? 18.074 0.924   -6.500  0.44 16.02 ?  132 PHE   A N    1 
ATOM   2946 C CA   A PHE   A 1 132 ? 18.670 0.222   -6.686  0.56 11.39 ?  132 PHE   A CA   1 
ATOM   2947 C CA   B PHE   A 1 132 ? 18.968 0.054   -7.256  0.44 15.42 ?  132 PHE   A CA   1 
ATOM   2948 C C    A PHE   A 1 132 ? 17.922 -0.531  -7.789  0.56 11.84 ?  132 PHE   A C    1 
ATOM   2949 C C    B PHE   A 1 132 ? 18.241 -0.705  -8.366  0.44 15.61 ?  132 PHE   A C    1 
ATOM   2950 O O    A PHE   A 1 132 ? 18.560 -1.165  -8.636  0.56 13.24 ?  132 PHE   A O    1 
ATOM   2951 O O    B PHE   A 1 132 ? 18.898 -1.325  -9.210  0.44 16.27 ?  132 PHE   A O    1 
ATOM   2952 C CB   A PHE   A 1 132 ? 19.465 -0.755  -5.808  0.56 11.17 ?  132 PHE   A CB   1 
ATOM   2953 C CB   B PHE   A 1 132 ? 19.714 -0.915  -6.323  0.44 14.05 ?  132 PHE   A CB   1 
ATOM   2954 C CG   A PHE   A 1 132 ? 20.704 -0.166  -5.154  0.56 11.59 ?  132 PHE   A CG   1 
ATOM   2955 C CG   B PHE   A 1 132 ? 20.871 -0.294  -5.569  0.44 14.45 ?  132 PHE   A CG   1 
ATOM   2956 C CD1  A PHE   A 1 132 ? 20.611 0.884   -4.252  0.56 12.20 ?  132 PHE   A CD1  1 
ATOM   2957 C CD1  B PHE   A 1 132 ? 20.668 0.730   -4.657  0.44 15.10 ?  132 PHE   A CD1  1 
ATOM   2958 C CD2  A PHE   A 1 132 ? 21.955 -0.719  -5.398  0.56 12.46 ?  132 PHE   A CD2  1 
ATOM   2959 C CD2  B PHE   A 1 132 ? 22.161 -0.776  -5.743  0.44 14.92 ?  132 PHE   A CD2  1 
ATOM   2960 C CE1  A PHE   A 1 132 ? 21.748 1.397   -3.644  0.56 13.59 ?  132 PHE   A CE1  1 
ATOM   2961 C CE1  B PHE   A 1 132 ? 21.737 1.282   -3.958  0.44 15.70 ?  132 PHE   A CE1  1 
ATOM   2962 C CE2  A PHE   A 1 132 ? 23.091 -0.215  -4.789  0.56 13.02 ?  132 PHE   A CE2  1 
ATOM   2963 C CE2  B PHE   A 1 132 ? 23.228 -0.236  -5.046  0.44 15.57 ?  132 PHE   A CE2  1 
ATOM   2964 C CZ   A PHE   A 1 132 ? 22.984 0.845   -3.909  0.56 13.21 ?  132 PHE   A CZ   1 
ATOM   2965 C CZ   B PHE   A 1 132 ? 23.014 0.795   -4.151  0.44 15.69 ?  132 PHE   A CZ   1 
ATOM   2966 H H    A PHE   A 1 132 ? 17.566 0.708   -5.109  0.56 12.52 ?  132 PHE   A H    1 
ATOM   2967 H H    B PHE   A 1 132 ? 17.830 0.604   -5.734  0.44 19.25 ?  132 PHE   A H    1 
ATOM   2968 H HA   A PHE   A 1 132 ? 19.307 0.813   -7.114  0.56 13.69 ?  132 PHE   A HA   1 
ATOM   2969 H HA   B PHE   A 1 132 ? 19.643 0.606   -7.676  0.44 18.53 ?  132 PHE   A HA   1 
ATOM   2970 H HB2  A PHE   A 1 132 ? 18.881 -1.070  -5.098  0.56 13.43 ?  132 PHE   A HB2  1 
ATOM   2971 H HB2  B PHE   A 1 132 ? 19.097 -1.256  -5.660  0.44 16.89 ?  132 PHE   A HB2  1 
ATOM   2972 H HB3  A PHE   A 1 132 ? 19.743 -1.498  -6.359  0.56 13.43 ?  132 PHE   A HB3  1 
ATOM   2973 H HB3  B PHE   A 1 132 ? 20.075 -1.648  -6.846  0.44 16.89 ?  132 PHE   A HB3  1 
ATOM   2974 H HD1  A PHE   A 1 132 ? 19.780 1.262   -4.071  0.56 14.67 ?  132 PHE   A HD1  1 
ATOM   2975 H HD1  B PHE   A 1 132 ? 19.814 1.065   -4.518  0.44 18.15 ?  132 PHE   A HD1  1 
ATOM   2976 H HD2  A PHE   A 1 132 ? 22.030 -1.432  -5.994  0.56 14.97 ?  132 PHE   A HD2  1 
ATOM   2977 H HD2  B PHE   A 1 132 ? 22.316 -1.469  -6.340  0.44 17.93 ?  132 PHE   A HD2  1 
ATOM   2978 H HE1  A PHE   A 1 132 ? 21.674 2.113   -3.051  0.56 16.33 ?  132 PHE   A HE1  1 
ATOM   2979 H HE1  B PHE   A 1 132 ? 21.591 1.977   -3.351  0.44 18.87 ?  132 PHE   A HE1  1 
ATOM   2980 H HE2  A PHE   A 1 132 ? 23.923 -0.587  -4.978  0.56 15.64 ?  132 PHE   A HE2  1 
ATOM   2981 H HE2  B PHE   A 1 132 ? 24.089 -0.564  -5.180  0.44 18.70 ?  132 PHE   A HE2  1 
ATOM   2982 H HZ   A PHE   A 1 132 ? 23.746 1.194   -3.503  0.56 15.88 ?  132 PHE   A HZ   1 
ATOM   2983 H HZ   B PHE   A 1 132 ? 23.730 1.165   -3.682  0.44 18.85 ?  132 PHE   A HZ   1 
ATOM   2984 N N    A GLY   A 1 133 ? 16.590 -0.493  -7.796  0.56 11.50 ?  133 GLY   A N    1 
ATOM   2985 N N    B GLY   A 1 133 ? 16.907 -0.680  -8.383  0.44 15.32 ?  133 GLY   A N    1 
ATOM   2986 C CA   A GLY   A 1 133 ? 15.820 -0.875  -8.965  0.56 12.70 ?  133 GLY   A CA   1 
ATOM   2987 C CA   B GLY   A 1 133 ? 16.139 -1.053  -9.547  0.44 15.22 ?  133 GLY   A CA   1 
ATOM   2988 C C    A GLY   A 1 133 ? 15.563 -2.350  -9.182  0.56 14.07 ?  133 GLY   A C    1 
ATOM   2989 C C    B GLY   A 1 133 ? 15.567 -2.458  -9.541  0.44 15.27 ?  133 GLY   A C    1 
ATOM   2990 O O    A GLY   A 1 133 ? 15.059 -2.705  -10.253 0.56 15.30 ?  133 GLY   A O    1 
ATOM   2991 O O    B GLY   A 1 133 ? 14.610 -2.714  -10.283 0.44 15.73 ?  133 GLY   A O    1 
ATOM   2992 H H    A GLY   A 1 133 ? 16.106 -0.242  -7.130  0.56 13.83 ?  133 GLY   A H    1 
ATOM   2993 H H    B GLY   A 1 133 ? 16.429 -0.442  -7.711  0.44 18.41 ?  133 GLY   A H    1 
ATOM   2994 H HA2  A GLY   A 1 133 ? 14.951 -0.443  -8.920  0.56 15.27 ?  133 GLY   A HA2  1 
ATOM   2995 H HA2  B GLY   A 1 133 ? 15.399 -0.437  -9.633  0.44 18.29 ?  133 GLY   A HA2  1 
ATOM   2996 H HA3  A GLY   A 1 133 ? 16.268 -0.545  -9.759  0.56 15.27 ?  133 GLY   A HA3  1 
ATOM   2997 H HA3  B GLY   A 1 133 ? 16.704 -0.952  -10.331 0.44 18.29 ?  133 GLY   A HA3  1 
ATOM   2998 N N    A ALA   A 1 134 ? 15.882 -3.223  -8.227  0.56 13.45 ?  134 ALA   A N    1 
ATOM   2999 N N    B ALA   A 1 134 ? 16.103 -3.366  -8.728  0.44 14.48 ?  134 ALA   A N    1 
ATOM   3000 C CA   A ALA   A 1 134 ? 15.561 -4.636  -8.383  0.56 13.77 ?  134 ALA   A CA   1 
ATOM   3001 C CA   B ALA   A 1 134 ? 15.718 -4.768  -8.837  0.44 14.73 ?  134 ALA   A CA   1 
ATOM   3002 C C    A ALA   A 1 134 ? 14.212 -4.967  -7.743  0.56 14.69 ?  134 ALA   A C    1 
ATOM   3003 C C    B ALA   A 1 134 ? 14.357 -5.018  -8.183  0.44 14.73 ?  134 ALA   A C    1 
ATOM   3004 O O    A ALA   A 1 134 ? 13.675 -4.211  -6.930  0.56 15.64 ?  134 ALA   A O    1 
ATOM   3005 O O    B ALA   A 1 134 ? 13.829 -4.191  -7.436  0.44 15.02 ?  134 ALA   A O    1 
ATOM   3006 C CB   A ALA   A 1 134 ? 16.649 -5.526  -7.782  0.56 14.36 ?  134 ALA   A CB   1 
ATOM   3007 C CB   B ALA   A 1 134 ? 16.791 -5.672  -8.228  0.44 15.54 ?  134 ALA   A CB   1 
ATOM   3008 H H    A ALA   A 1 134 ? 16.276 -3.021  -7.485  0.56 16.17 ?  134 ALA   A H    1 
ATOM   3009 H H    B ALA   A 1 134 ? 16.682 -3.196  -8.110  0.44 17.40 ?  134 ALA   A H    1 
ATOM   3010 H HA   A ALA   A 1 134 ? 15.500 -4.837  -9.327  0.56 16.54 ?  134 ALA   A HA   1 
ATOM   3011 H HA   B ALA   A 1 134 ? 15.637 -4.996  -9.775  0.44 17.69 ?  134 ALA   A HA   1 
ATOM   3012 H HB1  A ALA   A 1 134 ? 16.418 -6.453  -7.948  0.56 17.25 ?  134 ALA   A HB1  1 
ATOM   3013 H HB1  B ALA   A 1 134 ? 16.517 -6.598  -8.328  0.44 18.67 ?  134 ALA   A HB1  1 
ATOM   3014 H HB2  A ALA   A 1 134 ? 17.494 -5.314  -8.211  0.56 17.25 ?  134 ALA   A HB2  1 
ATOM   3015 H HB2  B ALA   A 1 134 ? 17.631 -5.525  -8.693  0.44 18.67 ?  134 ALA   A HB2  1 
ATOM   3016 H HB3  A ALA   A 1 134 ? 16.706 -5.360  -6.832  0.56 17.25 ?  134 ALA   A HB3  1 
ATOM   3017 H HB3  B ALA   A 1 134 ? 16.893 -5.457  -7.288  0.44 18.67 ?  134 ALA   A HB3  1 
ATOM   3018 N N    A ASP   A 1 135 ? 13.676 -6.125  -8.120  0.56 15.16 ?  135 ASP   A N    1 
ATOM   3019 N N    B ASP   A 1 135 ? 13.786 -6.187  -8.477  0.44 15.44 ?  135 ASP   A N    1 
ATOM   3020 C CA   A ASP   A 1 135 ? 12.427 -6.647  -7.573  0.56 15.98 ?  135 ASP   A CA   1 
ATOM   3021 C CA   B ASP   A 1 135 ? 12.502 -6.565  -7.895  0.44 16.29 ?  135 ASP   A CA   1 
ATOM   3022 C C    A ASP   A 1 135 ? 12.647 -7.044  -6.118  0.56 15.34 ?  135 ASP   A C    1 
ATOM   3023 C C    B ASP   A 1 135 ? 12.717 -7.076  -6.476  0.44 15.72 ?  135 ASP   A C    1 
ATOM   3024 O O    A ASP   A 1 135 ? 13.440 -7.958  -5.858  0.56 14.57 ?  135 ASP   A O    1 
ATOM   3025 O O    B ASP   A 1 135 ? 13.465 -8.041  -6.286  0.44 15.49 ?  135 ASP   A O    1 
ATOM   3026 C CB   A ASP   A 1 135 ? 12.033 -7.872  -8.404  0.56 18.10 ?  135 ASP   A CB   1 
ATOM   3027 C CB   B ASP   A 1 135 ? 11.830 -7.646  -8.731  0.44 18.22 ?  135 ASP   A CB   1 
ATOM   3028 C CG   A ASP   A 1 135 ? 10.766 -8.561  -7.906  0.56 19.98 ?  135 ASP   A CG   1 
ATOM   3029 C CG   B ASP   A 1 135 ? 10.431 -8.001  -8.230  0.44 20.11 ?  135 ASP   A CG   1 
ATOM   3030 O OD1  A ASP   A 1 135 ? 10.137 -8.084  -6.939  0.56 19.96 ?  135 ASP   A OD1  1 
ATOM   3031 O OD1  B ASP   A 1 135 ? 10.033 -7.512  -7.151  0.44 21.02 ?  135 ASP   A OD1  1 
ATOM   3032 O OD2  A ASP   A 1 135 ? 10.404 -9.599  -8.498  0.56 22.28 -1 135 ASP   A OD2  1 
ATOM   3033 O OD2  B ASP   A 1 135 ? 9.725  -8.770  -8.920  0.44 21.27 -1 135 ASP   A OD2  1 
ATOM   3034 H H    A ASP   A 1 135 ? 14.030 -6.648  -8.711  0.56 18.22 ?  135 ASP   A H    1 
ATOM   3035 H H    B ASP   A 1 135 ? 14.121 -6.773  -9.010  0.44 18.55 ?  135 ASP   A H    1 
ATOM   3036 H HA   A ASP   A 1 135 ? 11.726 -5.975  -7.639  0.56 19.20 ?  135 ASP   A HA   1 
ATOM   3037 H HA   B ASP   A 1 135 ? 11.931 -5.789  -7.878  0.44 19.57 ?  135 ASP   A HA   1 
ATOM   3038 H HB2  A ASP   A 1 135 ? 11.886 -7.596  -9.321  0.56 21.75 ?  135 ASP   A HB2  1 
ATOM   3039 H HB2  B ASP   A 1 135 ? 11.765 -7.333  -9.645  0.44 21.89 ?  135 ASP   A HB2  1 
ATOM   3040 H HB3  A ASP   A 1 135 ? 12.751 -8.521  -8.363  0.56 21.75 ?  135 ASP   A HB3  1 
ATOM   3041 H HB3  B ASP   A 1 135 ? 12.362 -8.453  -8.690  0.44 21.89 ?  135 ASP   A HB3  1 
ATOM   3042 N N    A PRO   A 1 136 ? 12.010 -6.388  -5.145  0.56 15.55 ?  136 PRO   A N    1 
ATOM   3043 N N    B PRO   A 1 136 ? 12.104 -6.463  -5.463  0.44 15.51 ?  136 PRO   A N    1 
ATOM   3044 C CA   A PRO   A 1 136 ? 12.260 -6.755  -3.740  0.56 15.42 ?  136 PRO   A CA   1 
ATOM   3045 C CA   B PRO   A 1 136 ? 12.321 -6.929  -4.082  0.44 15.28 ?  136 PRO   A CA   1 
ATOM   3046 C C    A PRO   A 1 136 ? 11.846 -8.174  -3.394  0.56 13.94 ?  136 PRO   A C    1 
ATOM   3047 C C    B PRO   A 1 136 ? 11.883 -8.358  -3.825  0.44 14.54 ?  136 PRO   A C    1 
ATOM   3048 O O    A PRO   A 1 136 ? 12.434 -8.766  -2.483  0.56 12.57 ?  136 PRO   A O    1 
ATOM   3049 O O    B PRO   A 1 136 ? 12.496 -9.025  -2.986  0.44 13.82 ?  136 PRO   A O    1 
ATOM   3050 C CB   A PRO   A 1 136 ? 11.454 -5.711  -2.955  0.56 16.49 ?  136 PRO   A CB   1 
ATOM   3051 C CB   B PRO   A 1 136 ? 11.523 -5.922  -3.241  0.44 15.94 ?  136 PRO   A CB   1 
ATOM   3052 C CG   A PRO   A 1 136 ? 10.381 -5.285  -3.900  0.56 17.52 ?  136 PRO   A CG   1 
ATOM   3053 C CG   B PRO   A 1 136 ? 10.571 -5.285  -4.208  0.44 16.68 ?  136 PRO   A CG   1 
ATOM   3054 C CD   A PRO   A 1 136 ? 11.006 -5.317  -5.267  0.56 16.44 ?  136 PRO   A CD   1 
ATOM   3055 C CD   B PRO   A 1 136 ? 11.289 -5.240  -5.506  0.44 16.01 ?  136 PRO   A CD   1 
ATOM   3056 H HA   A PRO   A 1 136 ? 13.203 -6.641  -3.526  0.56 18.52 ?  136 PRO   A HA   1 
ATOM   3057 H HA   B PRO   A 1 136 ? 13.261 -6.855  -3.845  0.44 18.36 ?  136 PRO   A HA   1 
ATOM   3058 H HB2  A PRO   A 1 136 ? 11.073 -6.115  -2.161  0.56 19.81 ?  136 PRO   A HB2  1 
ATOM   3059 H HB2  B PRO   A 1 136 ? 11.042 -6.389  -2.538  0.44 19.16 ?  136 PRO   A HB2  1 
ATOM   3060 H HB3  A PRO   A 1 136 ? 12.025 -4.959  -2.719  0.56 19.81 ?  136 PRO   A HB3  1 
ATOM   3061 H HB3  B PRO   A 1 136 ? 12.127 -5.263  -2.863  0.44 19.16 ?  136 PRO   A HB3  1 
ATOM   3062 H HG2  A PRO   A 1 136 ? 9.642  -5.905  -3.851  0.56 21.05 ?  136 PRO   A HG2  1 
ATOM   3063 H HG2  B PRO   A 1 136 ? 9.770  -5.827  -4.284  0.44 20.03 ?  136 PRO   A HG2  1 
ATOM   3064 H HG3  A PRO   A 1 136 ? 10.094 -4.385  -3.682  0.56 21.05 ?  136 PRO   A HG3  1 
ATOM   3065 H HG3  B PRO   A 1 136 ? 10.354 -4.389  -3.913  0.44 20.03 ?  136 PRO   A HG3  1 
ATOM   3066 H HD2  A PRO   A 1 136 ? 10.344 -5.556  -5.936  0.56 19.75 ?  136 PRO   A HD2  1 
ATOM   3067 H HD2  B PRO   A 1 136 ? 10.664 -5.283  -6.243  0.44 19.23 ?  136 PRO   A HD2  1 
ATOM   3068 H HD3  A PRO   A 1 136 ? 11.431 -4.469  -5.472  0.56 19.75 ?  136 PRO   A HD3  1 
ATOM   3069 H HD3  B PRO   A 1 136 ? 11.862 -4.457  -5.561  0.44 19.23 ?  136 PRO   A HD3  1 
ATOM   3070 N N    A ILE   A 1 137 ? 10.838 -8.726  -4.075  0.56 14.42 ?  137 ILE   A N    1 
ATOM   3071 N N    B ILE   A 1 137 ? 10.829 -8.845  -4.486  0.44 14.73 ?  137 ILE   A N    1 
ATOM   3072 C CA   A ILE   A 1 137 ? 10.462 -10.121 -3.850  0.56 14.73 ?  137 ILE   A CA   1 
ATOM   3073 C CA   B ILE   A 1 137 ? 10.457 -10.251 -4.337  0.44 14.88 ?  137 ILE   A CA   1 
ATOM   3074 C C    A ILE   A 1 137 ? 11.608 -11.043 -4.253  0.56 13.93 ?  137 ILE   A C    1 
ATOM   3075 C C    B ILE   A 1 137 ? 11.644 -11.139 -4.683  0.44 14.92 ?  137 ILE   A C    1 
ATOM   3076 O O    A ILE   A 1 137 ? 11.951 -11.991 -3.532  0.56 13.62 ?  137 ILE   A O    1 
ATOM   3077 O O    B ILE   A 1 137 ? 11.914 -12.141 -4.010  0.44 15.06 ?  137 ILE   A O    1 
ATOM   3078 C CB   A ILE   A 1 137 ? 9.161  -10.449 -4.609  0.56 15.62 ?  137 ILE   A CB   1 
ATOM   3079 C CB   B ILE   A 1 137 ? 9.217  -10.576 -5.192  0.44 15.27 ?  137 ILE   A CB   1 
ATOM   3080 C CG1  A ILE   A 1 137 ? 8.001  -9.572  -4.115  0.56 16.60 ?  137 ILE   A CG1  1 
ATOM   3081 C CG1  B ILE   A 1 137 ? 8.031  -9.708  -4.755  0.44 16.48 ?  137 ILE   A CG1  1 
ATOM   3082 C CG2  A ILE   A 1 137 ? 8.825  -11.931 -4.473  0.56 16.03 ?  137 ILE   A CG2  1 
ATOM   3083 C CG2  B ILE   A 1 137 ? 8.867  -12.060 -5.087  0.44 15.10 ?  137 ILE   A CG2  1 
ATOM   3084 C CD1  A ILE   A 1 137 ? 6.708  -9.774  -4.886  0.56 17.73 ?  137 ILE   A CD1  1 
ATOM   3085 C CD1  B ILE   A 1 137 ? 6.754  -9.941  -5.540  0.44 17.28 ?  137 ILE   A CD1  1 
ATOM   3086 H H    A ILE   A 1 137 ? 10.370 -8.314  -4.668  0.56 17.33 ?  137 ILE   A H    1 
ATOM   3087 H H    B ILE   A 1 137 ? 10.325 -8.395  -5.013  0.44 17.70 ?  137 ILE   A H    1 
ATOM   3088 H HA   A ILE   A 1 137 ? 10.295 -10.248 -2.907  0.56 17.70 ?  137 ILE   A HA   1 
ATOM   3089 H HA   B ILE   A 1 137 ? 10.227 -10.424 -3.412  0.44 17.88 ?  137 ILE   A HA   1 
ATOM   3090 H HB   A ILE   A 1 137 ? 9.300  -10.252 -5.548  0.56 18.77 ?  137 ILE   A HB   1 
ATOM   3091 H HB   B ILE   A 1 137 ? 9.415  -10.376 -6.118  0.44 18.35 ?  137 ILE   A HB   1 
ATOM   3092 H HG12 A ILE   A 1 137 ? 7.829  -9.771  -3.184  0.56 19.94 ?  137 ILE   A HG12 1 
ATOM   3093 H HG12 B ILE   A 1 137 ? 7.844  -9.884  -3.819  0.44 19.79 ?  137 ILE   A HG12 1 
ATOM   3094 H HG13 A ILE   A 1 137 ? 8.253  -8.635  -4.208  0.56 19.94 ?  137 ILE   A HG13 1 
ATOM   3095 H HG13 B ILE   A 1 137 ? 8.276  -8.772  -4.864  0.44 19.79 ?  137 ILE   A HG13 1 
ATOM   3096 H HG21 A ILE   A 1 137 ? 7.937  -12.103 -4.823  0.56 19.26 ?  137 ILE   A HG21 1 
ATOM   3097 H HG21 B ILE   A 1 137 ? 8.230  -12.286 -5.781  0.44 18.14 ?  137 ILE   A HG21 1 
ATOM   3098 H HG22 A ILE   A 1 137 ? 9.473  -12.444 -4.975  0.56 19.26 ?  137 ILE   A HG22 1 
ATOM   3099 H HG22 B ILE   A 1 137 ? 9.662  -12.596 -5.202  0.44 18.14 ?  137 ILE   A HG22 1 
ATOM   3100 H HG23 A ILE   A 1 137 ? 8.860  -12.172 -3.537  0.56 19.26 ?  137 ILE   A HG23 1 
ATOM   3101 H HG23 B ILE   A 1 137 ? 8.479  -12.227 -4.214  0.44 18.14 ?  137 ILE   A HG23 1 
ATOM   3102 H HD11 A ILE   A 1 137 ? 6.002  -10.011 -4.265  0.56 21.30 ?  137 ILE   A HD11 1 
ATOM   3103 H HD11 B ILE   A 1 137 ? 6.005  -9.724  -4.968  0.44 20.76 ?  137 ILE   A HD11 1 
ATOM   3104 H HD12 A ILE   A 1 137 ? 6.493  -8.950  -5.342  0.56 21.30 ?  137 ILE   A HD12 1 
ATOM   3105 H HD12 B ILE   A 1 137 ? 6.759  -9.367  -6.318  0.44 20.76 ?  137 ILE   A HD12 1 
ATOM   3106 H HD13 A ILE   A 1 137 ? 6.825  -10.481 -5.541  0.56 21.30 ?  137 ILE   A HD13 1 
ATOM   3107 H HD13 B ILE   A 1 137 ? 6.694  -10.867 -5.810  0.44 20.76 ?  137 ILE   A HD13 1 
ATOM   3108 N N    A HIS   A 1 138 ? 12.222 -10.771 -5.408  0.56 14.54 ?  138 HIS   A N    1 
ATOM   3109 N N    B HIS   A 1 138 ? 12.371 -10.782 -5.740  0.44 14.96 ?  138 HIS   A N    1 
ATOM   3110 C CA   A HIS   A 1 138 ? 13.377 -11.547 -5.844  0.56 14.70 ?  138 HIS   A CA   1 
ATOM   3111 C CA   B HIS   A 1 138 ? 13.580 -11.517 -6.089  0.44 15.43 ?  138 HIS   A CA   1 
ATOM   3112 C C    A HIS   A 1 138 ? 14.535 -11.398 -4.867  0.56 14.53 ?  138 HIS   A C    1 
ATOM   3113 C C    B HIS   A 1 138 ? 14.660 -11.369 -5.018  0.44 15.04 ?  138 HIS   A C    1 
ATOM   3114 O O    A HIS   A 1 138 ? 15.169 -12.388 -4.477  0.56 15.21 ?  138 HIS   A O    1 
ATOM   3115 O O    B HIS   A 1 138 ? 15.350 -12.344 -4.692  0.44 15.22 ?  138 HIS   A O    1 
ATOM   3116 C CB   A HIS   A 1 138 ? 13.788 -11.114 -7.251  0.56 15.45 ?  138 HIS   A CB   1 
ATOM   3117 C CB   B HIS   A 1 138 ? 14.088 -11.052 -7.450  0.44 16.65 ?  138 HIS   A CB   1 
ATOM   3118 C CG   A HIS   A 1 138 ? 15.082 -11.712 -7.712  0.56 16.58 ?  138 HIS   A CG   1 
ATOM   3119 C CG   B HIS   A 1 138 ? 15.325 -11.762 -7.898  0.44 17.52 ?  138 HIS   A CG   1 
ATOM   3120 N ND1  A HIS   A 1 138 ? 15.227 -13.057 -7.980  0.56 18.03 ?  138 HIS   A ND1  1 
ATOM   3121 N ND1  B HIS   A 1 138 ? 15.386 -13.131 -8.043  0.44 18.63 ?  138 HIS   A ND1  1 
ATOM   3122 C CD2  A HIS   A 1 138 ? 16.293 -11.150 -7.939  0.56 17.05 ?  138 HIS   A CD2  1 
ATOM   3123 C CD2  B HIS   A 1 138 ? 16.554 -11.294 -8.216  0.44 18.11 ?  138 HIS   A CD2  1 
ATOM   3124 C CE1  A HIS   A 1 138 ? 16.469 -13.295 -8.363  0.56 18.50 ?  138 HIS   A CE1  1 
ATOM   3125 C CE1  B HIS   A 1 138 ? 16.597 -13.474 -8.443  0.44 19.26 ?  138 HIS   A CE1  1 
ATOM   3126 N NE2  A HIS   A 1 138 ? 17.138 -12.156 -8.342  0.56 18.10 ?  138 HIS   A NE2  1 
ATOM   3127 N NE2  B HIS   A 1 138 ? 17.326 -12.379 -8.552  0.44 18.98 ?  138 HIS   A NE2  1 
ATOM   3128 H H    A HIS   A 1 138 ? 11.988 -10.141 -5.952  0.56 17.48 ?  138 HIS   A H    1 
ATOM   3129 H H    B HIS   A 1 138 ? 12.173 -10.137 -6.275  0.44 17.97 ?  138 HIS   A H    1 
ATOM   3130 H HA   A HIS   A 1 138 ? 13.134 -12.480 -5.879  0.56 17.66 ?  138 HIS   A HA   1 
ATOM   3131 H HA   B HIS   A 1 138 ? 13.360 -12.457 -6.165  0.44 18.53 ?  138 HIS   A HA   1 
ATOM   3132 H HB2  A HIS   A 1 138 ? 13.097 -11.385 -7.879  0.56 18.56 ?  138 HIS   A HB2  1 
ATOM   3133 H HB2  B HIS   A 1 138 ? 13.397 -11.209 -8.116  0.44 20.00 ?  138 HIS   A HB2  1 
ATOM   3134 H HB3  A HIS   A 1 138 ? 13.887 -10.149 -7.271  0.56 18.56 ?  138 HIS   A HB3  1 
ATOM   3135 H HB3  B HIS   A 1 138 ? 14.288 -10.104 -7.406  0.44 20.00 ?  138 HIS   A HB3  1 
ATOM   3136 H HD1  A HIS   A 1 138 ? 14.604 -13.648 -7.916  0.56 21.66 ?  138 HIS   A HD1  1 
ATOM   3137 H HD2  A HIS   A 1 138 ? 16.511 -10.252 -7.846  0.56 20.48 ?  138 HIS   A HD2  1 
ATOM   3138 H HD2  B HIS   A 1 138 ? 16.822 -10.403 -8.210  0.44 21.76 ?  138 HIS   A HD2  1 
ATOM   3139 H HE1  A HIS   A 1 138 ? 16.814 -14.127 -8.601  0.56 22.23 ?  138 HIS   A HE1  1 
ATOM   3140 H HE1  B HIS   A 1 138 ? 16.884 -14.340 -8.612  0.44 23.14 ?  138 HIS   A HE1  1 
ATOM   3141 H HE2  B HIS   A 1 138 ? 18.147 -12.350 -8.796  0.44 22.80 ?  138 HIS   A HE2  1 
ATOM   3142 N N    . SER   A 1 139 ? 14.832 -10.162 -4.465  1.00 14.23 ?  139 SER   A N    1 
ATOM   3143 C CA   . SER   A 1 139 ? 15.887 -9.949  -3.483  1.00 14.25 ?  139 SER   A CA   1 
ATOM   3144 C C    . SER   A 1 139 ? 15.663 -10.787 -2.228  1.00 13.71 ?  139 SER   A C    1 
ATOM   3145 O O    . SER   A 1 139 ? 16.609 -11.375 -1.691  1.00 13.84 ?  139 SER   A O    1 
ATOM   3146 C CB   . SER   A 1 139 ? 16.009 -8.466  -3.131  1.00 14.09 ?  139 SER   A CB   1 
ATOM   3147 O OG   . SER   A 1 139 ? 17.091 -8.280  -2.236  1.00 14.66 ?  139 SER   A OG   1 
ATOM   3148 H H    A SER   A 1 139 ? 14.439 -9.443  -4.733  0.56 17.10 ?  139 SER   A H    1 
ATOM   3149 H H    B SER   A 1 139 ? 14.362 -9.461  -4.645  0.44 17.10 ?  139 SER   A H    1 
ATOM   3150 H HA   . SER   A 1 139 ? 16.733 -10.222 -3.869  1.00 17.12 ?  139 SER   A HA   1 
ATOM   3151 H HB2  . SER   A 1 139 ? 16.169 -7.952  -3.935  1.00 16.93 ?  139 SER   A HB2  1 
ATOM   3152 H HB3  . SER   A 1 139 ? 15.189 -8.169  -2.700  1.00 16.93 ?  139 SER   A HB3  1 
ATOM   3153 H HG   . SER   A 1 139 ? 17.169 -7.462  -2.030  1.00 17.62 ?  139 SER   A HG   1 
ATOM   3154 N N    A LEU   A 1 140 ? 14.431 -10.807 -1.713  0.56 13.27 ?  140 LEU   A N    1 
ATOM   3155 N N    B LEU   A 1 140 ? 14.417 -10.878 -1.762  0.44 13.88 ?  140 LEU   A N    1 
ATOM   3156 C CA   A LEU   A 1 140 ? 14.156 -11.583 -0.505  0.56 13.16 ?  140 LEU   A CA   1 
ATOM   3157 C CA   B LEU   A 1 140 ? 14.124 -11.750 -0.629  0.44 13.92 ?  140 LEU   A CA   1 
ATOM   3158 C C    A LEU   A 1 140 ? 14.423 -13.068 -0.731  0.56 12.95 ?  140 LEU   A C    1 
ATOM   3159 C C    B LEU   A 1 140 ? 14.391 -13.211 -0.981  0.44 14.24 ?  140 LEU   A C    1 
ATOM   3160 O O    A LEU   A 1 140 ? 14.941 -13.760 0.158   0.56 13.58 ?  140 LEU   A O    1 
ATOM   3161 O O    B LEU   A 1 140 ? 14.948 -13.963 -0.170  0.44 14.94 ?  140 LEU   A O    1 
ATOM   3162 C CB   A LEU   A 1 140 ? 12.713 -11.358 -0.050  0.56 13.94 ?  140 LEU   A CB   1 
ATOM   3163 C CB   B LEU   A 1 140 ? 12.675 -11.542 -0.188  0.44 13.97 ?  140 LEU   A CB   1 
ATOM   3164 C CG   A LEU   A 1 140 ? 12.248 -12.327 1.042   0.56 14.62 ?  140 LEU   A CG   1 
ATOM   3165 C CG   B LEU   A 1 140 ? 12.188 -12.135 1.139   0.44 13.89 ?  140 LEU   A CG   1 
ATOM   3166 C CD1  A LEU   A 1 140 ? 13.127 -12.201 2.288   0.56 13.50 ?  140 LEU   A CD1  1 
ATOM   3167 C CD1  B LEU   A 1 140 ? 13.063 -11.723 2.314   0.44 13.90 ?  140 LEU   A CD1  1 
ATOM   3168 C CD2  A LEU   A 1 140 ? 10.771 -12.120 1.373   0.56 15.67 ?  140 LEU   A CD2  1 
ATOM   3169 C CD2  B LEU   A 1 140 ? 10.734 -11.724 1.379   0.44 13.60 ?  140 LEU   A CD2  1 
ATOM   3170 H H    A LEU   A 1 140 ? 13.752 -10.385 -2.035  0.56 15.95 ?  140 LEU   A H    1 
ATOM   3171 H H    B LEU   A 1 140 ? 13.740 -10.450 -2.077  0.44 16.67 ?  140 LEU   A H    1 
ATOM   3172 H HA   A LEU   A 1 140 ? 14.734 -11.275 0.208   0.56 15.82 ?  140 LEU   A HA   1 
ATOM   3173 H HA   B LEU   A 1 140 ? 14.701 -11.509 0.110   0.44 16.72 ?  140 LEU   A HA   1 
ATOM   3174 H HB2  A LEU   A 1 140 ? 12.625 -10.455 0.306   0.56 16.75 ?  140 LEU   A HB2  1 
ATOM   3175 H HB2  B LEU   A 1 140 ? 12.521 -10.588 -0.135  0.44 16.78 ?  140 LEU   A HB2  1 
ATOM   3176 H HB3  A LEU   A 1 140 ? 12.117 -11.464 -0.810  0.56 16.75 ?  140 LEU   A HB3  1 
ATOM   3177 H HB3  B LEU   A 1 140 ? 12.105 -11.913 -0.879  0.44 16.78 ?  140 LEU   A HB3  1 
ATOM   3178 H HG   A LEU   A 1 140 ? 12.331 -13.237 0.715   0.56 17.56 ?  140 LEU   A HG   1 
ATOM   3179 H HG   B LEU   A 1 140 ? 12.213 -13.103 1.078   0.44 16.69 ?  140 LEU   A HG   1 
ATOM   3180 H HD11 A LEU   A 1 140 ? 12.752 -12.754 2.993   0.56 16.22 ?  140 LEU   A HD11 1 
ATOM   3181 H HD11 B LEU   A 1 140 ? 12.667 -12.057 3.135   0.44 16.70 ?  140 LEU   A HD11 1 
ATOM   3182 H HD12 A LEU   A 1 140 ? 14.025 -12.503 2.077   0.56 16.22 ?  140 LEU   A HD12 1 
ATOM   3183 H HD12 B LEU   A 1 140 ? 13.948 -12.099 2.197   0.44 16.70 ?  140 LEU   A HD12 1 
ATOM   3184 H HD13 A LEU   A 1 140 ? 13.145 -11.275 2.569   0.56 16.22 ?  140 LEU   A HD13 1 
ATOM   3185 H HD13 B LEU   A 1 140 ? 13.114 -10.754 2.344   0.44 16.70 ?  140 LEU   A HD13 1 
ATOM   3186 H HD21 A LEU   A 1 140 ? 10.514 -12.748 2.067   0.56 18.82 ?  140 LEU   A HD21 1 
ATOM   3187 H HD21 B LEU   A 1 140 ? 10.430 -12.109 2.216   0.44 16.35 ?  140 LEU   A HD21 1 
ATOM   3188 H HD22 A LEU   A 1 140 ? 10.641 -11.212 1.683   0.56 18.82 ?  140 LEU   A HD22 1 
ATOM   3189 H HD22 B LEU   A 1 140 ? 10.681 -10.757 1.419   0.44 16.35 ?  140 LEU   A HD22 1 
ATOM   3190 H HD23 A LEU   A 1 140 ? 10.244 -12.278 0.574   0.56 18.82 ?  140 LEU   A HD23 1 
ATOM   3191 H HD23 B LEU   A 1 140 ? 10.188 -12.055 0.647   0.44 16.35 ?  140 LEU   A HD23 1 
ATOM   3192 N N    A ARG   A 1 141 ? 14.051 -13.577 -1.907  0.56 13.24 ?  141 ARG   A N    1 
ATOM   3193 N N    B ARG   A 1 141 ? 14.005 -13.629 -2.191  0.44 14.55 ?  141 ARG   A N    1 
ATOM   3194 C CA   A ARG   A 1 141 ? 14.278 -14.984 -2.219  0.56 14.14 ?  141 ARG   A CA   1 
ATOM   3195 C CA   B ARG   A 1 141 ? 14.270 -14.997 -2.630  0.44 15.80 ?  141 ARG   A CA   1 
ATOM   3196 C C    A ARG   A 1 141 ? 15.770 -15.298 -2.226  0.56 13.21 ?  141 ARG   A C    1 
ATOM   3197 C C    B ARG   A 1 141 ? 15.762 -15.303 -2.605  0.44 15.20 ?  141 ARG   A C    1 
ATOM   3198 O O    A ARG   A 1 141 ? 16.224 -16.249 -1.576  0.56 12.53 ?  141 ARG   A O    1 
ATOM   3199 O O    B ARG   A 1 141 ? 16.173 -16.394 -2.193  0.44 14.04 ?  141 ARG   A O    1 
ATOM   3200 C CB   A ARG   A 1 141 ? 13.654 -15.300 -3.579  0.56 15.26 ?  141 ARG   A CB   1 
ATOM   3201 C CB   B ARG   A 1 141 ? 13.710 -15.192 -4.039  0.44 17.37 ?  141 ARG   A CB   1 
ATOM   3202 C CG   A ARG   A 1 141 ? 13.650 -16.769 -3.961  0.56 16.91 ?  141 ARG   A CG   1 
ATOM   3203 C CG   B ARG   A 1 141 ? 13.836 -16.599 -4.594  0.44 18.67 ?  141 ARG   A CG   1 
ATOM   3204 C CD   A ARG   A 1 141 ? 12.606 -17.518 -3.177  0.56 19.51 ?  141 ARG   A CD   1 
ATOM   3205 C CD   B ARG   A 1 141 ? 12.803 -17.507 -3.983  0.44 19.73 ?  141 ARG   A CD   1 
ATOM   3206 N NE   A ARG   A 1 141 ? 13.211 -18.421 -2.211  0.56 20.97 ?  141 ARG   A NE   1 
ATOM   3207 N NE   B ARG   A 1 141 ? 13.274 -18.124 -2.751  0.44 19.99 ?  141 ARG   A NE   1 
ATOM   3208 C CZ   A ARG   A 1 141 ? 12.546 -18.992 -1.216  0.56 20.89 ?  141 ARG   A CZ   1 
ATOM   3209 C CZ   B ARG   A 1 141 ? 12.481 -18.556 -1.779  0.44 20.93 ?  141 ARG   A CZ   1 
ATOM   3210 N NH1  A ARG   A 1 141 ? 11.272 -18.713 -0.986  0.56 20.04 ?  141 ARG   A NH1  1 
ATOM   3211 N NH1  B ARG   A 1 141 ? 11.174 -18.356 -1.813  0.44 21.19 ?  141 ARG   A NH1  1 
ATOM   3212 N NH2  A ARG   A 1 141 ? 13.176 -19.855 -0.425  0.56 21.54 ?  141 ARG   A NH2  1 
ATOM   3213 N NH2  B ARG   A 1 141 ? 13.013 -19.204 -0.746  0.44 21.61 ?  141 ARG   A NH2  1 
ATOM   3214 H H    A ARG   A 1 141 ? 13.673 -13.126 -2.534  0.56 15.91 ?  141 ARG   A H    1 
ATOM   3215 H H    B ARG   A 1 141 ? 13.592 -13.145 -2.767  0.44 17.49 ?  141 ARG   A H    1 
ATOM   3216 H HA   A ARG   A 1 141 ? 13.850 -15.535 -1.549  0.56 16.99 ?  141 ARG   A HA   1 
ATOM   3217 H HA   B ARG   A 1 141 ? 13.826 -15.618 -2.034  0.44 18.99 ?  141 ARG   A HA   1 
ATOM   3218 H HB2  A ARG   A 1 141 ? 12.731 -14.992 -3.578  0.56 18.33 ?  141 ARG   A HB2  1 
ATOM   3219 H HB2  B ARG   A 1 141 ? 12.766 -14.962 -4.028  0.44 20.87 ?  141 ARG   A HB2  1 
ATOM   3220 H HB3  A ARG   A 1 141 ? 14.148 -14.821 -4.263  0.56 18.33 ?  141 ARG   A HB3  1 
ATOM   3221 H HB3  B ARG   A 1 141 ? 14.180 -14.600 -4.641  0.44 20.87 ?  141 ARG   A HB3  1 
ATOM   3222 H HG2  A ARG   A 1 141 ? 13.450 -16.857 -4.907  0.56 20.32 ?  141 ARG   A HG2  1 
ATOM   3223 H HG2  B ARG   A 1 141 ? 13.696 -16.578 -5.552  0.44 22.43 ?  141 ARG   A HG2  1 
ATOM   3224 H HG3  A ARG   A 1 141 ? 14.519 -17.157 -3.765  0.56 20.32 ?  141 ARG   A HG3  1 
ATOM   3225 H HG3  B ARG   A 1 141 ? 14.717 -16.954 -4.390  0.44 22.43 ?  141 ARG   A HG3  1 
ATOM   3226 H HD2  A ARG   A 1 141 ? 12.055 -16.886 -2.687  0.56 23.43 ?  141 ARG   A HD2  1 
ATOM   3227 H HD2  B ARG   A 1 141 ? 12.008 -16.991 -3.779  0.44 23.70 ?  141 ARG   A HD2  1 
ATOM   3228 H HD3  A ARG   A 1 141 ? 12.052 -18.030 -3.792  0.56 23.43 ?  141 ARG   A HD3  1 
ATOM   3229 H HD3  B ARG   A 1 141 ? 12.587 -18.212 -4.612  0.44 23.70 ?  141 ARG   A HD3  1 
ATOM   3230 H HE   A ARG   A 1 141 ? 14.003 -18.708 -2.374  0.56 25.19 ?  141 ARG   A HE   1 
ATOM   3231 H HE   B ARG   A 1 141 ? 14.122 -18.237 -2.656  0.44 24.01 ?  141 ARG   A HE   1 
ATOM   3232 H HH11 A ARG   A 1 141 ? 10.844 -18.169 -1.497  0.56 24.07 ?  141 ARG   A HH11 1 
ATOM   3233 H HH11 B ARG   A 1 141 ? 10.813 -17.943 -2.478  0.44 25.45 ?  141 ARG   A HH11 1 
ATOM   3234 H HH12 A ARG   A 1 141 ? 10.858 -19.094 -0.332  0.56 24.07 ?  141 ARG   A HH12 1 
ATOM   3235 H HH12 B ARG   A 1 141 ? 10.683 -18.638 -1.171  0.44 25.45 ?  141 ARG   A HH12 1 
ATOM   3236 H HH21 A ARG   A 1 141 ? 14.001 -20.042 -0.569  0.56 25.87 ?  141 ARG   A HH21 1 
ATOM   3237 H HH21 B ARG   A 1 141 ? 13.860 -19.340 -0.713  0.44 25.95 ?  141 ARG   A HH21 1 
ATOM   3238 H HH22 A ARG   A 1 141 ? 12.756 -20.223 0.229   0.56 25.87 ?  141 ARG   A HH22 1 
ATOM   3239 H HH22 B ARG   A 1 141 ? 12.507 -19.481 -0.106  0.44 25.95 ?  141 ARG   A HH22 1 
ATOM   3240 N N    A VAL   A 1 142 ? 16.551 -14.506 -2.969  0.56 13.50 ?  142 VAL   A N    1 
ATOM   3241 N N    B VAL   A 1 142 ? 16.592 -14.359 -3.054  0.44 15.24 ?  142 VAL   A N    1 
ATOM   3242 C CA   A VAL   A 1 142 ? 17.998 -14.708 -3.001  0.56 13.89 ?  142 VAL   A CA   1 
ATOM   3243 C CA   B VAL   A 1 142 ? 18.033 -14.592 -3.045  0.44 14.67 ?  142 VAL   A CA   1 
ATOM   3244 C C    A VAL   A 1 142 ? 18.573 -14.638 -1.592  0.56 13.55 ?  142 VAL   A C    1 
ATOM   3245 C C    B VAL   A 1 142 ? 18.560 -14.620 -1.615  0.44 13.86 ?  142 VAL   A C    1 
ATOM   3246 O O    A VAL   A 1 142 ? 19.457 -15.423 -1.227  0.56 14.41 ?  142 VAL   A O    1 
ATOM   3247 O O    B VAL   A 1 142 ? 19.397 -15.460 -1.261  0.44 14.40 ?  142 VAL   A O    1 
ATOM   3248 C CB   A VAL   A 1 142 ? 18.677 -13.714 -3.967  0.56 14.50 ?  142 VAL   A CB   1 
ATOM   3249 C CB   B VAL   A 1 142 ? 18.760 -13.548 -3.912  0.44 15.01 ?  142 VAL   A CB   1 
ATOM   3250 C CG1  A VAL   A 1 142 ? 20.193 -13.907 -3.952  0.56 14.36 ?  142 VAL   A CG1  1 
ATOM   3251 C CG1  B VAL   A 1 142 ? 20.264 -13.745 -3.814  0.44 15.10 ?  142 VAL   A CG1  1 
ATOM   3252 C CG2  A VAL   A 1 142 ? 18.143 -13.886 -5.387  0.56 15.25 ?  142 VAL   A CG2  1 
ATOM   3253 C CG2  B VAL   A 1 142 ? 18.317 -13.656 -5.360  0.44 15.21 ?  142 VAL   A CG2  1 
ATOM   3254 H H    A VAL   A 1 142 ? 16.270 -13.852 -3.460  0.56 16.22 ?  142 VAL   A H    1 
ATOM   3255 H H    B VAL   A 1 142 ? 16.350 -13.588 -3.365  0.44 18.31 ?  142 VAL   A H    1 
ATOM   3256 H HA   A VAL   A 1 142 ? 18.174 -15.595 -3.339  0.56 16.69 ?  142 VAL   A HA   1 
ATOM   3257 H HA   B VAL   A 1 142 ? 18.204 -15.457 -3.437  0.44 17.62 ?  142 VAL   A HA   1 
ATOM   3258 H HB   A VAL   A 1 142 ? 18.492 -12.805 -3.684  0.56 17.42 ?  142 VAL   A HB   1 
ATOM   3259 H HB   B VAL   A 1 142 ? 18.549 -12.653 -3.597  0.44 18.04 ?  142 VAL   A HB   1 
ATOM   3260 H HG11 A VAL   A 1 142 ? 20.584 -13.417 -4.694  0.56 17.25 ?  142 VAL   A HG11 1 
ATOM   3261 H HG11 B VAL   A 1 142 ? 20.696 -13.218 -4.504  0.44 18.14 ?  142 VAL   A HG11 1 
ATOM   3262 H HG12 A VAL   A 1 142 ? 20.550 -13.570 -3.114  0.56 17.25 ?  142 VAL   A HG12 1 
ATOM   3263 H HG12 B VAL   A 1 142 ? 20.567 -13.455 -2.940  0.44 18.14 ?  142 VAL   A HG12 1 
ATOM   3264 H HG13 A VAL   A 1 142 ? 20.394 -14.851 -4.041  0.56 17.25 ?  142 VAL   A HG13 1 
ATOM   3265 H HG13 B VAL   A 1 142 ? 20.465 -14.684 -3.942  0.44 18.14 ?  142 VAL   A HG13 1 
ATOM   3266 H HG21 A VAL   A 1 142 ? 18.621 -13.282 -5.981  0.56 18.32 ?  142 VAL   A HG21 1 
ATOM   3267 H HG21 B VAL   A 1 142 ? 18.796 -13.000 -5.889  0.44 18.28 ?  142 VAL   A HG21 1 
ATOM   3268 H HG22 A VAL   A 1 142 ? 18.289 -14.804 -5.668  0.56 18.32 ?  142 VAL   A HG22 1 
ATOM   3269 H HG22 B VAL   A 1 142 ? 18.516 -14.550 -5.681  0.44 18.28 ?  142 VAL   A HG22 1 
ATOM   3270 H HG23 A VAL   A 1 142 ? 17.199 -13.680 -5.396  0.56 18.32 ?  142 VAL   A HG23 1 
ATOM   3271 H HG23 B VAL   A 1 142 ? 17.363 -13.492 -5.410  0.44 18.28 ?  142 VAL   A HG23 1 
ATOM   3272 N N    . CYS   A 1 143 ? 18.084 -13.702 -0.774  1.00 13.65 ?  143 CYS   A N    1 
ATOM   3273 C CA   . CYS   A 1 143 ? 18.548 -13.637 0.611   1.00 14.20 ?  143 CYS   A CA   1 
ATOM   3274 C C    . CYS   A 1 143 ? 18.318 -14.970 1.321   1.00 14.51 ?  143 CYS   A C    1 
ATOM   3275 O O    . CYS   A 1 143 ? 19.233 -15.550 1.915   1.00 14.32 ?  143 CYS   A O    1 
ATOM   3276 C CB   . CYS   A 1 143 ? 17.824 -12.509 1.344   1.00 14.62 ?  143 CYS   A CB   1 
ATOM   3277 S SG   . CYS   A 1 143 ? 18.294 -12.336 3.063   1.00 15.02 ?  143 CYS   A SG   1 
ATOM   3278 H H    A CYS   A 1 143 ? 17.500 -13.110 -0.989  0.56 16.41 ?  143 CYS   A H    1 
ATOM   3279 H H    B CYS   A 1 143 ? 17.496 -13.111 -0.977  0.44 16.41 ?  143 CYS   A H    1 
ATOM   3280 H HA   . CYS   A 1 143 ? 19.499 -13.451 0.625   1.00 17.06 ?  143 CYS   A HA   1 
ATOM   3281 H HB2  . CYS   A 1 143 ? 18.014 -11.671 0.899   1.00 17.57 ?  143 CYS   A HB2  1 
ATOM   3282 H HB3  . CYS   A 1 143 ? 16.870 -12.683 1.314   1.00 17.57 ?  143 CYS   A HB3  1 
ATOM   3283 H HG   . CYS   A 1 143 ? 17.746 -11.380 3.522   1.00 18.05 ?  143 CYS   A HG   1 
ATOM   3284 N N    . VAL   A 1 144 ? 17.090 -15.480 1.251   1.00 14.96 ?  144 VAL   A N    1 
ATOM   3285 C CA   . VAL   A 1 144 ? 16.739 -16.709 1.955   1.00 16.30 ?  144 VAL   A CA   1 
ATOM   3286 C C    . VAL   A 1 144 ? 17.555 -17.885 1.441   1.00 16.00 ?  144 VAL   A C    1 
ATOM   3287 O O    . VAL   A 1 144 ? 17.921 -18.789 2.208   1.00 16.79 ?  144 VAL   A O    1 
ATOM   3288 C CB   . VAL   A 1 144 ? 15.223 -16.945 1.814   1.00 19.15 ?  144 VAL   A CB   1 
ATOM   3289 C CG1  . VAL   A 1 144 ? 14.857 -18.394 2.072   1.00 21.12 ?  144 VAL   A CG1  1 
ATOM   3290 C CG2  . VAL   A 1 144 ? 14.468 -15.962 2.727   1.00 18.95 ?  144 VAL   A CG2  1 
ATOM   3291 H H    . VAL   A 1 144 ? 16.437 -15.131 0.800   1.00 17.97 ?  144 VAL   A H    1 
ATOM   3292 H HA   . VAL   A 1 144 ? 16.931 -16.603 2.891   1.00 19.58 ?  144 VAL   A HA   1 
ATOM   3293 H HB   . VAL   A 1 144 ? 14.960 -16.735 0.898   1.00 23.01 ?  144 VAL   A HB   1 
ATOM   3294 H HG11 . VAL   A 1 144 ? 13.901 -18.447 2.237   1.00 25.37 ?  144 VAL   A HG11 1 
ATOM   3295 H HG12 . VAL   A 1 144 ? 15.083 -18.919 1.289   1.00 25.37 ?  144 VAL   A HG12 1 
ATOM   3296 H HG13 . VAL   A 1 144 ? 15.345 -18.705 2.844   1.00 25.37 ?  144 VAL   A HG13 1 
ATOM   3297 H HG21 . VAL   A 1 144 ? 13.509 -16.100 2.623   1.00 22.76 ?  144 VAL   A HG21 1 
ATOM   3298 H HG22 . VAL   A 1 144 ? 14.723 -16.125 3.648   1.00 22.76 ?  144 VAL   A HG22 1 
ATOM   3299 H HG23 . VAL   A 1 144 ? 14.693 -15.051 2.477   1.00 22.76 ?  144 VAL   A HG23 1 
ATOM   3300 N N    . ASP   A 1 145 ? 17.829 -17.908 0.141   1.00 16.21 ?  145 ASP   A N    1 
ATOM   3301 C CA   . ASP   A 1 145 ? 18.541 -19.015 -0.486  1.00 17.04 ?  145 ASP   A CA   1 
ATOM   3302 C C    . ASP   A 1 145 ? 20.059 -18.872 -0.419  1.00 16.90 ?  145 ASP   A C    1 
ATOM   3303 O O    . ASP   A 1 145 ? 20.764 -19.773 -0.882  1.00 18.25 ?  145 ASP   A O    1 
ATOM   3304 C CB   . ASP   A 1 145 ? 18.113 -19.147 -1.950  1.00 18.94 ?  145 ASP   A CB   1 
ATOM   3305 C CG   . ASP   A 1 145 ? 16.671 -19.606 -2.106  1.00 21.37 ?  145 ASP   A CG   1 
ATOM   3306 O OD1  . ASP   A 1 145 ? 16.082 -20.118 -1.128  1.00 22.18 ?  145 ASP   A OD1  1 
ATOM   3307 O OD2  . ASP   A 1 145 ? 16.124 -19.442 -3.216  1.00 22.46 -1 145 ASP   A OD2  1 
ATOM   3308 H H    . ASP   A 1 145 ? 17.595 -17.289 -0.415  1.00 19.47 ?  145 ASP   A H    1 
ATOM   3309 H HA   . ASP   A 1 145 ? 18.301 -19.835 -0.033  1.00 20.47 ?  145 ASP   A HA   1 
ATOM   3310 H HB2  . ASP   A 1 145 ? 18.206 -18.282 -2.385  1.00 22.75 ?  145 ASP   A HB2  1 
ATOM   3311 H HB3  . ASP   A 1 145 ? 18.678 -19.800 -2.386  1.00 22.75 ?  145 ASP   A HB3  1 
ATOM   3312 N N    . THR   A 1 146 ? 20.584 -17.771 0.125   1.00 14.85 ?  146 THR   A N    1 
ATOM   3313 C CA   . THR   A 1 146 ? 22.023 -17.522 0.156   1.00 14.68 ?  146 THR   A CA   1 
ATOM   3314 C C    . THR   A 1 146 ? 22.560 -17.346 1.564   1.00 14.53 ?  146 THR   A C    1 
ATOM   3315 O O    . THR   A 1 146 ? 23.632 -17.886 1.885   1.00 15.46 ?  146 THR   A O    1 
ATOM   3316 C CB   . THR   A 1 146 ? 22.359 -16.278 -0.685  1.00 14.51 ?  146 THR   A CB   1 
ATOM   3317 O OG1  . THR   A 1 146 ? 21.848 -16.443 -2.013  1.00 15.42 ?  146 THR   A OG1  1 
ATOM   3318 C CG2  . THR   A 1 146 ? 23.858 -16.044 -0.742  1.00 15.44 ?  146 THR   A CG2  1 
ATOM   3319 H H    . THR   A 1 146 ? 20.114 -17.137 0.478   1.00 17.85 ?  146 THR   A H    1 
ATOM   3320 H HA   . THR   A 1 146 ? 22.481 -18.275 -0.237  1.00 17.64 ?  146 THR   A HA   1 
ATOM   3321 H HB   . THR   A 1 146 ? 21.954 -15.494 -0.279  1.00 17.44 ?  146 THR   A HB   1 
ATOM   3322 H HG1  . THR   A 1 146 ? 21.016 -16.518 -1.987  1.00 18.53 ?  146 THR   A HG1  1 
ATOM   3323 H HG21 . THR   A 1 146 ? 24.064 -15.385 -1.423  1.00 18.55 ?  146 THR   A HG21 1 
ATOM   3324 H HG22 . THR   A 1 146 ? 24.180 -15.721 0.115   1.00 18.55 ?  146 THR   A HG22 1 
ATOM   3325 H HG23 . THR   A 1 146 ? 24.313 -16.873 -0.958  1.00 18.55 ?  146 THR   A HG23 1 
ATOM   3326 N N    . VAL   A 1 147 ? 21.887 -16.556 2.396   1.00 14.49 ?  147 VAL   A N    1 
ATOM   3327 C CA   . VAL   A 1 147 ? 22.379 -16.261 3.734   1.00 14.72 ?  147 VAL   A CA   1 
ATOM   3328 C C    . VAL   A 1 147 ? 22.060 -17.433 4.651   1.00 14.81 ?  147 VAL   A C    1 
ATOM   3329 O O    . VAL   A 1 147 ? 20.921 -17.919 4.693   1.00 15.24 ?  147 VAL   A O    1 
ATOM   3330 C CB   . VAL   A 1 147 ? 21.766 -14.953 4.256   1.00 14.69 ?  147 VAL   A CB   1 
ATOM   3331 C CG1  . VAL   A 1 147 ? 22.305 -14.639 5.633   1.00 15.80 ?  147 VAL   A CG1  1 
ATOM   3332 C CG2  . VAL   A 1 147 ? 22.016 -13.806 3.274   1.00 15.15 ?  147 VAL   A CG2  1 
ATOM   3333 H H    . VAL   A 1 147 ? 21.139 -16.174 2.209   1.00 17.41 ?  147 VAL   A H    1 
ATOM   3334 H HA   . VAL   A 1 147 ? 23.342 -16.155 3.705   1.00 17.69 ?  147 VAL   A HA   1 
ATOM   3335 H HB   . VAL   A 1 147 ? 20.808 -15.072 4.339   1.00 17.65 ?  147 VAL   A HB   1 
ATOM   3336 H HG11 . VAL   A 1 147 ? 22.052 -13.738 5.871   1.00 18.98 ?  147 VAL   A HG11 1 
ATOM   3337 H HG12 . VAL   A 1 147 ? 21.927 -15.269 6.271   1.00 18.98 ?  147 VAL   A HG12 1 
ATOM   3338 H HG13 . VAL   A 1 147 ? 23.271 -14.724 5.620   1.00 18.98 ?  147 VAL   A HG13 1 
ATOM   3339 H HG21 . VAL   A 1 147 ? 21.704 -12.982 3.674   1.00 18.21 ?  147 VAL   A HG21 1 
ATOM   3340 H HG22 . VAL   A 1 147 ? 22.963 -13.754 3.089   1.00 18.21 ?  147 VAL   A HG22 1 
ATOM   3341 H HG23 . VAL   A 1 147 ? 21.525 -13.987 2.457   1.00 18.21 ?  147 VAL   A HG23 1 
ATOM   3342 N N    . ARG   A 1 148 ? 23.071 -17.881 5.394   1.00 14.95 ?  148 ARG   A N    1 
ATOM   3343 C CA   . ARG   A 1 148 ? 22.939 -18.957 6.364   1.00 15.07 ?  148 ARG   A CA   1 
ATOM   3344 C C    . ARG   A 1 148 ? 23.049 -18.482 7.800   1.00 15.76 ?  148 ARG   A C    1 
ATOM   3345 O O    . ARG   A 1 148 ? 22.637 -19.209 8.711   1.00 17.22 ?  148 ARG   A O    1 
ATOM   3346 C CB   . ARG   A 1 148 ? 23.990 -20.051 6.106   1.00 16.25 ?  148 ARG   A CB   1 
ATOM   3347 C CG   . ARG   A 1 148 ? 23.847 -20.697 4.740   1.00 17.58 ?  148 ARG   A CG   1 
ATOM   3348 C CD   . ARG   A 1 148 ? 24.948 -21.719 4.463   1.00 18.21 ?  148 ARG   A CD   1 
ATOM   3349 N NE   . ARG   A 1 148 ? 26.284 -21.133 4.506   1.00 18.44 ?  148 ARG   A NE   1 
ATOM   3350 C CZ   . ARG   A 1 148 ? 26.812 -20.406 3.530   1.00 17.45 ?  148 ARG   A CZ   1 
ATOM   3351 N NH1  . ARG   A 1 148 ? 26.160 -20.197 2.395   1.00 17.90 ?  148 ARG   A NH1  1 
ATOM   3352 N NH2  . ARG   A 1 148 ? 28.020 -19.865 3.699   1.00 17.89 ?  148 ARG   A NH2  1 
ATOM   3353 H H    . ARG   A 1 148 ? 23.870 -17.561 5.350   1.00 17.96 ?  148 ARG   A H    1 
ATOM   3354 H HA   . ARG   A 1 148 ? 22.065 -19.362 6.261   1.00 18.11 ?  148 ARG   A HA   1 
ATOM   3355 H HB2  . ARG   A 1 148 ? 24.874 -19.669 6.163   1.00 19.53 ?  148 ARG   A HB2  1 
ATOM   3356 H HB3  . ARG   A 1 148 ? 23.885 -20.755 6.771   1.00 19.53 ?  148 ARG   A HB3  1 
ATOM   3357 H HG2  . ARG   A 1 148 ? 22.987 -21.145 4.692   1.00 21.12 ?  148 ARG   A HG2  1 
ATOM   3358 H HG3  . ARG   A 1 148 ? 23.892 -19.999 4.063   1.00 21.12 ?  148 ARG   A HG3  1 
ATOM   3359 H HD2  . ARG   A 1 148 ? 24.902 -22.413 5.132   1.00 21.87 ?  148 ARG   A HD2  1 
ATOM   3360 H HD3  . ARG   A 1 148 ? 24.808 -22.092 3.578   1.00 21.87 ?  148 ARG   A HD3  1 
ATOM   3361 H HE   . ARG   A 1 148 ? 26.752 -21.256 5.211   1.00 22.15 ?  148 ARG   A HE   1 
ATOM   3362 H HH11 . ARG   A 1 148 ? 25.382 -20.532 2.272   1.00 21.51 ?  148 ARG   A HH11 1 
ATOM   3363 H HH12 . ARG   A 1 148 ? 26.525 -19.719 1.772   1.00 21.51 ?  148 ARG   A HH12 1 
ATOM   3364 H HH21 . ARG   A 1 148 ? 28.446 -19.986 4.437   1.00 21.49 ?  148 ARG   A HH21 1 
ATOM   3365 H HH22 . ARG   A 1 148 ? 28.375 -19.388 3.075   1.00 21.49 ?  148 ARG   A HH22 1 
ATOM   3366 N N    . THR   A 1 149 ? 23.602 -17.292 8.016   1.00 16.12 ?  149 THR   A N    1 
ATOM   3367 C CA   . THR   A 1 149 ? 23.670 -16.682 9.330   1.00 16.31 ?  149 THR   A CA   1 
ATOM   3368 C C    . THR   A 1 149 ? 22.339 -15.987 9.625   1.00 15.97 ?  149 THR   A C    1 
ATOM   3369 O O    . THR   A 1 149 ? 21.411 -15.984 8.803   1.00 16.13 ?  149 THR   A O    1 
ATOM   3370 C CB   . THR   A 1 149 ? 24.866 -15.738 9.385   1.00 16.21 ?  149 THR   A CB   1 
ATOM   3371 O OG1  . THR   A 1 149 ? 24.741 -14.816 8.301   1.00 15.95 ?  149 THR   A OG1  1 
ATOM   3372 C CG2  . THR   A 1 149 ? 26.181 -16.530 9.272   1.00 16.04 ?  149 THR   A CG2  1 
ATOM   3373 H H    . THR   A 1 149 ? 23.957 -16.803 7.396   1.00 19.37 ?  149 THR   A H    1 
ATOM   3374 H HA   . THR   A 1 149 ? 23.796 -17.386 9.991   1.00 19.59 ?  149 THR   A HA   1 
ATOM   3375 H HB   . THR   A 1 149 ? 24.853 -15.268 10.232  1.00 19.48 ?  149 THR   A HB   1 
ATOM   3376 H HG1  . THR   A 1 149 ? 25.388 -14.279 8.315   1.00 19.17 ?  149 THR   A HG1  1 
ATOM   3377 H HG21 . THR   A 1 149 ? 26.935 -15.922 9.326   1.00 19.27 ?  149 THR   A HG21 1 
ATOM   3378 H HG22 . THR   A 1 149 ? 26.248 -17.179 9.992   1.00 19.27 ?  149 THR   A HG22 1 
ATOM   3379 H HG23 . THR   A 1 149 ? 26.216 -17.001 8.423   1.00 19.27 ?  149 THR   A HG23 1 
ATOM   3380 N N    . ASN   A 1 150 ? 22.203 -15.451 10.832  1.00 15.71 ?  150 ASN   A N    1 
ATOM   3381 C CA   . ASN   A 1 150 ? 20.915 -14.928 11.295  1.00 16.36 ?  150 ASN   A CA   1 
ATOM   3382 C C    . ASN   A 1 150 ? 20.743 -13.492 10.820  1.00 15.58 ?  150 ASN   A C    1 
ATOM   3383 O O    . ASN   A 1 150 ? 21.495 -12.599 11.230  1.00 16.22 ?  150 ASN   A O    1 
ATOM   3384 C CB   . ASN   A 1 150 ? 20.840 -15.025 12.812  1.00 18.83 ?  150 ASN   A CB   1 
ATOM   3385 C CG   . ASN   A 1 150 ? 20.744 -16.453 13.285  1.00 22.95 ?  150 ASN   A CG   1 
ATOM   3386 O OD1  . ASN   A 1 150 ? 20.144 -17.292 12.613  1.00 23.96 ?  150 ASN   A OD1  1 
ATOM   3387 N ND2  . ASN   A 1 150 ? 21.345 -16.747 14.435  1.00 25.64 ?  150 ASN   A ND2  1 
ATOM   3388 H H    . ASN   A 1 150 ? 22.840 -15.393 11.409  1.00 18.87 ?  150 ASN   A H    1 
ATOM   3389 H HA   . ASN   A 1 150 ? 20.199 -15.472 10.920  1.00 19.65 ?  150 ASN   A HA   1 
ATOM   3390 H HB2  . ASN   A 1 150 ? 21.638 -14.634 13.195  1.00 22.62 ?  150 ASN   A HB2  1 
ATOM   3391 H HB3  . ASN   A 1 150 ? 20.051 -14.559 13.121  1.00 22.62 ?  150 ASN   A HB3  1 
ATOM   3392 H HD21 . ASN   A 1 150 ? 21.323 -17.551 14.750  1.00 30.79 ?  150 ASN   A HD21 1 
ATOM   3393 H HD22 . ASN   A 1 150 ? 21.755 -16.131 14.878  1.00 30.79 ?  150 ASN   A HD22 1 
ATOM   3394 N N    . VAL   A 1 151 ? 19.764 -13.264 9.954   1.00 14.59 ?  151 VAL   A N    1 
ATOM   3395 C CA   . VAL   A 1 151 ? 19.557 -11.960 9.348   1.00 14.77 ?  151 VAL   A CA   1 
ATOM   3396 C C    . VAL   A 1 151 ? 18.171 -11.437 9.701   1.00 14.59 ?  151 VAL   A C    1 
ATOM   3397 O O    . VAL   A 1 151 ? 17.160 -12.146 9.558   1.00 16.07 ?  151 VAL   A O    1 
ATOM   3398 C CB   . VAL   A 1 151 ? 19.851 -11.971 7.834   1.00 16.35 ?  151 VAL   A CB   1 
ATOM   3399 C CG1  . VAL   A 1 151 ? 19.020 -12.997 7.105   1.00 17.47 ?  151 VAL   A CG1  1 
ATOM   3400 C CG2  . VAL   A 1 151 ? 19.684 -10.576 7.235   1.00 16.43 ?  151 VAL   A CG2  1 
ATOM   3401 H H    . VAL   A 1 151 ? 19.191 -13.860 9.704   1.00 17.53 ?  151 VAL   A H    1 
ATOM   3402 H HA   . VAL   A 1 151 ? 20.200 -11.346 9.742   1.00 17.75 ?  151 VAL   A HA   1 
ATOM   3403 H HB   . VAL   A 1 151 ? 20.784 -12.224 7.711   1.00 19.64 ?  151 VAL   A HB   1 
ATOM   3404 H HG11 . VAL   A 1 151 ? 19.187 -12.928 6.154   1.00 20.98 ?  151 VAL   A HG11 1 
ATOM   3405 H HG12 . VAL   A 1 151 ? 19.274 -13.887 7.418   1.00 20.98 ?  151 VAL   A HG12 1 
ATOM   3406 H HG13 . VAL   A 1 151 ? 18.083 -12.842 7.294   1.00 20.98 ?  151 VAL   A HG13 1 
ATOM   3407 H HG21 . VAL   A 1 151 ? 19.996 -10.591 6.313   1.00 19.74 ?  151 VAL   A HG21 1 
ATOM   3408 H HG22 . VAL   A 1 151 ? 18.747 -10.331 7.259   1.00 19.74 ?  151 VAL   A HG22 1 
ATOM   3409 H HG23 . VAL   A 1 151 ? 20.209 -9.945  7.749   1.00 19.74 ?  151 VAL   A HG23 1 
ATOM   3410 N N    A TYR   A 1 152 ? 18.139 -10.200 10.171  0.56 14.50 ?  152 TYR   A N    1 
ATOM   3411 N N    B TYR   A 1 152 ? 18.145 -10.184 10.166  0.44 14.62 ?  152 TYR   A N    1 
ATOM   3412 C CA   A TYR   A 1 152 ? 16.919 -9.483  10.498  0.56 14.19 ?  152 TYR   A CA   1 
ATOM   3413 C CA   B TYR   A 1 152 ? 16.950 -9.466  10.594  0.44 14.33 ?  152 TYR   A CA   1 
ATOM   3414 C C    A TYR   A 1 152 ? 16.735 -8.408  9.438   0.56 13.24 ?  152 TYR   A C    1 
ATOM   3415 C C    B TYR   A 1 152 ? 16.744 -8.330  9.606   0.44 13.13 ?  152 TYR   A C    1 
ATOM   3416 O O    A TYR   A 1 152 ? 17.532 -7.464  9.354   0.56 13.02 ?  152 TYR   A O    1 
ATOM   3417 O O    B TYR   A 1 152 ? 17.458 -7.323  9.647   0.44 13.06 ?  152 TYR   A O    1 
ATOM   3418 C CB   A TYR   A 1 152 ? 17.040 -8.924  11.912  0.56 15.01 ?  152 TYR   A CB   1 
ATOM   3419 C CB   B TYR   A 1 152 ? 17.140 -8.942  12.013  0.44 15.18 ?  152 TYR   A CB   1 
ATOM   3420 C CG   A TYR   A 1 152 ? 17.043 -10.040 12.930  0.56 15.67 ?  152 TYR   A CG   1 
ATOM   3421 C CG   B TYR   A 1 152 ? 17.061 -10.036 13.042  0.44 16.21 ?  152 TYR   A CG   1 
ATOM   3422 C CD1  A TYR   A 1 152 ? 18.216 -10.701 13.285  0.56 17.37 ?  152 TYR   A CD1  1 
ATOM   3423 C CD1  B TYR   A 1 152 ? 18.157 -10.844 13.311  0.44 17.38 ?  152 TYR   A CD1  1 
ATOM   3424 C CD2  A TYR   A 1 152 ? 15.860 -10.468 13.509  0.56 16.05 ?  152 TYR   A CD2  1 
ATOM   3425 C CD2  B TYR   A 1 152 ? 15.883 -10.277 13.733  0.44 16.42 ?  152 TYR   A CD2  1 
ATOM   3426 C CE1  A TYR   A 1 152 ? 18.210 -11.746 14.197  0.56 18.63 ?  152 TYR   A CE1  1 
ATOM   3427 C CE1  B TYR   A 1 152 ? 18.087 -11.860 14.242  0.44 18.83 ?  152 TYR   A CE1  1 
ATOM   3428 C CE2  A TYR   A 1 152 ? 15.839 -11.521 14.421  0.56 17.32 ?  152 TYR   A CE2  1 
ATOM   3429 C CE2  B TYR   A 1 152 ? 15.800 -11.296 14.671  0.44 17.90 ?  152 TYR   A CE2  1 
ATOM   3430 C CZ   A TYR   A 1 152 ? 17.019 -12.153 14.766  0.56 18.46 ?  152 TYR   A CZ   1 
ATOM   3431 C CZ   B TYR   A 1 152 ? 16.908 -12.084 14.923  0.44 18.97 ?  152 TYR   A CZ   1 
ATOM   3432 O OH   A TYR   A 1 152 ? 17.011 -13.199 15.672  0.56 20.59 ?  152 TYR   A OH   1 
ATOM   3433 O OH   B TYR   A 1 152 ? 16.844 -13.101 15.851  0.44 21.10 ?  152 TYR   A OH   1 
ATOM   3434 H H    A TYR   A 1 152 ? 18.855 -9.730  10.310  0.56 17.43 ?  152 TYR   A H    1 
ATOM   3435 H H    B TYR   A 1 152 ? 18.859 -9.694  10.226  0.44 17.57 ?  152 TYR   A H    1 
ATOM   3436 H HA   A TYR   A 1 152 ? 16.169 -10.097 10.461  0.56 17.05 ?  152 TYR   A HA   1 
ATOM   3437 H HA   B TYR   A 1 152 ? 16.184 -10.048 10.564  0.44 17.22 ?  152 TYR   A HA   1 
ATOM   3438 H HB2  A TYR   A 1 152 ? 17.872 -8.436  11.994  0.56 18.04 ?  152 TYR   A HB2  1 
ATOM   3439 H HB2  B TYR   A 1 152 ? 18.014 -8.527  12.084  0.44 18.23 ?  152 TYR   A HB2  1 
ATOM   3440 H HB3  A TYR   A 1 152 ? 16.285 -8.347  12.090  0.56 18.04 ?  152 TYR   A HB3  1 
ATOM   3441 H HB3  B TYR   A 1 152 ? 16.447 -8.293  12.207  0.44 18.23 ?  152 TYR   A HB3  1 
ATOM   3442 H HD1  A TYR   A 1 152 ? 19.019 -10.436 12.904  0.56 20.87 ?  152 TYR   A HD1  1 
ATOM   3443 H HD1  B TYR   A 1 152 ? 18.954 -10.696 12.850  0.44 20.88 ?  152 TYR   A HD1  1 
ATOM   3444 H HD2  A TYR   A 1 152 ? 15.057 -10.053 13.278  0.56 19.28 ?  152 TYR   A HD2  1 
ATOM   3445 H HD2  B TYR   A 1 152 ? 15.131 -9.748  13.562  0.44 19.73 ?  152 TYR   A HD2  1 
ATOM   3446 H HE1  A TYR   A 1 152 ? 19.000 -12.173 14.432  0.56 22.38 ?  152 TYR   A HE1  1 
ATOM   3447 H HE1  B TYR   A 1 152 ? 18.833 -12.386 14.411  0.44 22.61 ?  152 TYR   A HE1  1 
ATOM   3448 H HE2  A TYR   A 1 152 ? 15.033 -11.790 14.807  0.56 20.81 ?  152 TYR   A HE2  1 
ATOM   3449 H HE2  B TYR   A 1 152 ? 15.006 -11.445 15.131  0.44 21.50 ?  152 TYR   A HE2  1 
ATOM   3450 H HH   A TYR   A 1 152 ? 16.226 -13.334 15.945  0.56 24.72 ?  152 TYR   A HH   1 
ATOM   3451 H HH   B TYR   A 1 152 ? 16.092 -13.104 16.216  0.44 25.34 ?  152 TYR   A HH   1 
ATOM   3452 N N    A LEU   A 1 153 ? 15.712 -8.583  8.602   0.56 13.34 ?  153 LEU   A N    1 
ATOM   3453 N N    B LEU   A 1 153 ? 15.778 -8.506  8.709   0.44 13.14 ?  153 LEU   A N    1 
ATOM   3454 C CA   A LEU   A 1 153 ? 15.474 -7.723  7.448   0.56 13.40 ?  153 LEU   A CA   1 
ATOM   3455 C CA   B LEU   A 1 153 ? 15.517 -7.555  7.642   0.44 12.98 ?  153 LEU   A CA   1 
ATOM   3456 C C    A LEU   A 1 153 ? 14.485 -6.627  7.811   0.56 13.05 ?  153 LEU   A C    1 
ATOM   3457 C C    B LEU   A 1 153 ? 14.519 -6.502  8.101   0.44 13.08 ?  153 LEU   A C    1 
ATOM   3458 O O    A LEU   A 1 153 ? 13.345 -6.912  8.199   0.56 13.84 ?  153 LEU   A O    1 
ATOM   3459 O O    B LEU   A 1 153 ? 13.460 -6.832  8.651   0.44 13.58 ?  153 LEU   A O    1 
ATOM   3460 C CB   A LEU   A 1 153 ? 14.903 -8.537  6.289   0.56 13.39 ?  153 LEU   A CB   1 
ATOM   3461 C CB   B LEU   A 1 153 ? 14.965 -8.286  6.420   0.44 13.16 ?  153 LEU   A CB   1 
ATOM   3462 C CG   A LEU   A 1 153 ? 15.870 -9.485  5.584   0.56 13.23 ?  153 LEU   A CG   1 
ATOM   3463 C CG   B LEU   A 1 153 ? 15.886 -9.364  5.844   0.44 13.58 ?  153 LEU   A CG   1 
ATOM   3464 C CD1  A LEU   A 1 153 ? 15.084 -10.390 4.639   0.56 13.35 ?  153 LEU   A CD1  1 
ATOM   3465 C CD1  B LEU   A 1 153 ? 15.145 -10.174 4.785   0.44 14.18 ?  153 LEU   A CD1  1 
ATOM   3466 C CD2  A LEU   A 1 153 ? 16.933 -8.690  4.839   0.56 12.41 ?  153 LEU   A CD2  1 
ATOM   3467 C CD2  B LEU   A 1 153 ? 17.165 -8.760  5.273   0.44 13.24 ?  153 LEU   A CD2  1 
ATOM   3468 H H    A LEU   A 1 153 ? 15.123 -9.203  8.697   0.56 16.02 ?  153 LEU   A H    1 
ATOM   3469 H H    B LEU   A 1 153 ? 15.250 -9.183  8.701   0.44 15.79 ?  153 LEU   A H    1 
ATOM   3470 H HA   A LEU   A 1 153 ? 16.305 -7.322  7.168   0.56 16.10 ?  153 LEU   A HA   1 
ATOM   3471 H HA   B LEU   A 1 153 ? 16.339 -7.114  7.393   0.44 15.60 ?  153 LEU   A HA   1 
ATOM   3472 H HB2  A LEU   A 1 153 ? 14.165 -9.075  6.625   0.56 16.09 ?  153 LEU   A HB2  1 
ATOM   3473 H HB2  B LEU   A 1 153 ? 14.131 -8.716  6.670   0.44 15.81 ?  153 LEU   A HB2  1 
ATOM   3474 H HB3  A LEU   A 1 153 ? 14.569 -7.921  5.619   0.56 16.09 ?  153 LEU   A HB3  1 
ATOM   3475 H HB3  B LEU   A 1 153 ? 14.798 -7.638  5.720   0.44 15.81 ?  153 LEU   A HB3  1 
ATOM   3476 H HG   A LEU   A 1 153 ? 16.311 -10.047 6.247   0.56 15.90 ?  153 LEU   A HG   1 
ATOM   3477 H HG   B LEU   A 1 153 ? 16.138 -9.972  6.557   0.44 16.32 ?  153 LEU   A HG   1 
ATOM   3478 H HD11 A LEU   A 1 153 ? 15.683 -11.048 4.262   0.56 16.04 ?  153 LEU   A HD11 1 
ATOM   3479 H HD11 B LEU   A 1 153 ? 15.725 -10.882 4.466   0.44 17.04 ?  153 LEU   A HD11 1 
ATOM   3480 H HD12 A LEU   A 1 153 ? 14.377 -10.828 5.138   0.56 16.04 ?  153 LEU   A HD12 1 
ATOM   3481 H HD12 B LEU   A 1 153 ? 14.345 -10.553 5.181   0.44 17.04 ?  153 LEU   A HD12 1 
ATOM   3482 H HD13 A LEU   A 1 153 ? 14.701 -9.843  3.935   0.56 16.04 ?  153 LEU   A HD13 1 
ATOM   3483 H HD13 B LEU   A 1 153 ? 14.905 -9.586  4.051   0.44 17.04 ?  153 LEU   A HD13 1 
ATOM   3484 H HD21 A LEU   A 1 153 ? 17.463 -9.294  4.309   0.56 14.91 ?  153 LEU   A HD21 1 
ATOM   3485 H HD21 B LEU   A 1 153 ? 17.691 -9.463  4.862   0.44 15.91 ?  153 LEU   A HD21 1 
ATOM   3486 H HD22 A LEU   A 1 153 ? 16.487 -8.042  4.270   0.56 14.91 ?  153 LEU   A HD22 1 
ATOM   3487 H HD22 B LEU   A 1 153 ? 16.932 -8.089  4.614   0.44 15.91 ?  153 LEU   A HD22 1 
ATOM   3488 H HD23 A LEU   A 1 153 ? 17.489 -8.231  5.488   0.56 14.91 ?  153 LEU   A HD23 1 
ATOM   3489 H HD23 B LEU   A 1 153 ? 17.671 -8.350  5.995   0.44 15.91 ?  153 LEU   A HD23 1 
ATOM   3490 N N    A ALA   A 1 154 ? 14.911 -5.379  7.647   0.56 13.27 ?  154 ALA   A N    1 
ATOM   3491 N N    B ALA   A 1 154 ? 14.864 -5.235  7.864   0.44 13.11 ?  154 ALA   A N    1 
ATOM   3492 C CA   A ALA   A 1 154 ? 14.060 -4.219  7.861   0.56 13.91 ?  154 ALA   A CA   1 
ATOM   3493 C CA   B ALA   A 1 154 ? 13.982 -4.095  8.097   0.44 13.22 ?  154 ALA   A CA   1 
ATOM   3494 C C    A ALA   A 1 154 ? 13.556 -3.733  6.511   0.56 13.71 ?  154 ALA   A C    1 
ATOM   3495 C C    B ALA   A 1 154 ? 13.532 -3.585  6.731   0.44 12.60 ?  154 ALA   A C    1 
ATOM   3496 O O    A ALA   A 1 154 ? 14.353 -3.446  5.612   0.56 14.12 ?  154 ALA   A O    1 
ATOM   3497 O O    B ALA   A 1 154 ? 14.348 -3.081  5.955   0.44 12.46 ?  154 ALA   A O    1 
ATOM   3498 C CB   A ALA   A 1 154 ? 14.829 -3.103  8.566   0.56 14.53 ?  154 ALA   A CB   1 
ATOM   3499 C CB   B ALA   A 1 154 ? 14.718 -3.005  8.876   0.44 13.61 ?  154 ALA   A CB   1 
ATOM   3500 H H    A ALA   A 1 154 ? 15.711 -5.178  7.399   0.56 15.95 ?  154 ALA   A H    1 
ATOM   3501 H H    B ALA   A 1 154 ? 15.638 -4.996  7.558   0.44 15.76 ?  154 ALA   A H    1 
ATOM   3502 H HA   A ALA   A 1 154 ? 13.297 -4.471  8.405   0.56 16.71 ?  154 ALA   A HA   1 
ATOM   3503 H HA   B ALA   A 1 154 ? 13.205 -4.373  8.604   0.44 15.89 ?  154 ALA   A HA   1 
ATOM   3504 H HB1  A ALA   A 1 154 ? 14.234 -2.347  8.691   0.56 17.46 ?  154 ALA   A HB1  1 
ATOM   3505 H HB1  B ALA   A 1 154 ? 14.118 -2.257  9.023   0.44 16.36 ?  154 ALA   A HB1  1 
ATOM   3506 H HB2  A ALA   A 1 154 ? 15.137 -3.430  9.424   0.56 17.46 ?  154 ALA   A HB2  1 
ATOM   3507 H HB2  B ALA   A 1 154 ? 15.009 -3.366  9.730   0.44 16.36 ?  154 ALA   A HB2  1 
ATOM   3508 H HB3  A ALA   A 1 154 ? 15.582 -2.846  8.015   0.56 17.46 ?  154 ALA   A HB3  1 
ATOM   3509 H HB3  B ALA   A 1 154 ? 15.489 -2.712  8.364   0.44 16.36 ?  154 ALA   A HB3  1 
ATOM   3510 N N    A VAL   A 1 155 ? 12.235 -3.667  6.372   0.26 12.48 ?  155 VAL   A N    1 
ATOM   3511 N N    B VAL   A 1 155 ? 12.240 -3.726  6.440   0.44 11.77 ?  155 VAL   A N    1 
ATOM   3512 C CA   A VAL   A 1 155 ? 11.571 -3.141  5.186   0.26 13.66 ?  155 VAL   A CA   1 
ATOM   3513 C CA   B VAL   A 1 155 ? 11.641 -3.326  5.169   0.44 13.68 ?  155 VAL   A CA   1 
ATOM   3514 C CA   T VAL   A 1 155 ? 11.563 -3.266  5.236   0.30 15.22 ?  155 VAL   A CA   1 
ATOM   3515 C C    A VAL   A 1 155 ? 10.882 -1.847  5.592   0.26 14.56 ?  155 VAL   A C    1 
ATOM   3516 C C    B VAL   A 1 155 ? 10.899 -2.015  5.401   0.44 14.58 ?  155 VAL   A C    1 
ATOM   3517 C C    T VAL   A 1 155 ? 10.987 -1.889  5.573   0.30 15.22 ?  155 VAL   A C    1 
ATOM   3518 O O    A VAL   A 1 155 ? 9.961  -1.861  6.417   0.26 15.00 ?  155 VAL   A O    1 
ATOM   3519 O O    B VAL   A 1 155 ? 9.896  -1.979  6.116   0.44 14.48 ?  155 VAL   A O    1 
ATOM   3520 O O    T VAL   A 1 155 ? 10.168 -1.752  6.479   0.30 15.05 ?  155 VAL   A O    1 
ATOM   3521 C CB   A VAL   A 1 155 ? 10.569 -4.155  4.614   0.26 13.93 ?  155 VAL   A CB   1 
ATOM   3522 C CB   B VAL   A 1 155 ? 10.705 -4.416  4.625   0.44 14.76 ?  155 VAL   A CB   1 
ATOM   3523 C CB   T VAL   A 1 155 ? 10.506 -4.231  4.657   0.30 15.43 ?  155 VAL   A CB   1 
ATOM   3524 C CG1  A VAL   A 1 155 ? 9.912  -3.610  3.356   0.26 14.31 ?  155 VAL   A CG1  1 
ATOM   3525 C CG1  B VAL   A 1 155 ? 9.960  -3.932  3.386   0.44 15.00 ?  155 VAL   A CG1  1 
ATOM   3526 C CG1  T VAL   A 1 155 ? 9.854  -3.635  3.422   0.30 15.70 ?  155 VAL   A CG1  1 
ATOM   3527 C CG2  A VAL   A 1 155 ? 11.268 -5.480  4.332   0.26 14.12 ?  155 VAL   A CG2  1 
ATOM   3528 C CG2  B VAL   A 1 155 ? 11.498 -5.679  4.308   0.44 15.64 ?  155 VAL   A CG2  1 
ATOM   3529 C CG2  T VAL   A 1 155 ? 11.143 -5.582  4.330   0.30 15.38 ?  155 VAL   A CG2  1 
ATOM   3530 H H    A VAL   A 1 155 ? 11.682 -3.936  6.974   0.26 15.00 ?  155 VAL   A H    1 
ATOM   3531 H H    B VAL   A 1 155 ? 11.668 -4.063  6.986   0.44 14.15 ?  155 VAL   A H    1 
ATOM   3532 H HA   A VAL   A 1 155 ? 12.230 -2.940  4.505   0.26 16.42 ?  155 VAL   A HA   1 
ATOM   3533 H HA   B VAL   A 1 155 ? 12.337 -3.168  4.514   0.44 16.43 ?  155 VAL   A HA   1 
ATOM   3534 H HB   A VAL   A 1 155 ? 9.874  -4.317  5.271   0.26 16.74 ?  155 VAL   A HB   1 
ATOM   3535 H HB   B VAL   A 1 155 ? 10.046 -4.637  5.302   0.44 17.73 ?  155 VAL   A HB   1 
ATOM   3536 H HB   T VAL   A 1 155 ? 9.816  -4.378  5.321   0.30 18.54 ?  155 VAL   A HB   1 
ATOM   3537 H HG11 A VAL   A 1 155 ? 9.378  -4.312  2.952   0.26 17.20 ?  155 VAL   A HG11 1 
ATOM   3538 H HG11 B VAL   A 1 155 ? 9.549  -4.695  2.945   0.44 18.02 ?  155 VAL   A HG11 1 
ATOM   3539 H HG11 T VAL   A 1 155 ? 9.306  -4.314  2.998   0.30 18.87 ?  155 VAL   A HG11 1 
ATOM   3540 H HG12 A VAL   A 1 155 ? 9.344  -2.860  3.594   0.26 17.20 ?  155 VAL   A HG12 1 
ATOM   3541 H HG12 B VAL   A 1 155 ? 9.271  -3.301  3.651   0.44 18.02 ?  155 VAL   A HG12 1 
ATOM   3542 H HG12 T VAL   A 1 155 ? 9.301  -2.883  3.686   0.30 18.87 ?  155 VAL   A HG12 1 
ATOM   3543 H HG13 A VAL   A 1 155 ? 10.601 -3.322  2.739   0.26 17.20 ?  155 VAL   A HG13 1 
ATOM   3544 H HG13 B VAL   A 1 155 ? 10.587 -3.504  2.783   0.44 18.02 ?  155 VAL   A HG13 1 
ATOM   3545 H HG13 T VAL   A 1 155 ? 10.546 -3.340  2.810   0.30 18.87 ?  155 VAL   A HG13 1 
ATOM   3546 H HG21 A VAL   A 1 155 ? 10.646 -6.076  3.889   0.26 16.97 ?  155 VAL   A HG21 1 
ATOM   3547 H HG21 B VAL   A 1 155 ? 10.906 -6.333  3.907   0.44 18.79 ?  155 VAL   A HG21 1 
ATOM   3548 H HG21 T VAL   A 1 155 ? 10.465 -6.173  3.969   0.30 18.48 ?  155 VAL   A HG21 1 
ATOM   3549 H HG22 A VAL   A 1 155 ? 12.034 -5.315  3.759   0.26 16.97 ?  155 VAL   A HG22 1 
ATOM   3550 H HG22 B VAL   A 1 155 ? 12.211 -5.455  3.687   0.44 18.79 ?  155 VAL   A HG22 1 
ATOM   3551 H HG22 T VAL   A 1 155 ? 11.847 -5.448  3.672   0.30 18.48 ?  155 VAL   A HG22 1 
ATOM   3552 H HG23 A VAL   A 1 155 ? 11.562 -5.868  5.171   0.26 16.97 ?  155 VAL   A HG23 1 
ATOM   3553 H HG23 B VAL   A 1 155 ? 11.875 -6.029  5.130   0.44 18.79 ?  155 VAL   A HG23 1 
ATOM   3554 H HG23 T VAL   A 1 155 ? 11.518 -5.960  5.140   0.30 18.48 ?  155 VAL   A HG23 1 
ATOM   3555 N N    A PHE   A 1 156 ? 11.336 -0.727  5.027   0.26 15.10 ?  156 PHE   A N    1 
ATOM   3556 N N    B PHE   A 1 156 ? 11.380 -0.939  4.777   0.44 15.75 ?  156 PHE   A N    1 
ATOM   3557 N N    T PHE   A 1 156 ? 11.432 -0.871  4.835   0.30 15.50 ?  156 PHE   A N    1 
ATOM   3558 C CA   A PHE   A 1 156 ? 10.791 0.569   5.423   0.26 15.94 ?  156 PHE   A CA   1 
ATOM   3559 C CA   B PHE   A 1 156 ? 10.866 0.405   5.049   0.44 17.13 ?  156 PHE   A CA   1 
ATOM   3560 C CA   T PHE   A 1 156 ? 11.023 0.503   5.122   0.30 15.82 ?  156 PHE   A CA   1 
ATOM   3561 C C    A PHE   A 1 156 ? 9.334  0.722   4.997   0.26 15.93 ?  156 PHE   A C    1 
ATOM   3562 C C    B PHE   A 1 156 ? 9.417  0.563   4.591   0.44 17.48 ?  156 PHE   A C    1 
ATOM   3563 C C    T PHE   A 1 156 ? 9.562  0.734   4.762   0.30 16.26 ?  156 PHE   A C    1 
ATOM   3564 O O    A PHE   A 1 156 ? 8.506  1.229   5.765   0.26 16.29 ?  156 PHE   A O    1 
ATOM   3565 O O    B PHE   A 1 156 ? 8.577  1.105   5.321   0.44 18.03 ?  156 PHE   A O    1 
ATOM   3566 O O    T PHE   A 1 156 ? 8.806  1.344   5.529   0.30 16.94 ?  156 PHE   A O    1 
ATOM   3567 C CB   A PHE   A 1 156 ? 11.645 1.695   4.838   0.26 16.81 ?  156 PHE   A CB   1 
ATOM   3568 C CB   B PHE   A 1 156 ? 11.773 1.417   4.342   0.44 18.25 ?  156 PHE   A CB   1 
ATOM   3569 C CB   T PHE   A 1 156 ? 11.913 1.470   4.337   0.30 15.46 ?  156 PHE   A CB   1 
ATOM   3570 C CG   A PHE   A 1 156 ? 11.113 3.069   5.129   0.26 17.75 ?  156 PHE   A CG   1 
ATOM   3571 C CG   B PHE   A 1 156 ? 11.501 2.861   4.691   0.44 20.11 ?  156 PHE   A CG   1 
ATOM   3572 C CG   T PHE   A 1 156 ? 11.525 2.921   4.487   0.30 15.20 ?  156 PHE   A CG   1 
ATOM   3573 C CD1  A PHE   A 1 156 ? 11.028 3.523   6.433   0.26 17.72 ?  156 PHE   A CD1  1 
ATOM   3574 C CD1  B PHE   A 1 156 ? 11.821 3.362   5.946   0.44 21.04 ?  156 PHE   A CD1  1 
ATOM   3575 C CD1  T PHE   A 1 156 ? 11.904 3.634   5.615   0.30 15.56 ?  156 PHE   A CD1  1 
ATOM   3576 C CD2  A PHE   A 1 156 ? 10.704 3.908   4.103   0.26 18.35 ?  156 PHE   A CD2  1 
ATOM   3577 C CD2  B PHE   A 1 156 ? 10.973 3.729   3.748   0.44 21.23 ?  156 PHE   A CD2  1 
ATOM   3578 C CD2  T PHE   A 1 156 ? 10.801 3.575   3.498   0.30 15.86 ?  156 PHE   A CD2  1 
ATOM   3579 C CE1  A PHE   A 1 156 ? 10.542 4.784   6.711   0.26 18.01 ?  156 PHE   A CE1  1 
ATOM   3580 C CE1  B PHE   A 1 156 ? 11.590 4.693   6.263   0.44 21.82 ?  156 PHE   A CE1  1 
ATOM   3581 C CE1  T PHE   A 1 156 ? 11.560 4.966   5.762   0.30 16.21 ?  156 PHE   A CE1  1 
ATOM   3582 C CE2  A PHE   A 1 156 ? 10.213 5.172   4.376   0.26 18.66 ?  156 PHE   A CE2  1 
ATOM   3583 C CE2  B PHE   A 1 156 ? 10.741 5.061   4.057   0.44 21.89 ?  156 PHE   A CE2  1 
ATOM   3584 C CE2  T PHE   A 1 156 ? 10.453 4.908   3.640   0.30 16.52 ?  156 PHE   A CE2  1 
ATOM   3585 C CZ   A PHE   A 1 156 ? 10.136 5.611   5.682   0.26 18.49 ?  156 PHE   A CZ   1 
ATOM   3586 C CZ   B PHE   A 1 156 ? 11.051 5.544   5.316   0.44 21.94 ?  156 PHE   A CZ   1 
ATOM   3587 C CZ   T PHE   A 1 156 ? 10.835 5.605   4.776   0.30 16.52 ?  156 PHE   A CZ   1 
ATOM   3588 H H    A PHE   A 1 156 ? 11.949 -0.691  4.424   0.26 18.15 ?  156 PHE   A H    1 
ATOM   3589 H H    B PHE   A 1 156 ? 12.009 -0.958  4.196   0.44 18.92 ?  156 PHE   A H    1 
ATOM   3590 H H    T PHE   A 1 156 ? 11.970 -0.949  4.169   0.30 18.62 ?  156 PHE   A H    1 
ATOM   3591 H HA   A PHE   A 1 156 ? 10.827 0.647   6.388   0.26 19.15 ?  156 PHE   A HA   1 
ATOM   3592 H HA   B PHE   A 1 156 ? 10.903 0.579   6.003   0.44 20.58 ?  156 PHE   A HA   1 
ATOM   3593 H HA   T PHE   A 1 156 ? 11.138 0.684   6.067   0.30 19.00 ?  156 PHE   A HA   1 
ATOM   3594 H HB2  A PHE   A 1 156 ? 12.541 1.639   5.212   0.26 20.19 ?  156 PHE   A HB2  1 
ATOM   3595 H HB2  B PHE   A 1 156 ? 12.693 1.229   4.581   0.44 21.92 ?  156 PHE   A HB2  1 
ATOM   3596 H HB2  T PHE   A 1 156 ? 12.826 1.374   4.648   0.30 18.57 ?  156 PHE   A HB2  1 
ATOM   3597 H HB3  A PHE   A 1 156 ? 11.688 1.592   3.875   0.26 20.19 ?  156 PHE   A HB3  1 
ATOM   3598 H HB3  B PHE   A 1 156 ? 11.658 1.323   3.385   0.44 21.92 ?  156 PHE   A HB3  1 
ATOM   3599 H HB3  T PHE   A 1 156 ? 11.860 1.247   3.395   0.30 18.57 ?  156 PHE   A HB3  1 
ATOM   3600 H HD1  A PHE   A 1 156 ? 11.302 2.972   7.130   0.26 21.28 ?  156 PHE   A HD1  1 
ATOM   3601 H HD1  B PHE   A 1 156 ? 12.182 2.796   6.588   0.44 25.27 ?  156 PHE   A HD1  1 
ATOM   3602 H HD1  T PHE   A 1 156 ? 12.389 3.206   6.287   0.30 18.69 ?  156 PHE   A HD1  1 
ATOM   3603 H HD2  A PHE   A 1 156 ? 10.759 3.614   3.222   0.26 22.04 ?  156 PHE   A HD2  1 
ATOM   3604 H HD2  B PHE   A 1 156 ? 10.760 3.412   2.901   0.44 25.49 ?  156 PHE   A HD2  1 
ATOM   3605 H HD2  T PHE   A 1 156 ? 10.542 3.111   2.738   0.30 19.05 ?  156 PHE   A HD2  1 
ATOM   3606 H HE1  A PHE   A 1 156 ? 10.490 5.078   7.593   0.26 21.63 ?  156 PHE   A HE1  1 
ATOM   3607 H HE1  B PHE   A 1 156 ? 11.800 5.015   7.112   0.44 26.21 ?  156 PHE   A HE1  1 
ATOM   3608 H HE1  T PHE   A 1 156 ? 11.814 5.428   6.531   0.30 19.48 ?  156 PHE   A HE1  1 
ATOM   3609 H HE2  A PHE   A 1 156 ? 9.944  5.726   3.680   0.26 22.42 ?  156 PHE   A HE2  1 
ATOM   3610 H HE2  B PHE   A 1 156 ? 10.375 5.630   3.418   0.44 26.29 ?  156 PHE   A HE2  1 
ATOM   3611 H HE2  T PHE   A 1 156 ? 9.964  5.335   2.977   0.30 19.85 ?  156 PHE   A HE2  1 
ATOM   3612 H HZ   A PHE   A 1 156 ? 9.808  6.461   5.870   0.26 22.21 ?  156 PHE   A HZ   1 
ATOM   3613 H HZ   B PHE   A 1 156 ? 10.892 6.438   5.526   0.44 26.35 ?  156 PHE   A HZ   1 
ATOM   3614 H HZ   T PHE   A 1 156 ? 10.601 6.499   4.877   0.30 19.85 ?  156 PHE   A HZ   1 
ATOM   3615 N N    A ASP   A 1 157 ? 9.003  0.299   3.782   0.26 15.44 ?  157 ASP   A N    1 
ATOM   3616 N N    B ASP   A 1 157 ? 9.107  0.102   3.385   0.44 17.62 ?  157 ASP   A N    1 
ATOM   3617 N N    T ASP   A 1 157 ? 9.155  0.270   3.589   0.30 16.05 ?  157 ASP   A N    1 
ATOM   3618 C CA   A ASP   A 1 157 ? 7.675  0.527   3.225   0.26 16.24 ?  157 ASP   A CA   1 
ATOM   3619 C CA   B ASP   A 1 157 ? 7.841  0.421   2.735   0.44 17.95 ?  157 ASP   A CA   1 
ATOM   3620 C CA   T ASP   A 1 157 ? 7.840  0.565   3.043   0.30 16.31 ?  157 ASP   A CA   1 
ATOM   3621 C C    A ASP   A 1 157 ? 6.710  -0.525  3.764   0.26 16.60 ?  157 ASP   A C    1 
ATOM   3622 C C    B ASP   A 1 157 ? 6.743  -0.538  3.192   0.44 18.25 ?  157 ASP   A C    1 
ATOM   3623 C C    T ASP   A 1 157 ? 6.821  -0.414  3.615   0.30 16.95 ?  157 ASP   A C    1 
ATOM   3624 O O    A ASP   A 1 157 ? 6.900  -1.726  3.539   0.26 16.47 ?  157 ASP   A O    1 
ATOM   3625 O O    B ASP   A 1 157 ? 6.846  -1.754  2.995   0.44 17.99 ?  157 ASP   A O    1 
ATOM   3626 O O    T ASP   A 1 157 ? 6.939  -1.629  3.416   0.30 16.93 ?  157 ASP   A O    1 
ATOM   3627 C CB   A ASP   A 1 157 ? 7.753  0.463   1.701   0.26 17.03 ?  157 ASP   A CB   1 
ATOM   3628 C CB   B ASP   A 1 157 ? 8.038  0.352   1.225   0.44 18.52 ?  157 ASP   A CB   1 
ATOM   3629 C CB   T ASP   A 1 157 ? 7.914  0.433   1.526   0.30 16.13 ?  157 ASP   A CB   1 
ATOM   3630 C CG   A ASP   A 1 157 ? 6.477  0.921   1.025   0.26 18.22 ?  157 ASP   A CG   1 
ATOM   3631 C CG   B ASP   A 1 157 ? 6.865  0.897   0.457   0.44 19.12 ?  157 ASP   A CG   1 
ATOM   3632 C CG   T ASP   A 1 157 ? 6.744  1.069   0.838   0.30 15.98 ?  157 ASP   A CG   1 
ATOM   3633 O OD1  A ASP   A 1 157 ? 6.093  2.096   1.195   0.26 18.52 ?  157 ASP   A OD1  1 
ATOM   3634 O OD1  B ASP   A 1 157 ? 5.801  0.245   0.462   0.44 19.91 ?  157 ASP   A OD1  1 
ATOM   3635 O OD1  T ASP   A 1 157 ? 5.667  0.440   0.817   0.30 16.87 ?  157 ASP   A OD1  1 
ATOM   3636 O OD2  A ASP   A 1 157 ? 5.856  0.104   0.312   0.26 18.80 -1 157 ASP   A OD2  1 
ATOM   3637 O OD2  B ASP   A 1 157 ? 7.003  1.980   -0.147  0.44 19.67 -1 157 ASP   A OD2  1 
ATOM   3638 O OD2  T ASP   A 1 157 ? 6.882  2.207   0.349   0.30 15.52 -1 157 ASP   A OD2  1 
ATOM   3639 H H    A ASP   A 1 157 ? 9.537  -0.127  3.256   0.26 18.55 ?  157 ASP   A H    1 
ATOM   3640 H H    B ASP   A 1 157 ? 9.623  -0.399  2.916   0.44 21.17 ?  157 ASP   A H    1 
ATOM   3641 H H    T ASP   A 1 157 ? 9.633  -0.225  3.080   0.30 19.28 ?  157 ASP   A H    1 
ATOM   3642 H HA   A ASP   A 1 157 ? 7.360  1.408   3.483   0.26 19.51 ?  157 ASP   A HA   1 
ATOM   3643 H HA   B ASP   A 1 157 ? 7.578  1.324   2.975   0.44 21.57 ?  157 ASP   A HA   1 
ATOM   3644 H HA   T ASP   A 1 157 ? 7.577  1.479   3.262   0.30 19.59 ?  157 ASP   A HA   1 
ATOM   3645 H HB2  A ASP   A 1 157 ? 8.496  1.009   1.400   0.26 20.46 ?  157 ASP   A HB2  1 
ATOM   3646 H HB2  B ASP   A 1 157 ? 8.820  0.869   0.987   0.44 22.24 ?  157 ASP   A HB2  1 
ATOM   3647 H HB2  T ASP   A 1 157 ? 8.733  0.842   1.204   0.30 19.38 ?  157 ASP   A HB2  1 
ATOM   3648 H HB3  A ASP   A 1 157 ? 7.893  -0.451  1.431   0.26 20.46 ?  157 ASP   A HB3  1 
ATOM   3649 H HB3  B ASP   A 1 157 ? 8.156  -0.574  0.967   0.44 22.24 ?  157 ASP   A HB3  1 
ATOM   3650 H HB3  T ASP   A 1 157 ? 7.914  -0.511  1.294   0.30 19.38 ?  157 ASP   A HB3  1 
ATOM   3651 N N    A LYS   A 1 158 ? 5.673  -0.075  4.478   0.26 17.52 ?  158 LYS   A N    1 
ATOM   3652 N N    B LYS   A 1 158 ? 5.679  0.023   3.777   0.44 19.12 ?  158 LYS   A N    1 
ATOM   3653 N N    T LYS   A 1 158 ? 5.816  0.110   4.321   0.30 17.78 ?  158 LYS   A N    1 
ATOM   3654 C CA   A LYS   A 1 158 ? 4.701  -1.011  5.035   0.26 18.47 ?  158 LYS   A CA   1 
ATOM   3655 C CA   B LYS   A 1 158 ? 4.610  -0.791  4.351   0.44 20.12 ?  158 LYS   A CA   1 
ATOM   3656 C CA   T LYS   A 1 158 ? 4.822  -0.768  4.931   0.30 18.60 ?  158 LYS   A CA   1 
ATOM   3657 C C    A LYS   A 1 158 ? 3.946  -1.740  3.933   0.26 18.14 ?  158 LYS   A C    1 
ATOM   3658 C C    B LYS   A 1 158 ? 3.944  -1.657  3.288   0.44 19.45 ?  158 LYS   A C    1 
ATOM   3659 C C    T LYS   A 1 158 ? 4.052  -1.550  3.877   0.30 18.05 ?  158 LYS   A C    1 
ATOM   3660 O O    A LYS   A 1 158 ? 3.749  -2.958  4.009   0.26 18.41 ?  158 LYS   A O    1 
ATOM   3661 O O    B LYS   A 1 158 ? 3.740  -2.860  3.486   0.44 19.27 ?  158 LYS   A O    1 
ATOM   3662 O O    T LYS   A 1 158 ? 3.807  -2.751  4.044   0.30 18.13 ?  158 LYS   A O    1 
ATOM   3663 C CB   A LYS   A 1 158 ? 3.731  -0.278  5.963   0.26 19.99 ?  158 LYS   A CB   1 
ATOM   3664 C CB   B LYS   A 1 158 ? 3.590  0.121   5.041   0.44 21.87 ?  158 LYS   A CB   1 
ATOM   3665 C CB   T LYS   A 1 158 ? 3.862  0.033   5.811   0.30 20.19 ?  158 LYS   A CB   1 
ATOM   3666 C CG   A LYS   A 1 158 ? 2.501  -1.086  6.377   0.26 21.40 ?  158 LYS   A CG   1 
ATOM   3667 C CG   B LYS   A 1 158 ? 2.226  -0.511  5.298   0.44 24.17 ?  158 LYS   A CG   1 
ATOM   3668 C CG   T LYS   A 1 158 ? 2.635  -0.754  6.271   0.30 21.76 ?  158 LYS   A CG   1 
ATOM   3669 C CD   A LYS   A 1 158 ? 2.860  -2.353  7.153   0.26 22.35 ?  158 LYS   A CD   1 
ATOM   3670 C CD   B LYS   A 1 158 ? 2.309  -1.707  6.227   0.44 26.04 ?  158 LYS   A CD   1 
ATOM   3671 C CD   T LYS   A 1 158 ? 3.009  -1.996  7.083   0.30 23.36 ?  158 LYS   A CD   1 
ATOM   3672 C CE   A LYS   A 1 158 ? 1.603  -3.035  7.687   0.26 22.63 ?  158 LYS   A CE   1 
ATOM   3673 C CE   B LYS   A 1 158 ? 0.933  -2.319  6.456   0.44 27.23 ?  158 LYS   A CE   1 
ATOM   3674 C CE   T LYS   A 1 158 ? 1.762  -2.768  7.514   0.30 24.46 ?  158 LYS   A CE   1 
ATOM   3675 N NZ   A LYS   A 1 158 ? 1.875  -4.376  8.281   0.26 22.62 ?  158 LYS   A NZ   1 
ATOM   3676 N NZ   B LYS   A 1 158 ? 1.012  -3.606  7.202   0.44 27.77 ?  158 LYS   A NZ   1 
ATOM   3677 N NZ   T LYS   A 1 158 ? 2.076  -4.012  8.278   0.30 25.05 ?  158 LYS   A NZ   1 
ATOM   3678 H H    A LYS   A 1 158 ? 5.515  0.753   4.646   0.26 21.05 ?  158 LYS   A H    1 
ATOM   3679 H H    B LYS   A 1 158 ? 5.551  0.870   3.844   0.44 22.97 ?  158 LYS   A H    1 
ATOM   3680 H H    T LYS   A 1 158 ? 5.695  0.951   4.457   0.30 21.35 ?  158 LYS   A H    1 
ATOM   3681 H HA   A LYS   A 1 158 ? 5.170  -1.675  5.559   0.26 22.19 ?  158 LYS   A HA   1 
ATOM   3682 H HA   B LYS   A 1 158 ? 4.984  -1.379  5.026   0.44 24.17 ?  158 LYS   A HA   1 
ATOM   3683 H HA   T LYS   A 1 158 ? 5.281  -1.406  5.495   0.30 22.34 ?  158 LYS   A HA   1 
ATOM   3684 H HB2  A LYS   A 1 158 ? 4.205  -0.034  6.773   0.26 24.01 ?  158 LYS   A HB2  1 
ATOM   3685 H HB2  B LYS   A 1 158 ? 3.949  0.396   5.902   0.44 26.27 ?  158 LYS   A HB2  1 
ATOM   3686 H HB2  T LYS   A 1 158 ? 4.340  0.323   6.604   0.30 24.25 ?  158 LYS   A HB2  1 
ATOM   3687 H HB3  A LYS   A 1 158 ? 3.418  0.521   5.515   0.26 24.01 ?  158 LYS   A HB3  1 
ATOM   3688 H HB3  B LYS   A 1 158 ? 3.449  0.906   4.487   0.44 26.27 ?  158 LYS   A HB3  1 
ATOM   3689 H HB3  T LYS   A 1 158 ? 3.551  0.803   5.313   0.30 24.25 ?  158 LYS   A HB3  1 
ATOM   3690 H HG2  A LYS   A 1 158 ? 1.947  -0.537  6.952   0.26 25.70 ?  158 LYS   A HG2  1 
ATOM   3691 H HG2  B LYS   A 1 158 ? 1.655  0.150   5.716   0.44 29.03 ?  158 LYS   A HG2  1 
ATOM   3692 H HG2  T LYS   A 1 158 ? 2.094  -0.185  6.837   0.30 26.14 ?  158 LYS   A HG2  1 
ATOM   3693 H HG3  A LYS   A 1 158 ? 1.995  -1.346  5.590   0.26 25.70 ?  158 LYS   A HG3  1 
ATOM   3694 H HG3  B LYS   A 1 158 ? 1.831  -0.797  4.458   0.44 29.03 ?  158 LYS   A HG3  1 
ATOM   3695 H HG3  T LYS   A 1 158 ? 2.116  -1.039  5.501   0.30 26.14 ?  158 LYS   A HG3  1 
ATOM   3696 H HD2  A LYS   A 1 158 ? 3.318  -2.974  6.567   0.26 26.84 ?  158 LYS   A HD2  1 
ATOM   3697 H HD2  B LYS   A 1 158 ? 2.883  -2.383  5.836   0.44 31.27 ?  158 LYS   A HD2  1 
ATOM   3698 H HD2  T LYS   A 1 158 ? 3.557  -2.587  6.544   0.30 28.06 ?  158 LYS   A HD2  1 
ATOM   3699 H HD3  A LYS   A 1 158 ? 3.424  -2.119  7.907   0.26 26.84 ?  158 LYS   A HD3  1 
ATOM   3700 H HD3  B LYS   A 1 158 ? 2.661  -1.422  7.086   0.44 31.27 ?  158 LYS   A HD3  1 
ATOM   3701 H HD3  T LYS   A 1 158 ? 3.489  -1.726  7.882   0.30 28.06 ?  158 LYS   A HD3  1 
ATOM   3702 H HE2  A LYS   A 1 158 ? 1.208  -2.477  8.376   0.26 27.17 ?  158 LYS   A HE2  1 
ATOM   3703 H HE2  B LYS   A 1 158 ? 0.397  -1.703  6.977   0.44 32.69 ?  158 LYS   A HE2  1 
ATOM   3704 H HE2  T LYS   A 1 158 ? 1.216  -2.201  8.081   0.30 29.38 ?  158 LYS   A HE2  1 
ATOM   3705 H HE3  A LYS   A 1 158 ? 0.975  -3.154  6.959   0.26 27.17 ?  158 LYS   A HE3  1 
ATOM   3706 H HE3  B LYS   A 1 158 ? 0.509  -2.482  5.599   0.44 32.69 ?  158 LYS   A HE3  1 
ATOM   3707 H HE3  T LYS   A 1 158 ? 1.261  -3.025  6.725   0.30 29.38 ?  158 LYS   A HE3  1 
ATOM   3708 H HZ1  A LYS   A 1 158 ? 1.117  -4.737  8.577   0.26 27.16 ?  158 LYS   A HZ1  1 
ATOM   3709 H HZ1  B LYS   A 1 158 ? 0.194  -3.882  7.418   0.44 33.35 ?  158 LYS   A HZ1  1 
ATOM   3710 H HZ1  T LYS   A 1 158 ? 1.323  -4.428  8.507   0.30 30.08 ?  158 LYS   A HZ1  1 
ATOM   3711 H HZ2  A LYS   A 1 158 ? 2.232  -4.913  7.668   0.26 27.16 ?  158 LYS   A HZ2  1 
ATOM   3712 H HZ2  B LYS   A 1 158 ? 1.405  -4.226  6.700   0.44 33.35 ?  158 LYS   A HZ2  1 
ATOM   3713 H HZ2  T LYS   A 1 158 ? 2.567  -4.561  7.777   0.30 30.08 ?  158 LYS   A HZ2  1 
ATOM   3714 H HZ3  A LYS   A 1 158 ? 2.442  -4.298  8.963   0.26 27.16 ?  158 LYS   A HZ3  1 
ATOM   3715 H HZ3  B LYS   A 1 158 ? 1.485  -3.496  7.949   0.44 33.35 ?  158 LYS   A HZ3  1 
ATOM   3716 H HZ3  T LYS   A 1 158 ? 2.531  -3.810  9.016   0.30 30.08 ?  158 LYS   A HZ3  1 
ATOM   3717 N N    A ASN   A 1 159 ? 3.508  -1.014  2.902   0.26 17.77 ?  159 ASN   A N    1 
ATOM   3718 N N    B ASN   A 1 159 ? 3.587  -1.061  2.149   0.44 19.48 ?  159 ASN   A N    1 
ATOM   3719 N N    T ASN   A 1 159 ? 3.647  -0.892  2.796   0.30 18.03 ?  159 ASN   A N    1 
ATOM   3720 C CA   A ASN   A 1 159 ? 2.847  -1.677  1.786   0.26 17.31 ?  159 ASN   A CA   1 
ATOM   3721 C CA   B ASN   A 1 159 ? 2.895  -1.826  1.116   0.44 20.17 ?  159 ASN   A CA   1 
ATOM   3722 C CA   T ASN   A 1 159 ? 2.912  -1.582  1.743   0.30 18.35 ?  159 ASN   A CA   1 
ATOM   3723 C C    A ASN   A 1 159 ? 3.763  -2.720  1.162   0.26 16.09 ?  159 ASN   A C    1 
ATOM   3724 C C    B ASN   A 1 159 ? 3.769  -2.966  0.598   0.44 19.57 ?  159 ASN   A C    1 
ATOM   3725 C C    T ASN   A 1 159 ? 3.757  -2.686  1.118   0.30 18.35 ?  159 ASN   A C    1 
ATOM   3726 O O    A ASN   A 1 159 ? 3.337  -3.849  0.892   0.26 14.76 ?  159 ASN   A O    1 
ATOM   3727 O O    B ASN   A 1 159 ? 3.280  -4.069  0.333   0.44 19.80 ?  159 ASN   A O    1 
ATOM   3728 O O    T ASN   A 1 159 ? 3.243  -3.752  0.788   0.30 17.75 ?  159 ASN   A O    1 
ATOM   3729 C CB   A ASN   A 1 159 ? 2.367  -0.651  0.756   0.26 18.37 ?  159 ASN   A CB   1 
ATOM   3730 C CB   B ASN   A 1 159 ? 2.443  -0.894  -0.013  0.44 21.61 ?  159 ASN   A CB   1 
ATOM   3731 C CB   T ASN   A 1 159 ? 2.402  -0.597  0.684   0.30 19.08 ?  159 ASN   A CB   1 
ATOM   3732 C CG   A ASN   A 1 159 ? 1.103  0.071   1.197   0.26 19.60 ?  159 ASN   A CG   1 
ATOM   3733 C CG   B ASN   A 1 159 ? 1.419  0.140   0.452   0.44 23.23 ?  159 ASN   A CG   1 
ATOM   3734 C CG   T ASN   A 1 159 ? 1.134  0.124   1.121   0.30 20.00 ?  159 ASN   A CG   1 
ATOM   3735 O OD1  A ASN   A 1 159 ? 0.265  -0.499  1.898   0.26 20.33 ?  159 ASN   A OD1  1 
ATOM   3736 O OD1  B ASN   A 1 159 ? 0.670  -0.091  1.403   0.44 24.27 ?  159 ASN   A OD1  1 
ATOM   3737 O OD1  T ASN   A 1 159 ? 0.332  -0.419  1.883   0.30 20.75 ?  159 ASN   A OD1  1 
ATOM   3738 N ND2  A ASN   A 1 159 ? 0.958  1.325   0.786   0.26 19.80 ?  159 ASN   A ND2  1 
ATOM   3739 N ND2  B ASN   A 1 159 ? 1.380  1.284   -0.225  0.44 23.77 ?  159 ASN   A ND2  1 
ATOM   3740 N ND2  T ASN   A 1 159 ? 0.944  1.346   0.638   0.30 19.99 ?  159 ASN   A ND2  1 
ATOM   3741 H H    A ASN   A 1 159 ? 3.585  -0.163  2.822   0.26 21.34 ?  159 ASN   A H    1 
ATOM   3742 H H    B ASN   A 1 159 ? 3.739  -0.235  1.954   0.44 23.40 ?  159 ASN   A H    1 
ATOM   3743 H H    T ASN   A 1 159 ? 3.775  -0.054  2.652   0.30 21.66 ?  159 ASN   A H    1 
ATOM   3744 H HA   A ASN   A 1 159 ? 2.065  -2.144  2.115   0.26 20.80 ?  159 ASN   A HA   1 
ATOM   3745 H HA   B ASN   A 1 159 ? 2.098  -2.216  1.500   0.44 24.22 ?  159 ASN   A HA   1 
ATOM   3746 H HA   T ASN   A 1 159 ? 2.141  -2.011  2.134   0.30 22.04 ?  159 ASN   A HA   1 
ATOM   3747 H HB2  A ASN   A 1 159 ? 3.056  0.016   0.621   0.26 22.07 ?  159 ASN   A HB2  1 
ATOM   3748 H HB2  B ASN   A 1 159 ? 3.207  -0.409  -0.361  0.44 25.96 ?  159 ASN   A HB2  1 
ATOM   3749 H HB2  T ASN   A 1 159 ? 3.081  0.072   0.514   0.30 22.92 ?  159 ASN   A HB2  1 
ATOM   3750 H HB3  A ASN   A 1 159 ? 2.175  -1.103  -0.084  0.26 22.07 ?  159 ASN   A HB3  1 
ATOM   3751 H HB3  B ASN   A 1 159 ? 2.032  -1.417  -0.719  0.44 25.96 ?  159 ASN   A HB3  1 
ATOM   3752 H HB3  T ASN   A 1 159 ? 2.205  -1.085  -0.135  0.30 22.92 ?  159 ASN   A HB3  1 
ATOM   3753 H HD21 A ASN   A 1 159 ? 0.259  1.771   1.009   0.26 23.78 ?  159 ASN   A HD21 1 
ATOM   3754 H HD21 B ASN   A 1 159 ? 0.817  1.895   -0.001  0.44 28.55 ?  159 ASN   A HD21 1 
ATOM   3755 H HD21 T ASN   A 1 159 ? 0.240  1.788   0.856   0.30 24.01 ?  159 ASN   A HD21 1 
ATOM   3756 H HD22 A ASN   A 1 159 ? 1.565  1.689   0.300   0.26 23.78 ?  159 ASN   A HD22 1 
ATOM   3757 H HD22 B ASN   A 1 159 ? 1.914  1.412   -0.883  0.44 28.55 ?  159 ASN   A HD22 1 
ATOM   3758 H HD22 T ASN   A 1 159 ? 1.526  1.692   0.111   0.30 24.01 ?  159 ASN   A HD22 1 
ATOM   3759 N N    A LEU   A 1 160 ? 5.036  -2.383  0.961   0.26 15.88 ?  160 LEU   A N    1 
ATOM   3760 N N    B LEU   A 1 160 ? 5.075  -2.733  0.489   0.44 18.30 ?  160 LEU   A N    1 
ATOM   3761 N N    T LEU   A 1 160 ? 5.055  -2.454  0.975   0.30 18.86 ?  160 LEU   A N    1 
ATOM   3762 C CA   A LEU   A 1 160 ? 5.961  -3.391  0.458   0.26 15.35 ?  160 LEU   A CA   1 
ATOM   3763 C CA   B LEU   A 1 160 ? 5.969  -3.775  -0.004  0.44 17.39 ?  160 LEU   A CA   1 
ATOM   3764 C CA   T LEU   A 1 160 ? 5.931  -3.493  0.450   0.30 18.96 ?  160 LEU   A CA   1 
ATOM   3765 C C    A LEU   A 1 160 ? 6.121  -4.534  1.455   0.26 13.95 ?  160 LEU   A C    1 
ATOM   3766 C C    B LEU   A 1 160 ? 6.100  -4.912  1.000   0.44 16.24 ?  160 LEU   A C    1 
ATOM   3767 O O    A LEU   A 1 160 ? 6.135  -5.707  1.067   0.26 12.40 ?  160 LEU   A O    1 
ATOM   3768 O O    B LEU   A 1 160 ? 6.081  -6.088  0.622   0.44 16.26 ?  160 LEU   A O    1 
ATOM   3769 C CB   A LEU   A 1 160 ? 7.314  -2.772  0.113   0.26 16.27 ?  160 LEU   A CB   1 
ATOM   3770 C CB   B LEU   A 1 160 ? 7.338  -3.174  -0.292  0.44 17.27 ?  160 LEU   A CB   1 
ATOM   3771 C CB   T LEU   A 1 160 ? 7.281  -2.915  0.035   0.30 19.15 ?  160 LEU   A CB   1 
ATOM   3772 C CG   A LEU   A 1 160 ? 8.344  -3.796  -0.365  0.26 17.28 ?  160 LEU   A CG   1 
ATOM   3773 C CG   B LEU   A 1 160 ? 8.443  -4.184  -0.587  0.44 18.49 ?  160 LEU   A CG   1 
ATOM   3774 C CG   T LEU   A 1 160 ? 8.295  -3.948  -0.453  0.30 19.73 ?  160 LEU   A CG   1 
ATOM   3775 C CD1  A LEU   A 1 160 ? 7.821  -4.589  -1.553  0.26 17.71 ?  160 LEU   A CD1  1 
ATOM   3776 C CD1  B LEU   A 1 160 ? 8.087  -4.985  -1.816  0.44 18.98 ?  160 LEU   A CD1  1 
ATOM   3777 C CD1  T LEU   A 1 160 ? 7.776  -4.684  -1.675  0.30 20.13 ?  160 LEU   A CD1  1 
ATOM   3778 C CD2  A LEU   A 1 160 ? 9.647  -3.111  -0.710  0.26 17.40 ?  160 LEU   A CD2  1 
ATOM   3779 C CD2  B LEU   A 1 160 ? 9.772  -3.476  -0.762  0.44 19.09 ?  160 LEU   A CD2  1 
ATOM   3780 C CD2  T LEU   A 1 160 ? 9.608  -3.263  -0.758  0.30 19.68 ?  160 LEU   A CD2  1 
ATOM   3781 H H    A LEU   A 1 160 ? 5.379  -1.603  1.107   0.26 19.08 ?  160 LEU   A H    1 
ATOM   3782 H H    B LEU   A 1 160 ? 5.462  -2.000  0.711   0.44 21.98 ?  160 LEU   A H    1 
ATOM   3783 H H    T LEU   A 1 160 ? 5.453  -1.714  1.173   0.30 22.65 ?  160 LEU   A H    1 
ATOM   3784 H HA   A LEU   A 1 160 ? 5.595  -3.755  -0.359  0.26 18.44 ?  160 LEU   A HA   1 
ATOM   3785 H HA   B LEU   A 1 160 ? 5.614  -4.133  -0.831  0.44 20.89 ?  160 LEU   A HA   1 
ATOM   3786 H HB2  A LEU   A 1 160 ? 7.205  -2.096  -0.586  0.26 19.54 ?  160 LEU   A HB2  1 
ATOM   3787 H HB2  B LEU   A 1 160 ? 7.264  -2.588  -1.064  0.44 20.75 ?  160 LEU   A HB2  1 
ATOM   3788 H HB2  T LEU   A 1 160 ? 7.148  -2.265  -0.679  0.30 23.00 ?  160 LEU   A HB2  1 
ATOM   3789 H HB3  A LEU   A 1 160 ? 7.678  -2.366  0.910   0.26 19.54 ?  160 LEU   A HB3  1 
ATOM   3790 H HB3  B LEU   A 1 160 ? 7.615  -2.656  0.480   0.44 20.75 ?  160 LEU   A HB3  1 
ATOM   3791 H HB3  T LEU   A 1 160 ? 7.677  -2.481  0.804   0.30 23.00 ?  160 LEU   A HB3  1 
ATOM   3792 H HG   A LEU   A 1 160 ? 8.526  -4.419  0.356   0.26 20.76 ?  160 LEU   A HG   1 
ATOM   3793 H HG   B LEU   A 1 160 ? 8.533  -4.794  0.162   0.44 22.21 ?  160 LEU   A HG   1 
ATOM   3794 H HG   T LEU   A 1 160 ? 8.451  -4.597  0.252   0.30 23.69 ?  160 LEU   A HG   1 
ATOM   3795 H HD11 A LEU   A 1 160 ? 8.544  -5.121  -1.918  0.26 21.27 ?  160 LEU   A HD11 1 
ATOM   3796 H HD11 B LEU   A 1 160 ? 8.835  -5.550  -2.046  0.44 22.79 ?  160 LEU   A HD11 1 
ATOM   3797 H HD11 T LEU   A 1 160 ? 8.474  -5.271  -2.007  0.30 24.18 ?  160 LEU   A HD11 1 
ATOM   3798 H HD12 A LEU   A 1 160 ? 7.103  -5.171  -1.257  0.26 21.27 ?  160 LEU   A HD12 1 
ATOM   3799 H HD12 B LEU   A 1 160 ? 7.305  -5.525  -1.623  0.44 22.79 ?  160 LEU   A HD12 1 
ATOM   3800 H HD12 T LEU   A 1 160 ? 6.998  -5.205  -1.423  0.30 24.18 ?  160 LEU   A HD12 1 
ATOM   3801 H HD13 A LEU   A 1 160 ? 7.492  -3.972  -2.225  0.26 21.27 ?  160 LEU   A HD13 1 
ATOM   3802 H HD13 B LEU   A 1 160 ? 7.895  -4.371  -2.542  0.44 22.79 ?  160 LEU   A HD13 1 
ATOM   3803 H HD13 T LEU   A 1 160 ? 7.537  -4.036  -2.355  0.30 24.18 ?  160 LEU   A HD13 1 
ATOM   3804 H HD21 A LEU   A 1 160 ? 10.286 -3.781  -1.003  0.26 20.90 ?  160 LEU   A HD21 1 
ATOM   3805 H HD21 B LEU   A 1 160 ? 10.461 -4.135  -0.945  0.44 22.93 ?  160 LEU   A HD21 1 
ATOM   3806 H HD21 T LEU   A 1 160 ? 10.246 -3.926  -1.065  0.30 23.64 ?  160 LEU   A HD21 1 
ATOM   3807 H HD22 A LEU   A 1 160 ? 9.489  -2.471  -1.421  0.26 20.90 ?  160 LEU   A HD22 1 
ATOM   3808 H HD22 B LEU   A 1 160 ? 9.706  -2.853  -1.503  0.44 22.93 ?  160 LEU   A HD22 1 
ATOM   3809 H HD22 T LEU   A 1 160 ? 9.463  -2.598  -1.449  0.30 23.64 ?  160 LEU   A HD22 1 
ATOM   3810 H HD23 A LEU   A 1 160 ? 9.984  -2.656  0.078   0.26 20.90 ?  160 LEU   A HD23 1 
ATOM   3811 H HD23 B LEU   A 1 160 ? 9.988  -2.994  0.054   0.44 22.93 ?  160 LEU   A HD23 1 
ATOM   3812 H HD23 T LEU   A 1 160 ? 9.937  -2.836  0.049   0.30 23.64 ?  160 LEU   A HD23 1 
ATOM   3813 N N    A TYR   A 1 161 ? 6.238  -4.214  2.746   0.56 15.37 ?  161 TYR   A N    1 
ATOM   3814 N N    B TYR   A 1 161 ? 6.250  -4.578  2.280   0.44 15.79 ?  161 TYR   A N    1 
ATOM   3815 C CA   A TYR   A 1 161 ? 6.356  -5.266  3.751   0.56 15.66 ?  161 TYR   A CA   1 
ATOM   3816 C CA   B TYR   A 1 161 ? 6.340  -5.603  3.312   0.44 15.42 ?  161 TYR   A CA   1 
ATOM   3817 C C    A TYR   A 1 161 ? 5.205  -6.259  3.652   0.56 17.11 ?  161 TYR   A C    1 
ATOM   3818 C C    B TYR   A 1 161 ? 5.140  -6.535  3.245   0.44 16.35 ?  161 TYR   A C    1 
ATOM   3819 O O    A TYR   A 1 161 ? 5.417  -7.479  3.652   0.56 16.70 ?  161 TYR   A O    1 
ATOM   3820 O O    B TYR   A 1 161 ? 5.287  -7.764  3.239   0.44 15.65 ?  161 TYR   A O    1 
ATOM   3821 C CB   A TYR   A 1 161 ? 6.418  -4.671  5.160   0.56 16.02 ?  161 TYR   A CB   1 
ATOM   3822 C CB   B TYR   A 1 161 ? 6.430  -4.943  4.688   0.44 15.49 ?  161 TYR   A CB   1 
ATOM   3823 C CG   A TYR   A 1 161 ? 6.342  -5.744  6.223   0.56 15.85 ?  161 TYR   A CG   1 
ATOM   3824 C CG   B TYR   A 1 161 ? 6.318  -5.918  5.831   0.44 15.06 ?  161 TYR   A CG   1 
ATOM   3825 C CD1  A TYR   A 1 161 ? 7.479  -6.418  6.642   0.56 15.30 ?  161 TYR   A CD1  1 
ATOM   3826 C CD1  B TYR   A 1 161 ? 7.401  -6.693  6.215   0.44 15.26 ?  161 TYR   A CD1  1 
ATOM   3827 C CD2  A TYR   A 1 161 ? 5.125  -6.100  6.788   0.56 16.58 ?  161 TYR   A CD2  1 
ATOM   3828 C CD2  B TYR   A 1 161 ? 5.128  -6.059  6.532   0.44 15.62 ?  161 TYR   A CD2  1 
ATOM   3829 C CE1  A TYR   A 1 161 ? 7.408  -7.412  7.597   0.56 15.21 ?  161 TYR   A CE1  1 
ATOM   3830 C CE1  B TYR   A 1 161 ? 7.302  -7.590  7.261   0.44 14.72 ?  161 TYR   A CE1  1 
ATOM   3831 C CE2  A TYR   A 1 161 ? 5.044  -7.092  7.743   0.56 16.53 ?  161 TYR   A CE2  1 
ATOM   3832 C CE2  B TYR   A 1 161 ? 5.018  -6.950  7.580   0.44 15.24 ?  161 TYR   A CE2  1 
ATOM   3833 C CZ   A TYR   A 1 161 ? 6.187  -7.744  8.148   0.56 15.86 ?  161 TYR   A CZ   1 
ATOM   3834 C CZ   B TYR   A 1 161 ? 6.105  -7.714  7.940   0.44 15.06 ?  161 TYR   A CZ   1 
ATOM   3835 O OH   A TYR   A 1 161 ? 6.122  -8.739  9.100   0.56 16.85 ?  161 TYR   A OH   1 
ATOM   3836 O OH   B TYR   A 1 161 ? 6.004  -8.608  8.981   0.44 16.32 ?  161 TYR   A OH   1 
ATOM   3837 H H    A TYR   A 1 161 ? 6.260  -3.408  3.055   0.56 18.47 ?  161 TYR   A H    1 
ATOM   3838 H H    B TYR   A 1 161 ? 6.293  -3.776  2.574   0.44 18.97 ?  161 TYR   A H    1 
ATOM   3839 H HA   A TYR   A 1 161 ? 7.174  -5.753  3.598   0.56 18.81 ?  161 TYR   A HA   1 
ATOM   3840 H HA   B TYR   A 1 161 ? 7.138  -6.136  3.176   0.44 18.52 ?  161 TYR   A HA   1 
ATOM   3841 H HB2  A TYR   A 1 161 ? 7.259  -4.194  5.265   0.56 19.25 ?  161 TYR   A HB2  1 
ATOM   3842 H HB2  B TYR   A 1 161 ? 7.287  -4.494  4.762   0.44 18.61 ?  161 TYR   A HB2  1 
ATOM   3843 H HB3  A TYR   A 1 161 ? 5.673  -4.059  5.284   0.56 19.25 ?  161 TYR   A HB3  1 
ATOM   3844 H HB3  B TYR   A 1 161 ? 5.711  -4.296  4.774   0.44 18.61 ?  161 TYR   A HB3  1 
ATOM   3845 H HD1  A TYR   A 1 161 ? 8.304  -6.194  6.272   0.56 18.38 ?  161 TYR   A HD1  1 
ATOM   3846 H HD1  B TYR   A 1 161 ? 8.206  -6.613  5.757   0.44 18.33 ?  161 TYR   A HD1  1 
ATOM   3847 H HD2  A TYR   A 1 161 ? 4.346  -5.662  6.516   0.56 19.92 ?  161 TYR   A HD2  1 
ATOM   3848 H HD2  B TYR   A 1 161 ? 4.388  -5.544  6.296   0.44 18.77 ?  161 TYR   A HD2  1 
ATOM   3849 H HE1  A TYR   A 1 161 ? 8.180  -7.851  7.872   0.56 18.28 ?  161 TYR   A HE1  1 
ATOM   3850 H HE1  B TYR   A 1 161 ? 8.035  -8.109  7.508   0.44 17.69 ?  161 TYR   A HE1  1 
ATOM   3851 H HE2  A TYR   A 1 161 ? 4.217  -7.316  8.114   0.56 19.86 ?  161 TYR   A HE2  1 
ATOM   3852 H HE2  B TYR   A 1 161 ? 4.210  -7.037  8.046   0.44 18.31 ?  161 TYR   A HE2  1 
ATOM   3853 H HH   A TYR   A 1 161 ? 5.319  -8.837  9.349   0.56 20.25 ?  161 TYR   A HH   1 
ATOM   3854 H HH   B TYR   A 1 161 ? 5.225  -8.585  9.314   0.44 19.60 ?  161 TYR   A HH   1 
ATOM   3855 N N    A ASP   A 1 162 ? 3.970  -5.755  3.585   0.56 17.99 ?  162 ASP   A N    1 
ATOM   3856 N N    B ASP   A 1 162 ? 3.936  -5.956  3.209   0.44 17.20 ?  162 ASP   A N    1 
ATOM   3857 C CA   A ASP   A 1 162 ? 2.825  -6.660  3.535   0.56 18.06 ?  162 ASP   A CA   1 
ATOM   3858 C CA   B ASP   A 1 162 ? 2.723  -6.743  3.008   0.44 18.29 ?  162 ASP   A CA   1 
ATOM   3859 C C    A ASP   A 1 162 ? 2.862  -7.527  2.287   0.56 17.48 ?  162 ASP   A C    1 
ATOM   3860 C C    B ASP   A 1 162 ? 2.842  -7.601  1.755   0.44 18.05 ?  162 ASP   A C    1 
ATOM   3861 O O    A ASP   A 1 162 ? 2.532  -8.720  2.340   0.56 17.96 ?  162 ASP   A O    1 
ATOM   3862 O O    B ASP   A 1 162 ? 2.470  -8.782  1.756   0.44 17.93 ?  162 ASP   A O    1 
ATOM   3863 C CB   A ASP   A 1 162 ? 1.516  -5.878  3.597   0.56 18.58 ?  162 ASP   A CB   1 
ATOM   3864 C CB   B ASP   A 1 162 ? 1.512  -5.804  2.896   0.44 19.34 ?  162 ASP   A CB   1 
ATOM   3865 C CG   A ASP   A 1 162 ? 1.197  -5.379  4.977   0.56 20.08 ?  162 ASP   A CG   1 
ATOM   3866 C CG   B ASP   A 1 162 ? 1.201  -5.078  4.202   0.44 20.31 ?  162 ASP   A CG   1 
ATOM   3867 O OD1  A ASP   A 1 162 ? 1.835  -5.833  5.948   0.56 20.76 ?  162 ASP   A OD1  1 
ATOM   3868 O OD1  B ASP   A 1 162 ? 1.750  -5.467  5.253   0.44 20.52 ?  162 ASP   A OD1  1 
ATOM   3869 O OD2  A ASP   A 1 162 ? 0.296  -4.526  5.079   0.56 20.99 -1 162 ASP   A OD2  1 
ATOM   3870 O OD2  B ASP   A 1 162 ? 0.392  -4.124  4.175   0.44 21.06 -1 162 ASP   A OD2  1 
ATOM   3871 H H    A ASP   A 1 162 ? 3.769  -4.907  3.569   0.56 21.61 ?  162 ASP   A H    1 
ATOM   3872 H H    B ASP   A 1 162 ? 3.797  -5.109  3.303   0.44 20.66 ?  162 ASP   A H    1 
ATOM   3873 H HA   A ASP   A 1 162 ? 2.859  -7.245  4.299   0.56 21.70 ?  162 ASP   A HA   1 
ATOM   3874 H HA   B ASP   A 1 162 ? 2.573  -7.320  3.772   0.44 21.97 ?  162 ASP   A HA   1 
ATOM   3875 H HB2  A ASP   A 1 162 ? 1.569  -5.098  3.031   0.56 22.32 ?  162 ASP   A HB2  1 
ATOM   3876 H HB2  B ASP   A 1 162 ? 1.677  -5.139  2.203   0.44 23.24 ?  162 ASP   A HB2  1 
ATOM   3877 H HB3  A ASP   A 1 162 ? 0.786  -6.452  3.314   0.56 22.32 ?  162 ASP   A HB3  1 
ATOM   3878 H HB3  B ASP   A 1 162 ? 0.719  -6.315  2.672   0.44 23.24 ?  162 ASP   A HB3  1 
ATOM   3879 N N    A LYS   A 1 163 ? 3.237  -6.944  1.146   0.56 18.11 ?  163 LYS   A N    1 
ATOM   3880 N N    B LYS   A 1 163 ? 3.371  -7.021  0.676   0.44 18.83 ?  163 LYS   A N    1 
ATOM   3881 C CA   A LYS   A 1 163 ? 3.330  -7.745  -0.069  0.56 18.81 ?  163 LYS   A CA   1 
ATOM   3882 C CA   B LYS   A 1 163 ? 3.480  -7.745  -0.586  0.44 19.31 ?  163 LYS   A CA   1 
ATOM   3883 C C    A LYS   A 1 163 ? 4.437  -8.788  0.048   0.56 17.97 ?  163 LYS   A C    1 
ATOM   3884 C C    B LYS   A 1 163 ? 4.466  -8.911  -0.487  0.44 17.96 ?  163 LYS   A C    1 
ATOM   3885 O O    A LYS   A 1 163 ? 4.285  -9.922  -0.419  0.56 17.58 ?  163 LYS   A O    1 
ATOM   3886 O O    B LYS   A 1 163 ? 4.228  -9.982  -1.056  0.44 18.18 ?  163 LYS   A O    1 
ATOM   3887 C CB   A LYS   A 1 163 ? 3.545  -6.844  -1.287  0.56 21.24 ?  163 LYS   A CB   1 
ATOM   3888 C CB   B LYS   A 1 163 ? 3.885  -6.767  -1.694  0.44 21.57 ?  163 LYS   A CB   1 
ATOM   3889 C CG   A LYS   A 1 163 ? 3.700  -7.615  -2.588  0.56 24.00 ?  163 LYS   A CG   1 
ATOM   3890 C CG   B LYS   A 1 163 ? 3.981  -7.386  -3.074  0.44 23.85 ?  163 LYS   A CG   1 
ATOM   3891 C CD   A LYS   A 1 163 ? 4.031  -6.698  -3.748  0.56 26.85 ?  163 LYS   A CD   1 
ATOM   3892 C CD   B LYS   A 1 163 ? 4.458  -6.367  -4.099  0.44 25.80 ?  163 LYS   A CD   1 
ATOM   3893 C CE   A LYS   A 1 163 ? 4.023  -7.450  -5.069  0.56 28.83 ?  163 LYS   A CE   1 
ATOM   3894 C CE   B LYS   A 1 163 ? 4.602  -6.996  -5.475  0.44 27.50 ?  163 LYS   A CE   1 
ATOM   3895 N NZ   A LYS   A 1 163 ? 4.600  -6.635  -6.174  0.56 29.98 ?  163 LYS   A NZ   1 
ATOM   3896 N NZ   B LYS   A 1 163 ? 5.251  -6.078  -6.449  0.44 28.62 ?  163 LYS   A NZ   1 
ATOM   3897 H H    A LYS   A 1 163 ? 3.447  -6.104  1.054   0.56 21.75 ?  163 LYS   A H    1 
ATOM   3898 H H    B LYS   A 1 163 ? 3.664  -6.206  0.654   0.44 22.61 ?  163 LYS   A H    1 
ATOM   3899 H HA   A LYS   A 1 163 ? 2.486  -8.205  -0.195  0.56 22.59 ?  163 LYS   A HA   1 
ATOM   3900 H HA   B LYS   A 1 163 ? 2.606  -8.097  -0.814  0.44 23.20 ?  163 LYS   A HA   1 
ATOM   3901 H HB2  A LYS   A 1 163 ? 2.775  -6.249  -1.387  0.56 25.51 ?  163 LYS   A HB2  1 
ATOM   3902 H HB2  B LYS   A 1 163 ? 3.224  -6.052  -1.742  0.44 25.91 ?  163 LYS   A HB2  1 
ATOM   3903 H HB3  A LYS   A 1 163 ? 4.345  -6.314  -1.155  0.56 25.51 ?  163 LYS   A HB3  1 
ATOM   3904 H HB3  B LYS   A 1 163 ? 4.751  -6.390  -1.480  0.44 25.91 ?  163 LYS   A HB3  1 
ATOM   3905 H HG2  A LYS   A 1 163 ? 4.424  -8.255  -2.501  0.56 28.82 ?  163 LYS   A HG2  1 
ATOM   3906 H HG2  B LYS   A 1 163 ? 4.618  -8.116  -3.054  0.44 28.64 ?  163 LYS   A HG2  1 
ATOM   3907 H HG3  A LYS   A 1 163 ? 2.869  -8.074  -2.789  0.56 28.82 ?  163 LYS   A HG3  1 
ATOM   3908 H HG3  B LYS   A 1 163 ? 3.107  -7.706  -3.345  0.44 28.64 ?  163 LYS   A HG3  1 
ATOM   3909 H HD2  A LYS   A 1 163 ? 3.369  -5.992  -3.798  0.56 32.25 ?  163 LYS   A HD2  1 
ATOM   3910 H HD2  B LYS   A 1 163 ? 3.812  -5.646  -4.159  0.44 30.98 ?  163 LYS   A HD2  1 
ATOM   3911 H HD3  A LYS   A 1 163 ? 4.916  -6.322  -3.616  0.56 32.25 ?  163 LYS   A HD3  1 
ATOM   3912 H HD3  B LYS   A 1 163 ? 5.324  -6.022  -3.829  0.44 30.98 ?  163 LYS   A HD3  1 
ATOM   3913 H HE2  A LYS   A 1 163 ? 4.541  -8.265  -4.979  0.56 34.62 ?  163 LYS   A HE2  1 
ATOM   3914 H HE2  B LYS   A 1 163 ? 5.147  -7.793  -5.402  0.44 33.02 ?  163 LYS   A HE2  1 
ATOM   3915 H HE3  A LYS   A 1 163 ? 3.111  -7.667  -5.305  0.56 34.62 ?  163 LYS   A HE3  1 
ATOM   3916 H HE3  B LYS   A 1 163 ? 3.721  -7.226  -5.812  0.44 33.02 ?  163 LYS   A HE3  1 
ATOM   3917 H HZ1  A LYS   A 1 163 ? 4.586  -7.097  -6.935  0.56 35.99 ?  163 LYS   A HZ1  1 
ATOM   3918 H HZ1  B LYS   A 1 163 ? 4.747  -5.354  -6.563  0.44 34.37 ?  163 LYS   A HZ1  1 
ATOM   3919 H HZ2  A LYS   A 1 163 ? 4.125  -5.889  -6.280  0.56 35.99 ?  163 LYS   A HZ2  1 
ATOM   3920 H HZ2  B LYS   A 1 163 ? 6.049  -5.831  -6.146  0.44 34.37 ?  163 LYS   A HZ2  1 
ATOM   3921 H HZ3  A LYS   A 1 163 ? 5.443  -6.415  -5.986  0.56 35.99 ?  163 LYS   A HZ3  1 
ATOM   3922 H HZ3  B LYS   A 1 163 ? 5.351  -6.489  -7.232  0.44 34.37 ?  163 LYS   A HZ3  1 
ATOM   3923 N N    A LEU   A 1 164 ? 5.558  -8.425  0.672   0.56 16.53 ?  164 LEU   A N    1 
ATOM   3924 N N    B LEU   A 1 164 ? 5.576  -8.729  0.234   0.44 15.78 ?  164 LEU   A N    1 
ATOM   3925 C CA   A LEU   A 1 164 ? 6.646  -9.383  0.837   0.56 14.93 ?  164 LEU   A CA   1 
ATOM   3926 C CA   B LEU   A 1 164 ? 6.607  -9.766  0.295   0.44 15.62 ?  164 LEU   A CA   1 
ATOM   3927 C C    A LEU   A 1 164 ? 6.207  -10.563 1.692   0.56 14.85 ?  164 LEU   A C    1 
ATOM   3928 C C    B LEU   A 1 164 ? 6.148  -10.962 1.119   0.44 16.06 ?  164 LEU   A C    1 
ATOM   3929 O O    A LEU   A 1 164 ? 6.519  -11.722 1.386   0.56 13.95 ?  164 LEU   A O    1 
ATOM   3930 O O    B LEU   A 1 164 ? 6.426  -12.112 0.760   0.44 16.52 ?  164 LEU   A O    1 
ATOM   3931 C CB   A LEU   A 1 164 ? 7.837  -8.684  1.479   0.56 14.16 ?  164 LEU   A CB   1 
ATOM   3932 C CB   B LEU   A 1 164 ? 7.893  -9.195  0.890   0.44 15.29 ?  164 LEU   A CB   1 
ATOM   3933 C CG   A LEU   A 1 164 ? 8.671  -7.801  0.557   0.56 14.62 ?  164 LEU   A CG   1 
ATOM   3934 C CG   B LEU   A 1 164 ? 8.618  -8.148  0.045   0.44 15.24 ?  164 LEU   A CG   1 
ATOM   3935 C CD1  A LEU   A 1 164 ? 9.616  -6.966  1.389   0.56 13.82 ?  164 LEU   A CD1  1 
ATOM   3936 C CD1  B LEU   A 1 164 ? 9.621  -7.377  0.894   0.44 15.21 ?  164 LEU   A CD1  1 
ATOM   3937 C CD2  A LEU   A 1 164 ? 9.445  -8.651  -0.443  0.56 14.84 ?  164 LEU   A CD2  1 
ATOM   3938 C CD2  B LEU   A 1 164 ? 9.317  -8.803  -1.134  0.44 15.48 ?  164 LEU   A CD2  1 
ATOM   3939 H H    A LEU   A 1 164 ? 5.703  -7.634  1.002   0.56 19.86 ?  164 LEU   A H    1 
ATOM   3940 H H    B LEU   A 1 164 ? 5.752  -8.024  0.694   0.44 18.95 ?  164 LEU   A H    1 
ATOM   3941 H HA   A LEU   A 1 164 ? 6.910  -9.703  -0.039  0.56 17.94 ?  164 LEU   A HA   1 
ATOM   3942 H HA   B LEU   A 1 164 ? 6.793  -10.081 -0.599  0.44 18.77 ?  164 LEU   A HA   1 
ATOM   3943 H HB2  A LEU   A 1 164 ? 7.511  -8.117  2.197   0.56 17.01 ?  164 LEU   A HB2  1 
ATOM   3944 H HB2  B LEU   A 1 164 ? 7.678  -8.786  1.741   0.44 18.37 ?  164 LEU   A HB2  1 
ATOM   3945 H HB3  A LEU   A 1 164 ? 8.425  -9.359  1.836   0.56 17.01 ?  164 LEU   A HB3  1 
ATOM   3946 H HB3  B LEU   A 1 164 ? 8.510  -9.930  1.033   0.44 18.37 ?  164 LEU   A HB3  1 
ATOM   3947 H HG   A LEU   A 1 164 ? 8.089  -7.197  0.060   0.56 17.57 ?  164 LEU   A HG   1 
ATOM   3948 H HG   B LEU   A 1 164 ? 7.971  -7.514  -0.298  0.44 18.31 ?  164 LEU   A HG   1 
ATOM   3949 H HD11 A LEU   A 1 164 ? 10.149 -6.408  0.802   0.56 16.60 ?  164 LEU   A HD11 1 
ATOM   3950 H HD11 B LEU   A 1 164 ? 10.072 -6.724  0.337   0.44 18.27 ?  164 LEU   A HD11 1 
ATOM   3951 H HD12 A LEU   A 1 164 ? 9.097  -6.413  1.993   0.56 16.60 ?  164 LEU   A HD12 1 
ATOM   3952 H HD12 B LEU   A 1 164 ? 9.151  -6.929  1.615   0.44 18.27 ?  164 LEU   A HD12 1 
ATOM   3953 H HD13 A LEU   A 1 164 ? 10.191 -7.560  1.896   0.56 16.60 ?  164 LEU   A HD13 1 
ATOM   3954 H HD13 B LEU   A 1 164 ? 10.270 -8.000  1.262   0.44 18.27 ?  164 LEU   A HD13 1 
ATOM   3955 H HD21 A LEU   A 1 164 ? 10.053 -8.084  -0.940  0.56 17.84 ?  164 LEU   A HD21 1 
ATOM   3956 H HD21 B LEU   A 1 164 ? 9.782  -8.122  -1.640  0.44 18.59 ?  164 LEU   A HD21 1 
ATOM   3957 H HD22 A LEU   A 1 164 ? 9.941  -9.329  0.041   0.56 17.84 ?  164 LEU   A HD22 1 
ATOM   3958 H HD22 B LEU   A 1 164 ? 9.947  -9.460  -0.799  0.44 18.59 ?  164 LEU   A HD22 1 
ATOM   3959 H HD23 A LEU   A 1 164 ? 8.816  -9.074  -1.051  0.56 17.84 ?  164 LEU   A HD23 1 
ATOM   3960 H HD23 B LEU   A 1 164 ? 8.650  -9.235  -1.689  0.44 18.59 ?  164 LEU   A HD23 1 
ATOM   3961 N N    A VAL   A 1 165 ? 5.498  -10.282 2.783   0.56 14.19 ?  165 VAL   A N    1 
ATOM   3962 N N    B VAL   A 1 165 ? 5.477  -10.708 2.242   0.44 15.88 ?  165 VAL   A N    1 
ATOM   3963 C CA   A VAL   A 1 165 ? 4.994  -11.352 3.638   0.56 14.32 ?  165 VAL   A CA   1 
ATOM   3964 C CA   B VAL   A 1 165 ? 5.043  -11.789 3.123   0.44 16.27 ?  165 VAL   A CA   1 
ATOM   3965 C C    A VAL   A 1 165 ? 3.972  -12.198 2.890   0.56 14.57 ?  165 VAL   A C    1 
ATOM   3966 C C    B VAL   A 1 165 ? 4.033  -12.689 2.419   0.44 17.74 ?  165 VAL   A C    1 
ATOM   3967 O O    A VAL   A 1 165 ? 4.065  -13.431 2.859   0.56 15.15 ?  165 VAL   A O    1 
ATOM   3968 O O    B VAL   A 1 165 ? 4.108  -13.919 2.509   0.44 17.98 ?  165 VAL   A O    1 
ATOM   3969 C CB   A VAL   A 1 165 ? 4.416  -10.767 4.939   0.56 14.88 ?  165 VAL   A CB   1 
ATOM   3970 C CB   B VAL   A 1 165 ? 4.498  -11.198 4.439   0.44 16.30 ?  165 VAL   A CB   1 
ATOM   3971 C CG1  A VAL   A 1 165 ? 3.638  -11.829 5.702   0.56 15.27 ?  165 VAL   A CG1  1 
ATOM   3972 C CG1  B VAL   A 1 165 ? 3.891  -12.285 5.322   0.44 16.80 ?  165 VAL   A CG1  1 
ATOM   3973 C CG2  A VAL   A 1 165 ? 5.534  -10.185 5.795   0.56 15.53 ?  165 VAL   A CG2  1 
ATOM   3974 C CG2  B VAL   A 1 165 ? 5.608  -10.449 5.177   0.44 16.58 ?  165 VAL   A CG2  1 
ATOM   3975 H H    A VAL   A 1 165 ? 5.303  -9.482  3.046   0.56 17.05 ?  165 VAL   A H    1 
ATOM   3976 H H    B VAL   A 1 165 ? 5.256  -9.927  2.521   0.44 19.07 ?  165 VAL   A H    1 
ATOM   3977 H HA   A VAL   A 1 165 ? 5.733  -11.924 3.877   0.56 17.21 ?  165 VAL   A HA   1 
ATOM   3978 H HA   B VAL   A 1 165 ? 5.804  -12.342 3.349   0.44 19.54 ?  165 VAL   A HA   1 
ATOM   3979 H HB   A VAL   A 1 165 ? 3.804  -10.042 4.722   0.56 17.87 ?  165 VAL   A HB   1 
ATOM   3980 H HB   B VAL   A 1 165 ? 3.798  -10.559 4.235   0.44 19.58 ?  165 VAL   A HB   1 
ATOM   3981 H HG11 A VAL   A 1 165 ? 3.529  -11.540 6.622   0.56 18.34 ?  165 VAL   A HG11 1 
ATOM   3982 H HG11 B VAL   A 1 165 ? 3.765  -11.930 6.218   0.44 20.18 ?  165 VAL   A HG11 1 
ATOM   3983 H HG12 A VAL   A 1 165 ? 2.768  -11.944 5.288   0.56 18.34 ?  165 VAL   A HG12 1 
ATOM   3984 H HG12 B VAL   A 1 165 ? 3.035  -12.552 4.952   0.44 20.18 ?  165 VAL   A HG12 1 
ATOM   3985 H HG13 A VAL   A 1 165 ? 4.134  -12.661 5.675   0.56 18.34 ?  165 VAL   A HG13 1 
ATOM   3986 H HG13 B VAL   A 1 165 ? 4.494  -13.042 5.350   0.44 20.18 ?  165 VAL   A HG13 1 
ATOM   3987 H HG21 A VAL   A 1 165 ? 5.157  -9.860  6.628   0.56 18.66 ?  165 VAL   A HG21 1 
ATOM   3988 H HG21 B VAL   A 1 165 ? 5.253  -10.087 6.005   0.44 19.92 ?  165 VAL   A HG21 1 
ATOM   3989 H HG22 A VAL   A 1 165 ? 6.186  -10.878 5.974   0.56 18.66 ?  165 VAL   A HG22 1 
ATOM   3990 H HG22 B VAL   A 1 165 ? 6.333  -11.063 5.368   0.44 19.92 ?  165 VAL   A HG22 1 
ATOM   3991 H HG23 A VAL   A 1 165 ? 5.953  -9.452  5.314   0.56 18.66 ?  165 VAL   A HG23 1 
ATOM   3992 H HG23 B VAL   A 1 165 ? 5.929  -9.724  4.614   0.44 19.92 ?  165 VAL   A HG23 1 
ATOM   3993 N N    A SER   A 1 166 ? 2.988  -11.549 2.260   0.56 14.63 ?  166 SER   A N    1 
ATOM   3994 N N    B SER   A 1 166 ? 3.092  -12.093 1.687   0.44 18.58 ?  166 SER   A N    1 
ATOM   3995 C CA   A SER   A 1 166 ? 1.883  -12.293 1.659   0.56 15.11 ?  166 SER   A CA   1 
ATOM   3996 C CA   B SER   A 1 166 ? 1.992  -12.832 1.079   0.44 20.13 ?  166 SER   A CA   1 
ATOM   3997 C C    A SER   A 1 166 ? 2.337  -13.170 0.499   0.56 15.95 ?  166 SER   A C    1 
ATOM   3998 C C    B SER   A 1 166 ? 2.355  -13.484 -0.249  0.44 21.93 ?  166 SER   A C    1 
ATOM   3999 O O    A SER   A 1 166 ? 1.684  -14.180 0.201   0.56 17.61 ?  166 SER   A O    1 
ATOM   4000 O O    B SER   A 1 166 ? 1.539  -14.243 -0.782  0.44 22.66 ?  166 SER   A O    1 
ATOM   4001 C CB   A SER   A 1 166 ? 0.781  -11.338 1.199   0.56 16.82 ?  166 SER   A CB   1 
ATOM   4002 C CB   B SER   A 1 166 ? 0.785  -11.905 0.893   0.44 20.43 ?  166 SER   A CB   1 
ATOM   4003 O OG   A SER   A 1 166 ? 0.089  -10.794 2.308   0.56 18.87 ?  166 SER   A OG   1 
ATOM   4004 O OG   B SER   A 1 166 ? 1.106  -10.837 0.023   0.44 20.90 ?  166 SER   A OG   1 
ATOM   4005 H H    A SER   A 1 166 ? 2.932  -10.686 2.175   0.56 17.58 ?  166 SER   A H    1 
ATOM   4006 H H    B SER   A 1 166 ? 3.072  -11.259 1.522   0.44 22.32 ?  166 SER   A H    1 
ATOM   4007 H HA   A SER   A 1 166 ? 1.498  -12.871 2.333   0.56 18.15 ?  166 SER   A HA   1 
ATOM   4008 H HA   B SER   A 1 166 ? 1.718  -13.549 1.661   0.44 24.18 ?  166 SER   A HA   1 
ATOM   4009 H HB2  A SER   A 1 166 ? 1.175  -10.616 0.685   0.56 20.21 ?  166 SER   A HB2  1 
ATOM   4010 H HB2  B SER   A 1 166 ? 0.044  -12.407 0.514   0.44 24.54 ?  166 SER   A HB2  1 
ATOM   4011 H HB3  A SER   A 1 166 ? 0.145  -11.826 0.651   0.56 20.21 ?  166 SER   A HB3  1 
ATOM   4012 H HB3  B SER   A 1 166 ? 0.527  -11.546 1.760   0.44 24.54 ?  166 SER   A HB3  1 
ATOM   4013 H HG   A SER   A 1 166 ? -0.510 -10.263 2.044   0.56 22.66 ?  166 SER   A HG   1 
ATOM   4014 H HG   B SER   A 1 166 ? 1.727  -10.374 0.351   0.44 25.10 ?  166 SER   A HG   1 
ATOM   4015 N N    A SER   A 1 167 ? 3.430  -12.808 -0.171  0.56 15.94 ?  167 SER   A N    1 
ATOM   4016 N N    B SER   A 1 167 ? 3.550  -13.233 -0.785  0.44 22.62 ?  167 SER   A N    1 
ATOM   4017 C CA   A SER   A 1 167 ? 3.880  -13.549 -1.343  0.56 16.32 ?  167 SER   A CA   1 
ATOM   4018 C CA   B SER   A 1 167 ? 3.976  -13.819 -2.053  0.44 23.90 ?  167 SER   A CA   1 
ATOM   4019 C C    A SER   A 1 167 ? 5.011  -14.528 -1.041  0.56 16.16 ?  167 SER   A C    1 
ATOM   4020 C C    B SER   A 1 167 ? 5.179  -14.736 -1.887  0.44 25.47 ?  167 SER   A C    1 
ATOM   4021 O O    A SER   A 1 167 ? 5.490  -15.208 -1.958  0.56 17.00 ?  167 SER   A O    1 
ATOM   4022 O O    B SER   A 1 167 ? 5.722  -15.220 -2.887  0.44 25.82 ?  167 SER   A O    1 
ATOM   4023 C CB   A SER   A 1 167 ? 4.324  -12.578 -2.444  0.56 17.00 ?  167 SER   A CB   1 
ATOM   4024 C CB   B SER   A 1 167 ? 4.289  -12.727 -3.082  0.44 23.46 ?  167 SER   A CB   1 
ATOM   4025 O OG   A SER   A 1 167 ? 5.404  -11.774 -2.002  0.56 17.67 ?  167 SER   A OG   1 
ATOM   4026 O OG   B SER   A 1 167 ? 5.340  -11.893 -2.629  0.44 23.30 ?  167 SER   A OG   1 
ATOM   4027 H H    A SER   A 1 167 ? 3.922  -12.121 0.033   0.56 19.15 ?  167 SER   A H    1 
ATOM   4028 H H    B SER   A 1 167 ? 4.148  -12.731 -0.420  0.44 27.17 ?  167 SER   A H    1 
ATOM   4029 H HA   A SER   A 1 167 ? 3.125  -14.045 -1.688  0.56 19.60 ?  167 SER   A HA   1 
ATOM   4030 H HA   B SER   A 1 167 ? 3.257  -14.352 -2.414  0.44 28.71 ?  167 SER   A HA   1 
ATOM   4031 H HB2  A SER   A 1 167 ? 4.609  -13.092 -3.216  0.56 20.42 ?  167 SER   A HB2  1 
ATOM   4032 H HB2  B SER   A 1 167 ? 4.557  -13.142 -3.919  0.44 28.18 ?  167 SER   A HB2  1 
ATOM   4033 H HB3  A SER   A 1 167 ? 3.575  -12.006 -2.689  0.56 20.42 ?  167 SER   A HB3  1 
ATOM   4034 H HB3  B SER   A 1 167 ? 3.493  -12.187 -3.226  0.44 28.18 ?  167 SER   A HB3  1 
ATOM   4035 H HG   A SER   A 1 167 ? 5.159  -11.309 -1.343  0.56 21.22 ?  167 SER   A HG   1 
ATOM   4036 H HG   B SER   A 1 167 ? 5.117  -11.514 -1.912  0.44 27.99 ?  167 SER   A HG   1 
ATOM   4037 N N    A PHE   A 1 168 ? 5.458  -14.615 0.208   0.56 16.00 ?  168 PHE   A N    1 
ATOM   4038 N N    B PHE   A 1 168 ? 5.598  -14.999 -0.655  0.44 26.40 ?  168 PHE   A N    1 
ATOM   4039 C CA   A PHE   A 1 168 ? 6.632  -15.423 0.511   0.56 16.23 ?  168 PHE   A CA   1 
ATOM   4040 C CA   B PHE   A 1 168 ? 6.844  -15.713 -0.422  0.44 27.32 ?  168 PHE   A CA   1 
ATOM   4041 C C    A PHE   A 1 168 ? 6.316  -16.906 0.395   0.56 16.36 ?  168 PHE   A C    1 
ATOM   4042 C C    B PHE   A 1 168 ? 6.694  -17.187 -0.771  0.44 29.56 ?  168 PHE   A C    1 
ATOM   4043 O O    A PHE   A 1 168 ? 5.307  -17.378 0.924   0.56 18.73 ?  168 PHE   A O    1 
ATOM   4044 O O    B PHE   A 1 168 ? 5.711  -17.832 -0.392  0.44 30.18 ?  168 PHE   A O    1 
ATOM   4045 C CB   A PHE   A 1 168 ? 7.129  -15.136 1.921   0.56 15.41 ?  168 PHE   A CB   1 
ATOM   4046 C CB   B PHE   A 1 168 ? 7.258  -15.562 1.036   0.44 26.07 ?  168 PHE   A CB   1 
ATOM   4047 C CG   A PHE   A 1 168 ? 8.400  -15.866 2.253   0.56 14.59 ?  168 PHE   A CG   1 
ATOM   4048 C CG   B PHE   A 1 168 ? 8.546  -16.244 1.371   0.44 24.81 ?  168 PHE   A CG   1 
ATOM   4049 C CD1  A PHE   A 1 168 ? 9.591  -15.483 1.672   0.56 14.43 ?  168 PHE   A CD1  1 
ATOM   4050 C CD1  B PHE   A 1 168 ? 9.736  -15.819 0.806   0.44 24.33 ?  168 PHE   A CD1  1 
ATOM   4051 C CD2  A PHE   A 1 168 ? 8.398  -16.947 3.118   0.56 14.45 ?  168 PHE   A CD2  1 
ATOM   4052 C CD2  B PHE   A 1 168 ? 8.569  -17.308 2.254   0.44 23.94 ?  168 PHE   A CD2  1 
ATOM   4053 C CE1  A PHE   A 1 168 ? 10.759 -16.153 1.961   0.56 14.00 ?  168 PHE   A CE1  1 
ATOM   4054 C CE1  B PHE   A 1 168 ? 10.924 -16.448 1.114   0.44 23.83 ?  168 PHE   A CE1  1 
ATOM   4055 C CE2  A PHE   A 1 168 ? 9.570  -17.616 3.414   0.56 14.52 ?  168 PHE   A CE2  1 
ATOM   4056 C CE2  B PHE   A 1 168 ? 9.754  -17.940 2.564   0.44 23.49 ?  168 PHE   A CE2  1 
ATOM   4057 C CZ   A PHE   A 1 168 ? 10.747 -17.217 2.832   0.56 14.37 ?  168 PHE   A CZ   1 
ATOM   4058 C CZ   B PHE   A 1 168 ? 10.933 -17.508 1.995   0.44 23.40 ?  168 PHE   A CZ   1 
ATOM   4059 H H    A PHE   A 1 168 ? 5.112  -14.202 0.885   0.56 19.22 ?  168 PHE   A H    1 
ATOM   4060 H H    B PHE   A 1 168 ? 5.179  -14.775 0.058   0.44 31.70 ?  168 PHE   A H    1 
ATOM   4061 H HA   A PHE   A 1 168 ? 7.335  -15.204 -0.118  0.56 19.49 ?  168 PHE   A HA   1 
ATOM   4062 H HA   B PHE   A 1 168 ? 7.538  -15.337 -0.985  0.44 32.81 ?  168 PHE   A HA   1 
ATOM   4063 H HB2  A PHE   A 1 168 ? 7.294  -14.185 2.012   0.56 18.52 ?  168 PHE   A HB2  1 
ATOM   4064 H HB2  B PHE   A 1 168 ? 7.360  -14.619 1.231   0.44 31.31 ?  168 PHE   A HB2  1 
ATOM   4065 H HB3  A PHE   A 1 168 ? 6.448  -15.414 2.556   0.56 18.52 ?  168 PHE   A HB3  1 
ATOM   4066 H HB3  B PHE   A 1 168 ? 6.564  -15.944 1.596   0.44 31.31 ?  168 PHE   A HB3  1 
ATOM   4067 H HD1  A PHE   A 1 168 ? 9.606  -14.762 1.083   0.56 17.34 ?  168 PHE   A HD1  1 
ATOM   4068 H HD1  B PHE   A 1 168 ? 9.733  -15.106 0.207   0.44 29.22 ?  168 PHE   A HD1  1 
ATOM   4069 H HD2  A PHE   A 1 168 ? 7.598  -17.215 3.517   0.56 17.36 ?  168 PHE   A HD2  1 
ATOM   4070 H HD2  B PHE   A 1 168 ? 7.775  -17.603 2.635   0.44 28.76 ?  168 PHE   A HD2  1 
ATOM   4071 H HE1  A PHE   A 1 168 ? 11.561 -15.885 1.570   0.56 16.82 ?  168 PHE   A HE1  1 
ATOM   4072 H HE1  B PHE   A 1 168 ? 11.719 -16.157 0.728   0.44 28.62 ?  168 PHE   A HE1  1 
ATOM   4073 H HE2  A PHE   A 1 168 ? 9.555  -18.337 4.004   0.56 17.44 ?  168 PHE   A HE2  1 
ATOM   4074 H HE2  B PHE   A 1 168 ? 9.758  -18.655 3.157   0.44 28.21 ?  168 PHE   A HE2  1 
ATOM   4075 H HZ   A PHE   A 1 168 ? 11.538 -17.671 3.030   0.56 17.27 ?  168 PHE   A HZ   1 
ATOM   4076 H HZ   B PHE   A 1 168 ? 11.732 -17.933 2.204   0.44 28.10 ?  168 PHE   A HZ   1 
ATOM   4077 N N    A LEU   A 1 169 ? 7.202  -17.653 -0.252  0.56 17.26 ?  169 LEU   A N    1 
ATOM   4078 N N    B LEU   A 1 169 ? 7.685  -17.721 -1.481  0.44 30.90 ?  169 LEU   A N    1 
ATOM   4079 C CA   A LEU   A 1 169 ? 6.984  -19.081 -0.404  0.56 19.38 ?  169 LEU   A CA   1 
ATOM   4080 C CA   B LEU   A 1 169 ? 7.630  -19.087 -1.980  0.44 32.22 ?  169 LEU   A CA   1 
ATOM   4081 C C    A LEU   A 1 169 ? 7.809  -19.841 0.621   0.56 19.46 ?  169 LEU   A C    1 
ATOM   4082 C C    B LEU   A 1 169 ? 8.571  -20.012 -1.212  0.44 33.00 ?  169 LEU   A C    1 
ATOM   4083 O O    A LEU   A 1 169 ? 7.248  -20.412 1.559   0.56 20.38 ?  169 LEU   A O    1 
ATOM   4084 O O    B LEU   A 1 169 ? 8.386  -21.230 -1.190  0.44 33.11 ?  169 LEU   A O    1 
ATOM   4085 C CB   A LEU   A 1 169 ? 7.317  -19.539 -1.825  0.56 20.87 ?  169 LEU   A CB   1 
ATOM   4086 C CB   B LEU   A 1 169 ? 7.987  -19.108 -3.473  0.44 32.63 ?  169 LEU   A CB   1 
ATOM   4087 C CG   A LEU   A 1 169 ? 6.978  -20.999 -2.149  0.56 22.74 ?  169 LEU   A CG   1 
ATOM   4088 C CG   B LEU   A 1 169 ? 7.369  -20.203 -4.346  0.44 32.94 ?  169 LEU   A CG   1 
ATOM   4089 C CD1  A LEU   A 1 169 ? 5.531  -21.319 -1.803  0.56 23.30 ?  169 LEU   A CD1  1 
ATOM   4090 C CD1  B LEU   A 1 169 ? 5.966  -20.539 -3.875  0.44 33.23 ?  169 LEU   A CD1  1 
ATOM   4091 C CD2  A LEU   A 1 169 ? 7.252  -21.299 -3.615  0.56 23.05 ?  169 LEU   A CD2  1 
ATOM   4092 C CD2  B LEU   A 1 169 ? 7.343  -19.746 -5.798  0.44 33.00 ?  169 LEU   A CD2  1 
ATOM   4093 O OXT  A LEU   A 1 169 ? 9.040  -19.888 0.546   0.56 19.37 -1 169 LEU   A OXT  1 
ATOM   4094 O OXT  B LEU   A 1 169 ? 9.541  -19.570 -0.600  0.44 33.53 -1 169 LEU   A OXT  1 
ATOM   4095 H H    A LEU   A 1 169 ? 7.928  -17.358 -0.592  0.56 20.73 ?  169 LEU   A H    1 
ATOM   4096 H H    B LEU   A 1 169 ? 8.405  -17.303 -1.692  0.44 37.11 ?  169 LEU   A H    1 
ATOM   4097 H HA   A LEU   A 1 169 ? 6.052  -19.279 -0.230  0.56 23.27 ?  169 LEU   A HA   1 
ATOM   4098 H HA   B LEU   A 1 169 ? 6.728  -19.409 -1.855  0.44 38.69 ?  169 LEU   A HA   1 
ATOM   4099 H HB2  A LEU   A 1 169 ? 6.821  -18.985 -2.447  0.56 25.07 ?  169 LEU   A HB2  1 
ATOM   4100 H HB2  B LEU   A 1 169 ? 7.725  -18.259 -3.859  0.44 39.17 ?  169 LEU   A HB2  1 
ATOM   4101 H HB3  A LEU   A 1 169 ? 8.266  -19.425 -1.970  0.56 25.07 ?  169 LEU   A HB3  1 
ATOM   4102 H HB3  B LEU   A 1 169 ? 8.952  -19.203 -3.547  0.44 39.17 ?  169 LEU   A HB3  1 
ATOM   4103 H HG   A LEU   A 1 169 ? 7.544  -21.580 -1.618  0.56 27.31 ?  169 LEU   A HG   1 
ATOM   4104 H HG   B LEU   A 1 169 ? 7.913  -21.006 -4.292  0.44 39.55 ?  169 LEU   A HG   1 
ATOM   4105 H HD11 A LEU   A 1 169 ? 5.289  -22.169 -2.202  0.56 27.99 ?  169 LEU   A HD11 1 
ATOM   4106 H HD11 B LEU   A 1 169 ? 5.510  -21.026 -4.571  0.44 39.89 ?  169 LEU   A HD11 1 
ATOM   4107 H HD12 A LEU   A 1 169 ? 5.438  -21.370 -0.838  0.56 27.99 ?  169 LEU   A HD12 1 
ATOM   4108 H HD12 B LEU   A 1 169 ? 6.025  -21.083 -3.072  0.44 39.89 ?  169 LEU   A HD12 1 
ATOM   4109 H HD13 A LEU   A 1 169 ? 4.959  -20.616 -2.153  0.56 27.99 ?  169 LEU   A HD13 1 
ATOM   4110 H HD13 B LEU   A 1 169 ? 5.493  -19.712 -3.683  0.44 39.89 ?  169 LEU   A HD13 1 
ATOM   4111 H HD21 A LEU   A 1 169 ? 7.037  -22.228 -3.794  0.56 27.69 ?  169 LEU   A HD21 1 
ATOM   4112 H HD21 B LEU   A 1 169 ? 6.981  -20.458 -6.348  0.44 39.62 ?  169 LEU   A HD21 1 
ATOM   4113 H HD22 A LEU   A 1 169 ? 6.698  -20.721 -4.164  0.56 27.69 ?  169 LEU   A HD22 1 
ATOM   4114 H HD22 B LEU   A 1 169 ? 6.783  -18.956 -5.870  0.44 39.62 ?  169 LEU   A HD22 1 
ATOM   4115 H HD23 A LEU   A 1 169 ? 8.189  -21.134 -3.801  0.56 27.69 ?  169 LEU   A HD23 1 
ATOM   4116 H HD23 B LEU   A 1 169 ? 8.247  -19.537 -6.081  0.44 39.62 ?  169 LEU   A HD23 1 
ATOM   4117 N N    A SER   B 1 1   ? 50.830 -9.260  -23.706 0.56 28.32 ?  1   SER   B N    1 
ATOM   4118 N N    B SER   B 1 1   ? 50.709 -9.249  -23.680 0.44 26.40 ?  1   SER   B N    1 
ATOM   4119 C CA   A SER   B 1 1   ? 51.313 -10.309 -22.785 0.56 28.58 ?  1   SER   B CA   1 
ATOM   4120 C CA   B SER   B 1 1   ? 51.214 -10.243 -22.711 0.44 26.29 ?  1   SER   B CA   1 
ATOM   4121 C C    A SER   B 1 1   ? 50.231 -11.353 -22.529 0.56 28.11 ?  1   SER   B C    1 
ATOM   4122 C C    B SER   B 1 1   ? 50.173 -11.325 -22.467 0.44 25.61 ?  1   SER   B C    1 
ATOM   4123 O O    A SER   B 1 1   ? 49.045 -11.142 -22.813 0.56 28.26 ?  1   SER   B O    1 
ATOM   4124 O O    B SER   B 1 1   ? 48.972 -11.134 -22.700 0.44 25.79 ?  1   SER   B O    1 
ATOM   4125 C CB   A SER   B 1 1   ? 51.764 -9.696  -21.461 0.56 29.43 ?  1   SER   B CB   1 
ATOM   4126 C CB   B SER   B 1 1   ? 51.577 -9.576  -21.388 0.44 26.89 ?  1   SER   B CB   1 
ATOM   4127 O OG   A SER   B 1 1   ? 50.653 -9.376  -20.647 0.56 30.75 ?  1   SER   B OG   1 
ATOM   4128 O OG   B SER   B 1 1   ? 50.457 -9.533  -20.522 0.44 27.94 ?  1   SER   B OG   1 
ATOM   4129 H H1   A SER   B 1 1   ? 50.755 -9.603  -24.522 0.56 34.00 ?  1   SER   B H1   1 
ATOM   4130 H H1   B SER   B 1 1   ? 50.602 -9.641  -24.469 0.44 31.70 ?  1   SER   B H1   1 
ATOM   4131 H H2   A SER   B 1 1   ? 50.042 -8.969  -23.425 0.56 34.00 ?  1   SER   B H2   1 
ATOM   4132 H H2   B SER   B 1 1   ? 49.934 -8.932  -23.390 0.44 31.70 ?  1   SER   B H2   1 
ATOM   4133 H H3   A SER   B 1 1   ? 51.415 -8.591  -23.714 0.56 34.00 ?  1   SER   B H3   1 
ATOM   4134 H H3   B SER   B 1 1   ? 51.300 -8.589  -23.749 0.44 31.70 ?  1   SER   B H3   1 
ATOM   4135 H HA   A SER   B 1 1   ? 52.075 -10.740 -23.196 0.56 34.32 ?  1   SER   B HA   1 
ATOM   4136 H HA   B SER   B 1 1   ? 52.011 -10.649 -23.080 0.44 31.57 ?  1   SER   B HA   1 
ATOM   4137 H HB2  A SER   B 1 1   ? 52.322 -10.339 -20.999 0.56 35.34 ?  1   SER   B HB2  1 
ATOM   4138 H HB2  B SER   B 1 1   ? 52.283 -10.087 -20.967 0.44 32.30 ?  1   SER   B HB2  1 
ATOM   4139 H HB3  A SER   B 1 1   ? 52.267 -8.886  -21.639 0.56 35.34 ?  1   SER   B HB3  1 
ATOM   4140 H HB3  B SER   B 1 1   ? 51.880 -8.670  -21.562 0.44 32.30 ?  1   SER   B HB3  1 
ATOM   4141 H HG   A SER   B 1 1   ? 50.913 -8.969  -19.959 0.56 36.92 ?  1   SER   B HG   1 
ATOM   4142 H HG   B SER   B 1 1   ? 50.618 -9.018  -19.877 0.44 33.55 ?  1   SER   B HG   1 
ATOM   4143 N N    A MET   B 1 2   ? 50.661 -12.479 -21.973 0.56 27.77 ?  2   MET   B N    1 
ATOM   4144 N N    B MET   B 1 2   ? 50.649 -12.464 -21.985 0.44 24.98 ?  2   MET   B N    1 
ATOM   4145 C CA   A MET   B 1 2   ? 49.830 -13.666 -21.817 0.56 27.78 ?  2   MET   B CA   1 
ATOM   4146 C CA   B MET   B 1 2   ? 49.830 -13.653 -21.798 0.44 24.91 ?  2   MET   B CA   1 
ATOM   4147 C C    A MET   B 1 2   ? 49.575 -13.890 -20.333 0.56 25.19 ?  2   MET   B C    1 
ATOM   4148 C C    B MET   B 1 2   ? 49.585 -13.826 -20.311 0.44 23.61 ?  2   MET   B C    1 
ATOM   4149 O O    A MET   B 1 2   ? 50.496 -14.229 -19.585 0.56 25.36 ?  2   MET   B O    1 
ATOM   4150 O O    B MET   B 1 2   ? 50.524 -14.044 -19.541 0.44 23.38 ?  2   MET   B O    1 
ATOM   4151 C CB   A MET   B 1 2   ? 50.550 -14.860 -22.431 0.56 31.18 ?  2   MET   B CB   1 
ATOM   4152 C CB   B MET   B 1 2   ? 50.558 -14.852 -22.375 0.44 26.88 ?  2   MET   B CB   1 
ATOM   4153 C CG   A MET   B 1 2   ? 49.713 -16.120 -22.547 0.56 34.52 ?  2   MET   B CG   1 
ATOM   4154 C CG   B MET   B 1 2   ? 49.662 -16.008 -22.800 0.44 28.60 ?  2   MET   B CG   1 
ATOM   4155 S SD   A MET   B 1 2   ? 50.560 -17.370 -23.531 0.56 37.48 ?  2   MET   B SD   1 
ATOM   4156 S SD   B MET   B 1 2   ? 50.510 -17.104 -23.945 0.44 30.08 ?  2   MET   B SD   1 
ATOM   4157 C CE   A MET   B 1 2   ? 51.072 -16.363 -24.922 0.56 37.37 ?  2   MET   B CE   1 
ATOM   4158 C CE   B MET   B 1 2   ? 51.747 -16.001 -24.594 0.44 30.07 ?  2   MET   B CE   1 
ATOM   4159 H H    A MET   B 1 2   ? 51.462 -12.584 -21.674 0.56 33.35 ?  2   MET   B H    1 
ATOM   4160 H H    B MET   B 1 2   ? 51.474 -12.584 -21.754 0.44 29.99 ?  2   MET   B H    1 
ATOM   4161 H HA   A MET   B 1 2   ? 48.991 -13.544 -22.286 0.56 33.36 ?  2   MET   B HA   1 
ATOM   4162 H HA   B MET   B 1 2   ? 48.995 -13.564 -22.280 0.44 29.92 ?  2   MET   B HA   1 
ATOM   4163 H HB2  A MET   B 1 2   ? 50.837 -14.587 -23.313 0.56 37.44 ?  2   MET   B HB2  1 
ATOM   4164 H HB2  B MET   B 1 2   ? 50.988 -14.465 -23.141 0.44 32.28 ?  2   MET   B HB2  1 
ATOM   4165 H HB3  A MET   B 1 2   ? 51.324 -15.082 -21.893 0.56 37.44 ?  2   MET   B HB3  1 
ATOM   4166 H HB3  B MET   B 1 2   ? 51.221 -15.209 -21.759 0.44 32.28 ?  2   MET   B HB3  1 
ATOM   4167 H HG2  A MET   B 1 2   ? 49.553 -16.483 -21.659 0.56 41.45 ?  2   MET   B HG2  1 
ATOM   4168 H HG2  B MET   B 1 2   ? 49.391 -16.520 -22.014 0.44 34.34 ?  2   MET   B HG2  1 
ATOM   4169 H HG3  A MET   B 1 2   ? 48.871 -15.913 -22.982 0.56 41.45 ?  2   MET   B HG3  1 
ATOM   4170 H HG3  B MET   B 1 2   ? 48.883 -15.671 -23.259 0.44 34.34 ?  2   MET   B HG3  1 
ATOM   4171 H HE1  A MET   B 1 2   ? 51.232 -16.935 -25.676 0.56 44.86 ?  2   MET   B HE1  1 
ATOM   4172 H HE1  B MET   B 1 2   ? 52.218 -16.485 -25.247 0.44 36.11 ?  2   MET   B HE1  1 
ATOM   4173 H HE2  A MET   B 1 2   ? 50.361 -15.729 -25.126 0.56 44.86 ?  2   MET   B HE2  1 
ATOM   4174 H HE2  B MET   B 1 2   ? 51.301 -15.228 -24.993 0.44 36.11 ?  2   MET   B HE2  1 
ATOM   4175 H HE3  A MET   B 1 2   ? 51.884 -15.877 -24.690 0.56 44.86 ?  2   MET   B HE3  1 
ATOM   4176 H HE3  B MET   B 1 2   ? 52.376 -15.720 -23.898 0.44 36.11 ?  2   MET   B HE3  1 
ATOM   4177 N N    . VAL   B 1 3   ? 48.327 -13.700 -19.910 1.00 22.44 ?  3   VAL   B N    1 
ATOM   4178 C CA   . VAL   B 1 3   ? 47.919 -13.934 -18.535 1.00 20.85 ?  3   VAL   B CA   1 
ATOM   4179 C C    . VAL   B 1 3   ? 46.681 -14.823 -18.558 1.00 19.51 ?  3   VAL   B C    1 
ATOM   4180 O O    . VAL   B 1 3   ? 45.953 -14.897 -19.553 1.00 20.13 ?  3   VAL   B O    1 
ATOM   4181 C CB   . VAL   B 1 3   ? 47.647 -12.618 -17.770 1.00 22.62 ?  3   VAL   B CB   1 
ATOM   4182 C CG1  . VAL   B 1 3   ? 48.923 -11.769 -17.655 1.00 23.12 ?  3   VAL   B CG1  1 
ATOM   4183 C CG2  . VAL   B 1 3   ? 46.537 -11.836 -18.450 1.00 22.91 ?  3   VAL   B CG2  1 
ATOM   4184 H H    A VAL   B 1 3   ? 47.688 -13.437 -20.423 0.56 26.95 ?  3   VAL   B H    1 
ATOM   4185 H H    B VAL   B 1 3   ? 47.684 -13.459 -20.429 0.44 26.95 ?  3   VAL   B H    1 
ATOM   4186 H HA   . VAL   B 1 3   ? 48.625 -14.411 -18.070 1.00 25.04 ?  3   VAL   B HA   1 
ATOM   4187 H HB   . VAL   B 1 3   ? 47.353 -12.839 -16.871 1.00 27.17 ?  3   VAL   B HB   1 
ATOM   4188 H HG11 . VAL   B 1 3   ? 48.713 -10.961 -17.164 1.00 27.77 ?  3   VAL   B HG11 1 
ATOM   4189 H HG12 . VAL   B 1 3   ? 49.596 -12.281 -17.182 1.00 27.77 ?  3   VAL   B HG12 1 
ATOM   4190 H HG13 . VAL   B 1 3   ? 49.232 -11.550 -18.545 1.00 27.77 ?  3   VAL   B HG13 1 
ATOM   4191 H HG21 . VAL   B 1 3   ? 46.466 -10.965 -18.036 1.00 27.52 ?  3   VAL   B HG21 1 
ATOM   4192 H HG22 . VAL   B 1 3   ? 46.744 -11.743 -19.392 1.00 27.52 ?  3   VAL   B HG22 1 
ATOM   4193 H HG23 . VAL   B 1 3   ? 45.698 -12.320 -18.345 1.00 27.52 ?  3   VAL   B HG23 1 
ATOM   4194 N N    . ASN   B 1 4   ? 46.453 -15.513 -17.443 1.00 17.63 ?  4   ASN   B N    1 
ATOM   4195 C CA   . ASN   B 1 4   ? 45.311 -16.417 -17.320 1.00 16.96 ?  4   ASN   B CA   1 
ATOM   4196 C C    . ASN   B 1 4   ? 45.246 -17.378 -18.504 1.00 17.47 ?  4   ASN   B C    1 
ATOM   4197 O O    . ASN   B 1 4   ? 44.184 -17.624 -19.072 1.00 17.80 ?  4   ASN   B O    1 
ATOM   4198 C CB   . ASN   B 1 4   ? 43.996 -15.642 -17.168 1.00 16.52 ?  4   ASN   B CB   1 
ATOM   4199 C CG   . ASN   B 1 4   ? 43.951 -14.830 -15.891 1.00 16.50 ?  4   ASN   B CG   1 
ATOM   4200 O OD1  . ASN   B 1 4   ? 44.233 -15.340 -14.810 1.00 16.22 ?  4   ASN   B OD1  1 
ATOM   4201 N ND2  . ASN   B 1 4   ? 43.629 -13.549 -16.014 1.00 16.88 ?  4   ASN   B ND2  1 
ATOM   4202 H H    . ASN   B 1 4   ? 46.960 -15.485 -16.748 1.00 21.18 ?  4   ASN   B H    1 
ATOM   4203 H HA   . ASN   B 1 4   ? 45.434 -16.949 -16.519 1.00 20.38 ?  4   ASN   B HA   1 
ATOM   4204 H HB2  . ASN   B 1 4   ? 43.900 -15.034 -17.915 1.00 19.85 ?  4   ASN   B HB2  1 
ATOM   4205 H HB3  . ASN   B 1 4   ? 43.261 -16.273 -17.151 1.00 19.85 ?  4   ASN   B HB3  1 
ATOM   4206 H HD21 . ASN   B 1 4   ? 43.595 -13.043 -15.317 1.00 20.28 ?  4   ASN   B HD21 1 
ATOM   4207 H HD22 . ASN   B 1 4   ? 43.449 -13.219 -16.789 1.00 20.28 ?  4   ASN   B HD22 1 
ATOM   4208 N N    . SER   B 1 5   ? 46.399 -17.926 -18.882 1.00 18.21 ?  5   SER   B N    1 
ATOM   4209 C CA   . SER   B 1 5   ? 46.484 -18.841 -20.018 1.00 20.63 ?  5   SER   B CA   1 
ATOM   4210 C C    . SER   B 1 5   ? 46.460 -20.271 -19.489 1.00 22.56 ?  5   SER   B C    1 
ATOM   4211 O O    . SER   B 1 5   ? 47.473 -20.959 -19.416 1.00 25.09 ?  5   SER   B O    1 
ATOM   4212 C CB   . SER   B 1 5   ? 47.743 -18.558 -20.839 1.00 22.61 ?  5   SER   B CB   1 
ATOM   4213 O OG   . SER   B 1 5   ? 48.912 -18.654 -20.042 1.00 25.87 ?  5   SER   B OG   1 
ATOM   4214 H H    . SER   B 1 5   ? 47.153 -17.804 -18.486 1.00 21.87 ?  5   SER   B H    1 
ATOM   4215 H HA   . SER   B 1 5   ? 45.715 -18.715 -20.595 1.00 24.78 ?  5   SER   B HA   1 
ATOM   4216 H HB2  . SER   B 1 5   ? 47.801 -19.205 -21.564 1.00 27.15 ?  5   SER   B HB2  1 
ATOM   4217 H HB3  . SER   B 1 5   ? 47.680 -17.663 -21.206 1.00 27.15 ?  5   SER   B HB3  1 
ATOM   4218 H HG   . SER   B 1 5   ? 48.979 -19.429 -19.728 1.00 31.06 ?  5   SER   B HG   1 
ATOM   4219 N N    . PHE   B 1 6   ? 45.264 -20.689 -19.082 1.00 23.61 ?  6   PHE   B N    1 
ATOM   4220 C CA   . PHE   B 1 6   ? 45.052 -22.030 -18.554 1.00 23.37 ?  6   PHE   B CA   1 
ATOM   4221 C C    . PHE   B 1 6   ? 44.959 -23.009 -19.715 1.00 27.00 ?  6   PHE   B C    1 
ATOM   4222 O O    . PHE   B 1 6   ? 44.252 -22.750 -20.693 1.00 29.05 ?  6   PHE   B O    1 
ATOM   4223 C CB   . PHE   B 1 6   ? 43.765 -22.070 -17.731 1.00 21.70 ?  6   PHE   B CB   1 
ATOM   4224 C CG   . PHE   B 1 6   ? 43.808 -21.213 -16.498 1.00 19.19 ?  6   PHE   B CG   1 
ATOM   4225 C CD1  . PHE   B 1 6   ? 44.313 -21.713 -15.313 1.00 17.81 ?  6   PHE   B CD1  1 
ATOM   4226 C CD2  . PHE   B 1 6   ? 43.349 -19.903 -16.528 1.00 17.91 ?  6   PHE   B CD2  1 
ATOM   4227 C CE1  . PHE   B 1 6   ? 44.351 -20.926 -14.174 1.00 16.80 ?  6   PHE   B CE1  1 
ATOM   4228 C CE2  . PHE   B 1 6   ? 43.389 -19.110 -15.401 1.00 18.43 ?  6   PHE   B CE2  1 
ATOM   4229 C CZ   . PHE   B 1 6   ? 43.892 -19.615 -14.224 1.00 17.63 ?  6   PHE   B CZ   1 
ATOM   4230 H H    . PHE   B 1 6   ? 44.545 -20.216 -19.112 1.00 28.35 ?  6   PHE   B H    1 
ATOM   4231 H HA   . PHE   B 1 6   ? 45.795 -22.286 -17.991 1.00 28.07 ?  6   PHE   B HA   1 
ATOM   4232 H HB2  . PHE   B 1 6   ? 43.029 -21.758 -18.284 1.00 26.06 ?  6   PHE   B HB2  1 
ATOM   4233 H HB3  . PHE   B 1 6   ? 43.598 -22.984 -17.451 1.00 26.06 ?  6   PHE   B HB3  1 
ATOM   4234 H HD1  . PHE   B 1 6   ? 44.632 -22.588 -15.279 1.00 21.39 ?  6   PHE   B HD1  1 
ATOM   4235 H HD2  . PHE   B 1 6   ? 43.004 -19.560 -17.317 1.00 21.51 ?  6   PHE   B HD2  1 
ATOM   4236 H HE1  . PHE   B 1 6   ? 44.704 -21.266 -13.381 1.00 20.19 ?  6   PHE   B HE1  1 
ATOM   4237 H HE2  . PHE   B 1 6   ? 43.072 -18.237 -15.432 1.00 22.14 ?  6   PHE   B HE2  1 
ATOM   4238 H HZ   . PHE   B 1 6   ? 43.922 -19.087 -13.459 1.00 21.18 ?  6   PHE   B HZ   1 
ATOM   4239 N N    A SER   B 1 7   ? 45.681 -24.125 -19.610 0.56 27.64 ?  7   SER   B N    1 
ATOM   4240 N N    B SER   B 1 7   ? 45.680 -24.125 -19.614 0.44 27.64 ?  7   SER   B N    1 
ATOM   4241 C CA   A SER   B 1 7   ? 45.767 -25.101 -20.687 0.56 29.81 ?  7   SER   B CA   1 
ATOM   4242 C CA   B SER   B 1 7   ? 45.740 -25.094 -20.698 0.44 29.39 ?  7   SER   B CA   1 
ATOM   4243 C C    A SER   B 1 7   ? 45.675 -26.509 -20.119 0.56 29.58 ?  7   SER   B C    1 
ATOM   4244 C C    B SER   B 1 7   ? 45.691 -26.508 -20.140 0.44 29.45 ?  7   SER   B C    1 
ATOM   4245 O O    A SER   B 1 7   ? 46.282 -26.815 -19.089 0.56 30.21 ?  7   SER   B O    1 
ATOM   4246 O O    B SER   B 1 7   ? 46.345 -26.816 -19.140 0.44 30.02 ?  7   SER   B O    1 
ATOM   4247 C CB   A SER   B 1 7   ? 47.086 -24.944 -21.460 0.56 32.00 ?  7   SER   B CB   1 
ATOM   4248 C CB   B SER   B 1 7   ? 47.012 -24.907 -21.537 0.44 30.93 ?  7   SER   B CB   1 
ATOM   4249 O OG   A SER   B 1 7   ? 47.188 -25.903 -22.499 0.56 33.70 ?  7   SER   B OG   1 
ATOM   4250 O OG   B SER   B 1 7   ? 46.862 -25.494 -22.818 0.44 31.90 ?  7   SER   B OG   1 
ATOM   4251 H H    A SER   B 1 7   ? 46.145 -24.338 -18.915 0.56 33.19 ?  7   SER   B H    1 
ATOM   4252 H H    B SER   B 1 7   ? 46.152 -24.340 -18.925 0.44 33.19 ?  7   SER   B H    1 
ATOM   4253 H HA   A SER   B 1 7   ? 45.036 -24.972 -21.307 0.56 35.79 ?  7   SER   B HA   1 
ATOM   4254 H HA   B SER   B 1 7   ? 44.978 -24.975 -21.278 0.44 35.29 ?  7   SER   B HA   1 
ATOM   4255 H HB2  A SER   B 1 7   ? 47.120 -24.055 -21.850 0.56 38.42 ?  7   SER   B HB2  1 
ATOM   4256 H HB2  B SER   B 1 7   ? 47.183 -23.958 -21.646 0.44 37.14 ?  7   SER   B HB2  1 
ATOM   4257 H HB3  A SER   B 1 7   ? 47.830 -25.063 -20.849 0.56 38.42 ?  7   SER   B HB3  1 
ATOM   4258 H HB3  B SER   B 1 7   ? 47.760 -25.327 -21.082 0.44 37.14 ?  7   SER   B HB3  1 
ATOM   4259 H HG   A SER   B 1 7   ? 47.914 -25.804 -22.913 0.56 40.46 ?  7   SER   B HG   1 
ATOM   4260 H HG   B SER   B 1 7   ? 47.566 -25.387 -23.267 0.44 38.31 ?  7   SER   B HG   1 
ATOM   4261 N N    . GLY   B 1 8   ? 44.912 -27.363 -20.800 1.00 29.17 ?  8   GLY   B N    1 
ATOM   4262 C CA   . GLY   B 1 8   ? 44.844 -28.759 -20.433 1.00 28.50 ?  8   GLY   B CA   1 
ATOM   4263 C C    . GLY   B 1 8   ? 43.935 -29.085 -19.279 1.00 26.91 ?  8   GLY   B C    1 
ATOM   4264 O O    . GLY   B 1 8   ? 44.102 -30.145 -18.664 1.00 28.44 ?  8   GLY   B O    1 
ATOM   4265 H H    A GLY   B 1 8   ? 44.428 -27.149 -21.475 0.56 35.03 ?  8   GLY   B H    1 
ATOM   4266 H H    B GLY   B 1 8   ? 44.418 -27.148 -21.468 0.44 35.03 ?  8   GLY   B H    1 
ATOM   4267 H HA2  . GLY   B 1 8   ? 44.534 -29.268 -21.192 1.00 34.22 ?  8   GLY   B HA2  1 
ATOM   4268 H HA3  . GLY   B 1 8   ? 45.729 -29.068 -20.198 1.00 34.22 ?  8   GLY   B HA3  1 
ATOM   4269 N N    . TYR   B 1 9   ? 42.959 -28.234 -18.976 1.00 25.39 ?  9   TYR   B N    1 
ATOM   4270 C CA   . TYR   B 1 9   ? 42.033 -28.520 -17.893 1.00 23.25 ?  9   TYR   B CA   1 
ATOM   4271 C C    . TYR   B 1 9   ? 40.841 -29.315 -18.392 1.00 22.32 ?  9   TYR   B C    1 
ATOM   4272 O O    . TYR   B 1 9   ? 40.404 -29.176 -19.538 1.00 24.29 ?  9   TYR   B O    1 
ATOM   4273 C CB   . TYR   B 1 9   ? 41.538 -27.240 -17.226 1.00 22.49 ?  9   TYR   B CB   1 
ATOM   4274 C CG   . TYR   B 1 9   ? 42.583 -26.624 -16.325 1.00 21.62 ?  9   TYR   B CG   1 
ATOM   4275 C CD1  . TYR   B 1 9   ? 43.665 -25.938 -16.857 1.00 21.64 ?  9   TYR   B CD1  1 
ATOM   4276 C CD2  . TYR   B 1 9   ? 42.500 -26.743 -14.945 1.00 20.95 ?  9   TYR   B CD2  1 
ATOM   4277 C CE1  . TYR   B 1 9   ? 44.638 -25.379 -16.037 1.00 21.42 ?  9   TYR   B CE1  1 
ATOM   4278 C CE2  . TYR   B 1 9   ? 43.469 -26.193 -14.116 1.00 21.13 ?  9   TYR   B CE2  1 
ATOM   4279 C CZ   . TYR   B 1 9   ? 44.535 -25.508 -14.668 1.00 21.41 ?  9   TYR   B CZ   1 
ATOM   4280 O OH   . TYR   B 1 9   ? 45.496 -24.969 -13.850 1.00 22.33 ?  9   TYR   B OH   1 
ATOM   4281 H H    . TYR   B 1 9   ? 42.794 -27.497 -19.394 1.00 30.49 ?  9   TYR   B H    1 
ATOM   4282 H HA   . TYR   B 1 9   ? 42.476 -29.048 -17.218 1.00 27.93 ?  9   TYR   B HA   1 
ATOM   4283 H HB2  . TYR   B 1 9   ? 41.293 -26.584 -17.901 1.00 27.01 ?  9   TYR   B HB2  1 
ATOM   4284 H HB3  . TYR   B 1 9   ? 40.771 -27.456 -16.678 1.00 27.01 ?  9   TYR   B HB3  1 
ATOM   4285 H HD1  . TYR   B 1 9   ? 43.736 -25.847 -17.779 1.00 25.99 ?  9   TYR   B HD1  1 
ATOM   4286 H HD2  . TYR   B 1 9   ? 41.779 -27.207 -14.569 1.00 25.16 ?  9   TYR   B HD2  1 
ATOM   4287 H HE1  . TYR   B 1 9   ? 45.350 -24.926 -16.409 1.00 25.72 ?  9   TYR   B HE1  1 
ATOM   4288 H HE2  . TYR   B 1 9   ? 43.390 -26.288 -13.191 1.00 25.37 ?  9   TYR   B HE2  1 
ATOM   4289 H HH   . TYR   B 1 9   ? 46.076 -24.586 -14.313 1.00 26.82 ?  9   TYR   B HH   1 
ATOM   4290 N N    . LEU   B 1 10  ? 40.328 -30.163 -17.507 1.00 20.68 ?  10  LEU   B N    1 
ATOM   4291 C CA   . LEU   B 1 10  ? 39.120 -30.931 -17.758 1.00 20.84 ?  10  LEU   B CA   1 
ATOM   4292 C C    . LEU   B 1 10  ? 37.934 -30.157 -17.204 1.00 20.22 ?  10  LEU   B C    1 
ATOM   4293 O O    . LEU   B 1 10  ? 37.952 -29.730 -16.046 1.00 19.53 ?  10  LEU   B O    1 
ATOM   4294 C CB   . LEU   B 1 10  ? 39.224 -32.287 -17.058 1.00 21.82 ?  10  LEU   B CB   1 
ATOM   4295 C CG   . LEU   B 1 10  ? 38.096 -33.270 -17.361 1.00 23.11 ?  10  LEU   B CG   1 
ATOM   4296 C CD1  . LEU   B 1 10  ? 38.206 -33.767 -18.793 1.00 24.17 ?  10  LEU   B CD1  1 
ATOM   4297 C CD2  . LEU   B 1 10  ? 38.101 -34.429 -16.380 1.00 23.73 ?  10  LEU   B CD2  1 
ATOM   4298 H H    . LEU   B 1 10  ? 40.666 -30.314 -16.726 1.00 24.84 ?  10  LEU   B H    1 
ATOM   4299 H HA   . LEU   B 1 10  ? 38.996 -31.069 -18.708 1.00 25.03 ?  10  LEU   B HA   1 
ATOM   4300 H HB2  . LEU   B 1 10  ? 40.056 -32.707 -17.327 1.00 26.20 ?  10  LEU   B HB2  1 
ATOM   4301 H HB3  . LEU   B 1 10  ? 39.232 -32.140 -16.098 1.00 26.20 ?  10  LEU   B HB3  1 
ATOM   4302 H HG   . LEU   B 1 10  ? 37.246 -32.810 -17.270 1.00 27.75 ?  10  LEU   B HG   1 
ATOM   4303 H HD11 . LEU   B 1 10  ? 37.535 -34.448 -18.942 1.00 29.03 ?  10  LEU   B HD11 1 
ATOM   4304 H HD12 . LEU   B 1 10  ? 38.060 -33.020 -19.396 1.00 29.03 ?  10  LEU   B HD12 1 
ATOM   4305 H HD13 . LEU   B 1 10  ? 39.092 -34.135 -18.930 1.00 29.03 ?  10  LEU   B HD13 1 
ATOM   4306 H HD21 . LEU   B 1 10  ? 37.373 -35.030 -16.603 1.00 28.50 ?  10  LEU   B HD21 1 
ATOM   4307 H HD22 . LEU   B 1 10  ? 38.948 -34.891 -16.446 1.00 28.50 ?  10  LEU   B HD22 1 
ATOM   4308 H HD23 . LEU   B 1 10  ? 37.979 -34.079 -15.483 1.00 28.50 ?  10  LEU   B HD23 1 
ATOM   4309 N N    . LYS   B 1 11  ? 36.911 -29.980 -18.031 1.00 20.98 ?  11  LYS   B N    1 
ATOM   4310 C CA   . LYS   B 1 11  ? 35.706 -29.275 -17.621 1.00 23.53 ?  11  LYS   B CA   1 
ATOM   4311 C C    . LYS   B 1 11  ? 34.858 -30.202 -16.755 1.00 22.43 ?  11  LYS   B C    1 
ATOM   4312 O O    . LYS   B 1 11  ? 34.503 -31.309 -17.183 1.00 24.45 ?  11  LYS   B O    1 
ATOM   4313 C CB   . LYS   B 1 11  ? 34.932 -28.850 -18.870 1.00 27.82 ?  11  LYS   B CB   1 
ATOM   4314 C CG   . LYS   B 1 11  ? 33.800 -27.867 -18.634 1.00 32.05 ?  11  LYS   B CG   1 
ATOM   4315 C CD   . LYS   B 1 11  ? 33.054 -27.585 -19.937 1.00 35.17 ?  11  LYS   B CD   1 
ATOM   4316 C CE   . LYS   B 1 11  ? 32.058 -26.444 -19.789 1.00 37.52 ?  11  LYS   B CE   1 
ATOM   4317 N NZ   . LYS   B 1 11  ? 32.727 -25.125 -19.610 1.00 38.96 ?  11  LYS   B NZ   1 
ATOM   4318 H H    . LYS   B 1 11  ? 36.883 -30.267 -18.843 1.00 25.20 ?  11  LYS   B H    1 
ATOM   4319 H HA   . LYS   B 1 11  ? 35.941 -28.481 -17.111 1.00 28.26 ?  11  LYS   B HA   1 
ATOM   4320 H HB2  . LYS   B 1 11  ? 35.552 -28.431 -19.490 1.00 33.40 ?  11  LYS   B HB2  1 
ATOM   4321 H HB3  . LYS   B 1 11  ? 34.549 -29.640 -19.281 1.00 33.40 ?  11  LYS   B HB3  1 
ATOM   4322 H HG2  . LYS   B 1 11  ? 33.172 -28.245 -18.000 1.00 38.49 ?  11  LYS   B HG2  1 
ATOM   4323 H HG3  . LYS   B 1 11  ? 34.160 -27.031 -18.301 1.00 38.49 ?  11  LYS   B HG3  1 
ATOM   4324 H HD2  . LYS   B 1 11  ? 33.695 -27.340 -20.624 1.00 42.23 ?  11  LYS   B HD2  1 
ATOM   4325 H HD3  . LYS   B 1 11  ? 32.567 -28.380 -20.205 1.00 42.23 ?  11  LYS   B HD3  1 
ATOM   4326 H HE2  . LYS   B 1 11  ? 31.508 -26.396 -20.587 1.00 45.05 ?  11  LYS   B HE2  1 
ATOM   4327 H HE3  . LYS   B 1 11  ? 31.502 -26.614 -19.013 1.00 45.05 ?  11  LYS   B HE3  1 
ATOM   4328 H HZ1  . LYS   B 1 11  ? 32.117 -24.481 -19.535 1.00 46.77 ?  11  LYS   B HZ1  1 
ATOM   4329 H HZ2  . LYS   B 1 11  ? 33.229 -25.135 -18.876 1.00 46.77 ?  11  LYS   B HZ2  1 
ATOM   4330 H HZ3  . LYS   B 1 11  ? 33.245 -24.949 -20.313 1.00 46.77 ?  11  LYS   B HZ3  1 
ATOM   4331 N N    . LEU   B 1 12  ? 34.543 -29.760 -15.537 1.00 20.10 ?  12  LEU   B N    1 
ATOM   4332 C CA   . LEU   B 1 12  ? 33.587 -30.459 -14.686 1.00 19.48 ?  12  LEU   B CA   1 
ATOM   4333 C C    . LEU   B 1 12  ? 32.201 -29.844 -14.771 1.00 19.67 ?  12  LEU   B C    1 
ATOM   4334 O O    . LEU   B 1 12  ? 31.209 -30.556 -14.934 1.00 20.43 ?  12  LEU   B O    1 
ATOM   4335 C CB   . LEU   B 1 12  ? 34.053 -30.478 -13.225 1.00 18.97 ?  12  LEU   B CB   1 
ATOM   4336 C CG   . LEU   B 1 12  ? 35.398 -31.154 -12.961 1.00 18.61 ?  12  LEU   B CG   1 
ATOM   4337 C CD1  . LEU   B 1 12  ? 35.781 -31.079 -11.492 1.00 18.86 ?  12  LEU   B CD1  1 
ATOM   4338 C CD2  . LEU   B 1 12  ? 35.400 -32.597 -13.437 1.00 18.96 ?  12  LEU   B CD2  1 
ATOM   4339 H H    . LEU   B 1 12  ? 34.867 -29.041 -15.178 1.00 24.14 ?  12  LEU   B H    1 
ATOM   4340 H HA   . LEU   B 1 12  ? 33.513 -31.373 -14.989 1.00 23.40 ?  12  LEU   B HA   1 
ATOM   4341 H HB2  . LEU   B 1 12  ? 34.115 -29.566 -12.912 1.00 22.78 ?  12  LEU   B HB2  1 
ATOM   4342 H HB3  . LEU   B 1 12  ? 33.381 -30.952 -12.702 1.00 22.78 ?  12  LEU   B HB3  1 
ATOM   4343 H HG   . LEU   B 1 12  ? 36.076 -30.680 -13.459 1.00 22.36 ?  12  LEU   B HG   1 
ATOM   4344 H HD11 . LEU   B 1 12  ? 36.642 -31.514 -11.368 1.00 22.66 ?  12  LEU   B HD11 1 
ATOM   4345 H HD12 . LEU   B 1 12  ? 35.840 -30.150 -11.223 1.00 22.66 ?  12  LEU   B HD12 1 
ATOM   4346 H HD13 . LEU   B 1 12  ? 35.106 -31.535 -10.962 1.00 22.66 ?  12  LEU   B HD13 1 
ATOM   4347 H HD21 . LEU   B 1 12  ? 36.218 -33.025 -13.145 1.00 22.77 ?  12  LEU   B HD21 1 
ATOM   4348 H HD22 . LEU   B 1 12  ? 34.632 -33.058 -13.060 1.00 22.77 ?  12  LEU   B HD22 1 
ATOM   4349 H HD23 . LEU   B 1 12  ? 35.347 -32.609 -14.406 1.00 22.77 ?  12  LEU   B HD23 1 
ATOM   4350 N N    . THR   B 1 13  ? 32.119 -28.527 -14.644 1.00 19.60 ?  13  THR   B N    1 
ATOM   4351 C CA   . THR   B 1 13  ? 30.899 -27.774 -14.865 1.00 19.72 ?  13  THR   B CA   1 
ATOM   4352 C C    . THR   B 1 13  ? 31.246 -26.595 -15.766 1.00 22.12 ?  13  THR   B C    1 
ATOM   4353 O O    . THR   B 1 13  ? 32.395 -26.425 -16.190 1.00 23.18 ?  13  THR   B O    1 
ATOM   4354 C CB   . THR   B 1 13  ? 30.297 -27.277 -13.546 1.00 19.42 ?  13  THR   B CB   1 
ATOM   4355 O OG1  . THR   B 1 13  ? 31.143 -26.256 -13.007 1.00 18.66 ?  13  THR   B OG1  1 
ATOM   4356 C CG2  . THR   B 1 13  ? 30.172 -28.413 -12.540 1.00 19.29 ?  13  THR   B CG2  1 
ATOM   4357 H H    . THR   B 1 13  ? 32.781 -28.029 -14.413 1.00 23.54 ?  13  THR   B H    1 
ATOM   4358 H HA   . THR   B 1 13  ? 30.241 -28.336 -15.305 1.00 23.69 ?  13  THR   B HA   1 
ATOM   4359 H HB   . THR   B 1 13  ? 29.410 -26.909 -13.709 1.00 23.33 ?  13  THR   B HB   1 
ATOM   4360 H HG1  . THR   B 1 13  ? 30.838 -25.488 -13.212 1.00 22.41 ?  13  THR   B HG1  1 
ATOM   4361 H HG21 . THR   B 1 13  ? 29.677 -28.112 -11.761 1.00 23.17 ?  13  THR   B HG21 1 
ATOM   4362 H HG22 . THR   B 1 13  ? 29.704 -29.158 -12.944 1.00 23.17 ?  13  THR   B HG22 1 
ATOM   4363 H HG23 . THR   B 1 13  ? 31.053 -28.704 -12.261 1.00 23.17 ?  13  THR   B HG23 1 
ATOM   4364 N N    A ASP   B 1 14  ? 30.245 -25.760 -16.041 0.56 23.05 ?  14  ASP   B N    1 
ATOM   4365 N N    B ASP   B 1 14  ? 30.247 -25.757 -16.049 0.44 22.91 ?  14  ASP   B N    1 
ATOM   4366 C CA   A ASP   B 1 14  ? 30.478 -24.618 -16.915 0.56 24.45 ?  14  ASP   B CA   1 
ATOM   4367 C CA   B ASP   B 1 14  ? 30.476 -24.614 -16.925 0.44 24.01 ?  14  ASP   B CA   1 
ATOM   4368 C C    A ASP   B 1 14  ? 31.584 -23.718 -16.380 0.56 22.89 ?  14  ASP   B C    1 
ATOM   4369 C C    B ASP   B 1 14  ? 31.502 -23.638 -16.367 0.44 22.54 ?  14  ASP   B C    1 
ATOM   4370 O O    A ASP   B 1 14  ? 32.287 -23.072 -17.167 0.56 24.33 ?  14  ASP   B O    1 
ATOM   4371 O O    B ASP   B 1 14  ? 32.033 -22.822 -17.128 0.44 23.58 ?  14  ASP   B O    1 
ATOM   4372 C CB   A ASP   B 1 14  ? 29.184 -23.828 -17.110 0.56 27.71 ?  14  ASP   B CB   1 
ATOM   4373 C CB   B ASP   B 1 14  ? 29.171 -23.866 -17.190 0.44 26.85 ?  14  ASP   B CB   1 
ATOM   4374 C CG   A ASP   B 1 14  ? 28.208 -24.520 -18.036 0.56 30.55 ?  14  ASP   B CG   1 
ATOM   4375 C CG   B ASP   B 1 14  ? 28.287 -24.577 -18.194 0.44 29.32 ?  14  ASP   B CG   1 
ATOM   4376 O OD1  A ASP   B 1 14  ? 28.569 -25.553 -18.646 0.56 31.19 ?  14  ASP   B OD1  1 
ATOM   4377 O OD1  B ASP   B 1 14  ? 28.830 -25.275 -19.079 0.44 29.98 ?  14  ASP   B OD1  1 
ATOM   4378 O OD2  A ASP   B 1 14  ? 27.066 -24.030 -18.148 0.56 31.96 -1 14  ASP   B OD2  1 
ATOM   4379 O OD2  B ASP   B 1 14  ? 27.049 -24.446 -18.100 0.44 30.52 -1 14  ASP   B OD2  1 
ATOM   4380 H H    A ASP   B 1 14  ? 29.449 -25.819 -15.725 0.56 27.69 ?  14  ASP   B H    1 
ATOM   4381 H H    B ASP   B 1 14  ? 29.446 -25.823 -15.748 0.44 27.51 ?  14  ASP   B H    1 
ATOM   4382 H HA   A ASP   B 1 14  ? 30.768 -24.934 -17.778 0.56 29.36 ?  14  ASP   B HA   1 
ATOM   4383 H HA   B ASP   B 1 14  ? 30.811 -24.936 -17.774 0.44 28.83 ?  14  ASP   B HA   1 
ATOM   4384 H HB2  A ASP   B 1 14  ? 28.737 -23.725 -16.259 0.56 33.27 ?  14  ASP   B HB2  1 
ATOM   4385 H HB2  B ASP   B 1 14  ? 28.680 -23.785 -16.357 0.44 32.25 ?  14  ASP   B HB2  1 
ATOM   4386 H HB3  A ASP   B 1 14  ? 29.392 -22.960 -17.489 0.56 33.27 ?  14  ASP   B HB3  1 
ATOM   4387 H HB3  B ASP   B 1 14  ? 29.382 -22.980 -17.534 0.44 32.25 ?  14  ASP   B HB3  1 
ATOM   4388 N N    . ASN   B 1 15  ? 31.772 -23.677 -15.058 1.00 20.77 ?  15  ASN   B N    1 
ATOM   4389 C CA   . ASN   B 1 15  ? 32.739 -22.767 -14.453 1.00 17.89 ?  15  ASN   B CA   1 
ATOM   4390 C C    . ASN   B 1 15  ? 33.831 -23.423 -13.616 1.00 16.51 ?  15  ASN   B C    1 
ATOM   4391 O O    . ASN   B 1 15  ? 34.694 -22.700 -13.107 1.00 16.12 ?  15  ASN   B O    1 
ATOM   4392 C CB   . ASN   B 1 15  ? 32.033 -21.713 -13.586 1.00 18.02 ?  15  ASN   B CB   1 
ATOM   4393 C CG   . ASN   B 1 15  ? 31.404 -22.314 -12.346 1.00 18.18 ?  15  ASN   B CG   1 
ATOM   4394 O OD1  . ASN   B 1 15  ? 30.461 -23.107 -12.438 1.00 19.78 ?  15  ASN   B OD1  1 
ATOM   4395 N ND2  . ASN   B 1 15  ? 31.925 -21.964 -11.183 1.00 16.74 ?  15  ASN   B ND2  1 
ATOM   4396 H H    A ASN   B 1 15  ? 31.348 -24.166 -14.492 0.56 24.95 ?  15  ASN   B H    1 
ATOM   4397 H H    B ASN   B 1 15  ? 31.379 -24.195 -14.496 0.44 24.95 ?  15  ASN   B H    1 
ATOM   4398 H HA   . ASN   B 1 15  ? 33.188 -22.278 -15.153 1.00 21.49 ?  15  ASN   B HA   1 
ATOM   4399 H HB2  . ASN   B 1 15  ? 32.683 -21.040 -13.302 1.00 21.64 ?  15  ASN   B HB2  1 
ATOM   4400 H HB3  . ASN   B 1 15  ? 31.332 -21.280 -14.106 1.00 21.64 ?  15  ASN   B HB3  1 
ATOM   4401 H HD21 . ASN   B 1 15  ? 31.600 -22.275 -10.451 1.00 20.10 ?  15  ASN   B HD21 1 
ATOM   4402 H HD22 . ASN   B 1 15  ? 32.597 -21.417 -11.150 1.00 20.10 ?  15  ASN   B HD22 1 
ATOM   4403 N N    . VAL   B 1 16  ? 33.822 -24.744 -13.436 1.00 15.95 ?  16  VAL   B N    1 
ATOM   4404 C CA   . VAL   B 1 16  ? 34.826 -25.435 -12.630 1.00 15.85 ?  16  VAL   B CA   1 
ATOM   4405 C C    . VAL   B 1 16  ? 35.613 -26.378 -13.525 1.00 16.03 ?  16  VAL   B C    1 
ATOM   4406 O O    . VAL   B 1 16  ? 35.034 -27.272 -14.166 1.00 16.61 ?  16  VAL   B O    1 
ATOM   4407 C CB   . VAL   B 1 16  ? 34.206 -26.197 -11.448 1.00 16.60 ?  16  VAL   B CB   1 
ATOM   4408 C CG1  . VAL   B 1 16  ? 35.298 -26.939 -10.657 1.00 16.45 ?  16  VAL   B CG1  1 
ATOM   4409 C CG2  . VAL   B 1 16  ? 33.400 -25.247 -10.557 1.00 17.18 ?  16  VAL   B CG2  1 
ATOM   4410 H H    . VAL   B 1 16  ? 33.219 -25.272 -13.768 1.00 19.16 ?  16  VAL   B H    1 
ATOM   4411 H HA   . VAL   B 1 16  ? 35.437 -24.777 -12.268 1.00 19.04 ?  16  VAL   B HA   1 
ATOM   4412 H HB   . VAL   B 1 16  ? 33.592 -26.864 -11.793 1.00 19.94 ?  16  VAL   B HB   1 
ATOM   4413 H HG11 . VAL   B 1 16  ? 34.927 -27.234 -9.810  1.00 19.76 ?  16  VAL   B HG11 1 
ATOM   4414 H HG12 . VAL   B 1 16  ? 35.601 -27.700 -11.170 1.00 19.76 ?  16  VAL   B HG12 1 
ATOM   4415 H HG13 . VAL   B 1 16  ? 36.037 -26.328 -10.495 1.00 19.76 ?  16  VAL   B HG13 1 
ATOM   4416 H HG21 . VAL   B 1 16  ? 33.069 -25.740 -9.788  1.00 20.63 ?  16  VAL   B HG21 1 
ATOM   4417 H HG22 . VAL   B 1 16  ? 33.969 -24.522 -10.268 1.00 20.63 ?  16  VAL   B HG22 1 
ATOM   4418 H HG23 . VAL   B 1 16  ? 32.649 -24.898 -11.068 1.00 20.63 ?  16  VAL   B HG23 1 
ATOM   4419 N N    . TYR   B 1 17  ? 36.935 -26.199 -13.522 1.00 16.49 ?  17  TYR   B N    1 
ATOM   4420 C CA   . TYR   B 1 17  ? 37.877 -26.962 -14.325 1.00 17.07 ?  17  TYR   B CA   1 
ATOM   4421 C C    . TYR   B 1 17  ? 38.937 -27.571 -13.416 1.00 15.94 ?  17  TYR   B C    1 
ATOM   4422 O O    . TYR   B 1 17  ? 39.222 -27.048 -12.336 1.00 16.20 ?  17  TYR   B O    1 
ATOM   4423 C CB   . TYR   B 1 17  ? 38.575 -26.057 -15.353 1.00 20.34 ?  17  TYR   B CB   1 
ATOM   4424 C CG   . TYR   B 1 17  ? 37.644 -25.289 -16.263 1.00 24.62 ?  17  TYR   B CG   1 
ATOM   4425 C CD1  . TYR   B 1 17  ? 37.098 -24.073 -15.872 1.00 26.37 ?  17  TYR   B CD1  1 
ATOM   4426 C CD2  . TYR   B 1 17  ? 37.316 -25.780 -17.520 1.00 26.78 ?  17  TYR   B CD2  1 
ATOM   4427 C CE1  . TYR   B 1 17  ? 36.246 -23.366 -16.709 1.00 28.29 ?  17  TYR   B CE1  1 
ATOM   4428 C CE2  . TYR   B 1 17  ? 36.470 -25.083 -18.362 1.00 28.39 ?  17  TYR   B CE2  1 
ATOM   4429 C CZ   . TYR   B 1 17  ? 35.935 -23.878 -17.952 1.00 29.27 ?  17  TYR   B CZ   1 
ATOM   4430 O OH   . TYR   B 1 17  ? 35.093 -23.183 -18.791 1.00 30.69 ?  17  TYR   B OH   1 
ATOM   4431 H H    . TYR   B 1 17  ? 37.324 -25.594 -13.039 1.00 19.81 ?  17  TYR   B H    1 
ATOM   4432 H HA   . TYR   B 1 17  ? 37.399 -27.666 -14.797 1.00 20.51 ?  17  TYR   B HA   1 
ATOM   4433 H HB2  . TYR   B 1 17  ? 39.131 -25.418 -14.887 1.00 24.43 ?  17  TYR   B HB2  1 
ATOM   4434 H HB3  . TYR   B 1 17  ? 39.118 -26.618 -15.921 1.00 24.43 ?  17  TYR   B HB3  1 
ATOM   4435 H HD1  . TYR   B 1 17  ? 37.306 -23.725 -15.036 1.00 31.66 ?  17  TYR   B HD1  1 
ATOM   4436 H HD2  . TYR   B 1 17  ? 37.669 -26.591 -17.805 1.00 32.16 ?  17  TYR   B HD2  1 
ATOM   4437 H HE1  . TYR   B 1 17  ? 35.888 -22.553 -16.433 1.00 33.97 ?  17  TYR   B HE1  1 
ATOM   4438 H HE2  . TYR   B 1 17  ? 36.255 -25.426 -19.202 1.00 34.09 ?  17  TYR   B HE2  1 
ATOM   4439 H HH   . TYR   B 1 17  ? 34.846 -22.471 -18.419 1.00 36.85 ?  17  TYR   B HH   1 
ATOM   4440 N N    . ILE   B 1 18  ? 39.534 -28.676 -13.852 1.00 16.15 ?  18  ILE   B N    1 
ATOM   4441 C CA   . ILE   B 1 18  ? 40.459 -29.405 -12.995 1.00 16.48 ?  18  ILE   B CA   1 
ATOM   4442 C C    . ILE   B 1 18  ? 41.615 -29.951 -13.821 1.00 16.29 ?  18  ILE   B C    1 
ATOM   4443 O O    . ILE   B 1 18  ? 41.454 -30.321 -14.988 1.00 17.76 ?  18  ILE   B O    1 
ATOM   4444 C CB   . ILE   B 1 18  ? 39.725 -30.521 -12.198 1.00 16.41 ?  18  ILE   B CB   1 
ATOM   4445 C CG1  . ILE   B 1 18  ? 40.608 -31.070 -11.071 1.00 17.00 ?  18  ILE   B CG1  1 
ATOM   4446 C CG2  . ILE   B 1 18  ? 39.226 -31.640 -13.129 1.00 16.45 ?  18  ILE   B CG2  1 
ATOM   4447 C CD1  . ILE   B 1 18  ? 39.833 -31.873 -10.032 1.00 18.71 ?  18  ILE   B CD1  1 
ATOM   4448 H H    . ILE   B 1 18  ? 39.404 -29.022 -14.624 1.00 19.41 ?  18  ILE   B H    1 
ATOM   4449 H HA   . ILE   B 1 18  ? 40.815 -28.789 -12.340 1.00 19.79 ?  18  ILE   B HA   1 
ATOM   4450 H HB   . ILE   B 1 18  ? 38.939 -30.133 -11.777 1.00 19.72 ?  18  ILE   B HB   1 
ATOM   4451 H HG12 . ILE   B 1 18  ? 41.284 -31.649 -11.451 1.00 20.42 ?  18  ILE   B HG12 1 
ATOM   4452 H HG13 . ILE   B 1 18  ? 41.029 -30.324 -10.613 1.00 20.42 ?  18  ILE   B HG13 1 
ATOM   4453 H HG21 . ILE   B 1 18  ? 38.653 -32.245 -12.627 1.00 19.76 ?  18  ILE   B HG21 1 
ATOM   4454 H HG22 . ILE   B 1 18  ? 38.721 -31.241 -13.856 1.00 19.76 ?  18  ILE   B HG22 1 
ATOM   4455 H HG23 . ILE   B 1 18  ? 39.986 -32.125 -13.482 1.00 19.76 ?  18  ILE   B HG23 1 
ATOM   4456 H HD11 . ILE   B 1 18  ? 40.446 -32.170 -9.339  1.00 22.48 ?  18  ILE   B HD11 1 
ATOM   4457 H HD12 . ILE   B 1 18  ? 39.144 -31.312 -9.644  1.00 22.48 ?  18  ILE   B HD12 1 
ATOM   4458 H HD13 . ILE   B 1 18  ? 39.428 -32.643 -10.463 1.00 22.48 ?  18  ILE   B HD13 1 
ATOM   4459 N N    . LYS   B 1 19  ? 42.787 -30.017 -13.192 1.00 16.82 ?  19  LYS   B N    1 
ATOM   4460 C CA   . LYS   B 1 19  ? 43.995 -30.482 -13.855 1.00 17.70 ?  19  LYS   B CA   1 
ATOM   4461 C C    . LYS   B 1 19  ? 44.901 -31.157 -12.835 1.00 17.82 ?  19  LYS   B C    1 
ATOM   4462 O O    . LYS   B 1 19  ? 44.986 -30.734 -11.681 1.00 16.99 ?  19  LYS   B O    1 
ATOM   4463 C CB   . LYS   B 1 19  ? 44.747 -29.312 -14.497 1.00 19.22 ?  19  LYS   B CB   1 
ATOM   4464 C CG   . LYS   B 1 19  ? 45.926 -29.715 -15.363 1.00 21.52 ?  19  LYS   B CG   1 
ATOM   4465 C CD   . LYS   B 1 19  ? 46.659 -28.486 -15.878 1.00 23.94 ?  19  LYS   B CD   1 
ATOM   4466 C CE   . LYS   B 1 19  ? 47.809 -28.854 -16.792 1.00 26.04 ?  19  LYS   B CE   1 
ATOM   4467 N NZ   . LYS   B 1 19  ? 48.533 -27.654 -17.289 1.00 27.44 ?  19  LYS   B NZ   1 
ATOM   4468 H H    . LYS   B 1 19  ? 42.886 -29.800 -12.366 1.00 20.20 ?  19  LYS   B H    1 
ATOM   4469 H HA   . LYS   B 1 19  ? 43.748 -31.125 -14.542 1.00 21.27 ?  19  LYS   B HA   1 
ATOM   4470 H HB2  . LYS   B 1 19  ? 44.122 -28.826 -15.056 1.00 23.09 ?  19  LYS   B HB2  1 
ATOM   4471 H HB3  . LYS   B 1 19  ? 45.070 -28.736 -13.787 1.00 23.09 ?  19  LYS   B HB3  1 
ATOM   4472 H HG2  . LYS   B 1 19  ? 46.536 -30.252 -14.836 1.00 25.84 ?  19  LYS   B HG2  1 
ATOM   4473 H HG3  . LYS   B 1 19  ? 45.595 -30.227 -16.122 1.00 25.84 ?  19  LYS   B HG3  1 
ATOM   4474 H HD2  . LYS   B 1 19  ? 46.035 -27.931 -16.374 1.00 28.75 ?  19  LYS   B HD2  1 
ATOM   4475 H HD3  . LYS   B 1 19  ? 47.012 -27.992 -15.120 1.00 28.75 ?  19  LYS   B HD3  1 
ATOM   4476 H HE2  . LYS   B 1 19  ? 48.436 -29.409 -16.303 1.00 31.27 ?  19  LYS   B HE2  1 
ATOM   4477 H HE3  . LYS   B 1 19  ? 47.461 -29.340 -17.557 1.00 31.27 ?  19  LYS   B HE3  1 
ATOM   4478 H HZ1  . LYS   B 1 19  ? 49.153 -27.896 -17.880 1.00 32.96 ?  19  LYS   B HZ1  1 
ATOM   4479 H HZ2  . LYS   B 1 19  ? 47.962 -27.094 -17.683 1.00 32.96 ?  19  LYS   B HZ2  1 
ATOM   4480 H HZ3  . LYS   B 1 19  ? 48.928 -27.233 -16.612 1.00 32.96 ?  19  LYS   B HZ3  1 
ATOM   4481 N N    . ASN   B 1 20  ? 45.581 -32.208 -13.271 1.00 18.93 ?  20  ASN   B N    1 
ATOM   4482 C CA   . ASN   B 1 20  ? 46.600 -32.858 -12.451 1.00 20.01 ?  20  ASN   B CA   1 
ATOM   4483 C C    . ASN   B 1 20  ? 47.881 -32.050 -12.622 1.00 20.53 ?  20  ASN   B C    1 
ATOM   4484 O O    . ASN   B 1 20  ? 48.536 -32.124 -13.667 1.00 22.55 ?  20  ASN   B O    1 
ATOM   4485 C CB   . ASN   B 1 20  ? 46.761 -34.310 -12.897 1.00 21.78 ?  20  ASN   B CB   1 
ATOM   4486 C CG   . ASN   B 1 20  ? 47.906 -35.031 -12.203 1.00 23.49 ?  20  ASN   B CG   1 
ATOM   4487 O OD1  . ASN   B 1 20  ? 48.548 -35.909 -12.797 1.00 26.09 ?  20  ASN   B OD1  1 
ATOM   4488 N ND2  . ASN   B 1 20  ? 48.156 -34.695 -10.947 1.00 22.74 ?  20  ASN   B ND2  1 
ATOM   4489 H H    . ASN   B 1 20  ? 45.471 -32.562 -14.045 1.00 22.74 ?  20  ASN   B H    1 
ATOM   4490 H HA   . ASN   B 1 20  ? 46.319 -32.839 -11.519 1.00 24.04 ?  20  ASN   B HA   1 
ATOM   4491 H HB2  . ASN   B 1 20  ? 45.938 -34.789 -12.702 1.00 26.15 ?  20  ASN   B HB2  1 
ATOM   4492 H HB3  . ASN   B 1 20  ? 46.928 -34.321 -13.851 1.00 26.15 ?  20  ASN   B HB3  1 
ATOM   4493 H HD21 . ASN   B 1 20  ? 48.796 -35.072 -10.520 1.00 27.31 ?  20  ASN   B HD21 1 
ATOM   4494 H HD22 . ASN   B 1 20  ? 47.687 -34.081 -10.556 1.00 27.31 ?  20  ASN   B HD22 1 
ATOM   4495 N N    . ALA   B 1 21  ? 48.234 -31.251 -11.611 1.00 20.27 ?  21  ALA   B N    1 
ATOM   4496 C CA   . ALA   B 1 21  ? 49.363 -30.346 -11.766 1.00 21.01 ?  21  ALA   B CA   1 
ATOM   4497 C C    . ALA   B 1 21  ? 49.822 -29.819 -10.414 1.00 19.39 ?  21  ALA   B C    1 
ATOM   4498 O O    . ALA   B 1 21  ? 49.078 -29.824 -9.429  1.00 19.38 ?  21  ALA   B O    1 
ATOM   4499 C CB   . ALA   B 1 21  ? 49.002 -29.194 -12.700 1.00 22.98 ?  21  ALA   B CB   1 
ATOM   4500 H H    . ALA   B 1 21  ? 47.840 -31.221 -10.837 1.00 24.35 ?  21  ALA   B H    1 
ATOM   4501 H HA   . ALA   B 1 21  ? 50.099 -30.841 -12.157 1.00 25.24 ?  21  ALA   B HA   1 
ATOM   4502 H HB1  . ALA   B 1 21  ? 49.796 -28.666 -12.848 1.00 27.60 ?  21  ALA   B HB1  1 
ATOM   4503 H HB2  . ALA   B 1 21  ? 48.687 -29.568 -13.538 1.00 27.60 ?  21  ALA   B HB2  1 
ATOM   4504 H HB3  . ALA   B 1 21  ? 48.306 -28.665 -12.288 1.00 27.60 ?  21  ALA   B HB3  1 
ATOM   4505 N N    . ASP   B 1 22  ? 51.085 -29.383 -10.400 1.00 18.40 ?  22  ASP   B N    1 
ATOM   4506 C CA   . ASP   B 1 22  ? 51.711 -28.672 -9.287  1.00 17.86 ?  22  ASP   B CA   1 
ATOM   4507 C C    . ASP   B 1 22  ? 51.299 -27.203 -9.369  1.00 16.48 ?  22  ASP   B C    1 
ATOM   4508 O O    . ASP   B 1 22  ? 51.606 -26.528 -10.356 1.00 16.50 ?  22  ASP   B O    1 
ATOM   4509 C CB   . ASP   B 1 22  ? 53.230 -28.836 -9.458  1.00 19.21 ?  22  ASP   B CB   1 
ATOM   4510 C CG   . ASP   B 1 22  ? 54.058 -28.085 -8.424  1.00 20.79 ?  22  ASP   B CG   1 
ATOM   4511 O OD1  . ASP   B 1 22  ? 53.696 -26.965 -8.023  1.00 20.44 ?  22  ASP   B OD1  1 
ATOM   4512 O OD2  . ASP   B 1 22  ? 55.125 -28.612 -8.038  1.00 23.13 -1 22  ASP   B OD2  1 
ATOM   4513 H H    . ASP   B 1 22  ? 51.627 -29.501 -11.059 1.00 22.10 ?  22  ASP   B H    1 
ATOM   4514 H HA   . ASP   B 1 22  ? 51.437 -29.045 -8.436  1.00 21.45 ?  22  ASP   B HA   1 
ATOM   4515 H HB2  . ASP   B 1 22  ? 53.461 -29.769 -9.388  1.00 23.08 ?  22  ASP   B HB2  1 
ATOM   4516 H HB3  . ASP   B 1 22  ? 53.487 -28.491 -10.329 1.00 23.08 ?  22  ASP   B HB3  1 
ATOM   4517 N N    . ILE   B 1 23  ? 50.586 -26.712 -8.346  1.00 15.31 ?  23  ILE   B N    1 
ATOM   4518 C CA   . ILE   B 1 23  ? 50.006 -25.365 -8.409  1.00 14.70 ?  23  ILE   B CA   1 
ATOM   4519 C C    . ILE   B 1 23  ? 51.069 -24.282 -8.556  1.00 13.88 ?  23  ILE   B C    1 
ATOM   4520 O O    . ILE   B 1 23  ? 50.811 -23.242 -9.173  1.00 13.78 ?  23  ILE   B O    1 
ATOM   4521 C CB   . ILE   B 1 23  ? 49.071 -25.118 -7.207  1.00 15.15 ?  23  ILE   B CB   1 
ATOM   4522 C CG1  . ILE   B 1 23  ? 48.246 -23.847 -7.408  1.00 15.87 ?  23  ILE   B CG1  1 
ATOM   4523 C CG2  . ILE   B 1 23  ? 49.844 -25.086 -5.908  1.00 15.81 ?  23  ILE   B CG2  1 
ATOM   4524 C CD1  . ILE   B 1 23  ? 47.131 -23.664 -6.375  1.00 16.01 ?  23  ILE   B CD1  1 
ATOM   4525 H H    . ILE   B 1 23  ? 50.422 -27.138 -7.623  1.00 18.39 ?  23  ILE   B H    1 
ATOM   4526 H HA   . ILE   B 1 23  ? 49.454 -25.319 -9.203  1.00 17.67 ?  23  ILE   B HA   1 
ATOM   4527 H HB   . ILE   B 1 23  ? 48.450 -25.864 -7.163  1.00 18.20 ?  23  ILE   B HB   1 
ATOM   4528 H HG12 . ILE   B 1 23  ? 48.841 -23.079 -7.344  1.00 19.07 ?  23  ILE   B HG12 1 
ATOM   4529 H HG13 . ILE   B 1 23  ? 47.840 -23.870 -8.288  1.00 19.07 ?  23  ILE   B HG13 1 
ATOM   4530 H HG21 . ILE   B 1 23  ? 49.220 -25.082 -5.168  1.00 18.99 ?  23  ILE   B HG21 1 
ATOM   4531 H HG22 . ILE   B 1 23  ? 50.412 -25.872 -5.859  1.00 18.99 ?  23  ILE   B HG22 1 
ATOM   4532 H HG23 . ILE   B 1 23  ? 50.391 -24.284 -5.886  1.00 18.99 ?  23  ILE   B HG23 1 
ATOM   4533 H HD11 . ILE   B 1 23  ? 46.614 -22.879 -6.608  1.00 19.24 ?  23  ILE   B HD11 1 
ATOM   4534 H HD12 . ILE   B 1 23  ? 46.567 -24.451 -6.384  1.00 19.24 ?  23  ILE   B HD12 1 
ATOM   4535 H HD13 . ILE   B 1 23  ? 47.531 -23.551 -5.498  1.00 19.24 ?  23  ILE   B HD13 1 
ATOM   4536 N N    . VAL   B 1 24  ? 52.263 -24.489 -7.991  1.00 14.19 ?  24  VAL   B N    1 
ATOM   4537 C CA   . VAL   B 1 24  ? 53.339 -23.511 -8.153  1.00 15.34 ?  24  VAL   B CA   1 
ATOM   4538 C C    . VAL   B 1 24  ? 53.797 -23.465 -9.602  1.00 15.60 ?  24  VAL   B C    1 
ATOM   4539 O O    . VAL   B 1 24  ? 53.940 -22.390 -10.194 1.00 16.06 ?  24  VAL   B O    1 
ATOM   4540 C CB   . VAL   B 1 24  ? 54.512 -23.833 -7.210  1.00 16.26 ?  24  VAL   B CB   1 
ATOM   4541 C CG1  . VAL   B 1 24  ? 55.716 -22.952 -7.529  1.00 16.91 ?  24  VAL   B CG1  1 
ATOM   4542 C CG2  . VAL   B 1 24  ? 54.089 -23.673 -5.768  1.00 16.90 ?  24  VAL   B CG2  1 
ATOM   4543 H H    . VAL   B 1 24  ? 52.470 -25.173 -7.513  1.00 17.05 ?  24  VAL   B H    1 
ATOM   4544 H HA   . VAL   B 1 24  ? 53.003 -22.632 -7.915  1.00 18.43 ?  24  VAL   B HA   1 
ATOM   4545 H HB   . VAL   B 1 24  ? 54.778 -24.757 -7.337  1.00 19.53 ?  24  VAL   B HB   1 
ATOM   4546 H HG11 . VAL   B 1 24  ? 56.312 -22.945 -6.764  1.00 20.31 ?  24  VAL   B HG11 1 
ATOM   4547 H HG12 . VAL   B 1 24  ? 56.173 -23.311 -8.303  1.00 20.31 ?  24  VAL   B HG12 1 
ATOM   4548 H HG13 . VAL   B 1 24  ? 55.405 -22.050 -7.711  1.00 20.31 ?  24  VAL   B HG13 1 
ATOM   4549 H HG21 . VAL   B 1 24  ? 54.824 -23.931 -5.191  1.00 20.30 ?  24  VAL   B HG21 1 
ATOM   4550 H HG22 . VAL   B 1 24  ? 53.855 -22.744 -5.610  1.00 20.30 ?  24  VAL   B HG22 1 
ATOM   4551 H HG23 . VAL   B 1 24  ? 53.320 -24.240 -5.598  1.00 20.30 ?  24  VAL   B HG23 1 
ATOM   4552 N N    A GLU   B 1 25  ? 54.052 -24.634 -10.193 0.56 16.46 ?  25  GLU   B N    1 
ATOM   4553 N N    B GLU   B 1 25  ? 54.035 -24.635 -10.198 0.44 16.55 ?  25  GLU   B N    1 
ATOM   4554 C CA   A GLU   B 1 25  ? 54.457 -24.660 -11.593 0.56 18.03 ?  25  GLU   B CA   1 
ATOM   4555 C CA   B GLU   B 1 25  ? 54.426 -24.670 -11.602 0.44 18.09 ?  25  GLU   B CA   1 
ATOM   4556 C C    A GLU   B 1 25  ? 53.346 -24.137 -12.491 0.56 16.79 ?  25  GLU   B C    1 
ATOM   4557 C C    B GLU   B 1 25  ? 53.311 -24.142 -12.494 0.44 17.22 ?  25  GLU   B C    1 
ATOM   4558 O O    A GLU   B 1 25  ? 53.610 -23.417 -13.462 0.56 17.42 ?  25  GLU   B O    1 
ATOM   4559 O O    B GLU   B 1 25  ? 53.573 -23.428 -13.469 0.44 17.66 ?  25  GLU   B O    1 
ATOM   4560 C CB   A GLU   B 1 25  ? 54.892 -26.068 -11.992 0.56 21.82 ?  25  GLU   B CB   1 
ATOM   4561 C CB   B GLU   B 1 25  ? 54.836 -26.088 -11.997 0.44 21.29 ?  25  GLU   B CB   1 
ATOM   4562 C CG   A GLU   B 1 25  ? 56.163 -26.519 -11.283 0.56 25.97 ?  25  GLU   B CG   1 
ATOM   4563 C CG   B GLU   B 1 25  ? 56.121 -26.549 -11.323 0.44 24.80 ?  25  GLU   B CG   1 
ATOM   4564 C CD   A GLU   B 1 25  ? 57.276 -25.476 -11.331 0.56 29.48 ?  25  GLU   B CD   1 
ATOM   4565 C CD   B GLU   B 1 25  ? 57.285 -25.600 -11.550 0.44 27.71 ?  25  GLU   B CD   1 
ATOM   4566 O OE1  A GLU   B 1 25  ? 57.666 -25.060 -12.445 0.56 31.15 ?  25  GLU   B OE1  1 
ATOM   4567 O OE1  B GLU   B 1 25  ? 57.693 -25.439 -12.720 0.44 29.12 ?  25  GLU   B OE1  1 
ATOM   4568 O OE2  A GLU   B 1 25  ? 57.751 -25.052 -10.252 0.56 30.74 -1 25  GLU   B OE2  1 
ATOM   4569 O OE2  B GLU   B 1 25  ? 57.789 -25.008 -10.567 0.44 28.81 -1 25  GLU   B OE2  1 
ATOM   4570 H H    A GLU   B 1 25  ? 53.994 -25.401 -9.816  0.56 19.77 ?  25  GLU   B H    1 
ATOM   4571 H H    B GLU   B 1 25  ? 53.974 -25.401 -9.818  0.44 19.88 ?  25  GLU   B H    1 
ATOM   4572 H HA   A GLU   B 1 25  ? 55.204 -24.058 -11.709 0.56 21.66 ?  25  GLU   B HA   1 
ATOM   4573 H HA   B GLU   B 1 25  ? 55.184 -24.083 -11.727 0.44 21.73 ?  25  GLU   B HA   1 
ATOM   4574 H HB2  A GLU   B 1 25  ? 54.183 -26.692 -11.763 0.56 26.20 ?  25  GLU   B HB2  1 
ATOM   4575 H HB2  B GLU   B 1 25  ? 54.128 -26.701 -11.739 0.44 25.57 ?  25  GLU   B HB2  1 
ATOM   4576 H HB3  A GLU   B 1 25  ? 55.053 -26.088 -12.947 0.56 26.20 ?  25  GLU   B HB3  1 
ATOM   4577 H HB3  B GLU   B 1 25  ? 54.968 -26.121 -12.956 0.44 25.57 ?  25  GLU   B HB3  1 
ATOM   4578 H HG2  A GLU   B 1 25  ? 55.963 -26.686 -10.352 0.56 31.19 ?  25  GLU   B HG2  1 
ATOM   4579 H HG2  B GLU   B 1 25  ? 55.968 -26.626 -10.371 0.44 29.79 ?  25  GLU   B HG2  1 
ATOM   4580 H HG3  A GLU   B 1 25  ? 56.487 -27.328 -11.708 0.56 31.19 ?  25  GLU   B HG3  1 
ATOM   4581 H HG3  B GLU   B 1 25  ? 56.383 -27.401 -11.696 0.44 29.79 ?  25  GLU   B HG3  1 
ATOM   4582 N N    A GLU   B 1 26  ? 52.093 -24.464 -12.166 0.56 15.52 ?  26  GLU   B N    1 
ATOM   4583 N N    B GLU   B 1 26  ? 52.057 -24.467 -12.164 0.44 16.31 ?  26  GLU   B N    1 
ATOM   4584 C CA   A GLU   B 1 26  ? 50.965 -23.938 -12.930 0.56 16.37 ?  26  GLU   B CA   1 
ATOM   4585 C CA   B GLU   B 1 26  ? 50.931 -23.940 -12.929 0.44 16.92 ?  26  GLU   B CA   1 
ATOM   4586 C C    A GLU   B 1 26  ? 50.921 -22.420 -12.857 0.56 15.54 ?  26  GLU   B C    1 
ATOM   4587 C C    B GLU   B 1 26  ? 50.879 -22.423 -12.851 0.44 15.72 ?  26  GLU   B C    1 
ATOM   4588 O O    A GLU   B 1 26  ? 50.755 -21.744 -13.877 0.56 16.74 ?  26  GLU   B O    1 
ATOM   4589 O O    B GLU   B 1 26  ? 50.662 -21.750 -13.863 0.44 16.62 ?  26  GLU   B O    1 
ATOM   4590 C CB   A GLU   B 1 26  ? 49.654 -24.526 -12.407 0.56 17.61 ?  26  GLU   B CB   1 
ATOM   4591 C CB   B GLU   B 1 26  ? 49.616 -24.531 -12.416 0.44 18.33 ?  26  GLU   B CB   1 
ATOM   4592 C CG   A GLU   B 1 26  ? 49.307 -25.875 -12.994 0.56 19.80 ?  26  GLU   B CG   1 
ATOM   4593 C CG   B GLU   B 1 26  ? 49.139 -25.749 -13.181 0.44 20.56 ?  26  GLU   B CG   1 
ATOM   4594 C CD   A GLU   B 1 26  ? 49.137 -25.857 -14.507 0.56 20.84 ?  26  GLU   B CD   1 
ATOM   4595 C CD   B GLU   B 1 26  ? 48.822 -25.426 -14.639 0.44 21.35 ?  26  GLU   B CD   1 
ATOM   4596 O OE1  A GLU   B 1 26  ? 48.313 -25.071 -15.023 0.56 20.56 ?  26  GLU   B OE1  1 
ATOM   4597 O OE1  B GLU   B 1 26  ? 47.741 -24.860 -14.922 0.44 22.48 ?  26  GLU   B OE1  1 
ATOM   4598 O OE2  A GLU   B 1 26  ? 49.831 -26.644 -15.177 0.56 21.75 -1 26  GLU   B OE2  1 
ATOM   4599 O OE2  B GLU   B 1 26  ? 49.663 -25.726 -15.500 0.44 20.76 -1 26  GLU   B OE2  1 
ATOM   4600 H H    A GLU   B 1 26  ? 51.868 -24.985 -11.517 0.56 18.64 ?  26  GLU   B H    1 
ATOM   4601 H H    B GLU   B 1 26  ? 51.835 -24.982 -11.512 0.44 19.60 ?  26  GLU   B H    1 
ATOM   4602 H HA   A GLU   B 1 26  ? 51.062 -24.192 -13.858 0.56 19.67 ?  26  GLU   B HA   1 
ATOM   4603 H HA   B GLU   B 1 26  ? 51.037 -24.188 -13.859 0.44 20.32 ?  26  GLU   B HA   1 
ATOM   4604 H HB2  A GLU   B 1 26  ? 49.721 -24.632 -11.440 0.56 21.16 ?  26  GLU   B HB2  1 
ATOM   4605 H HB2  B GLU   B 1 26  ? 49.727 -24.785 -11.488 0.44 22.02 ?  26  GLU   B HB2  1 
ATOM   4606 H HB3  A GLU   B 1 26  ? 48.929 -23.912 -12.611 0.56 21.16 ?  26  GLU   B HB3  1 
ATOM   4607 H HB3  B GLU   B 1 26  ? 48.922 -23.853 -12.488 0.44 22.02 ?  26  GLU   B HB3  1 
ATOM   4608 H HG2  A GLU   B 1 26  ? 50.029 -26.479 -12.802 0.56 23.78 ?  26  GLU   B HG2  1 
ATOM   4609 H HG2  B GLU   B 1 26  ? 49.828 -26.435 -13.123 0.44 24.70 ?  26  GLU   B HG2  1 
ATOM   4610 H HG3  A GLU   B 1 26  ? 48.481 -26.180 -12.591 0.56 23.78 ?  26  GLU   B HG3  1 
ATOM   4611 H HG3  B GLU   B 1 26  ? 48.319 -26.071 -12.781 0.44 24.70 ?  26  GLU   B HG3  1 
ATOM   4612 N N    . ALA   B 1 27  ? 51.063 -21.867 -11.652 1.00 14.70 ?  27  ALA   B N    1 
ATOM   4613 C CA   . ALA   B 1 27  ? 51.024 -20.419 -11.504 1.00 14.63 ?  27  ALA   B CA   1 
ATOM   4614 C C    . ALA   B 1 27  ? 52.098 -19.757 -12.358 1.00 15.77 ?  27  ALA   B C    1 
ATOM   4615 O O    . ALA   B 1 27  ? 51.841 -18.750 -13.034 1.00 15.94 ?  27  ALA   B O    1 
ATOM   4616 C CB   . ALA   B 1 27  ? 51.170 -20.037 -10.030 1.00 14.65 ?  27  ALA   B CB   1 
ATOM   4617 H H    A ALA   B 1 27  ? 51.183 -22.306 -10.920 0.56 17.66 ?  27  ALA   B H    1 
ATOM   4618 H H    B ALA   B 1 27  ? 51.202 -22.306 -10.923 0.44 17.66 ?  27  ALA   B H    1 
ATOM   4619 H HA   . ALA   B 1 27  ? 50.169 -20.095 -11.809 1.00 17.57 ?  27  ALA   B HA   1 
ATOM   4620 H HB1  . ALA   B 1 27  ? 51.134 -19.070 -9.949  1.00 17.60 ?  27  ALA   B HB1  1 
ATOM   4621 H HB2  . ALA   B 1 27  ? 50.433 -20.432 -9.529  1.00 17.60 ?  27  ALA   B HB2  1 
ATOM   4622 H HB3  . ALA   B 1 27  ? 52.012 -20.369 -9.691  1.00 17.60 ?  27  ALA   B HB3  1 
ATOM   4623 N N    . LYS   B 1 28  ? 53.309 -20.318 -12.359 1.00 17.31 ?  28  LYS   B N    1 
ATOM   4624 C CA   . LYS   B 1 28  ? 54.382 -19.703 -13.131 1.00 19.54 ?  28  LYS   B CA   1 
ATOM   4625 C C    . LYS   B 1 28  ? 54.121 -19.793 -14.628 1.00 20.56 ?  28  LYS   B C    1 
ATOM   4626 O O    . LYS   B 1 28  ? 54.539 -18.904 -15.380 1.00 21.50 ?  28  LYS   B O    1 
ATOM   4627 C CB   . LYS   B 1 28  ? 55.740 -20.295 -12.735 1.00 22.20 ?  28  LYS   B CB   1 
ATOM   4628 C CG   . LYS   B 1 28  ? 56.122 -19.964 -11.294 1.00 25.52 ?  28  LYS   B CG   1 
ATOM   4629 C CD   . LYS   B 1 28  ? 57.553 -20.355 -10.945 1.00 29.32 ?  28  LYS   B CD   1 
ATOM   4630 C CE   . LYS   B 1 28  ? 57.679 -21.837 -10.691 1.00 33.06 ?  28  LYS   B CE   1 
ATOM   4631 N NZ   . LYS   B 1 28  ? 59.042 -22.190 -10.197 1.00 36.76 ?  28  LYS   B NZ   1 
ATOM   4632 H H    . LYS   B 1 28  ? 53.531 -21.037 -11.936 1.00 20.80 ?  28  LYS   B H    1 
ATOM   4633 H HA   . LYS   B 1 28  ? 54.414 -18.763 -12.913 1.00 23.47 ?  28  LYS   B HA   1 
ATOM   4634 H HB2  . LYS   B 1 28  ? 55.712 -21.259 -12.821 1.00 26.67 ?  28  LYS   B HB2  1 
ATOM   4635 H HB3  . LYS   B 1 28  ? 56.432 -19.930 -13.315 1.00 26.67 ?  28  LYS   B HB3  1 
ATOM   4636 H HG2  . LYS   B 1 28  ? 56.029 -19.007 -11.159 1.00 30.65 ?  28  LYS   B HG2  1 
ATOM   4637 H HG3  . LYS   B 1 28  ? 55.526 -20.441 -10.697 1.00 30.65 ?  28  LYS   B HG3  1 
ATOM   4638 H HD2  . LYS   B 1 28  ? 58.135 -20.118 -11.684 1.00 35.21 ?  28  LYS   B HD2  1 
ATOM   4639 H HD3  . LYS   B 1 28  ? 57.821 -19.881 -10.142 1.00 35.21 ?  28  LYS   B HD3  1 
ATOM   4640 H HE2  . LYS   B 1 28  ? 57.032 -22.103 -10.018 1.00 39.69 ?  28  LYS   B HE2  1 
ATOM   4641 H HE3  . LYS   B 1 28  ? 57.520 -22.319 -11.518 1.00 39.69 ?  28  LYS   B HE3  1 
ATOM   4642 H HZ1  . LYS   B 1 28  ? 59.096 -23.066 -10.053 1.00 44.13 ?  28  LYS   B HZ1  1 
ATOM   4643 H HZ2  . LYS   B 1 28  ? 59.653 -21.956 -10.801 1.00 44.13 ?  28  LYS   B HZ2  1 
ATOM   4644 H HZ3  . LYS   B 1 28  ? 59.209 -21.760 -9.435  1.00 44.13 ?  28  LYS   B HZ3  1 
ATOM   4645 N N    A LYS   B 1 29  ? 53.429 -20.844 -15.079 0.56 21.65 ?  29  LYS   B N    1 
ATOM   4646 N N    B LYS   B 1 29  ? 53.398 -20.821 -15.072 0.44 21.72 ?  29  LYS   B N    1 
ATOM   4647 C CA   A LYS   B 1 29  ? 53.140 -20.984 -16.504 0.56 23.56 ?  29  LYS   B CA   1 
ATOM   4648 C CA   B LYS   B 1 29  ? 53.135 -20.991 -16.495 0.44 23.49 ?  29  LYS   B CA   1 
ATOM   4649 C C    A LYS   B 1 29  ? 51.901 -20.193 -16.916 0.56 22.70 ?  29  LYS   B C    1 
ATOM   4650 C C    B LYS   B 1 29  ? 51.877 -20.260 -16.949 0.44 22.60 ?  29  LYS   B C    1 
ATOM   4651 O O    A LYS   B 1 29  ? 51.919 -19.499 -17.939 0.56 24.19 ?  29  LYS   B O    1 
ATOM   4652 O O    B LYS   B 1 29  ? 51.852 -19.696 -18.048 0.44 23.63 ?  29  LYS   B O    1 
ATOM   4653 C CB   A LYS   B 1 29  ? 52.990 -22.462 -16.872 0.56 27.02 ?  29  LYS   B CB   1 
ATOM   4654 C CB   B LYS   B 1 29  ? 53.022 -22.480 -16.832 0.44 26.68 ?  29  LYS   B CB   1 
ATOM   4655 C CG   A LYS   B 1 29  ? 52.796 -22.719 -18.360 0.56 30.02 ?  29  LYS   B CG   1 
ATOM   4656 C CG   B LYS   B 1 29  ? 52.882 -22.770 -18.316 0.44 29.47 ?  29  LYS   B CG   1 
ATOM   4657 C CD   A LYS   B 1 29  ? 52.994 -24.189 -18.690 0.56 32.49 ?  29  LYS   B CD   1 
ATOM   4658 C CD   B LYS   B 1 29  ? 53.019 -24.260 -18.615 0.44 31.73 ?  29  LYS   B CD   1 
ATOM   4659 C CE   A LYS   B 1 29  ? 51.944 -25.055 -18.015 0.56 34.35 ?  29  LYS   B CE   1 
ATOM   4660 C CE   B LYS   B 1 29  ? 51.822 -25.059 -18.118 0.44 33.45 ?  29  LYS   B CE   1 
ATOM   4661 N NZ   A LYS   B 1 29  ? 52.141 -26.495 -18.328 0.56 35.44 ?  29  LYS   B NZ   1 
ATOM   4662 N NZ   B LYS   B 1 29  ? 51.967 -26.518 -18.407 0.44 34.40 ?  29  LYS   B NZ   1 
ATOM   4663 H H    A LYS   B 1 29  ? 53.129 -21.485 -14.585 0.56 26.00 ?  29  LYS   B H    1 
ATOM   4664 H H    B LYS   B 1 29  ? 53.041 -21.424 -14.566 0.44 26.09 ?  29  LYS   B H    1 
ATOM   4665 H HA   A LYS   B 1 29  ? 53.882 -20.634 -17.007 0.56 28.29 ?  29  LYS   B HA   1 
ATOM   4666 H HA   B LYS   B 1 29  ? 53.882 -20.629 -16.989 0.44 28.21 ?  29  LYS   B HA   1 
ATOM   4667 H HB2  A LYS   B 1 29  ? 53.793 -22.939 -16.599 0.56 32.44 ?  29  LYS   B HB2  1 
ATOM   4668 H HB2  B LYS   B 1 29  ? 53.822 -22.927 -16.518 0.44 32.04 ?  29  LYS   B HB2  1 
ATOM   4669 H HB3  A LYS   B 1 29  ? 52.222 -22.829 -16.410 0.56 32.44 ?  29  LYS   B HB3  1 
ATOM   4670 H HB3  B LYS   B 1 29  ? 52.244 -22.842 -16.385 0.44 32.04 ?  29  LYS   B HB3  1 
ATOM   4671 H HG2  A LYS   B 1 29  ? 51.894 -22.469 -18.618 0.56 36.05 ?  29  LYS   B HG2  1 
ATOM   4672 H HG2  B LYS   B 1 29  ? 52.008 -22.477 -18.616 0.44 35.38 ?  29  LYS   B HG2  1 
ATOM   4673 H HG3  A LYS   B 1 29  ? 53.445 -22.204 -18.867 0.56 36.05 ?  29  LYS   B HG3  1 
ATOM   4674 H HG3  B LYS   B 1 29  ? 53.578 -22.297 -18.800 0.44 35.38 ?  29  LYS   B HG3  1 
ATOM   4675 H HD2  A LYS   B 1 29  ? 52.924 -24.318 -19.649 0.56 39.01 ?  29  LYS   B HD2  1 
ATOM   4676 H HD2  B LYS   B 1 29  ? 53.089 -24.386 -19.574 0.44 38.10 ?  29  LYS   B HD2  1 
ATOM   4677 H HD3  A LYS   B 1 29  ? 53.868 -24.473 -18.377 0.56 39.01 ?  29  LYS   B HD3  1 
ATOM   4678 H HD3  B LYS   B 1 29  ? 53.813 -24.602 -18.175 0.44 38.10 ?  29  LYS   B HD3  1 
ATOM   4679 H HE2  A LYS   B 1 29  ? 52.004 -24.946 -17.053 0.56 41.24 ?  29  LYS   B HE2  1 
ATOM   4680 H HE2  B LYS   B 1 29  ? 51.739 -24.949 -17.158 0.44 40.16 ?  29  LYS   B HE2  1 
ATOM   4681 H HE3  A LYS   B 1 29  ? 51.064 -24.790 -18.328 0.56 41.24 ?  29  LYS   B HE3  1 
ATOM   4682 H HE3  B LYS   B 1 29  ? 51.019 -24.742 -18.562 0.44 40.16 ?  29  LYS   B HE3  1 
ATOM   4683 H HZ1  A LYS   B 1 29  ? 51.516 -26.981 -17.923 0.56 42.56 ?  29  LYS   B HZ1  1 
ATOM   4684 H HZ1  B LYS   B 1 29  ? 51.255 -26.961 -18.107 0.44 41.30 ?  29  LYS   B HZ1  1 
ATOM   4685 H HZ2  A LYS   B 1 29  ? 52.086 -26.625 -19.207 0.56 42.56 ?  29  LYS   B HZ2  1 
ATOM   4686 H HZ2  B LYS   B 1 29  ? 52.040 -26.649 -19.284 0.44 41.30 ?  29  LYS   B HZ2  1 
ATOM   4687 H HZ3  A LYS   B 1 29  ? 52.942 -26.760 -18.046 0.56 42.56 ?  29  LYS   B HZ3  1 
ATOM   4688 H HZ3  B LYS   B 1 29  ? 52.695 -26.837 -18.006 0.44 41.30 ?  29  LYS   B HZ3  1 
ATOM   4689 N N    . VAL   B 1 30  ? 50.824 -20.281 -16.129 1.00 21.21 ?  30  VAL   B N    1 
ATOM   4690 C CA   . VAL   B 1 30  ? 49.547 -19.660 -16.501 1.00 20.90 ?  30  VAL   B CA   1 
ATOM   4691 C C    . VAL   B 1 30  ? 49.562 -18.149 -16.331 1.00 19.54 ?  30  VAL   B C    1 
ATOM   4692 O O    . VAL   B 1 30  ? 48.830 -17.429 -17.030 1.00 20.61 ?  30  VAL   B O    1 
ATOM   4693 C CB   . VAL   B 1 30  ? 48.442 -20.275 -15.620 1.00 22.23 ?  30  VAL   B CB   1 
ATOM   4694 C CG1  . VAL   B 1 30  ? 47.166 -19.454 -15.678 1.00 22.84 ?  30  VAL   B CG1  1 
ATOM   4695 C CG2  . VAL   B 1 30  ? 48.187 -21.716 -16.022 1.00 23.20 ?  30  VAL   B CG2  1 
ATOM   4696 H H    A VAL   B 1 30  ? 50.804 -20.695 -15.370 0.56 25.47 ?  30  VAL   B H    1 
ATOM   4697 H H    B VAL   B 1 30  ? 50.806 -20.690 -15.367 0.44 25.47 ?  30  VAL   B H    1 
ATOM   4698 H HA   . VAL   B 1 30  ? 49.346 -19.878 -17.424 1.00 25.10 ?  30  VAL   B HA   1 
ATOM   4699 H HB   . VAL   B 1 30  ? 48.744 -20.286 -14.697 1.00 26.70 ?  30  VAL   B HB   1 
ATOM   4700 H HG11 . VAL   B 1 30  ? 46.421 -20.033 -15.449 1.00 27.42 ?  30  VAL   B HG11 1 
ATOM   4701 H HG12 . VAL   B 1 30  ? 47.225 -18.730 -15.040 1.00 27.42 ?  30  VAL   B HG12 1 
ATOM   4702 H HG13 . VAL   B 1 30  ? 47.047 -19.116 -16.573 1.00 27.42 ?  30  VAL   B HG13 1 
ATOM   4703 H HG21 . VAL   B 1 30  ? 47.495 -22.092 -15.449 1.00 27.86 ?  30  VAL   B HG21 1 
ATOM   4704 H HG22 . VAL   B 1 30  ? 47.890 -21.740 -16.947 1.00 27.86 ?  30  VAL   B HG22 1 
ATOM   4705 H HG23 . VAL   B 1 30  ? 49.005 -22.226 -15.925 1.00 27.86 ?  30  VAL   B HG23 1 
ATOM   4706 N N    A LYS   B 1 31  ? 50.372 -17.648 -15.406 0.56 19.09 ?  31  LYS   B N    1 
ATOM   4707 N N    B LYS   B 1 31  ? 50.345 -17.653 -15.383 0.44 19.32 ?  31  LYS   B N    1 
ATOM   4708 C CA   A LYS   B 1 31  ? 50.390 -16.236 -15.040 0.56 19.32 ?  31  LYS   B CA   1 
ATOM   4709 C CA   B LYS   B 1 31  ? 50.388 -16.240 -15.038 0.44 19.52 ?  31  LYS   B CA   1 
ATOM   4710 C C    A LYS   B 1 31  ? 48.995 -15.731 -14.659 0.56 17.48 ?  31  LYS   B C    1 
ATOM   4711 C C    B LYS   B 1 31  ? 48.987 -15.754 -14.677 0.44 17.49 ?  31  LYS   B C    1 
ATOM   4712 O O    A LYS   B 1 31  ? 48.472 -14.800 -15.281 0.56 17.90 ?  31  LYS   B O    1 
ATOM   4713 O O    B LYS   B 1 31  ? 48.445 -14.857 -15.338 0.44 17.55 ?  31  LYS   B O    1 
ATOM   4714 C CB   A LYS   B 1 31  ? 51.010 -15.386 -16.139 0.56 21.96 ?  31  LYS   B CB   1 
ATOM   4715 C CB   B LYS   B 1 31  ? 51.020 -15.445 -16.182 0.44 22.09 ?  31  LYS   B CB   1 
ATOM   4716 C CG   A LYS   B 1 31  ? 52.450 -15.785 -16.450 0.56 24.54 ?  31  LYS   B CG   1 
ATOM   4717 C CG   B LYS   B 1 31  ? 52.433 -15.917 -16.513 0.44 24.29 ?  31  LYS   B CG   1 
ATOM   4718 C CD   A LYS   B 1 31  ? 53.023 -14.991 -17.608 0.56 27.35 ?  31  LYS   B CD   1 
ATOM   4719 C CD   B LYS   B 1 31  ? 53.003 -15.215 -17.731 0.44 26.62 ?  31  LYS   B CD   1 
ATOM   4720 C CE   A LYS   B 1 31  ? 54.501 -15.279 -17.796 0.56 29.32 ?  31  LYS   B CE   1 
ATOM   4721 C CE   B LYS   B 1 31  ? 54.491 -15.476 -17.868 0.44 28.52 ?  31  LYS   B CE   1 
ATOM   4722 N NZ   A LYS   B 1 31  ? 55.298 -14.882 -16.600 0.56 30.62 ?  31  LYS   B NZ   1 
ATOM   4723 N NZ   B LYS   B 1 31  ? 55.224 -15.075 -16.635 0.44 29.75 ?  31  LYS   B NZ   1 
ATOM   4724 H H    A LYS   B 1 31  ? 50.945 -18.126 -14.972 0.56 22.92 ?  31  LYS   B H    1 
ATOM   4725 H H    B LYS   B 1 31  ? 50.880 -18.138 -14.919 0.44 23.21 ?  31  LYS   B H    1 
ATOM   4726 H HA   A LYS   B 1 31  ? 50.948 -16.148 -14.261 0.56 23.20 ?  31  LYS   B HA   1 
ATOM   4727 H HA   B LYS   B 1 31  ? 50.950 -16.138 -14.259 0.44 23.44 ?  31  LYS   B HA   1 
ATOM   4728 H HB2  A LYS   B 1 31  ? 50.494 -15.484 -16.953 0.56 26.38 ?  31  LYS   B HB2  1 
ATOM   4729 H HB2  B LYS   B 1 31  ? 50.482 -15.542 -16.981 0.44 26.54 ?  31  LYS   B HB2  1 
ATOM   4730 H HB3  A LYS   B 1 31  ? 51.015 -14.461 -15.853 0.56 26.38 ?  31  LYS   B HB3  1 
ATOM   4731 H HB3  B LYS   B 1 31  ? 51.075 -14.512 -15.925 0.44 26.54 ?  31  LYS   B HB3  1 
ATOM   4732 H HG2  A LYS   B 1 31  ? 52.999 -15.621 -15.667 0.56 29.47 ?  31  LYS   B HG2  1 
ATOM   4733 H HG2  B LYS   B 1 31  ? 53.008 -15.736 -15.753 0.44 29.17 ?  31  LYS   B HG2  1 
ATOM   4734 H HG3  A LYS   B 1 31  ? 52.477 -16.726 -16.685 0.56 29.47 ?  31  LYS   B HG3  1 
ATOM   4735 H HG3  B LYS   B 1 31  ? 52.418 -16.870 -16.697 0.44 29.17 ?  31  LYS   B HG3  1 
ATOM   4736 H HD2  A LYS   B 1 31  ? 52.556 -15.239 -18.422 0.56 32.84 ?  31  LYS   B HD2  1 
ATOM   4737 H HD2  B LYS   B 1 31  ? 52.560 -15.547 -18.527 0.44 31.96 ?  31  LYS   B HD2  1 
ATOM   4738 H HD3  A LYS   B 1 31  ? 52.913 -14.046 -17.429 0.56 32.84 ?  31  LYS   B HD3  1 
ATOM   4739 H HD3  B LYS   B 1 31  ? 52.867 -14.260 -17.641 0.44 31.96 ?  31  LYS   B HD3  1 
ATOM   4740 H HE2  A LYS   B 1 31  ? 54.628 -16.231 -17.942 0.56 35.21 ?  31  LYS   B HE2  1 
ATOM   4741 H HE2  B LYS   B 1 31  ? 54.640 -16.423 -18.018 0.44 34.25 ?  31  LYS   B HE2  1 
ATOM   4742 H HE3  A LYS   B 1 31  ? 54.829 -14.777 -18.558 0.56 35.21 ?  31  LYS   B HE3  1 
ATOM   4743 H HE3  B LYS   B 1 31  ? 54.840 -14.959 -18.612 0.44 34.25 ?  31  LYS   B HE3  1 
ATOM   4744 H HZ1  A LYS   B 1 31  ? 56.167 -14.984 -16.765 0.56 36.76 ?  31  LYS   B HZ1  1 
ATOM   4745 H HZ1  B LYS   B 1 31  ? 56.099 -15.055 -16.794 0.44 35.72 ?  31  LYS   B HZ1  1 
ATOM   4746 H HZ2  A LYS   B 1 31  ? 55.139 -14.031 -16.398 0.56 36.76 ?  31  LYS   B HZ2  1 
ATOM   4747 H HZ2  B LYS   B 1 31  ? 54.959 -14.266 -16.374 0.44 35.72 ?  31  LYS   B HZ2  1 
ATOM   4748 H HZ3  A LYS   B 1 31  ? 55.076 -15.391 -15.903 0.56 36.76 ?  31  LYS   B HZ3  1 
ATOM   4749 H HZ3  B LYS   B 1 31  ? 55.062 -15.657 -15.981 0.44 35.72 ?  31  LYS   B HZ3  1 
ATOM   4750 N N    . PRO   B 1 32  ? 48.378 -16.316 -13.633 1.00 15.69 ?  32  PRO   B N    1 
ATOM   4751 C CA   . PRO   B 1 32  ? 47.004 -15.948 -13.281 1.00 15.19 ?  32  PRO   B CA   1 
ATOM   4752 C C    . PRO   B 1 32  ? 46.933 -14.605 -12.576 1.00 14.71 ?  32  PRO   B C    1 
ATOM   4753 O O    . PRO   B 1 32  ? 47.860 -14.188 -11.874 1.00 16.39 ?  32  PRO   B O    1 
ATOM   4754 C CB   . PRO   B 1 32  ? 46.597 -17.061 -12.310 1.00 15.37 ?  32  PRO   B CB   1 
ATOM   4755 C CG   . PRO   B 1 32  ? 47.894 -17.427 -11.633 1.00 15.56 ?  32  PRO   B CG   1 
ATOM   4756 C CD   . PRO   B 1 32  ? 48.951 -17.299 -12.689 1.00 15.81 ?  32  PRO   B CD   1 
ATOM   4757 H HA   . PRO   B 1 32  ? 46.429 -15.962 -14.069 1.00 18.25 ?  32  PRO   B HA   1 
ATOM   4758 H HB2  . PRO   B 1 32  ? 45.954 -16.719 -11.670 1.00 18.46 ?  32  PRO   B HB2  1 
ATOM   4759 H HB3  . PRO   B 1 32  ? 46.235 -17.817 -12.799 1.00 18.46 ?  32  PRO   B HB3  1 
ATOM   4760 H HG2  . PRO   B 1 32  ? 48.069 -16.812 -10.901 1.00 18.69 ?  32  PRO   B HG2  1 
ATOM   4761 H HG3  . PRO   B 1 32  ? 47.851 -18.340 -11.307 1.00 18.69 ?  32  PRO   B HG3  1 
ATOM   4762 H HD2  . PRO   B 1 32  ? 49.772 -16.953 -12.299 1.00 19.00 ?  32  PRO   B HD2  1 
ATOM   4763 H HD3  . PRO   B 1 32  ? 49.094 -18.150 -13.123 1.00 19.00 ?  32  PRO   B HD3  1 
ATOM   4764 N N    . THR   B 1 33  ? 45.783 -13.945 -12.740 1.00 14.67 ?  33  THR   B N    1 
ATOM   4765 C CA   . THR   B 1 33  ? 45.500 -12.766 -11.929 1.00 14.32 ?  33  THR   B CA   1 
ATOM   4766 C C    . THR   B 1 33  ? 45.459 -13.120 -10.449 1.00 14.01 ?  33  THR   B C    1 
ATOM   4767 O O    . THR   B 1 33  ? 45.946 -12.351 -9.606  1.00 15.00 ?  33  THR   B O    1 
ATOM   4768 C CB   . THR   B 1 33  ? 44.181 -12.127 -12.373 1.00 15.40 ?  33  THR   B CB   1 
ATOM   4769 O OG1  . THR   B 1 33  ? 44.215 -11.887 -13.781 1.00 15.47 ?  33  THR   B OG1  1 
ATOM   4770 C CG2  . THR   B 1 33  ? 43.932 -10.828 -11.630 1.00 16.66 ?  33  THR   B CG2  1 
ATOM   4771 H H    . THR   B 1 33  ? 45.162 -14.161 -13.305 1.00 17.63 ?  33  THR   B H    1 
ATOM   4772 H HA   . THR   B 1 33  ? 46.203 -12.120 -12.069 1.00 17.21 ?  33  THR   B HA   1 
ATOM   4773 H HB   . THR   B 1 33  ? 43.448 -12.740 -12.184 1.00 18.50 ?  33  THR   B HB   1 
ATOM   4774 H HG1  . THR   B 1 33  ? 43.504 -11.510 -14.034 1.00 18.58 ?  33  THR   B HG1  1 
ATOM   4775 H HG21 . THR   B 1 33  ? 43.178 -10.365 -12.012 1.00 20.02 ?  33  THR   B HG21 1 
ATOM   4776 H HG22 . THR   B 1 33  ? 43.750 -11.015 -10.693 1.00 20.02 ?  33  THR   B HG22 1 
ATOM   4777 H HG23 . THR   B 1 33  ? 44.719 -10.263 -11.688 1.00 20.02 ?  33  THR   B HG23 1 
ATOM   4778 N N    . VAL   B 1 34  ? 44.890 -14.285 -10.112 1.00 13.46 ?  34  VAL   B N    1 
ATOM   4779 C CA   . VAL   B 1 34  ? 44.686 -14.675 -8.721  1.00 13.23 ?  34  VAL   B CA   1 
ATOM   4780 C C    . VAL   B 1 34  ? 45.104 -16.126 -8.545  1.00 12.49 ?  34  VAL   B C    1 
ATOM   4781 O O    . VAL   B 1 34  ? 44.577 -17.015 -9.227  1.00 13.06 ?  34  VAL   B O    1 
ATOM   4782 C CB   . VAL   B 1 34  ? 43.220 -14.520 -8.267  1.00 14.46 ?  34  VAL   B CB   1 
ATOM   4783 C CG1  . VAL   B 1 34  ? 43.063 -14.973 -6.825  1.00 14.41 ?  34  VAL   B CG1  1 
ATOM   4784 C CG2  . VAL   B 1 34  ? 42.734 -13.088 -8.446  1.00 15.23 ?  34  VAL   B CG2  1 
ATOM   4785 H H    . VAL   B 1 34  ? 44.618 -14.876 -10.679 1.00 16.17 ?  34  VAL   B H    1 
ATOM   4786 H HA   . VAL   B 1 34  ? 45.240 -14.125 -8.146  1.00 15.90 ?  34  VAL   B HA   1 
ATOM   4787 H HB   . VAL   B 1 34  ? 42.657 -15.081 -8.821  1.00 17.37 ?  34  VAL   B HB   1 
ATOM   4788 H HG11 . VAL   B 1 34  ? 42.224 -14.627 -6.475  1.00 17.31 ?  34  VAL   B HG11 1 
ATOM   4789 H HG12 . VAL   B 1 34  ? 43.057 -15.940 -6.797  1.00 17.31 ?  34  VAL   B HG12 1 
ATOM   4790 H HG13 . VAL   B 1 34  ? 43.802 -14.624 -6.303  1.00 17.31 ?  34  VAL   B HG13 1 
ATOM   4791 H HG21 . VAL   B 1 34  ? 41.815 -13.022 -8.141  1.00 18.30 ?  34  VAL   B HG21 1 
ATOM   4792 H HG22 . VAL   B 1 34  ? 43.297 -12.493 -7.924  1.00 18.30 ?  34  VAL   B HG22 1 
ATOM   4793 H HG23 . VAL   B 1 34  ? 42.786 -12.847 -9.386  1.00 18.30 ?  34  VAL   B HG23 1 
ATOM   4794 N N    . VAL   B 1 35  ? 46.010 -16.378 -7.605  1.00 11.57 ?  35  VAL   B N    1 
ATOM   4795 C CA   . VAL   B 1 35  ? 46.232 -17.725 -7.081  1.00 11.46 ?  35  VAL   B CA   1 
ATOM   4796 C C    . VAL   B 1 35  ? 45.690 -17.769 -5.662  1.00 10.85 ?  35  VAL   B C    1 
ATOM   4797 O O    . VAL   B 1 35  ? 45.912 -16.847 -4.875  1.00 11.18 ?  35  VAL   B O    1 
ATOM   4798 C CB   . VAL   B 1 35  ? 47.715 -18.160 -7.154  1.00 12.21 ?  35  VAL   B CB   1 
ATOM   4799 C CG1  . VAL   B 1 35  ? 48.621 -17.301 -6.258  1.00 13.12 ?  35  VAL   B CG1  1 
ATOM   4800 C CG2  . VAL   B 1 35  ? 47.850 -19.638 -6.796  1.00 12.69 ?  35  VAL   B CG2  1 
ATOM   4801 H H    . VAL   B 1 35  ? 46.516 -15.776 -7.249  1.00 13.91 ?  35  VAL   B H    1 
ATOM   4802 H HA   . VAL   B 1 35  ? 45.716 -18.350 -7.604  1.00 13.78 ?  35  VAL   B HA   1 
ATOM   4803 H HB   . VAL   B 1 35  ? 48.019 -18.057 -8.071  1.00 14.68 ?  35  VAL   B HB   1 
ATOM   4804 H HG11 . VAL   B 1 35  ? 49.542 -17.544 -6.429  1.00 15.77 ?  35  VAL   B HG11 1 
ATOM   4805 H HG12 . VAL   B 1 35  ? 48.473 -16.370 -6.472  1.00 15.77 ?  35  VAL   B HG12 1 
ATOM   4806 H HG13 . VAL   B 1 35  ? 48.395 -17.474 -5.333  1.00 15.77 ?  35  VAL   B HG13 1 
ATOM   4807 H HG21 . VAL   B 1 35  ? 48.765 -19.917 -6.920  1.00 15.25 ?  35  VAL   B HG21 1 
ATOM   4808 H HG22 . VAL   B 1 35  ? 47.585 -19.765 -5.867  1.00 15.25 ?  35  VAL   B HG22 1 
ATOM   4809 H HG23 . VAL   B 1 35  ? 47.261 -20.161 -7.372  1.00 15.25 ?  35  VAL   B HG23 1 
ATOM   4810 N N    . VAL   B 1 36  ? 44.975 -18.846 -5.337  1.00 11.21 ?  36  VAL   B N    1 
ATOM   4811 C CA   . VAL   B 1 36  ? 44.427 -19.036 -4.005  1.00 10.63 ?  36  VAL   B CA   1 
ATOM   4812 C C    . VAL   B 1 36  ? 45.434 -19.800 -3.153  1.00 10.75 ?  36  VAL   B C    1 
ATOM   4813 O O    . VAL   B 1 36  ? 45.968 -20.840 -3.573  1.00 11.51 ?  36  VAL   B O    1 
ATOM   4814 C CB   . VAL   B 1 36  ? 43.090 -19.798 -4.077  1.00 11.11 ?  36  VAL   B CB   1 
ATOM   4815 C CG1  . VAL   B 1 36  ? 42.587 -20.162 -2.686  1.00 11.72 ?  36  VAL   B CG1  1 
ATOM   4816 C CG2  . VAL   B 1 36  ? 42.065 -18.973 -4.832  1.00 12.07 ?  36  VAL   B CG2  1 
ATOM   4817 H H    . VAL   B 1 36  ? 44.806 -19.495 -5.873  1.00 13.47 ?  36  VAL   B H    1 
ATOM   4818 H HA   . VAL   B 1 36  ? 44.263 -18.170 -3.592  1.00 12.77 ?  36  VAL   B HA   1 
ATOM   4819 H HB   . VAL   B 1 36  ? 43.225 -20.621 -4.563  1.00 13.36 ?  36  VAL   B HB   1 
ATOM   4820 H HG11 . VAL   B 1 36  ? 41.647 -20.402 -2.742  1.00 14.09 ?  36  VAL   B HG11 1 
ATOM   4821 H HG12 . VAL   B 1 36  ? 43.098 -20.907 -2.343  1.00 14.09 ?  36  VAL   B HG12 1 
ATOM   4822 H HG13 . VAL   B 1 36  ? 42.688 -19.390 -2.100  1.00 14.09 ?  36  VAL   B HG13 1 
ATOM   4823 H HG21 . VAL   B 1 36  ? 41.221 -19.454 -4.848  1.00 14.51 ?  36  VAL   B HG21 1 
ATOM   4824 H HG22 . VAL   B 1 36  ? 41.949 -18.120 -4.386  1.00 14.51 ?  36  VAL   B HG22 1 
ATOM   4825 H HG23 . VAL   B 1 36  ? 42.379 -18.832 -5.739  1.00 14.51 ?  36  VAL   B HG23 1 
ATOM   4826 N N    . ASN   B 1 37  ? 45.642 -19.319 -1.931  1.00 11.20 ?  37  ASN   B N    1 
ATOM   4827 C CA   . ASN   B 1 37  ? 46.396 -20.035 -0.918  1.00 11.71 ?  37  ASN   B CA   1 
ATOM   4828 C C    . ASN   B 1 37  ? 45.440 -20.699 0.066   1.00 11.92 ?  37  ASN   B C    1 
ATOM   4829 O O    . ASN   B 1 37  ? 44.430 -20.115 0.476   1.00 11.79 ?  37  ASN   B O    1 
ATOM   4830 C CB   . ASN   B 1 37  ? 47.324 -19.088 -0.161  1.00 11.42 ?  37  ASN   B CB   1 
ATOM   4831 C CG   . ASN   B 1 37  ? 48.176 -19.805 0.846   1.00 12.00 ?  37  ASN   B CG   1 
ATOM   4832 O OD1  . ASN   B 1 37  ? 48.509 -20.984 0.670   1.00 12.52 ?  37  ASN   B OD1  1 
ATOM   4833 N ND2  . ASN   B 1 37  ? 48.528 -19.107 1.923   1.00 11.81 ?  37  ASN   B ND2  1 
ATOM   4834 H H    . ASN   B 1 37  ? 45.343 -18.551 -1.656  1.00 13.46 ?  37  ASN   B H    1 
ATOM   4835 H HA   . ASN   B 1 37  ? 46.934 -20.719 -1.338  1.00 14.07 ?  37  ASN   B HA   1 
ATOM   4836 H HB2  . ASN   B 1 37  ? 47.921 -18.653 -0.793  1.00 13.72 ?  37  ASN   B HB2  1 
ATOM   4837 H HB3  . ASN   B 1 37  ? 46.798 -18.423 0.309   1.00 13.72 ?  37  ASN   B HB3  1 
ATOM   4838 H HD21 . ASN   B 1 37  ? 49.027 -19.463 2.529   1.00 14.20 ?  37  ASN   B HD21 1 
ATOM   4839 H HD22 . ASN   B 1 37  ? 48.290 -18.286 2.005   1.00 14.20 ?  37  ASN   B HD22 1 
ATOM   4840 N N    . ALA   B 1 38  ? 45.782 -21.932 0.441   1.00 11.78 ?  38  ALA   B N    1 
ATOM   4841 C CA   . ALA   B 1 38  ? 45.134 -22.672 1.529   1.00 12.57 ?  38  ALA   B CA   1 
ATOM   4842 C C    . ALA   B 1 38  ? 45.723 -22.183 2.852   1.00 12.09 ?  38  ALA   B C    1 
ATOM   4843 O O    . ALA   B 1 38  ? 46.626 -22.790 3.441   1.00 12.76 ?  38  ALA   B O    1 
ATOM   4844 C CB   . ALA   B 1 38  ? 45.361 -24.166 1.355   1.00 13.49 ?  38  ALA   B CB   1 
ATOM   4845 H H    . ALA   B 1 38  ? 46.424 -22.375 0.069   1.00 14.16 ?  38  ALA   B H    1 
ATOM   4846 H HA   . ALA   B 1 38  ? 44.186 -22.492 1.521   1.00 15.11 ?  38  ALA   B HA   1 
ATOM   4847 H HB1  . ALA   B 1 38  ? 44.920 -24.636 2.087   1.00 16.21 ?  38  ALA   B HB1  1 
ATOM   4848 H HB2  . ALA   B 1 38  ? 44.978 -24.447 0.510   1.00 16.21 ?  38  ALA   B HB2  1 
ATOM   4849 H HB3  . ALA   B 1 38  ? 46.309 -24.351 1.371   1.00 16.21 ?  38  ALA   B HB3  1 
ATOM   4850 N N    . ALA   B 1 39  ? 45.208 -21.039 3.306   1.00 11.96 ?  39  ALA   B N    1 
ATOM   4851 C CA   . ALA   B 1 39  ? 45.757 -20.299 4.431   1.00 12.63 ?  39  ALA   B CA   1 
ATOM   4852 C C    . ALA   B 1 39  ? 45.139 -20.740 5.754   1.00 12.51 ?  39  ALA   B C    1 
ATOM   4853 O O    . ALA   B 1 39  ? 44.101 -21.398 5.803   1.00 12.96 ?  39  ALA   B O    1 
ATOM   4854 C CB   . ALA   B 1 39  ? 45.523 -18.798 4.232   1.00 12.55 ?  39  ALA   B CB   1 
ATOM   4855 H H    . ALA   B 1 39  ? 44.512 -20.666 2.962   1.00 14.37 ?  39  ALA   B H    1 
ATOM   4856 H HA   . ALA   B 1 39  ? 46.709 -20.455 4.478   1.00 15.18 ?  39  ALA   B HA   1 
ATOM   4857 H HB1  . ALA   B 1 39  ? 45.894 -18.318 4.988   1.00 15.08 ?  39  ALA   B HB1  1 
ATOM   4858 H HB2  . ALA   B 1 39  ? 45.964 -18.517 3.414   1.00 15.08 ?  39  ALA   B HB2  1 
ATOM   4859 H HB3  . ALA   B 1 39  ? 44.570 -18.630 4.167   1.00 15.08 ?  39  ALA   B HB3  1 
ATOM   4860 N N    . ASN   B 1 40  ? 45.784 -20.331 6.840   1.00 13.30 ?  40  ASN   B N    1 
ATOM   4861 C CA   . ASN   B 1 40  ? 45.212 -20.369 8.177   1.00 14.21 ?  40  ASN   B CA   1 
ATOM   4862 C C    . ASN   B 1 40  ? 45.030 -18.942 8.694   1.00 13.54 ?  40  ASN   B C    1 
ATOM   4863 O O    . ASN   B 1 40  ? 45.446 -17.968 8.056   1.00 12.85 ?  40  ASN   B O    1 
ATOM   4864 C CB   . ASN   B 1 40  ? 46.058 -21.239 9.124   1.00 14.59 ?  40  ASN   B CB   1 
ATOM   4865 C CG   . ASN   B 1 40  ? 47.516 -20.821 9.168   1.00 15.72 ?  40  ASN   B CG   1 
ATOM   4866 O OD1  . ASN   B 1 40  ? 47.830 -19.638 9.287   1.00 17.93 ?  40  ASN   B OD1  1 
ATOM   4867 N ND2  . ASN   B 1 40  ? 48.416 -21.788 9.080   1.00 16.07 ?  40  ASN   B ND2  1 
ATOM   4868 H H    . ASN   B 1 40  ? 46.586 -20.020 6.825   1.00 15.98 ?  40  ASN   B H    1 
ATOM   4869 H HA   . ASN   B 1 40  ? 44.330 -20.764 8.127   1.00 17.08 ?  40  ASN   B HA   1 
ATOM   4870 H HB2  . ASN   B 1 40  ? 45.692 -21.168 10.023  1.00 17.53 ?  40  ASN   B HB2  1 
ATOM   4871 H HB3  . ASN   B 1 40  ? 46.014 -22.158 8.822   1.00 17.53 ?  40  ASN   B HB3  1 
ATOM   4872 H HD21 . ASN   B 1 40  ? 49.253 -21.601 9.106   1.00 19.31 ?  40  ASN   B HD21 1 
ATOM   4873 H HD22 . ASN   B 1 40  ? 48.159 -22.607 8.995   1.00 19.31 ?  40  ASN   B HD22 1 
ATOM   4874 N N    . VAL   B 1 41  ? 44.384 -18.816 9.858   1.00 13.63 ?  41  VAL   B N    1 
ATOM   4875 C CA   . VAL   B 1 41  ? 43.924 -17.496 10.304  1.00 14.18 ?  41  VAL   B CA   1 
ATOM   4876 C C    . VAL   B 1 41  ? 45.075 -16.541 10.599  1.00 14.07 ?  41  VAL   B C    1 
ATOM   4877 O O    . VAL   B 1 41  ? 44.899 -15.319 10.508  1.00 14.36 ?  41  VAL   B O    1 
ATOM   4878 C CB   . VAL   B 1 41  ? 42.948 -17.581 11.494  1.00 15.88 ?  41  VAL   B CB   1 
ATOM   4879 C CG1  . VAL   B 1 41  ? 41.651 -18.264 11.083  1.00 15.78 ?  41  VAL   B CG1  1 
ATOM   4880 C CG2  . VAL   B 1 41  ? 43.608 -18.266 12.691  1.00 17.01 ?  41  VAL   B CG2  1 
ATOM   4881 H H    . VAL   B 1 41  ? 44.208 -19.459 10.391  1.00 16.38 ?  41  VAL   B H    1 
ATOM   4882 H HA   . VAL   B 1 41  ? 43.425 -17.101 9.576   1.00 17.03 ?  41  VAL   B HA   1 
ATOM   4883 H HB   . VAL   B 1 41  ? 42.720 -16.680 11.770  1.00 19.08 ?  41  VAL   B HB   1 
ATOM   4884 H HG11 . VAL   B 1 41  ? 41.039 -18.265 11.836  1.00 18.96 ?  41  VAL   B HG11 1 
ATOM   4885 H HG12 . VAL   B 1 41  ? 41.260 -17.782 10.339  1.00 18.96 ?  41  VAL   B HG12 1 
ATOM   4886 H HG13 . VAL   B 1 41  ? 41.846 -19.179 10.817  1.00 18.96 ?  41  VAL   B HG13 1 
ATOM   4887 H HG21 . VAL   B 1 41  ? 42.973 -18.302 13.424  1.00 20.43 ?  41  VAL   B HG21 1 
ATOM   4888 H HG22 . VAL   B 1 41  ? 43.870 -19.166 12.437  1.00 20.43 ?  41  VAL   B HG22 1 
ATOM   4889 H HG23 . VAL   B 1 41  ? 44.389 -17.757 12.956  1.00 20.43 ?  41  VAL   B HG23 1 
ATOM   4890 N N    . TYR   B 1 42  ? 46.250 -17.056 10.965  1.00 14.09 ?  42  TYR   B N    1 
ATOM   4891 C CA   . TYR   B 1 42  ? 47.405 -16.209 11.233  1.00 14.41 ?  42  TYR   B CA   1 
ATOM   4892 C C    . TYR   B 1 42  ? 48.369 -16.131 10.051  1.00 13.78 ?  42  TYR   B C    1 
ATOM   4893 O O    . TYR   B 1 42  ? 49.457 -15.554 10.185  1.00 15.39 ?  42  TYR   B O    1 
ATOM   4894 C CB   . TYR   B 1 42  ? 48.094 -16.626 12.538  1.00 16.66 ?  42  TYR   B CB   1 
ATOM   4895 C CG   . TYR   B 1 42  ? 47.502 -15.930 13.764  1.00 16.94 ?  42  TYR   B CG   1 
ATOM   4896 C CD1  . TYR   B 1 42  ? 47.716 -14.572 13.978  1.00 16.67 ?  42  TYR   B CD1  1 
ATOM   4897 C CD2  . TYR   B 1 42  ? 46.731 -16.616 14.692  1.00 19.03 ?  42  TYR   B CD2  1 
ATOM   4898 C CE1  . TYR   B 1 42  ? 47.187 -13.919 15.077  1.00 17.39 ?  42  TYR   B CE1  1 
ATOM   4899 C CE2  . TYR   B 1 42  ? 46.194 -15.966 15.803  1.00 18.96 ?  42  TYR   B CE2  1 
ATOM   4900 C CZ   . TYR   B 1 42  ? 46.428 -14.613 15.988  1.00 19.12 ?  42  TYR   B CZ   1 
ATOM   4901 O OH   . TYR   B 1 42  ? 45.915 -13.945 17.083  1.00 22.18 ?  42  TYR   B OH   1 
ATOM   4902 H H    . TYR   B 1 42  ? 46.399 -17.903 11.060  1.00 16.93 ?  42  TYR   B H    1 
ATOM   4903 H HA   . TYR   B 1 42  ? 47.076 -15.313 11.375  1.00 17.31 ?  42  TYR   B HA   1 
ATOM   4904 H HB2  . TYR   B 1 42  ? 47.993 -17.583 12.663  1.00 20.02 ?  42  TYR   B HB2  1 
ATOM   4905 H HB3  . TYR   B 1 42  ? 49.033 -16.394 12.488  1.00 20.02 ?  42  TYR   B HB3  1 
ATOM   4906 H HD1  . TYR   B 1 42  ? 48.233 -14.092 13.367  1.00 20.02 ?  42  TYR   B HD1  1 
ATOM   4907 H HD2  . TYR   B 1 42  ? 46.567 -17.526 14.569  1.00 22.86 ?  42  TYR   B HD2  1 
ATOM   4908 H HE1  . TYR   B 1 42  ? 47.351 -13.012 15.199  1.00 20.89 ?  42  TYR   B HE1  1 
ATOM   4909 H HE2  . TYR   B 1 42  ? 45.677 -16.441 16.415  1.00 22.77 ?  42  TYR   B HE2  1 
ATOM   4910 H HH   . TYR   B 1 42  ? 46.141 -13.138 17.052  1.00 26.63 ?  42  TYR   B HH   1 
ATOM   4911 N N    . LEU   B 1 43  ? 47.965 -16.635 8.887   1.00 12.73 ?  43  LEU   B N    1 
ATOM   4912 C CA   . LEU   B 1 43  ? 48.780 -16.585 7.677   1.00 12.74 ?  43  LEU   B CA   1 
ATOM   4913 C C    . LEU   B 1 43  ? 50.191 -17.085 7.945   1.00 12.56 ?  43  LEU   B C    1 
ATOM   4914 O O    . LEU   B 1 43  ? 51.176 -16.496 7.496   1.00 13.76 ?  43  LEU   B O    1 
ATOM   4915 C CB   . LEU   B 1 43  ? 48.808 -15.190 7.050   1.00 12.82 ?  43  LEU   B CB   1 
ATOM   4916 C CG   . LEU   B 1 43  ? 47.451 -14.570 6.703   1.00 13.43 ?  43  LEU   B CG   1 
ATOM   4917 C CD1  . LEU   B 1 43  ? 47.655 -13.173 6.111   1.00 14.71 ?  43  LEU   B CD1  1 
ATOM   4918 C CD2  . LEU   B 1 43  ? 46.655 -15.460 5.760   1.00 13.65 ?  43  LEU   B CD2  1 
ATOM   4919 H H    . LEU   B 1 43  ? 47.206 -17.024 8.768   1.00 15.30 ?  43  LEU   B H    1 
ATOM   4920 H HA   . LEU   B 1 43  ? 48.383 -17.180 7.022   1.00 15.31 ?  43  LEU   B HA   1 
ATOM   4921 H HB2  . LEU   B 1 43  ? 49.256 -14.587 7.658   1.00 15.40 ?  43  LEU   B HB2  1 
ATOM   4922 H HB3  . LEU   B 1 43  ? 49.315 -15.243 6.219   1.00 15.40 ?  43  LEU   B HB3  1 
ATOM   4923 H HG   . LEU   B 1 43  ? 46.941 -14.466 7.518   1.00 16.14 ?  43  LEU   B HG   1 
ATOM   4924 H HD11 . LEU   B 1 43  ? 46.784 -12.793 5.901   1.00 17.68 ?  43  LEU   B HD11 1 
ATOM   4925 H HD12 . LEU   B 1 43  ? 48.107 -12.617 6.763   1.00 17.68 ?  43  LEU   B HD12 1 
ATOM   4926 H HD13 . LEU   B 1 43  ? 48.186 -13.245 5.306   1.00 17.68 ?  43  LEU   B HD13 1 
ATOM   4927 H HD21 . LEU   B 1 43  ? 45.849 -14.991 5.485   1.00 16.41 ?  43  LEU   B HD21 1 
ATOM   4928 H HD22 . LEU   B 1 43  ? 47.195 -15.667 4.983   1.00 16.41 ?  43  LEU   B HD22 1 
ATOM   4929 H HD23 . LEU   B 1 43  ? 46.415 -16.277 6.225   1.00 16.41 ?  43  LEU   B HD23 1 
ATOM   4930 N N    . LYS   B 1 44  ? 50.283 -18.209 8.659   1.00 13.22 ?  44  LYS   B N    1 
ATOM   4931 C CA   . LYS   B 1 44  ? 51.549 -18.885 8.909   1.00 13.78 ?  44  LYS   B CA   1 
ATOM   4932 C C    . LYS   B 1 44  ? 51.673 -20.006 7.888   1.00 13.31 ?  44  LYS   B C    1 
ATOM   4933 O O    . LYS   B 1 44  ? 50.980 -21.025 7.978   1.00 14.54 ?  44  LYS   B O    1 
ATOM   4934 C CB   . LYS   B 1 44  ? 51.596 -19.398 10.346  1.00 15.20 ?  44  LYS   B CB   1 
ATOM   4935 C CG   . LYS   B 1 44  ? 51.798 -18.288 11.358  1.00 17.86 ?  44  LYS   B CG   1 
ATOM   4936 C CD   . LYS   B 1 44  ? 53.015 -17.445 10.947  1.00 21.49 ?  44  LYS   B CD   1 
ATOM   4937 C CE   . LYS   B 1 44  ? 53.565 -16.598 12.063  1.00 24.73 ?  44  LYS   B CE   1 
ATOM   4938 N NZ   . LYS   B 1 44  ? 54.702 -15.738 11.650  1.00 25.75 ?  44  LYS   B NZ   1 
ATOM   4939 H H    . LYS   B 1 44  ? 49.606 -18.602 9.017   1.00 15.89 ?  44  LYS   B H    1 
ATOM   4940 H HA   . LYS   B 1 44  ? 52.279 -18.271 8.745   1.00 16.56 ?  44  LYS   B HA   1 
ATOM   4941 H HB2  . LYS   B 1 44  ? 50.749 -19.836 10.552  1.00 18.27 ?  44  LYS   B HB2  1 
ATOM   4942 H HB3  . LYS   B 1 44  ? 52.323 -20.026 10.437  1.00 18.27 ?  44  LYS   B HB3  1 
ATOM   4943 H HG2  . LYS   B 1 44  ? 51.015 -17.721 11.385  1.00 21.45 ?  44  LYS   B HG2  1 
ATOM   4944 H HG3  . LYS   B 1 44  ? 51.972 -18.677 12.233  1.00 21.45 ?  44  LYS   B HG3  1 
ATOM   4945 H HD2  . LYS   B 1 44  ? 53.713 -18.045 10.624  1.00 25.81 ?  44  LYS   B HD2  1 
ATOM   4946 H HD3  . LYS   B 1 44  ? 52.744 -16.846 10.230  1.00 25.81 ?  44  LYS   B HD3  1 
ATOM   4947 H HE2  . LYS   B 1 44  ? 52.860 -16.010 12.349  1.00 29.69 ?  44  LYS   B HE2  1 
ATOM   4948 H HE3  . LYS   B 1 44  ? 53.855 -17.177 12.788  1.00 29.69 ?  44  LYS   B HE3  1 
ATOM   4949 H HZ1  . LYS   B 1 44  ? 54.985 -15.259 12.344  1.00 30.93 ?  44  LYS   B HZ1  1 
ATOM   4950 H HZ2  . LYS   B 1 44  ? 55.374 -16.237 11.349  1.00 30.93 ?  44  LYS   B HZ2  1 
ATOM   4951 H HZ3  . LYS   B 1 44  ? 54.443 -15.183 11.003  1.00 30.93 ?  44  LYS   B HZ3  1 
ATOM   4952 N N    . HIS   B 1 45  ? 52.527 -19.795 6.889   1.00 12.89 ?  45  HIS   B N    1 
ATOM   4953 C CA   . HIS   B 1 45  ? 52.554 -20.634 5.692   1.00 12.58 ?  45  HIS   B CA   1 
ATOM   4954 C C    . HIS   B 1 45  ? 53.579 -21.754 5.853   1.00 15.36 ?  45  HIS   B C    1 
ATOM   4955 O O    . HIS   B 1 45  ? 54.643 -21.772 5.234   1.00 18.00 ?  45  HIS   B O    1 
ATOM   4956 C CB   . HIS   B 1 45  ? 52.863 -19.783 4.473   1.00 13.07 ?  45  HIS   B CB   1 
ATOM   4957 C CG   . HIS   B 1 45  ? 51.996 -18.576 4.365   1.00 12.85 ?  45  HIS   B CG   1 
ATOM   4958 N ND1  . HIS   B 1 45  ? 50.618 -18.650 4.344   1.00 13.15 ?  45  HIS   B ND1  1 
ATOM   4959 C CD2  . HIS   B 1 45  ? 52.315 -17.266 4.274   1.00 13.43 ?  45  HIS   B CD2  1 
ATOM   4960 C CE1  . HIS   B 1 45  ? 50.131 -17.427 4.237   1.00 13.30 ?  45  HIS   B CE1  1 
ATOM   4961 N NE2  . HIS   B 1 45  ? 51.138 -16.571 4.191   1.00 13.70 ?  45  HIS   B NE2  1 
ATOM   4962 H H    . HIS   B 1 45  ? 53.097 -19.150 6.873   1.00 15.48 ?  45  HIS   B H    1 
ATOM   4963 H HA   . HIS   B 1 45  ? 51.676 -21.036 5.565   1.00 15.11 ?  45  HIS   B HA   1 
ATOM   4964 H HB2  . HIS   B 1 45  ? 53.783 -19.489 4.517   1.00 15.70 ?  45  HIS   B HB2  1 
ATOM   4965 H HB3  . HIS   B 1 45  ? 52.728 -20.322 3.671   1.00 15.70 ?  45  HIS   B HB3  1 
ATOM   4966 H HD2  . HIS   B 1 45  ? 53.172 -16.904 4.269   1.00 16.14 ?  45  HIS   B HD2  1 
ATOM   4967 H HE1  . HIS   B 1 45  ? 49.227 -17.205 4.192   1.00 15.98 ?  45  HIS   B HE1  1 
ATOM   4968 H HE2  . HIS   B 1 45  ? 51.062 -15.714 4.132   1.00 16.46 ?  45  HIS   B HE2  1 
ATOM   4969 N N    A GLY   B 1 46  ? 53.215 -22.725 6.686   0.56 16.50 ?  46  GLY   B N    1 
ATOM   4970 N N    B GLY   B 1 46  ? 53.226 -22.710 6.702   0.44 16.47 ?  46  GLY   B N    1 
ATOM   4971 C CA   A GLY   B 1 46  ? 54.145 -23.766 7.081   0.56 18.26 ?  46  GLY   B CA   1 
ATOM   4972 C CA   B GLY   B 1 46  ? 54.153 -23.767 7.044   0.44 17.87 ?  46  GLY   B CA   1 
ATOM   4973 C C    A GLY   B 1 46  ? 54.181 -25.014 6.221   0.56 19.27 ?  46  GLY   B C    1 
ATOM   4974 C C    B GLY   B 1 46  ? 54.167 -24.917 6.059   0.44 18.66 ?  46  GLY   B C    1 
ATOM   4975 O O    A GLY   B 1 46  ? 55.263 -25.503 5.882   0.56 21.57 ?  46  GLY   B O    1 
ATOM   4976 O O    B GLY   B 1 46  ? 55.194 -25.211 5.437   0.44 19.85 ?  46  GLY   B O    1 
ATOM   4977 H H    A GLY   B 1 46  ? 52.434 -22.788 7.047   0.56 19.83 ?  46  GLY   B H    1 
ATOM   4978 H H    B GLY   B 1 46  ? 52.457 -22.762 7.090   0.44 19.79 ?  46  GLY   B H    1 
ATOM   4979 H HA2  A GLY   B 1 46  ? 55.038 -23.391 7.097   0.56 21.94 ?  46  GLY   B HA2  1 
ATOM   4980 H HA2  B GLY   B 1 46  ? 55.047 -23.397 7.090   0.44 21.47 ?  46  GLY   B HA2  1 
ATOM   4981 H HA3  A GLY   B 1 46  ? 53.924 -24.050 7.979   0.56 21.94 ?  46  GLY   B HA3  1 
ATOM   4982 H HA3  B GLY   B 1 46  ? 53.923 -24.110 7.923   0.44 21.47 ?  46  GLY   B HA3  1 
ATOM   4983 N N    . GLY   B 1 47  ? 53.018 -25.567 5.885   1.00 19.07 ?  47  GLY   B N    1 
ATOM   4984 C CA   . GLY   B 1 47  ? 52.948 -26.843 5.206   1.00 17.39 ?  47  GLY   B CA   1 
ATOM   4985 C C    . GLY   B 1 47  ? 52.039 -26.825 3.994   1.00 15.38 ?  47  GLY   B C    1 
ATOM   4986 O O    . GLY   B 1 47  ? 51.387 -25.825 3.696   1.00 14.77 ?  47  GLY   B O    1 
ATOM   4987 H H    A GLY   B 1 47  ? 52.248 -25.228 6.066   0.56 22.91 ?  47  GLY   B H    1 
ATOM   4988 H H    B GLY   B 1 47  ? 52.253 -25.277 6.154   0.44 22.91 ?  47  GLY   B H    1 
ATOM   4989 H HA2  . GLY   B 1 47  ? 53.833 -27.108 4.909   1.00 20.89 ?  47  GLY   B HA2  1 
ATOM   4990 H HA3  . GLY   B 1 47  ? 52.621 -27.517 5.821   1.00 20.89 ?  47  GLY   B HA3  1 
ATOM   4991 N N    . GLY   B 1 48  ? 51.995 -27.968 3.311   1.00 14.86 ?  48  GLY   B N    1 
ATOM   4992 C CA   . GLY   B 1 48  ? 51.063 -28.118 2.210   1.00 14.07 ?  48  GLY   B CA   1 
ATOM   4993 C C    . GLY   B 1 48  ? 51.204 -27.015 1.185   1.00 13.33 ?  48  GLY   B C    1 
ATOM   4994 O O    . GLY   B 1 48  ? 52.309 -26.555 0.878   1.00 14.11 ?  48  GLY   B O    1 
ATOM   4995 H H    . GLY   B 1 48  ? 52.490 -28.648 3.457   1.00 17.86 ?  48  GLY   B H    1 
ATOM   4996 H HA2  . GLY   B 1 48  ? 51.217 -28.974 1.768   1.00 16.91 ?  48  GLY   B HA2  1 
ATOM   4997 H HA3  . GLY   B 1 48  ? 50.153 -28.110 2.543   1.00 16.91 ?  48  GLY   B HA3  1 
ATOM   4998 N N    . VAL   B 1 49  ? 50.061 -26.586 0.644   1.00 13.26 ?  49  VAL   B N    1 
ATOM   4999 C CA   . VAL   B 1 49  ? 50.054 -25.569 -0.405  1.00 13.44 ?  49  VAL   B CA   1 
ATOM   5000 C C    . VAL   B 1 49  ? 50.712 -24.282 0.080   1.00 12.61 ?  49  VAL   B C    1 
ATOM   5001 O O    . VAL   B 1 49  ? 51.506 -23.666 -0.638  1.00 13.17 ?  49  VAL   B O    1 
ATOM   5002 C CB   . VAL   B 1 49  ? 48.613 -25.316 -0.897  1.00 14.62 ?  49  VAL   B CB   1 
ATOM   5003 C CG1  . VAL   B 1 49  ? 48.548 -24.075 -1.784  1.00 14.84 ?  49  VAL   B CG1  1 
ATOM   5004 C CG2  . VAL   B 1 49  ? 48.078 -26.537 -1.649  1.00 16.69 ?  49  VAL   B CG2  1 
ATOM   5005 H H    . VAL   B 1 49  ? 49.273 -26.868 0.866   1.00 15.93 ?  49  VAL   B H    1 
ATOM   5006 H HA   . VAL   B 1 49  ? 50.562 -25.893 -1.160  1.00 16.15 ?  49  VAL   B HA   1 
ATOM   5007 H HB   . VAL   B 1 49  ? 48.036 -25.164 -0.133  1.00 17.57 ?  49  VAL   B HB   1 
ATOM   5008 H HG11 . VAL   B 1 49  ? 47.719 -24.090 -2.290  1.00 17.83 ?  49  VAL   B HG11 1 
ATOM   5009 H HG12 . VAL   B 1 49  ? 48.575 -23.281 -1.226  1.00 17.83 ?  49  VAL   B HG12 1 
ATOM   5010 H HG13 . VAL   B 1 49  ? 49.303 -24.079 -2.392  1.00 17.83 ?  49  VAL   B HG13 1 
ATOM   5011 H HG21 . VAL   B 1 49  ? 47.173 -26.354 -1.946  1.00 20.05 ?  49  VAL   B HG21 1 
ATOM   5012 H HG22 . VAL   B 1 49  ? 48.649 -26.707 -2.416  1.00 20.05 ?  49  VAL   B HG22 1 
ATOM   5013 H HG23 . VAL   B 1 49  ? 48.086 -27.300 -1.053  1.00 20.05 ?  49  VAL   B HG23 1 
ATOM   5014 N N    . ALA   B 1 50  ? 50.366 -23.835 1.287   1.00 12.40 ?  50  ALA   B N    1 
ATOM   5015 C CA   . ALA   B 1 50  ? 50.890 -22.558 1.759   1.00 12.40 ?  50  ALA   B CA   1 
ATOM   5016 C C    . ALA   B 1 50  ? 52.412 -22.590 1.865   1.00 12.68 ?  50  ALA   B C    1 
ATOM   5017 O O    . ALA   B 1 50  ? 53.092 -21.621 1.500   1.00 12.34 ?  50  ALA   B O    1 
ATOM   5018 C CB   . ALA   B 1 50  ? 50.269 -22.202 3.104   1.00 12.38 ?  50  ALA   B CB   1 
ATOM   5019 H H    . ALA   B 1 50  ? 49.837 -24.235 1.837   1.00 14.90 ?  50  ALA   B H    1 
ATOM   5020 H HA   . ALA   B 1 50  ? 50.656 -21.863 1.132   1.00 14.90 ?  50  ALA   B HA   1 
ATOM   5021 H HB1  . ALA   B 1 50  ? 50.630 -21.350 3.407   1.00 14.88 ?  50  ALA   B HB1  1 
ATOM   5022 H HB2  . ALA   B 1 50  ? 49.307 -22.131 3.001   1.00 14.88 ?  50  ALA   B HB2  1 
ATOM   5023 H HB3  . ALA   B 1 50  ? 50.483 -22.894 3.750   1.00 14.88 ?  50  ALA   B HB3  1 
ATOM   5024 N N    . GLY   B 1 51  ? 52.960 -23.686 2.378   1.00 13.11 ?  51  GLY   B N    1 
ATOM   5025 C CA   . GLY   B 1 51  ? 54.402 -23.790 2.451   1.00 14.24 ?  51  GLY   B CA   1 
ATOM   5026 C C    . GLY   B 1 51  ? 55.051 -23.747 1.084   1.00 13.89 ?  51  GLY   B C    1 
ATOM   5027 O O    . GLY   B 1 51  ? 56.100 -23.121 0.908   1.00 14.41 ?  51  GLY   B O    1 
ATOM   5028 H H    . GLY   B 1 51  ? 52.532 -24.371 2.672   1.00 15.75 ?  51  GLY   B H    1 
ATOM   5029 H HA2  . GLY   B 1 51  ? 54.757 -23.059 2.975   1.00 17.11 ?  51  GLY   B HA2  1 
ATOM   5030 H HA3  . GLY   B 1 51  ? 54.650 -24.627 2.874   1.00 17.11 ?  51  GLY   B HA3  1 
ATOM   5031 N N    . ALA   B 1 52  ? 54.443 -24.409 0.098   1.00 13.01 ?  52  ALA   B N    1 
ATOM   5032 C CA   . ALA   B 1 52  ? 55.007 -24.421 -1.246  1.00 13.33 ?  52  ALA   B CA   1 
ATOM   5033 C C    . ALA   B 1 52  ? 54.933 -23.044 -1.896  1.00 12.29 ?  52  ALA   B C    1 
ATOM   5034 O O    . ALA   B 1 52  ? 55.905 -22.590 -2.523  1.00 13.79 ?  52  ALA   B O    1 
ATOM   5035 C CB   . ALA   B 1 52  ? 54.287 -25.457 -2.102  1.00 14.16 ?  52  ALA   B CB   1 
ATOM   5036 H H    . ALA   B 1 52  ? 53.707 -24.846 0.176   1.00 15.64 ?  52  ALA   B H    1 
ATOM   5037 H HA   . ALA   B 1 52  ? 55.941 -24.674 -1.195  1.00 16.02 ?  52  ALA   B HA   1 
ATOM   5038 H HB1  . ALA   B 1 52  ? 54.675 -25.457 -2.995  1.00 17.01 ?  52  ALA   B HB1  1 
ATOM   5039 H HB2  . ALA   B 1 52  ? 54.399 -26.332 -1.698  1.00 17.01 ?  52  ALA   B HB2  1 
ATOM   5040 H HB3  . ALA   B 1 52  ? 53.347 -25.232 -2.152  1.00 17.01 ?  52  ALA   B HB3  1 
ATOM   5041 N N    . LEU   B 1 53  ? 53.788 -22.363 -1.774  1.00 12.06 ?  53  LEU   B N    1 
ATOM   5042 C CA   . LEU   B 1 53  ? 53.678 -21.025 -2.349  1.00 12.65 ?  53  LEU   B CA   1 
ATOM   5043 C C    . LEU   B 1 53  ? 54.688 -20.085 -1.703  1.00 12.54 ?  53  LEU   B C    1 
ATOM   5044 O O    . LEU   B 1 53  ? 55.390 -19.336 -2.393  1.00 13.00 ?  53  LEU   B O    1 
ATOM   5045 C CB   . LEU   B 1 53  ? 52.258 -20.468 -2.190  1.00 13.13 ?  53  LEU   B CB   1 
ATOM   5046 C CG   . LEU   B 1 53  ? 51.119 -21.200 -2.908  1.00 13.10 ?  53  LEU   B CG   1 
ATOM   5047 C CD1  . LEU   B 1 53  ? 49.783 -20.583 -2.568  1.00 14.62 ?  53  LEU   B CD1  1 
ATOM   5048 C CD2  . LEU   B 1 53  ? 51.318 -21.209 -4.412  1.00 14.98 ?  53  LEU   B CD2  1 
ATOM   5049 H H    . LEU   B 1 53  ? 53.088 -22.643 -1.373  1.00 14.50 ?  53  LEU   B H    1 
ATOM   5050 H HA   . LEU   B 1 53  ? 53.882 -21.071 -3.300  1.00 15.21 ?  53  LEU   B HA   1 
ATOM   5051 H HB2  . LEU   B 1 53  ? 52.044 -20.472 -1.246  1.00 15.78 ?  53  LEU   B HB2  1 
ATOM   5052 H HB3  . LEU   B 1 53  ? 52.258 -19.555 -2.514  1.00 15.78 ?  53  LEU   B HB3  1 
ATOM   5053 H HG   . LEU   B 1 53  ? 51.097 -22.119 -2.610  1.00 15.74 ?  53  LEU   B HG   1 
ATOM   5054 H HD11 . LEU   B 1 53  ? 49.077 -21.066 -3.035  1.00 17.57 ?  53  LEU   B HD11 1 
ATOM   5055 H HD12 . LEU   B 1 53  ? 49.637 -20.649 -1.608  1.00 17.57 ?  53  LEU   B HD12 1 
ATOM   5056 H HD13 . LEU   B 1 53  ? 49.776 -19.653 -2.839  1.00 17.57 ?  53  LEU   B HD13 1 
ATOM   5057 H HD21 . LEU   B 1 53  ? 50.627 -21.759 -4.821  1.00 17.99 ?  53  LEU   B HD21 1 
ATOM   5058 H HD22 . LEU   B 1 53  ? 51.255 -20.303 -4.750  1.00 17.99 ?  53  LEU   B HD22 1 
ATOM   5059 H HD23 . LEU   B 1 53  ? 52.190 -21.581 -4.617  1.00 17.99 ?  53  LEU   B HD23 1 
ATOM   5060 N N    . ASN   B 1 54  ? 54.777 -20.107 -0.375  1.00 11.95 ?  54  ASN   B N    1 
ATOM   5061 C CA   . ASN   B 1 54  ? 55.694 -19.191 0.291   1.00 13.34 ?  54  ASN   B CA   1 
ATOM   5062 C C    . ASN   B 1 54  ? 57.137 -19.485 -0.100  1.00 13.63 ?  54  ASN   B C    1 
ATOM   5063 O O    . ASN   B 1 54  ? 57.923 -18.558 -0.336  1.00 13.30 ?  54  ASN   B O    1 
ATOM   5064 C CB   . ASN   B 1 54  ? 55.540 -19.266 1.803   1.00 13.92 ?  54  ASN   B CB   1 
ATOM   5065 C CG   . ASN   B 1 54  ? 56.513 -18.349 2.513   1.00 14.07 ?  54  ASN   B CG   1 
ATOM   5066 O OD1  . ASN   B 1 54  ? 56.533 -17.138 2.265   1.00 13.97 ?  54  ASN   B OD1  1 
ATOM   5067 N ND2  . ASN   B 1 54  ? 57.348 -18.916 3.373   1.00 15.59 ?  54  ASN   B ND2  1 
ATOM   5068 H H    . ASN   B 1 54  ? 54.330 -20.624 0.140   1.00 14.36 ?  54  ASN   B H    1 
ATOM   5069 H HA   . ASN   B 1 54  ? 55.489 -18.286 0.012   1.00 16.03 ?  54  ASN   B HA   1 
ATOM   5070 H HB2  . ASN   B 1 54  ? 54.637 -19.001 2.044   1.00 16.73 ?  54  ASN   B HB2  1 
ATOM   5071 H HB3  . ASN   B 1 54  ? 55.709 -20.176 2.095   1.00 16.73 ?  54  ASN   B HB3  1 
ATOM   5072 H HD21 . ASN   B 1 54  ? 57.922 -18.435 3.794   1.00 18.72 ?  54  ASN   B HD21 1 
ATOM   5073 H HD22 . ASN   B 1 54  ? 57.313 -19.764 3.512   1.00 18.72 ?  54  ASN   B HD22 1 
ATOM   5074 N N    . LYS   B 1 55  ? 57.515 -20.766 -0.151  1.00 14.21 ?  55  LYS   B N    1 
ATOM   5075 C CA   . LYS   B 1 55  ? 58.870 -21.114 -0.568  1.00 15.07 ?  55  LYS   B CA   1 
ATOM   5076 C C    . LYS   B 1 55  ? 59.167 -20.578 -1.962  1.00 14.99 ?  55  LYS   B C    1 
ATOM   5077 O O    . LYS   B 1 55  ? 60.266 -20.073 -2.220  1.00 15.76 ?  55  LYS   B O    1 
ATOM   5078 C CB   . LYS   B 1 55  ? 59.061 -22.630 -0.514  1.00 16.83 ?  55  LYS   B CB   1 
ATOM   5079 C CG   . LYS   B 1 55  ? 60.418 -23.103 -1.002  1.00 20.44 ?  55  LYS   B CG   1 
ATOM   5080 C CD   . LYS   B 1 55  ? 60.586 -24.602 -0.809  1.00 24.43 ?  55  LYS   B CD   1 
ATOM   5081 C CE   . LYS   B 1 55  ? 60.711 -24.971 0.668   1.00 27.72 ?  55  LYS   B CE   1 
ATOM   5082 N NZ   . LYS   B 1 55  ? 61.054 -26.400 0.865   1.00 29.77 ?  55  LYS   B NZ   1 
ATOM   5083 H H    . LYS   B 1 55  ? 57.009 -21.437 0.042   1.00 17.08 ?  55  LYS   B H    1 
ATOM   5084 H HA   . LYS   B 1 55  ? 59.499 -20.713 0.048   1.00 18.10 ?  55  LYS   B HA   1 
ATOM   5085 H HB2  . LYS   B 1 55  ? 58.954 -22.919 0.407   1.00 20.22 ?  55  LYS   B HB2  1 
ATOM   5086 H HB3  . LYS   B 1 55  ? 58.383 -23.051 -1.066  1.00 20.22 ?  55  LYS   B HB3  1 
ATOM   5087 H HG2  . LYS   B 1 55  ? 60.503 -22.907 -1.948  1.00 24.56 ?  55  LYS   B HG2  1 
ATOM   5088 H HG3  . LYS   B 1 55  ? 61.112 -22.649 -0.500  1.00 24.56 ?  55  LYS   B HG3  1 
ATOM   5089 H HD2  . LYS   B 1 55  ? 59.812 -25.064 -1.171  1.00 29.34 ?  55  LYS   B HD2  1 
ATOM   5090 H HD3  . LYS   B 1 55  ? 61.392 -24.897 -1.263  1.00 29.34 ?  55  LYS   B HD3  1 
ATOM   5091 H HE2  . LYS   B 1 55  ? 61.411 -24.427 1.067   1.00 33.29 ?  55  LYS   B HE2  1 
ATOM   5092 H HE3  . LYS   B 1 55  ? 59.864 -24.796 1.110   1.00 33.29 ?  55  LYS   B HE3  1 
ATOM   5093 H HZ1  . LYS   B 1 55  ? 61.103 -26.580 1.735   1.00 35.75 ?  55  LYS   B HZ1  1 
ATOM   5094 H HZ2  . LYS   B 1 55  ? 60.427 -26.912 0.497   1.00 35.75 ?  55  LYS   B HZ2  1 
ATOM   5095 H HZ3  . LYS   B 1 55  ? 61.836 -26.578 0.485   1.00 35.75 ?  55  LYS   B HZ3  1 
ATOM   5096 N N    . ALA   B 1 56  ? 58.195 -20.667 -2.873  1.00 14.77 ?  56  ALA   B N    1 
ATOM   5097 C CA   . ALA   B 1 56  ? 58.419 -20.172 -4.223  1.00 15.28 ?  56  ALA   B CA   1 
ATOM   5098 C C    . ALA   B 1 56  ? 58.706 -18.677 -4.224  1.00 14.89 ?  56  ALA   B C    1 
ATOM   5099 O O    . ALA   B 1 56  ? 59.442 -18.191 -5.093  1.00 15.82 ?  56  ALA   B O    1 
ATOM   5100 C CB   . ALA   B 1 56  ? 57.218 -20.496 -5.112  1.00 16.09 ?  56  ALA   B CB   1 
ATOM   5101 H H    . ALA   B 1 56  ? 57.404 -20.984 -2.730  1.00 17.75 ?  56  ALA   B H    1 
ATOM   5102 H HA   . ALA   B 1 56  ? 59.194 -20.613 -4.591  1.00 18.36 ?  56  ALA   B HA   1 
ATOM   5103 H HB1  . ALA   B 1 56  ? 57.391 -20.163 -6.008  1.00 19.33 ?  56  ALA   B HB1  1 
ATOM   5104 H HB2  . ALA   B 1 56  ? 57.098 -21.458 -5.135  1.00 19.33 ?  56  ALA   B HB2  1 
ATOM   5105 H HB3  . ALA   B 1 56  ? 56.427 -20.071 -4.748  1.00 19.33 ?  56  ALA   B HB3  1 
ATOM   5106 N N    . THR   B 1 57  ? 58.132 -17.933 -3.273  1.00 14.42 ?  57  THR   B N    1 
ATOM   5107 C CA   . THR   B 1 57  ? 58.371 -16.499 -3.163  1.00 14.87 ?  57  THR   B CA   1 
ATOM   5108 C C    . THR   B 1 57  ? 59.623 -16.168 -2.358  1.00 15.56 ?  57  THR   B C    1 
ATOM   5109 O O    . THR   B 1 57  ? 59.875 -14.988 -2.077  1.00 15.57 ?  57  THR   B O    1 
ATOM   5110 C CB   . THR   B 1 57  ? 57.173 -15.764 -2.535  1.00 14.02 ?  57  THR   B CB   1 
ATOM   5111 O OG1  . THR   B 1 57  ? 57.149 -15.979 -1.118  1.00 14.37 ?  57  THR   B OG1  1 
ATOM   5112 C CG2  . THR   B 1 57  ? 55.861 -16.188 -3.172  1.00 13.90 ?  57  THR   B CG2  1 
ATOM   5113 H H    . THR   B 1 57  ? 57.583 -18.240 -2.679  1.00 17.32 ?  57  THR   B H    1 
ATOM   5114 H HA   . THR   B 1 57  ? 58.494 -16.141 -4.056  1.00 17.87 ?  57  THR   B HA   1 
ATOM   5115 H HB   . THR   B 1 57  ? 57.277 -14.812 -2.701  1.00 16.85 ?  57  THR   B HB   1 
ATOM   5116 H HG1  . THR   B 1 57  ? 57.069 -16.800 -0.959  1.00 17.26 ?  57  THR   B HG1  1 
ATOM   5117 H HG21 . THR   B 1 57  ? 55.138 -15.621 -2.867  1.00 16.70 ?  57  THR   B HG21 1 
ATOM   5118 H HG22 . THR   B 1 57  ? 55.921 -16.128 -4.141  1.00 16.70 ?  57  THR   B HG22 1 
ATOM   5119 H HG23 . THR   B 1 57  ? 55.657 -17.108 -2.934  1.00 16.70 ?  57  THR   B HG23 1 
ATOM   5120 N N    . ASN   B 1 58  ? 60.415 -17.169 -1.989  1.00 15.92 ?  58  ASN   B N    1 
ATOM   5121 C CA   . ASN   B 1 58  ? 61.615 -16.952 -1.183  1.00 18.80 ?  58  ASN   B CA   1 
ATOM   5122 C C    . ASN   B 1 58  ? 61.281 -16.229 0.121   1.00 16.93 ?  58  ASN   B C    1 
ATOM   5123 O O    . ASN   B 1 58  ? 62.025 -15.360 0.583   1.00 17.61 ?  58  ASN   B O    1 
ATOM   5124 C CB   . ASN   B 1 58  ? 62.708 -16.217 -1.969  1.00 25.18 ?  58  ASN   B CB   1 
ATOM   5125 C CG   . ASN   B 1 58  ? 64.085 -16.395 -1.359  1.00 35.25 ?  58  ASN   B CG   1 
ATOM   5126 O OD1  . ASN   B 1 58  ? 64.368 -17.411 -0.724  1.00 37.12 ?  58  ASN   B OD1  1 
ATOM   5127 N ND2  . ASN   B 1 58  ? 64.950 -15.406 -1.551  1.00 42.99 ?  58  ASN   B ND2  1 
ATOM   5128 H H    . ASN   B 1 58  ? 60.281 -17.997 -2.195  1.00 19.13 ?  58  ASN   B H    1 
ATOM   5129 H HA   . ASN   B 1 58  ? 61.978 -17.825 -0.957  1.00 22.58 ?  58  ASN   B HA   1 
ATOM   5130 H HB2  . ASN   B 1 58  ? 62.738 -16.561 -2.879  1.00 30.23 ?  58  ASN   B HB2  1 
ATOM   5131 H HB3  . ASN   B 1 58  ? 62.510 -15.269 -1.981  1.00 30.23 ?  58  ASN   B HB3  1 
ATOM   5132 H HD21 . ASN   B 1 58  ? 65.745 -15.461 -1.225  1.00 51.61 ?  58  ASN   B HD21 1 
ATOM   5133 H HD22 . ASN   B 1 58  ? 64.716 -14.711 -1.999  1.00 51.61 ?  58  ASN   B HD22 1 
ATOM   5134 N N    . ASN   B 1 59  ? 60.151 -16.600 0.725   1.00 15.96 ?  59  ASN   B N    1 
ATOM   5135 C CA   . ASN   B 1 59  ? 59.681 -16.129 2.027   1.00 15.59 ?  59  ASN   B CA   1 
ATOM   5136 C C    . ASN   B 1 59  ? 59.082 -14.728 1.965   1.00 14.99 ?  59  ASN   B C    1 
ATOM   5137 O O    . ASN   B 1 59  ? 58.652 -14.215 3.008   1.00 15.00 ?  59  ASN   B O    1 
ATOM   5138 C CB   . ASN   B 1 59  ? 60.759 -16.185 3.126   1.00 16.66 ?  59  ASN   B CB   1 
ATOM   5139 C CG   . ASN   B 1 59  ? 60.173 -16.347 4.511   1.00 17.70 ?  59  ASN   B CG   1 
ATOM   5140 O OD1  . ASN   B 1 59  ? 59.340 -17.227 4.750   1.00 17.87 ?  59  ASN   B OD1  1 
ATOM   5141 N ND2  . ASN   B 1 59  ? 60.599 -15.496 5.434   1.00 18.30 ?  59  ASN   B ND2  1 
ATOM   5142 H H    . ASN   B 1 59  ? 59.607 -17.176 0.376   1.00 19.18 ?  59  ASN   B H    1 
ATOM   5143 H HA   . ASN   B 1 59  ? 58.977 -16.727 2.316   1.00 18.73 ?  59  ASN   B HA   1 
ATOM   5144 H HB2  . ASN   B 1 59  ? 61.350 -16.939 2.967   1.00 20.01 ?  59  ASN   B HB2  1 
ATOM   5145 H HB3  . ASN   B 1 59  ? 61.269 -15.359 3.118   1.00 20.01 ?  59  ASN   B HB3  1 
ATOM   5146 H HD21 . ASN   B 1 59  ? 60.300 -15.548 6.241   1.00 21.98 ?  59  ASN   B HD21 1 
ATOM   5147 H HD22 . ASN   B 1 59  ? 61.181 -14.894 5.234   1.00 21.98 ?  59  ASN   B HD22 1 
ATOM   5148 N N    . ALA   B 1 60  ? 59.020 -14.094 0.790   1.00 15.07 ?  60  ALA   B N    1 
ATOM   5149 C CA   . ALA   B 1 60  ? 58.427 -12.762 0.710   1.00 15.11 ?  60  ALA   B CA   1 
ATOM   5150 C C    . ALA   B 1 60  ? 56.959 -12.790 1.108   1.00 14.00 ?  60  ALA   B C    1 
ATOM   5151 O O    . ALA   B 1 60  ? 56.453 -11.839 1.718   1.00 14.43 ?  60  ALA   B O    1 
ATOM   5152 C CB   . ALA   B 1 60  ? 58.591 -12.186 -0.697  1.00 16.25 ?  60  ALA   B CB   1 
ATOM   5153 H H    . ALA   B 1 60  ? 59.317 -14.412 0.047   1.00 18.10 ?  60  ALA   B H    1 
ATOM   5154 H HA   . ALA   B 1 60  ? 58.891 -12.181 1.328   1.00 18.16 ?  60  ALA   B HA   1 
ATOM   5155 H HB1  . ALA   B 1 60  ? 58.189 -11.307 -0.722  1.00 19.52 ?  60  ALA   B HB1  1 
ATOM   5156 H HB2  . ALA   B 1 60  ? 59.538 -12.127 -0.904  1.00 19.52 ?  60  ALA   B HB2  1 
ATOM   5157 H HB3  . ALA   B 1 60  ? 58.152 -12.774 -1.331  1.00 19.52 ?  60  ALA   B HB3  1 
ATOM   5158 N N    . MET   B 1 61  ? 56.252 -13.871 0.768   1.00 13.21 ?  61  MET   B N    1 
ATOM   5159 C CA   . MET   B 1 61  ? 54.855 -13.985 1.157   1.00 13.00 ?  61  MET   B CA   1 
ATOM   5160 C C    . MET   B 1 61  ? 54.711 -13.977 2.675   1.00 13.22 ?  61  MET   B C    1 
ATOM   5161 O O    . MET   B 1 61  ? 53.804 -13.328 3.214   1.00 12.85 ?  61  MET   B O    1 
ATOM   5162 C CB   . MET   B 1 61  ? 54.276 -15.258 0.537   1.00 13.09 ?  61  MET   B CB   1 
ATOM   5163 C CG   . MET   B 1 61  ? 52.833 -15.543 0.941   1.00 12.91 ?  61  MET   B CG   1 
ATOM   5164 S SD   . MET   B 1 61  ? 52.182 -17.050 0.187   1.00 13.49 ?  61  MET   B SD   1 
ATOM   5165 C CE   . MET   B 1 61  ? 51.939 -16.467 -1.489  1.00 14.81 ?  61  MET   B CE   1 
ATOM   5166 H H    . MET   B 1 61  ? 56.557 -14.545 0.316   1.00 15.88 ?  61  MET   B H    1 
ATOM   5167 H HA   . MET   B 1 61  ? 54.365 -13.238 0.788   1.00 15.62 ?  61  MET   B HA   1 
ATOM   5168 H HB2  . MET   B 1 61  ? 54.298 -15.179 -0.432  1.00 15.73 ?  61  MET   B HB2  1 
ATOM   5169 H HB3  . MET   B 1 61  ? 54.815 -16.020 0.811   1.00 15.73 ?  61  MET   B HB3  1 
ATOM   5170 H HG2  . MET   B 1 61  ? 52.789 -15.656 1.905   1.00 15.52 ?  61  MET   B HG2  1 
ATOM   5171 H HG3  . MET   B 1 61  ? 52.275 -14.800 0.668   1.00 15.52 ?  61  MET   B HG3  1 
ATOM   5172 H HE1  . MET   B 1 61  ? 51.548 -17.176 -2.017  1.00 17.80 ?  61  MET   B HE1  1 
ATOM   5173 H HE2  . MET   B 1 61  ? 51.339 -15.699 -1.473  1.00 17.80 ?  61  MET   B HE2  1 
ATOM   5174 H HE3  . MET   B 1 61  ? 52.794 -16.203 -1.862  1.00 17.80 ?  61  MET   B HE3  1 
ATOM   5175 N N    . GLN   B 1 62  ? 55.587 -14.695 3.384   1.00 12.78 ?  62  GLN   B N    1 
ATOM   5176 C CA   . GLN   B 1 62  ? 55.475 -14.748 4.838   1.00 12.96 ?  62  GLN   B CA   1 
ATOM   5177 C C    . GLN   B 1 62  ? 55.755 -13.389 5.464   1.00 13.62 ?  62  GLN   B C    1 
ATOM   5178 O O    . GLN   B 1 62  ? 55.070 -12.983 6.408   1.00 14.01 ?  62  GLN   B O    1 
ATOM   5179 C CB   . GLN   B 1 62  ? 56.433 -15.792 5.415   1.00 13.54 ?  62  GLN   B CB   1 
ATOM   5180 C CG   . GLN   B 1 62  ? 56.199 -16.054 6.896   1.00 14.19 ?  62  GLN   B CG   1 
ATOM   5181 C CD   . GLN   B 1 62  ? 54.826 -16.659 7.138   1.00 14.10 ?  62  GLN   B CD   1 
ATOM   5182 O OE1  . GLN   B 1 62  ? 54.579 -17.812 6.785   1.00 14.22 ?  62  GLN   B OE1  1 
ATOM   5183 N NE2  . GLN   B 1 62  ? 53.906 -15.870 7.692   1.00 14.04 ?  62  GLN   B NE2  1 
ATOM   5184 H H    . GLN   B 1 62  ? 56.239 -15.147 3.055   1.00 15.36 ?  62  GLN   B H    1 
ATOM   5185 H HA   . GLN   B 1 62  ? 54.568 -15.006 5.074   1.00 15.57 ?  62  GLN   B HA   1 
ATOM   5186 H HB2  . GLN   B 1 62  ? 56.310 -16.632 4.942   1.00 16.27 ?  62  GLN   B HB2  1 
ATOM   5187 H HB3  . GLN   B 1 62  ? 57.344 -15.480 5.304   1.00 16.27 ?  62  GLN   B HB3  1 
ATOM   5188 H HG2  . GLN   B 1 62  ? 56.870 -16.674 7.220   1.00 17.04 ?  62  GLN   B HG2  1 
ATOM   5189 H HG3  . GLN   B 1 62  ? 56.256 -15.215 7.384   1.00 17.04 ?  62  GLN   B HG3  1 
ATOM   5190 H HE21 . GLN   B 1 62  ? 54.106 -15.065 7.912   1.00 16.87 ?  62  GLN   B HE21 1 
ATOM   5191 H HE22 . GLN   B 1 62  ? 53.116 -16.175 7.839   1.00 16.87 ?  62  GLN   B HE22 1 
ATOM   5192 N N    . VAL   B 1 63  ? 56.779 -12.687 4.977   1.00 13.75 ?  63  VAL   B N    1 
ATOM   5193 C CA   . VAL   B 1 63  ? 57.085 -11.364 5.519   1.00 15.38 ?  63  VAL   B CA   1 
ATOM   5194 C C    . VAL   B 1 63  ? 55.894 -10.430 5.334   1.00 14.41 ?  63  VAL   B C    1 
ATOM   5195 O O    . VAL   B 1 63  ? 55.486 -9.719  6.261   1.00 14.51 ?  63  VAL   B O    1 
ATOM   5196 C CB   . VAL   B 1 63  ? 58.369 -10.806 4.883   1.00 16.66 ?  63  VAL   B CB   1 
ATOM   5197 C CG1  . VAL   B 1 63  ? 58.597 -9.364  5.329   1.00 17.39 ?  63  VAL   B CG1  1 
ATOM   5198 C CG2  . VAL   B 1 63  ? 59.562 -11.679 5.267   1.00 17.42 ?  63  VAL   B CG2  1 
ATOM   5199 H H    . VAL   B 1 63  ? 57.293 -12.951 4.339   1.00 16.52 ?  63  VAL   B H    1 
ATOM   5200 H HA   . VAL   B 1 63  ? 57.248 -11.454 6.468   1.00 18.48 ?  63  VAL   B HA   1 
ATOM   5201 H HB   . VAL   B 1 63  ? 58.289 -10.823 3.916   1.00 20.02 ?  63  VAL   B HB   1 
ATOM   5202 H HG11 . VAL   B 1 63  ? 59.516 -9.119  5.139   1.00 20.89 ?  63  VAL   B HG11 1 
ATOM   5203 H HG12 . VAL   B 1 63  ? 57.992 -8.787  4.844   1.00 20.89 ?  63  VAL   B HG12 1 
ATOM   5204 H HG13 . VAL   B 1 63  ? 58.430 -9.303  6.282   1.00 20.89 ?  63  VAL   B HG13 1 
ATOM   5205 H HG21 . VAL   B 1 63  ? 60.370 -11.304 4.875   1.00 20.92 ?  63  VAL   B HG21 1 
ATOM   5206 H HG22 . VAL   B 1 63  ? 59.647 -11.692 6.236   1.00 20.92 ?  63  VAL   B HG22 1 
ATOM   5207 H HG23 . VAL   B 1 63  ? 59.424 -12.579 4.937   1.00 20.92 ?  63  VAL   B HG23 1 
ATOM   5208 N N    . GLU   B 1 64  ? 55.324 -10.422 4.132   1.00 13.90 ?  64  GLU   B N    1 
ATOM   5209 C CA   . GLU   B 1 64  ? 54.164 -9.580  3.854   1.00 13.59 ?  64  GLU   B CA   1 
ATOM   5210 C C    . GLU   B 1 64  ? 52.977 -9.978  4.729   1.00 13.40 ?  64  GLU   B C    1 
ATOM   5211 O O    . GLU   B 1 64  ? 52.233 -9.116  5.230   1.00 13.33 ?  64  GLU   B O    1 
ATOM   5212 C CB   . GLU   B 1 64  ? 53.812 -9.735  2.372   1.00 14.02 ?  64  GLU   B CB   1 
ATOM   5213 C CG   . GLU   B 1 64  ? 52.549 -8.999  1.934   1.00 14.76 ?  64  GLU   B CG   1 
ATOM   5214 C CD   . GLU   B 1 64  ? 52.018 -9.486  0.593   1.00 15.35 ?  64  GLU   B CD   1 
ATOM   5215 O OE1  . GLU   B 1 64  ? 52.195 -10.696 0.286   1.00 16.16 ?  64  GLU   B OE1  1 
ATOM   5216 O OE2  . GLU   B 1 64  ? 51.394 -8.665  -0.132  1.00 15.86 -1 64  GLU   B OE2  1 
ATOM   5217 H H    . GLU   B 1 64  ? 55.592 -10.892 3.459   1.00 16.71 ?  64  GLU   B H    1 
ATOM   5218 H HA   . GLU   B 1 64  ? 54.383 -8.654  4.023   1.00 16.33 ?  64  GLU   B HA   1 
ATOM   5219 H HB2  . GLU   B 1 64  ? 54.545 -9.383  1.836   1.00 16.84 ?  64  GLU   B HB2  1 
ATOM   5220 H HB3  . GLU   B 1 64  ? 53.691 -10.675 2.173   1.00 16.84 ?  64  GLU   B HB3  1 
ATOM   5221 H HG2  . GLU   B 1 64  ? 51.847 -9.140  2.594   1.00 17.73 ?  64  GLU   B HG2  1 
ATOM   5222 H HG3  . GLU   B 1 64  ? 52.743 -8.057  1.855   1.00 17.73 ?  64  GLU   B HG3  1 
ATOM   5223 N N    . SER   B 1 65  ? 52.783 -11.284 4.911   1.00 12.96 ?  65  SER   B N    1 
ATOM   5224 C CA   . SER   B 1 65  ? 51.675 -11.789 5.713   1.00 13.29 ?  65  SER   B CA   1 
ATOM   5225 C C    . SER   B 1 65  ? 51.809 -11.391 7.177   1.00 13.35 ?  65  SER   B C    1 
ATOM   5226 O O    . SER   B 1 65  ? 50.812 -11.014 7.812   1.00 13.22 ?  65  SER   B O    1 
ATOM   5227 C CB   . SER   B 1 65  ? 51.591 -13.311 5.583   1.00 13.44 ?  65  SER   B CB   1 
ATOM   5228 O OG   . SER   B 1 65  ? 51.249 -13.711 4.269   1.00 13.23 ?  65  SER   B OG   1 
ATOM   5229 H H    . SER   B 1 65  ? 53.289 -11.905 4.588   1.00 15.57 ?  65  SER   B H    1 
ATOM   5230 H HA   . SER   B 1 65  ? 50.846 -11.413 5.379   1.00 15.98 ?  65  SER   B HA   1 
ATOM   5231 H HB2  . SER   B 1 65  ? 52.446 -13.694 5.818   1.00 16.15 ?  65  SER   B HB2  1 
ATOM   5232 H HB3  . SER   B 1 65  ? 50.906 -13.635 6.196   1.00 16.15 ?  65  SER   B HB3  1 
ATOM   5233 H HG   . SER   B 1 65  ? 51.831 -13.422 3.727   1.00 15.90 ?  65  SER   B HG   1 
ATOM   5234 N N    . ASP   B 1 66  ? 53.018 -11.490 7.745   1.00 13.46 ?  66  ASP   B N    1 
ATOM   5235 C CA   . ASP   B 1 66  ? 53.202 -11.094 9.139   1.00 13.80 ?  66  ASP   B CA   1 
ATOM   5236 C C    . ASP   B 1 66  ? 52.890 -9.614  9.335   1.00 14.60 ?  66  ASP   B C    1 
ATOM   5237 O O    . ASP   B 1 66  ? 52.311 -9.220  10.354  1.00 14.81 ?  66  ASP   B O    1 
ATOM   5238 C CB   . ASP   B 1 66  ? 54.631 -11.396 9.599   1.00 15.72 ?  66  ASP   B CB   1 
ATOM   5239 C CG   . ASP   B 1 66  ? 54.904 -12.897 9.754   1.00 16.87 ?  66  ASP   B CG   1 
ATOM   5240 O OD1  . ASP   B 1 66  ? 53.949 -13.706 9.698   1.00 18.42 ?  66  ASP   B OD1  1 
ATOM   5241 O OD2  . ASP   B 1 66  ? 56.084 -13.268 9.939   1.00 19.84 -1 66  ASP   B OD2  1 
ATOM   5242 H H    . ASP   B 1 66  ? 53.726 -11.783 7.355   1.00 16.17 ?  66  ASP   B H    1 
ATOM   5243 H HA   . ASP   B 1 66  ? 52.600 -11.601 9.701   1.00 16.59 ?  66  ASP   B HA   1 
ATOM   5244 H HB2  . ASP   B 1 66  ? 55.258 -11.040 8.948   1.00 18.88 ?  66  ASP   B HB2  1 
ATOM   5245 H HB3  . ASP   B 1 66  ? 54.784 -10.980 10.464  1.00 18.88 ?  66  ASP   B HB3  1 
ATOM   5246 N N    . ASP   B 1 67  ? 53.266 -8.774  8.366   1.00 13.61 ?  67  ASP   B N    1 
ATOM   5247 C CA   . ASP   B 1 67  ? 52.922 -7.361  8.446   1.00 14.68 ?  67  ASP   B CA   1 
ATOM   5248 C C    . ASP   B 1 67  ? 51.413 -7.148  8.359   1.00 14.77 ?  67  ASP   B C    1 
ATOM   5249 O O    . ASP   B 1 67  ? 50.855 -6.337  9.108   1.00 14.92 ?  67  ASP   B O    1 
ATOM   5250 C CB   . ASP   B 1 67  ? 53.641 -6.590  7.345   1.00 16.17 ?  67  ASP   B CB   1 
ATOM   5251 C CG   . ASP   B 1 67  ? 53.211 -5.148  7.291   1.00 17.33 ?  67  ASP   B CG   1 
ATOM   5252 O OD1  . ASP   B 1 67  ? 53.697 -4.330  8.104   1.00 18.59 ?  67  ASP   B OD1  1 
ATOM   5253 O OD2  . ASP   B 1 67  ? 52.354 -4.844  6.451   1.00 18.30 -1 67  ASP   B OD2  1 
ATOM   5254 H H    . ASP   B 1 67  ? 53.713 -8.997  7.668   1.00 16.35 ?  67  ASP   B H    1 
ATOM   5255 H HA   . ASP   B 1 67  ? 53.221 -7.010  9.300   1.00 17.63 ?  67  ASP   B HA   1 
ATOM   5256 H HB2  . ASP   B 1 67  ? 54.598 -6.618  7.512   1.00 19.42 ?  67  ASP   B HB2  1 
ATOM   5257 H HB3  . ASP   B 1 67  ? 53.444 -7.002  6.488   1.00 19.42 ?  67  ASP   B HB3  1 
ATOM   5258 N N    . TYR   B 1 68  ? 50.733 -7.878  7.466   1.00 14.69 ?  68  TYR   B N    1 
ATOM   5259 C CA   . TYR   B 1 68  ? 49.277 -7.795  7.389   1.00 15.63 ?  68  TYR   B CA   1 
ATOM   5260 C C    . TYR   B 1 68  ? 48.639 -8.143  8.730   1.00 14.23 ?  68  TYR   B C    1 
ATOM   5261 O O    . TYR   B 1 68  ? 47.708 -7.462  9.181   1.00 15.05 ?  68  TYR   B O    1 
ATOM   5262 C CB   . TYR   B 1 68  ? 48.746 -8.721  6.289   1.00 15.79 ?  68  TYR   B CB   1 
ATOM   5263 C CG   . TYR   B 1 68  ? 47.240 -8.867  6.344   1.00 16.88 ?  68  TYR   B CG   1 
ATOM   5264 C CD1  . TYR   B 1 68  ? 46.647 -9.825  7.158   1.00 17.82 ?  68  TYR   B CD1  1 
ATOM   5265 C CD2  . TYR   B 1 68  ? 46.412 -8.031  5.611   1.00 18.22 ?  68  TYR   B CD2  1 
ATOM   5266 C CE1  . TYR   B 1 68  ? 45.284 -9.947  7.242   1.00 19.16 ?  68  TYR   B CE1  1 
ATOM   5267 C CE2  . TYR   B 1 68  ? 45.028 -8.155  5.685   1.00 19.02 ?  68  TYR   B CE2  1 
ATOM   5268 C CZ   . TYR   B 1 68  ? 44.488 -9.112  6.507   1.00 19.27 ?  68  TYR   B CZ   1 
ATOM   5269 O OH   . TYR   B 1 68  ? 43.120 -9.241  6.606   1.00 20.80 ?  68  TYR   B OH   1 
ATOM   5270 H H    . TYR   B 1 68  ? 51.091 -8.429  6.904   1.00 17.65 ?  68  TYR   B H    1 
ATOM   5271 H HA   . TYR   B 1 68  ? 49.030 -6.886  7.166   1.00 18.78 ?  68  TYR   B HA   1 
ATOM   5272 H HB2  . TYR   B 1 68  ? 48.974 -8.352  5.424   1.00 18.97 ?  68  TYR   B HB2  1 
ATOM   5273 H HB3  . TYR   B 1 68  ? 49.133 -9.601  6.395   1.00 18.97 ?  68  TYR   B HB3  1 
ATOM   5274 H HD1  . TYR   B 1 68  ? 47.182 -10.397 7.659   1.00 21.40 ?  68  TYR   B HD1  1 
ATOM   5275 H HD2  . TYR   B 1 68  ? 46.781 -7.372  5.074   1.00 21.89 ?  68  TYR   B HD2  1 
ATOM   5276 H HE1  . TYR   B 1 68  ? 44.899 -10.606 7.782   1.00 23.02 ?  68  TYR   B HE1  1 
ATOM   5277 H HE2  . TYR   B 1 68  ? 44.469 -7.586  5.200   1.00 22.84 ?  68  TYR   B HE2  1 
ATOM   5278 H HH   . TYR   B 1 68  ? 42.722 -8.688  6.103   1.00 24.98 ?  68  TYR   B HH   1 
ATOM   5279 N N    . ILE   B 1 69  ? 49.123 -9.207  9.377   1.00 14.13 ?  69  ILE   B N    1 
ATOM   5280 C CA   . ILE   B 1 69  ? 48.564 -9.635  10.660  1.00 15.02 ?  69  ILE   B CA   1 
ATOM   5281 C C    . ILE   B 1 69  ? 48.813 -8.593  11.744  1.00 14.56 ?  69  ILE   B C    1 
ATOM   5282 O O    . ILE   B 1 69  ? 47.940 -8.323  12.579  1.00 14.80 ?  69  ILE   B O    1 
ATOM   5283 C CB   . ILE   B 1 69  ? 49.139 -11.010 11.050  1.00 15.50 ?  69  ILE   B CB   1 
ATOM   5284 C CG1  . ILE   B 1 69  ? 48.601 -12.115 10.130  1.00 16.08 ?  69  ILE   B CG1  1 
ATOM   5285 C CG2  . ILE   B 1 69  ? 48.855 -11.330 12.515  1.00 16.43 ?  69  ILE   B CG2  1 
ATOM   5286 C CD1  . ILE   B 1 69  ? 47.129 -12.441 10.303  1.00 16.90 ?  69  ILE   B CD1  1 
ATOM   5287 H H    . ILE   B 1 69  ? 49.769 -9.697  9.094   1.00 16.97 ?  69  ILE   B H    1 
ATOM   5288 H HA   . ILE   B 1 69  ? 47.605 -9.732  10.559  1.00 18.04 ?  69  ILE   B HA   1 
ATOM   5289 H HB   . ILE   B 1 69  ? 50.100 -10.972 10.937  1.00 18.63 ?  69  ILE   B HB   1 
ATOM   5290 H HG12 . ILE   B 1 69  ? 48.736 -11.839 9.207   1.00 19.32 ?  69  ILE   B HG12 1 
ATOM   5291 H HG13 . ILE   B 1 69  ? 49.108 -12.928 10.297  1.00 19.32 ?  69  ILE   B HG13 1 
ATOM   5292 H HG21 . ILE   B 1 69  ? 48.994 -12.278 12.661  1.00 19.73 ?  69  ILE   B HG21 1 
ATOM   5293 H HG22 . ILE   B 1 69  ? 49.463 -10.820 13.075  1.00 19.73 ?  69  ILE   B HG22 1 
ATOM   5294 H HG23 . ILE   B 1 69  ? 47.937 -11.094 12.720  1.00 19.73 ?  69  ILE   B HG23 1 
ATOM   5295 H HD11 . ILE   B 1 69  ? 46.893 -13.142 9.672   1.00 20.30 ?  69  ILE   B HD11 1 
ATOM   5296 H HD12 . ILE   B 1 69  ? 46.981 -12.752 11.208  1.00 20.30 ?  69  ILE   B HD12 1 
ATOM   5297 H HD13 . ILE   B 1 69  ? 46.607 -11.649 10.127  1.00 20.30 ?  69  ILE   B HD13 1 
ATOM   5298 N N    . ALA   B 1 70  ? 50.007 -8.005  11.768  1.00 14.69 ?  70  ALA   B N    1 
ATOM   5299 C CA   . ALA   B 1 70  ? 50.290 -6.966  12.755  1.00 14.41 ?  70  ALA   B CA   1 
ATOM   5300 C C    . ALA   B 1 70  ? 49.289 -5.824  12.647  1.00 15.01 ?  70  ALA   B C    1 
ATOM   5301 O O    . ALA   B 1 70  ? 48.838 -5.283  13.662  1.00 15.78 ?  70  ALA   B O    1 
ATOM   5302 C CB   . ALA   B 1 70  ? 51.715 -6.448  12.572  1.00 14.68 ?  70  ALA   B CB   1 
ATOM   5303 H H    . ALA   B 1 70  ? 50.651 -8.182  11.231  1.00 17.65 ?  70  ALA   B H    1 
ATOM   5304 H HA   . ALA   B 1 70  ? 50.223 -7.347  13.642  1.00 17.31 ?  70  ALA   B HA   1 
ATOM   5305 H HB1  . ALA   B 1 70  ? 51.908 -5.796  13.266  1.00 17.63 ?  70  ALA   B HB1  1 
ATOM   5306 H HB2  . ALA   B 1 70  ? 52.337 -7.191  12.640  1.00 17.63 ?  70  ALA   B HB2  1 
ATOM   5307 H HB3  . ALA   B 1 70  ? 51.797 -6.032  11.698  1.00 17.63 ?  70  ALA   B HB3  1 
ATOM   5308 N N    . THR   B 1 71  ? 48.920 -5.454  11.424  1.00 15.11 ?  71  THR   B N    1 
ATOM   5309 C CA   . THR   B 1 71  ? 48.023 -4.323  11.213  1.00 15.84 ?  71  THR   B CA   1 
ATOM   5310 C C    . THR   B 1 71  ? 46.555 -4.695  11.420  1.00 16.99 ?  71  THR   B C    1 
ATOM   5311 O O    . THR   B 1 71  ? 45.774 -3.888  11.943  1.00 18.37 ?  71  THR   B O    1 
ATOM   5312 C CB   . THR   B 1 71  ? 48.242 -3.757  9.807   1.00 17.96 ?  71  THR   B CB   1 
ATOM   5313 O OG1  . THR   B 1 71  ? 49.569 -3.223  9.709   1.00 19.87 ?  71  THR   B OG1  1 
ATOM   5314 C CG2  . THR   B 1 71  ? 47.223 -2.678  9.475   1.00 18.69 ?  71  THR   B CG2  1 
ATOM   5315 H H    . THR   B 1 71  ? 49.173 -5.846  10.701  1.00 18.16 ?  71  THR   B H    1 
ATOM   5316 H HA   . THR   B 1 71  ? 48.245 -3.627  11.848  1.00 19.03 ?  71  THR   B HA   1 
ATOM   5317 H HB   . THR   B 1 71  ? 48.151 -4.466  9.155   1.00 21.58 ?  71  THR   B HB   1 
ATOM   5318 H HG1  . THR   B 1 71  ? 49.696 -2.891  8.942   1.00 23.87 ?  71  THR   B HG1  1 
ATOM   5319 H HG21 . THR   B 1 71  ? 47.525 -2.158  8.709   1.00 22.45 ?  71  THR   B HG21 1 
ATOM   5320 H HG22 . THR   B 1 71  ? 46.368 -3.076  9.262   1.00 22.45 ?  71  THR   B HG22 1 
ATOM   5321 H HG23 . THR   B 1 71  ? 47.116 -2.076  10.231  1.00 22.45 ?  71  THR   B HG23 1 
ATOM   5322 N N    . ASN   B 1 72  ? 46.162 -5.906  11.026  1.00 16.98 ?  72  ASN   B N    1 
ATOM   5323 C CA   . ASN   B 1 72  ? 44.759 -6.265  10.903  1.00 17.29 ?  72  ASN   B CA   1 
ATOM   5324 C C    . ASN   B 1 72  ? 44.291 -7.351  11.860  1.00 17.56 ?  72  ASN   B C    1 
ATOM   5325 O O    . ASN   B 1 72  ? 43.076 -7.505  12.034  1.00 19.41 ?  72  ASN   B O    1 
ATOM   5326 C CB   . ASN   B 1 72  ? 44.455 -6.705  9.462   1.00 18.20 ?  72  ASN   B CB   1 
ATOM   5327 C CG   . ASN   B 1 72  ? 44.737 -5.610  8.453   1.00 18.96 ?  72  ASN   B CG   1 
ATOM   5328 O OD1  . ASN   B 1 72  ? 45.763 -5.621  7.766   1.00 20.32 ?  72  ASN   B OD1  1 
ATOM   5329 N ND2  . ASN   B 1 72  ? 43.852 -4.638  8.385   1.00 20.57 ?  72  ASN   B ND2  1 
ATOM   5330 H H    . ASN   B 1 72  ? 46.704 -6.553  10.828  1.00 20.40 ?  72  ASN   B H    1 
ATOM   5331 H HA   . ASN   B 1 72  ? 44.228 -5.478  11.084  1.00 20.77 ?  72  ASN   B HA   1 
ATOM   5332 H HB2  . ASN   B 1 72  ? 45.009 -7.470  9.240   1.00 21.87 ?  72  ASN   B HB2  1 
ATOM   5333 H HB3  . ASN   B 1 72  ? 43.518 -6.939  9.395   1.00 21.87 ?  72  ASN   B HB3  1 
ATOM   5334 H HD21 . ASN   B 1 72  ? 43.966 -3.991  7.828   1.00 24.71 ?  72  ASN   B HD21 1 
ATOM   5335 H HD22 . ASN   B 1 72  ? 43.149 -4.659  8.879   1.00 24.71 ?  72  ASN   B HD22 1 
ATOM   5336 N N    . GLY   B 1 73  ? 45.195 -8.101  12.481  1.00 17.28 ?  73  GLY   B N    1 
ATOM   5337 C CA   . GLY   B 1 73  ? 44.805 -9.237  13.277  1.00 16.45 ?  73  GLY   B CA   1 
ATOM   5338 C C    . GLY   B 1 73  ? 44.446 -10.428 12.413  1.00 15.26 ?  73  GLY   B C    1 
ATOM   5339 O O    . GLY   B 1 73  ? 44.436 -10.354 11.182  1.00 14.93 ?  73  GLY   B O    1 
ATOM   5340 H H    . GLY   B 1 73  ? 46.048 -7.963  12.458  1.00 20.75 ?  73  GLY   B H    1 
ATOM   5341 H HA2  . GLY   B 1 73  ? 45.536 -9.486  13.868  1.00 19.76 ?  73  GLY   B HA2  1 
ATOM   5342 H HA3  . GLY   B 1 73  ? 44.036 -9.005  13.821  1.00 19.76 ?  73  GLY   B HA3  1 
ATOM   5343 N N    . PRO   B 1 74  ? 44.142 -11.552 13.058  1.00 15.19 ?  74  PRO   B N    1 
ATOM   5344 C CA   . PRO   B 1 74  ? 43.882 -12.791 12.321  1.00 14.55 ?  74  PRO   B CA   1 
ATOM   5345 C C    . PRO   B 1 74  ? 42.594 -12.731 11.513  1.00 14.39 ?  74  PRO   B C    1 
ATOM   5346 O O    . PRO   B 1 74  ? 41.656 -11.994 11.832  1.00 15.98 ?  74  PRO   B O    1 
ATOM   5347 C CB   . PRO   B 1 74  ? 43.780 -13.840 13.436  1.00 15.73 ?  74  PRO   B CB   1 
ATOM   5348 C CG   . PRO   B 1 74  ? 43.366 -13.065 14.650  1.00 17.39 ?  74  PRO   B CG   1 
ATOM   5349 C CD   . PRO   B 1 74  ? 44.056 -11.740 14.517  1.00 16.76 ?  74  PRO   B CD   1 
ATOM   5350 H HA   . PRO   B 1 74  ? 44.633 -13.004 11.739  1.00 17.48 ?  74  PRO   B HA   1 
ATOM   5351 H HB2  . PRO   B 1 74  ? 43.109 -14.500 13.200  1.00 18.90 ?  74  PRO   B HB2  1 
ATOM   5352 H HB3  . PRO   B 1 74  ? 44.644 -14.261 13.573  1.00 18.90 ?  74  PRO   B HB3  1 
ATOM   5353 H HG2  . PRO   B 1 74  ? 42.401 -12.949 14.651  1.00 20.88 ?  74  PRO   B HG2  1 
ATOM   5354 H HG3  . PRO   B 1 74  ? 43.657 -13.524 15.451  1.00 20.88 ?  74  PRO   B HG3  1 
ATOM   5355 H HD2  . PRO   B 1 74  ? 43.517 -11.036 14.922  1.00 20.13 ?  74  PRO   B HD2  1 
ATOM   5356 H HD3  . PRO   B 1 74  ? 44.941 -11.777 14.911  1.00 20.13 ?  74  PRO   B HD3  1 
ATOM   5357 N N    . LEU   B 1 75  ? 42.561 -13.539 10.460  1.00 13.66 ?  75  LEU   B N    1 
ATOM   5358 C CA   . LEU   B 1 75  ? 41.350 -13.743 9.686   1.00 13.79 ?  75  LEU   B CA   1 
ATOM   5359 C C    . LEU   B 1 75  ? 40.360 -14.581 10.490  1.00 14.06 ?  75  LEU   B C    1 
ATOM   5360 O O    . LEU   B 1 75  ? 40.699 -15.170 11.514  1.00 15.04 ?  75  LEU   B O    1 
ATOM   5361 C CB   . LEU   B 1 75  ? 41.669 -14.473 8.382   1.00 13.55 ?  75  LEU   B CB   1 
ATOM   5362 C CG   . LEU   B 1 75  ? 42.509 -13.715 7.348   1.00 15.76 ?  75  LEU   B CG   1 
ATOM   5363 C CD1  . LEU   B 1 75  ? 42.710 -14.540 6.082   1.00 17.39 ?  75  LEU   B CD1  1 
ATOM   5364 C CD2  . LEU   B 1 75  ? 41.901 -12.382 7.014   1.00 19.23 ?  75  LEU   B CD2  1 
ATOM   5365 H H    . LEU   B 1 75  ? 43.242 -13.991 10.171  1.00 16.42 ?  75  LEU   B H    1 
ATOM   5366 H HA   . LEU   B 1 75  ? 40.944 -12.888 9.480   1.00 16.57 ?  75  LEU   B HA   1 
ATOM   5367 H HB2  . LEU   B 1 75  ? 42.153 -15.288 8.599   1.00 16.28 ?  75  LEU   B HB2  1 
ATOM   5368 H HB3  . LEU   B 1 75  ? 40.832 -14.708 7.951   1.00 16.28 ?  75  LEU   B HB3  1 
ATOM   5369 H HG   . LEU   B 1 75  ? 43.388 -13.549 7.726   1.00 18.94 ?  75  LEU   B HG   1 
ATOM   5370 H HD11 . LEU   B 1 75  ? 43.253 -14.033 5.454   1.00 20.89 ?  75  LEU   B HD11 1 
ATOM   5371 H HD12 . LEU   B 1 75  ? 43.162 -15.369 6.310   1.00 20.89 ?  75  LEU   B HD12 1 
ATOM   5372 H HD13 . LEU   B 1 75  ? 41.846 -14.733 5.687   1.00 20.89 ?  75  LEU   B HD13 1 
ATOM   5373 H HD21 . LEU   B 1 75  ? 42.373 -11.997 6.259   1.00 23.09 ?  75  LEU   B HD21 1 
ATOM   5374 H HD22 . LEU   B 1 75  ? 40.967 -12.510 6.792   1.00 23.09 ?  75  LEU   B HD22 1 
ATOM   5375 H HD23 . LEU   B 1 75  ? 41.981 -11.795 7.785   1.00 23.09 ?  75  LEU   B HD23 1 
ATOM   5376 N N    . LYS   B 1 76  ? 39.122 -14.638 9.998   1.00 15.82 ?  76  LYS   B N    1 
ATOM   5377 C CA   . LYS   B 1 76  ? 38.136 -15.596 10.479  1.00 17.15 ?  76  LYS   B CA   1 
ATOM   5378 C C    . LYS   B 1 76  ? 38.236 -16.877 9.659   1.00 15.71 ?  76  LYS   B C    1 
ATOM   5379 O O    . LYS   B 1 76  ? 38.522 -16.836 8.466   1.00 15.07 ?  76  LYS   B O    1 
ATOM   5380 C CB   . LYS   B 1 76  ? 36.714 -15.046 10.289  1.00 18.55 ?  76  LYS   B CB   1 
ATOM   5381 C CG   . LYS   B 1 76  ? 36.423 -13.673 10.910  1.00 19.92 ?  76  LYS   B CG   1 
ATOM   5382 C CD   . LYS   B 1 76  ? 35.011 -13.169 10.557  1.00 20.86 ?  76  LYS   B CD   1 
ATOM   5383 C CE   . LYS   B 1 76  ? 34.740 -11.799 11.168  1.00 23.08 ?  76  LYS   B CE   1 
ATOM   5384 N NZ   . LYS   B 1 76  ? 33.463 -11.182 10.718  1.00 23.71 ?  76  LYS   B NZ   1 
ATOM   5385 H H    . LYS   B 1 76  ? 38.832 -14.130 9.365   1.00 19.01 ?  76  LYS   B H    1 
ATOM   5386 H HA   . LYS   B 1 76  ? 38.293 -15.805 11.410  1.00 20.60 ?  76  LYS   B HA   1 
ATOM   5387 H HB2  . LYS   B 1 76  ? 36.546 -14.978 9.337   1.00 22.28 ?  76  LYS   B HB2  1 
ATOM   5388 H HB3  . LYS   B 1 76  ? 36.097 -15.680 10.681  1.00 22.28 ?  76  LYS   B HB3  1 
ATOM   5389 H HG2  . LYS   B 1 76  ? 36.496 -13.741 11.875  1.00 23.93 ?  76  LYS   B HG2  1 
ATOM   5390 H HG3  . LYS   B 1 76  ? 37.072 -13.031 10.573  1.00 23.93 ?  76  LYS   B HG3  1 
ATOM   5391 H HD2  . LYS   B 1 76  ? 34.929 -13.098 9.591   1.00 25.06 ?  76  LYS   B HD2  1 
ATOM   5392 H HD3  . LYS   B 1 76  ? 34.355 -13.795 10.902  1.00 25.06 ?  76  LYS   B HD3  1 
ATOM   5393 H HE2  . LYS   B 1 76  ? 34.705 -11.891 12.130  1.00 27.72 ?  76  LYS   B HE2  1 
ATOM   5394 H HE3  . LYS   B 1 76  ? 35.462 -11.202 10.918  1.00 27.72 ?  76  LYS   B HE3  1 
ATOM   5395 H HZ1  . LYS   B 1 76  ? 33.356 -10.384 11.105  1.00 28.48 ?  76  LYS   B HZ1  1 
ATOM   5396 H HZ2  . LYS   B 1 76  ? 33.465 -11.072 9.834   1.00 28.48 ?  76  LYS   B HZ2  1 
ATOM   5397 H HZ3  . LYS   B 1 76  ? 32.774 -11.701 10.941  1.00 28.48 ?  76  LYS   B HZ3  1 
ATOM   5398 N N    . VAL   B 1 77  ? 37.988 -18.023 10.304  1.00 16.38 ?  77  VAL   B N    1 
ATOM   5399 C CA   . VAL   B 1 77  ? 37.787 -19.246 9.535   1.00 16.42 ?  77  VAL   B CA   1 
ATOM   5400 C C    . VAL   B 1 77  ? 36.596 -19.024 8.617   1.00 14.76 ?  77  VAL   B C    1 
ATOM   5401 O O    . VAL   B 1 77  ? 35.529 -18.588 9.064   1.00 15.14 ?  77  VAL   B O    1 
ATOM   5402 C CB   . VAL   B 1 77  ? 37.579 -20.454 10.460  1.00 17.97 ?  77  VAL   B CB   1 
ATOM   5403 C CG1  . VAL   B 1 77  ? 37.282 -21.697 9.625   1.00 18.54 ?  77  VAL   B CG1  1 
ATOM   5404 C CG2  . VAL   B 1 77  ? 38.805 -20.674 11.344  1.00 19.11 ?  77  VAL   B CG2  1 
ATOM   5405 H H    . VAL   B 1 77  ? 37.944 -18.116 11.151  1.00 19.68 ?  77  VAL   B H    1 
ATOM   5406 H HA   . VAL   B 1 77  ? 38.564 -19.415 8.978   1.00 19.73 ?  77  VAL   B HA   1 
ATOM   5407 H HB   . VAL   B 1 77  ? 36.812 -20.285 11.030  1.00 21.58 ?  77  VAL   B HB   1 
ATOM   5408 H HG11 . VAL   B 1 77  ? 37.320 -22.475 10.200  1.00 22.27 ?  77  VAL   B HG11 1 
ATOM   5409 H HG12 . VAL   B 1 77  ? 36.395 -21.619 9.235   1.00 22.27 ?  77  VAL   B HG12 1 
ATOM   5410 H HG13 . VAL   B 1 77  ? 37.946 -21.771 8.922   1.00 22.27 ?  77  VAL   B HG13 1 
ATOM   5411 H HG21 . VAL   B 1 77  ? 38.660 -21.463 11.883  1.00 22.96 ?  77  VAL   B HG21 1 
ATOM   5412 H HG22 . VAL   B 1 77  ? 39.580 -20.790 10.777  1.00 22.96 ?  77  VAL   B HG22 1 
ATOM   5413 H HG23 . VAL   B 1 77  ? 38.919 -19.896 11.912  1.00 22.96 ?  77  VAL   B HG23 1 
ATOM   5414 N N    . GLY   B 1 78  ? 36.775 -19.310 7.330   1.00 13.92 ?  78  GLY   B N    1 
ATOM   5415 C CA   . GLY   B 1 78  ? 35.804 -18.995 6.312   1.00 13.87 ?  78  GLY   B CA   1 
ATOM   5416 C C    . GLY   B 1 78  ? 36.051 -17.685 5.598   1.00 13.75 ?  78  GLY   B C    1 
ATOM   5417 O O    . GLY   B 1 78  ? 35.365 -17.408 4.606   1.00 13.91 ?  78  GLY   B O    1 
ATOM   5418 H H    . GLY   B 1 78  ? 37.473 -19.707 7.019   1.00 16.73 ?  78  GLY   B H    1 
ATOM   5419 H HA2  . GLY   B 1 78  ? 35.796 -19.693 5.649   1.00 16.66 ?  78  GLY   B HA2  1 
ATOM   5420 H HA3  . GLY   B 1 78  ? 34.924 -18.948 6.720   1.00 16.66 ?  78  GLY   B HA3  1 
ATOM   5421 N N    . GLY   B 1 79  ? 37.000 -16.875 6.079   1.00 13.74 ?  79  GLY   B N    1 
ATOM   5422 C CA   . GLY   B 1 79  ? 37.305 -15.588 5.488   1.00 13.90 ?  79  GLY   B CA   1 
ATOM   5423 C C    . GLY   B 1 79  ? 38.537 -15.620 4.591   1.00 13.11 ?  79  GLY   B C    1 
ATOM   5424 O O    . GLY   B 1 79  ? 39.150 -16.659 4.350   1.00 13.50 ?  79  GLY   B O    1 
ATOM   5425 H H    . GLY   B 1 79  ? 37.497 -17.058 6.758   1.00 16.51 ?  79  GLY   B H    1 
ATOM   5426 H HA2  . GLY   B 1 79  ? 36.552 -15.289 4.954   1.00 16.70 ?  79  GLY   B HA2  1 
ATOM   5427 H HA3  . GLY   B 1 79  ? 37.458 -14.935 6.190   1.00 16.70 ?  79  GLY   B HA3  1 
ATOM   5428 N N    . SER   B 1 80  ? 38.901 -14.436 4.101   1.00 13.13 ?  80  SER   B N    1 
ATOM   5429 C CA   . SER   B 1 80  ? 40.016 -14.313 3.171   1.00 12.56 ?  80  SER   B CA   1 
ATOM   5430 C C    . SER   B 1 80  ? 40.608 -12.910 3.227   1.00 12.25 ?  80  SER   B C    1 
ATOM   5431 O O    . SER   B 1 80  ? 39.992 -11.968 3.732   1.00 13.55 ?  80  SER   B O    1 
ATOM   5432 C CB   . SER   B 1 80  ? 39.581 -14.605 1.732   1.00 13.08 ?  80  SER   B CB   1 
ATOM   5433 O OG   . SER   B 1 80  ? 38.726 -13.588 1.231   1.00 14.37 ?  80  SER   B OG   1 
ATOM   5434 H H    . SER   B 1 80  ? 38.529 -13.688 4.298   1.00 15.78 ?  80  SER   B H    1 
ATOM   5435 H HA   . SER   B 1 80  ? 40.704 -14.948 3.419   1.00 15.10 ?  80  SER   B HA   1 
ATOM   5436 H HB2  . SER   B 1 80  ? 40.366 -14.651 1.163   1.00 15.72 ?  80  SER   B HB2  1 
ATOM   5437 H HB3  . SER   B 1 80  ? 39.106 -15.450 1.708   1.00 15.72 ?  80  SER   B HB3  1 
ATOM   5438 H HG   . SER   B 1 80  ? 38.033 -13.533 1.713   1.00 17.26 ?  80  SER   B HG   1 
ATOM   5439 N N    . CYS   B 1 81  ? 41.791 -12.770 2.635   1.00 12.04 ?  81  CYS   B N    1 
ATOM   5440 C CA   . CYS   B 1 81  ? 42.348 -11.458 2.325   1.00 12.26 ?  81  CYS   B CA   1 
ATOM   5441 C C    . CYS   B 1 81  ? 43.114 -11.539 1.012   1.00 11.71 ?  81  CYS   B C    1 
ATOM   5442 O O    . CYS   B 1 81  ? 43.609 -12.605 0.631   1.00 12.76 ?  81  CYS   B O    1 
ATOM   5443 C CB   . CYS   B 1 81  ? 43.247 -10.907 3.442   1.00 13.13 ?  81  CYS   B CB   1 
ATOM   5444 S SG   . CYS   B 1 81  ? 44.753 -11.854 3.692   1.00 13.94 ?  81  CYS   B SG   1 
ATOM   5445 H H    . CYS   B 1 81  ? 42.301 -13.426 2.393   1.00 14.48 ?  81  CYS   B H    1 
ATOM   5446 H HA   . CYS   B 1 81  ? 41.613 -10.832 2.199   1.00 14.73 ?  81  CYS   B HA   1 
ATOM   5447 H HB2  . CYS   B 1 81  ? 43.501 -9.997  3.220   1.00 15.78 ?  81  CYS   B HB2  1 
ATOM   5448 H HB3  . CYS   B 1 81  ? 42.744 -10.909 4.275   1.00 15.78 ?  81  CYS   B HB3  1 
ATOM   5449 H HG   . CYS   B 1 81  ? 45.381 -11.352 4.590   1.00 16.75 ?  81  CYS   B HG   1 
ATOM   5450 N N    . VAL   B 1 82  ? 43.222 -10.398 0.332   1.00 12.34 ?  82  VAL   B N    1 
ATOM   5451 C CA   . VAL   B 1 82  ? 43.987 -10.280 -0.908  1.00 12.56 ?  82  VAL   B CA   1 
ATOM   5452 C C    . VAL   B 1 82  ? 45.329 -9.635  -0.596  1.00 12.99 ?  82  VAL   B C    1 
ATOM   5453 O O    . VAL   B 1 82  ? 45.384 -8.520  -0.057  1.00 13.40 ?  82  VAL   B O    1 
ATOM   5454 C CB   . VAL   B 1 82  ? 43.236 -9.452  -1.962  1.00 13.89 ?  82  VAL   B CB   1 
ATOM   5455 C CG1  . VAL   B 1 82  ? 44.065 -9.338  -3.235  1.00 15.41 ?  82  VAL   B CG1  1 
ATOM   5456 C CG2  . VAL   B 1 82  ? 41.882 -10.068 -2.257  1.00 14.91 ?  82  VAL   B CG2  1 
ATOM   5457 H H    . VAL   B 1 82  ? 42.850 -9.654  0.572   1.00 14.83 ?  82  VAL   B H    1 
ATOM   5458 H HA   . VAL   B 1 82  ? 44.146 -11.163 -1.270  1.00 15.09 ?  82  VAL   B HA   1 
ATOM   5459 H HB   . VAL   B 1 82  ? 43.087 -8.560  -1.623  1.00 16.70 ?  82  VAL   B HB   1 
ATOM   5460 H HG11 . VAL   B 1 82  ? 43.504 -9.013  -3.954  1.00 18.51 ?  82  VAL   B HG11 1 
ATOM   5461 H HG12 . VAL   B 1 82  ? 44.799 -8.723  -3.084  1.00 18.51 ?  82  VAL   B HG12 1 
ATOM   5462 H HG13 . VAL   B 1 82  ? 44.415 -10.217 -3.465  1.00 18.51 ?  82  VAL   B HG13 1 
ATOM   5463 H HG21 . VAL   B 1 82  ? 41.447 -9.564  -2.962  1.00 17.91 ?  82  VAL   B HG21 1 
ATOM   5464 H HG22 . VAL   B 1 82  ? 42.007 -10.990 -2.543  1.00 17.91 ?  82  VAL   B HG22 1 
ATOM   5465 H HG23 . VAL   B 1 82  ? 41.341 -10.047 -1.452  1.00 17.91 ?  82  VAL   B HG23 1 
ATOM   5466 N N    . LEU   B 1 83  ? 46.407 -10.333 -0.948  1.00 12.03 ?  83  LEU   B N    1 
ATOM   5467 C CA   . LEU   B 1 83  ? 47.762 -9.815  -0.836  1.00 12.31 ?  83  LEU   B CA   1 
ATOM   5468 C C    . LEU   B 1 83  ? 48.457 -9.967  -2.188  1.00 12.56 ?  83  LEU   B C    1 
ATOM   5469 O O    . LEU   B 1 83  ? 47.854 -10.404 -3.174  1.00 11.76 ?  83  LEU   B O    1 
ATOM   5470 C CB   . LEU   B 1 83  ? 48.521 -10.501 0.309   1.00 12.84 ?  83  LEU   B CB   1 
ATOM   5471 C CG   . LEU   B 1 83  ? 48.008 -10.147 1.710   1.00 13.65 ?  83  LEU   B CG   1 
ATOM   5472 C CD1  . LEU   B 1 83  ? 48.635 -11.020 2.777   1.00 14.37 ?  83  LEU   B CD1  1 
ATOM   5473 C CD2  . LEU   B 1 83  ? 48.221 -8.665  2.036   1.00 15.03 ?  83  LEU   B CD2  1 
ATOM   5474 H H    . LEU   B 1 83  ? 46.370 -11.141 -1.258  1.00 14.46 ?  83  LEU   B H    1 
ATOM   5475 H HA   . LEU   B 1 83  ? 47.711 -8.871  -0.641  1.00 14.79 ?  83  LEU   B HA   1 
ATOM   5476 H HB2  . LEU   B 1 83  ? 48.452 -11.460 0.197   1.00 15.44 ?  83  LEU   B HB2  1 
ATOM   5477 H HB3  . LEU   B 1 83  ? 49.453 -10.233 0.258   1.00 15.44 ?  83  LEU   B HB3  1 
ATOM   5478 H HG   . LEU   B 1 83  ? 47.054 -10.312 1.728   1.00 16.40 ?  83  LEU   B HG   1 
ATOM   5479 H HD11 . LEU   B 1 83  ? 48.275 -10.773 3.642   1.00 17.26 ?  83  LEU   B HD11 1 
ATOM   5480 H HD12 . LEU   B 1 83  ? 48.420 -11.953 2.589   1.00 17.26 ?  83  LEU   B HD12 1 
ATOM   5481 H HD13 . LEU   B 1 83  ? 49.596 -10.899 2.767   1.00 17.26 ?  83  LEU   B HD13 1 
ATOM   5482 H HD21 . LEU   B 1 83  ? 48.021 -8.518  2.973   1.00 18.06 ?  83  LEU   B HD21 1 
ATOM   5483 H HD22 . LEU   B 1 83  ? 49.143 -8.430  1.852   1.00 18.06 ?  83  LEU   B HD22 1 
ATOM   5484 H HD23 . LEU   B 1 83  ? 47.627 -8.132  1.483   1.00 18.06 ?  83  LEU   B HD23 1 
ATOM   5485 N N    . SER   B 1 84  ? 49.733 -9.598  -2.239  1.00 13.50 ?  84  SER   B N    1 
ATOM   5486 C CA   . SER   B 1 84  ? 50.470 -9.729  -3.485  1.00 13.80 ?  84  SER   B CA   1 
ATOM   5487 C C    . SER   B 1 84  ? 50.634 -11.194 -3.877  1.00 12.43 ?  84  SER   B C    1 
ATOM   5488 O O    . SER   B 1 84  ? 50.742 -12.079 -3.033  1.00 11.82 ?  84  SER   B O    1 
ATOM   5489 C CB   . SER   B 1 84  ? 51.861 -9.113  -3.339  1.00 15.24 ?  84  SER   B CB   1 
ATOM   5490 O OG   . SER   B 1 84  ? 52.613 -9.327  -4.519  1.00 16.74 ?  84  SER   B OG   1 
ATOM   5491 H H    . SER   B 1 84  ? 50.168 -9.253  -1.585  1.00 16.22 ?  84  SER   B H    1 
ATOM   5492 H HA   . SER   B 1 84  ? 50.000 -9.270  -4.195  1.00 16.58 ?  84  SER   B HA   1 
ATOM   5493 H HB2  . SER   B 1 84  ? 51.769 -8.157  -3.180  1.00 18.31 ?  84  SER   B HB2  1 
ATOM   5494 H HB3  . SER   B 1 84  ? 52.314 -9.527  -2.584  1.00 18.31 ?  84  SER   B HB3  1 
ATOM   5495 H HG   . SER   B 1 84  ? 53.383 -8.980  -4.425  1.00 20.11 ?  84  SER   B HG   1 
ATOM   5496 N N    . GLY   B 1 85  ? 50.692 -11.433 -5.178  1.00 13.23 ?  85  GLY   B N    1 
ATOM   5497 C CA   . GLY   B 1 85  ? 51.043 -12.736 -5.692  1.00 14.06 ?  85  GLY   B CA   1 
ATOM   5498 C C    . GLY   B 1 85  ? 52.513 -12.928 -6.008  1.00 13.67 ?  85  GLY   B C    1 
ATOM   5499 O O    . GLY   B 1 85  ? 52.895 -14.009 -6.467  1.00 13.58 ?  85  GLY   B O    1 
ATOM   5500 H H    . GLY   B 1 85  ? 50.535 -10.854 -5.784  1.00 15.90 ?  85  GLY   B H    1 
ATOM   5501 H HA2  . GLY   B 1 85  ? 50.790 -13.415 -5.041  1.00 16.89 ?  85  GLY   B HA2  1 
ATOM   5502 H HA3  . GLY   B 1 85  ? 50.544 -12.902 -6.502  1.00 16.89 ?  85  GLY   B HA3  1 
ATOM   5503 N N    . HIS   B 1 86  ? 53.362 -11.921 -5.796  1.00 13.18 ?  86  HIS   B N    1 
ATOM   5504 C CA   . HIS   B 1 86  ? 54.826 -12.079 -5.882  1.00 13.49 ?  86  HIS   B CA   1 
ATOM   5505 C C    . HIS   B 1 86  ? 55.200 -12.603 -7.267  1.00 13.85 ?  86  HIS   B C    1 
ATOM   5506 O O    . HIS   B 1 86  ? 54.807 -11.999 -8.278  1.00 14.51 ?  86  HIS   B O    1 
ATOM   5507 C CB   . HIS   B 1 86  ? 55.320 -12.910 -4.700  1.00 14.44 ?  86  HIS   B CB   1 
ATOM   5508 C CG   . HIS   B 1 86  ? 55.005 -12.295 -3.378  1.00 14.38 ?  86  HIS   B CG   1 
ATOM   5509 N ND1  . HIS   B 1 86  ? 55.844 -11.397 -2.756  1.00 15.92 ?  86  HIS   B ND1  1 
ATOM   5510 C CD2  . HIS   B 1 86  ? 53.926 -12.429 -2.571  1.00 14.50 ?  86  HIS   B CD2  1 
ATOM   5511 C CE1  . HIS   B 1 86  ? 55.290 -10.998 -1.624  1.00 15.56 ?  86  HIS   B CE1  1 
ATOM   5512 N NE2  . HIS   B 1 86  ? 54.123 -11.606 -1.491  1.00 14.72 ?  86  HIS   B NE2  1 
ATOM   5513 H H    . HIS   B 1 86  ? 53.118 -11.124 -5.597  1.00 15.84 ?  86  HIS   B H    1 
ATOM   5514 H HA   . HIS   B 1 86  ? 55.232 -11.204 -5.792  1.00 16.22 ?  86  HIS   B HA   1 
ATOM   5515 H HB2  . HIS   B 1 86  ? 54.902 -13.787 -4.728  1.00 17.35 ?  86  HIS   B HB2  1 
ATOM   5516 H HB3  . HIS   B 1 86  ? 56.286 -13.007 -4.757  1.00 17.35 ?  86  HIS   B HB3  1 
ATOM   5517 H HD2  . HIS   B 1 86  ? 53.175 -12.958 -2.732  1.00 17.42 ?  86  HIS   B HD2  1 
ATOM   5518 H HE1  . HIS   B 1 86  ? 55.665 -10.411 -1.009  1.00 18.69 ?  86  HIS   B HE1  1 
ATOM   5519 H HE2  . HIS   B 1 86  ? 53.582 -11.518 -0.823  1.00 17.69 ?  86  HIS   B HE2  1 
ATOM   5520 N N    . ASN   B 1 87  ? 55.964 -13.689 -7.367  1.00 14.34 ?  87  ASN   B N    1 
ATOM   5521 C CA   . ASN   B 1 87  ? 56.359 -14.263 -8.644  1.00 15.20 ?  87  ASN   B CA   1 
ATOM   5522 C C    . ASN   B 1 87  ? 55.376 -15.303 -9.153  1.00 15.50 ?  87  ASN   B C    1 
ATOM   5523 O O    . ASN   B 1 87  ? 55.688 -16.000 -10.123 1.00 17.10 ?  87  ASN   B O    1 
ATOM   5524 C CB   . ASN   B 1 87  ? 57.751 -14.893 -8.528  1.00 16.85 ?  87  ASN   B CB   1 
ATOM   5525 C CG   . ASN   B 1 87  ? 57.803 -16.012 -7.493  1.00 17.70 ?  87  ASN   B CG   1 
ATOM   5526 O OD1  . ASN   B 1 87  ? 57.178 -15.922 -6.429  1.00 16.65 ?  87  ASN   B OD1  1 
ATOM   5527 N ND2  . ASN   B 1 87  ? 58.530 -17.091 -7.814  1.00 19.92 ?  87  ASN   B ND2  1 
ATOM   5528 H H    . ASN   B 1 87  ? 56.267 -14.126 -6.691  1.00 17.23 ?  87  ASN   B H    1 
ATOM   5529 H HA   . ASN   B 1 87  ? 56.408 -13.561 -9.303  1.00 18.26 ?  87  ASN   B HA   1 
ATOM   5530 H HB2  . ASN   B 1 87  ? 58.004 -15.269 -9.390  1.00 20.24 ?  87  ASN   B HB2  1 
ATOM   5531 H HB3  . ASN   B 1 87  ? 58.387 -14.213 -8.265  1.00 20.24 ?  87  ASN   B HB3  1 
ATOM   5532 H HD21 . ASN   B 1 87  ? 58.594 -17.749 -7.265  1.00 23.92 ?  87  ASN   B HD21 1 
ATOM   5533 H HD22 . ASN   B 1 87  ? 58.946 -17.125 -8.571  1.00 23.92 ?  87  ASN   B HD22 1 
ATOM   5534 N N    . LEU   B 1 88  ? 54.198 -15.409 -8.537  1.00 14.01 ?  88  LEU   B N    1 
ATOM   5535 C CA   . LEU   B 1 88  ? 53.217 -16.439 -8.862  1.00 14.13 ?  88  LEU   B CA   1 
ATOM   5536 C C    . LEU   B 1 88  ? 51.986 -15.920 -9.584  1.00 13.85 ?  88  LEU   B C    1 
ATOM   5537 O O    . LEU   B 1 88  ? 51.382 -16.669 -10.361 1.00 15.68 ?  88  LEU   B O    1 
ATOM   5538 C CB   . LEU   B 1 88  ? 52.747 -17.125 -7.577  1.00 15.09 ?  88  LEU   B CB   1 
ATOM   5539 C CG   . LEU   B 1 88  ? 53.871 -17.777 -6.786  1.00 17.51 ?  88  LEU   B CG   1 
ATOM   5540 C CD1  . LEU   B 1 88  ? 53.379 -18.199 -5.414  1.00 19.08 ?  88  LEU   B CD1  1 
ATOM   5541 C CD2  . LEU   B 1 88  ? 54.423 -18.959 -7.560  1.00 20.53 ?  88  LEU   B CD2  1 
ATOM   5542 H H    . LEU   B 1 88  ? 53.939 -14.884 -7.901  1.00 16.83 ?  88  LEU   B H    1 
ATOM   5543 H HA   . LEU   B 1 88  ? 53.625 -17.099 -9.430  1.00 16.97 ?  88  LEU   B HA   1 
ATOM   5544 H HB2  . LEU   B 1 88  ? 52.319 -16.472 -7.004  1.00 18.13 ?  88  LEU   B HB2  1 
ATOM   5545 H HB3  . LEU   B 1 88  ? 52.108 -17.821 -7.812  1.00 18.13 ?  88  LEU   B HB3  1 
ATOM   5546 H HG   . LEU   B 1 88  ? 54.585 -17.135 -6.662  1.00 21.03 ?  88  LEU   B HG   1 
ATOM   5547 H HD11 . LEU   B 1 88  ? 54.076 -18.703 -4.968  1.00 22.92 ?  88  LEU   B HD11 1 
ATOM   5548 H HD12 . LEU   B 1 88  ? 53.156 -17.409 -4.899  1.00 22.92 ?  88  LEU   B HD12 1 
ATOM   5549 H HD13 . LEU   B 1 88  ? 52.589 -18.755 -5.523  1.00 22.92 ?  88  LEU   B HD13 1 
ATOM   5550 H HD21 . LEU   B 1 88  ? 55.043 -19.443 -6.993  1.00 24.66 ?  88  LEU   B HD21 1 
ATOM   5551 H HD22 . LEU   B 1 88  ? 53.689 -19.537 -7.819  1.00 24.66 ?  88  LEU   B HD22 1 
ATOM   5552 H HD23 . LEU   B 1 88  ? 54.882 -18.632 -8.350  1.00 24.66 ?  88  LEU   B HD23 1 
ATOM   5553 N N    . ALA   B 1 89  ? 51.587 -14.681 -9.319  1.00 12.73 ?  89  ALA   B N    1 
ATOM   5554 C CA   . ALA   B 1 89  ? 50.299 -14.172 -9.768  1.00 12.16 ?  89  ALA   B CA   1 
ATOM   5555 C C    . ALA   B 1 89  ? 50.282 -12.684 -9.476  1.00 13.05 ?  89  ALA   B C    1 
ATOM   5556 O O    . ALA   B 1 89  ? 51.102 -12.181 -8.707  1.00 13.46 ?  89  ALA   B O    1 
ATOM   5557 C CB   . ALA   B 1 89  ? 49.151 -14.834 -9.009  1.00 12.23 ?  89  ALA   B CB   1 
ATOM   5558 H H    . ALA   B 1 89  ? 52.045 -14.097 -8.878  1.00 15.30 ?  89  ALA   B H    1 
ATOM   5559 H HA   . ALA   B 1 89  ? 50.183 -14.317 -10.725 1.00 14.61 ?  89  ALA   B HA   1 
ATOM   5560 H HB1  . ALA   B 1 89  ? 48.307 -14.484 -9.345  1.00 14.70 ?  89  ALA   B HB1  1 
ATOM   5561 H HB2  . ALA   B 1 89  ? 49.192 -15.791 -9.156  1.00 14.70 ?  89  ALA   B HB2  1 
ATOM   5562 H HB3  . ALA   B 1 89  ? 49.242 -14.633 -8.069  1.00 14.70 ?  89  ALA   B HB3  1 
ATOM   5563 N N    . LYS   B 1 90  ? 49.309 -11.982 -10.054 1.00 13.92 ?  90  LYS   B N    1 
ATOM   5564 C CA   . LYS   B 1 90  ? 49.126 -10.595 -9.646  1.00 13.86 ?  90  LYS   B CA   1 
ATOM   5565 C C    . LYS   B 1 90  ? 48.804 -10.525 -8.158  1.00 13.07 ?  90  LYS   B C    1 
ATOM   5566 O O    . LYS   B 1 90  ? 49.457 -9.790  -7.400  1.00 14.20 ?  90  LYS   B O    1 
ATOM   5567 C CB   . LYS   B 1 90  ? 48.049 -9.929  -10.499 1.00 15.36 ?  90  LYS   B CB   1 
ATOM   5568 C CG   . LYS   B 1 90  ? 47.739 -8.499  -10.090 1.00 15.74 ?  90  LYS   B CG   1 
ATOM   5569 C CD   . LYS   B 1 90  ? 48.936 -7.587  -10.173 1.00 18.28 ?  90  LYS   B CD   1 
ATOM   5570 C CE   . LYS   B 1 90  ? 48.472 -6.182  -9.880  1.00 19.97 ?  90  LYS   B CE   1 
ATOM   5571 N NZ   . LYS   B 1 90  ? 49.609 -5.238  -9.834  1.00 19.36 ?  90  LYS   B NZ   1 
ATOM   5572 H H    . LYS   B 1 90  ? 48.767 -12.271 -10.663 1.00 16.73 ?  90  LYS   B H    1 
ATOM   5573 H HA   . LYS   B 1 90  ? 49.952 -10.117 -9.794  1.00 16.66 ?  90  LYS   B HA   1 
ATOM   5574 H HB2  . LYS   B 1 90  ? 48.346 -9.908  -11.426 1.00 18.45 ?  90  LYS   B HB2  1 
ATOM   5575 H HB3  . LYS   B 1 90  ? 47.227 -10.440 -10.435 1.00 18.45 ?  90  LYS   B HB3  1 
ATOM   5576 H HG2  . LYS   B 1 90  ? 47.051 -8.143  -10.680 1.00 18.92 ?  90  LYS   B HG2  1 
ATOM   5577 H HG3  . LYS   B 1 90  ? 47.412 -8.491  -9.174  1.00 18.92 ?  90  LYS   B HG3  1 
ATOM   5578 H HD2  . LYS   B 1 90  ? 49.594 -7.842  -9.508  1.00 21.96 ?  90  LYS   B HD2  1 
ATOM   5579 H HD3  . LYS   B 1 90  ? 49.312 -7.614  -11.065 1.00 21.96 ?  90  LYS   B HD3  1 
ATOM   5580 H HE2  . LYS   B 1 90  ? 47.865 -5.883  -10.579 1.00 23.99 ?  90  LYS   B HE2  1 
ATOM   5581 H HE3  . LYS   B 1 90  ? 48.025 -6.153  -9.019  1.00 23.99 ?  90  LYS   B HE3  1 
ATOM   5582 H HZ1  . LYS   B 1 90  ? 49.320 -4.410  -9.663  1.00 23.25 ?  90  LYS   B HZ1  1 
ATOM   5583 H HZ2  . LYS   B 1 90  ? 50.182 -5.477  -9.197  1.00 23.25 ?  90  LYS   B HZ2  1 
ATOM   5584 H HZ3  . LYS   B 1 90  ? 50.035 -5.232  -10.617 1.00 23.25 ?  90  LYS   B HZ3  1 
ATOM   5585 N N    . HIS   B 1 91  ? 47.831 -11.333 -7.717  1.00 12.16 ?  91  HIS   B N    1 
ATOM   5586 C CA   . HIS   B 1 91  ? 47.361 -11.355 -6.345  1.00 12.38 ?  91  HIS   B CA   1 
ATOM   5587 C C    . HIS   B 1 91  ? 47.346 -12.781 -5.823  1.00 11.76 ?  91  HIS   B C    1 
ATOM   5588 O O    . HIS   B 1 91  ? 47.122 -13.735 -6.579  1.00 11.82 ?  91  HIS   B O    1 
ATOM   5589 C CB   . HIS   B 1 91  ? 45.909 -10.862 -6.232  1.00 13.99 ?  91  HIS   B CB   1 
ATOM   5590 C CG   . HIS   B 1 91  ? 45.711 -9.447  -6.649  1.00 17.42 ?  91  HIS   B CG   1 
ATOM   5591 N ND1  . HIS   B 1 91  ? 46.338 -8.386  -6.031  1.00 19.83 ?  91  HIS   B ND1  1 
ATOM   5592 C CD2  . HIS   B 1 91  ? 44.917 -8.911  -7.602  1.00 19.62 ?  91  HIS   B CD2  1 
ATOM   5593 C CE1  . HIS   B 1 91  ? 45.961 -7.256  -6.605  1.00 20.93 ?  91  HIS   B CE1  1 
ATOM   5594 N NE2  . HIS   B 1 91  ? 45.091 -7.548  -7.556  1.00 21.12 ?  91  HIS   B NE2  1 
ATOM   5595 H H    . HIS   B 1 91  ? 47.407 -11.890 -8.225  1.00 14.61 ?  91  HIS   B H    1 
ATOM   5596 H HA   . HIS   B 1 91  ? 47.933 -10.799 -5.787  1.00 14.88 ?  91  HIS   B HA   1 
ATOM   5597 H HB2  . HIS   B 1 91  ? 45.346 -11.412 -6.792  1.00 16.81 ?  91  HIS   B HB2  1 
ATOM   5598 H HB3  . HIS   B 1 91  ? 45.627 -10.935 -5.305  1.00 16.81 ?  91  HIS   B HB3  1 
ATOM   5599 H HD2  . HIS   B 1 91  ? 44.363 -9.366  -8.189  1.00 23.56 ?  91  HIS   B HD2  1 
ATOM   5600 H HE1  . HIS   B 1 91  ? 46.247 -6.398  -6.369  1.00 25.13 ?  91  HIS   B HE1  1 
ATOM   5601 H HE2  . HIS   B 1 91  ? 44.708 -6.967  -8.071  1.00 25.36 ?  91  HIS   B HE2  1 
ATOM   5602 N N    . CYS   B 1 92  ? 47.531 -12.913 -4.514  1.00 11.32 ?  92  CYS   B N    1 
ATOM   5603 C CA   . CYS   B 1 92  ? 47.221 -14.147 -3.804  1.00 10.79 ?  92  CYS   B CA   1 
ATOM   5604 C C    . CYS   B 1 92  ? 46.004 -13.905 -2.924  1.00 10.81 ?  92  CYS   B C    1 
ATOM   5605 O O    . CYS   B 1 92  ? 46.005 -12.992 -2.086  1.00 11.75 ?  92  CYS   B O    1 
ATOM   5606 C CB   . CYS   B 1 92  ? 48.398 -14.608 -2.949  1.00 11.47 ?  92  CYS   B CB   1 
ATOM   5607 S SG   . CYS   B 1 92  ? 48.034 -16.138 -2.042  1.00 11.58 ?  92  CYS   B SG   1 
ATOM   5608 H H    . CYS   B 1 92  ? 47.857 -12.289 -4.011  1.00 13.60 ?  92  CYS   B H    1 
ATOM   5609 H HA   . CYS   B 1 92  ? 47.016 -14.839 -4.451  1.00 12.97 ?  92  CYS   B HA   1 
ATOM   5610 H HB2  . CYS   B 1 92  ? 49.159 -14.769 -3.520  1.00 13.78 ?  92  CYS   B HB2  1 
ATOM   5611 H HB3  . CYS   B 1 92  ? 48.599 -13.918 -2.300  1.00 13.78 ?  92  CYS   B HB3  1 
ATOM   5612 H HG   . CYS   B 1 92  ? 49.000 -16.450 -1.413  1.00 13.92 ?  92  CYS   B HG   1 
ATOM   5613 N N    . LEU   B 1 93  ? 44.959 -14.701 -3.138  1.00 10.68 ?  93  LEU   B N    1 
ATOM   5614 C CA   . LEU   B 1 93  ? 43.785 -14.709 -2.276  1.00 10.76 ?  93  LEU   B CA   1 
ATOM   5615 C C    . LEU   B 1 93  ? 44.010 -15.769 -1.204  1.00 10.53 ?  93  LEU   B C    1 
ATOM   5616 O O    . LEU   B 1 93  ? 43.964 -16.973 -1.489  1.00 11.10 ?  93  LEU   B O    1 
ATOM   5617 C CB   . LEU   B 1 93  ? 42.528 -15.014 -3.087  1.00 11.89 ?  93  LEU   B CB   1 
ATOM   5618 C CG   . LEU   B 1 93  ? 41.231 -15.023 -2.277  1.00 12.32 ?  93  LEU   B CG   1 
ATOM   5619 C CD1  . LEU   B 1 93  ? 40.877 -13.631 -1.815  1.00 12.93 ?  93  LEU   B CD1  1 
ATOM   5620 C CD2  . LEU   B 1 93  ? 40.094 -15.623 -3.087  1.00 12.37 ?  93  LEU   B CD2  1 
ATOM   5621 H H    . LEU   B 1 93  ? 44.909 -15.264 -3.794  1.00 12.84 ?  93  LEU   B H    1 
ATOM   5622 H HA   . LEU   B 1 93  ? 43.684 -13.843 -1.853  1.00 12.93 ?  93  LEU   B HA   1 
ATOM   5623 H HB2  . LEU   B 1 93  ? 42.434 -14.338 -3.781  1.00 14.30 ?  93  LEU   B HB2  1 
ATOM   5624 H HB3  . LEU   B 1 93  ? 42.626 -15.886 -3.497  1.00 14.30 ?  93  LEU   B HB3  1 
ATOM   5625 H HG   . LEU   B 1 93  ? 41.357 -15.572 -1.490  1.00 14.81 ?  93  LEU   B HG   1 
ATOM   5626 H HD11 . LEU   B 1 93  ? 40.018 -13.652 -1.373  1.00 15.54 ?  93  LEU   B HD11 1 
ATOM   5627 H HD12 . LEU   B 1 93  ? 41.561 -13.313 -1.206  1.00 15.54 ?  93  LEU   B HD12 1 
ATOM   5628 H HD13 . LEU   B 1 93  ? 40.833 -13.042 -2.593  1.00 15.54 ?  93  LEU   B HD13 1 
ATOM   5629 H HD21 . LEU   B 1 93  ? 39.288 -15.616 -2.546  1.00 14.87 ?  93  LEU   B HD21 1 
ATOM   5630 H HD22 . LEU   B 1 93  ? 39.962 -15.097 -3.888  1.00 14.87 ?  93  LEU   B HD22 1 
ATOM   5631 H HD23 . LEU   B 1 93  ? 40.324 -16.537 -3.323  1.00 14.87 ?  93  LEU   B HD23 1 
ATOM   5632 N N    . HIS   B 1 94  ? 44.276 -15.337 0.017   1.00 10.34 ?  94  HIS   B N    1 
ATOM   5633 C CA   . HIS   B 1 94  ? 44.499 -16.243 1.133   1.00 10.90 ?  94  HIS   B CA   1 
ATOM   5634 C C    . HIS   B 1 94  ? 43.135 -16.591 1.714   1.00 11.88 ?  94  HIS   B C    1 
ATOM   5635 O O    . HIS   B 1 94  ? 42.471 -15.713 2.267   1.00 13.01 ?  94  HIS   B O    1 
ATOM   5636 C CB   . HIS   B 1 94  ? 45.370 -15.567 2.190   1.00 11.74 ?  94  HIS   B CB   1 
ATOM   5637 C CG   . HIS   B 1 94  ? 46.754 -15.265 1.723   1.00 11.53 ?  94  HIS   B CG   1 
ATOM   5638 N ND1  . HIS   B 1 94  ? 47.776 -16.183 1.815   1.00 11.68 ?  94  HIS   B ND1  1 
ATOM   5639 C CD2  . HIS   B 1 94  ? 47.269 -14.165 1.123   1.00 11.63 ?  94  HIS   B CD2  1 
ATOM   5640 C CE1  . HIS   B 1 94  ? 48.873 -15.635 1.320   1.00 11.75 ?  94  HIS   B CE1  1 
ATOM   5641 N NE2  . HIS   B 1 94  ? 48.594 -14.417 0.887   1.00 11.81 ?  94  HIS   B NE2  1 
ATOM   5642 H H    . HIS   B 1 94  ? 44.348 -14.502 0.222   1.00 12.44 ?  94  HIS   B H    1 
ATOM   5643 H HA   . HIS   B 1 94  ? 44.933 -17.054 0.822   1.00 13.10 ?  94  HIS   B HA   1 
ATOM   5644 H HB2  . HIS   B 1 94  ? 44.956 -14.736 2.447   1.00 14.11 ?  94  HIS   B HB2  1 
ATOM   5645 H HB3  . HIS   B 1 94  ? 45.438 -16.161 2.953   1.00 14.11 ?  94  HIS   B HB3  1 
ATOM   5646 H HD2  . HIS   B 1 94  ? 46.812 -13.386 0.918   1.00 13.98 ?  94  HIS   B HD2  1 
ATOM   5647 H HE1  . HIS   B 1 94  ? 49.702 -16.059 1.267   1.00 14.12 ?  94  HIS   B HE1  1 
ATOM   5648 H HE2  . HIS   B 1 94  ? 49.151 -13.884 0.520   1.00 14.19 ?  94  HIS   B HE2  1 
ATOM   5649 N N    . VAL   B 1 95  ? 42.702 -17.848 1.569   1.00 11.26 ?  95  VAL   B N    1 
ATOM   5650 C CA   . VAL   B 1 95  ? 41.370 -18.275 2.001   1.00 11.69 ?  95  VAL   B CA   1 
ATOM   5651 C C    . VAL   B 1 95  ? 41.527 -19.301 3.106   1.00 11.72 ?  95  VAL   B C    1 
ATOM   5652 O O    . VAL   B 1 95  ? 42.306 -20.251 2.960   1.00 12.30 ?  95  VAL   B O    1 
ATOM   5653 C CB   . VAL   B 1 95  ? 40.550 -18.885 0.847   1.00 11.70 ?  95  VAL   B CB   1 
ATOM   5654 C CG1  . VAL   B 1 95  ? 39.169 -19.331 1.330   1.00 13.37 ?  95  VAL   B CG1  1 
ATOM   5655 C CG2  . VAL   B 1 95  ? 40.433 -17.904 -0.299  1.00 12.01 ?  95  VAL   B CG2  1 
ATOM   5656 H H    . VAL   B 1 95  ? 43.167 -18.480 1.217   1.00 13.54 ?  95  VAL   B H    1 
ATOM   5657 H HA   . VAL   B 1 95  ? 40.881 -17.513 2.355   1.00 14.04 ?  95  VAL   B HA   1 
ATOM   5658 H HB   . VAL   B 1 95  ? 41.010 -19.664 0.515   1.00 14.07 ?  95  VAL   B HB   1 
ATOM   5659 H HG11 . VAL   B 1 95  ? 38.614 -19.527 0.555   1.00 16.07 ?  95  VAL   B HG11 1 
ATOM   5660 H HG12 . VAL   B 1 95  ? 39.264 -20.124 1.875   1.00 16.07 ?  95  VAL   B HG12 1 
ATOM   5661 H HG13 . VAL   B 1 95  ? 38.765 -18.614 1.845   1.00 16.07 ?  95  VAL   B HG13 1 
ATOM   5662 H HG21 . VAL   B 1 95  ? 39.857 -18.281 -0.981  1.00 14.43 ?  95  VAL   B HG21 1 
ATOM   5663 H HG22 . VAL   B 1 95  ? 40.045 -17.074 0.035   1.00 14.43 ?  95  VAL   B HG22 1 
ATOM   5664 H HG23 . VAL   B 1 95  ? 41.313 -17.734 -0.659  1.00 14.43 ?  95  VAL   B HG23 1 
ATOM   5665 N N    . VAL   B 1 96  ? 40.789 -19.123 4.200   1.00 11.99 ?  96  VAL   B N    1 
ATOM   5666 C CA   . VAL   B 1 96  ? 40.872 -20.027 5.350   1.00 12.87 ?  96  VAL   B CA   1 
ATOM   5667 C C    . VAL   B 1 96  ? 39.685 -20.988 5.305   1.00 13.68 ?  96  VAL   B C    1 
ATOM   5668 O O    . VAL   B 1 96  ? 38.566 -20.634 5.682   1.00 13.97 ?  96  VAL   B O    1 
ATOM   5669 C CB   . VAL   B 1 96  ? 40.925 -19.274 6.685   1.00 13.75 ?  96  VAL   B CB   1 
ATOM   5670 C CG1  . VAL   B 1 96  ? 41.088 -20.262 7.839   1.00 13.80 ?  96  VAL   B CG1  1 
ATOM   5671 C CG2  . VAL   B 1 96  ? 42.050 -18.245 6.691   1.00 14.19 ?  96  VAL   B CG2  1 
ATOM   5672 H H    . VAL   B 1 96  ? 40.221 -18.484 4.308   1.00 14.41 ?  96  VAL   B H    1 
ATOM   5673 H HA   . VAL   B 1 96  ? 41.683 -20.555 5.279   1.00 15.47 ?  96  VAL   B HA   1 
ATOM   5674 H HB   . VAL   B 1 96  ? 40.088 -18.803 6.814   1.00 16.52 ?  96  VAL   B HB   1 
ATOM   5675 H HG11 . VAL   B 1 96  ? 41.278 -19.771 8.654   1.00 16.58 ?  96  VAL   B HG11 1 
ATOM   5676 H HG12 . VAL   B 1 96  ? 40.268 -20.770 7.946   1.00 16.58 ?  96  VAL   B HG12 1 
ATOM   5677 H HG13 . VAL   B 1 96  ? 41.825 -20.865 7.641   1.00 16.58 ?  96  VAL   B HG13 1 
ATOM   5678 H HG21 . VAL   B 1 96  ? 42.093 -17.827 7.566   1.00 17.05 ?  96  VAL   B HG21 1 
ATOM   5679 H HG22 . VAL   B 1 96  ? 42.888 -18.688 6.493   1.00 17.05 ?  96  VAL   B HG22 1 
ATOM   5680 H HG23 . VAL   B 1 96  ? 41.864 -17.571 6.015   1.00 17.05 ?  96  VAL   B HG23 1 
ATOM   5681 N N    . GLY   B 1 97  ? 39.923 -22.225 4.872   1.00 13.27 ?  97  GLY   B N    1 
ATOM   5682 C CA   . GLY   B 1 97  ? 38.948 -23.277 5.030   1.00 14.44 ?  97  GLY   B CA   1 
ATOM   5683 C C    . GLY   B 1 97  ? 39.089 -23.882 6.408   1.00 15.79 ?  97  GLY   B C    1 
ATOM   5684 O O    . GLY   B 1 97  ? 40.131 -23.744 7.064   1.00 15.97 ?  97  GLY   B O    1 
ATOM   5685 H H    . GLY   B 1 97  ? 40.649 -22.463 4.469   1.00 15.95 ?  97  GLY   B H    1 
ATOM   5686 H HA2  . GLY   B 1 97  ? 38.056 -22.909 4.922   1.00 17.35 ?  97  GLY   B HA2  1 
ATOM   5687 H HA3  . GLY   B 1 97  ? 39.090 -23.961 4.359   1.00 17.35 ?  97  GLY   B HA3  1 
ATOM   5688 N N    . PRO   B 1 98  ? 38.043 -24.556 6.881   1.00 16.24 ?  98  PRO   B N    1 
ATOM   5689 C CA   . PRO   B 1 98  ? 38.142 -25.245 8.171   1.00 17.71 ?  98  PRO   B CA   1 
ATOM   5690 C C    . PRO   B 1 98  ? 39.171 -26.367 8.124   1.00 17.52 ?  98  PRO   B C    1 
ATOM   5691 O O    . PRO   B 1 98  ? 39.271 -27.106 7.146   1.00 17.91 ?  98  PRO   B O    1 
ATOM   5692 C CB   . PRO   B 1 98  ? 36.723 -25.783 8.391   1.00 18.43 ?  98  PRO   B CB   1 
ATOM   5693 C CG   . PRO   B 1 98  ? 36.144 -25.904 7.035   1.00 18.28 ?  98  PRO   B CG   1 
ATOM   5694 C CD   . PRO   B 1 98  ? 36.723 -24.749 6.253   1.00 17.11 ?  98  PRO   B CD   1 
ATOM   5695 H HA   . PRO   B 1 98  ? 38.369 -24.620 8.872   1.00 21.27 ?  98  PRO   B HA   1 
ATOM   5696 H HB2  . PRO   B 1 98  ? 36.767 -26.651 8.825   1.00 22.14 ?  98  PRO   B HB2  1 
ATOM   5697 H HB3  . PRO   B 1 98  ? 36.215 -25.156 8.925   1.00 22.14 ?  98  PRO   B HB3  1 
ATOM   5698 H HG2  . PRO   B 1 98  ? 36.410 -26.754 6.642   1.00 21.96 ?  98  PRO   B HG2  1 
ATOM   5699 H HG3  . PRO   B 1 98  ? 35.180 -25.839 7.084   1.00 21.96 ?  98  PRO   B HG3  1 
ATOM   5700 H HD2  . PRO   B 1 98  ? 36.818 -24.992 5.314   1.00 20.56 ?  98  PRO   B HD2  1 
ATOM   5701 H HD3  . PRO   B 1 98  ? 36.177 -23.958 6.362   1.00 20.56 ?  98  PRO   B HD3  1 
ATOM   5702 N N    . ASN   B 1 99  ? 39.938 -26.488 9.204   1.00 19.15 ?  99  ASN   B N    1 
ATOM   5703 C CA   . ASN   B 1 99  ? 40.919 -27.561 9.367   1.00 20.44 ?  99  ASN   B CA   1 
ATOM   5704 C C    . ASN   B 1 99  ? 40.310 -28.630 10.271  1.00 22.92 ?  99  ASN   B C    1 
ATOM   5705 O O    . ASN   B 1 99  ? 40.280 -28.474 11.494  1.00 24.11 ?  99  ASN   B O    1 
ATOM   5706 C CB   . ASN   B 1 99  ? 42.202 -26.999 9.965   1.00 20.45 ?  99  ASN   B CB   1 
ATOM   5707 C CG   . ASN   B 1 99  ? 43.330 -28.009 9.992   1.00 21.27 ?  99  ASN   B CG   1 
ATOM   5708 O OD1  . ASN   B 1 99  ? 43.112 -29.189 10.220  1.00 21.85 ?  99  ASN   B OD1  1 
ATOM   5709 N ND2  . ASN   B 1 99  ? 44.540 -27.544 9.752   1.00 21.27 ?  99  ASN   B ND2  1 
ATOM   5710 H H    . ASN   B 1 99  ? 39.904 -25.946 9.871   1.00 23.00 ?  99  ASN   B H    1 
ATOM   5711 H HA   . ASN   B 1 99  ? 41.111 -27.964 8.509   1.00 24.55 ?  99  ASN   B HA   1 
ATOM   5712 H HB2  . ASN   B 1 99  ? 42.478 -26.241 9.439   1.00 24.56 ?  99  ASN   B HB2  1 
ATOM   5713 H HB3  . ASN   B 1 99  ? 42.019 -26.726 10.881  1.00 24.56 ?  99  ASN   B HB3  1 
ATOM   5714 H HD21 . ASN   B 1 99  ? 45.210 -28.075 9.746   1.00 25.55 ?  99  ASN   B HD21 1 
ATOM   5715 H HD22 . ASN   B 1 99  ? 44.646 -26.706 9.591   1.00 25.55 ?  99  ASN   B HD22 1 
ATOM   5716 N N    . VAL   B 1 100 ? 39.816 -29.713 9.662   1.00 25.46 ?  100 VAL   B N    1 
ATOM   5717 C CA   . VAL   B 1 100 ? 39.198 -30.799 10.426  1.00 28.76 ?  100 VAL   B CA   1 
ATOM   5718 C C    . VAL   B 1 100 ? 40.213 -31.483 11.332  1.00 29.76 ?  100 VAL   B C    1 
ATOM   5719 O O    . VAL   B 1 100 ? 39.855 -32.000 12.397  1.00 30.56 ?  100 VAL   B O    1 
ATOM   5720 C CB   . VAL   B 1 100 ? 38.507 -31.794 9.471   1.00 30.96 ?  100 VAL   B CB   1 
ATOM   5721 C CG1  . VAL   B 1 100 ? 38.004 -33.011 10.231  1.00 32.00 ?  100 VAL   B CG1  1 
ATOM   5722 C CG2  . VAL   B 1 100 ? 37.356 -31.110 8.749   1.00 31.17 ?  100 VAL   B CG2  1 
ATOM   5723 H H    . VAL   B 1 100 ? 39.810 -29.834 8.808   1.00 30.58 ?  100 VAL   B H    1 
ATOM   5724 H HA   . VAL   B 1 100 ? 38.501 -30.422 10.987  1.00 34.54 ?  100 VAL   B HA   1 
ATOM   5725 H HB   . VAL   B 1 100 ? 39.145 -32.099 8.807   1.00 37.17 ?  100 VAL   B HB   1 
ATOM   5726 H HG11 . VAL   B 1 100 ? 37.396 -33.510 9.660   1.00 38.42 ?  100 VAL   B HG11 1 
ATOM   5727 H HG12 . VAL   B 1 100 ? 38.758 -33.571 10.475  1.00 38.42 ?  100 VAL   B HG12 1 
ATOM   5728 H HG13 . VAL   B 1 100 ? 37.537 -32.716 11.028  1.00 38.42 ?  100 VAL   B HG13 1 
ATOM   5729 H HG21 . VAL   B 1 100 ? 36.911 -31.757 8.177   1.00 37.43 ?  100 VAL   B HG21 1 
ATOM   5730 H HG22 . VAL   B 1 100 ? 36.730 -30.767 9.407   1.00 37.43 ?  100 VAL   B HG22 1 
ATOM   5731 H HG23 . VAL   B 1 100 ? 37.707 -30.383 8.214   1.00 37.43 ?  100 VAL   B HG23 1 
ATOM   5732 N N    . ASN   B 1 101 ? 41.486 -31.517 10.927  1.00 30.18 ?  101 ASN   B N    1 
ATOM   5733 C CA   . ASN   B 1 101 ? 42.525 -32.067 11.792  1.00 31.28 ?  101 ASN   B CA   1 
ATOM   5734 C C    . ASN   B 1 101 ? 42.738 -31.231 13.046  1.00 33.66 ?  101 ASN   B C    1 
ATOM   5735 O O    . ASN   B 1 101 ? 43.389 -31.705 13.986  1.00 34.85 ?  101 ASN   B O    1 
ATOM   5736 C CB   . ASN   B 1 101 ? 43.841 -32.212 11.027  1.00 30.26 ?  101 ASN   B CB   1 
ATOM   5737 C CG   . ASN   B 1 101 ? 43.825 -33.380 10.059  1.00 29.34 ?  101 ASN   B CG   1 
ATOM   5738 O OD1  . ASN   B 1 101 ? 43.151 -34.375 10.294  1.00 30.35 ?  101 ASN   B OD1  1 
ATOM   5739 N ND2  . ASN   B 1 101 ? 44.565 -33.259 8.966   1.00 28.55 ?  101 ASN   B ND2  1 
ATOM   5740 H H    . ASN   B 1 101 ? 41.763 -31.239 10.161  1.00 36.23 ?  101 ASN   B H    1 
ATOM   5741 H HA   . ASN   B 1 101 ? 42.250 -32.952 12.072  1.00 37.56 ?  101 ASN   B HA   1 
ATOM   5742 H HB2  . ASN   B 1 101 ? 44.007 -31.406 10.517  1.00 36.34 ?  101 ASN   B HB2  1 
ATOM   5743 H HB3  . ASN   B 1 101 ? 44.561 -32.357 11.662  1.00 36.34 ?  101 ASN   B HB3  1 
ATOM   5744 H HD21 . ASN   B 1 101 ? 44.584 -33.897 8.390   1.00 34.28 ?  101 ASN   B HD21 1 
ATOM   5745 H HD22 . ASN   B 1 101 ? 45.018 -32.542 8.831   1.00 34.28 ?  101 ASN   B HD22 1 
ATOM   5746 N N    . LYS   B 1 102 ? 42.216 -30.005 13.073  1.00 36.42 ?  102 LYS   B N    1 
ATOM   5747 C CA   . LYS   B 1 102 ? 42.168 -29.182 14.273  1.00 39.38 ?  102 LYS   B CA   1 
ATOM   5748 C C    . LYS   B 1 102 ? 40.773 -29.131 14.883  1.00 38.92 ?  102 LYS   B C    1 
ATOM   5749 O O    . LYS   B 1 102 ? 40.532 -28.326 15.787  1.00 39.39 ?  102 LYS   B O    1 
ATOM   5750 C CB   . LYS   B 1 102 ? 42.637 -27.761 13.961  1.00 42.79 ?  102 LYS   B CB   1 
ATOM   5751 C CG   . LYS   B 1 102 ? 44.108 -27.633 13.606  1.00 46.31 ?  102 LYS   B CG   1 
ATOM   5752 C CD   . LYS   B 1 102 ? 44.408 -26.224 13.118  1.00 48.91 ?  102 LYS   B CD   1 
ATOM   5753 C CE   . LYS   B 1 102 ? 45.895 -25.992 12.916  1.00 51.27 ?  102 LYS   B CE   1 
ATOM   5754 N NZ   . LYS   B 1 102 ? 46.164 -24.605 12.433  1.00 52.48 ?  102 LYS   B NZ   1 
ATOM   5755 H H    . LYS   B 1 102 ? 41.872 -29.620 12.384  1.00 43.73 ?  102 LYS   B H    1 
ATOM   5756 H HA   . LYS   B 1 102 ? 42.770 -29.555 14.933  1.00 47.28 ?  102 LYS   B HA   1 
ATOM   5757 H HB2  . LYS   B 1 102 ? 42.124 -27.423 13.211  1.00 51.37 ?  102 LYS   B HB2  1 
ATOM   5758 H HB3  . LYS   B 1 102 ? 42.476 -27.206 14.741  1.00 51.37 ?  102 LYS   B HB3  1 
ATOM   5759 H HG2  . LYS   B 1 102 ? 44.650 -27.808 14.392  1.00 55.59 ?  102 LYS   B HG2  1 
ATOM   5760 H HG3  . LYS   B 1 102 ? 44.327 -28.258 12.897  1.00 55.59 ?  102 LYS   B HG3  1 
ATOM   5761 H HD2  . LYS   B 1 102 ? 43.961 -26.079 12.269  1.00 58.72 ?  102 LYS   B HD2  1 
ATOM   5762 H HD3  . LYS   B 1 102 ? 44.089 -25.585 13.775  1.00 58.72 ?  102 LYS   B HD3  1 
ATOM   5763 H HE2  . LYS   B 1 102 ? 46.357 -26.116 13.760  1.00 61.54 ?  102 LYS   B HE2  1 
ATOM   5764 H HE3  . LYS   B 1 102 ? 46.230 -26.616 12.253  1.00 61.54 ?  102 LYS   B HE3  1 
ATOM   5765 H HZ1  . LYS   B 1 102 ? 47.038 -24.486 12.320  1.00 63.00 ?  102 LYS   B HZ1  1 
ATOM   5766 H HZ2  . LYS   B 1 102 ? 45.750 -24.468 11.657  1.00 63.00 ?  102 LYS   B HZ2  1 
ATOM   5767 H HZ3  . LYS   B 1 102 ? 45.865 -24.013 13.027  1.00 63.00 ?  102 LYS   B HZ3  1 
ATOM   5768 N N    . GLY   B 1 103 ? 39.846 -29.956 14.401  1.00 37.97 ?  103 GLY   B N    1 
ATOM   5769 C CA   . GLY   B 1 103 ? 38.515 -30.018 14.969  1.00 37.76 ?  103 GLY   B CA   1 
ATOM   5770 C C    . GLY   B 1 103 ? 37.572 -28.921 14.533  1.00 36.89 ?  103 GLY   B C    1 
ATOM   5771 O O    . GLY   B 1 103 ? 36.486 -28.799 15.109  1.00 37.32 ?  103 GLY   B O    1 
ATOM   5772 H H    . GLY   B 1 103 ? 39.966 -30.489 13.738  1.00 45.59 ?  103 GLY   B H    1 
ATOM   5773 H HA2  . GLY   B 1 103 ? 38.113 -30.869 14.736  1.00 45.33 ?  103 GLY   B HA2  1 
ATOM   5774 H HA3  . GLY   B 1 103 ? 38.583 -29.975 15.936  1.00 45.33 ?  103 GLY   B HA3  1 
ATOM   5775 N N    A GLU   B 1 104 ? 37.953 -28.112 13.548  0.56 35.85 ?  104 GLU   B N    1 
ATOM   5776 N N    B GLU   B 1 104 ? 37.939 -28.127 13.531  0.44 36.17 ?  104 GLU   B N    1 
ATOM   5777 C CA   A GLU   B 1 104 ? 37.106 -27.017 13.104  0.56 34.87 ?  104 GLU   B CA   1 
ATOM   5778 C CA   B GLU   B 1 104 ? 37.076 -27.049 13.076  0.44 35.43 ?  104 GLU   B CA   1 
ATOM   5779 C C    A GLU   B 1 104 ? 35.917 -27.545 12.302  0.56 34.70 ?  104 GLU   B C    1 
ATOM   5780 C C    B GLU   B 1 104 ? 35.906 -27.600 12.262  0.44 35.30 ?  104 GLU   B C    1 
ATOM   5781 O O    A GLU   B 1 104 ? 35.951 -28.636 11.724  0.56 34.89 ?  104 GLU   B O    1 
ATOM   5782 O O    B GLU   B 1 104 ? 35.960 -28.700 11.705  0.44 35.48 ?  104 GLU   B O    1 
ATOM   5783 C CB   A GLU   B 1 104 ? 37.926 -26.013 12.290  0.56 33.96 ?  104 GLU   B CB   1 
ATOM   5784 C CB   B GLU   B 1 104 ? 37.885 -26.032 12.271  0.44 34.71 ?  104 GLU   B CB   1 
ATOM   5785 C CG   A GLU   B 1 104 ? 39.038 -25.366 13.110  0.56 32.96 ?  104 GLU   B CG   1 
ATOM   5786 C CG   B GLU   B 1 104 ? 38.991 -25.388 13.097  0.44 33.93 ?  104 GLU   B CG   1 
ATOM   5787 C CD   A GLU   B 1 104 ? 39.954 -24.474 12.297  0.56 31.81 ?  104 GLU   B CD   1 
ATOM   5788 C CD   B GLU   B 1 104 ? 39.914 -24.502 12.285  0.44 33.04 ?  104 GLU   B CD   1 
ATOM   5789 O OE1  A GLU   B 1 104 ? 39.945 -24.561 11.052  0.56 30.39 ?  104 GLU   B OE1  1 
ATOM   5790 O OE1  B GLU   B 1 104 ? 39.869 -24.560 11.038  0.44 32.19 ?  104 GLU   B OE1  1 
ATOM   5791 O OE2  A GLU   B 1 104 ? 40.696 -23.684 12.917  0.56 31.84 -1 104 GLU   B OE2  1 
ATOM   5792 O OE2  B GLU   B 1 104 ? 40.693 -23.748 12.903  0.44 32.99 -1 104 GLU   B OE2  1 
ATOM   5793 H H    A GLU   B 1 104 ? 38.701 -28.171 13.128  0.56 43.05 ?  104 GLU   B H    1 
ATOM   5794 H H    B GLU   B 1 104 ? 38.684 -28.189 13.105  0.44 43.43 ?  104 GLU   B H    1 
ATOM   5795 H HA   A GLU   B 1 104 ? 36.761 -26.554 13.882  0.56 41.87 ?  104 GLU   B HA   1 
ATOM   5796 H HA   B GLU   B 1 104 ? 36.712 -26.593 13.849  0.44 42.54 ?  104 GLU   B HA   1 
ATOM   5797 H HB2  A GLU   B 1 104 ? 38.334 -26.469 11.538  0.56 40.77 ?  104 GLU   B HB2  1 
ATOM   5798 H HB2  B GLU   B 1 104 ? 38.294 -26.478 11.513  0.44 41.68 ?  104 GLU   B HB2  1 
ATOM   5799 H HB3  A GLU   B 1 104 ? 37.338 -25.308 11.972  0.56 40.77 ?  104 GLU   B HB3  1 
ATOM   5800 H HB3  B GLU   B 1 104 ? 37.291 -25.328 11.961  0.44 41.68 ?  104 GLU   B HB3  1 
ATOM   5801 H HG2  A GLU   B 1 104 ? 38.639 -24.827 13.813  0.56 39.58 ?  104 GLU   B HG2  1 
ATOM   5802 H HG2  B GLU   B 1 104 ? 38.588 -24.846 13.794  0.44 40.74 ?  104 GLU   B HG2  1 
ATOM   5803 H HG3  A GLU   B 1 104 ? 39.589 -26.060 13.501  0.56 39.58 ?  104 GLU   B HG3  1 
ATOM   5804 H HG3  B GLU   B 1 104 ? 39.533 -26.086 13.497  0.44 40.74 ?  104 GLU   B HG3  1 
ATOM   5805 N N    A ASP   B 1 105 ? 34.852 -26.746 12.274  0.56 34.55 ?  105 ASP   B N    1 
ATOM   5806 N N    B ASP   B 1 105 ? 34.834 -26.810 12.201  0.44 35.18 ?  105 ASP   B N    1 
ATOM   5807 C CA   A ASP   B 1 105 ? 33.578 -27.188 11.718  0.56 34.67 ?  105 ASP   B CA   1 
ATOM   5808 C CA   B ASP   B 1 105 ? 33.569 -27.265 11.637  0.44 35.11 ?  105 ASP   B CA   1 
ATOM   5809 C C    A ASP   B 1 105 ? 33.654 -27.244 10.198  0.56 32.35 ?  105 ASP   B C    1 
ATOM   5810 C C    B ASP   B 1 105 ? 33.654 -27.291 10.116  0.44 33.39 ?  105 ASP   B C    1 
ATOM   5811 O O    A ASP   B 1 105 ? 33.857 -26.218 9.540   0.56 31.29 ?  105 ASP   B O    1 
ATOM   5812 O O    B ASP   B 1 105 ? 33.855 -26.251 9.480   0.44 32.88 ?  105 ASP   B O    1 
ATOM   5813 C CB   A ASP   B 1 105 ? 32.467 -26.235 12.154  0.56 37.02 ?  105 ASP   B CB   1 
ATOM   5814 C CB   B ASP   B 1 105 ? 32.436 -26.346 12.091  0.44 36.77 ?  105 ASP   B CB   1 
ATOM   5815 C CG   A ASP   B 1 105 ? 31.095 -26.697 11.708  0.56 38.84 ?  105 ASP   B CG   1 
ATOM   5816 C CG   B ASP   B 1 105 ? 31.066 -26.892 11.733  0.44 37.96 ?  105 ASP   B CG   1 
ATOM   5817 O OD1  A ASP   B 1 105 ? 30.983 -27.831 11.197  0.56 38.98 ?  105 ASP   B OD1  1 
ATOM   5818 O OD1  B ASP   B 1 105 ? 30.999 -27.956 11.081  0.44 38.14 ?  105 ASP   B OD1  1 
ATOM   5819 O OD2  A ASP   B 1 105 ? 30.128 -25.921 11.863  0.56 39.96 -1 105 ASP   B OD2  1 
ATOM   5820 O OD2  B ASP   B 1 105 ? 30.054 -26.262 12.109  0.44 38.58 -1 105 ASP   B OD2  1 
ATOM   5821 H H    A ASP   B 1 105 ? 34.843 -25.941 12.569  0.56 41.48 ?  105 ASP   B H    1 
ATOM   5822 H H    B ASP   B 1 105 ? 34.817 -25.997 12.476  0.44 42.23 ?  105 ASP   B H    1 
ATOM   5823 H HA   A ASP   B 1 105 ? 33.367 -28.075 12.050  0.56 41.62 ?  105 ASP   B HA   1 
ATOM   5824 H HA   B ASP   B 1 105 ? 33.374 -28.162 11.950  0.44 42.15 ?  105 ASP   B HA   1 
ATOM   5825 H HB2  A ASP   B 1 105 ? 32.471 -26.162 13.123  0.56 44.45 ?  105 ASP   B HB2  1 
ATOM   5826 H HB2  B ASP   B 1 105 ? 32.474 -26.246 13.056  0.44 44.15 ?  105 ASP   B HB2  1 
ATOM   5827 H HB3  A ASP   B 1 105 ? 32.617 -25.365 11.756  0.56 44.45 ?  105 ASP   B HB3  1 
ATOM   5828 H HB3  B ASP   B 1 105 ? 32.538 -25.479 11.665  0.44 44.15 ?  105 ASP   B HB3  1 
ATOM   5829 N N    A ILE   B 1 106 ? 33.465 -28.443 9.641   0.56 31.55 ?  106 ILE   B N    1 
ATOM   5830 N N    B ILE   B 1 106 ? 33.486 -28.482 9.535   0.44 32.47 ?  106 ILE   B N    1 
ATOM   5831 C CA   A ILE   B 1 106 ? 33.464 -28.626 8.195   0.56 30.11 ?  106 ILE   B CA   1 
ATOM   5832 C CA   B ILE   B 1 106 ? 33.484 -28.633 8.085   0.44 31.35 ?  106 ILE   B CA   1 
ATOM   5833 C C    A ILE   B 1 106 ? 32.378 -27.797 7.521   0.56 28.73 ?  106 ILE   B C    1 
ATOM   5834 C C    B ILE   B 1 106 ? 32.379 -27.810 7.433   0.44 30.18 ?  106 ILE   B C    1 
ATOM   5835 O O    A ILE   B 1 106 ? 32.480 -27.497 6.326   0.56 28.27 ?  106 ILE   B O    1 
ATOM   5836 O O    B ILE   B 1 106 ? 32.452 -27.515 6.235   0.44 29.94 ?  106 ILE   B O    1 
ATOM   5837 C CB   A ILE   B 1 106 ? 33.342 -30.132 7.862   0.56 30.24 ?  106 ILE   B CB   1 
ATOM   5838 C CB   B ILE   B 1 106 ? 33.390 -30.133 7.719   0.44 31.51 ?  106 ILE   B CB   1 
ATOM   5839 C CG1  A ILE   B 1 106 ? 33.593 -30.390 6.375   0.56 30.43 ?  106 ILE   B CG1  1 
ATOM   5840 C CG1  B ILE   B 1 106 ? 33.682 -30.357 6.234   0.44 31.77 ?  106 ILE   B CG1  1 
ATOM   5841 C CG2  A ILE   B 1 106 ? 31.973 -30.664 8.267   0.56 30.77 ?  106 ILE   B CG2  1 
ATOM   5842 C CG2  B ILE   B 1 106 ? 32.018 -30.688 8.074   0.44 31.86 ?  106 ILE   B CG2  1 
ATOM   5843 C CD1  A ILE   B 1 106 ? 34.967 -29.978 5.914   0.56 30.29 ?  106 ILE   B CD1  1 
ATOM   5844 C CD1  B ILE   B 1 106 ? 35.042 -29.867 5.804   0.44 31.85 ?  106 ILE   B CD1  1 
ATOM   5845 H H    A ILE   B 1 106 ? 33.336 -29.167 10.084  0.56 37.88 ?  106 ILE   B H    1 
ATOM   5846 H H    B ILE   B 1 106 ? 33.380 -29.219 9.962   0.44 38.99 ?  106 ILE   B H    1 
ATOM   5847 H HA   A ILE   B 1 106 ? 34.312 -28.316 7.852   0.56 36.15 ?  106 ILE   B HA   1 
ATOM   5848 H HA   B ILE   B 1 106 ? 34.324 -28.297 7.748   0.44 37.64 ?  106 ILE   B HA   1 
ATOM   5849 H HB   A ILE   B 1 106 ? 34.013 -30.611 8.371   0.56 36.30 ?  106 ILE   B HB   1 
ATOM   5850 H HB   B ILE   B 1 106 ? 34.053 -30.615 8.235   0.44 37.83 ?  106 ILE   B HB   1 
ATOM   5851 H HG12 A ILE   B 1 106 ? 33.500 -31.342 6.203   0.56 36.54 ?  106 ILE   B HG12 1 
ATOM   5852 H HG12 B ILE   B 1 106 ? 33.641 -31.310 6.048   0.44 38.15 ?  106 ILE   B HG12 1 
ATOM   5853 H HG13 A ILE   B 1 106 ? 32.943 -29.899 5.852   0.56 36.54 ?  106 ILE   B HG13 1 
ATOM   5854 H HG13 B ILE   B 1 106 ? 33.017 -29.892 5.707   0.44 38.15 ?  106 ILE   B HG13 1 
ATOM   5855 H HG21 A ILE   B 1 106 ? 31.974 -31.631 8.187   0.56 36.94 ?  106 ILE   B HG21 1 
ATOM   5856 H HG21 B ILE   B 1 106 ? 32.041 -31.655 8.003   0.44 38.25 ?  106 ILE   B HG21 1 
ATOM   5857 H HG22 A ILE   B 1 106 ? 31.795 -30.409 9.186   0.56 36.94 ?  106 ILE   B HG22 1 
ATOM   5858 H HG22 B ILE   B 1 106 ? 31.800 -30.429 8.983   0.44 38.25 ?  106 ILE   B HG22 1 
ATOM   5859 H HG23 A ILE   B 1 106 ? 31.299 -30.286 7.682   0.56 36.94 ?  106 ILE   B HG23 1 
ATOM   5860 H HG23 B ILE   B 1 106 ? 31.360 -30.327 7.460   0.44 38.25 ?  106 ILE   B HG23 1 
ATOM   5861 H HD11 A ILE   B 1 106 ? 35.145 -30.381 5.051   0.56 36.37 ?  106 ILE   B HD11 1 
ATOM   5862 H HD11 B ILE   B 1 106 ? 35.268 -30.274 4.955   0.44 38.24 ?  106 ILE   B HD11 1 
ATOM   5863 H HD12 A ILE   B 1 106 ? 35.000 -29.011 5.839   0.56 36.37 ?  106 ILE   B HD12 1 
ATOM   5864 H HD12 B ILE   B 1 106 ? 35.014 -28.901 5.711   0.44 38.24 ?  106 ILE   B HD12 1 
ATOM   5865 H HD13 A ILE   B 1 106 ? 35.623 -30.282 6.562   0.56 36.37 ?  106 ILE   B HD13 1 
ATOM   5866 H HD13 B ILE   B 1 106 ? 35.695 -30.117 6.476   0.44 38.24 ?  106 ILE   B HD13 1 
ATOM   5867 N N    A GLN   B 1 107 ? 31.340 -27.400 8.263   0.56 28.52 ?  107 GLN   B N    1 
ATOM   5868 N N    B GLN   B 1 107 ? 31.354 -27.424 8.197   0.44 29.81 ?  107 GLN   B N    1 
ATOM   5869 C CA   A GLN   B 1 107 ? 30.261 -26.617 7.673   0.56 28.75 ?  107 GLN   B CA   1 
ATOM   5870 C CA   B GLN   B 1 107 ? 30.265 -26.626 7.644   0.44 29.54 ?  107 GLN   B CA   1 
ATOM   5871 C C    A GLN   B 1 107 ? 30.745 -25.271 7.152   0.56 26.49 ?  107 GLN   B C    1 
ATOM   5872 C C    B GLN   B 1 107 ? 30.734 -25.259 7.162   0.44 27.00 ?  107 GLN   B C    1 
ATOM   5873 O O    A GLN   B 1 107 ? 30.112 -24.706 6.255   0.56 26.52 ?  107 GLN   B O    1 
ATOM   5874 O O    B GLN   B 1 107 ? 30.075 -24.662 6.304   0.44 27.09 ?  107 GLN   B O    1 
ATOM   5875 C CB   A GLN   B 1 107 ? 29.142 -26.411 8.699   0.56 32.03 ?  107 GLN   B CB   1 
ATOM   5876 C CB   B GLN   B 1 107 ? 29.155 -26.473 8.688   0.44 32.22 ?  107 GLN   B CB   1 
ATOM   5877 C CG   A GLN   B 1 107 ? 27.817 -25.926 8.116   0.56 35.10 ?  107 GLN   B CG   1 
ATOM   5878 C CG   B GLN   B 1 107 ? 27.812 -26.014 8.131   0.44 34.78 ?  107 GLN   B CG   1 
ATOM   5879 C CD   A GLN   B 1 107 ? 27.746 -24.415 7.974   0.56 37.39 ?  107 GLN   B CD   1 
ATOM   5880 C CD   B GLN   B 1 107 ? 27.686 -24.502 8.066   0.44 36.72 ?  107 GLN   B CD   1 
ATOM   5881 O OE1  A GLN   B 1 107 ? 28.559 -23.686 8.546   0.56 38.18 ?  107 GLN   B OE1  1 
ATOM   5882 O OE1  B GLN   B 1 107 ? 28.462 -23.775 8.687   0.44 37.34 ?  107 GLN   B OE1  1 
ATOM   5883 N NE2  A GLN   B 1 107 ? 26.767 -23.937 7.211   0.56 38.24 ?  107 GLN   B NE2  1 
ATOM   5884 N NE2  B GLN   B 1 107 ? 26.700 -24.023 7.315   0.44 37.48 ?  107 GLN   B NE2  1 
ATOM   5885 H H    A GLN   B 1 107 ? 31.246 -27.558 9.100   0.56 34.25 ?  107 GLN   B H    1 
ATOM   5886 H H    B GLN   B 1 107 ? 31.266 -27.611 9.028   0.44 35.79 ?  107 GLN   B H    1 
ATOM   5887 H HA   A GLN   B 1 107 ? 29.889 -27.109 6.925   0.56 34.52 ?  107 GLN   B HA   1 
ATOM   5888 H HA   B GLN   B 1 107 ? 29.890 -27.094 6.883   0.44 35.47 ?  107 GLN   B HA   1 
ATOM   5889 H HB2  A GLN   B 1 107 ? 28.974 -27.255 9.140   0.56 38.46 ?  107 GLN   B HB2  1 
ATOM   5890 H HB2  B GLN   B 1 107 ? 29.013 -27.331 9.113   0.44 38.69 ?  107 GLN   B HB2  1 
ATOM   5891 H HB3  A GLN   B 1 107 ? 29.435 -25.755 9.350   0.56 38.46 ?  107 GLN   B HB3  1 
ATOM   5892 H HB3  B GLN   B 1 107 ? 29.438 -25.825 9.352   0.44 38.69 ?  107 GLN   B HB3  1 
ATOM   5893 H HG2  A GLN   B 1 107 ? 27.695 -26.311 7.235   0.56 42.14 ?  107 GLN   B HG2  1 
ATOM   5894 H HG2  B GLN   B 1 107 ? 27.705 -26.360 7.231   0.44 41.76 ?  107 GLN   B HG2  1 
ATOM   5895 H HG3  A GLN   B 1 107 ? 27.093 -26.208 8.701   0.56 42.14 ?  107 GLN   B HG3  1 
ATOM   5896 H HG3  B GLN   B 1 107 ? 27.100 -26.353 8.700   0.44 41.76 ?  107 GLN   B HG3  1 
ATOM   5897 H HE21 A GLN   B 1 107 ? 26.217 -24.477 6.826   0.56 45.91 ?  107 GLN   B HE21 1 
ATOM   5898 H HE21 B GLN   B 1 107 ? 26.177 -24.561 6.895   0.44 44.99 ?  107 GLN   B HE21 1 
ATOM   5899 H HE22 A GLN   B 1 107 ? 26.680 -23.088 7.102   0.56 45.91 ?  107 GLN   B HE22 1 
ATOM   5900 H HE22 B GLN   B 1 107 ? 26.585 -23.173 7.249   0.44 44.99 ?  107 GLN   B HE22 1 
ATOM   5901 N N    . LEU   B 1 108 ? 31.857 -24.753 7.681   1.00 24.59 ?  108 LEU   B N    1 
ATOM   5902 C CA   . LEU   B 1 108 ? 32.394 -23.458 7.257   1.00 21.18 ?  108 LEU   B CA   1 
ATOM   5903 C C    . LEU   B 1 108 ? 33.051 -23.498 5.886   1.00 18.34 ?  108 LEU   B C    1 
ATOM   5904 O O    . LEU   B 1 108 ? 33.485 -22.445 5.392   1.00 17.07 ?  108 LEU   B O    1 
ATOM   5905 C CB   . LEU   B 1 108 ? 33.381 -22.932 8.300   1.00 21.26 ?  108 LEU   B CB   1 
ATOM   5906 C CG   . LEU   B 1 108 ? 32.759 -22.402 9.592   1.00 22.91 ?  108 LEU   B CG   1 
ATOM   5907 C CD1  . LEU   B 1 108 ? 33.778 -22.405 10.712  1.00 23.21 ?  108 LEU   B CD1  1 
ATOM   5908 C CD2  . LEU   B 1 108 ? 32.221 -20.995 9.379   1.00 23.62 ?  108 LEU   B CD2  1 
ATOM   5909 H H    A LEU   B 1 108 ? 32.311 -25.131 8.303   0.56 29.52 ?  108 LEU   B H    1 
ATOM   5910 H H    B LEU   B 1 108 ? 32.320 -25.140 8.290   0.44 29.52 ?  108 LEU   B H    1 
ATOM   5911 H HA   . LEU   B 1 108 ? 31.664 -22.829 7.206   1.00 25.44 ?  108 LEU   B HA   1 
ATOM   5912 H HB2  . LEU   B 1 108 ? 33.982 -23.650 8.546   1.00 25.54 ?  108 LEU   B HB2  1 
ATOM   5913 H HB3  . LEU   B 1 108 ? 33.884 -22.205 7.906   1.00 25.54 ?  108 LEU   B HB3  1 
ATOM   5914 H HG   . LEU   B 1 108 ? 32.017 -22.972 9.856   1.00 27.51 ?  108 LEU   B HG   1 
ATOM   5915 H HD11 . LEU   B 1 108 ? 33.351 -22.107 11.532  1.00 27.88 ?  108 LEU   B HD11 1 
ATOM   5916 H HD12 . LEU   B 1 108 ? 34.119 -23.305 10.826  1.00 27.88 ?  108 LEU   B HD12 1 
ATOM   5917 H HD13 . LEU   B 1 108 ? 34.502 -21.802 10.480  1.00 27.88 ?  108 LEU   B HD13 1 
ATOM   5918 H HD21 . LEU   B 1 108 ? 31.829 -20.675 10.208  1.00 28.37 ?  108 LEU   B HD21 1 
ATOM   5919 H HD22 . LEU   B 1 108 ? 32.951 -20.415 9.115   1.00 28.37 ?  108 LEU   B HD22 1 
ATOM   5920 H HD23 . LEU   B 1 108 ? 31.546 -21.017 8.683   1.00 28.37 ?  108 LEU   B HD23 1 
ATOM   5921 N N    . LEU   B 1 109 ? 33.122 -24.672 5.261   1.00 16.98 ?  109 LEU   B N    1 
ATOM   5922 C CA   . LEU   B 1 109 ? 33.754 -24.788 3.952   1.00 16.02 ?  109 LEU   B CA   1 
ATOM   5923 C C    . LEU   B 1 109 ? 32.984 -24.021 2.884   1.00 15.40 ?  109 LEU   B C    1 
ATOM   5924 O O    . LEU   B 1 109 ? 33.596 -23.440 1.979   1.00 14.72 ?  109 LEU   B O    1 
ATOM   5925 C CB   . LEU   B 1 109 ? 33.878 -26.268 3.585   1.00 16.37 ?  109 LEU   B CB   1 
ATOM   5926 C CG   . LEU   B 1 109 ? 34.650 -26.633 2.320   1.00 16.07 ?  109 LEU   B CG   1 
ATOM   5927 C CD1  . LEU   B 1 109 ? 36.026 -25.980 2.313   1.00 16.19 ?  109 LEU   B CD1  1 
ATOM   5928 C CD2  . LEU   B 1 109 ? 34.778 -28.147 2.201   1.00 16.62 ?  109 LEU   B CD2  1 
ATOM   5929 H H    . LEU   B 1 109 ? 32.838 -25.415 5.574   1.00 20.40 ?  109 LEU   B H    1 
ATOM   5930 H HA   . LEU   B 1 109 ? 34.649 -24.415 3.991   1.00 19.25 ?  109 LEU   B HA   1 
ATOM   5931 H HB2  . LEU   B 1 109 ? 34.318 -26.723 4.319   1.00 19.67 ?  109 LEU   B HB2  1 
ATOM   5932 H HB3  . LEU   B 1 109 ? 32.984 -26.627 3.480   1.00 19.67 ?  109 LEU   B HB3  1 
ATOM   5933 H HG   . LEU   B 1 109 ? 34.159 -26.322 1.543   1.00 19.31 ?  109 LEU   B HG   1 
ATOM   5934 H HD11 . LEU   B 1 109 ? 36.546 -26.351 1.581   1.00 19.45 ?  109 LEU   B HD11 1 
ATOM   5935 H HD12 . LEU   B 1 109 ? 35.917 -25.027 2.193   1.00 19.45 ?  109 LEU   B HD12 1 
ATOM   5936 H HD13 . LEU   B 1 109 ? 36.464 -26.167 3.157   1.00 19.45 ?  109 LEU   B HD13 1 
ATOM   5937 H HD21 . LEU   B 1 109 ? 35.338 -28.359 1.435   1.00 19.97 ?  109 LEU   B HD21 1 
ATOM   5938 H HD22 . LEU   B 1 109 ? 35.182 -28.496 3.010   1.00 19.97 ?  109 LEU   B HD22 1 
ATOM   5939 H HD23 . LEU   B 1 109 ? 33.896 -28.535 2.079   1.00 19.97 ?  109 LEU   B HD23 1 
ATOM   5940 N N    . LYS   B 1 110 ? 31.651 -23.985 2.969   1.00 15.00 ?  110 LYS   B N    1 
ATOM   5941 C CA   . LYS   B 1 110 ? 30.895 -23.232 1.974   1.00 14.90 ?  110 LYS   B CA   1 
ATOM   5942 C C    . LYS   B 1 110 ? 31.230 -21.741 2.049   1.00 14.98 ?  110 LYS   B C    1 
ATOM   5943 O O    . LYS   B 1 110 ? 31.479 -21.093 1.024   1.00 14.78 ?  110 LYS   B O    1 
ATOM   5944 C CB   . LYS   B 1 110 ? 29.390 -23.479 2.127   1.00 15.56 ?  110 LYS   B CB   1 
ATOM   5945 C CG   . LYS   B 1 110 ? 28.579 -22.880 0.973   1.00 15.99 ?  110 LYS   B CG   1 
ATOM   5946 C CD   . LYS   B 1 110 ? 27.103 -23.264 1.028   1.00 16.49 ?  110 LYS   B CD   1 
ATOM   5947 C CE   . LYS   B 1 110 ? 26.356 -22.745 -0.204  1.00 17.53 ?  110 LYS   B CE   1 
ATOM   5948 N NZ   . LYS   B 1 110 ? 26.691 -23.482 -1.452  1.00 17.68 ?  110 LYS   B NZ   1 
ATOM   5949 H H    . LYS   B 1 110 ? 31.178 -24.375 3.570   1.00 18.02 ?  110 LYS   B H    1 
ATOM   5950 H HA   . LYS   B 1 110 ? 31.150 -23.540 1.091   1.00 17.90 ?  110 LYS   B HA   1 
ATOM   5951 H HB2  . LYS   B 1 110 ? 29.227 -24.435 2.145   1.00 18.69 ?  110 LYS   B HB2  1 
ATOM   5952 H HB3  . LYS   B 1 110 ? 29.084 -23.073 2.952   1.00 18.69 ?  110 LYS   B HB3  1 
ATOM   5953 H HG2  . LYS   B 1 110 ? 28.639 -21.915 1.011   1.00 19.21 ?  110 LYS   B HG2  1 
ATOM   5954 H HG3  . LYS   B 1 110 ? 28.939 -23.205 0.133   1.00 19.21 ?  110 LYS   B HG3  1 
ATOM   5955 H HD2  . LYS   B 1 110 ? 27.020 -24.230 1.052   1.00 19.81 ?  110 LYS   B HD2  1 
ATOM   5956 H HD3  . LYS   B 1 110 ? 26.698 -22.872 1.820   1.00 19.81 ?  110 LYS   B HD3  1 
ATOM   5957 H HE2  . LYS   B 1 110 ? 25.402 -22.827 -0.054  1.00 21.06 ?  110 LYS   B HE2  1 
ATOM   5958 H HE3  . LYS   B 1 110 ? 26.588 -21.810 -0.339  1.00 21.06 ?  110 LYS   B HE3  1 
ATOM   5959 H HZ1  . LYS   B 1 110 ? 26.235 -23.142 -2.136  1.00 21.24 ?  110 LYS   B HZ1  1 
ATOM   5960 H HZ2  . LYS   B 1 110 ? 27.562 -23.413 -1.621  1.00 21.24 ?  110 LYS   B HZ2  1 
ATOM   5961 H HZ3  . LYS   B 1 110 ? 26.481 -24.341 -1.360  1.00 21.24 ?  110 LYS   B HZ3  1 
ATOM   5962 N N    . SER   B 1 111 ? 31.263 -21.189 3.266   1.00 15.25 ?  111 SER   B N    1 
ATOM   5963 C CA   . SER   B 1 111 ? 31.649 -19.791 3.436   1.00 14.99 ?  111 SER   B CA   1 
ATOM   5964 C C    . SER   B 1 111 ? 33.026 -19.535 2.837   1.00 14.47 ?  111 SER   B C    1 
ATOM   5965 O O    . SER   B 1 111 ? 33.246 -18.508 2.175   1.00 14.86 ?  111 SER   B O    1 
ATOM   5966 C CB   . SER   B 1 111 ? 31.650 -19.434 4.920   1.00 16.44 ?  111 SER   B CB   1 
ATOM   5967 O OG   . SER   B 1 111 ? 30.352 -19.421 5.468   1.00 18.07 ?  111 SER   B OG   1 
ATOM   5968 H H    . SER   B 1 111 ? 31.079 -21.606 3.996   1.00 18.32 ?  111 SER   B H    1 
ATOM   5969 H HA   . SER   B 1 111 ? 31.008 -19.227 2.983   1.00 18.01 ?  111 SER   B HA   1 
ATOM   5970 H HB2  . SER   B 1 111 ? 32.177 -20.094 5.399   1.00 19.76 ?  111 SER   B HB2  1 
ATOM   5971 H HB3  . SER   B 1 111 ? 32.048 -18.558 5.026   1.00 19.76 ?  111 SER   B HB3  1 
ATOM   5972 H HG   . SER   B 1 111 ? 30.384 -19.211 6.285   1.00 21.71 ?  111 SER   B HG   1 
ATOM   5973 N N    . ALA   B 1 112 ? 33.967 -20.457 3.058   1.00 14.30 ?  112 ALA   B N    1 
ATOM   5974 C CA   . ALA   B 1 112 ? 35.311 -20.284 2.515   1.00 14.07 ?  112 ALA   B CA   1 
ATOM   5975 C C    . ALA   B 1 112 ? 35.280 -20.197 0.992   1.00 13.49 ?  112 ALA   B C    1 
ATOM   5976 O O    . ALA   B 1 112 ? 35.902 -19.310 0.390   1.00 13.60 ?  112 ALA   B O    1 
ATOM   5977 C CB   . ALA   B 1 112 ? 36.211 -21.424 2.998   1.00 14.39 ?  112 ALA   B CB   1 
ATOM   5978 H H    . ALA   B 1 112 ? 33.851 -21.181 3.515   1.00 17.18 ?  112 ALA   B H    1 
ATOM   5979 H HA   . ALA   B 1 112 ? 35.674 -19.453 2.851   1.00 16.91 ?  112 ALA   B HA   1 
ATOM   5980 H HB1  . ALA   B 1 112 ? 37.102 -21.289 2.634   1.00 17.29 ?  112 ALA   B HB1  1 
ATOM   5981 H HB2  . ALA   B 1 112 ? 36.247 -21.406 3.968   1.00 17.29 ?  112 ALA   B HB2  1 
ATOM   5982 H HB3  . ALA   B 1 112 ? 35.850 -22.266 2.693   1.00 17.29 ?  112 ALA   B HB3  1 
ATOM   5983 N N    . TYR   B 1 113 ? 34.548 -21.107 0.345   1.00 13.62 ?  113 TYR   B N    1 
ATOM   5984 C CA   . TYR   B 1 113 ? 34.467 -21.068 -1.109  1.00 13.56 ?  113 TYR   B CA   1 
ATOM   5985 C C    . TYR   B 1 113 ? 33.762 -19.816 -1.625  1.00 13.27 ?  113 TYR   B C    1 
ATOM   5986 O O    . TYR   B 1 113 ? 34.028 -19.396 -2.755  1.00 12.66 ?  113 TYR   B O    1 
ATOM   5987 C CB   . TYR   B 1 113 ? 33.788 -22.329 -1.651  1.00 13.44 ?  113 TYR   B CB   1 
ATOM   5988 C CG   . TYR   B 1 113 ? 34.749 -23.478 -1.894  1.00 13.88 ?  113 TYR   B CG   1 
ATOM   5989 C CD1  . TYR   B 1 113 ? 35.751 -23.386 -2.850  1.00 14.66 ?  113 TYR   B CD1  1 
ATOM   5990 C CD2  . TYR   B 1 113 ? 34.643 -24.654 -1.175  1.00 14.49 ?  113 TYR   B CD2  1 
ATOM   5991 C CE1  . TYR   B 1 113 ? 36.631 -24.416 -3.079  1.00 14.12 ?  113 TYR   B CE1  1 
ATOM   5992 C CE2  . TYR   B 1 113 ? 35.516 -25.715 -1.400  1.00 14.59 ?  113 TYR   B CE2  1 
ATOM   5993 C CZ   . TYR   B 1 113 ? 36.508 -25.589 -2.357  1.00 14.00 ?  113 TYR   B CZ   1 
ATOM   5994 O OH   . TYR   B 1 113 ? 37.394 -26.610 -2.621  1.00 15.21 ?  113 TYR   B OH   1 
ATOM   5995 H H    . TYR   B 1 113 ? 34.089 -21.742 0.718   1.00 16.36 ?  113 TYR   B H    1 
ATOM   5996 H HA   . TYR   B 1 113 ? 35.370 -21.052 -1.453  1.00 16.30 ?  113 TYR   B HA   1 
ATOM   5997 H HB2  . TYR   B 1 113 ? 33.124 -22.630 -1.007  1.00 16.15 ?  113 TYR   B HB2  1 
ATOM   5998 H HB3  . TYR   B 1 113 ? 33.358 -22.116 -2.491  1.00 16.15 ?  113 TYR   B HB3  1 
ATOM   5999 H HD1  . TYR   B 1 113 ? 35.836 -22.593 -3.335  1.00 17.61 ?  113 TYR   B HD1  1 
ATOM   6000 H HD2  . TYR   B 1 113 ? 33.973 -24.741 -0.537  1.00 17.42 ?  113 TYR   B HD2  1 
ATOM   6001 H HE1  . TYR   B 1 113 ? 37.294 -24.327 -3.726  1.00 16.97 ?  113 TYR   B HE1  1 
ATOM   6002 H HE2  . TYR   B 1 113 ? 35.430 -26.505 -0.914  1.00 17.53 ?  113 TYR   B HE2  1 
ATOM   6003 H HH   . TYR   B 1 113 ? 37.218 -27.274 -2.129  1.00 18.27 ?  113 TYR   B HH   1 
ATOM   6004 N N    . GLU   B 1 114 ? 32.832 -19.236 -0.852  1.00 13.24 ?  114 GLU   B N    1 
ATOM   6005 C CA   . GLU   B 1 114 ? 32.155 -18.023 -1.311  1.00 12.98 ?  114 GLU   B CA   1 
ATOM   6006 C C    . GLU   B 1 114 ? 33.143 -16.902 -1.610  1.00 13.05 ?  114 GLU   B C    1 
ATOM   6007 O O    . GLU   B 1 114 ? 32.869 -16.042 -2.450  1.00 13.49 ?  114 GLU   B O    1 
ATOM   6008 C CB   . GLU   B 1 114 ? 31.102 -17.585 -0.293  1.00 14.11 ?  114 GLU   B CB   1 
ATOM   6009 C CG   . GLU   B 1 114 ? 29.871 -18.505 -0.370  1.00 14.38 ?  114 GLU   B CG   1 
ATOM   6010 C CD   . GLU   B 1 114 ? 28.850 -18.326 0.740   1.00 14.16 ?  114 GLU   B CD   1 
ATOM   6011 O OE1  . GLU   B 1 114 ? 29.143 -17.708 1.783   1.00 14.05 ?  114 GLU   B OE1  1 
ATOM   6012 O OE2  . GLU   B 1 114 ? 27.731 -18.869 0.578   1.00 14.58 -1 114 GLU   B OE2  1 
ATOM   6013 H H    . GLU   B 1 114 ? 32.581 -19.526 -0.075  1.00 15.91 ?  114 GLU   B H    1 
ATOM   6014 H HA   . GLU   B 1 114 ? 31.696 -18.228 -2.132  1.00 15.60 ?  114 GLU   B HA   1 
ATOM   6015 H HB2  . GLU   B 1 114 ? 31.469 -17.642 0.605   1.00 16.96 ?  114 GLU   B HB2  1 
ATOM   6016 H HB3  . GLU   B 1 114 ? 30.821 -16.679 -0.488  1.00 16.96 ?  114 GLU   B HB3  1 
ATOM   6017 H HG2  . GLU   B 1 114 ? 29.426 -18.334 -1.210  1.00 17.27 ?  114 GLU   B HG2  1 
ATOM   6018 H HG3  . GLU   B 1 114 ? 30.179 -19.420 -0.336  1.00 17.27 ?  114 GLU   B HG3  1 
ATOM   6019 N N    . ASN   B 1 115 ? 34.315 -16.909 -0.969  1.00 12.73 ?  115 ASN   B N    1 
ATOM   6020 C CA   . ASN   B 1 115 ? 35.308 -15.874 -1.269  1.00 12.19 ?  115 ASN   B CA   1 
ATOM   6021 C C    . ASN   B 1 115 ? 35.720 -15.903 -2.735  1.00 12.46 ?  115 ASN   B C    1 
ATOM   6022 O O    . ASN   B 1 115 ? 36.106 -14.864 -3.298  1.00 12.64 ?  115 ASN   B O    1 
ATOM   6023 C CB   . ASN   B 1 115 ? 36.542 -16.035 -0.377  1.00 13.50 ?  115 ASN   B CB   1 
ATOM   6024 C CG   . ASN   B 1 115 ? 36.259 -15.774 1.085   1.00 13.75 ?  115 ASN   B CG   1 
ATOM   6025 O OD1  . ASN   B 1 115 ? 36.241 -14.621 1.528   1.00 15.34 ?  115 ASN   B OD1  1 
ATOM   6026 N ND2  . ASN   B 1 115 ? 36.093 -16.843 1.860   1.00 13.64 ?  115 ASN   B ND2  1 
ATOM   6027 H H    . ASN   B 1 115 ? 34.554 -17.476 -0.362  1.00 15.30 ?  115 ASN   B H    1 
ATOM   6028 H HA   . ASN   B 1 115 ? 34.924 -15.007 -1.088  1.00 14.64 ?  115 ASN   B HA   1 
ATOM   6029 H HB2  . ASN   B 1 115 ? 36.884 -16.938 -0.460  1.00 16.22 ?  115 ASN   B HB2  1 
ATOM   6030 H HB3  . ASN   B 1 115 ? 37.221 -15.398 -0.658  1.00 16.22 ?  115 ASN   B HB3  1 
ATOM   6031 H HD21 . ASN   B 1 115 ? 35.937 -16.753 2.701   1.00 16.39 ?  115 ASN   B HD21 1 
ATOM   6032 H HD22 . ASN   B 1 115 ? 36.127 -17.638 1.517   1.00 16.39 ?  115 ASN   B HD22 1 
ATOM   6033 N N    . PHE   B 1 116 ? 35.688 -17.082 -3.366  1.00 12.47 ?  116 PHE   B N    1 
ATOM   6034 C CA   . PHE   B 1 116 ? 36.115 -17.177 -4.756  1.00 13.12 ?  116 PHE   B CA   1 
ATOM   6035 C C    . PHE   B 1 116 ? 35.216 -16.353 -5.671  1.00 12.48 ?  116 PHE   B C    1 
ATOM   6036 O O    . PHE   B 1 116 ? 35.650 -15.921 -6.745  1.00 13.24 ?  116 PHE   B O    1 
ATOM   6037 C CB   . PHE   B 1 116 ? 36.078 -18.621 -5.273  1.00 12.22 ?  116 PHE   B CB   1 
ATOM   6038 C CG   . PHE   B 1 116 ? 37.151 -19.580 -4.721  1.00 12.47 ?  116 PHE   B CG   1 
ATOM   6039 C CD1  . PHE   B 1 116 ? 37.795 -19.397 -3.511  1.00 13.19 ?  116 PHE   B CD1  1 
ATOM   6040 C CD2  . PHE   B 1 116 ? 37.451 -20.722 -5.448  1.00 12.97 ?  116 PHE   B CD2  1 
ATOM   6041 C CE1  . PHE   B 1 116 ? 38.721 -20.329 -3.056  1.00 12.98 ?  116 PHE   B CE1  1 
ATOM   6042 C CE2  . PHE   B 1 116 ? 38.373 -21.659 -4.999  1.00 12.93 ?  116 PHE   B CE2  1 
ATOM   6043 C CZ   . PHE   B 1 116 ? 38.997 -21.466 -3.808  1.00 13.02 ?  116 PHE   B CZ   1 
ATOM   6044 H H    . PHE   B 1 116 ? 35.417 -17.828 -3.019  1.00 14.98 ?  116 PHE   B H    1 
ATOM   6045 H HA   . PHE   B 1 116 ? 37.021 -16.849 -4.838  1.00 15.76 ?  116 PHE   B HA   1 
ATOM   6046 H HB2  . PHE   B 1 116 ? 35.209 -19.002 -5.057  1.00 14.69 ?  116 PHE   B HB2  1 
ATOM   6047 H HB3  . PHE   B 1 116 ? 36.181 -18.602 -6.240  1.00 14.69 ?  116 PHE   B HB3  1 
ATOM   6048 H HD1  . PHE   B 1 116 ? 37.600 -18.648 -2.993  1.00 15.85 ?  116 PHE   B HD1  1 
ATOM   6049 H HD2  . PHE   B 1 116 ? 37.012 -20.870 -6.258  1.00 15.59 ?  116 PHE   B HD2  1 
ATOM   6050 H HE1  . PHE   B 1 116 ? 39.156 -20.198 -2.244  1.00 15.60 ?  116 PHE   B HE1  1 
ATOM   6051 H HE2  . PHE   B 1 116 ? 38.557 -22.408 -5.512  1.00 15.54 ?  116 PHE   B HE2  1 
ATOM   6052 H HZ   . PHE   B 1 116 ? 39.631 -22.080 -3.512  1.00 15.65 ?  116 PHE   B HZ   1 
ATOM   6053 N N    . ASN   B 1 117 ? 33.955 -16.148 -5.283  1.00 12.80 ?  117 ASN   B N    1 
ATOM   6054 C CA   . ASN   B 1 117 ? 33.004 -15.450 -6.149  1.00 13.61 ?  117 ASN   B CA   1 
ATOM   6055 C C    . ASN   B 1 117 ? 33.322 -13.971 -6.305  1.00 14.44 ?  117 ASN   B C    1 
ATOM   6056 O O    . ASN   B 1 117 ? 32.720 -13.317 -7.157  1.00 15.30 ?  117 ASN   B O    1 
ATOM   6057 C CB   . ASN   B 1 117 ? 31.578 -15.674 -5.655  1.00 13.34 ?  117 ASN   B CB   1 
ATOM   6058 C CG   . ASN   B 1 117 ? 31.122 -17.078 -5.917  1.00 13.78 ?  117 ASN   B CG   1 
ATOM   6059 O OD1  . ASN   B 1 117 ? 31.482 -17.673 -6.938  1.00 14.89 ?  117 ASN   B OD1  1 
ATOM   6060 N ND2  . ASN   B 1 117 ? 30.378 -17.649 -4.980  1.00 13.46 ?  117 ASN   B ND2  1 
ATOM   6061 H H    . ASN   B 1 117 ? 33.629 -16.402 -4.526  1.00 15.39 ?  117 ASN   B H    1 
ATOM   6062 H HA   . ASN   B 1 117 ? 33.061 -15.847 -7.028  1.00 16.35 ?  117 ASN   B HA   1 
ATOM   6063 H HB2  . ASN   B 1 117 ? 31.537 -15.515 -4.695  1.00 16.03 ?  117 ASN   B HB2  1 
ATOM   6064 H HB3  . ASN   B 1 117 ? 30.979 -15.061 -6.115  1.00 16.03 ?  117 ASN   B HB3  1 
ATOM   6065 H HD21 . ASN   B 1 117 ? 30.089 -18.454 -5.092  1.00 16.17 ?  117 ASN   B HD21 1 
ATOM   6066 H HD22 . ASN   B 1 117 ? 30.151 -17.208 -4.279  1.00 16.17 ?  117 ASN   B HD22 1 
ATOM   6067 N N    . GLN   B 1 118 ? 34.260 -13.444 -5.533  1.00 13.43 ?  118 GLN   B N    1 
ATOM   6068 C CA   . GLN   B 1 118 ? 34.683 -12.061 -5.677  1.00 14.23 ?  118 GLN   B CA   1 
ATOM   6069 C C    . GLN   B 1 118 ? 35.756 -11.873 -6.744  1.00 14.21 ?  118 GLN   B C    1 
ATOM   6070 O O    . GLN   B 1 118 ? 36.224 -10.746 -6.933  1.00 15.66 ?  118 GLN   B O    1 
ATOM   6071 C CB   . GLN   B 1 118 ? 35.154 -11.510 -4.325  1.00 14.41 ?  118 GLN   B CB   1 
ATOM   6072 C CG   . GLN   B 1 118 ? 34.075 -11.559 -3.258  1.00 14.46 ?  118 GLN   B CG   1 
ATOM   6073 C CD   . GLN   B 1 118 ? 32.904 -10.650 -3.579  1.00 14.33 ?  118 GLN   B CD   1 
ATOM   6074 O OE1  . GLN   B 1 118 ? 33.091 -9.512  -4.017  1.00 15.45 ?  118 GLN   B OE1  1 
ATOM   6075 N NE2  . GLN   B 1 118 ? 31.690 -11.149 -3.382  1.00 14.88 ?  118 GLN   B NE2  1 
ATOM   6076 H H    . GLN   B 1 118 ? 34.684 -13.866 -4.911  1.00 16.14 ?  118 GLN   B H    1 
ATOM   6077 H HA   . GLN   B 1 118 ? 33.922 -11.534 -5.961  1.00 17.10 ?  118 GLN   B HA   1 
ATOM   6078 H HB2  . GLN   B 1 118 ? 35.908 -12.026 -4.016  1.00 17.32 ?  118 GLN   B HB2  1 
ATOM   6079 H HB3  . GLN   B 1 118 ? 35.414 -10.577 -4.437  1.00 17.32 ?  118 GLN   B HB3  1 
ATOM   6080 H HG2  . GLN   B 1 118 ? 33.744 -12.470 -3.187  1.00 17.38 ?  118 GLN   B HG2  1 
ATOM   6081 H HG3  . GLN   B 1 118 ? 34.453 -11.276 -2.412  1.00 17.38 ?  118 GLN   B HG3  1 
ATOM   6082 H HE21 . GLN   B 1 118 ? 31.602 -11.949 -3.067  1.00 17.88 ?  118 GLN   B HE21 1 
ATOM   6083 H HE22 . GLN   B 1 118 ? 31.000 -10.674 -3.549  1.00 17.88 ?  118 GLN   B HE22 1 
ATOM   6084 N N    . HIS   B 1 119 ? 36.109 -12.932 -7.476  1.00 13.07 ?  119 HIS   B N    1 
ATOM   6085 C CA   . HIS   B 1 119 ? 37.158 -12.883 -8.488  1.00 13.70 ?  119 HIS   B CA   1 
ATOM   6086 C C    . HIS   B 1 119 ? 36.675 -13.614 -9.725  1.00 13.71 ?  119 HIS   B C    1 
ATOM   6087 O O    . HIS   B 1 119 ? 36.160 -14.728 -9.623  1.00 14.62 ?  119 HIS   B O    1 
ATOM   6088 C CB   . HIS   B 1 119 ? 38.429 -13.520 -7.930  1.00 13.82 ?  119 HIS   B CB   1 
ATOM   6089 C CG   . HIS   B 1 119 ? 38.897 -12.831 -6.693  1.00 15.00 ?  119 HIS   B CG   1 
ATOM   6090 N ND1  . HIS   B 1 119 ? 39.725 -11.727 -6.726  1.00 16.34 ?  119 HIS   B ND1  1 
ATOM   6091 C CD2  . HIS   B 1 119 ? 38.576 -13.027 -5.392  1.00 16.05 ?  119 HIS   B CD2  1 
ATOM   6092 C CE1  . HIS   B 1 119 ? 39.921 -11.300 -5.492  1.00 17.46 ?  119 HIS   B CE1  1 
ATOM   6093 N NE2  . HIS   B 1 119 ? 39.220 -12.056 -4.667  1.00 17.30 ?  119 HIS   B NE2  1 
ATOM   6094 H H    . HIS   B 1 119 ? 35.743 -13.711 -7.409  1.00 15.71 ?  119 HIS   B H    1 
ATOM   6095 H HA   . HIS   B 1 119 ? 37.346 -11.957 -8.721  1.00 16.46 ?  119 HIS   B HA   1 
ATOM   6096 H HB2  . HIS   B 1 119 ? 38.252 -14.448 -7.719  1.00 16.61 ?  119 HIS   B HB2  1 
ATOM   6097 H HB3  . HIS   B 1 119 ? 39.133 -13.459 -8.599  1.00 16.61 ?  119 HIS   B HB3  1 
ATOM   6098 H HD2  . HIS   B 1 119 ? 38.005 -13.685 -5.059  1.00 19.28 ?  119 HIS   B HD2  1 
ATOM   6099 H HE1  . HIS   B 1 119 ? 40.472 -10.596 -5.241  1.00 20.98 ?  119 HIS   B HE1  1 
ATOM   6100 H HE2  . HIS   B 1 119 ? 39.206 -11.988 -3.808  1.00 20.78 ?  119 HIS   B HE2  1 
ATOM   6101 N N    A GLU   B 1 120 ? 36.834 -12.995 -10.895 0.56 14.53 ?  120 GLU   B N    1 
ATOM   6102 N N    B GLU   B 1 120 ? 36.835 -12.989 -10.892 0.44 14.61 ?  120 GLU   B N    1 
ATOM   6103 C CA   A GLU   B 1 120 ? 36.247 -13.573 -12.099 0.56 16.13 ?  120 GLU   B CA   1 
ATOM   6104 C CA   B GLU   B 1 120 ? 36.263 -13.557 -12.107 0.44 16.05 ?  120 GLU   B CA   1 
ATOM   6105 C C    A GLU   B 1 120 ? 36.924 -14.874 -12.517 0.56 14.93 ?  120 GLU   B C    1 
ATOM   6106 C C    B GLU   B 1 120 ? 36.921 -14.876 -12.496 0.44 14.89 ?  120 GLU   B C    1 
ATOM   6107 O O    A GLU   B 1 120 ? 36.267 -15.743 -13.101 0.56 15.01 ?  120 GLU   B O    1 
ATOM   6108 O O    B GLU   B 1 120 ? 36.245 -15.763 -13.029 0.44 14.90 ?  120 GLU   B O    1 
ATOM   6109 C CB   A GLU   B 1 120 ? 36.254 -12.554 -13.239 0.56 19.73 ?  120 GLU   B CB   1 
ATOM   6110 C CB   B GLU   B 1 120 ? 36.341 -12.545 -13.249 0.44 19.29 ?  120 GLU   B CB   1 
ATOM   6111 C CG   A GLU   B 1 120 ? 35.234 -11.437 -13.057 0.56 24.22 ?  120 GLU   B CG   1 
ATOM   6112 C CG   B GLU   B 1 120 ? 35.441 -11.334 -13.057 0.44 23.41 ?  120 GLU   B CG   1 
ATOM   6113 C CD   A GLU   B 1 120 ? 35.088 -10.550 -14.279 0.56 27.90 ?  120 GLU   B CD   1 
ATOM   6114 C CD   B GLU   B 1 120 ? 35.415 -10.431 -14.278 0.44 27.24 ?  120 GLU   B CD   1 
ATOM   6115 O OE1  A GLU   B 1 120 ? 36.111 -10.225 -14.920 0.56 29.96 ?  120 GLU   B OE1  1 
ATOM   6116 O OE1  B GLU   B 1 120 ? 36.374 -10.493 -15.079 0.44 29.16 ?  120 GLU   B OE1  1 
ATOM   6117 O OE2  A GLU   B 1 120 ? 33.938 -10.179 -14.599 0.56 29.79 -1 120 GLU   B OE2  1 
ATOM   6118 O OE2  B GLU   B 1 120 ? 34.448 -9.658  -14.434 0.44 28.74 -1 120 GLU   B OE2  1 
ATOM   6119 H H    A GLU   B 1 120 ? 37.264 -12.257 -11.015 0.56 17.46 ?  120 GLU   B H    1 
ATOM   6120 H H    B GLU   B 1 120 ? 37.262 -12.248 -11.003 0.44 17.55 ?  120 GLU   B H    1 
ATOM   6121 H HA   A GLU   B 1 120 ? 35.322 -13.784 -11.911 0.56 19.37 ?  120 GLU   B HA   1 
ATOM   6122 H HA   B GLU   B 1 120 ? 35.328 -13.740 -11.947 0.44 19.28 ?  120 GLU   B HA   1 
ATOM   6123 H HB2  A GLU   B 1 120 ? 37.131 -12.147 -13.293 0.56 23.70 ?  120 GLU   B HB2  1 
ATOM   6124 H HB2  B GLU   B 1 120 ? 37.250 -12.221 -13.327 0.44 23.16 ?  120 GLU   B HB2  1 
ATOM   6125 H HB3  A GLU   B 1 120 ? 36.047 -13.010 -14.069 0.56 23.70 ?  120 GLU   B HB3  1 
ATOM   6126 H HB3  B GLU   B 1 120 ? 36.074 -12.980 -14.075 0.44 23.16 ?  120 GLU   B HB3  1 
ATOM   6127 H HG2  A GLU   B 1 120 ? 34.363 -11.828 -12.892 0.56 29.09 ?  120 GLU   B HG2  1 
ATOM   6128 H HG2  B GLU   B 1 120 ? 34.536 -11.639 -12.857 0.44 28.11 ?  120 GLU   B HG2  1 
ATOM   6129 H HG3  A GLU   B 1 120 ? 35.501 -10.885 -12.306 0.56 29.09 ?  120 GLU   B HG3  1 
ATOM   6130 H HG3  B GLU   B 1 120 ? 35.775 -10.799 -12.322 0.44 28.11 ?  120 GLU   B HG3  1 
ATOM   6131 N N    . VAL   B 1 121 ? 38.221 -15.022 -12.251 1.00 13.96 ?  121 VAL   B N    1 
ATOM   6132 C CA   . VAL   B 1 121 ? 38.960 -16.235 -12.605 1.00 13.20 ?  121 VAL   B CA   1 
ATOM   6133 C C    . VAL   B 1 121 ? 40.075 -16.442 -11.588 1.00 13.88 ?  121 VAL   B C    1 
ATOM   6134 O O    . VAL   B 1 121 ? 40.752 -15.482 -11.193 1.00 14.00 ?  121 VAL   B O    1 
ATOM   6135 C CB   . VAL   B 1 121 ? 39.475 -16.183 -14.063 1.00 15.85 ?  121 VAL   B CB   1 
ATOM   6136 C CG1  . VAL   B 1 121 ? 40.342 -14.956 -14.292 1.00 17.51 ?  121 VAL   B CG1  1 
ATOM   6137 C CG2  . VAL   B 1 121 ? 40.222 -17.461 -14.431 1.00 17.47 ?  121 VAL   B CG2  1 
ATOM   6138 H H    A VAL   B 1 121 ? 38.710 -14.420 -11.873 0.56 16.77 ?  121 VAL   B H    1 
ATOM   6139 H H    B VAL   B 1 121 ? 38.714 -14.418 -11.881 0.44 16.77 ?  121 VAL   B H    1 
ATOM   6140 H HA   . VAL   B 1 121 ? 38.350 -16.986 -12.540 1.00 15.86 ?  121 VAL   B HA   1 
ATOM   6141 H HB   . VAL   B 1 121 ? 38.708 -16.117 -14.659 1.00 19.04 ?  121 VAL   B HB   1 
ATOM   6142 H HG11 . VAL   B 1 121 ? 40.657 -14.958 -15.209 1.00 21.03 ?  121 VAL   B HG11 1 
ATOM   6143 H HG12 . VAL   B 1 121 ? 39.812 -14.159 -14.128 1.00 21.03 ?  121 VAL   B HG12 1 
ATOM   6144 H HG13 . VAL   B 1 121 ? 41.096 -14.983 -13.683 1.00 21.03 ?  121 VAL   B HG13 1 
ATOM   6145 H HG21 . VAL   B 1 121 ? 40.431 -17.444 -15.379 1.00 20.98 ?  121 VAL   B HG21 1 
ATOM   6146 H HG22 . VAL   B 1 121 ? 41.044 -17.508 -13.916 1.00 20.98 ?  121 VAL   B HG22 1 
ATOM   6147 H HG23 . VAL   B 1 121 ? 39.662 -18.228 -14.232 1.00 20.98 ?  121 VAL   B HG23 1 
ATOM   6148 N N    . LEU   B 1 122 ? 40.245 -17.696 -11.146 1.00 13.03 ?  122 LEU   B N    1 
ATOM   6149 C CA   . LEU   B 1 122 ? 41.224 -18.054 -10.123 1.00 12.82 ?  122 LEU   B CA   1 
ATOM   6150 C C    . LEU   B 1 122 ? 41.877 -19.388 -10.451 1.00 12.73 ?  122 LEU   B C    1 
ATOM   6151 O O    . LEU   B 1 122 ? 41.222 -20.312 -10.955 1.00 13.36 ?  122 LEU   B O    1 
ATOM   6152 C CB   . LEU   B 1 122 ? 40.573 -18.265 -8.740  1.00 14.86 ?  122 LEU   B CB   1 
ATOM   6153 C CG   . LEU   B 1 122 ? 39.542 -17.238 -8.259  1.00 15.04 ?  122 LEU   B CG   1 
ATOM   6154 C CD1  . LEU   B 1 122 ? 38.140 -17.581 -8.727  1.00 15.57 ?  122 LEU   B CD1  1 
ATOM   6155 C CD2  . LEU   B 1 122 ? 39.579 -17.130 -6.756  1.00 14.31 ?  122 LEU   B CD2  1 
ATOM   6156 H H    . LEU   B 1 122 ? 39.790 -18.372 -11.430 1.00 15.65 ?  122 LEU   B H    1 
ATOM   6157 H HA   . LEU   B 1 122 ? 41.903 -17.364 -10.051 1.00 15.41 ?  122 LEU   B HA   1 
ATOM   6158 H HB2  . LEU   B 1 122 ? 40.125 -19.121 -8.749  1.00 17.86 ?  122 LEU   B HB2  1 
ATOM   6159 H HB3  . LEU   B 1 122 ? 41.279 -18.279 -8.077  1.00 17.86 ?  122 LEU   B HB3  1 
ATOM   6160 H HG   . LEU   B 1 122 ? 39.774 -16.366 -8.619  1.00 18.07 ?  122 LEU   B HG   1 
ATOM   6161 H HD11 . LEU   B 1 122 ? 37.518 -16.925 -8.364  1.00 18.71 ?  122 LEU   B HD11 1 
ATOM   6162 H HD12 . LEU   B 1 122 ? 38.115 -17.547 -9.698  1.00 18.71 ?  122 LEU   B HD12 1 
ATOM   6163 H HD13 . LEU   B 1 122 ? 37.908 -18.464 -8.417  1.00 18.71 ?  122 LEU   B HD13 1 
ATOM   6164 H HD21 . LEU   B 1 122 ? 38.899 -16.503 -6.462  1.00 17.20 ?  122 LEU   B HD21 1 
ATOM   6165 H HD22 . LEU   B 1 122 ? 39.411 -18.004 -6.370  1.00 17.20 ?  122 LEU   B HD22 1 
ATOM   6166 H HD23 . LEU   B 1 122 ? 40.457 -16.813 -6.480  1.00 17.20 ?  122 LEU   B HD23 1 
ATOM   6167 N N    . LEU   B 1 123 ? 43.156 -19.496 -10.082 1.00 11.69 ?  123 LEU   B N    1 
ATOM   6168 C CA   . LEU   B 1 123 ? 43.864 -20.766 -9.954  1.00 12.02 ?  123 LEU   B CA   1 
ATOM   6169 C C    . LEU   B 1 123 ? 43.838 -21.153 -8.480  1.00 11.90 ?  123 LEU   B C    1 
ATOM   6170 O O    . LEU   B 1 123 ? 44.190 -20.329 -7.630  1.00 11.90 ?  123 LEU   B O    1 
ATOM   6171 C CB   . LEU   B 1 123 ? 45.311 -20.592 -10.421 1.00 12.46 ?  123 LEU   B CB   1 
ATOM   6172 C CG   . LEU   B 1 123 ? 46.253 -21.779 -10.176 1.00 13.03 ?  123 LEU   B CG   1 
ATOM   6173 C CD1  . LEU   B 1 123 ? 45.828 -23.027 -10.941 1.00 13.93 ?  123 LEU   B CD1  1 
ATOM   6174 C CD2  . LEU   B 1 123 ? 47.663 -21.386 -10.566 1.00 14.13 ?  123 LEU   B CD2  1 
ATOM   6175 H H    . LEU   B 1 123 ? 43.648 -18.819 -9.880  1.00 14.05 ?  123 LEU   B H    1 
ATOM   6176 H HA   . LEU   B 1 123 ? 43.423 -21.457 -10.479 1.00 14.44 ?  123 LEU   B HA   1 
ATOM   6177 H HB2  . LEU   B 1 123 ? 45.297 -20.427 -11.376 1.00 14.97 ?  123 LEU   B HB2  1 
ATOM   6178 H HB3  . LEU   B 1 123 ? 45.682 -19.825 -9.963  1.00 14.97 ?  123 LEU   B HB3  1 
ATOM   6179 H HG   . LEU   B 1 123 ? 46.254 -21.991 -9.229  1.00 15.65 ?  123 LEU   B HG   1 
ATOM   6180 H HD11 . LEU   B 1 123 ? 46.464 -23.734 -10.760 1.00 16.74 ?  123 LEU   B HD11 1 
ATOM   6181 H HD12 . LEU   B 1 123 ? 44.943 -23.291 -10.646 1.00 16.74 ?  123 LEU   B HD12 1 
ATOM   6182 H HD13 . LEU   B 1 123 ? 45.816 -22.823 -11.889 1.00 16.74 ?  123 LEU   B HD13 1 
ATOM   6183 H HD21 . LEU   B 1 123 ? 48.252 -22.137 -10.409 1.00 16.98 ?  123 LEU   B HD21 1 
ATOM   6184 H HD22 . LEU   B 1 123 ? 47.672 -21.145 -11.506 1.00 16.98 ?  123 LEU   B HD22 1 
ATOM   6185 H HD23 . LEU   B 1 123 ? 47.939 -20.627 -10.028 1.00 16.98 ?  123 LEU   B HD23 1 
ATOM   6186 N N    . ALA   B 1 124 ? 43.401 -22.380 -8.168  1.00 11.80 ?  124 ALA   B N    1 
ATOM   6187 C CA   . ALA   B 1 124 ? 43.143 -22.699 -6.772  1.00 11.95 ?  124 ALA   B CA   1 
ATOM   6188 C C    . ALA   B 1 124 ? 43.411 -24.160 -6.440  1.00 11.57 ?  124 ALA   B C    1 
ATOM   6189 O O    . ALA   B 1 124 ? 43.283 -25.040 -7.307  1.00 12.13 ?  124 ALA   B O    1 
ATOM   6190 C CB   . ALA   B 1 124 ? 41.689 -22.382 -6.398  1.00 12.77 ?  124 ALA   B CB   1 
ATOM   6191 H H    . ALA   B 1 124 ? 43.248 -23.026 -8.729  1.00 14.18 ?  124 ALA   B H    1 
ATOM   6192 H HA   . ALA   B 1 124 ? 43.715 -22.145 -6.227  1.00 14.36 ?  124 ALA   B HA   1 
ATOM   6193 H HB1  . ALA   B 1 124 ? 41.538 -22.594 -5.466  1.00 15.34 ?  124 ALA   B HB1  1 
ATOM   6194 H HB2  . ALA   B 1 124 ? 41.522 -21.431 -6.548  1.00 15.34 ?  124 ALA   B HB2  1 
ATOM   6195 H HB3  . ALA   B 1 124 ? 41.090 -22.904 -6.958  1.00 15.34 ?  124 ALA   B HB3  1 
ATOM   6196 N N    . PRO   B 1 125 ? 43.712 -24.445 -5.177  1.00 11.81 ?  125 PRO   B N    1 
ATOM   6197 C CA   . PRO   B 1 125 ? 43.650 -25.810 -4.651  1.00 12.41 ?  125 PRO   B CA   1 
ATOM   6198 C C    . PRO   B 1 125 ? 42.250 -26.084 -4.104  1.00 13.47 ?  125 PRO   B C    1 
ATOM   6199 O O    . PRO   B 1 125 ? 41.453 -25.170 -3.905  1.00 13.58 ?  125 PRO   B O    1 
ATOM   6200 C CB   . PRO   B 1 125 ? 44.637 -25.733 -3.482  1.00 13.55 ?  125 PRO   B CB   1 
ATOM   6201 C CG   . PRO   B 1 125 ? 44.397 -24.349 -2.918  1.00 13.77 ?  125 PRO   B CG   1 
ATOM   6202 C CD   . PRO   B 1 125 ? 44.039 -23.471 -4.118  1.00 12.68 ?  125 PRO   B CD   1 
ATOM   6203 H HA   . PRO   B 1 125 ? 43.927 -26.476 -5.303  1.00 14.91 ?  125 PRO   B HA   1 
ATOM   6204 H HB2  . PRO   B 1 125 ? 44.428 -26.418 -2.825  1.00 16.28 ?  125 PRO   B HB2  1 
ATOM   6205 H HB3  . PRO   B 1 125 ? 45.548 -25.824 -3.801  1.00 16.28 ?  125 PRO   B HB3  1 
ATOM   6206 H HG2  . PRO   B 1 125 ? 43.660 -24.379 -2.285  1.00 16.54 ?  125 PRO   B HG2  1 
ATOM   6207 H HG3  . PRO   B 1 125 ? 45.204 -24.030 -2.482  1.00 16.54 ?  125 PRO   B HG3  1 
ATOM   6208 H HD2  . PRO   B 1 125 ? 43.269 -22.919 -3.919  1.00 15.24 ?  125 PRO   B HD2  1 
ATOM   6209 H HD3  . PRO   B 1 125 ? 44.807 -22.928 -4.375  1.00 15.24 ?  125 PRO   B HD3  1 
ATOM   6210 N N    . LEU   B 1 126 ? 41.989 -27.356 -3.793  1.00 13.73 ?  126 LEU   B N    1 
ATOM   6211 C CA   . LEU   B 1 126 ? 40.767 -27.715 -3.080  1.00 14.21 ?  126 LEU   B CA   1 
ATOM   6212 C C    . LEU   B 1 126 ? 40.887 -27.311 -1.616  1.00 14.20 ?  126 LEU   B C    1 
ATOM   6213 O O    . LEU   B 1 126 ? 41.787 -27.765 -0.908  1.00 16.10 ?  126 LEU   B O    1 
ATOM   6214 C CB   . LEU   B 1 126 ? 40.520 -29.213 -3.188  1.00 15.23 ?  126 LEU   B CB   1 
ATOM   6215 C CG   . LEU   B 1 126 ? 39.977 -29.707 -4.529  1.00 16.38 ?  126 LEU   B CG   1 
ATOM   6216 C CD1  . LEU   B 1 126 ? 40.004 -31.218 -4.582  1.00 18.65 ?  126 LEU   B CD1  1 
ATOM   6217 C CD2  . LEU   B 1 126 ? 38.570 -29.203 -4.779  1.00 16.97 ?  126 LEU   B CD2  1 
ATOM   6218 H H    . LEU   B 1 126 ? 42.512 -28.020 -3.965  1.00 16.50 ?  126 LEU   B H    1 
ATOM   6219 H HA   . LEU   B 1 126 ? 40.022 -27.237 -3.466  1.00 17.08 ?  126 LEU   B HA   1 
ATOM   6220 H HB2  . LEU   B 1 126 ? 41.358 -29.669 -3.025  1.00 18.30 ?  126 LEU   B HB2  1 
ATOM   6221 H HB3  . LEU   B 1 126 ? 39.878 -29.459 -2.506  1.00 18.30 ?  126 LEU   B HB3  1 
ATOM   6222 H HG   . LEU   B 1 126 ? 40.548 -29.369 -5.240  1.00 19.68 ?  126 LEU   B HG   1 
ATOM   6223 H HD11 . LEU   B 1 126 ? 39.657 -31.507 -5.440  1.00 22.40 ?  126 LEU   B HD11 1 
ATOM   6224 H HD12 . LEU   B 1 126 ? 40.916 -31.522 -4.470  1.00 22.40 ?  126 LEU   B HD12 1 
ATOM   6225 H HD13 . LEU   B 1 126 ? 39.447 -31.565 -3.866  1.00 22.40 ?  126 LEU   B HD13 1 
ATOM   6226 H HD21 . LEU   B 1 126 ? 38.221 -29.622 -5.580  1.00 20.38 ?  126 LEU   B HD21 1 
ATOM   6227 H HD22 . LEU   B 1 126 ? 38.013 -29.426 -4.017  1.00 20.38 ?  126 LEU   B HD22 1 
ATOM   6228 H HD23 . LEU   B 1 126 ? 38.591 -28.237 -4.897  1.00 20.38 ?  126 LEU   B HD23 1 
ATOM   6229 N N    . LEU   B 1 127 ? 39.964 -26.476 -1.153  1.00 14.05 ?  127 LEU   B N    1 
ATOM   6230 C CA   . LEU   B 1 127 ? 40.018 -25.988 0.215   1.00 14.47 ?  127 LEU   B CA   1 
ATOM   6231 C C    . LEU   B 1 127 ? 39.738 -27.109 1.210   1.00 14.22 ?  127 LEU   B C    1 
ATOM   6232 O O    . LEU   B 1 127 ? 38.910 -27.998 0.982   1.00 14.73 ?  127 LEU   B O    1 
ATOM   6233 C CB   . LEU   B 1 127 ? 39.002 -24.864 0.427   1.00 15.32 ?  127 LEU   B CB   1 
ATOM   6234 C CG   . LEU   B 1 127 ? 39.191 -23.607 -0.419  1.00 15.56 ?  127 LEU   B CG   1 
ATOM   6235 C CD1  . LEU   B 1 127 ? 38.069 -22.622 -0.133  1.00 16.21 ?  127 LEU   B CD1  1 
ATOM   6236 C CD2  . LEU   B 1 127 ? 40.558 -22.972 -0.170  1.00 16.63 ?  127 LEU   B CD2  1 
ATOM   6237 H H    . LEU   B 1 127 ? 39.304 -26.169 -1.612  1.00 16.88 ?  127 LEU   B H    1 
ATOM   6238 H HA   . LEU   B 1 127 ? 40.905 -25.629 0.394   1.00 17.39 ?  127 LEU   B HA   1 
ATOM   6239 H HB2  . LEU   B 1 127 ? 38.118 -25.210 0.231   1.00 18.40 ?  127 LEU   B HB2  1 
ATOM   6240 H HB3  . LEU   B 1 127 ? 39.038 -24.590 1.360   1.00 18.40 ?  127 LEU   B HB3  1 
ATOM   6241 H HG   . LEU   B 1 127 ? 39.139 -23.844 -1.353  1.00 18.70 ?  127 LEU   B HG   1 
ATOM   6242 H HD11 . LEU   B 1 127 ? 38.205 -21.818 -0.670  1.00 19.48 ?  127 LEU   B HD11 1 
ATOM   6243 H HD12 . LEU   B 1 127 ? 37.219 -23.026 -0.362  1.00 19.48 ?  127 LEU   B HD12 1 
ATOM   6244 H HD13 . LEU   B 1 127 ? 38.079 -22.384 0.809   1.00 19.48 ?  127 LEU   B HD13 1 
ATOM   6245 H HD21 . LEU   B 1 127 ? 40.599 -22.115 -0.621  1.00 19.98 ?  127 LEU   B HD21 1 
ATOM   6246 H HD22 . LEU   B 1 127 ? 40.681 -22.848 0.786   1.00 19.98 ?  127 LEU   B HD22 1 
ATOM   6247 H HD23 . LEU   B 1 127 ? 41.246 -23.563 -0.515  1.00 19.98 ?  127 LEU   B HD23 1 
ATOM   6248 N N    . SER   B 1 128 ? 40.414 -27.021 2.348   1.00 14.48 ?  128 SER   B N    1 
ATOM   6249 C CA   . SER   B 1 128 ? 40.283 -27.923 3.479   1.00 14.96 ?  128 SER   B CA   1 
ATOM   6250 C C    . SER   B 1 128 ? 40.770 -29.336 3.182   1.00 16.42 ?  128 SER   B C    1 
ATOM   6251 O O    . SER   B 1 128 ? 40.664 -30.198 4.051   1.00 17.86 ?  128 SER   B O    1 
ATOM   6252 C CB   . SER   B 1 128 ? 38.872 -27.920 4.085   1.00 15.43 ?  128 SER   B CB   1 
ATOM   6253 O OG   . SER   B 1 128 ? 38.577 -26.635 4.635   1.00 15.79 ?  128 SER   B OG   1 
ATOM   6254 H H    . SER   B 1 128 ? 40.987 -26.390 2.497   1.00 17.40 ?  128 SER   B H    1 
ATOM   6255 H HA   . SER   B 1 128 ? 40.862 -27.586 4.169   1.00 17.97 ?  128 SER   B HA   1 
ATOM   6256 H HB2  . SER   B 1 128 ? 38.219 -28.133 3.395   1.00 18.53 ?  128 SER   B HB2  1 
ATOM   6257 H HB3  . SER   B 1 128 ? 38.828 -28.589 4.793   1.00 18.53 ?  128 SER   B HB3  1 
ATOM   6258 H HG   . SER   B 1 128 ? 39.139 -26.448 5.228   1.00 18.97 ?  128 SER   B HG   1 
ATOM   6259 N N    . ALA   B 1 129 ? 41.344 -29.580 2.001   1.00 17.54 ?  129 ALA   B N    1 
ATOM   6260 C CA   . ALA   B 1 129 ? 41.887 -30.881 1.646   1.00 18.80 ?  129 ALA   B CA   1 
ATOM   6261 C C    . ALA   B 1 129 ? 43.286 -31.051 2.224   1.00 17.76 ?  129 ALA   B C    1 
ATOM   6262 O O    . ALA   B 1 129 ? 43.839 -30.157 2.870   1.00 17.65 ?  129 ALA   B O    1 
ATOM   6263 C CB   . ALA   B 1 129 ? 41.927 -31.042 0.128   1.00 20.39 ?  129 ALA   B CB   1 
ATOM   6264 H H    . ALA   B 1 129 ? 41.432 -28.990 1.376   1.00 21.07 ?  129 ALA   B H    1 
ATOM   6265 H HA   . ALA   B 1 129 ? 41.321 -31.575 2.010   1.00 22.58 ?  129 ALA   B HA   1 
ATOM   6266 H HB1  . ALA   B 1 129 ? 42.279 -31.919 -0.088  1.00 24.49 ?  129 ALA   B HB1  1 
ATOM   6267 H HB2  . ALA   B 1 129 ? 41.028 -30.950 -0.222  1.00 24.49 ?  129 ALA   B HB2  1 
ATOM   6268 H HB3  . ALA   B 1 129 ? 42.500 -30.354 -0.248  1.00 24.49 ?  129 ALA   B HB3  1 
ATOM   6269 N N    . GLY   B 1 130 ? 43.869 -32.221 1.971   1.00 17.72 ?  130 GLY   B N    1 
ATOM   6270 C CA   . GLY   B 1 130 ? 45.259 -32.443 2.325   1.00 18.51 ?  130 GLY   B CA   1 
ATOM   6271 C C    . GLY   B 1 130 ? 45.472 -32.355 3.817   1.00 18.33 ?  130 GLY   B C    1 
ATOM   6272 O O    . GLY   B 1 130 ? 44.769 -32.999 4.610   1.00 18.85 ?  130 GLY   B O    1 
ATOM   6273 H H    . GLY   B 1 130 ? 43.488 -32.891 1.590   1.00 21.28 ?  130 GLY   B H    1 
ATOM   6274 H HA2  . GLY   B 1 130 ? 45.539 -33.324 2.023   1.00 22.23 ?  130 GLY   B HA2  1 
ATOM   6275 H HA3  . GLY   B 1 130 ? 45.821 -31.780 1.891   1.00 22.23 ?  130 GLY   B HA3  1 
ATOM   6276 N N    . ILE   B 1 131 ? 46.450 -31.530 4.209   1.00 18.51 ?  131 ILE   B N    1 
ATOM   6277 C CA   . ILE   B 1 131 ? 46.813 -31.401 5.610   1.00 19.48 ?  131 ILE   B CA   1 
ATOM   6278 C C    . ILE   B 1 131 ? 45.696 -30.809 6.447   1.00 18.90 ?  131 ILE   B C    1 
ATOM   6279 O O    . ILE   B 1 131 ? 45.765 -30.877 7.675   1.00 20.67 ?  131 ILE   B O    1 
ATOM   6280 C CB   . ILE   B 1 131 ? 48.134 -30.615 5.803   1.00 21.41 ?  131 ILE   B CB   1 
ATOM   6281 C CG1  . ILE   B 1 131 ? 47.958 -29.129 5.451   1.00 22.50 ?  131 ILE   B CG1  1 
ATOM   6282 C CG2  . ILE   B 1 131 ? 49.256 -31.234 4.971   1.00 22.42 ?  131 ILE   B CG2  1 
ATOM   6283 C CD1  . ILE   B 1 131 ? 49.166 -28.263 5.790   1.00 23.72 ?  131 ILE   B CD1  1 
ATOM   6284 H H    . ILE   B 1 131 ? 46.915 -31.036 3.679   1.00 22.23 ?  131 ILE   B H    1 
ATOM   6285 H HA   . ILE   B 1 131 ? 46.965 -32.286 5.962   1.00 23.40 ?  131 ILE   B HA   1 
ATOM   6286 H HB   . ILE   B 1 131 ? 48.381 -30.673 6.741   1.00 25.72 ?  131 ILE   B HB   1 
ATOM   6287 H HG12 . ILE   B 1 131 ? 47.794 -29.057 4.498   1.00 27.03 ?  131 ILE   B HG12 1 
ATOM   6288 H HG13 . ILE   B 1 131 ? 47.198 -28.771 5.940   1.00 27.03 ?  131 ILE   B HG13 1 
ATOM   6289 H HG21 . ILE   B 1 131 ? 50.095 -30.821 5.220   1.00 26.93 ?  131 ILE   B HG21 1 
ATOM   6290 H HG22 . ILE   B 1 131 ? 49.285 -32.185 5.144   1.00 26.93 ?  131 ILE   B HG22 1 
ATOM   6291 H HG23 . ILE   B 1 131 ? 49.071 -31.072 4.031   1.00 26.93 ?  131 ILE   B HG23 1 
ATOM   6292 H HD11 . ILE   B 1 131 ? 48.942 -27.334 5.624   1.00 28.49 ?  131 ILE   B HD11 1 
ATOM   6293 H HD12 . ILE   B 1 131 ? 49.391 -28.388 6.725   1.00 28.49 ?  131 ILE   B HD12 1 
ATOM   6294 H HD13 . ILE   B 1 131 ? 49.912 -28.529 5.231   1.00 28.49 ?  131 ILE   B HD13 1 
ATOM   6295 N N    . PHE   B 1 132 ? 44.669 -30.222 5.818   1.00 17.53 ?  132 PHE   B N    1 
ATOM   6296 C CA   . PHE   B 1 132 ? 43.507 -29.720 6.542   1.00 17.62 ?  132 PHE   B CA   1 
ATOM   6297 C C    . PHE   B 1 132 ? 42.488 -30.812 6.872   1.00 19.15 ?  132 PHE   B C    1 
ATOM   6298 O O    . PHE   B 1 132 ? 41.587 -30.565 7.680   1.00 21.06 ?  132 PHE   B O    1 
ATOM   6299 C CB   . PHE   B 1 132 ? 42.822 -28.595 5.754   1.00 16.80 ?  132 PHE   B CB   1 
ATOM   6300 C CG   . PHE   B 1 132 ? 43.520 -27.250 5.842   1.00 16.37 ?  132 PHE   B CG   1 
ATOM   6301 C CD1  . PHE   B 1 132 ? 44.803 -27.076 5.351   1.00 17.57 ?  132 PHE   B CD1  1 
ATOM   6302 C CD2  . PHE   B 1 132 ? 42.858 -26.146 6.369   1.00 16.14 ?  132 PHE   B CD2  1 
ATOM   6303 C CE1  . PHE   B 1 132 ? 45.425 -25.833 5.419   1.00 18.54 ?  132 PHE   B CE1  1 
ATOM   6304 C CE2  . PHE   B 1 132 ? 43.468 -24.901 6.431   1.00 16.90 ?  132 PHE   B CE2  1 
ATOM   6305 C CZ   . PHE   B 1 132 ? 44.752 -24.750 5.962   1.00 18.09 ?  132 PHE   B CZ   1 
ATOM   6306 H H    . PHE   B 1 132 ? 44.622 -30.110 4.967   1.00 21.06 ?  132 PHE   B H    1 
ATOM   6307 H HA   . PHE   B 1 132 ? 43.806 -29.343 7.381   1.00 21.16 ?  132 PHE   B HA   1 
ATOM   6308 H HB2  . PHE   B 1 132 ? 42.795 -28.848 4.821   1.00 20.18 ?  132 PHE   B HB2  1 
ATOM   6309 H HB3  . PHE   B 1 132 ? 41.917 -28.484 6.091   1.00 20.18 ?  132 PHE   B HB3  1 
ATOM   6310 H HD1  . PHE   B 1 132 ? 45.258 -27.803 4.991   1.00 21.10 ?  132 PHE   B HD1  1 
ATOM   6311 H HD2  . PHE   B 1 132 ? 41.990 -26.248 6.694   1.00 19.39 ?  132 PHE   B HD2  1 
ATOM   6312 H HE1  . PHE   B 1 132 ? 46.292 -25.731 5.099   1.00 22.27 ?  132 PHE   B HE1  1 
ATOM   6313 H HE2  . PHE   B 1 132 ? 43.016 -24.177 6.804   1.00 20.30 ?  132 PHE   B HE2  1 
ATOM   6314 H HZ   . PHE   B 1 132 ? 45.169 -23.916 6.009   1.00 21.73 ?  132 PHE   B HZ   1 
ATOM   6315 N N    . GLY   B 1 133 ? 42.586 -31.998 6.264   1.00 18.95 ?  133 GLY   B N    1 
ATOM   6316 C CA   . GLY   B 1 133 ? 41.880 -33.167 6.757   1.00 20.23 ?  133 GLY   B CA   1 
ATOM   6317 C C    . GLY   B 1 133 ? 40.475 -33.421 6.244   1.00 20.90 ?  133 GLY   B C    1 
ATOM   6318 O O    . GLY   B 1 133 ? 39.892 -34.441 6.617   1.00 22.41 ?  133 GLY   B O    1 
ATOM   6319 H H    . GLY   B 1 133 ? 43.066 -32.145 5.565   1.00 22.76 ?  133 GLY   B H    1 
ATOM   6320 H HA2  . GLY   B 1 133 ? 42.415 -33.951 6.555   1.00 24.30 ?  133 GLY   B HA2  1 
ATOM   6321 H HA3  . GLY   B 1 133 ? 41.816 -33.098 7.721   1.00 24.30 ?  133 GLY   B HA3  1 
ATOM   6322 N N    . ALA   B 1 134 ? 39.901 -32.548 5.423   1.00 19.83 ?  134 ALA   B N    1 
ATOM   6323 C CA   . ALA   B 1 134 ? 38.579 -32.836 4.883   1.00 19.68 ?  134 ALA   B CA   1 
ATOM   6324 C C    . ALA   B 1 134 ? 38.675 -33.822 3.723   1.00 19.46 ?  134 ALA   B C    1 
ATOM   6325 O O    . ALA   B 1 134 ? 39.732 -34.004 3.111   1.00 20.48 ?  134 ALA   B O    1 
ATOM   6326 C CB   . ALA   B 1 134 ? 37.899 -31.556 4.402   1.00 19.66 ?  134 ALA   B CB   1 
ATOM   6327 H H    . ALA   B 1 134 ? 40.241 -31.793 5.179   1.00 23.82 ?  134 ALA   B H    1 
ATOM   6328 H HA   . ALA   B 1 134 ? 38.029 -33.231 5.578   1.00 23.64 ?  134 ALA   B HA   1 
ATOM   6329 H HB1  . ALA   B 1 134 ? 37.012 -31.776 4.075   1.00 23.61 ?  134 ALA   B HB1  1 
ATOM   6330 H HB2  . ALA   B 1 134 ? 37.833 -30.935 5.144   1.00 23.61 ?  134 ALA   B HB2  1 
ATOM   6331 H HB3  . ALA   B 1 134 ? 38.427 -31.165 3.689   1.00 23.61 ?  134 ALA   B HB3  1 
ATOM   6332 N N    . ASP   B 1 135 ? 37.545 -34.454 3.422   1.00 20.02 ?  135 ASP   B N    1 
ATOM   6333 C CA   . ASP   B 1 135 ? 37.457 -35.340 2.274   1.00 20.80 ?  135 ASP   B CA   1 
ATOM   6334 C C    . ASP   B 1 135 ? 37.548 -34.500 1.007   1.00 19.22 ?  135 ASP   B C    1 
ATOM   6335 O O    . ASP   B 1 135 ? 36.688 -33.631 0.789   1.00 19.18 ?  135 ASP   B O    1 
ATOM   6336 C CB   . ASP   B 1 135 ? 36.126 -36.086 2.325   1.00 22.81 ?  135 ASP   B CB   1 
ATOM   6337 C CG   . ASP   B 1 135 ? 35.967 -37.097 1.204   1.00 24.45 ?  135 ASP   B CG   1 
ATOM   6338 O OD1  . ASP   B 1 135 ? 36.813 -37.134 0.288   1.00 24.61 ?  135 ASP   B OD1  1 
ATOM   6339 O OD2  . ASP   B 1 135 ? 34.996 -37.883 1.255   1.00 27.36 -1 135 ASP   B OD2  1 
ATOM   6340 H H    . ASP   B 1 135 ? 36.815 -34.378 3.866   1.00 24.04 ?  135 ASP   B H    1 
ATOM   6341 H HA   . ASP   B 1 135 ? 38.183 -35.982 2.302   1.00 24.99 ?  135 ASP   B HA   1 
ATOM   6342 H HB2  . ASP   B 1 135 ? 36.072 -36.563 3.166   1.00 27.39 ?  135 ASP   B HB2  1 
ATOM   6343 H HB3  . ASP   B 1 135 ? 35.406 -35.446 2.254   1.00 27.39 ?  135 ASP   B HB3  1 
ATOM   6344 N N    . PRO   B 1 136 ? 38.558 -34.701 0.159   1.00 19.24 ?  136 PRO   B N    1 
ATOM   6345 C CA   . PRO   B 1 136 ? 38.647 -33.886 -1.064  1.00 18.50 ?  136 PRO   B CA   1 
ATOM   6346 C C    . PRO   B 1 136 ? 37.454 -34.051 -1.984  1.00 17.71 ?  136 PRO   B C    1 
ATOM   6347 O O    . PRO   B 1 136 ? 37.125 -33.114 -2.719  1.00 17.07 ?  136 PRO   B O    1 
ATOM   6348 C CB   . PRO   B 1 136 ? 39.959 -34.357 -1.711  1.00 19.06 ?  136 PRO   B CB   1 
ATOM   6349 C CG   . PRO   B 1 136 ? 40.180 -35.742 -1.148  1.00 20.94 ?  136 PRO   B CG   1 
ATOM   6350 C CD   . PRO   B 1 136 ? 39.654 -35.682 0.253   1.00 20.58 ?  136 PRO   B CD   1 
ATOM   6351 H HA   . PRO   B 1 136 ? 38.730 -32.949 -0.839  1.00 22.22 ?  136 PRO   B HA   1 
ATOM   6352 H HB2  . PRO   B 1 136 ? 39.864 -34.388 -2.678  1.00 22.89 ?  136 PRO   B HB2  1 
ATOM   6353 H HB3  . PRO   B 1 136 ? 40.682 -33.761 -1.458  1.00 22.89 ?  136 PRO   B HB3  1 
ATOM   6354 H HG2  . PRO   B 1 136 ? 39.685 -36.396 -1.669  1.00 25.15 ?  136 PRO   B HG2  1 
ATOM   6355 H HG3  . PRO   B 1 136 ? 41.127 -35.954 -1.147  1.00 25.15 ?  136 PRO   B HG3  1 
ATOM   6356 H HD2  . PRO   B 1 136 ? 39.313 -36.547 0.525   1.00 24.72 ?  136 PRO   B HD2  1 
ATOM   6357 H HD3  . PRO   B 1 136 ? 40.338 -35.358 0.863   1.00 24.72 ?  136 PRO   B HD3  1 
ATOM   6358 N N    . ILE   B 1 137 ? 36.799 -35.217 -1.971  1.00 18.36 ?  137 ILE   B N    1 
ATOM   6359 C CA   . ILE   B 1 137 ? 35.572 -35.390 -2.744  1.00 18.31 ?  137 ILE   B CA   1 
ATOM   6360 C C    . ILE   B 1 137 ? 34.501 -34.417 -2.262  1.00 18.17 ?  137 ILE   B C    1 
ATOM   6361 O O    . ILE   B 1 137 ? 33.781 -33.802 -3.064  1.00 17.77 ?  137 ILE   B O    1 
ATOM   6362 C CB   . ILE   B 1 137 ? 35.100 -36.857 -2.670  1.00 20.41 ?  137 ILE   B CB   1 
ATOM   6363 C CG1  . ILE   B 1 137 ? 36.133 -37.777 -3.326  1.00 22.37 ?  137 ILE   B CG1  1 
ATOM   6364 C CG2  . ILE   B 1 137 ? 33.717 -37.008 -3.311  1.00 21.35 ?  137 ILE   B CG2  1 
ATOM   6365 C CD1  . ILE   B 1 137 ? 35.806 -39.254 -3.220  1.00 24.58 ?  137 ILE   B CD1  1 
ATOM   6366 H H    . ILE   B 1 137 ? 37.040 -35.913 -1.528  1.00 22.05 ?  137 ILE   B H    1 
ATOM   6367 H HA   . ILE   B 1 137 ? 35.754 -35.187 -3.675  1.00 22.00 ?  137 ILE   B HA   1 
ATOM   6368 H HB   . ILE   B 1 137 ? 35.023 -37.105 -1.741  1.00 24.52 ?  137 ILE   B HB   1 
ATOM   6369 H HG12 . ILE   B 1 137 ? 36.199 -37.563 -4.268  1.00 26.86 ?  137 ILE   B HG12 1 
ATOM   6370 H HG13 . ILE   B 1 137 ? 36.992 -37.641 -2.896  1.00 26.86 ?  137 ILE   B HG13 1 
ATOM   6371 H HG21 . ILE   B 1 137 ? 33.453 -37.941 -3.303  1.00 25.65 ?  137 ILE   B HG21 1 
ATOM   6372 H HG22 . ILE   B 1 137 ? 33.069 -36.495 -2.803  1.00 25.65 ?  137 ILE   B HG22 1 
ATOM   6373 H HG23 . ILE   B 1 137 ? 33.752 -36.684 -4.224  1.00 25.65 ?  137 ILE   B HG23 1 
ATOM   6374 H HD11 . ILE   B 1 137 ? 36.455 -39.749 -3.742  1.00 29.52 ?  137 ILE   B HD11 1 
ATOM   6375 H HD12 . ILE   B 1 137 ? 35.851 -39.530 -2.289  1.00 29.52 ?  137 ILE   B HD12 1 
ATOM   6376 H HD13 . ILE   B 1 137 ? 34.919 -39.425 -3.572  1.00 29.52 ?  137 ILE   B HD13 1 
ATOM   6377 N N    . HIS   B 1 138 ? 34.377 -34.261 -0.945  1.00 18.32 ?  138 HIS   B N    1 
ATOM   6378 C CA   . HIS   B 1 138 ? 33.426 -33.292 -0.415  1.00 18.75 ?  138 HIS   B CA   1 
ATOM   6379 C C    . HIS   B 1 138 ? 33.844 -31.865 -0.749  1.00 17.51 ?  138 HIS   B C    1 
ATOM   6380 O O    . HIS   B 1 138 ? 32.996 -31.016 -1.048  1.00 17.85 ?  138 HIS   B O    1 
ATOM   6381 C CB   . HIS   B 1 138 ? 33.307 -33.460 1.093   1.00 20.36 ?  138 HIS   B CB   1 
ATOM   6382 C CG   . HIS   B 1 138 ? 32.377 -32.475 1.720   1.00 21.63 ?  138 HIS   B CG   1 
ATOM   6383 N ND1  . HIS   B 1 138 ? 31.045 -32.389 1.372   1.00 23.29 ?  138 HIS   B ND1  1 
ATOM   6384 C CD2  . HIS   B 1 138 ? 32.587 -31.511 2.647   1.00 22.07 ?  138 HIS   B CD2  1 
ATOM   6385 C CE1  . HIS   B 1 138 ? 30.472 -31.427 2.070   1.00 23.14 ?  138 HIS   B CE1  1 
ATOM   6386 N NE2  . HIS   B 1 138 ? 31.384 -30.882 2.856   1.00 22.58 ?  138 HIS   B NE2  1 
ATOM   6387 H H    . HIS   B 1 138 ? 34.830 -34.693 -0.351  1.00 22.01 ?  138 HIS   B H    1 
ATOM   6388 H HA   . HIS   B 1 138 ? 32.556 -33.461 -0.805  1.00 22.53 ?  138 HIS   B HA   1 
ATOM   6389 H HB2  . HIS   B 1 138 ? 32.970 -34.350 1.290   1.00 24.46 ?  138 HIS   B HB2  1 
ATOM   6390 H HB3  . HIS   B 1 138 ? 34.179 -33.340 1.498   1.00 24.46 ?  138 HIS   B HB3  1 
ATOM   6391 H HD1  . HIS   B 1 138 ? 30.647 -32.887 0.792   1.00 27.96 ?  138 HIS   B HD1  1 
ATOM   6392 H HD2  . HIS   B 1 138 ? 33.382 -31.326 3.084   1.00 26.51 ?  138 HIS   B HD2  1 
ATOM   6393 H HE1  . HIS   B 1 138 ? 29.570 -31.180 2.022   1.00 27.80 ?  138 HIS   B HE1  1 
ATOM   6394 N N    . SER   B 1 139 ? 35.139 -31.571 -0.685  1.00 17.15 ?  139 SER   B N    1 
ATOM   6395 C CA   . SER   B 1 139 ? 35.580 -30.226 -1.017  1.00 16.64 ?  139 SER   B CA   1 
ATOM   6396 C C    . SER   B 1 139 ? 35.238 -29.885 -2.458  1.00 15.66 ?  139 SER   B C    1 
ATOM   6397 O O    . SER   B 1 139 ? 34.793 -28.769 -2.742  1.00 15.88 ?  139 SER   B O    1 
ATOM   6398 C CB   . SER   B 1 139 ? 37.076 -30.091 -0.765  1.00 16.84 ?  139 SER   B CB   1 
ATOM   6399 O OG   . SER   B 1 139 ? 37.479 -28.757 -1.001  1.00 16.65 ?  139 SER   B OG   1 
ATOM   6400 H H    . SER   B 1 139 ? 35.761 -32.118 -0.464  1.00 20.61 ?  139 SER   B H    1 
ATOM   6401 H HA   . SER   B 1 139 ? 35.117 -29.593 -0.451  1.00 19.99 ?  139 SER   B HA   1 
ATOM   6402 H HB2  . SER   B 1 139 ? 37.262 -30.335 0.157   1.00 20.23 ?  139 SER   B HB2  1 
ATOM   6403 H HB3  . SER   B 1 139 ? 37.558 -30.678 -1.368  1.00 20.23 ?  139 SER   B HB3  1 
ATOM   6404 H HG   . SER   B 1 139 ? 38.305 -28.676 -0.843  1.00 20.00 ?  139 SER   B HG   1 
ATOM   6405 N N    . LEU   B 1 140 ? 35.425 -30.832 -3.381  1.00 15.24 ?  140 LEU   B N    1 
ATOM   6406 C CA   . LEU   B 1 140 ? 35.060 -30.586 -4.772  1.00 15.34 ?  140 LEU   B CA   1 
ATOM   6407 C C    . LEU   B 1 140 ? 33.559 -30.350 -4.906  1.00 15.63 ?  140 LEU   B C    1 
ATOM   6408 O O    . LEU   B 1 140 ? 33.128 -29.463 -5.647  1.00 15.64 ?  140 LEU   B O    1 
ATOM   6409 C CB   . LEU   B 1 140 ? 35.521 -31.754 -5.646  1.00 15.09 ?  140 LEU   B CB   1 
ATOM   6410 C CG   . LEU   B 1 140 ? 35.173 -31.648 -7.126  1.00 15.35 ?  140 LEU   B CG   1 
ATOM   6411 C CD1  . LEU   B 1 140 ? 35.728 -30.362 -7.719  1.00 16.59 ?  140 LEU   B CD1  1 
ATOM   6412 C CD2  . LEU   B 1 140 ? 35.663 -32.888 -7.874  1.00 16.19 ?  140 LEU   B CD2  1 
ATOM   6413 H H    . LEU   B 1 140 ? 35.751 -31.613 -3.233  1.00 18.31 ?  140 LEU   B H    1 
ATOM   6414 H HA   . LEU   B 1 140 ? 35.518 -29.790 -5.082  1.00 18.43 ?  140 LEU   B HA   1 
ATOM   6415 H HB2  . LEU   B 1 140 ? 36.488 -31.827 -5.584  1.00 18.13 ?  140 LEU   B HB2  1 
ATOM   6416 H HB3  . LEU   B 1 140 ? 35.115 -32.570 -5.317  1.00 18.13 ?  140 LEU   B HB3  1 
ATOM   6417 H HG   . LEU   B 1 140 ? 34.210 -31.613 -7.217  1.00 18.45 ?  140 LEU   B HG   1 
ATOM   6418 H HD11 . LEU   B 1 140 ? 35.627 -30.391 -8.681  1.00 19.93 ?  140 LEU   B HD11 1 
ATOM   6419 H HD12 . LEU   B 1 140 ? 35.236 -29.608 -7.356  1.00 19.93 ?  140 LEU   B HD12 1 
ATOM   6420 H HD13 . LEU   B 1 140 ? 36.667 -30.288 -7.485  1.00 19.93 ?  140 LEU   B HD13 1 
ATOM   6421 H HD21 . LEU   B 1 140 ? 35.431 -32.798 -8.812  1.00 19.45 ?  140 LEU   B HD21 1 
ATOM   6422 H HD22 . LEU   B 1 140 ? 36.622 -32.958 -7.772  1.00 19.45 ?  140 LEU   B HD22 1 
ATOM   6423 H HD23 . LEU   B 1 140 ? 35.228 -33.668 -7.497  1.00 19.45 ?  140 LEU   B HD23 1 
ATOM   6424 N N    . ARG   B 1 141 ? 32.753 -31.143 -4.196  1.00 15.46 ?  141 ARG   B N    1 
ATOM   6425 C CA   . ARG   B 1 141 ? 31.304 -30.964 -4.176  1.00 17.14 ?  141 ARG   B CA   1 
ATOM   6426 C C    . ARG   B 1 141 ? 30.929 -29.551 -3.753  1.00 16.95 ?  141 ARG   B C    1 
ATOM   6427 O O    . ARG   B 1 141 ? 30.130 -28.876 -4.418  1.00 16.96 ?  141 ARG   B O    1 
ATOM   6428 C CB   . ARG   B 1 141 ? 30.724 -31.980 -3.186  1.00 18.08 ?  141 ARG   B CB   1 
ATOM   6429 C CG   . ARG   B 1 141 ? 29.258 -31.857 -2.864  1.00 19.84 ?  141 ARG   B CG   1 
ATOM   6430 C CD   . ARG   B 1 141 ? 28.463 -32.502 -3.929  1.00 21.39 ?  141 ARG   B CD   1 
ATOM   6431 N NE   . ARG   B 1 141 ? 28.207 -31.601 -5.042  1.00 21.42 ?  141 ARG   B NE   1 
ATOM   6432 C CZ   . ARG   B 1 141 ? 28.194 -31.965 -6.316  1.00 20.85 ?  141 ARG   B CZ   1 
ATOM   6433 N NH1  . ARG   B 1 141 ? 28.613 -33.162 -6.702  1.00 20.74 ?  141 ARG   B NH1  1 
ATOM   6434 N NH2  . ARG   B 1 141 ? 27.751 -31.105 -7.228  1.00 20.90 ?  141 ARG   B NH2  1 
ATOM   6435 H H    . ARG   B 1 141 ? 33.032 -31.794 -3.713  1.00 18.58 ?  141 ARG   B H    1 
ATOM   6436 H HA   . ARG   B 1 141 ? 30.937 -31.131 -5.055  1.00 20.59 ?  141 ARG   B HA   1 
ATOM   6437 H HB2  . ARG   B 1 141 ? 30.877 -32.868 -3.543  1.00 21.72 ?  141 ARG   B HB2  1 
ATOM   6438 H HB3  . ARG   B 1 141 ? 31.206 -31.891 -2.350  1.00 21.72 ?  141 ARG   B HB3  1 
ATOM   6439 H HG2  . ARG   B 1 141 ? 29.078 -32.303 -2.023  1.00 23.83 ?  141 ARG   B HG2  1 
ATOM   6440 H HG3  . ARG   B 1 141 ? 29.000 -30.918 -2.804  1.00 23.83 ?  141 ARG   B HG3  1 
ATOM   6441 H HD2  . ARG   B 1 141 ? 28.945 -33.281 -4.257  1.00 25.69 ?  141 ARG   B HD2  1 
ATOM   6442 H HD3  . ARG   B 1 141 ? 27.616 -32.778 -3.560  1.00 25.69 ?  141 ARG   B HD3  1 
ATOM   6443 H HE   . ARG   B 1 141 ? 28.033 -30.779 -4.857  1.00 25.72 ?  141 ARG   B HE   1 
ATOM   6444 H HH11 . ARG   B 1 141 ? 28.885 -33.737 -6.125  1.00 24.91 ?  141 ARG   B HH11 1 
ATOM   6445 H HH12 . ARG   B 1 141 ? 28.598 -33.370 -7.535  1.00 24.91 ?  141 ARG   B HH12 1 
ATOM   6446 H HH21 . ARG   B 1 141 ? 27.495 -30.317 -6.990  1.00 25.10 ?  141 ARG   B HH21 1 
ATOM   6447 H HH22 . ARG   B 1 141 ? 27.762 -31.316 -8.062  1.00 25.10 ?  141 ARG   B HH22 1 
ATOM   6448 N N    . VAL   B 1 142 ? 31.466 -29.104 -2.617  1.00 16.34 ?  142 VAL   B N    1 
ATOM   6449 C CA   . VAL   B 1 142 ? 31.144 -27.764 -2.135  1.00 15.49 ?  142 VAL   B CA   1 
ATOM   6450 C C    . VAL   B 1 142 ? 31.624 -26.711 -3.127  1.00 15.53 ?  142 VAL   B C    1 
ATOM   6451 O O    . VAL   B 1 142 ? 30.923 -25.728 -3.395  1.00 15.97 ?  142 VAL   B O    1 
ATOM   6452 C CB   . VAL   B 1 142 ? 31.698 -27.537 -0.715  1.00 16.22 ?  142 VAL   B CB   1 
ATOM   6453 C CG1  . VAL   B 1 142 ? 31.396 -26.113 -0.235  1.00 16.36 ?  142 VAL   B CG1  1 
ATOM   6454 C CG2  . VAL   B 1 142 ? 31.131 -28.568 0.247   1.00 17.44 ?  142 VAL   B CG2  1 
ATOM   6455 H H    . VAL   B 1 142 ? 32.004 -29.549 -2.113  1.00 19.63 ?  142 VAL   B H    1 
ATOM   6456 H HA   . VAL   B 1 142 ? 30.182 -27.683 -2.075  1.00 18.61 ?  142 VAL   B HA   1 
ATOM   6457 H HB   . VAL   B 1 142 ? 32.666 -27.646 -0.733  1.00 19.49 ?  142 VAL   B HB   1 
ATOM   6458 H HG11 . VAL   B 1 142 ? 31.604 -26.048 0.708   1.00 19.66 ?  142 VAL   B HG11 1 
ATOM   6459 H HG12 . VAL   B 1 142 ? 31.946 -25.487 -0.737  1.00 19.66 ?  142 VAL   B HG12 1 
ATOM   6460 H HG13 . VAL   B 1 142 ? 30.459 -25.925 -0.385  1.00 19.66 ?  142 VAL   B HG13 1 
ATOM   6461 H HG21 . VAL   B 1 142 ? 31.459 -28.382 1.141   1.00 20.94 ?  142 VAL   B HG21 1 
ATOM   6462 H HG22 . VAL   B 1 142 ? 30.166 -28.519 0.229   1.00 20.94 ?  142 VAL   B HG22 1 
ATOM   6463 H HG23 . VAL   B 1 142 ? 31.423 -29.454 -0.030  1.00 20.94 ?  142 VAL   B HG23 1 
ATOM   6464 N N    . CYS   B 1 143 ? 32.809 -26.910 -3.705  1.00 15.29 ?  143 CYS   B N    1 
ATOM   6465 C CA   . CYS   B 1 143 ? 33.303 -25.976 -4.714  1.00 15.08 ?  143 CYS   B CA   1 
ATOM   6466 C C    . CYS   B 1 143 ? 32.301 -25.836 -5.857  1.00 14.94 ?  143 CYS   B C    1 
ATOM   6467 O O    . CYS   B 1 143 ? 31.899 -24.727 -6.228  1.00 14.95 ?  143 CYS   B O    1 
ATOM   6468 C CB   . CYS   B 1 143 ? 34.662 -26.459 -5.235  1.00 15.29 ?  143 CYS   B CB   1 
ATOM   6469 S SG   . CYS   B 1 143 ? 35.405 -25.372 -6.486  1.00 15.06 ?  143 CYS   B SG   1 
ATOM   6470 H H    . CYS   B 1 143 ? 33.340 -27.563 -3.526  1.00 18.37 ?  143 CYS   B H    1 
ATOM   6471 H HA   . CYS   B 1 143 ? 33.432 -25.105 -4.309  1.00 18.12 ?  143 CYS   B HA   1 
ATOM   6472 H HB2  . CYS   B 1 143 ? 35.287 -26.522 -4.491  1.00 18.36 ?  143 CYS   B HB2  1 
ATOM   6473 H HB3  . CYS   B 1 143 ? 34.553 -27.334 -5.634  1.00 18.36 ?  143 CYS   B HB3  1 
ATOM   6474 H HG   . CYS   B 1 143 ? 36.486 -25.794 -6.794  1.00 18.09 ?  143 CYS   B HG   1 
ATOM   6475 N N    . VAL   B 1 144 ? 31.891 -26.962 -6.435  1.00 15.88 ?  144 VAL   B N    1 
ATOM   6476 C CA   . VAL   B 1 144 ? 30.994 -26.913 -7.583  1.00 16.57 ?  144 VAL   B CA   1 
ATOM   6477 C C    . VAL   B 1 144 ? 29.650 -26.295 -7.223  1.00 16.92 ?  144 VAL   B C    1 
ATOM   6478 O O    . VAL   B 1 144 ? 29.038 -25.597 -8.041  1.00 17.84 ?  144 VAL   B O    1 
ATOM   6479 C CB   . VAL   B 1 144 ? 30.839 -28.336 -8.138  1.00 18.99 ?  144 VAL   B CB   1 
ATOM   6480 C CG1  . VAL   B 1 144 ? 29.553 -28.485 -8.948  1.00 21.58 ?  144 VAL   B CG1  1 
ATOM   6481 C CG2  . VAL   B 1 144 ? 32.073 -28.737 -8.945  1.00 19.39 ?  144 VAL   B CG2  1 
ATOM   6482 H H    . VAL   B 1 144 ? 32.115 -27.754 -6.183  1.00 19.08 ?  144 VAL   B H    1 
ATOM   6483 H HA   . VAL   B 1 144 ? 31.394 -26.370 -8.275  1.00 19.91 ?  144 VAL   B HA   1 
ATOM   6484 H HB   . VAL   B 1 144 ? 30.778 -28.954 -7.392  1.00 22.82 ?  144 VAL   B HB   1 
ATOM   6485 H HG11 . VAL   B 1 144 ? 29.623 -29.287 -9.495  1.00 25.92 ?  144 VAL   B HG11 1 
ATOM   6486 H HG12 . VAL   B 1 144 ? 28.804 -28.571 -8.340  1.00 25.92 ?  144 VAL   B HG12 1 
ATOM   6487 H HG13 . VAL   B 1 144 ? 29.445 -27.711 -9.516  1.00 25.92 ?  144 VAL   B HG13 1 
ATOM   6488 H HG21 . VAL   B 1 144 ? 31.954 -29.640 -9.282  1.00 23.29 ?  144 VAL   B HG21 1 
ATOM   6489 H HG22 . VAL   B 1 144 ? 32.177 -28.120 -9.689  1.00 23.29 ?  144 VAL   B HG22 1 
ATOM   6490 H HG23 . VAL   B 1 144 ? 32.853 -28.697 -8.372  1.00 23.29 ?  144 VAL   B HG23 1 
ATOM   6491 N N    . ASP   B 1 145 ? 29.178 -26.524 -6.004  1.00 16.57 ?  145 ASP   B N    1 
ATOM   6492 C CA   . ASP   B 1 145 ? 27.871 -26.045 -5.578  1.00 17.27 ?  145 ASP   B CA   1 
ATOM   6493 C C    . ASP   B 1 145 ? 27.902 -24.626 -5.037  1.00 16.87 ?  145 ASP   B C    1 
ATOM   6494 O O    . ASP   B 1 145 ? 26.841 -24.081 -4.700  1.00 18.98 ?  145 ASP   B O    1 
ATOM   6495 C CB   . ASP   B 1 145 ? 27.294 -26.953 -4.487  1.00 18.87 ?  145 ASP   B CB   1 
ATOM   6496 C CG   . ASP   B 1 145 ? 26.929 -28.335 -4.988  1.00 20.76 ?  145 ASP   B CG   1 
ATOM   6497 O OD1  . ASP   B 1 145 ? 26.818 -28.537 -6.216  1.00 21.34 ?  145 ASP   B OD1  1 
ATOM   6498 O OD2  . ASP   B 1 145 ? 26.744 -29.220 -4.131  1.00 22.84 -1 145 ASP   B OD2  1 
ATOM   6499 H H    . ASP   B 1 145 ? 29.609 -26.945 -5.393  1.00 19.90 ?  145 ASP   B H    1 
ATOM   6500 H HA   . ASP   B 1 145 ? 27.270 -26.044 -6.335  1.00 20.74 ?  145 ASP   B HA   1 
ATOM   6501 H HB2  . ASP   B 1 145 ? 27.951 -27.062 -3.791  1.00 22.67 ?  145 ASP   B HB2  1 
ATOM   6502 H HB3  . ASP   B 1 145 ? 26.492 -26.535 -4.131  1.00 22.67 ?  145 ASP   B HB3  1 
ATOM   6503 N N    . THR   B 1 146 ? 29.082 -24.018 -4.939  1.00 15.46 ?  146 THR   B N    1 
ATOM   6504 C CA   . THR   B 1 146 ? 29.217 -22.694 -4.339  1.00 15.29 ?  146 THR   B CA   1 
ATOM   6505 C C    . THR   B 1 146 ? 29.844 -21.667 -5.264  1.00 15.03 ?  146 THR   B C    1 
ATOM   6506 O O    . THR   B 1 146 ? 29.391 -20.504 -5.309  1.00 15.31 ?  146 THR   B O    1 
ATOM   6507 C CB   . THR   B 1 146 ? 30.054 -22.792 -3.057  1.00 15.66 ?  146 THR   B CB   1 
ATOM   6508 O OG1  . THR   B 1 146 ? 29.466 -23.763 -2.180  1.00 15.86 ?  146 THR   B OG1  1 
ATOM   6509 C CG2  . THR   B 1 146 ? 30.146 -21.445 -2.361  1.00 16.02 ?  146 THR   B CG2  1 
ATOM   6510 H H    . THR   B 1 146 ? 29.833 -24.343 -5.223  1.00 18.58 ?  146 THR   B H    1 
ATOM   6511 H HA   . THR   B 1 146 ? 28.342 -22.364 -4.095  1.00 18.37 ?  146 THR   B HA   1 
ATOM   6512 H HB   . THR   B 1 146 ? 30.956 -23.063 -3.283  1.00 18.81 ?  146 THR   B HB   1 
ATOM   6513 H HG1  . THR   B 1 146 ? 29.485 -24.522 -2.537  1.00 19.05 ?  146 THR   B HG1  1 
ATOM   6514 H HG21 . THR   B 1 146 ? 30.477 -21.557 -1.457  1.00 19.25 ?  146 THR   B HG21 1 
ATOM   6515 H HG22 . THR   B 1 146 ? 30.760 -20.860 -2.844  1.00 19.25 ?  146 THR   B HG22 1 
ATOM   6516 H HG23 . THR   B 1 146 ? 29.275 -21.024 -2.329  1.00 19.25 ?  146 THR   B HG23 1 
ATOM   6517 N N    . VAL   B 1 147 ? 30.916 -22.043 -5.960  1.00 14.75 ?  147 VAL   B N    1 
ATOM   6518 C CA   . VAL   B 1 147 ? 31.638 -21.107 -6.808  1.00 14.68 ?  147 VAL   B CA   1 
ATOM   6519 C C    . VAL   B 1 147 ? 30.901 -20.972 -8.128  1.00 14.75 ?  147 VAL   B C    1 
ATOM   6520 O O    . VAL   B 1 147 ? 30.523 -21.974 -8.752  1.00 15.69 ?  147 VAL   B O    1 
ATOM   6521 C CB   . VAL   B 1 147 ? 33.089 -21.570 -7.013  1.00 14.53 ?  147 VAL   B CB   1 
ATOM   6522 C CG1  . VAL   B 1 147 ? 33.841 -20.536 -7.836  1.00 13.90 ?  147 VAL   B CG1  1 
ATOM   6523 C CG2  . VAL   B 1 147 ? 33.773 -21.767 -5.669  1.00 14.34 ?  147 VAL   B CG2  1 
ATOM   6524 H H    . VAL   B 1 147 ? 31.240 -22.843 -5.962  1.00 17.73 ?  147 VAL   B H    1 
ATOM   6525 H HA   . VAL   B 1 147 ? 31.655 -20.240 -6.380  1.00 17.64 ?  147 VAL   B HA   1 
ATOM   6526 H HB   . VAL   B 1 147 ? 33.100 -22.412 -7.496  1.00 17.46 ?  147 VAL   B HB   1 
ATOM   6527 H HG11 . VAL   B 1 147 ? 34.785 -20.747 -7.824  1.00 16.70 ?  147 VAL   B HG11 1 
ATOM   6528 H HG12 . VAL   B 1 147 ? 33.509 -20.548 -8.748  1.00 16.70 ?  147 VAL   B HG12 1 
ATOM   6529 H HG13 . VAL   B 1 147 ? 33.695 -19.656 -7.445  1.00 16.70 ?  147 VAL   B HG13 1 
ATOM   6530 H HG21 . VAL   B 1 147 ? 34.710 -21.959 -5.816  1.00 17.23 ?  147 VAL   B HG21 1 
ATOM   6531 H HG22 . VAL   B 1 147 ? 33.678 -20.954 -5.147  1.00 17.23 ?  147 VAL   B HG22 1 
ATOM   6532 H HG23 . VAL   B 1 147 ? 33.350 -22.507 -5.206  1.00 17.23 ?  147 VAL   B HG23 1 
ATOM   6533 N N    . ARG   B 1 148 ? 30.699 -19.721 -8.553  1.00 14.51 ?  148 ARG   B N    1 
ATOM   6534 C CA   . ARG   B 1 148 ? 30.074 -19.402 -9.827  1.00 14.83 ?  148 ARG   B CA   1 
ATOM   6535 C C    . ARG   B 1 148 ? 31.029 -18.729 -10.801 1.00 14.43 ?  148 ARG   B C    1 
ATOM   6536 O O    . ARG   B 1 148 ? 30.745 -18.704 -12.001 1.00 16.35 ?  148 ARG   B O    1 
ATOM   6537 C CB   . ARG   B 1 148 ? 28.833 -18.518 -9.612  1.00 15.20 ?  148 ARG   B CB   1 
ATOM   6538 C CG   . ARG   B 1 148 ? 27.758 -19.228 -8.803  1.00 15.80 ?  148 ARG   B CG   1 
ATOM   6539 C CD   . ARG   B 1 148 ? 26.551 -18.340 -8.481  1.00 16.69 ?  148 ARG   B CD   1 
ATOM   6540 N NE   . ARG   B 1 148 ? 26.935 -17.138 -7.750  1.00 17.04 ?  148 ARG   B NE   1 
ATOM   6541 C CZ   . ARG   B 1 148 ? 27.245 -17.105 -6.459  1.00 16.33 ?  148 ARG   B CZ   1 
ATOM   6542 N NH1  . ARG   B 1 148 ? 27.183 -18.191 -5.699  1.00 15.92 ?  148 ARG   B NH1  1 
ATOM   6543 N NH2  . ARG   B 1 148 ? 27.645 -15.957 -5.918  1.00 16.33 ?  148 ARG   B NH2  1 
ATOM   6544 H H    . ARG   B 1 148 ? 30.926 -19.018 -8.099  1.00 17.43 ?  148 ARG   B H    1 
ATOM   6545 H HA   . ARG   B 1 148 ? 29.775 -20.223 -10.236 1.00 17.82 ?  148 ARG   B HA   1 
ATOM   6546 H HB2  . ARG   B 1 148 ? 29.089 -17.714 -9.130  1.00 18.27 ?  148 ARG   B HB2  1 
ATOM   6547 H HB3  . ARG   B 1 148 ? 28.455 -18.282 -10.474 1.00 18.27 ?  148 ARG   B HB3  1 
ATOM   6548 H HG2  . ARG   B 1 148 ? 27.438 -19.993 -9.311  1.00 18.99 ?  148 ARG   B HG2  1 
ATOM   6549 H HG3  . ARG   B 1 148 ? 28.140 -19.529 -7.965  1.00 18.99 ?  148 ARG   B HG3  1 
ATOM   6550 H HD2  . ARG   B 1 148 ? 26.129 -18.069 -9.309  1.00 20.05 ?  148 ARG   B HD2  1 
ATOM   6551 H HD3  . ARG   B 1 148 ? 25.926 -18.842 -7.935  1.00 20.05 ?  148 ARG   B HD3  1 
ATOM   6552 H HE   . ARG   B 1 148 ? 26.973 -16.401 -8.186  1.00 20.47 ?  148 ARG   B HE   1 
ATOM   6553 H HH11 . ARG   B 1 148 ? 26.928 -18.944 -6.037  1.00 19.12 ?  148 ARG   B HH11 1 
ATOM   6554 H HH12 . ARG   B 1 148 ? 27.384 -18.148 -4.864  1.00 19.12 ?  148 ARG   B HH12 1 
ATOM   6555 H HH21 . ARG   B 1 148 ? 27.691 -15.248 -6.400  1.00 19.61 ?  148 ARG   B HH21 1 
ATOM   6556 H HH22 . ARG   B 1 148 ? 27.845 -15.920 -5.082  1.00 19.61 ?  148 ARG   B HH22 1 
ATOM   6557 N N    . THR   B 1 149 ? 32.141 -18.179 -10.313 1.00 14.60 ?  149 THR   B N    1 
ATOM   6558 C CA   . THR   B 1 149 ? 33.181 -17.622 -11.165 1.00 14.64 ?  149 THR   B CA   1 
ATOM   6559 C C    . THR   B 1 149 ? 34.057 -18.764 -11.683 1.00 14.27 ?  149 THR   B C    1 
ATOM   6560 O O    . THR   B 1 149 ? 33.863 -19.937 -11.341 1.00 14.82 ?  149 THR   B O    1 
ATOM   6561 C CB   . THR   B 1 149 ? 33.961 -16.573 -10.381 1.00 15.31 ?  149 THR   B CB   1 
ATOM   6562 O OG1  . THR   B 1 149 ? 34.416 -17.173 -9.164  1.00 15.08 ?  149 THR   B OG1  1 
ATOM   6563 C CG2  . THR   B 1 149 ? 33.085 -15.359 -10.091 1.00 15.88 ?  149 THR   B CG2  1 
ATOM   6564 H H    . THR   B 1 149 ? 32.312 -18.113 -9.468  1.00 17.54 ?  149 THR   B H    1 
ATOM   6565 H HA   . THR   B 1 149 ? 32.767 -17.183 -11.922 1.00 17.59 ?  149 THR   B HA   1 
ATOM   6566 H HB   . THR   B 1 149 ? 34.727 -16.291 -10.894 1.00 18.39 ?  149 THR   B HB   1 
ATOM   6567 H HG1  . THR   B 1 149 ? 34.840 -16.603 -8.698  1.00 18.11 ?  149 THR   B HG1  1 
ATOM   6568 H HG21 . THR   B 1 149 ? 33.596 -14.693 -9.600  1.00 19.08 ?  149 THR   B HG21 1 
ATOM   6569 H HG22 . THR   B 1 149 ? 32.780 -14.967 -10.924 1.00 19.08 ?  149 THR   B HG22 1 
ATOM   6570 H HG23 . THR   B 1 149 ? 32.317 -15.617 -9.561  1.00 19.08 ?  149 THR   B HG23 1 
ATOM   6571 N N    . ASN   B 1 150 ? 35.025 -18.442 -12.533 1.00 14.24 ?  150 ASN   B N    1 
ATOM   6572 C CA   . ASN   B 1 150 ? 35.788 -19.473 -13.230 1.00 14.57 ?  150 ASN   B CA   1 
ATOM   6573 C C    . ASN   B 1 150 ? 36.954 -19.921 -12.354 1.00 14.23 ?  150 ASN   B C    1 
ATOM   6574 O O    . ASN   B 1 150 ? 37.891 -19.154 -12.110 1.00 15.05 ?  150 ASN   B O    1 
ATOM   6575 C CB   . ASN   B 1 150 ? 36.256 -18.960 -14.585 1.00 16.54 ?  150 ASN   B CB   1 
ATOM   6576 C CG   . ASN   B 1 150 ? 35.108 -18.733 -15.528 1.00 19.70 ?  150 ASN   B CG   1 
ATOM   6577 O OD1  . ASN   B 1 150 ? 34.197 -19.546 -15.597 1.00 20.76 ?  150 ASN   B OD1  1 
ATOM   6578 N ND2  . ASN   B 1 150 ? 35.123 -17.616 -16.236 1.00 21.62 ?  150 ASN   B ND2  1 
ATOM   6579 H H    . ASN   B 1 150 ? 35.260 -17.637 -12.719 1.00 17.11 ?  150 ASN   B H    1 
ATOM   6580 H HA   . ASN   B 1 150 ? 35.208 -20.240 -13.381 1.00 17.51 ?  150 ASN   B HA   1 
ATOM   6581 H HB2  . ASN   B 1 150 ? 36.717 -18.117 -14.463 1.00 19.87 ?  150 ASN   B HB2  1 
ATOM   6582 H HB3  . ASN   B 1 150 ? 36.850 -19.615 -14.982 1.00 19.87 ?  150 ASN   B HB3  1 
ATOM   6583 H HD21 . ASN   B 1 150 ? 34.487 -17.443 -16.793 1.00 25.97 ?  150 ASN   B HD21 1 
ATOM   6584 H HD22 . ASN   B 1 150 ? 35.777 -17.062 -16.152 1.00 25.97 ?  150 ASN   B HD22 1 
ATOM   6585 N N    . VAL   B 1 151 ? 36.900 -21.163 -11.881 1.00 13.96 ?  151 VAL   B N    1 
ATOM   6586 C CA   . VAL   B 1 151 ? 37.918 -21.697 -10.986 1.00 14.18 ?  151 VAL   B CA   1 
ATOM   6587 C C    . VAL   B 1 151 ? 38.619 -22.872 -11.656 1.00 14.16 ?  151 VAL   B C    1 
ATOM   6588 O O    . VAL   B 1 151 ? 37.974 -23.799 -12.170 1.00 15.24 ?  151 VAL   B O    1 
ATOM   6589 C CB   . VAL   B 1 151 ? 37.362 -22.041 -9.586  1.00 15.13 ?  151 VAL   B CB   1 
ATOM   6590 C CG1  . VAL   B 1 151 ? 36.223 -23.054 -9.659  1.00 16.23 ?  151 VAL   B CG1  1 
ATOM   6591 C CG2  . VAL   B 1 151 ? 38.482 -22.513 -8.662  1.00 14.73 ?  151 VAL   B CG2  1 
ATOM   6592 H H    . VAL   B 1 151 ? 36.270 -21.725 -12.070 1.00 16.78 ?  151 VAL   B H    1 
ATOM   6593 H HA   . VAL   B 1 151 ? 38.583 -21.002 -10.855 1.00 17.03 ?  151 VAL   B HA   1 
ATOM   6594 H HB   . VAL   B 1 151 ? 36.996 -21.226 -9.199  1.00 18.17 ?  151 VAL   B HB   1 
ATOM   6595 H HG11 . VAL   B 1 151 ? 35.901 -23.232 -8.761  1.00 19.50 ?  151 VAL   B HG11 1 
ATOM   6596 H HG12 . VAL   B 1 151 ? 35.507 -22.691 -10.202 1.00 19.50 ?  151 VAL   B HG12 1 
ATOM   6597 H HG13 . VAL   B 1 151 ? 36.557 -23.875 -10.057 1.00 19.50 ?  151 VAL   B HG13 1 
ATOM   6598 H HG21 . VAL   B 1 151 ? 38.127 -22.601 -7.762  1.00 17.70 ?  151 VAL   B HG21 1 
ATOM   6599 H HG22 . VAL   B 1 151 ? 38.811 -23.366 -8.974  1.00 17.70 ?  151 VAL   B HG22 1 
ATOM   6600 H HG23 . VAL   B 1 151 ? 39.196 -21.855 -8.669  1.00 17.70 ?  151 VAL   B HG23 1 
ATOM   6601 N N    . TYR   B 1 152 ? 39.946 -22.789 -11.675 1.00 13.38 ?  152 TYR   B N    1 
ATOM   6602 C CA   . TYR   B 1 152 ? 40.843 -23.779 -12.253 1.00 13.78 ?  152 TYR   B CA   1 
ATOM   6603 C C    . TYR   B 1 152 ? 41.564 -24.456 -11.093 1.00 13.52 ?  152 TYR   B C    1 
ATOM   6604 O O    . TYR   B 1 152 ? 42.426 -23.844 -10.453 1.00 13.51 ?  152 TYR   B O    1 
ATOM   6605 C CB   . TYR   B 1 152 ? 41.821 -23.082 -13.201 1.00 14.63 ?  152 TYR   B CB   1 
ATOM   6606 C CG   . TYR   B 1 152 ? 41.146 -22.610 -14.469 1.00 15.28 ?  152 TYR   B CG   1 
ATOM   6607 C CD1  . TYR   B 1 152 ? 40.511 -21.370 -14.541 1.00 15.80 ?  152 TYR   B CD1  1 
ATOM   6608 C CD2  . TYR   B 1 152 ? 41.114 -23.425 -15.584 1.00 16.52 ?  152 TYR   B CD2  1 
ATOM   6609 C CE1  . TYR   B 1 152 ? 39.875 -20.964 -15.700 1.00 17.50 ?  152 TYR   B CE1  1 
ATOM   6610 C CE2  . TYR   B 1 152 ? 40.481 -23.035 -16.741 1.00 17.31 ?  152 TYR   B CE2  1 
ATOM   6611 C CZ   . TYR   B 1 152 ? 39.867 -21.798 -16.798 1.00 17.22 ?  152 TYR   B CZ   1 
ATOM   6612 O OH   . TYR   B 1 152 ? 39.239 -21.409 -17.956 1.00 20.33 ?  152 TYR   B OH   1 
ATOM   6613 H H    . TYR   B 1 152 ? 40.379 -22.118 -11.329 1.00 16.07 ?  152 TYR   B H    1 
ATOM   6614 H HA   . TYR   B 1 152 ? 40.330 -24.437 -12.742 1.00 16.55 ?  152 TYR   B HA   1 
ATOM   6615 H HB2  . TYR   B 1 152 ? 42.199 -22.308 -12.750 1.00 17.57 ?  152 TYR   B HB2  1 
ATOM   6616 H HB3  . TYR   B 1 152 ? 42.523 -23.703 -13.440 1.00 17.57 ?  152 TYR   B HB3  1 
ATOM   6617 H HD1  . TYR   B 1 152 ? 40.519 -20.808 -13.799 1.00 18.99 ?  152 TYR   B HD1  1 
ATOM   6618 H HD2  . TYR   B 1 152 ? 41.519 -24.263 -15.548 1.00 19.85 ?  152 TYR   B HD2  1 
ATOM   6619 H HE1  . TYR   B 1 152 ? 39.463 -20.130 -15.746 1.00 21.02 ?  152 TYR   B HE1  1 
ATOM   6620 H HE2  . TYR   B 1 152 ? 40.474 -23.597 -17.485 1.00 20.79 ?  152 TYR   B HE2  1 
ATOM   6621 H HH   . TYR   B 1 152 ? 38.911 -20.637 -17.859 1.00 24.42 ?  152 TYR   B HH   1 
ATOM   6622 N N    . LEU   B 1 153 ? 41.189 -25.708 -10.815 1.00 13.47 ?  153 LEU   B N    1 
ATOM   6623 C CA   . LEU   B 1 153 ? 41.702 -26.458 -9.680  1.00 13.35 ?  153 LEU   B CA   1 
ATOM   6624 C C    . LEU   B 1 153 ? 42.926 -27.261 -10.087 1.00 13.22 ?  153 LEU   B C    1 
ATOM   6625 O O    . LEU   B 1 153 ? 42.901 -27.985 -11.083 1.00 14.17 ?  153 LEU   B O    1 
ATOM   6626 C CB   . LEU   B 1 153 ? 40.626 -27.417 -9.168  1.00 13.17 ?  153 LEU   B CB   1 
ATOM   6627 C CG   . LEU   B 1 153 ? 39.380 -26.744 -8.596  1.00 14.30 ?  153 LEU   B CG   1 
ATOM   6628 C CD1  . LEU   B 1 153 ? 38.256 -27.764 -8.451  1.00 15.12 ?  153 LEU   B CD1  1 
ATOM   6629 C CD2  . LEU   B 1 153 ? 39.692 -26.090 -7.254  1.00 14.83 ?  153 LEU   B CD2  1 
ATOM   6630 H H    . LEU   B 1 153 ? 40.609 -26.147 -11.281 1.00 16.19 ?  153 LEU   B H    1 
ATOM   6631 H HA   . LEU   B 1 153 ? 41.937 -25.847 -8.967  1.00 16.04 ?  153 LEU   B HA   1 
ATOM   6632 H HB2  . LEU   B 1 153 ? 40.339 -27.985 -9.896  1.00 15.83 ?  153 LEU   B HB2  1 
ATOM   6633 H HB3  . LEU   B 1 153 ? 41.008 -27.962 -8.459  1.00 15.83 ?  153 LEU   B HB3  1 
ATOM   6634 H HG   . LEU   B 1 153 ? 39.082 -26.044 -9.204  1.00 17.18 ?  153 LEU   B HG   1 
ATOM   6635 H HD11 . LEU   B 1 153 ? 37.455 -27.304 -8.143  1.00 18.17 ?  153 LEU   B HD11 1 
ATOM   6636 H HD12 . LEU   B 1 153 ? 38.093 -28.169 -9.311  1.00 18.17 ?  153 LEU   B HD12 1 
ATOM   6637 H HD13 . LEU   B 1 153 ? 38.523 -28.430 -7.805  1.00 18.17 ?  153 LEU   B HD13 1 
ATOM   6638 H HD21 . LEU   B 1 153 ? 38.881 -25.717 -6.880  1.00 17.82 ?  153 LEU   B HD21 1 
ATOM   6639 H HD22 . LEU   B 1 153 ? 40.054 -26.764 -6.654  1.00 17.82 ?  153 LEU   B HD22 1 
ATOM   6640 H HD23 . LEU   B 1 153 ? 40.350 -25.387 -7.388  1.00 17.82 ?  153 LEU   B HD23 1 
ATOM   6641 N N    . ALA   B 1 154 ? 43.986 -27.144 -9.296  1.00 13.39 ?  154 ALA   B N    1 
ATOM   6642 C CA   . ALA   B 1 154 ? 45.217 -27.902 -9.485  1.00 14.88 ?  154 ALA   B CA   1 
ATOM   6643 C C    . ALA   B 1 154 ? 45.292 -28.976 -8.409  1.00 15.81 ?  154 ALA   B C    1 
ATOM   6644 O O    . ALA   B 1 154 ? 45.251 -28.672 -7.210  1.00 17.48 ?  154 ALA   B O    1 
ATOM   6645 C CB   . ALA   B 1 154 ? 46.432 -26.978 -9.432  1.00 15.54 ?  154 ALA   B CB   1 
ATOM   6646 H H    . ALA   B 1 154 ? 44.011 -26.607 -8.622  1.00 16.10 ?  154 ALA   B H    1 
ATOM   6647 H HA   . ALA   B 1 154 ? 45.197 -28.330 -10.353 1.00 17.88 ?  154 ALA   B HA   1 
ATOM   6648 H HB1  . ALA   B 1 154 ? 47.235 -27.502 -9.559  1.00 18.68 ?  154 ALA   B HB1  1 
ATOM   6649 H HB2  . ALA   B 1 154 ? 46.357 -26.311 -10.137 1.00 18.68 ?  154 ALA   B HB2  1 
ATOM   6650 H HB3  . ALA   B 1 154 ? 46.458 -26.535 -8.567  1.00 18.68 ?  154 ALA   B HB3  1 
ATOM   6651 N N    . VAL   B 1 155 ? 45.382 -30.228 -8.839  1.00 14.89 ?  155 VAL   B N    1 
ATOM   6652 C CA   . VAL   B 1 155 ? 45.489 -31.372 -7.941  1.00 15.51 ?  155 VAL   B CA   1 
ATOM   6653 C C    . VAL   B 1 155 ? 46.822 -32.047 -8.218  1.00 14.85 ?  155 VAL   B C    1 
ATOM   6654 O O    . VAL   B 1 155 ? 47.049 -32.548 -9.326  1.00 16.57 ?  155 VAL   B O    1 
ATOM   6655 C CB   . VAL   B 1 155 ? 44.326 -32.361 -8.119  1.00 16.60 ?  155 VAL   B CB   1 
ATOM   6656 C CG1  . VAL   B 1 155 ? 44.510 -33.554 -7.192  1.00 16.81 ?  155 VAL   B CG1  1 
ATOM   6657 C CG2  . VAL   B 1 155 ? 42.996 -31.658 -7.841  1.00 17.43 ?  155 VAL   B CG2  1 
ATOM   6658 H H    . VAL   B 1 155 ? 45.399 -30.450 -9.673  1.00 17.89 ?  155 VAL   B H    1 
ATOM   6659 H HA   . VAL   B 1 155 ? 45.485 -31.066 -7.024  1.00 18.64 ?  155 VAL   B HA   1 
ATOM   6660 H HB   . VAL   B 1 155 ? 44.310 -32.683 -9.035  1.00 19.94 ?  155 VAL   B HB   1 
ATOM   6661 H HG11 . VAL   B 1 155 ? 43.679 -34.054 -7.150  1.00 20.20 ?  155 VAL   B HG11 1 
ATOM   6662 H HG12 . VAL   B 1 155 ? 45.217 -34.120 -7.535  1.00 20.20 ?  155 VAL   B HG12 1 
ATOM   6663 H HG13 . VAL   B 1 155 ? 44.742 -33.231 -6.306  1.00 20.20 ?  155 VAL   B HG13 1 
ATOM   6664 H HG21 . VAL   B 1 155 ? 42.277 -32.310 -7.904  1.00 20.94 ?  155 VAL   B HG21 1 
ATOM   6665 H HG22 . VAL   B 1 155 ? 43.021 -31.283 -6.947  1.00 20.94 ?  155 VAL   B HG22 1 
ATOM   6666 H HG23 . VAL   B 1 155 ? 42.864 -30.956 -8.494  1.00 20.94 ?  155 VAL   B HG23 1 
ATOM   6667 N N    . PHE   B 1 156 ? 47.690 -32.082 -7.205  1.00 15.72 ?  156 PHE   B N    1 
ATOM   6668 C CA   . PHE   B 1 156 ? 49.063 -32.551 -7.410  1.00 16.72 ?  156 PHE   B CA   1 
ATOM   6669 C C    . PHE   B 1 156 ? 49.143 -34.052 -7.681  1.00 18.09 ?  156 PHE   B C    1 
ATOM   6670 O O    . PHE   B 1 156 ? 49.851 -34.493 -8.596  1.00 19.60 ?  156 PHE   B O    1 
ATOM   6671 C CB   . PHE   B 1 156 ? 49.907 -32.190 -6.190  1.00 16.49 ?  156 PHE   B CB   1 
ATOM   6672 C CG   . PHE   B 1 156 ? 51.332 -32.648 -6.277  1.00 17.44 ?  156 PHE   B CG   1 
ATOM   6673 C CD1  . PHE   B 1 156 ? 52.186 -32.131 -7.236  1.00 19.19 ?  156 PHE   B CD1  1 
ATOM   6674 C CD2  . PHE   B 1 156 ? 51.826 -33.578 -5.383  1.00 17.83 ?  156 PHE   B CD2  1 
ATOM   6675 C CE1  . PHE   B 1 156 ? 53.510 -32.549 -7.310  1.00 19.70 ?  156 PHE   B CE1  1 
ATOM   6676 C CE2  . PHE   B 1 156 ? 53.144 -33.994 -5.450  1.00 19.07 ?  156 PHE   B CE2  1 
ATOM   6677 C CZ   . PHE   B 1 156 ? 53.983 -33.478 -6.416  1.00 19.49 ?  156 PHE   B CZ   1 
ATOM   6678 H H    . PHE   B 1 156 ? 47.512 -31.846 -6.400  1.00 18.89 ?  156 PHE   B H    1 
ATOM   6679 H HA   . PHE   B 1 156 ? 49.437 -32.088 -8.176  1.00 20.09 ?  156 PHE   B HA   1 
ATOM   6680 H HB2  . PHE   B 1 156 ? 49.913 -31.227 -6.090  1.00 19.81 ?  156 PHE   B HB2  1 
ATOM   6681 H HB3  . PHE   B 1 156 ? 49.516 -32.602 -5.405  1.00 19.81 ?  156 PHE   B HB3  1 
ATOM   6682 H HD1  . PHE   B 1 156 ? 51.873 -31.499 -7.846  1.00 23.05 ?  156 PHE   B HD1  1 
ATOM   6683 H HD2  . PHE   B 1 156 ? 51.262 -33.930 -4.733  1.00 21.42 ?  156 PHE   B HD2  1 
ATOM   6684 H HE1  . PHE   B 1 156 ? 54.080 -32.197 -7.963  1.00 23.66 ?  156 PHE   B HE1  1 
ATOM   6685 H HE2  . PHE   B 1 156 ? 53.467 -34.629 -4.848  1.00 22.91 ?  156 PHE   B HE2  1 
ATOM   6686 H HZ   . PHE   B 1 156 ? 54.872 -33.762 -6.464  1.00 23.41 ?  156 PHE   B HZ   1 
ATOM   6687 N N    . ASP   B 1 157 ? 48.487 -34.860 -6.861  1.00 18.62 ?  157 ASP   B N    1 
ATOM   6688 C CA   . ASP   B 1 157 ? 48.628 -36.311 -6.950  1.00 19.92 ?  157 ASP   B CA   1 
ATOM   6689 C C    . ASP   B 1 157 ? 47.714 -36.867 -8.038  1.00 20.09 ?  157 ASP   B C    1 
ATOM   6690 O O    . ASP   B 1 157 ? 46.488 -36.740 -7.945  1.00 19.02 ?  157 ASP   B O    1 
ATOM   6691 C CB   . ASP   B 1 157 ? 48.261 -36.920 -5.602  1.00 21.26 ?  157 ASP   B CB   1 
ATOM   6692 C CG   . ASP   B 1 157 ? 48.414 -38.425 -5.577  1.00 23.39 ?  157 ASP   B CG   1 
ATOM   6693 O OD1  . ASP   B 1 157 ? 48.742 -39.031 -6.624  1.00 23.96 ?  157 ASP   B OD1  1 
ATOM   6694 O OD2  . ASP   B 1 157 ? 48.209 -38.999 -4.494  1.00 25.56 -1 157 ASP   B OD2  1 
ATOM   6695 H H    . ASP   B 1 157 ? 47.962 -34.596 -6.242  1.00 22.36 ?  157 ASP   B H    1 
ATOM   6696 H HA   . ASP   B 1 157 ? 49.548 -36.546 -7.159  1.00 23.93 ?  157 ASP   B HA   1 
ATOM   6697 H HB2  . ASP   B 1 157 ? 48.823 -36.529 -4.915  1.00 25.53 ?  157 ASP   B HB2  1 
ATOM   6698 H HB3  . ASP   B 1 157 ? 47.328 -36.719 -5.412  1.00 25.53 ?  157 ASP   B HB3  1 
ATOM   6699 N N    A LYS   B 1 158 ? 48.312 -37.501 -9.056  0.56 20.73 ?  158 LYS   B N    1 
ATOM   6700 N N    B LYS   B 1 158 ? 48.310 -37.513 -9.048  0.44 20.63 ?  158 LYS   B N    1 
ATOM   6701 C CA   A LYS   B 1 158 ? 47.538 -38.100 -10.144 0.56 21.59 ?  158 LYS   B CA   1 
ATOM   6702 C CA   B LYS   B 1 158 ? 47.530 -38.092 -10.142 0.44 21.46 ?  158 LYS   B CA   1 
ATOM   6703 C C    A LYS   B 1 158 ? 46.473 -39.061 -9.622  0.56 21.72 ?  158 LYS   B C    1 
ATOM   6704 C C    B LYS   B 1 158 ? 46.473 -39.063 -9.624  0.44 21.59 ?  158 LYS   B C    1 
ATOM   6705 O O    A LYS   B 1 158 ? 45.367 -39.139 -10.173 0.56 21.94 ?  158 LYS   B O    1 
ATOM   6706 O O    B LYS   B 1 158 ? 45.369 -39.144 -10.178 0.44 21.69 ?  158 LYS   B O    1 
ATOM   6707 C CB   A LYS   B 1 158 ? 48.488 -38.822 -11.109 0.56 23.31 ?  158 LYS   B CB   1 
ATOM   6708 C CB   B LYS   B 1 158 ? 48.472 -38.789 -11.130 0.44 22.94 ?  158 LYS   B CB   1 
ATOM   6709 C CG   A LYS   B 1 158 ? 47.814 -39.750 -12.113 0.56 25.22 ?  158 LYS   B CG   1 
ATOM   6710 C CG   B LYS   B 1 158 ? 47.792 -39.686 -12.159 0.44 24.58 ?  158 LYS   B CG   1 
ATOM   6711 C CD   A LYS   B 1 158 ? 46.940 -38.994 -13.094 0.56 26.97 ?  158 LYS   B CD   1 
ATOM   6712 C CD   B LYS   B 1 158 ? 46.908 -38.903 -13.113 0.44 26.21 ?  158 LYS   B CD   1 
ATOM   6713 C CE   A LYS   B 1 158 ? 46.347 -39.938 -14.129 0.56 28.07 ?  158 LYS   B CE   1 
ATOM   6714 C CE   B LYS   B 1 158 ? 46.329 -39.814 -14.187 0.44 27.31 ?  158 LYS   B CE   1 
ATOM   6715 N NZ   A LYS   B 1 158 ? 45.285 -39.286 -14.943 0.56 28.24 ?  158 LYS   B NZ   1 
ATOM   6716 N NZ   B LYS   B 1 158 ? 45.279 -39.138 -15.001 0.44 27.67 ?  158 LYS   B NZ   1 
ATOM   6717 H H    A LYS   B 1 158 ? 49.167 -37.592 -9.137  0.56 24.90 ?  158 LYS   B H    1 
ATOM   6718 H H    B LYS   B 1 158 ? 49.162 -37.631 -9.118  0.44 24.78 ?  158 LYS   B H    1 
ATOM   6719 H HA   A LYS   B 1 158 ? 47.098 -37.393 -10.641 0.56 25.93 ?  158 LYS   B HA   1 
ATOM   6720 H HA   B LYS   B 1 158 ? 47.082 -37.376 -10.620 0.44 25.77 ?  158 LYS   B HA   1 
ATOM   6721 H HB2  A LYS   B 1 158 ? 48.982 -38.155 -11.619 0.56 27.99 ?  158 LYS   B HB2  1 
ATOM   6722 H HB2  B LYS   B 1 158 ? 48.966 -38.110 -11.623 0.44 27.55 ?  158 LYS   B HB2  1 
ATOM   6723 H HB3  A LYS   B 1 158 ? 49.113 -39.354 -10.592 0.56 27.99 ?  158 LYS   B HB3  1 
ATOM   6724 H HB3  B LYS   B 1 158 ? 49.096 -39.338 -10.630 0.44 27.55 ?  158 LYS   B HB3  1 
ATOM   6725 H HG2  A LYS   B 1 158 ? 48.502 -40.208 -12.621 0.56 30.28 ?  158 LYS   B HG2  1 
ATOM   6726 H HG2  B LYS   B 1 158 ? 48.476 -40.129 -12.684 0.44 29.52 ?  158 LYS   B HG2  1 
ATOM   6727 H HG3  A LYS   B 1 158 ? 47.266 -40.402 -11.648 0.56 30.28 ?  158 LYS   B HG3  1 
ATOM   6728 H HG3  B LYS   B 1 158 ? 47.248 -40.351 -11.708 0.44 29.52 ?  158 LYS   B HG3  1 
ATOM   6729 H HD2  A LYS   B 1 158 ? 46.212 -38.566 -12.617 0.56 32.39 ?  158 LYS   B HD2  1 
ATOM   6730 H HD2  B LYS   B 1 158 ? 46.174 -38.505 -12.620 0.44 31.47 ?  158 LYS   B HD2  1 
ATOM   6731 H HD3  A LYS   B 1 158 ? 47.475 -38.330 -13.558 0.56 32.39 ?  158 LYS   B HD3  1 
ATOM   6732 H HD3  B LYS   B 1 158 ? 47.436 -38.215 -13.548 0.44 31.47 ?  158 LYS   B HD3  1 
ATOM   6733 H HE2  A LYS   B 1 158 ? 47.049 -40.232 -14.730 0.56 33.70 ?  158 LYS   B HE2  1 
ATOM   6734 H HE2  B LYS   B 1 158 ? 47.041 -40.093 -14.785 0.44 32.80 ?  158 LYS   B HE2  1 
ATOM   6735 H HE3  A LYS   B 1 158 ? 45.956 -40.702 -13.677 0.56 33.70 ?  158 LYS   B HE3  1 
ATOM   6736 H HE3  B LYS   B 1 158 ? 45.929 -40.590 -13.763 0.44 32.80 ?  158 LYS   B HE3  1 
ATOM   6737 H HZ1  A LYS   B 1 158 ? 44.959 -39.862 -15.536 0.56 33.91 ?  158 LYS   B HZ1  1 
ATOM   6738 H HZ1  B LYS   B 1 158 ? 44.963 -39.698 -15.616 0.44 33.22 ?  158 LYS   B HZ1  1 
ATOM   6739 H HZ2  A LYS   B 1 158 ? 44.625 -39.009 -14.414 0.56 33.91 ?  158 LYS   B HZ2  1 
ATOM   6740 H HZ2  B LYS   B 1 158 ? 44.609 -38.877 -14.476 0.44 33.22 ?  158 LYS   B HZ2  1 
ATOM   6741 H HZ3  A LYS   B 1 158 ? 45.623 -38.584 -15.374 0.56 33.91 ?  158 LYS   B HZ3  1 
ATOM   6742 H HZ3  B LYS   B 1 158 ? 45.623 -38.425 -15.408 0.44 33.22 ?  158 LYS   B HZ3  1 
ATOM   6743 N N    . ASN   B 1 159 ? 46.791 -39.817 -8.570  1.00 21.94 ?  159 ASN   B N    1 
ATOM   6744 C CA   . ASN   B 1 159 ? 45.834 -40.792 -8.052  1.00 22.77 ?  159 ASN   B CA   1 
ATOM   6745 C C    . ASN   B 1 159 ? 44.641 -40.111 -7.375  1.00 21.55 ?  159 ASN   B C    1 
ATOM   6746 O O    . ASN   B 1 159 ? 43.508 -40.605 -7.463  1.00 21.87 ?  159 ASN   B O    1 
ATOM   6747 C CB   . ASN   B 1 159 ? 46.541 -41.767 -7.114  1.00 24.64 ?  159 ASN   B CB   1 
ATOM   6748 C CG   . ASN   B 1 159 ? 47.559 -42.625 -7.836  1.00 26.54 ?  159 ASN   B CG   1 
ATOM   6749 O OD1  . ASN   B 1 159 ? 47.311 -43.092 -8.957  1.00 27.12 ?  159 ASN   B OD1  1 
ATOM   6750 N ND2  . ASN   B 1 159 ? 48.715 -42.837 -7.203  1.00 27.44 ?  159 ASN   B ND2  1 
ATOM   6751 H H    A ASN   B 1 159 ? 47.542 -39.780 -8.153  0.56 26.35 ?  159 ASN   B H    1 
ATOM   6752 H H    B ASN   B 1 159 ? 47.542 -39.779 -8.153  0.44 26.35 ?  159 ASN   B H    1 
ATOM   6753 H HA   . ASN   B 1 159 ? 45.500 -41.305 -8.808  1.00 27.35 ?  159 ASN   B HA   1 
ATOM   6754 H HB2  . ASN   B 1 159 ? 47.005 -41.268 -6.426  1.00 29.59 ?  159 ASN   B HB2  1 
ATOM   6755 H HB3  . ASN   B 1 159 ? 45.885 -42.357 -6.723  1.00 29.59 ?  159 ASN   B HB3  1 
ATOM   6756 H HD21 . ASN   B 1 159 ? 49.331 -43.323 -7.567  1.00 32.95 ?  159 ASN   B HD21 1 
ATOM   6757 H HD22 . ASN   B 1 159 ? 48.847 -42.508 -6.418  1.00 32.95 ?  159 ASN   B HD22 1 
ATOM   6758 N N    . LEU   B 1 160 ? 44.861 -38.983 -6.694  1.00 21.01 ?  160 LEU   B N    1 
ATOM   6759 C CA   . LEU   B 1 160 ? 43.730 -38.246 -6.146  1.00 20.01 ?  160 LEU   B CA   1 
ATOM   6760 C C    . LEU   B 1 160 ? 42.944 -37.570 -7.257  1.00 18.96 ?  160 LEU   B C    1 
ATOM   6761 O O    . LEU   B 1 160 ? 41.708 -37.573 -7.235  1.00 18.73 ?  160 LEU   B O    1 
ATOM   6762 C CB   . LEU   B 1 160 ? 44.203 -37.222 -5.116  1.00 19.24 ?  160 LEU   B CB   1 
ATOM   6763 C CG   . LEU   B 1 160 ? 43.077 -36.307 -4.612  1.00 18.75 ?  160 LEU   B CG   1 
ATOM   6764 C CD1  . LEU   B 1 160 ? 41.950 -37.124 -4.005  1.00 20.15 ?  160 LEU   B CD1  1 
ATOM   6765 C CD2  . LEU   B 1 160 ? 43.611 -35.302 -3.602  1.00 18.59 ?  160 LEU   B CD2  1 
ATOM   6766 H H    . LEU   B 1 160 ? 45.636 -38.641 -6.547  1.00 25.24 ?  160 LEU   B H    1 
ATOM   6767 H HA   . LEU   B 1 160 ? 43.140 -38.875 -5.707  1.00 24.04 ?  160 LEU   B HA   1 
ATOM   6768 H HB2  . LEU   B 1 160 ? 44.572 -37.699 -4.355  1.00 23.11 ?  160 LEU   B HB2  1 
ATOM   6769 H HB3  . LEU   B 1 160 ? 44.889 -36.668 -5.522  1.00 23.11 ?  160 LEU   B HB3  1 
ATOM   6770 H HG   . LEU   B 1 160 ? 42.717 -35.808 -5.361  1.00 22.52 ?  160 LEU   B HG   1 
ATOM   6771 H HD11 . LEU   B 1 160 ? 41.334 -36.527 -3.563  1.00 24.21 ?  160 LEU   B HD11 1 
ATOM   6772 H HD12 . LEU   B 1 160 ? 41.493 -37.613 -4.710  1.00 24.21 ?  160 LEU   B HD12 1 
ATOM   6773 H HD13 . LEU   B 1 160 ? 42.325 -37.752 -3.363  1.00 24.21 ?  160 LEU   B HD13 1 
ATOM   6774 H HD21 . LEU   B 1 160 ? 42.884 -34.732 -3.320  1.00 22.33 ?  160 LEU   B HD21 1 
ATOM   6775 H HD22 . LEU   B 1 160 ? 43.973 -35.786 -2.843  1.00 22.33 ?  160 LEU   B HD22 1 
ATOM   6776 H HD23 . LEU   B 1 160 ? 44.308 -34.775 -4.023  1.00 22.33 ?  160 LEU   B HD23 1 
ATOM   6777 N N    . TYR   B 1 161 ? 43.642 -37.002 -8.245  1.00 19.13 ?  161 TYR   B N    1 
ATOM   6778 C CA   . TYR   B 1 161 ? 42.967 -36.447 -9.414  1.00 19.11 ?  161 TYR   B CA   1 
ATOM   6779 C C    . TYR   B 1 161 ? 42.017 -37.472 -10.022 1.00 19.18 ?  161 TYR   B C    1 
ATOM   6780 O O    . TYR   B 1 161 ? 40.845 -37.177 -10.273 1.00 19.05 ?  161 TYR   B O    1 
ATOM   6781 C CB   . TYR   B 1 161 ? 44.002 -35.970 -10.446 1.00 19.44 ?  161 TYR   B CB   1 
ATOM   6782 C CG   . TYR   B 1 161 ? 43.421 -35.513 -11.768 1.00 20.33 ?  161 TYR   B CG   1 
ATOM   6783 C CD1  . TYR   B 1 161 ? 43.022 -34.192 -11.950 1.00 20.33 ?  161 TYR   B CD1  1 
ATOM   6784 C CD2  . TYR   B 1 161 ? 43.259 -36.396 -12.833 1.00 20.98 ?  161 TYR   B CD2  1 
ATOM   6785 C CE1  . TYR   B 1 161 ? 42.484 -33.765 -13.145 1.00 21.88 ?  161 TYR   B CE1  1 
ATOM   6786 C CE2  . TYR   B 1 161 ? 42.718 -35.975 -14.035 1.00 21.92 ?  161 TYR   B CE2  1 
ATOM   6787 C CZ   . TYR   B 1 161 ? 42.335 -34.656 -14.185 1.00 22.44 ?  161 TYR   B CZ   1 
ATOM   6788 O OH   . TYR   B 1 161 ? 41.796 -34.226 -15.375 1.00 24.72 ?  161 TYR   B OH   1 
ATOM   6789 H H    . TYR   B 1 161 ? 44.496 -36.942 -8.271  1.00 22.98 ?  161 TYR   B H    1 
ATOM   6790 H HA   . TYR   B 1 161 ? 42.442 -35.679 -9.145  1.00 22.96 ?  161 TYR   B HA   1 
ATOM   6791 H HB2  . TYR   B 1 161 ? 44.490 -35.219 -10.073 1.00 23.35 ?  161 TYR   B HB2  1 
ATOM   6792 H HB3  . TYR   B 1 161 ? 44.614 -36.696 -10.637 1.00 23.35 ?  161 TYR   B HB3  1 
ATOM   6793 H HD1  . TYR   B 1 161 ? 43.118 -33.582 -11.256 1.00 24.42 ?  161 TYR   B HD1  1 
ATOM   6794 H HD2  . TYR   B 1 161 ? 43.511 -37.287 -12.740 1.00 25.20 ?  161 TYR   B HD2  1 
ATOM   6795 H HE1  . TYR   B 1 161 ? 42.222 -32.873 -13.250 1.00 26.28 ?  161 TYR   B HE1  1 
ATOM   6796 H HE2  . TYR   B 1 161 ? 42.612 -36.575 -14.742 1.00 26.33 ?  161 TYR   B HE2  1 
ATOM   6797 H HH   . TYR   B 1 161 ? 41.759 -34.862 -15.925 1.00 29.69 ?  161 TYR   B HH   1 
ATOM   6798 N N    . ASP   B 1 162 ? 42.505 -38.693 -10.247 1.00 19.57 ?  162 ASP   B N    1 
ATOM   6799 C CA   . ASP   B 1 162 ? 41.666 -39.723 -10.849 1.00 19.96 ?  162 ASP   B CA   1 
ATOM   6800 C C    . ASP   B 1 162 ? 40.466 -40.052 -9.970  1.00 19.77 ?  162 ASP   B C    1 
ATOM   6801 O O    . ASP   B 1 162 ? 39.355 -40.257 -10.474 1.00 20.60 ?  162 ASP   B O    1 
ATOM   6802 C CB   . ASP   B 1 162 ? 42.483 -40.994 -11.095 1.00 21.31 ?  162 ASP   B CB   1 
ATOM   6803 C CG   . ASP   B 1 162 ? 43.507 -40.844 -12.207 1.00 22.91 ?  162 ASP   B CG   1 
ATOM   6804 O OD1  . ASP   B 1 162 ? 43.403 -39.906 -13.016 1.00 23.88 ?  162 ASP   B OD1  1 
ATOM   6805 O OD2  . ASP   B 1 162 ? 44.407 -41.710 -12.295 1.00 24.18 -1 162 ASP   B OD2  1 
ATOM   6806 H H    . ASP   B 1 162 ? 43.304 -38.941 -10.066 1.00 23.51 ?  162 ASP   B H    1 
ATOM   6807 H HA   . ASP   B 1 162 ? 41.333 -39.412 -11.702 1.00 23.97 ?  162 ASP   B HA   1 
ATOM   6808 H HB2  . ASP   B 1 162 ? 42.965 -41.225 -10.288 1.00 25.60 ?  162 ASP   B HB2  1 
ATOM   6809 H HB3  . ASP   B 1 162 ? 41.886 -41.714 -11.348 1.00 25.60 ?  162 ASP   B HB3  1 
ATOM   6810 N N    . LYS   B 1 163 ? 40.673 -40.138 -8.655  1.00 18.69 ?  163 LYS   B N    1 
ATOM   6811 C CA   . LYS   B 1 163 ? 39.553 -40.402 -7.757  1.00 18.93 ?  163 LYS   B CA   1 
ATOM   6812 C C    . LYS   B 1 163 ? 38.515 -39.285 -7.823  1.00 18.15 ?  163 LYS   B C    1 
ATOM   6813 O O    . LYS   B 1 163 ? 37.303 -39.546 -7.796  1.00 18.93 ?  163 LYS   B O    1 
ATOM   6814 C CB   . LYS   B 1 163 ? 40.048 -40.575 -6.326  1.00 21.43 ?  163 LYS   B CB   1 
ATOM   6815 C CG   . LYS   B 1 163 ? 38.971 -41.068 -5.390  1.00 26.31 ?  163 LYS   B CG   1 
ATOM   6816 C CD   . LYS   B 1 163 ? 39.466 -41.232 -3.968  1.00 30.11 ?  163 LYS   B CD   1 
ATOM   6817 C CE   . LYS   B 1 163 ? 38.388 -41.871 -3.101  1.00 34.24 ?  163 LYS   B CE   1 
ATOM   6818 N NZ   . LYS   B 1 163 ? 38.644 -41.688 -1.646  1.00 36.47 ?  163 LYS   B NZ   1 
ATOM   6819 H H    . LYS   B 1 163 ? 41.439 -40.055 -8.268  1.00 22.45 ?  163 LYS   B H    1 
ATOM   6820 H HA   . LYS   B 1 163 ? 39.122 -41.228 -8.026  1.00 22.73 ?  163 LYS   B HA   1 
ATOM   6821 H HB2  . LYS   B 1 163 ? 40.771 -41.225 -6.316  1.00 25.74 ?  163 LYS   B HB2  1 
ATOM   6822 H HB3  . LYS   B 1 163 ? 40.366 -39.723 -5.993  1.00 25.74 ?  163 LYS   B HB3  1 
ATOM   6823 H HG2  . LYS   B 1 163 ? 38.241 -40.432 -5.383  1.00 31.60 ?  163 LYS   B HG2  1 
ATOM   6824 H HG3  . LYS   B 1 163 ? 38.654 -41.933 -5.701  1.00 31.60 ?  163 LYS   B HG3  1 
ATOM   6825 H HD2  . LYS   B 1 163 ? 40.246 -41.810 -3.963  1.00 36.15 ?  163 LYS   B HD2  1 
ATOM   6826 H HD3  . LYS   B 1 163 ? 39.684 -40.363 -3.601  1.00 36.15 ?  163 LYS   B HD3  1 
ATOM   6827 H HE2  . LYS   B 1 163 ? 37.528 -41.476 -3.313  1.00 41.11 ?  163 LYS   B HE2  1 
ATOM   6828 H HE3  . LYS   B 1 163 ? 38.363 -42.822 -3.284  1.00 41.11 ?  163 LYS   B HE3  1 
ATOM   6829 H HZ1  . LYS   B 1 163 ? 37.994 -42.071 -1.173  1.00 43.79 ?  163 LYS   B HZ1  1 
ATOM   6830 H HZ2  . LYS   B 1 163 ? 39.420 -42.061 -1.426  1.00 43.79 ?  163 LYS   B HZ2  1 
ATOM   6831 H HZ3  . LYS   B 1 163 ? 38.672 -40.821 -1.448  1.00 43.79 ?  163 LYS   B HZ3  1 
ATOM   6832 N N    . LEU   B 1 164 ? 38.975 -38.034 -7.898  1.00 16.74 ?  164 LEU   B N    1 
ATOM   6833 C CA   . LEU   B 1 164 ? 38.064 -36.894 -7.949  1.00 16.32 ?  164 LEU   B CA   1 
ATOM   6834 C C    . LEU   B 1 164 ? 37.279 -36.874 -9.255  1.00 17.28 ?  164 LEU   B C    1 
ATOM   6835 O O    . LEU   B 1 164 ? 36.053 -36.675 -9.255  1.00 18.76 ?  164 LEU   B O    1 
ATOM   6836 C CB   . LEU   B 1 164 ? 38.867 -35.602 -7.781  1.00 15.90 ?  164 LEU   B CB   1 
ATOM   6837 C CG   . LEU   B 1 164 ? 39.413 -35.319 -6.382  1.00 16.68 ?  164 LEU   B CG   1 
ATOM   6838 C CD1  . LEU   B 1 164 ? 40.474 -34.229 -6.452  1.00 16.99 ?  164 LEU   B CD1  1 
ATOM   6839 C CD2  . LEU   B 1 164 ? 38.303 -34.901 -5.436  1.00 18.50 ?  164 LEU   B CD2  1 
ATOM   6840 H H    . LEU   B 1 164 ? 39.816 -37.823 -7.920  1.00 20.12 ?  164 LEU   B H    1 
ATOM   6841 H HA   . LEU   B 1 164 ? 37.440 -36.960 -7.221  1.00 19.61 ?  164 LEU   B HA   1 
ATOM   6842 H HB2  . LEU   B 1 164 ? 39.633 -35.634 -8.384  1.00 19.10 ?  164 LEU   B HB2  1 
ATOM   6843 H HB3  . LEU   B 1 164 ? 38.303 -34.858 -8.022  1.00 19.10 ?  164 LEU   B HB3  1 
ATOM   6844 H HG   . LEU   B 1 164 ? 39.837 -36.121 -6.032  1.00 20.04 ?  164 LEU   B HG   1 
ATOM   6845 H HD11 . LEU   B 1 164 ? 40.806 -34.050 -5.556  1.00 20.41 ?  164 LEU   B HD11 1 
ATOM   6846 H HD12 . LEU   B 1 164 ? 41.205 -34.525 -7.018  1.00 20.41 ?  164 LEU   B HD12 1 
ATOM   6847 H HD13 . LEU   B 1 164 ? 40.077 -33.423 -6.821  1.00 20.41 ?  164 LEU   B HD13 1 
ATOM   6848 H HD21 . LEU   B 1 164 ? 38.688 -34.686 -4.574  1.00 22.22 ?  164 LEU   B HD21 1 
ATOM   6849 H HD22 . LEU   B 1 164 ? 37.854 -34.127 -5.805  1.00 22.22 ?  164 LEU   B HD22 1 
ATOM   6850 H HD23 . LEU   B 1 164 ? 37.679 -35.638 -5.347  1.00 22.22 ?  164 LEU   B HD23 1 
ATOM   6851 N N    . VAL   B 1 165 ? 37.968 -37.057 -10.382 1.00 18.72 ?  165 VAL   B N    1 
ATOM   6852 C CA   . VAL   B 1 165 ? 37.305 -37.002 -11.680 1.00 20.52 ?  165 VAL   B CA   1 
ATOM   6853 C C    . VAL   B 1 165 ? 36.375 -38.197 -11.849 1.00 22.66 ?  165 VAL   B C    1 
ATOM   6854 O O    . VAL   B 1 165 ? 35.208 -38.052 -12.236 1.00 24.16 ?  165 VAL   B O    1 
ATOM   6855 C CB   . VAL   B 1 165 ? 38.343 -36.932 -12.816 1.00 21.39 ?  165 VAL   B CB   1 
ATOM   6856 C CG1  . VAL   B 1 165 ? 37.660 -37.047 -14.161 1.00 22.89 ?  165 VAL   B CG1  1 
ATOM   6857 C CG2  . VAL   B 1 165 ? 39.139 -35.642 -12.736 1.00 20.84 ?  165 VAL   B CG2  1 
ATOM   6858 H H    . VAL   B 1 165 ? 38.822 -37.211 -10.425 1.00 22.49 ?  165 VAL   B H    1 
ATOM   6859 H HA   . VAL   B 1 165 ? 36.771 -36.196 -11.724 1.00 24.64 ?  165 VAL   B HA   1 
ATOM   6860 H HB   . VAL   B 1 165 ? 38.970 -37.668 -12.727 1.00 25.69 ?  165 VAL   B HB   1 
ATOM   6861 H HG11 . VAL   B 1 165 ? 38.265 -36.744 -14.852 1.00 27.49 ?  165 VAL   B HG11 1 
ATOM   6862 H HG12 . VAL   B 1 165 ? 37.430 -37.979 -14.314 1.00 27.49 ?  165 VAL   B HG12 1 
ATOM   6863 H HG13 . VAL   B 1 165 ? 36.859 -36.505 -14.154 1.00 27.49 ?  165 VAL   B HG13 1 
ATOM   6864 H HG21 . VAL   B 1 165 ? 39.769 -35.608 -13.477 1.00 25.03 ?  165 VAL   B HG21 1 
ATOM   6865 H HG22 . VAL   B 1 165 ? 38.529 -34.888 -12.793 1.00 25.03 ?  165 VAL   B HG22 1 
ATOM   6866 H HG23 . VAL   B 1 165 ? 39.622 -35.613 -11.895 1.00 25.03 ?  165 VAL   B HG23 1 
ATOM   6867 N N    . SER   B 1 166 ? 36.888 -39.401 -11.561 1.00 23.61 ?  166 SER   B N    1 
ATOM   6868 C CA   . SER   B 1 166 ? 36.132 -40.617 -11.832 1.00 24.50 ?  166 SER   B CA   1 
ATOM   6869 C C    . SER   B 1 166 ? 34.871 -40.691 -10.986 1.00 24.58 ?  166 SER   B C    1 
ATOM   6870 O O    . SER   B 1 166 ? 33.898 -41.314 -11.403 1.00 26.34 ?  166 SER   B O    1 
ATOM   6871 C CB   . SER   B 1 166 ? 37.000 -41.871 -11.646 1.00 25.11 ?  166 SER   B CB   1 
ATOM   6872 O OG   . SER   B 1 166 ? 37.351 -42.071 -10.288 1.00 25.18 ?  166 SER   B OG   1 
ATOM   6873 H H    . SER   B 1 166 ? 37.674 -39.533 -11.223 1.00 28.35 ?  166 SER   B H    1 
ATOM   6874 H HA   . SER   B 1 166 ? 35.857 -40.602 -12.760 1.00 29.42 ?  166 SER   B HA   1 
ATOM   6875 H HB2  . SER   B 1 166 ? 36.505 -42.644 -11.959 1.00 30.16 ?  166 SER   B HB2  1 
ATOM   6876 H HB3  . SER   B 1 166 ? 37.813 -41.772 -12.174 1.00 30.16 ?  166 SER   B HB3  1 
ATOM   6877 H HG   . SER   B 1 166 ? 37.798 -41.414 -10.012 1.00 30.24 ?  166 SER   B HG   1 
ATOM   6878 N N    . SER   B 1 167 ? 34.857 -40.074 -9.808  1.00 22.88 ?  167 SER   B N    1 
ATOM   6879 C CA   . SER   B 1 167 ? 33.699 -40.119 -8.921  1.00 22.99 ?  167 SER   B CA   1 
ATOM   6880 C C    . SER   B 1 167 ? 32.789 -38.890 -9.014  1.00 22.11 ?  167 SER   B C    1 
ATOM   6881 O O    . SER   B 1 167 ? 31.709 -38.898 -8.415  1.00 22.42 ?  167 SER   B O    1 
ATOM   6882 C CB   . SER   B 1 167 ? 34.154 -40.310 -7.466  1.00 22.94 ?  167 SER   B CB   1 
ATOM   6883 O OG   . SER   B 1 167 ? 34.810 -39.140 -6.985  1.00 23.10 ?  167 SER   B OG   1 
ATOM   6884 H H    . SER   B 1 167 ? 35.511 -39.622 -9.500  1.00 27.48 ?  167 SER   B H    1 
ATOM   6885 H HA   . SER   B 1 167 ? 33.166 -40.899 -9.158  1.00 27.61 ?  167 SER   B HA   1 
ATOM   6886 H HB2  . SER   B 1 167 ? 33.374 -40.501 -6.918  1.00 27.55 ?  167 SER   B HB2  1 
ATOM   6887 H HB3  . SER   B 1 167 ? 34.768 -41.071 -7.428  1.00 27.55 ?  167 SER   B HB3  1 
ATOM   6888 H HG   . SER   B 1 167 ? 35.482 -38.990 -7.453  1.00 27.75 ?  167 SER   B HG   1 
ATOM   6889 N N    . PHE   B 1 168 ? 33.174 -37.844 -9.749  1.00 21.70 ?  168 PHE   B N    1 
ATOM   6890 C CA   . PHE   B 1 168 ? 32.328 -36.652 -9.827  1.00 20.38 ?  168 PHE   B CA   1 
ATOM   6891 C C    . PHE   B 1 168 ? 31.035 -36.927 -10.593 1.00 17.94 ?  168 PHE   B C    1 
ATOM   6892 O O    . PHE   B 1 168 ? 29.971 -36.355 -10.272 1.00 17.95 ?  168 PHE   B O    1 
ATOM   6893 C CB   . PHE   B 1 168 ? 33.103 -35.510 -10.481 1.00 21.31 ?  168 PHE   B CB   1 
ATOM   6894 C CG   . PHE   B 1 168 ? 32.292 -34.271 -10.667 1.00 21.25 ?  168 PHE   B CG   1 
ATOM   6895 C CD1  . PHE   B 1 168 ? 31.927 -33.507 -9.570  1.00 22.39 ?  168 PHE   B CD1  1 
ATOM   6896 C CD2  . PHE   B 1 168 ? 31.875 -33.874 -11.925 1.00 20.43 ?  168 PHE   B CD2  1 
ATOM   6897 C CE1  . PHE   B 1 168 ? 31.161 -32.366 -9.720  1.00 21.86 ?  168 PHE   B CE1  1 
ATOM   6898 C CE2  . PHE   B 1 168 ? 31.119 -32.717 -12.088 1.00 21.79 ?  168 PHE   B CE2  1 
ATOM   6899 C CZ   . PHE   B 1 168 ? 30.757 -31.963 -10.980 1.00 22.00 ?  168 PHE   B CZ   1 
ATOM   6900 H H    . PHE   B 1 168 ? 33.899 -37.807 -10.205 1.00 26.06 ?  168 PHE   B H    1 
ATOM   6901 H HA   . PHE   B 1 168 ? 32.085 -36.382 -8.931  1.00 24.48 ?  168 PHE   B HA   1 
ATOM   6902 H HB2  . PHE   B 1 168 ? 33.860 -35.288 -9.919  1.00 25.60 ?  168 PHE   B HB2  1 
ATOM   6903 H HB3  . PHE   B 1 168 ? 33.410 -35.798 -11.354 1.00 25.60 ?  168 PHE   B HB3  1 
ATOM   6904 H HD1  . PHE   B 1 168 ? 32.192 -33.775 -8.721  1.00 26.89 ?  168 PHE   B HD1  1 
ATOM   6905 H HD2  . PHE   B 1 168 ? 32.113 -34.375 -12.669 1.00 24.53 ?  168 PHE   B HD2  1 
ATOM   6906 H HE1  . PHE   B 1 168 ? 30.925 -31.867 -8.976  1.00 26.26 ?  168 PHE   B HE1  1 
ATOM   6907 H HE2  . PHE   B 1 168 ? 30.841 -32.458 -12.938 1.00 26.17 ?  168 PHE   B HE2  1 
ATOM   6908 H HZ   . PHE   B 1 168 ? 30.242 -31.196 -11.085 1.00 26.42 ?  168 PHE   B HZ   1 
ATOM   6909 N N    . LEU   B 1 169 ? 31.111 -37.784 -11.610 1.00 18.73 ?  169 LEU   B N    1 
ATOM   6910 C CA   . LEU   B 1 169 ? 29.949 -38.123 -12.426 1.00 21.15 ?  169 LEU   B CA   1 
ATOM   6911 C C    . LEU   B 1 169 ? 29.931 -39.567 -12.901 1.00 24.09 ?  169 LEU   B C    1 
ATOM   6912 O O    . LEU   B 1 169 ? 29.023 -39.972 -13.630 1.00 26.51 ?  169 LEU   B O    1 
ATOM   6913 C CB   . LEU   B 1 169 ? 29.889 -37.217 -13.653 1.00 22.78 ?  169 LEU   B CB   1 
ATOM   6914 C CG   . LEU   B 1 169 ? 28.653 -36.326 -13.763 1.00 25.74 ?  169 LEU   B CG   1 
ATOM   6915 C CD1  . LEU   B 1 169 ? 28.609 -35.695 -15.133 1.00 27.05 ?  169 LEU   B CD1  1 
ATOM   6916 C CD2  . LEU   B 1 169 ? 27.375 -37.104 -13.487 1.00 25.61 ?  169 LEU   B CD2  1 
ATOM   6917 O OXT  . LEU   B 1 169 ? 30.820 -40.347 -12.584 1.00 25.05 -1 169 LEU   B OXT  1 
ATOM   6918 H H    . LEU   B 1 169 ? 31.833 -38.179 -11.861 1.00 22.50 ?  169 LEU   B H    1 
ATOM   6919 H HA   . LEU   B 1 169 ? 29.156 -37.974 -11.895 1.00 25.40 ?  169 LEU   B HA   1 
ATOM   6920 H HB2  . LEU   B 1 169 ? 30.664 -36.634 -13.647 1.00 27.35 ?  169 LEU   B HB2  1 
ATOM   6921 H HB3  . LEU   B 1 169 ? 29.912 -37.772 -14.450 1.00 27.35 ?  169 LEU   B HB3  1 
ATOM   6922 H HG   . LEU   B 1 169 ? 28.717 -35.613 -13.107 1.00 30.91 ?  169 LEU   B HG   1 
ATOM   6923 H HD11 . LEU   B 1 169 ? 27.838 -35.108 -15.183 1.00 32.49 ?  169 LEU   B HD11 1 
ATOM   6924 H HD12 . LEU   B 1 169 ? 29.423 -35.188 -15.271 1.00 32.49 ?  169 LEU   B HD12 1 
ATOM   6925 H HD13 . LEU   B 1 169 ? 28.536 -36.396 -15.798 1.00 32.49 ?  169 LEU   B HD13 1 
ATOM   6926 H HD21 . LEU   B 1 169 ? 26.636 -36.671 -13.935 1.00 30.75 ?  169 LEU   B HD21 1 
ATOM   6927 H HD22 . LEU   B 1 169 ? 27.482 -38.011 -13.822 1.00 30.75 ?  169 LEU   B HD22 1 
ATOM   6928 H HD23 . LEU   B 1 169 ? 27.219 -37.126 -12.530 1.00 30.75 ?  169 LEU   B HD23 1 
HETATM 6929 C C1   T TFA   C 2 .   ? 12.177 -1.245  1.415   0.30 11.11 ?  201 TFA   A C1   1 
HETATM 6930 C C2   T TFA   C 2 .   ? 12.778 -1.731  0.081   0.30 13.25 ?  201 TFA   A C2   1 
HETATM 6931 O O    T TFA   C 2 .   ? 12.855 -1.513  2.405   0.30 10.01 ?  201 TFA   A O    1 
HETATM 6932 F F1   T TFA   C 2 .   ? 12.765 -3.072  0.059   0.30 15.08 ?  201 TFA   A F1   1 
HETATM 6933 F F2   T TFA   C 2 .   ? 12.096 -1.324  -1.000  0.30 13.16 ?  201 TFA   A F2   1 
HETATM 6934 F F3   T TFA   C 2 .   ? 14.034 -1.323  -0.100  0.30 15.37 ?  201 TFA   A F3   1 
HETATM 6935 O OXT  T TFA   C 2 .   ? 11.106 -0.665  1.314   0.30 10.64 ?  201 TFA   A OXT  1 
HETATM 6936 N N2   B A1A85 D 3 .   ? 15.159 -0.092  4.056   0.44 18.41 ?  202 A1A85 A N2   1 
HETATM 6937 C C3   B A1A85 D 3 .   ? 15.260 -0.825  0.196   0.44 20.97 ?  202 A1A85 A C3   1 
HETATM 6938 C C6   B A1A85 D 3 .   ? 15.046 -0.062  5.432   0.44 17.57 ?  202 A1A85 A C6   1 
HETATM 6939 C C9   B A1A85 D 3 .   ? 15.681 3.767   3.850   0.44 17.25 ?  202 A1A85 A C9   1 
HETATM 6940 C C1   B A1A85 D 3 .   ? 13.926 1.391   -0.054  0.44 21.01 ?  202 A1A85 A C1   1 
HETATM 6941 C C10  B A1A85 D 3 .   ? 15.658 4.389   5.107   0.44 16.11 ?  202 A1A85 A C10  1 
HETATM 6942 C C11  B A1A85 D 3 .   ? 14.876 2.029   1.048   0.44 19.36 ?  202 A1A85 A C11  1 
HETATM 6943 C C2   B A1A85 D 3 .   ? 14.670 0.218   -0.787  0.44 21.12 ?  202 A1A85 A C2   1 
HETATM 6944 C C4   B A1A85 D 3 .   ? 16.163 -0.151  1.269   0.44 20.47 ?  202 A1A85 A C4   1 
HETATM 6945 C C5   B A1A85 D 3 .   ? 15.369 1.063   3.360   0.44 18.58 ?  202 A1A85 A C5   1 
HETATM 6946 C C7   B A1A85 D 3 .   ? 15.328 2.180   5.505   0.44 16.70 ?  202 A1A85 A C7   1 
HETATM 6947 C C8   B A1A85 D 3 .   ? 15.468 2.323   4.076   0.44 17.36 ?  202 A1A85 A C8   1 
HETATM 6948 N N1   B A1A85 D 3 .   ? 15.474 0.977   1.925   0.44 19.50 ?  202 A1A85 A N1   1 
HETATM 6949 N N3   B A1A85 D 3 .   ? 15.116 1.032   6.187   0.44 16.77 ?  202 A1A85 A N3   1 
HETATM 6950 N N4   B A1A85 D 3 .   ? 15.455 3.426   6.027   0.44 16.02 ?  202 A1A85 A N4   1 
HETATM 6951 O O1   B A1A85 D 3 .   ? 13.563 2.393   -0.984  0.44 22.29 ?  202 A1A85 A O1   1 
HETATM 6952 H H6   B A1A85 D 3 .   ? 15.848 -1.616  -0.370  0.44 25.18 ?  202 A1A85 A H6   1 
HETATM 6953 H H5   B A1A85 D 3 .   ? 14.454 -1.405  0.702   0.44 25.18 ?  202 A1A85 A H5   1 
HETATM 6954 H H9   B A1A85 D 3 .   ? 14.868 -1.018  5.994   0.44 21.11 ?  202 A1A85 A H9   1 
HETATM 6955 H H10  B A1A85 D 3 .   ? 15.829 4.309   2.936   0.44 20.72 ?  202 A1A85 A H10  1 
HETATM 6956 H H1   B A1A85 D 3 .   ? 13.007 1.021   0.463   0.44 25.23 ?  202 A1A85 A H1   1 
HETATM 6957 H H11  B A1A85 D 3 .   ? 15.763 5.430   5.453   0.44 19.35 ?  202 A1A85 A H11  1 
HETATM 6958 H H14  B A1A85 D 3 .   ? 14.301 2.763   1.666   0.44 23.26 ?  202 A1A85 A H14  1 
HETATM 6959 H H13  B A1A85 D 3 .   ? 15.686 2.620   0.550   0.44 23.26 ?  202 A1A85 A H13  1 
HETATM 6960 H H4   B A1A85 D 3 .   ? 15.491 0.611   -1.412  0.44 25.36 ?  202 A1A85 A H4   1 
HETATM 6961 H H3   B A1A85 D 3 .   ? 13.974 -0.281  -1.513  0.44 25.36 ?  202 A1A85 A H3   1 
HETATM 6962 H H7   B A1A85 D 3 .   ? 17.138 0.182   0.816   0.44 24.59 ?  202 A1A85 A H7   1 
HETATM 6963 H H8   B A1A85 D 3 .   ? 16.474 -0.939  2.023   0.44 24.59 ?  202 A1A85 A H8   1 
HETATM 6964 H H12  B A1A85 D 3 .   ? 15.389 3.621   7.072   0.44 19.24 ?  202 A1A85 A H12  1 
HETATM 6965 H H2   B A1A85 D 3 .   ? 12.591 2.543   -0.986  0.44 26.77 ?  202 A1A85 A H2   1 
HETATM 6966 O O    . HOH   E 4 .   ? 11.887 0.317   14.668  1.00 35.63 ?  301 HOH   A O    1 
HETATM 6967 O O    . HOH   E 4 .   ? 4.707  3.657   0.295   1.00 22.95 ?  302 HOH   A O    1 
HETATM 6968 O O    A HOH   E 4 .   ? 14.729 -4.516  20.386  0.56 37.45 ?  303 HOH   A O    1 
HETATM 6969 O O    . HOH   E 4 .   ? 15.036 -12.144 18.651  1.00 47.40 ?  304 HOH   A O    1 
HETATM 6970 O O    . HOH   E 4 .   ? 18.572 -2.374  -16.459 1.00 47.29 ?  305 HOH   A O    1 
HETATM 6971 O O    . HOH   E 4 .   ? 17.001 -17.907 14.972  1.00 30.37 ?  306 HOH   A O    1 
HETATM 6972 O O    . HOH   E 4 .   ? 10.472 -22.364 -1.232  1.00 49.95 ?  307 HOH   A O    1 
HETATM 6973 O O    . HOH   E 4 .   ? 7.611  -6.305  -6.715  1.00 43.44 ?  308 HOH   A O    1 
HETATM 6974 O O    . HOH   E 4 .   ? 11.748 -10.791 -10.108 1.00 52.36 ?  309 HOH   A O    1 
HETATM 6975 O O    . HOH   E 4 .   ? 14.618 -13.824 16.658  1.00 30.87 ?  310 HOH   A O    1 
HETATM 6976 O O    . HOH   E 4 .   ? 9.483  -16.202 -2.320  1.00 38.01 ?  311 HOH   A O    1 
HETATM 6977 O O    . HOH   E 4 .   ? 19.473 -11.034 24.093  1.00 84.42 ?  312 HOH   A O    1 
HETATM 6978 O O    . HOH   E 4 .   ? 34.367 -1.809  12.519  1.00 39.08 ?  313 HOH   A O    1 
HETATM 6979 O O    . HOH   E 4 .   ? 28.964 0.541   -9.724  1.00 24.14 ?  314 HOH   A O    1 
HETATM 6980 O O    . HOH   E 4 .   ? 28.031 -6.214  19.597  1.00 43.14 ?  315 HOH   A O    1 
HETATM 6981 O O    . HOH   E 4 .   ? 30.191 -13.313 -8.470  1.00 29.55 ?  316 HOH   A O    1 
HETATM 6982 O O    . HOH   E 4 .   ? 18.925 -21.912 7.032   1.00 37.46 ?  317 HOH   A O    1 
HETATM 6983 O O    . HOH   E 4 .   ? 9.880  -21.317 5.550   1.00 22.37 ?  318 HOH   A O    1 
HETATM 6984 O O    . HOH   E 4 .   ? 16.969 -19.198 4.822   1.00 17.77 ?  319 HOH   A O    1 
HETATM 6985 O O    A HOH   E 4 .   ? 14.607 -3.601  3.061   0.56 14.73 ?  320 HOH   A O    1 
HETATM 6986 O O    . HOH   E 4 .   ? 0.747  -4.196  -0.098  1.00 29.94 ?  321 HOH   A O    1 
HETATM 6987 O O    . HOH   E 4 .   ? 26.875 11.474  1.623   1.00 18.62 ?  322 HOH   A O    1 
HETATM 6988 O O    . HOH   E 4 .   ? -0.661 -8.336  2.066   1.00 41.22 ?  323 HOH   A O    1 
HETATM 6989 O O    . HOH   E 4 .   ? 14.197 -4.570  -12.031 1.00 34.31 ?  324 HOH   A O    1 
HETATM 6990 O O    . HOH   E 4 .   ? 6.773  -7.957  11.692  1.00 20.00 ?  325 HOH   A O    1 
HETATM 6991 O O    . HOH   E 4 .   ? 24.104 -7.654  14.433  1.00 18.76 ?  326 HOH   A O    1 
HETATM 6992 O O    . HOH   E 4 .   ? 42.358 10.558  5.084   1.00 21.33 ?  327 HOH   A O    1 
HETATM 6993 O O    . HOH   E 4 .   ? 14.027 -22.994 7.385   1.00 20.75 ?  328 HOH   A O    1 
HETATM 6994 O O    . HOH   E 4 .   ? 3.612  -9.308  9.763   1.00 27.14 ?  329 HOH   A O    1 
HETATM 6995 O O    . HOH   E 4 .   ? 22.703 12.486  1.528   1.00 17.05 ?  330 HOH   A O    1 
HETATM 6996 O O    . HOH   E 4 .   ? 28.727 -10.557 -14.024 1.00 43.67 ?  331 HOH   A O    1 
HETATM 6997 O O    . HOH   E 4 .   ? 22.247 5.408   18.972  1.00 42.49 ?  332 HOH   A O    1 
HETATM 6998 O O    . HOH   E 4 .   ? 36.088 -5.100  -0.523  1.00 33.10 ?  333 HOH   A O    1 
HETATM 6999 O O    . HOH   E 4 .   ? 37.440 2.840   10.251  1.00 29.02 ?  334 HOH   A O    1 
HETATM 7000 O O    . HOH   E 4 .   ? 19.995 -12.505 -8.891  1.00 27.47 ?  335 HOH   A O    1 
HETATM 7001 O O    . HOH   E 4 .   ? 38.202 10.243  7.121   1.00 47.60 ?  336 HOH   A O    1 
HETATM 7002 O O    B HOH   E 4 .   ? 14.881 -2.814  3.377   0.44 19.68 ?  337 HOH   A O    1 
HETATM 7003 O O    A HOH   E 4 .   ? -0.506 -3.025  3.036   0.56 29.34 ?  338 HOH   A O    1 
HETATM 7004 O O    . HOH   E 4 .   ? 9.044  -10.032 19.254  1.00 39.39 ?  339 HOH   A O    1 
HETATM 7005 O O    . HOH   E 4 .   ? 10.879 1.713   12.399  1.00 24.89 ?  340 HOH   A O    1 
HETATM 7006 O O    . HOH   E 4 .   ? 16.079 2.925   -1.703  1.00 19.25 ?  341 HOH   A O    1 
HETATM 7007 O O    . HOH   E 4 .   ? 14.980 4.134   17.636  1.00 41.98 ?  342 HOH   A O    1 
HETATM 7008 O O    . HOH   E 4 .   ? 44.280 7.161   6.443   1.00 26.58 ?  343 HOH   A O    1 
HETATM 7009 O O    . HOH   E 4 .   ? 27.549 -6.129  -14.019 1.00 41.59 ?  344 HOH   A O    1 
HETATM 7010 O O    . HOH   E 4 .   ? 18.545 9.542   8.964   1.00 23.49 ?  345 HOH   A O    1 
HETATM 7011 O O    . HOH   E 4 .   ? 14.331 -21.201 -4.205  1.00 33.27 ?  346 HOH   A O    1 
HETATM 7012 O O    . HOH   E 4 .   ? 43.337 7.758   2.693   1.00 37.01 ?  347 HOH   A O    1 
HETATM 7013 O O    . HOH   E 4 .   ? 31.018 -18.048 7.807   1.00 20.46 ?  348 HOH   A O    1 
HETATM 7014 O O    . HOH   E 4 .   ? 38.508 4.996   7.019   1.00 16.74 ?  349 HOH   A O    1 
HETATM 7015 O O    . HOH   E 4 .   ? 18.589 -19.314 13.547  1.00 36.72 ?  350 HOH   A O    1 
HETATM 7016 O O    . HOH   E 4 .   ? 42.543 4.323   5.505   1.00 34.59 ?  351 HOH   A O    1 
HETATM 7017 O O    . HOH   E 4 .   ? 20.658 -19.725 -5.104  1.00 28.36 ?  352 HOH   A O    1 
HETATM 7018 O O    . HOH   E 4 .   ? 8.776  -11.969 17.078  1.00 38.44 ?  353 HOH   A O    1 
HETATM 7019 O O    . HOH   E 4 .   ? 33.997 -1.087  -8.960  1.00 27.31 ?  354 HOH   A O    1 
HETATM 7020 O O    . HOH   E 4 .   ? 39.775 -1.020  -5.113  1.00 23.52 ?  355 HOH   A O    1 
HETATM 7021 O O    . HOH   E 4 .   ? 28.356 -0.120  -13.416 1.00 40.61 ?  356 HOH   A O    1 
HETATM 7022 O O    . HOH   E 4 .   ? 21.292 -2.257  -2.531  1.00 16.76 ?  357 HOH   A O    1 
HETATM 7023 O O    . HOH   E 4 .   ? 31.626 8.211   14.872  1.00 27.32 ?  358 HOH   A O    1 
HETATM 7024 O O    A HOH   E 4 .   ? 14.244 0.633   6.755   0.56 16.21 ?  359 HOH   A O    1 
HETATM 7025 O O    . HOH   E 4 .   ? 27.445 13.848  2.751   1.00 30.35 ?  360 HOH   A O    1 
HETATM 7026 O O    . HOH   E 4 .   ? 24.029 -2.080  -2.126  1.00 12.13 ?  361 HOH   A O    1 
HETATM 7027 O O    . HOH   E 4 .   ? 31.875 -9.322  -6.680  1.00 25.21 ?  362 HOH   A O    1 
HETATM 7028 O O    . HOH   E 4 .   ? 25.701 -0.756  -7.350  1.00 17.71 ?  363 HOH   A O    1 
HETATM 7029 O O    . HOH   E 4 .   ? 22.497 -11.858 21.826  1.00 54.39 ?  364 HOH   A O    1 
HETATM 7030 O O    . HOH   E 4 .   ? 13.562 -15.214 -7.609  1.00 28.59 ?  365 HOH   A O    1 
HETATM 7031 O O    . HOH   E 4 .   ? 31.089 -13.905 -2.443  1.00 16.11 ?  366 HOH   A O    1 
HETATM 7032 O O    . HOH   E 4 .   ? 7.834  -21.476 4.037   1.00 47.56 ?  367 HOH   A O    1 
HETATM 7033 O O    . HOH   E 4 .   ? 27.326 -10.521 14.123  1.00 19.73 ?  368 HOH   A O    1 
HETATM 7034 O O    . HOH   E 4 .   ? 35.748 -12.580 6.911   1.00 17.34 ?  369 HOH   A O    1 
HETATM 7035 O O    . HOH   E 4 .   ? 33.503 -16.892 8.108   1.00 21.32 ?  370 HOH   A O    1 
HETATM 7036 O O    . HOH   E 4 .   ? 30.748 3.124   8.268   1.00 13.35 ?  371 HOH   A O    1 
HETATM 7037 O O    . HOH   E 4 .   ? 13.237 -1.473  -6.846  1.00 19.97 ?  372 HOH   A O    1 
HETATM 7038 O O    . HOH   E 4 .   ? 24.558 -17.442 12.750  1.00 27.10 ?  373 HOH   A O    1 
HETATM 7039 O O    T HOH   E 4 .   ? 15.383 -0.370  2.345   0.30 14.64 ?  374 HOH   A O    1 
HETATM 7040 O O    . HOH   E 4 .   ? 21.822 -21.857 8.490   1.00 31.61 ?  375 HOH   A O    1 
HETATM 7041 O O    . HOH   E 4 .   ? 37.161 -2.850  9.780   1.00 46.87 ?  376 HOH   A O    1 
HETATM 7042 O O    . HOH   E 4 .   ? 22.024 -19.312 11.421  1.00 39.35 ?  377 HOH   A O    1 
HETATM 7043 O O    . HOH   E 4 .   ? 23.917 -15.681 -9.200  1.00 39.23 ?  378 HOH   A O    1 
HETATM 7044 O O    . HOH   E 4 .   ? 24.362 3.609   -1.852  1.00 18.10 ?  379 HOH   A O    1 
HETATM 7045 O O    . HOH   E 4 .   ? 31.847 -7.271  -9.804  1.00 22.90 ?  380 HOH   A O    1 
HETATM 7046 O O    . HOH   E 4 .   ? 17.147 -17.732 -5.160  1.00 28.87 ?  381 HOH   A O    1 
HETATM 7047 O O    . HOH   E 4 .   ? 21.842 -13.677 -8.244  1.00 41.23 ?  382 HOH   A O    1 
HETATM 7048 O O    . HOH   E 4 .   ? 18.867 -0.705  -1.752  1.00 19.19 ?  383 HOH   A O    1 
HETATM 7049 O O    . HOH   E 4 .   ? 33.612 -7.114  4.341   1.00 17.86 ?  384 HOH   A O    1 
HETATM 7050 O O    . HOH   E 4 .   ? 20.046 4.574   -7.633  1.00 21.71 ?  385 HOH   A O    1 
HETATM 7051 O O    . HOH   E 4 .   ? 44.041 8.572   -2.874  1.00 30.34 ?  386 HOH   A O    1 
HETATM 7052 O O    . HOH   E 4 .   ? 24.534 1.998   -7.008  1.00 20.47 ?  387 HOH   A O    1 
HETATM 7053 O O    . HOH   E 4 .   ? 6.573  -3.107  12.638  1.00 31.59 ?  388 HOH   A O    1 
HETATM 7054 O O    . HOH   E 4 .   ? 37.267 12.030  4.942   1.00 26.11 ?  389 HOH   A O    1 
HETATM 7055 O O    . HOH   E 4 .   ? 21.284 3.044   -0.291  1.00 15.97 ?  390 HOH   A O    1 
HETATM 7056 O O    . HOH   E 4 .   ? 16.517 -21.992 0.911   1.00 32.28 ?  391 HOH   A O    1 
HETATM 7057 O O    . HOH   E 4 .   ? 13.753 -4.819  17.331  1.00 29.95 ?  392 HOH   A O    1 
HETATM 7058 O O    . HOH   E 4 .   ? 21.133 10.259  14.987  1.00 36.95 ?  393 HOH   A O    1 
HETATM 7059 O O    . HOH   E 4 .   ? 16.159 16.590  8.453   1.00 45.95 ?  394 HOH   A O    1 
HETATM 7060 O O    . HOH   E 4 .   ? 15.224 -8.101  -9.959  1.00 25.62 ?  395 HOH   A O    1 
HETATM 7061 O O    A HOH   E 4 .   ? 17.474 -1.668  0.407   0.56 19.25 ?  396 HOH   A O    1 
HETATM 7062 O O    . HOH   E 4 .   ? 15.124 -21.411 14.180  1.00 21.07 ?  397 HOH   A O    1 
HETATM 7063 O O    . HOH   E 4 .   ? 37.506 -2.059  5.900   1.00 30.02 ?  398 HOH   A O    1 
HETATM 7064 O O    . HOH   E 4 .   ? 27.950 0.823   -7.172  1.00 15.40 ?  399 HOH   A O    1 
HETATM 7065 O O    . HOH   E 4 .   ? 23.455 11.404  4.017   1.00 14.21 ?  400 HOH   A O    1 
HETATM 7066 O O    A HOH   E 4 .   ? 7.967  -12.545 -0.913  0.56 17.88 ?  401 HOH   A O    1 
HETATM 7067 O O    . HOH   E 4 .   ? -1.565 -4.774  7.442   1.00 49.82 ?  402 HOH   A O    1 
HETATM 7068 O O    A HOH   E 4 .   ? 11.043 -0.326  1.885   0.70 25.79 ?  403 HOH   A O    1 
HETATM 7069 O O    . HOH   E 4 .   ? 6.292  -5.432  10.881  1.00 19.82 ?  404 HOH   A O    1 
HETATM 7070 O O    . HOH   E 4 .   ? 23.927 -20.237 -1.389  1.00 19.39 ?  405 HOH   A O    1 
HETATM 7071 O O    . HOH   E 4 .   ? 30.557 1.937   16.701  1.00 22.39 ?  406 HOH   A O    1 
HETATM 7072 O O    . HOH   E 4 .   ? 27.256 2.376   18.721  1.00 33.03 ?  407 HOH   A O    1 
HETATM 7073 O O    . HOH   E 4 .   ? 32.711 -9.222  5.957   1.00 20.35 ?  408 HOH   A O    1 
HETATM 7074 O O    . HOH   E 4 .   ? 20.507 -19.976 2.732   1.00 22.08 ?  409 HOH   A O    1 
HETATM 7075 O O    . HOH   E 4 .   ? 14.515 -0.604  -12.352 1.00 23.42 ?  410 HOH   A O    1 
HETATM 7076 O O    . HOH   E 4 .   ? 10.356 -13.678 -1.836  1.00 18.39 ?  411 HOH   A O    1 
HETATM 7077 O O    . HOH   E 4 .   ? 26.889 4.207   -0.692  1.00 13.78 ?  412 HOH   A O    1 
HETATM 7078 O O    . HOH   E 4 .   ? 14.472 -24.590 11.570  1.00 46.18 ?  413 HOH   A O    1 
HETATM 7079 O O    . HOH   E 4 .   ? 44.863 -0.674  3.066   1.00 42.12 ?  414 HOH   A O    1 
HETATM 7080 O O    . HOH   E 4 .   ? 32.688 -4.270  -9.865  1.00 30.46 ?  415 HOH   A O    1 
HETATM 7081 O O    . HOH   E 4 .   ? 30.222 -12.836 13.538  1.00 21.16 ?  416 HOH   A O    1 
HETATM 7082 O O    . HOH   E 4 .   ? 41.567 1.495   5.025   1.00 39.71 ?  417 HOH   A O    1 
HETATM 7083 O O    . HOH   E 4 .   ? 30.953 6.182   -12.219 1.00 28.84 ?  418 HOH   A O    1 
HETATM 7084 O O    . HOH   E 4 .   ? 5.390  2.961   4.621   1.00 36.87 ?  419 HOH   A O    1 
HETATM 7085 O O    . HOH   E 4 .   ? 15.955 6.877   2.874   1.00 18.87 ?  420 HOH   A O    1 
HETATM 7086 O O    . HOH   E 4 .   ? 18.209 4.336   -15.264 1.00 58.59 ?  421 HOH   A O    1 
HETATM 7087 O O    . HOH   E 4 .   ? 38.105 -1.321  -1.892  1.00 20.45 ?  422 HOH   A O    1 
HETATM 7088 O O    . HOH   E 4 .   ? 29.951 -10.019 13.067  1.00 24.72 ?  423 HOH   A O    1 
HETATM 7089 O O    . HOH   E 4 .   ? 35.108 -5.223  -3.077  1.00 18.95 ?  424 HOH   A O    1 
HETATM 7090 O O    . HOH   E 4 .   ? 36.666 -4.925  5.430   1.00 25.27 ?  425 HOH   A O    1 
HETATM 7091 O O    . HOH   E 4 .   ? 40.911 -8.230  -6.889  1.00 37.05 ?  426 HOH   A O    1 
HETATM 7092 O O    . HOH   E 4 .   ? 15.841 2.127   24.659  1.00 47.72 ?  427 HOH   A O    1 
HETATM 7093 O O    A HOH   E 4 .   ? 18.846 2.076   -0.791  0.56 12.24 ?  428 HOH   A O    1 
HETATM 7094 O O    A HOH   E 4 .   ? 15.770 -0.889  5.231   0.56 18.05 ?  429 HOH   A O    1 
HETATM 7095 O O    . HOH   E 4 .   ? 24.010 3.930   -4.824  1.00 20.73 ?  430 HOH   A O    1 
HETATM 7096 O O    . HOH   E 4 .   ? 15.452 11.675  7.900   1.00 49.99 ?  431 HOH   A O    1 
HETATM 7097 O O    B HOH   E 4 .   ? 11.862 -1.659  -3.373  0.44 25.97 ?  432 HOH   A O    1 
HETATM 7098 O O    . HOH   E 4 .   ? 32.446 -10.608 3.312   1.00 33.49 ?  433 HOH   A O    1 
HETATM 7099 O O    . HOH   E 4 .   ? 11.521 -10.678 16.840  1.00 27.65 ?  434 HOH   A O    1 
HETATM 7100 O O    . HOH   E 4 .   ? 18.314 -15.838 16.132  1.00 43.92 ?  435 HOH   A O    1 
HETATM 7101 O O    . HOH   E 4 .   ? 16.182 -14.168 20.116  1.00 55.97 ?  436 HOH   A O    1 
HETATM 7102 O O    . HOH   E 4 .   ? 22.518 8.233   18.329  1.00 46.48 ?  437 HOH   A O    1 
HETATM 7103 O O    . HOH   E 4 .   ? 21.381 -14.656 17.776  1.00 53.59 ?  438 HOH   A O    1 
HETATM 7104 O O    . HOH   E 4 .   ? 26.987 -3.160  19.475  1.00 40.76 ?  439 HOH   A O    1 
HETATM 7105 O O    . HOH   E 4 .   ? 23.407 -20.863 1.313   1.00 21.38 ?  440 HOH   A O    1 
HETATM 7106 O O    . HOH   E 4 .   ? 37.710 -8.793  -3.362  1.00 24.47 ?  441 HOH   A O    1 
HETATM 7107 O O    . HOH   E 4 .   ? 23.423 -7.986  17.068  1.00 25.13 ?  442 HOH   A O    1 
HETATM 7108 O O    . HOH   E 4 .   ? 34.393 -8.048  -0.547  1.00 30.91 ?  443 HOH   A O    1 
HETATM 7109 O O    . HOH   E 4 .   ? 23.224 7.358   -3.259  1.00 37.56 ?  444 HOH   A O    1 
HETATM 7110 O O    . HOH   E 4 .   ? 20.505 -17.621 24.830  1.00 58.12 ?  445 HOH   A O    1 
HETATM 7111 O O    A HOH   E 4 .   ? 14.001 -0.284  3.418   0.26 19.73 ?  446 HOH   A O    1 
HETATM 7112 O O    . HOH   E 4 .   ? 30.536 14.775  2.689   1.00 21.22 ?  447 HOH   A O    1 
HETATM 7113 O O    . HOH   E 4 .   ? 31.321 -12.782 0.021   1.00 22.94 ?  448 HOH   A O    1 
HETATM 7114 O O    . HOH   E 4 .   ? 21.345 -9.066  21.297  1.00 57.63 ?  449 HOH   A O    1 
HETATM 7115 O O    . HOH   E 4 .   ? 29.797 -1.875  -12.755 1.00 49.58 ?  450 HOH   A O    1 
HETATM 7116 O O    . HOH   E 4 .   ? 32.385 -15.832 10.932  1.00 31.80 ?  451 HOH   A O    1 
HETATM 7117 O O    . HOH   E 4 .   ? 25.351 8.216   -4.886  1.00 42.52 ?  452 HOH   A O    1 
HETATM 7118 O O    . HOH   E 4 .   ? 29.763 -16.040 10.899  1.00 36.59 ?  453 HOH   A O    1 
HETATM 7119 O O    . HOH   E 4 .   ? 24.663 5.692   20.676  1.00 54.88 ?  454 HOH   A O    1 
HETATM 7120 O O    . HOH   E 4 .   ? 27.842 7.089   -6.635  1.00 43.79 ?  455 HOH   A O    1 
HETATM 7121 O O    B HOH   E 4 .   ? 18.497 2.219   -0.946  0.44 18.28 ?  456 HOH   A O    1 
HETATM 7122 O O    . HOH   E 4 .   ? 19.858 -17.328 -5.125  1.00 25.96 ?  457 HOH   A O    1 
HETATM 7123 O O    . HOH   E 4 .   ? 27.327 -11.219 16.690  1.00 40.30 ?  458 HOH   A O    1 
HETATM 7124 O O    . HOH   E 4 .   ? 21.872 5.079   -5.868  1.00 36.91 ?  459 HOH   A O    1 
HETATM 7125 O O    . HOH   E 4 .   ? 11.015 -14.933 -6.192  1.00 38.75 ?  460 HOH   A O    1 
HETATM 7126 O O    . HOH   E 4 .   ? 23.144 -22.432 -3.221  1.00 40.28 ?  461 HOH   A O    1 
HETATM 7127 O O    . HOH   E 4 .   ? 24.574 14.776  7.753   1.00 39.62 ?  462 HOH   A O    1 
HETATM 7128 O O    . HOH   E 4 .   ? 39.632 -7.015  -3.454  1.00 48.21 ?  463 HOH   A O    1 
HETATM 7129 O O    . HOH   E 4 .   ? 18.770 11.050  11.183  1.00 32.99 ?  464 HOH   A O    1 
HETATM 7130 O O    . HOH   E 4 .   ? 15.771 -21.508 3.646   1.00 28.14 ?  465 HOH   A O    1 
HETATM 7131 O O    . HOH   E 4 .   ? 18.135 -16.149 -8.986  1.00 42.61 ?  466 HOH   A O    1 
HETATM 7132 O O    . HOH   E 4 .   ? 26.945 11.698  -1.434  1.00 37.29 ?  467 HOH   A O    1 
HETATM 7133 O O    . HOH   E 4 .   ? 12.164 1.587   17.240  1.00 42.70 ?  468 HOH   A O    1 
HETATM 7134 O O    . HOH   E 4 .   ? 23.379 13.742  5.484   1.00 19.96 ?  469 HOH   A O    1 
HETATM 7135 O O    . HOH   E 4 .   ? 12.041 -13.254 16.289  1.00 54.37 ?  470 HOH   A O    1 
HETATM 7136 O O    . HOH   E 4 .   ? 23.088 11.797  -4.084  1.00 22.33 ?  471 HOH   A O    1 
HETATM 7137 O O    . HOH   E 4 .   ? 25.791 10.802  -3.817  1.00 30.94 ?  472 HOH   A O    1 
HETATM 7138 O O    . HOH   E 4 .   ? 8.073  -3.261  -5.973  1.00 47.81 ?  473 HOH   A O    1 
HETATM 7139 O O    . HOH   E 4 .   ? 16.863 -20.409 16.057  1.00 32.88 ?  474 HOH   A O    1 
HETATM 7140 O O    . HOH   E 4 .   ? 35.127 7.469   12.223  1.00 40.10 ?  475 HOH   A O    1 
HETATM 7141 O O    . HOH   E 4 .   ? 28.747 9.066   17.555  1.00 39.45 ?  476 HOH   A O    1 
HETATM 7142 O O    . HOH   E 4 .   ? 15.788 -17.132 -7.095  1.00 34.49 ?  477 HOH   A O    1 
HETATM 7143 O O    . HOH   E 4 .   ? 17.421 -18.682 19.771  1.00 56.94 ?  478 HOH   A O    1 
HETATM 7144 O O    . HOH   E 4 .   ? 40.975 -3.940  -0.414  1.00 41.39 ?  479 HOH   A O    1 
HETATM 7145 O O    . HOH   E 4 .   ? 16.174 -23.367 5.776   1.00 32.97 ?  480 HOH   A O    1 
HETATM 7146 O O    . HOH   E 4 .   ? 13.823 -25.085 8.915   1.00 36.37 ?  481 HOH   A O    1 
HETATM 7147 O O    . HOH   E 4 .   ? 31.472 -0.544  -10.556 1.00 31.47 ?  482 HOH   A O    1 
HETATM 7148 O O    . HOH   E 4 .   ? 13.916 -10.347 -11.011 1.00 36.24 ?  483 HOH   A O    1 
HETATM 7149 O O    . HOH   E 4 .   ? 30.782 0.755   19.214  1.00 41.49 ?  484 HOH   A O    1 
HETATM 7150 O O    . HOH   E 4 .   ? 20.056 -22.268 4.256   1.00 33.24 ?  485 HOH   A O    1 
HETATM 7151 O O    . HOH   E 4 .   ? 44.525 10.452  -1.563  1.00 35.62 ?  486 HOH   A O    1 
HETATM 7152 O O    . HOH   E 4 .   ? 39.137 2.436   7.351   1.00 33.67 ?  487 HOH   A O    1 
HETATM 7153 O O    . HOH   E 4 .   ? 28.759 -7.972  -15.292 1.00 52.31 ?  488 HOH   A O    1 
HETATM 7154 O O    . HOH   E 4 .   ? 16.141 -6.791  -12.051 1.00 43.83 ?  489 HOH   A O    1 
HETATM 7155 O O    . HOH   E 4 .   ? 41.729 9.360   -3.941  1.00 31.54 ?  490 HOH   A O    1 
HETATM 7156 O O    . HOH   E 4 .   ? 18.354 -23.092 1.918   1.00 53.38 ?  491 HOH   A O    1 
HETATM 7157 O O    . HOH   E 4 .   ? 23.160 -12.818 19.299  1.00 51.26 ?  492 HOH   A O    1 
HETATM 7158 O O    . HOH   E 4 .   ? 28.608 -4.686  -12.333 1.00 41.01 ?  493 HOH   A O    1 
HETATM 7159 O O    . HOH   E 4 .   ? 25.729 -18.827 -11.854 1.00 42.25 ?  494 HOH   A O    1 
HETATM 7160 O O    . HOH   E 4 .   ? 40.621 -0.315  -7.699  1.00 35.08 ?  495 HOH   A O    1 
HETATM 7161 O O    B HOH   E 4 .   ? 14.727 7.876   4.937   0.44 26.72 ?  496 HOH   A O    1 
HETATM 7162 O O    . HOH   E 4 .   ? 37.365 -6.576  7.625   1.00 29.90 ?  497 HOH   A O    1 
HETATM 7163 O O    . HOH   E 4 .   ? 30.762 -5.816  -11.921 1.00 48.72 ?  498 HOH   A O    1 
HETATM 7164 O O    . HOH   E 4 .   ? 39.483 -0.012  6.667   1.00 33.54 ?  499 HOH   A O    1 
HETATM 7165 O O    . HOH   E 4 .   ? 37.947 13.913  6.734   1.00 38.42 ?  500 HOH   A O    1 
HETATM 7166 O O    . HOH   E 4 .   ? 20.604 -16.051 -7.468  1.00 30.28 ?  501 HOH   A O    1 
HETATM 7167 O O    . HOH   E 4 .   ? 30.736 5.804   -14.754 1.00 38.75 ?  502 HOH   A O    1 
HETATM 7168 O O    . HOH   E 4 .   ? 28.943 14.463  0.797   1.00 51.10 ?  503 HOH   A O    1 
HETATM 7169 O O    . HOH   E 4 .   ? 22.020 -23.946 4.552   1.00 30.60 ?  504 HOH   A O    1 
HETATM 7170 O O    . HOH   E 4 .   ? 36.330 -6.505  10.286  1.00 50.46 ?  505 HOH   A O    1 
HETATM 7171 O O    T HOH   E 4 .   ? 11.906 -2.105  -3.698  0.30 13.46 ?  506 HOH   A O    1 
HETATM 7172 O O    . HOH   E 4 .   ? 17.263 -6.622  -14.190 1.00 45.50 ?  507 HOH   A O    1 
HETATM 7173 O O    A HOH   E 4 .   ? 14.829 8.707   4.830   0.56 36.73 ?  508 HOH   A O    1 
HETATM 7174 O O    . HOH   E 4 .   ? 24.088 9.093   -7.219  1.00 42.30 ?  509 HOH   A O    1 
HETATM 7175 O O    . HOH   E 4 .   ? 15.745 -12.301 27.331  1.00 46.16 ?  510 HOH   A O    1 
HETATM 7176 O O    . HOH   E 4 .   ? 16.283 -21.129 18.743  1.00 45.05 ?  511 HOH   A O    1 
HETATM 7177 O O    . HOH   E 4 .   ? 14.703 -22.694 19.903  1.00 38.60 ?  512 HOH   A O    1 
HETATM 7178 O O    . HOH   F 4 .   ? 29.831 -22.406 5.549   1.00 21.95 ?  201 HOH   B O    1 
HETATM 7179 O O    . HOH   F 4 .   ? 37.933 -39.371 -0.127  1.00 40.66 ?  202 HOH   B O    1 
HETATM 7180 O O    . HOH   F 4 .   ? 41.634 -36.096 -17.081 1.00 36.32 ?  203 HOH   B O    1 
HETATM 7181 O O    . HOH   F 4 .   ? 27.654 -29.120 -1.764  1.00 35.77 ?  204 HOH   B O    1 
HETATM 7182 O O    . HOH   F 4 .   ? 30.980 -28.686 4.496   1.00 32.56 ?  205 HOH   B O    1 
HETATM 7183 O O    . HOH   F 4 .   ? 48.074 -6.877  15.545  1.00 28.34 ?  206 HOH   B O    1 
HETATM 7184 O O    . HOH   F 4 .   ? 52.923 -13.472 -20.308 1.00 36.55 ?  207 HOH   B O    1 
HETATM 7185 O O    . HOH   F 4 .   ? 59.111 -18.684 6.890   1.00 37.04 ?  208 HOH   B O    1 
HETATM 7186 O O    . HOH   F 4 .   ? 50.165 -3.360  7.181   1.00 36.63 ?  209 HOH   B O    1 
HETATM 7187 O O    . HOH   F 4 .   ? 29.970 -26.243 4.150   1.00 30.46 ?  210 HOH   B O    1 
HETATM 7188 O O    . HOH   F 4 .   ? 58.183 -12.874 8.432   1.00 32.39 ?  211 HOH   B O    1 
HETATM 7189 O O    . HOH   F 4 .   ? 41.214 -7.849  5.473   1.00 41.48 ?  212 HOH   B O    1 
HETATM 7190 O O    . HOH   F 4 .   ? 30.188 -40.987 -7.961  1.00 19.39 ?  213 HOH   B O    1 
HETATM 7191 O O    . HOH   F 4 .   ? 54.492 -9.421  -8.670  1.00 20.03 ?  214 HOH   B O    1 
HETATM 7192 O O    . HOH   F 4 .   ? 27.894 -41.855 -15.094 1.00 37.33 ?  215 HOH   B O    1 
HETATM 7193 O O    . HOH   F 4 .   ? 37.112 -19.847 -18.073 1.00 42.09 ?  216 HOH   B O    1 
HETATM 7194 O O    . HOH   F 4 .   ? 57.705 -24.467 5.065   1.00 39.27 ?  217 HOH   B O    1 
HETATM 7195 O O    . HOH   F 4 .   ? 56.371 -19.724 7.158   1.00 30.30 ?  218 HOH   B O    1 
HETATM 7196 O O    . HOH   F 4 .   ? 56.658 -30.772 -7.696  1.00 30.21 ?  219 HOH   B O    1 
HETATM 7197 O O    . HOH   F 4 .   ? 34.803 -24.610 13.881  1.00 41.77 ?  220 HOH   B O    1 
HETATM 7198 O O    . HOH   F 4 .   ? 26.498 -19.305 -1.754  1.00 15.82 ?  221 HOH   B O    1 
HETATM 7199 O O    . HOH   F 4 .   ? 49.422 -22.760 -19.749 1.00 50.34 ?  222 HOH   B O    1 
HETATM 7200 O O    . HOH   F 4 .   ? 34.505 -36.371 -7.093  1.00 20.88 ?  223 HOH   B O    1 
HETATM 7201 O O    . HOH   F 4 .   ? 41.490 -39.212 -14.766 1.00 24.11 ?  224 HOH   B O    1 
HETATM 7202 O O    . HOH   F 4 .   ? 57.173 -26.916 -7.616  1.00 42.31 ?  225 HOH   B O    1 
HETATM 7203 O O    . HOH   F 4 .   ? 32.740 -43.752 -11.236 1.00 24.64 ?  226 HOH   B O    1 
HETATM 7204 O O    . HOH   F 4 .   ? 50.678 -6.073  0.184   1.00 29.31 ?  227 HOH   B O    1 
HETATM 7205 O O    . HOH   F 4 .   ? 44.860 -43.587 -10.392 1.00 28.84 ?  228 HOH   B O    1 
HETATM 7206 O O    . HOH   F 4 .   ? 51.621 -6.433  4.377   1.00 21.76 ?  229 HOH   B O    1 
HETATM 7207 O O    . HOH   F 4 .   ? 44.449 -7.068  2.037   1.00 35.92 ?  230 HOH   B O    1 
HETATM 7208 O O    . HOH   F 4 .   ? 57.397 -16.316 -12.215 1.00 19.27 ?  231 HOH   B O    1 
HETATM 7209 O O    . HOH   F 4 .   ? 34.271 -18.295 11.459  1.00 26.56 ?  232 HOH   B O    1 
HETATM 7210 O O    . HOH   F 4 .   ? 44.497 -27.750 -0.645  1.00 24.19 ?  233 HOH   B O    1 
HETATM 7211 O O    . HOH   F 4 .   ? 25.387 -25.861 -1.194  1.00 35.42 ?  234 HOH   B O    1 
HETATM 7212 O O    . HOH   F 4 .   ? 35.097 -7.993  -2.967  1.00 19.33 ?  235 HOH   B O    1 
HETATM 7213 O O    . HOH   F 4 .   ? 46.404 -1.524  13.148  1.00 29.28 ?  236 HOH   B O    1 
HETATM 7214 O O    . HOH   F 4 .   ? 50.724 -12.967 -0.452  1.00 12.73 ?  237 HOH   B O    1 
HETATM 7215 O O    . HOH   F 4 .   ? 38.475 -11.062 -2.235  1.00 20.41 ?  238 HOH   B O    1 
HETATM 7216 O O    . HOH   F 4 .   ? 55.380 -16.554 -14.264 1.00 33.20 ?  239 HOH   B O    1 
HETATM 7217 O O    . HOH   F 4 .   ? 57.621 -24.350 -3.728  1.00 22.21 ?  240 HOH   B O    1 
HETATM 7218 O O    . HOH   F 4 .   ? 39.301 -10.892 6.154   1.00 24.77 ?  241 HOH   B O    1 
HETATM 7219 O O    . HOH   F 4 .   ? 48.574 -36.469 -15.482 1.00 46.71 ?  242 HOH   B O    1 
HETATM 7220 O O    . HOH   F 4 .   ? 31.758 -17.787 -14.384 1.00 30.28 ?  243 HOH   B O    1 
HETATM 7221 O O    . HOH   F 4 .   ? 50.892 -39.929 -8.083  1.00 37.50 ?  244 HOH   B O    1 
HETATM 7222 O O    . HOH   F 4 .   ? 42.554 -25.330 2.726   1.00 16.61 ?  245 HOH   B O    1 
HETATM 7223 O O    . HOH   F 4 .   ? 47.394 -7.265  -3.745  1.00 41.80 ?  246 HOH   B O    1 
HETATM 7224 O O    . HOH   F 4 .   ? 40.351 -12.770 -11.482 1.00 16.80 ?  247 HOH   B O    1 
HETATM 7225 O O    . HOH   F 4 .   ? 40.552 -16.066 14.120  1.00 26.32 ?  248 HOH   B O    1 
HETATM 7226 O O    . HOH   F 4 .   ? 42.970 -43.236 -8.109  1.00 30.51 ?  249 HOH   B O    1 
HETATM 7227 O O    . HOH   F 4 .   ? 42.617 -22.825 3.915   1.00 13.22 ?  250 HOH   B O    1 
HETATM 7228 O O    . HOH   F 4 .   ? 29.783 -34.151 -0.343  1.00 41.06 ?  251 HOH   B O    1 
HETATM 7229 O O    . HOH   F 4 .   ? 41.343 -9.586  13.152  1.00 24.00 ?  252 HOH   B O    1 
HETATM 7230 O O    . HOH   F 4 .   ? 46.855 -29.523 9.824   1.00 35.23 ?  253 HOH   B O    1 
HETATM 7231 O O    . HOH   F 4 .   ? 45.122 -34.922 6.824   1.00 46.73 ?  254 HOH   B O    1 
HETATM 7232 O O    . HOH   F 4 .   ? 28.413 -19.688 -13.125 1.00 26.65 ?  255 HOH   B O    1 
HETATM 7233 O O    . HOH   F 4 .   ? 39.502 -11.073 0.367   1.00 17.81 ?  256 HOH   B O    1 
HETATM 7234 O O    . HOH   F 4 .   ? 41.846 -23.463 9.353   1.00 21.34 ?  257 HOH   B O    1 
HETATM 7235 O O    . HOH   F 4 .   ? 58.197 -10.636 -4.019  1.00 21.42 ?  258 HOH   B O    1 
HETATM 7236 O O    . HOH   F 4 .   ? 30.507 -42.207 -10.542 1.00 32.70 ?  259 HOH   B O    1 
HETATM 7237 O O    . HOH   F 4 .   ? 30.837 -15.697 2.702   1.00 15.57 ?  260 HOH   B O    1 
HETATM 7238 O O    . HOH   F 4 .   ? 35.987 -43.425 -8.270  1.00 38.58 ?  261 HOH   B O    1 
HETATM 7239 O O    . HOH   F 4 .   ? 27.107 -31.810 -9.851  1.00 21.86 ?  262 HOH   B O    1 
HETATM 7240 O O    . HOH   F 4 .   ? 47.899 -24.519 -17.728 1.00 35.09 ?  263 HOH   B O    1 
HETATM 7241 O O    . HOH   F 4 .   ? 29.719 -25.189 -10.719 1.00 18.90 ?  264 HOH   B O    1 
HETATM 7242 O O    . HOH   F 4 .   ? 34.964 -33.315 -19.072 1.00 33.93 ?  265 HOH   B O    1 
HETATM 7243 O O    . HOH   F 4 .   ? 51.486 -13.782 11.025  1.00 27.38 ?  266 HOH   B O    1 
HETATM 7244 O O    . HOH   F 4 .   ? 42.318 -9.877  9.412   1.00 21.77 ?  267 HOH   B O    1 
HETATM 7245 O O    . HOH   F 4 .   ? 56.134 -23.621 -14.673 1.00 28.61 ?  268 HOH   B O    1 
HETATM 7246 O O    . HOH   F 4 .   ? 43.396 -15.815 -12.172 1.00 15.10 ?  269 HOH   B O    1 
HETATM 7247 O O    . HOH   F 4 .   ? 49.687 -0.460  10.209  1.00 29.09 ?  270 HOH   B O    1 
HETATM 7248 O O    . HOH   F 4 .   ? 42.359 -34.661 3.866   1.00 27.42 ?  271 HOH   B O    1 
HETATM 7249 O O    . HOH   F 4 .   ? 56.888 -8.630  8.442   1.00 20.00 ?  272 HOH   B O    1 
HETATM 7250 O O    . HOH   F 4 .   ? 48.046 -22.739 5.872   1.00 19.74 ?  273 HOH   B O    1 
HETATM 7251 O O    . HOH   F 4 .   ? 28.243 -34.349 -9.299  1.00 19.25 ?  274 HOH   B O    1 
HETATM 7252 O O    . HOH   F 4 .   ? 38.904 -11.871 12.446  1.00 37.84 ?  275 HOH   B O    1 
HETATM 7253 O O    . HOH   F 4 .   ? 28.427 -30.949 -14.663 1.00 34.14 ?  276 HOH   B O    1 
HETATM 7254 O O    . HOH   F 4 .   ? 34.491 -12.740 2.705   1.00 24.44 ?  277 HOH   B O    1 
HETATM 7255 O O    . HOH   F 4 .   ? 43.157 -32.398 -17.048 1.00 27.42 ?  278 HOH   B O    1 
HETATM 7256 O O    . HOH   F 4 .   ? 57.483 -9.224  1.405   1.00 21.26 ?  279 HOH   B O    1 
HETATM 7257 O O    . HOH   F 4 .   ? 49.274 -28.702 -6.824  1.00 17.09 ?  280 HOH   B O    1 
HETATM 7258 O O    . HOH   F 4 .   ? 49.972 -24.640 5.850   1.00 35.26 ?  281 HOH   B O    1 
HETATM 7259 O O    . HOH   F 4 .   ? 46.581 -31.218 -4.737  1.00 24.20 ?  282 HOH   B O    1 
HETATM 7260 O O    . HOH   F 4 .   ? 27.952 -22.871 -7.927  1.00 20.12 ?  283 HOH   B O    1 
HETATM 7261 O O    . HOH   F 4 .   ? 48.377 -25.032 3.185   1.00 15.22 ?  284 HOH   B O    1 
HETATM 7262 O O    . HOH   F 4 .   ? 48.626 -12.107 -14.318 1.00 27.04 ?  285 HOH   B O    1 
HETATM 7263 O O    . HOH   F 4 .   ? 47.025 -33.959 -4.559  1.00 20.51 ?  286 HOH   B O    1 
HETATM 7264 O O    . HOH   F 4 .   ? 52.509 -10.353 12.986  1.00 23.89 ?  287 HOH   B O    1 
HETATM 7265 O O    . HOH   F 4 .   ? 33.534 -15.304 -13.903 1.00 22.86 ?  288 HOH   B O    1 
HETATM 7266 O O    . HOH   F 4 .   ? 57.056 -12.156 12.414  1.00 42.79 ?  289 HOH   B O    1 
HETATM 7267 O O    . HOH   F 4 .   ? 48.682 -19.984 6.014   1.00 15.25 ?  290 HOH   B O    1 
HETATM 7268 O O    . HOH   F 4 .   ? 45.287 -33.376 -15.892 1.00 27.00 ?  291 HOH   B O    1 
HETATM 7269 O O    . HOH   F 4 .   ? 41.116 -5.443  11.545  1.00 47.43 ?  292 HOH   B O    1 
HETATM 7270 O O    . HOH   F 4 .   ? 27.522 -26.550 -15.495 1.00 34.01 ?  293 HOH   B O    1 
HETATM 7271 O O    . HOH   F 4 .   ? 36.793 -12.719 -1.483  1.00 29.11 ?  294 HOH   B O    1 
HETATM 7272 O O    . HOH   F 4 .   ? 38.437 -12.208 -16.172 1.00 48.40 ?  295 HOH   B O    1 
HETATM 7273 O O    . HOH   F 4 .   ? 51.689 -6.044  -7.980  1.00 43.72 ?  296 HOH   B O    1 
HETATM 7274 O O    . HOH   F 4 .   ? 42.745 -12.270 -18.467 1.00 30.26 ?  297 HOH   B O    1 
HETATM 7275 O O    . HOH   F 4 .   ? 51.171 -37.630 -9.551  1.00 29.98 ?  298 HOH   B O    1 
HETATM 7276 O O    . HOH   F 4 .   ? 37.409 -17.872 13.154  1.00 35.10 ?  299 HOH   B O    1 
HETATM 7277 O O    . HOH   F 4 .   ? 62.684 -13.561 4.795   1.00 28.41 ?  300 HOH   B O    1 
HETATM 7278 O O    . HOH   F 4 .   ? 52.514 -35.684 -8.605  1.00 31.99 ?  301 HOH   B O    1 
HETATM 7279 O O    . HOH   F 4 .   ? 59.779 -15.251 8.223   1.00 32.99 ?  302 HOH   B O    1 
HETATM 7280 O O    . HOH   F 4 .   ? 53.011 -16.088 -12.735 1.00 27.80 ?  303 HOH   B O    1 
HETATM 7281 O O    . HOH   F 4 .   ? 37.324 -35.647 7.323   1.00 36.08 ?  304 HOH   B O    1 
HETATM 7282 O O    . HOH   F 4 .   ? 45.846 -40.346 -3.411  1.00 33.19 ?  305 HOH   B O    1 
HETATM 7283 O O    . HOH   F 4 .   ? 42.854 -20.172 -20.664 1.00 40.71 ?  306 HOH   B O    1 
HETATM 7284 O O    . HOH   F 4 .   ? 38.382 -9.377  -13.262 1.00 31.19 ?  307 HOH   B O    1 
HETATM 7285 O O    . HOH   F 4 .   ? 44.029 -29.329 -4.616  1.00 25.69 ?  308 HOH   B O    1 
HETATM 7286 O O    . HOH   F 4 .   ? 44.618 -27.429 2.092   1.00 17.66 ?  309 HOH   B O    1 
HETATM 7287 O O    . HOH   F 4 .   ? 53.468 -30.188 4.577   1.00 20.28 ?  310 HOH   B O    1 
HETATM 7288 O O    . HOH   F 4 .   ? 35.032 -33.574 4.709   1.00 32.91 ?  311 HOH   B O    1 
HETATM 7289 O O    . HOH   F 4 .   ? 43.195 -21.375 10.749  1.00 17.44 ?  312 HOH   B O    1 
HETATM 7290 O O    . HOH   F 4 .   ? 53.610 -12.613 -22.192 1.00 37.57 ?  313 HOH   B O    1 
HETATM 7291 O O    . HOH   F 4 .   ? 25.949 -21.430 -3.453  1.00 19.09 ?  314 HOH   B O    1 
HETATM 7292 O O    . HOH   F 4 .   ? 37.876 -10.220 -10.736 1.00 20.31 ?  315 HOH   B O    1 
HETATM 7293 O O    . HOH   F 4 .   ? 38.299 -12.648 7.958   1.00 19.77 ?  316 HOH   B O    1 
HETATM 7294 O O    . HOH   F 4 .   ? 52.431 -29.271 -13.047 1.00 27.37 ?  317 HOH   B O    1 
HETATM 7295 O O    . HOH   F 4 .   ? 40.262 -10.837 -9.510  1.00 19.26 ?  318 HOH   B O    1 
HETATM 7296 O O    . HOH   F 4 .   ? 42.463 -9.705  -14.784 1.00 45.25 ?  319 HOH   B O    1 
HETATM 7297 O O    . HOH   F 4 .   ? 36.965 -30.601 -20.942 1.00 33.31 ?  320 HOH   B O    1 
HETATM 7298 O O    . HOH   F 4 .   ? 41.707 -8.055  1.399   1.00 25.66 ?  321 HOH   B O    1 
HETATM 7299 O O    . HOH   F 4 .   ? 36.746 -12.370 4.296   1.00 19.23 ?  322 HOH   B O    1 
HETATM 7300 O O    . HOH   F 4 .   ? 26.341 -21.019 -6.195  1.00 18.74 ?  323 HOH   B O    1 
HETATM 7301 O O    . HOH   F 4 .   ? 44.115 -1.747  7.650   1.00 49.33 ?  324 HOH   B O    1 
HETATM 7302 O O    . HOH   F 4 .   ? 47.244 -24.432 8.257   1.00 27.16 ?  325 HOH   B O    1 
HETATM 7303 O O    . HOH   F 4 .   ? 44.641 -24.538 9.640   1.00 23.51 ?  326 HOH   B O    1 
HETATM 7304 O O    . HOH   F 4 .   ? 32.796 -34.578 -5.801  1.00 18.64 ?  327 HOH   B O    1 
HETATM 7305 O O    . HOH   F 4 .   ? 51.337 -33.085 -10.808 1.00 45.37 ?  328 HOH   B O    1 
HETATM 7306 O O    . HOH   F 4 .   ? 43.494 -15.410 18.128  1.00 32.39 ?  329 HOH   B O    1 
HETATM 7307 O O    . HOH   F 4 .   ? 27.729 -14.798 -9.481  1.00 39.18 ?  330 HOH   B O    1 
HETATM 7308 O O    . HOH   F 4 .   ? 43.117 -34.530 0.171   1.00 23.60 ?  331 HOH   B O    1 
HETATM 7309 O O    . HOH   F 4 .   ? 45.636 -36.320 -16.035 1.00 36.86 ?  332 HOH   B O    1 
HETATM 7310 O O    . HOH   F 4 .   ? 57.477 -21.934 3.509   1.00 33.90 ?  333 HOH   B O    1 
HETATM 7311 O O    . HOH   F 4 .   ? 62.876 -20.215 -0.672  1.00 38.49 ?  334 HOH   B O    1 
HETATM 7312 O O    . HOH   F 4 .   ? 59.962 -17.244 -10.492 1.00 35.86 ?  335 HOH   B O    1 
HETATM 7313 O O    . HOH   F 4 .   ? 33.676 -31.125 11.063  1.00 38.22 ?  336 HOH   B O    1 
HETATM 7314 O O    . HOH   F 4 .   ? 48.033 -32.756 -16.613 1.00 43.91 ?  337 HOH   B O    1 
HETATM 7315 O O    . HOH   F 4 .   ? 47.462 -27.396 2.082   1.00 16.81 ?  338 HOH   B O    1 
HETATM 7316 O O    . HOH   F 4 .   ? 37.008 -45.090 -9.679  1.00 36.28 ?  339 HOH   B O    1 
HETATM 7317 O O    . HOH   F 4 .   ? 42.853 -43.540 -14.277 1.00 43.34 ?  340 HOH   B O    1 
HETATM 7318 O O    . HOH   F 4 .   ? 41.233 -24.492 15.903  1.00 47.72 ?  341 HOH   B O    1 
HETATM 7319 O O    . HOH   F 4 .   ? 37.090 -15.178 -16.584 1.00 43.90 ?  342 HOH   B O    1 
HETATM 7320 O O    . HOH   F 4 .   ? 46.798 -19.887 12.339  1.00 32.67 ?  343 HOH   B O    1 
HETATM 7321 O O    . HOH   F 4 .   ? 28.883 -42.897 -12.351 1.00 44.76 ?  344 HOH   B O    1 
HETATM 7322 O O    . HOH   F 4 .   ? 34.447 -10.298 7.808   1.00 23.12 ?  345 HOH   B O    1 
HETATM 7323 O O    . HOH   F 4 .   ? 38.584 -22.362 15.010  1.00 43.46 ?  346 HOH   B O    1 
HETATM 7324 O O    . HOH   F 4 .   ? 32.981 -14.636 1.088   1.00 23.04 ?  347 HOH   B O    1 
HETATM 7325 O O    . HOH   F 4 .   ? 39.520 -23.590 -20.419 1.00 40.30 ?  348 HOH   B O    1 
HETATM 7326 O O    . HOH   F 4 .   ? 44.194 -37.386 -17.648 1.00 35.52 ?  349 HOH   B O    1 
HETATM 7327 O O    . HOH   F 4 .   ? 33.705 -9.574  -8.846  1.00 33.28 ?  350 HOH   B O    1 
HETATM 7328 O O    . HOH   F 4 .   ? 62.526 -20.079 -4.754  1.00 45.98 ?  351 HOH   B O    1 
HETATM 7329 O O    . HOH   F 4 .   ? 40.367 -43.494 -9.090  1.00 27.94 ?  352 HOH   B O    1 
HETATM 7330 O O    . HOH   F 4 .   ? 39.812 -44.268 -11.153 1.00 44.18 ?  353 HOH   B O    1 
HETATM 7331 O O    . HOH   F 4 .   ? 27.745 -26.583 -0.435  1.00 33.10 ?  354 HOH   B O    1 
HETATM 7332 O O    . HOH   F 4 .   ? 33.962 -7.856  11.490  1.00 42.60 ?  355 HOH   B O    1 
HETATM 7333 O O    . HOH   F 4 .   ? 55.708 -8.273  10.852  1.00 26.13 ?  356 HOH   B O    1 
HETATM 7334 O O    . HOH   F 4 .   ? 23.212 -23.584 6.882   1.00 35.23 ?  357 HOH   B O    1 
HETATM 7335 O O    . HOH   F 4 .   ? 36.144 -8.467  -9.704  1.00 36.37 ?  358 HOH   B O    1 
HETATM 7336 O O    . HOH   F 4 .   ? 56.556 -7.235  3.032   1.00 27.97 ?  359 HOH   B O    1 
HETATM 7337 O O    . HOH   F 4 .   ? 56.820 -21.610 -16.367 1.00 40.93 ?  360 HOH   B O    1 
HETATM 7338 O O    . HOH   F 4 .   ? 61.474 -19.888 1.849   1.00 37.62 ?  361 HOH   B O    1 
HETATM 7339 O O    . HOH   F 4 .   ? 27.109 -25.920 -11.221 1.00 35.40 ?  362 HOH   B O    1 
HETATM 7340 O O    . HOH   F 4 .   ? 40.284 -8.806  9.896   1.00 39.25 ?  363 HOH   B O    1 
HETATM 7341 O O    . HOH   F 4 .   ? 40.450 -11.286 -13.916 1.00 33.59 ?  364 HOH   B O    1 
HETATM 7342 O O    . HOH   F 4 .   ? 43.156 -12.656 -21.169 1.00 46.68 ?  365 HOH   B O    1 
HETATM 7343 O O    . HOH   F 4 .   ? 48.235 -26.390 8.919   1.00 44.81 ?  366 HOH   B O    1 
HETATM 7344 O O    . HOH   F 4 .   ? 36.129 -8.636  9.071   1.00 30.80 ?  367 HOH   B O    1 
HETATM 7345 O O    . HOH   F 4 .   ? 54.225 -5.717  2.962   1.00 36.79 ?  368 HOH   B O    1 
HETATM 7346 O O    . HOH   F 4 .   ? 58.871 -10.387 9.307   1.00 39.39 ?  369 HOH   B O    1 
HETATM 7347 O O    . HOH   F 4 .   ? 32.665 -23.559 14.109  1.00 41.48 ?  370 HOH   B O    1 
HETATM 7348 O O    . HOH   F 4 .   ? 39.863 -6.977  7.850   1.00 38.93 ?  371 HOH   B O    1 
HETATM 7349 O O    . HOH   F 4 .   ? 52.036 -12.922 13.341  1.00 28.96 ?  372 HOH   B O    1 
HETATM 7350 O O    . HOH   F 4 .   ? 63.025 -12.399 6.947   1.00 39.97 ?  373 HOH   B O    1 
HETATM 7351 O O    . HOH   F 4 .   ? 41.819 -10.019 -17.446 1.00 53.68 ?  374 HOH   B O    1 
HETATM 7352 O O    . HOH   F 4 .   ? 56.042 -7.759  -0.624  1.00 37.83 ?  375 HOH   B O    1 
HETATM 7353 O O    . HOH   F 4 .   ? 42.713 -17.222 -23.036 1.00 47.09 ?  376 HOH   B O    1 
HETATM 7354 O O    . HOH   F 4 .   ? 40.076 -7.720  3.196   1.00 41.53 ?  377 HOH   B O    1 
HETATM 7355 O O    . HOH   F 4 .   ? 38.005 -10.458 10.027  1.00 29.78 ?  378 HOH   B O    1 
HETATM 7356 O O    . HOH   F 4 .   ? 41.818 -6.668  -4.859  1.00 47.51 ?  379 HOH   B O    1 
HETATM 7357 O O    . HOH   F 4 .   ? 36.472 -22.798 13.346  1.00 36.90 ?  380 HOH   B O    1 
HETATM 7358 O O    . HOH   F 4 .   ? 44.007 -5.565  -3.521  1.00 42.35 ?  381 HOH   B O    1 
HETATM 7359 O O    . HOH   F 4 .   ? 52.856 -29.860 7.266   1.00 24.63 ?  382 HOH   B O    1 
HETATM 7360 O O    . HOH   F 4 .   ? 39.576 -13.975 15.687  1.00 55.11 ?  383 HOH   B O    1 
HETATM 7361 O O    . HOH   F 4 .   ? 46.772 -5.420  2.870   1.00 39.09 ?  384 HOH   B O    1 
HETATM 7362 O O    . HOH   F 4 .   ? 60.462 -22.238 2.910   1.00 46.66 ?  385 HOH   B O    1 
HETATM 7363 O O    . HOH   F 4 .   ? 40.993 -9.767  15.836  1.00 50.08 ?  386 HOH   B O    1 
HETATM 7364 O O    . HOH   F 4 .   ? 23.927 -20.834 -7.609  1.00 30.24 ?  387 HOH   B O    1 
HETATM 7365 O O    . HOH   F 4 .   ? 35.257 -20.355 13.322  1.00 37.93 ?  388 HOH   B O    1 
HETATM 7366 O O    . HOH   F 4 .   ? 35.372 -33.726 7.434   1.00 47.31 ?  389 HOH   B O    1 
HETATM 7367 O O    . HOH   F 4 .   ? 23.168 -23.755 1.546   1.00 35.61 ?  390 HOH   B O    1 
HETATM 7368 O O    . HOH   F 4 .   ? 40.703 -6.577  -0.838  1.00 28.40 ?  391 HOH   B O    1 
HETATM 7369 O O    . HOH   F 4 .   ? 44.090 -31.748 -3.780  1.00 39.93 ?  392 HOH   B O    1 
HETATM 7370 O O    . HOH   F 4 .   ? 26.596 -27.923 -13.407 1.00 37.17 ?  393 HOH   B O    1 
HETATM 7371 O O    . HOH   F 4 .   ? 27.929 -27.073 2.333   1.00 29.99 ?  394 HOH   B O    1 
HETATM 7372 O O    . HOH   F 4 .   ? 26.844 -30.642 -12.540 1.00 27.69 ?  395 HOH   B O    1 
HETATM 7373 O O    . HOH   F 4 .   ? 24.676 -20.592 -10.545 1.00 42.29 ?  396 HOH   B O    1 
HETATM 7374 O O    . HOH   F 4 .   ? 34.348 -33.450 9.664   1.00 38.83 ?  397 HOH   B O    1 
HETATM 7375 O O    . HOH   F 4 .   ? 50.695 -30.864 8.864   1.00 31.86 ?  398 HOH   B O    1 
HETATM 7376 O O    . HOH   F 4 .   ? 57.660 -6.523  -2.337  1.00 35.33 ?  399 HOH   B O    1 
HETATM 7377 O O    . HOH   F 4 .   ? 45.716 -20.116 15.273  1.00 50.47 ?  400 HOH   B O    1 
HETATM 7378 O O    . HOH   F 4 .   ? 40.909 -11.749 -22.218 1.00 41.40 ?  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   ? 0.7065 0.7273 0.8359 -0.0073 -0.0215 0.0612  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6987 0.7103 0.8171 -0.0139 -0.0165 0.0451  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.7013 0.7223 0.8256 -0.0078 -0.0220 0.0609  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6937 0.7057 0.8063 -0.0145 -0.0170 0.0445  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6801 0.7046 0.7856 -0.0156 -0.0221 0.0630  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6730 0.6883 0.7639 -0.0206 -0.0177 0.0453  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6849 0.7078 0.7993 -0.0147 -0.0232 0.0653  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6776 0.6916 0.7765 -0.0200 -0.0179 0.0469  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.7131 0.7317 0.8434 -0.0020 -0.0209 0.0594  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7051 0.7152 0.8258 -0.0102 -0.0157 0.0440  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.7170 0.7349 0.8536 -0.0008 -0.0199 0.0594  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7096 0.7192 0.8358 -0.0094 -0.0147 0.0443  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.7162 0.7337 0.8535 0.0007  -0.0200 0.0597  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7075 0.7169 0.8356 -0.0079 -0.0148 0.0445  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6515 0.6816 0.7149 -0.0255 -0.0192 0.0633  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6452 0.6654 0.6945 -0.0282 -0.0165 0.0453  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.6216 0.6567 0.6392 -0.0378 -0.0176 0.0608  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.6164 0.6407 0.6203 -0.0368 -0.0168 0.0433  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.5799 0.6232 0.5915 -0.0533 -0.0048 0.0476  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5781 0.6092 0.5711 -0.0476 -0.0059 0.0345  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.5847 0.6256 0.5877 -0.0516 -0.0074 0.0496  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.5821 0.6115 0.5665 -0.0473 -0.0075 0.0363  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.6318 0.6630 0.6084 -0.0371 -0.0280 0.0715  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6245 0.6456 0.5922 -0.0364 -0.0272 0.0504  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.6413 0.6680 0.5810 -0.0384 -0.0340 0.0801  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6322 0.6495 0.5676 -0.0370 -0.0342 0.0554  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.6464 0.6685 0.5700 -0.0393 -0.0363 0.0836  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6369 0.6502 0.5573 -0.0370 -0.0374 0.0574  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.6439 0.6715 0.5706 -0.0389 -0.0355 0.0846  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6335 0.6517 0.5594 -0.0371 -0.0355 0.0586  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.5309 0.5844 0.5465 -0.0717 0.0098  0.0350  5   SER   A N   
60   N N   B SER   A 5   ? 0.5339 0.5731 0.5276 -0.0593 0.0055  0.0248  5   SER   A N   
61   C CA  A SER   A 5   ? 0.4803 0.5435 0.5052 -0.0869 0.0251  0.0259  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4883 0.5359 0.4891 -0.0695 0.0157  0.0167  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4263 0.4952 0.4364 -0.1027 0.0435  0.0279  5   SER   A C   
64   C C   B SER   A 5   ? 0.4400 0.4933 0.4316 -0.0791 0.0292  0.0131  5   SER   A C   
65   O O   A SER   A 5   ? 0.4303 0.4990 0.4369 -0.1010 0.0479  0.0231  5   SER   A O   
66   O O   B SER   A 5   ? 0.4418 0.4951 0.4283 -0.0793 0.0306  0.0081  5   SER   A O   
67   C CB  A SER   A 5   ? 0.4851 0.5491 0.5240 -0.0847 0.0261  0.0166  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.4918 0.5399 0.5021 -0.0685 0.0152  0.0123  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.4886 0.5521 0.5397 -0.0828 0.0289  0.0100  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.4945 0.5417 0.5136 -0.0677 0.0158  0.0081  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3661 0.4416 0.3670 -0.1197 0.0547  0.0369  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3882 0.4483 0.3793 -0.0888 0.0383  0.0142  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.3095 0.3881 0.3016 -0.1332 0.0558  0.0514  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3382 0.4047 0.3380 -0.0951 0.0417  0.0162  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.2970 0.3751 0.2661 -0.1361 0.0624  0.0474  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3164 0.3874 0.3335 -0.0992 0.0522  0.0168  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.2998 0.3803 0.2714 -0.1412 0.0616  0.0513  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3153 0.3902 0.3293 -0.0982 0.0678  0.0201  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2756 0.3536 0.2771 -0.1350 0.0423  0.0633  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.3140 0.3806 0.3065 -0.0937 0.0363  0.0184  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2491 0.3278 0.2644 -0.1290 0.0309  0.0645  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2951 0.3585 0.2907 -0.0920 0.0268  0.0204  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2384 0.3169 0.2526 -0.1233 0.0234  0.0540  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2878 0.3468 0.2819 -0.0890 0.0214  0.0188  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2484 0.3209 0.2641 -0.1127 0.0410  0.0697  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2902 0.3511 0.2949 -0.0894 0.0287  0.0261  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2344 0.3108 0.2535 -0.1180 0.0234  0.0478  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2843 0.3415 0.2799 -0.0860 0.0229  0.0239  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2462 0.3158 0.2684 -0.1074 0.0339  0.0606  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2857 0.3443 0.2872 -0.0889 0.0289  0.0266  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2377 0.3079 0.2632 -0.1171 0.0175  0.0474  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2853 0.3425 0.2860 -0.0857 0.0233  0.0247  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2785 0.3561 0.2454 -0.1349 0.0687  0.0338  7   SER   A N   
122  N N   B SER   A 7   ? 0.2949 0.3664 0.3178 -0.1046 0.0502  0.0119  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2739 0.3452 0.2425 -0.1192 0.0774  0.0107  7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2782 0.3484 0.3129 -0.0995 0.0461  -0.0030 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2601 0.3200 0.2260 -0.0984 0.0859  0.0178  7   SER   A C   
126  C C   B SER   A 7   ? 0.2566 0.3156 0.2740 -0.0964 0.0470  -0.0055 7   SER   A C   
127  O O   A SER   A 7   ? 0.2791 0.3261 0.2388 -0.0852 0.0855  0.0228  7   SER   A O   
128  O O   B SER   A 7   ? 0.2592 0.3158 0.2885 -0.0972 0.0521  -0.0070 7   SER   A O   
129  C CB  A SER   A 7   ? 0.2904 0.3566 0.2566 -0.1212 0.0744  -0.0012 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.2884 0.3601 0.3528 -0.0904 0.0369  -0.0058 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.3111 0.3695 0.2982 -0.1108 0.0647  -0.0135 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.2972 0.3674 0.3832 -0.0866 0.0263  -0.0048 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2350 0.2922 0.2251 -0.0849 0.0727  0.0081  8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2310 0.2807 0.2328 -0.0916 0.0414  -0.0102 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.2226 0.2631 0.2239 -0.0595 0.0570  0.0051  8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2140 0.2533 0.2104 -0.0688 0.0384  -0.0056 8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1973 0.2327 0.2305 -0.0401 0.0438  0.0073  8   GLY   A C   
148  C C   B GLY   A 8   ? 0.1934 0.2287 0.1914 -0.0473 0.0342  -0.0030 8   GLY   A C   
149  O O   A GLY   A 8   ? 0.2009 0.2274 0.2401 -0.0206 0.0439  -0.0113 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.1972 0.2279 0.1917 -0.0280 0.0413  -0.0062 8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1719 0.2173 0.2383 -0.0302 0.0327  0.0330  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1758 0.2057 0.1903 -0.0388 0.0300  -0.0124 9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1495 0.2023 0.2124 -0.0225 0.0270  0.0334  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1658 0.1868 0.1817 -0.0273 0.0212  -0.0100 9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1466 0.1775 0.1905 -0.0096 0.0324  0.0346  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1628 0.1607 0.1628 -0.0158 0.0248  0.0148  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1714 0.1996 0.2177 -0.0068 0.0171  0.0318  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1758 0.1611 0.1482 -0.0108 0.0282  0.0100  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1468 0.2226 0.2239 -0.0153 0.0264  0.0340  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1581 0.1974 0.2109 -0.0187 0.0209  -0.0089 9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1521 0.2349 0.2248 -0.0161 0.0307  0.0319  9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1527 0.1999 0.2193 -0.0125 0.0306  -0.0004 9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1632 0.2416 0.2277 -0.0248 0.0352  0.0308  9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1550 0.1971 0.2201 -0.0257 0.0441  0.0001  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1449 0.2366 0.2249 -0.0120 0.0208  0.0373  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1556 0.1980 0.2295 -0.0166 0.0201  0.0051  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1680 0.2413 0.2296 -0.0249 0.0370  0.0242  9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1680 0.1984 0.2316 -0.0287 0.0480  -0.0089 9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1438 0.2357 0.2237 -0.0173 0.0228  0.0334  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1574 0.1998 0.2445 -0.0269 0.0207  -0.0018 9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1554 0.2370 0.2390 -0.0258 0.0395  0.0245  9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1685 0.1997 0.2525 -0.0327 0.0413  -0.0080 9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1584 0.2439 0.2656 -0.0388 0.0465  0.0176  9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1816 0.2031 0.2815 -0.0401 0.0431  -0.0147 9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1429 0.1584 0.1846 -0.0145 0.0342  0.0217  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1592 0.1515 0.1833 -0.0132 0.0167  0.0210  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1500 0.1592 0.1969 -0.0091 0.0104  0.0205  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1518 0.1510 0.1884 -0.0178 0.0204  0.0350  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1562 0.1537 0.1873 -0.0074 0.0092  0.0193  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1439 0.1429 0.1830 -0.0134 0.0305  0.0273  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1705 0.1391 0.1692 -0.0109 0.0314  0.0104  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1511 0.1396 0.1819 -0.0149 0.0556  0.0225  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1553 0.1701 0.2277 -0.0120 -0.0042 0.0329  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1570 0.1638 0.2217 -0.0198 -0.0042 0.0619  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1695 0.1874 0.2907 -0.0155 -0.0207 0.0366  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1685 0.1781 0.2655 -0.0102 -0.0423 0.0763  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1865 0.1980 0.3285 -0.0263 -0.0054 0.0404  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1830 0.1913 0.2927 -0.0119 -0.0259 0.0717  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1899 0.2067 0.3102 -0.0143 -0.0184 0.0272  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1874 0.1948 0.2757 -0.0047 -0.0565 0.0740  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1580 0.1547 0.1874 -0.0154 0.0108  0.0260  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1381 0.1410 0.1576 -0.0137 0.0314  0.0323  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1645 0.1440 0.1810 -0.0296 0.0133  0.0254  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1438 0.1371 0.1870 -0.0140 0.0325  0.0139  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1533 0.1409 0.1877 -0.0363 0.0135  0.0110  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1345 0.1496 0.2067 -0.0148 0.0355  -0.0144 11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1602 0.1521 0.2144 -0.0358 0.0064  0.0020  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1407 0.1588 0.2554 -0.0306 0.0496  -0.0299 11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1801 0.1358 0.1602 -0.0256 0.0035  0.0264  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1522 0.1333 0.1779 -0.0148 0.0379  0.0165  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1936 0.1435 0.1574 -0.0230 0.0088  0.0229  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1685 0.1359 0.1917 -0.0188 0.0339  0.0120  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.2076 0.1415 0.1585 -0.0093 0.0118  0.0103  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1855 0.1500 0.2050 -0.0129 0.0354  0.0233  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.2151 0.1471 0.1451 -0.0073 0.0212  0.0058  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1834 0.1568 0.2161 -0.0059 0.0345  0.0180  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.2145 0.1526 0.1557 0.0034  0.0212  0.0297  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.1766 0.1535 0.2057 0.0028  0.0254  0.0081  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1534 0.1455 0.1691 -0.0186 0.0075  0.0161  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1333 0.1446 0.1958 -0.0219 0.0359  0.0017  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1535 0.1608 0.1781 -0.0139 -0.0005 0.0281  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1437 0.1495 0.1891 -0.0187 0.0185  0.0107  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1567 0.1658 0.1652 -0.0238 0.0132  0.0266  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1559 0.1406 0.1799 -0.0293 0.0099  0.0019  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1659 0.1784 0.1692 -0.0221 0.0168  0.0129  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1616 0.1418 0.1767 -0.0208 0.0235  -0.0049 12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1695 0.1785 0.2042 -0.0116 0.0111  0.0443  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1491 0.1542 0.1943 -0.0223 0.0073  0.0169  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1732 0.1916 0.2388 -0.0116 0.0161  0.0565  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1610 0.1713 0.2114 -0.0088 0.0189  0.0271  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1841 0.1946 0.2122 -0.0129 0.0279  0.0641  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1718 0.1685 0.1964 -0.0023 0.0273  0.0425  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1727 0.2013 0.2604 -0.0169 0.0020  0.0593  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1664 0.1838 0.2305 -0.0119 0.0203  0.0282  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1479 0.1575 0.1476 -0.0168 0.0157  0.0140  13  THR   A N   
320  N N   B THR   A 13  ? 0.1565 0.1378 0.1908 -0.0291 0.0152  -0.0061 13  THR   A N   
321  C CA  A THR   A 13  ? 0.1527 0.1546 0.1746 -0.0243 0.0227  0.0025  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1542 0.1458 0.1963 -0.0228 0.0370  -0.0145 13  THR   A CA  
323  C C   A THR   A 13  ? 0.1536 0.1495 0.1844 -0.0176 0.0166  0.0191  13  THR   A C   
324  C C   B THR   A 13  ? 0.1480 0.1441 0.2051 -0.0233 0.0369  -0.0114 13  THR   A C   
325  O O   A THR   A 13  ? 0.1578 0.1488 0.1627 -0.0168 0.0093  0.0284  13  THR   A O   
326  O O   B THR   A 13  ? 0.1477 0.1505 0.2137 -0.0112 0.0386  -0.0118 13  THR   A O   
327  C CB  A THR   A 13  ? 0.1576 0.1675 0.1705 -0.0222 0.0252  0.0022  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1683 0.1580 0.2021 -0.0147 0.0227  -0.0085 13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1453 0.1671 0.1749 -0.0285 0.0268  0.0140  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1758 0.1512 0.1912 -0.0121 0.0122  -0.0029 13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1667 0.1837 0.1936 -0.0155 0.0272  -0.0049 13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1830 0.1762 0.2077 -0.0162 0.0303  -0.0118 13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1600 0.1496 0.2102 -0.0233 0.0238  0.0228  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1554 0.1526 0.2227 -0.0250 0.0301  0.0006  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1686 0.1530 0.2391 -0.0177 0.0187  0.0438  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1702 0.1690 0.2215 -0.0157 0.0170  0.0184  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1588 0.1567 0.2090 -0.0171 0.0100  0.0362  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1569 0.1601 0.1799 -0.0173 0.0151  0.0119  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1713 0.1691 0.2108 -0.0241 0.0197  0.0285  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1625 0.1688 0.1889 -0.0173 0.0337  0.0247  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.1955 0.1642 0.3048 -0.0172 0.0117  0.0585  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.1984 0.2016 0.2849 -0.0011 0.0048  0.0319  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.2183 0.1938 0.3658 -0.0245 0.0173  0.0625  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.2246 0.2362 0.3414 0.0036  0.0005  0.0354  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.2379 0.2131 0.3887 -0.0199 0.0094  0.0789  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.2386 0.2480 0.3659 0.0157  -0.0065 0.0472  14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.2300 0.2080 0.3942 -0.0151 -0.0035 0.0386  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.2321 0.2503 0.3561 0.0020  -0.0092 0.0310  14  ASP   A OD2 
371  N N   A ASN   A 15  ? 0.1454 0.1460 0.1925 -0.0113 0.0064  0.0337  15  ASN   A N   
372  N N   B ASN   A 15  ? 0.1474 0.1518 0.1628 -0.0231 0.0136  0.0061  15  ASN   A N   
373  C CA  A ASN   A 15  ? 0.1436 0.1462 0.1826 -0.0097 0.0067  0.0118  15  ASN   A CA  
374  C CA  B ASN   A 15  ? 0.1484 0.1430 0.1585 -0.0197 0.0233  -0.0020 15  ASN   A CA  
375  C C   A ASN   A 15  ? 0.1361 0.1433 0.1712 -0.0099 0.0115  0.0164  15  ASN   A C   
376  C C   B ASN   A 15  ? 0.1472 0.1397 0.1613 -0.0210 0.0178  -0.0140 15  ASN   A C   
377  O O   A ASN   A 15  ? 0.1476 0.1477 0.1694 -0.0126 -0.0010 0.0110  15  ASN   A O   
378  O O   B ASN   A 15  ? 0.1522 0.1389 0.1687 -0.0169 0.0031  -0.0154 15  ASN   A O   
379  C CB  A ASN   A 15  ? 0.1493 0.1540 0.1676 -0.0070 0.0062  0.0088  15  ASN   A CB  
380  C CB  B ASN   A 15  ? 0.1461 0.1370 0.1385 -0.0184 0.0329  0.0065  15  ASN   A CB  
381  C CG  A ASN   A 15  ? 0.1489 0.1666 0.1699 -0.0065 0.0074  -0.0037 15  ASN   A CG  
382  C CG  B ASN   A 15  ? 0.1535 0.1501 0.1525 -0.0165 0.0359  -0.0050 15  ASN   A CG  
383  O OD1 A ASN   A 15  ? 0.1565 0.1743 0.1766 -0.0188 0.0112  -0.0042 15  ASN   A OD1 
384  O OD1 B ASN   A 15  ? 0.1666 0.1490 0.1647 -0.0285 0.0264  -0.0147 15  ASN   A OD1 
385  N ND2 A ASN   A 15  ? 0.1505 0.1703 0.1622 -0.0037 0.0135  -0.0007 15  ASN   A ND2 
386  N ND2 B ASN   A 15  ? 0.1511 0.1640 0.1471 -0.0183 0.0345  -0.0039 15  ASN   A ND2 
399  N N   A VAL   A 16  ? 0.1374 0.1382 0.1683 -0.0125 0.0074  0.0227  16  VAL   A N   
400  N N   B VAL   A 16  ? 0.1465 0.1392 0.1567 -0.0259 0.0197  -0.0194 16  VAL   A N   
401  C CA  A VAL   A 16  ? 0.1426 0.1430 0.1538 -0.0201 0.0003  0.0156  16  VAL   A CA  
402  C CA  B VAL   A 16  ? 0.1438 0.1387 0.1454 -0.0207 0.0148  -0.0200 16  VAL   A CA  
403  C C   A VAL   A 16  ? 0.1373 0.1551 0.1652 -0.0161 0.0018  0.0084  16  VAL   A C   
404  C C   B VAL   A 16  ? 0.1419 0.1340 0.1557 -0.0174 0.0183  -0.0008 16  VAL   A C   
405  O O   A VAL   A 16  ? 0.1356 0.1602 0.1684 -0.0185 0.0219  -0.0036 16  VAL   A O   
406  O O   B VAL   A 16  ? 0.1422 0.1278 0.1409 -0.0211 0.0173  0.0092  16  VAL   A O   
407  C CB  A VAL   A 16  ? 0.1583 0.1491 0.1452 0.0001  0.0028  0.0143  16  VAL   A CB  
408  C CB  B VAL   A 16  ? 0.1513 0.1391 0.1501 -0.0089 0.0133  -0.0171 16  VAL   A CB  
409  C CG1 A VAL   A 16  ? 0.1655 0.1459 0.1401 -0.0015 0.0077  0.0085  16  VAL   A CG1 
410  C CG1 B VAL   A 16  ? 0.1562 0.1477 0.1680 -0.0087 0.0018  -0.0210 16  VAL   A CG1 
411  C CG2 A VAL   A 16  ? 0.1600 0.1683 0.1551 0.0099  0.0305  -0.0010 16  VAL   A CG2 
412  C CG2 B VAL   A 16  ? 0.1577 0.1294 0.1415 -0.0140 0.0351  -0.0090 16  VAL   A CG2 
431  N N   A TYR   A 17  ? 0.1415 0.1502 0.1866 -0.0118 0.0171  0.0192  17  TYR   A N   
432  N N   B TYR   A 17  ? 0.1389 0.1340 0.1585 -0.0134 0.0308  0.0054  17  TYR   A N   
433  C CA  A TYR   A 17  ? 0.1420 0.1438 0.1747 -0.0141 0.0114  0.0210  17  TYR   A CA  
434  C CA  B TYR   A 17  ? 0.1440 0.1392 0.1635 -0.0181 0.0349  0.0117  17  TYR   A CA  
435  C C   A TYR   A 17  ? 0.1409 0.1487 0.1922 -0.0096 0.0094  0.0331  17  TYR   A C   
436  C C   B TYR   A 17  ? 0.1523 0.1358 0.1794 -0.0168 0.0259  0.0010  17  TYR   A C   
437  O O   A TYR   A 17  ? 0.1348 0.1561 0.1716 -0.0148 0.0158  0.0347  17  TYR   A O   
438  O O   B TYR   A 17  ? 0.1522 0.1307 0.1781 -0.0180 0.0336  0.0077  17  TYR   A O   
439  C CB  A TYR   A 17  ? 0.1503 0.1419 0.1799 -0.0139 -0.0084 0.0222  17  TYR   A CB  
440  C CB  B TYR   A 17  ? 0.1479 0.1465 0.1767 -0.0075 0.0379  0.0189  17  TYR   A CB  
441  C CG  A TYR   A 17  ? 0.1615 0.1479 0.1762 -0.0128 -0.0183 0.0179  17  TYR   A CG  
442  C CG  B TYR   A 17  ? 0.1671 0.1652 0.2072 -0.0015 0.0328  0.0178  17  TYR   A CG  
443  C CD1 A TYR   A 17  ? 0.1706 0.1588 0.2009 -0.0120 -0.0161 0.0199  17  TYR   A CD1 
444  C CD1 B TYR   A 17  ? 0.1778 0.1768 0.2234 0.0166  0.0359  0.0075  17  TYR   A CD1 
445  C CD2 A TYR   A 17  ? 0.1688 0.1466 0.1770 -0.0240 -0.0052 0.0168  17  TYR   A CD2 
446  C CD2 B TYR   A 17  ? 0.1769 0.1716 0.2127 -0.0096 0.0371  0.0270  17  TYR   A CD2 
447  C CE1 A TYR   A 17  ? 0.1675 0.1654 0.2129 -0.0125 -0.0145 0.0239  17  TYR   A CE1 
448  C CE1 B TYR   A 17  ? 0.1878 0.1859 0.2295 0.0156  0.0305  0.0097  17  TYR   A CE1 
449  C CE2 A TYR   A 17  ? 0.1795 0.1528 0.1832 -0.0270 -0.0105 0.0135  17  TYR   A CE2 
450  C CE2 B TYR   A 17  ? 0.1888 0.1773 0.2307 -0.0031 0.0272  0.0222  17  TYR   A CE2 
451  C CZ  A TYR   A 17  ? 0.1805 0.1535 0.1861 -0.0208 -0.0113 0.0242  17  TYR   A CZ  
452  C CZ  B TYR   A 17  ? 0.1917 0.1841 0.2393 0.0064  0.0172  0.0259  17  TYR   A CZ  
453  O OH  A TYR   A 17  ? 0.2047 0.1557 0.2091 -0.0141 -0.0009 0.0182  17  TYR   A OH  
454  O OH  B TYR   A 17  ? 0.1994 0.1977 0.2590 0.0134  0.0197  0.0250  17  TYR   A OH  
473  N N   A ILE   A 18  ? 0.1334 0.1522 0.2135 -0.0079 0.0124  0.0603  18  ILE   A N   
474  N N   B ILE   A 18  ? 0.1597 0.1473 0.1919 -0.0195 0.0295  0.0308  18  ILE   A N   
475  C CA  A ILE   A 18  ? 0.1322 0.1529 0.2157 -0.0067 0.0083  0.0526  18  ILE   A CA  
476  C CA  B ILE   A 18  ? 0.1670 0.1531 0.2116 -0.0216 0.0255  0.0356  18  ILE   A CA  
477  C C   A ILE   A 18  ? 0.1281 0.1629 0.2232 -0.0107 0.0111  0.0550  18  ILE   A C   
478  C C   B ILE   A 18  ? 0.1631 0.1631 0.2327 -0.0260 0.0318  0.0350  18  ILE   A C   
479  O O   A ILE   A 18  ? 0.1200 0.1770 0.2362 -0.0161 0.0214  0.0686  18  ILE   A O   
480  O O   B ILE   A 18  ? 0.1611 0.1753 0.2530 -0.0258 0.0411  0.0398  18  ILE   A O   
481  C CB  A ILE   A 18  ? 0.1415 0.1550 0.2132 -0.0051 0.0147  0.0633  18  ILE   A CB  
482  C CB  B ILE   A 18  ? 0.1787 0.1568 0.2019 -0.0174 0.0233  0.0514  18  ILE   A CB  
483  C CG1 A ILE   A 18  ? 0.1558 0.1770 0.2178 0.0006  0.0039  0.0680  18  ILE   A CG1 
484  C CG1 B ILE   A 18  ? 0.1867 0.1721 0.2038 -0.0133 0.0155  0.0397  18  ILE   A CG1 
485  C CG2 A ILE   A 18  ? 0.1548 0.1668 0.2383 -0.0133 0.0145  0.0649  18  ILE   A CG2 
486  C CG2 B ILE   A 18  ? 0.1780 0.1472 0.2104 -0.0095 0.0265  0.0531  18  ILE   A CG2 
487  C CD1 A ILE   A 18  ? 0.1696 0.1935 0.2392 0.0043  -0.0018 0.0681  18  ILE   A CD1 
488  C CD1 B ILE   A 18  ? 0.2043 0.1876 0.2303 -0.0128 0.0122  0.0415  18  ILE   A CD1 
511  N N   A LYS   A 19  ? 0.1333 0.1588 0.2267 -0.0004 0.0251  0.0398  19  LYS   A N   
512  N N   B LYS   A 19  ? 0.1672 0.1681 0.2418 -0.0213 0.0369  0.0349  19  LYS   A N   
513  C CA  A LYS   A 19  ? 0.1594 0.1748 0.2174 0.0034  0.0268  0.0402  19  LYS   A CA  
514  C CA  B LYS   A 19  ? 0.1728 0.1806 0.2280 -0.0119 0.0243  0.0292  19  LYS   A CA  
515  C C   A LYS   A 19  ? 0.1571 0.1690 0.2281 -0.0049 0.0242  0.0430  19  LYS   A C   
516  C C   B LYS   A 19  ? 0.1561 0.1725 0.2317 -0.0065 0.0311  0.0351  19  LYS   A C   
517  O O   A LYS   A 19  ? 0.1514 0.1655 0.2340 -0.0103 0.0224  0.0426  19  LYS   A O   
518  O O   B LYS   A 19  ? 0.1482 0.1589 0.2151 -0.0093 0.0382  0.0339  19  LYS   A O   
519  C CB  A LYS   A 19  ? 0.1795 0.2016 0.2141 -0.0037 0.0386  0.0443  19  LYS   A CB  
520  C CB  B LYS   A 19  ? 0.1918 0.2045 0.2272 -0.0140 0.0213  0.0290  19  LYS   A CB  
521  C CG  A LYS   A 19  ? 0.2093 0.2244 0.2054 -0.0126 0.0383  0.0347  19  LYS   A CG  
522  C CG  B LYS   A 19  ? 0.2105 0.2188 0.2368 -0.0176 0.0158  0.0243  19  LYS   A CG  
523  C CD  A LYS   A 19  ? 0.2343 0.2449 0.2033 -0.0229 0.0443  0.0379  19  LYS   A CD  
524  C CD  B LYS   A 19  ? 0.2264 0.2342 0.2387 -0.0168 0.0099  0.0200  19  LYS   A CD  
525  C CE  A LYS   A 19  ? 0.2499 0.2583 0.2119 -0.0380 0.0311  0.0302  19  LYS   A CE  
526  C CE  B LYS   A 19  ? 0.2387 0.2459 0.2511 -0.0193 0.0116  0.0177  19  LYS   A CE  
527  N NZ  A LYS   A 19  ? 0.2591 0.2685 0.2341 -0.0521 0.0308  0.0197  19  LYS   A NZ  
528  N NZ  B LYS   A 19  ? 0.2469 0.2572 0.2584 -0.0184 0.0085  0.0119  19  LYS   A NZ  
555  N N   A ASN   A 20  ? 0.1627 0.1733 0.2321 -0.0141 0.0273  0.0418  20  ASN   A N   
556  N N   B ASN   A 20  ? 0.1527 0.1842 0.2475 -0.0054 0.0313  0.0492  20  ASN   A N   
557  C CA  A ASN   A 20  ? 0.1715 0.1820 0.2266 -0.0073 0.0306  0.0299  20  ASN   A CA  
558  C CA  B ASN   A 20  ? 0.1509 0.1952 0.2461 0.0080  0.0317  0.0470  20  ASN   A CA  
559  C C   A ASN   A 20  ? 0.1754 0.1955 0.2322 -0.0134 0.0459  0.0295  20  ASN   A C   
560  C C   B ASN   A 20  ? 0.1629 0.2056 0.2487 0.0135  0.0394  0.0515  20  ASN   A C   
561  O O   A ASN   A 20  ? 0.1867 0.2034 0.2350 -0.0194 0.0384  0.0314  20  ASN   A O   
562  O O   B ASN   A 20  ? 0.1788 0.2184 0.2518 0.0130  0.0225  0.0535  20  ASN   A O   
563  C CB  A ASN   A 20  ? 0.1864 0.1809 0.2265 0.0016  0.0329  0.0263  20  ASN   A CB  
564  C CB  B ASN   A 20  ? 0.1446 0.1936 0.2418 0.0067  0.0270  0.0434  20  ASN   A CB  
565  C CG  A ASN   A 20  ? 0.2032 0.1816 0.2369 0.0119  0.0379  0.0090  20  ASN   A CG  
566  C CG  B ASN   A 20  ? 0.1377 0.1879 0.2298 0.0081  0.0333  0.0326  20  ASN   A CG  
567  O OD1 A ASN   A 20  ? 0.2333 0.2037 0.2893 0.0143  0.0539  -0.0107 20  ASN   A OD1 
568  O OD1 B ASN   A 20  ? 0.1432 0.1759 0.2338 0.0157  0.0359  0.0215  20  ASN   A OD1 
569  N ND2 A ASN   A 20  ? 0.2034 0.1660 0.2233 0.0205  0.0238  0.0256  20  ASN   A ND2 
570  N ND2 B ASN   A 20  ? 0.1490 0.1833 0.2263 0.0048  0.0351  0.0442  20  ASN   A ND2 
583  N N   A ALA   A 21  ? 0.1796 0.1956 0.2497 -0.0188 0.0397  0.0246  21  ALA   A N   
584  N N   B ALA   A 21  ? 0.1694 0.2015 0.2582 0.0066  0.0511  0.0397  21  ALA   A N   
585  C CA  A ALA   A 21  ? 0.1849 0.1956 0.2489 -0.0243 0.0305  0.0381  21  ALA   A CA  
586  C CA  B ALA   A 21  ? 0.1815 0.1976 0.2607 0.0010  0.0427  0.0301  21  ALA   A CA  
587  C C   A ALA   A 21  ? 0.1817 0.1858 0.2459 -0.0177 0.0222  0.0284  21  ALA   A C   
588  C C   B ALA   A 21  ? 0.1672 0.1776 0.2359 -0.0065 0.0569  0.0102  21  ALA   A C   
589  O O   A ALA   A 21  ? 0.1892 0.1958 0.2532 -0.0143 0.0155  0.0255  21  ALA   A O   
590  O O   B ALA   A 21  ? 0.1660 0.1740 0.2348 -0.0017 0.0677  -0.0028 21  ALA   A O   
591  C CB  A ALA   A 21  ? 0.1900 0.2062 0.2574 -0.0285 0.0358  0.0407  21  ALA   A CB  
592  C CB  B ALA   A 21  ? 0.1967 0.2105 0.2822 0.0072  0.0187  0.0209  21  ALA   A CB  
603  N N   A ASP   A 22  ? 0.1785 0.1753 0.2551 -0.0139 0.0166  0.0271  22  ASP   A N   
604  N N   B ASP   A 22  ? 0.1648 0.1698 0.2391 -0.0109 0.0570  0.0064  22  ASP   A N   
605  C CA  A ASP   A 22  ? 0.1841 0.1668 0.2414 -0.0024 0.0066  0.0332  22  ASP   A CA  
606  C CA  B ASP   A 22  ? 0.1746 0.1654 0.2235 -0.0114 0.0587  0.0151  22  ASP   A CA  
607  C C   A ASP   A 22  ? 0.1745 0.1693 0.2216 -0.0012 0.0100  0.0280  22  ASP   A C   
608  C C   B ASP   A 22  ? 0.1653 0.1710 0.1946 -0.0217 0.0790  0.0175  22  ASP   A C   
609  O O   A ASP   A 22  ? 0.1796 0.1772 0.2527 -0.0075 0.0057  0.0254  22  ASP   A O   
610  O O   B ASP   A 22  ? 0.1716 0.1755 0.1922 -0.0306 0.0764  0.0076  22  ASP   A O   
611  C CB  A ASP   A 22  ? 0.2090 0.1724 0.2787 0.0019  0.0144  0.0145  22  ASP   A CB  
612  C CB  B ASP   A 22  ? 0.2004 0.1664 0.2404 -0.0025 0.0609  0.0064  22  ASP   A CB  
613  C CG  A ASP   A 22  ? 0.2287 0.1795 0.3094 0.0001  0.0110  0.0004  22  ASP   A CG  
614  C CG  B ASP   A 22  ? 0.2202 0.1716 0.2619 0.0061  0.0653  0.0036  22  ASP   A CG  
615  O OD1 A ASP   A 22  ? 0.2204 0.1668 0.3314 -0.0105 0.0018  0.0051  22  ASP   A OD1 
616  O OD1 B ASP   A 22  ? 0.2204 0.1704 0.2356 -0.0064 0.0567  0.0058  22  ASP   A OD1 
617  O OD2 A ASP   A 22  ? 0.2515 0.1965 0.3152 0.0148  0.0200  -0.0216 22  ASP   A OD2 
618  O OD2 B ASP   A 22  ? 0.2434 0.1868 0.3020 0.0142  0.0707  0.0141  22  ASP   A OD2 
627  N N   A ILE   A 23  ? 0.1696 0.1739 0.2102 0.0097  0.0165  0.0328  23  ILE   A N   
628  N N   B ILE   A 23  ? 0.1637 0.1685 0.2105 -0.0110 0.0594  0.0169  23  ILE   A N   
629  C CA  A ILE   A 23  ? 0.1714 0.1687 0.2070 0.0012  0.0319  0.0288  23  ILE   A CA  
630  C CA  B ILE   A 23  ? 0.1621 0.1750 0.1922 -0.0137 0.0504  0.0191  23  ILE   A CA  
631  C C   A ILE   A 23  ? 0.1718 0.1806 0.2007 -0.0074 0.0393  0.0271  23  ILE   A C   
632  C C   B ILE   A 23  ? 0.1686 0.1926 0.1916 -0.0298 0.0478  0.0094  23  ILE   A C   
633  O O   A ILE   A 23  ? 0.1771 0.2021 0.2122 -0.0113 0.0211  0.0142  23  ILE   A O   
634  O O   B ILE   A 23  ? 0.1694 0.2024 0.2004 -0.0264 0.0429  0.0074  23  ILE   A O   
635  C CB  A ILE   A 23  ? 0.1818 0.1610 0.1901 0.0067  0.0317  0.0259  23  ILE   A CB  
636  C CB  B ILE   A 23  ? 0.1671 0.1729 0.1869 0.0033  0.0330  0.0295  23  ILE   A CB  
637  C CG1 A ILE   A 23  ? 0.1862 0.1552 0.1865 0.0045  0.0288  0.0121  23  ILE   A CG1 
638  C CG1 B ILE   A 23  ? 0.1662 0.1705 0.1788 0.0045  0.0214  0.0142  23  ILE   A CG1 
639  C CG2 A ILE   A 23  ? 0.1848 0.1662 0.1947 0.0153  0.0359  0.0388  23  ILE   A CG2 
640  C CG2 B ILE   A 23  ? 0.1710 0.1719 0.2116 0.0186  0.0287  0.0296  23  ILE   A CG2 
641  C CD1 A ILE   A 23  ? 0.1883 0.1594 0.2082 0.0092  -0.0005 -0.0084 23  ILE   A CD1 
642  C CD1 B ILE   A 23  ? 0.1660 0.1684 0.1933 0.0023  -0.0014 0.0172  23  ILE   A CD1 
665  N N   A VAL   A 24  ? 0.1735 0.1823 0.2063 -0.0061 0.0347  0.0110  24  VAL   A N   
666  N N   B VAL   A 24  ? 0.1820 0.2007 0.2117 -0.0396 0.0341  -0.0008 24  VAL   A N   
667  C CA  A VAL   A 24  ? 0.1881 0.1954 0.2290 -0.0111 0.0305  -0.0015 24  VAL   A CA  
668  C CA  B VAL   A 24  ? 0.1995 0.2089 0.2361 -0.0487 0.0345  0.0046  24  VAL   A CA  
669  C C   A VAL   A 24  ? 0.1950 0.2123 0.2244 -0.0163 0.0317  0.0029  24  VAL   A C   
670  C C   B VAL   A 24  ? 0.2140 0.2291 0.2413 -0.0415 0.0430  -0.0025 24  VAL   A C   
671  O O   A VAL   A 24  ? 0.2106 0.2217 0.2320 -0.0191 0.0362  0.0040  24  VAL   A O   
672  O O   B VAL   A 24  ? 0.2264 0.2384 0.2556 -0.0359 0.0533  0.0019  24  VAL   A O   
673  C CB  A VAL   A 24  ? 0.1913 0.1921 0.2445 -0.0112 0.0278  -0.0054 24  VAL   A CB  
674  C CB  B VAL   A 24  ? 0.1998 0.2042 0.2594 -0.0600 0.0289  0.0245  24  VAL   A CB  
675  C CG1 A VAL   A 24  ? 0.1961 0.2033 0.2488 0.0027  0.0292  -0.0255 24  VAL   A CG1 
676  C CG1 B VAL   A 24  ? 0.2146 0.2164 0.2767 -0.0495 0.0244  0.0244  24  VAL   A CG1 
677  C CG2 A VAL   A 24  ? 0.1970 0.1895 0.2550 -0.0201 0.0314  0.0034  24  VAL   A CG2 
678  C CG2 B VAL   A 24  ? 0.1903 0.1967 0.2603 -0.0673 0.0243  0.0234  24  VAL   A CG2 
697  N N   A GLU   A 25  ? 0.1951 0.2218 0.2261 -0.0271 0.0394  -0.0014 25  GLU   A N   
698  N N   B GLU   A 25  ? 0.2202 0.2479 0.2422 -0.0379 0.0585  -0.0083 25  GLU   A N   
699  C CA  A GLU   A 25  ? 0.2157 0.2505 0.2423 -0.0061 0.0436  -0.0089 25  GLU   A CA  
700  C CA  B GLU   A 25  ? 0.2350 0.2711 0.2472 -0.0342 0.0633  -0.0168 25  GLU   A CA  
701  C C   A GLU   A 25  ? 0.2030 0.2569 0.1981 -0.0207 0.0547  -0.0019 25  GLU   A C   
702  C C   B GLU   A 25  ? 0.2236 0.2760 0.2221 -0.0380 0.0706  -0.0165 25  GLU   A C   
703  O O   A GLU   A 25  ? 0.2022 0.2665 0.2160 -0.0246 0.0522  -0.0107 25  GLU   A O   
704  O O   B GLU   A 25  ? 0.2298 0.2824 0.2374 -0.0404 0.0704  -0.0253 25  GLU   A O   
705  C CB  A GLU   A 25  ? 0.2470 0.2769 0.2820 0.0121  0.0436  -0.0010 25  GLU   A CB  
706  C CB  B GLU   A 25  ? 0.2627 0.2905 0.2700 -0.0250 0.0699  -0.0131 25  GLU   A CB  
707  C CG  A GLU   A 25  ? 0.2841 0.3012 0.3432 0.0136  0.0424  -0.0006 25  GLU   A CG  
708  C CG  B GLU   A 25  ? 0.2982 0.3120 0.3264 -0.0178 0.0625  -0.0074 25  GLU   A CG  
709  C CD  A GLU   A 25  ? 0.3163 0.3248 0.3946 0.0148  0.0343  -0.0094 25  GLU   A CD  
710  C CD  B GLU   A 25  ? 0.3255 0.3284 0.3852 -0.0121 0.0483  -0.0117 25  GLU   A CD  
711  O OE1 A GLU   A 25  ? 0.3325 0.3340 0.4140 0.0155  0.0319  -0.0168 25  GLU   A OE1 
712  O OE1 B GLU   A 25  ? 0.3396 0.3348 0.4137 -0.0056 0.0448  -0.0161 25  GLU   A OE1 
713  O OE2 A GLU   A 25  ? 0.3222 0.3346 0.4281 0.0125  0.0211  -0.0203 25  GLU   A OE2 
714  O OE2 B GLU   A 25  ? 0.3346 0.3320 0.4108 -0.0142 0.0372  -0.0173 25  GLU   A OE2 
727  N N   A GLU   A 26  ? 0.1966 0.2517 0.2076 -0.0361 0.0569  0.0023  26  GLU   A N   
728  N N   B GLU   A 26  ? 0.2077 0.2715 0.2102 -0.0419 0.0795  -0.0143 26  GLU   A N   
729  C CA  A GLU   A 26  ? 0.2004 0.2478 0.1926 -0.0462 0.0526  0.0030  26  GLU   A CA  
730  C CA  B GLU   A 26  ? 0.2041 0.2717 0.2016 -0.0470 0.0635  -0.0018 26  GLU   A CA  
731  C C   A GLU   A 26  ? 0.1966 0.2445 0.1886 -0.0445 0.0360  0.0077  26  GLU   A C   
732  C C   B GLU   A 26  ? 0.1995 0.2551 0.1937 -0.0470 0.0457  -0.0039 26  GLU   A C   
733  O O   A GLU   A 26  ? 0.2028 0.2432 0.1836 -0.0461 0.0253  0.0112  26  GLU   A O   
734  O O   B GLU   A 26  ? 0.2058 0.2521 0.1775 -0.0505 0.0511  -0.0099 26  GLU   A O   
735  C CB  A GLU   A 26  ? 0.2236 0.2533 0.2204 -0.0495 0.0496  -0.0048 26  GLU   A CB  
736  C CB  B GLU   A 26  ? 0.2120 0.2867 0.2109 -0.0491 0.0431  0.0021  26  GLU   A CB  
737  C CG  A GLU   A 26  ? 0.2522 0.2743 0.2909 -0.0582 0.0549  -0.0153 26  GLU   A CG  
738  C CG  B GLU   A 26  ? 0.2237 0.3065 0.2229 -0.0505 0.0350  0.0014  26  GLU   A CG  
739  C CD  A GLU   A 26  ? 0.2676 0.2871 0.3302 -0.0742 0.0736  -0.0242 26  GLU   A CD  
740  C CD  B GLU   A 26  ? 0.2249 0.3177 0.2177 -0.0586 0.0443  0.0127  26  GLU   A CD  
741  O OE1 A GLU   A 26  ? 0.2648 0.3004 0.3275 -0.0822 0.0945  -0.0579 26  GLU   A OE1 
742  O OE1 B GLU   A 26  ? 0.2380 0.3300 0.1991 -0.0545 0.0600  0.0213  26  GLU   A OE1 
743  O OE2 A GLU   A 26  ? 0.2801 0.2911 0.3307 -0.0723 0.0774  -0.0157 26  GLU   A OE2 
744  O OE2 B GLU   A 26  ? 0.2106 0.3153 0.1857 -0.0674 0.0522  0.0129  26  GLU   A OE2 
757  N N   . ALA   A 27  ? 0.1843 0.2413 0.1861 -0.0480 0.0425  0.0078  27  ALA   A N   
758  C CA  . ALA   A 27  ? 0.1863 0.2603 0.1835 -0.0378 0.0264  0.0114  27  ALA   A CA  
759  C C   . ALA   A 27  ? 0.2119 0.2873 0.2023 -0.0486 0.0200  -0.0105 27  ALA   A C   
760  O O   . ALA   A 27  ? 0.2169 0.2835 0.2167 -0.0531 0.0105  -0.0025 27  ALA   A O   
761  C CB  . ALA   A 27  ? 0.1669 0.2607 0.1709 -0.0349 0.0183  0.0070  27  ALA   A CB  
768  N N   A LYS   A 28  ? 0.2399 0.3126 0.2111 -0.0461 0.0271  -0.0363 28  LYS   A N   
769  N N   B LYS   A 28  ? 0.2333 0.3009 0.2097 -0.0462 0.0269  -0.0310 28  LYS   A N   
770  C CA  A LYS   A 28  ? 0.2787 0.3467 0.2263 -0.0345 0.0366  -0.0449 28  LYS   A CA  
771  C CA  B LYS   A 28  ? 0.2648 0.3226 0.2253 -0.0339 0.0355  -0.0383 28  LYS   A CA  
772  C C   A LYS   A 28  ? 0.3067 0.3729 0.2268 -0.0387 0.0491  -0.0363 28  LYS   A C   
773  C C   B LYS   A 28  ? 0.2910 0.3417 0.2333 -0.0281 0.0345  -0.0323 28  LYS   A C   
774  O O   A LYS   A 28  ? 0.3213 0.3783 0.2456 -0.0352 0.0240  -0.0383 28  LYS   A O   
775  O O   B LYS   A 28  ? 0.3028 0.3438 0.2484 -0.0244 0.0199  -0.0327 28  LYS   A O   
776  C CB  A LYS   A 28  ? 0.2943 0.3589 0.2701 -0.0187 0.0305  -0.0478 28  LYS   A CB  
777  C CB  B LYS   A 28  ? 0.2769 0.3301 0.2519 -0.0261 0.0408  -0.0395 28  LYS   A CB  
778  C CG  A LYS   A 28  ? 0.3062 0.3669 0.3064 -0.0067 0.0334  -0.0485 28  LYS   A CG  
779  C CG  B LYS   A 28  ? 0.2881 0.3373 0.2828 -0.0209 0.0472  -0.0411 28  LYS   A CG  
780  C CD  A LYS   A 28  ? 0.3132 0.3771 0.3513 0.0017  0.0388  -0.0536 28  LYS   A CD  
781  C CD  B LYS   A 28  ? 0.2966 0.3466 0.3245 -0.0159 0.0534  -0.0480 28  LYS   A CD  
782  C CE  A LYS   A 28  ? 0.3190 0.3825 0.3897 0.0046  0.0419  -0.0511 28  LYS   A CE  
783  C CE  B LYS   A 28  ? 0.3036 0.3509 0.3516 -0.0145 0.0593  -0.0511 28  LYS   A CE  
784  N NZ  A LYS   A 28  ? 0.3247 0.3842 0.4069 0.0071  0.0481  -0.0463 28  LYS   A NZ  
785  N NZ  B LYS   A 28  ? 0.3065 0.3523 0.3722 -0.0137 0.0600  -0.0476 28  LYS   A NZ  
812  N N   A LYS   A 29  ? 0.3172 0.3924 0.2222 -0.0491 0.0883  -0.0132 29  LYS   A N   
813  N N   B LYS   A 29  ? 0.3037 0.3587 0.2371 -0.0266 0.0503  -0.0137 29  LYS   A N   
814  C CA  A LYS   A 29  ? 0.3347 0.4133 0.2382 -0.0561 0.1018  0.0045  29  LYS   A CA  
815  C CA  B LYS   A 29  ? 0.3192 0.3769 0.2525 -0.0250 0.0543  0.0024  29  LYS   A CA  
816  C C   A LYS   A 29  ? 0.3371 0.4060 0.2114 -0.0710 0.0876  0.0196  29  LYS   A C   
817  C C   B LYS   A 29  ? 0.3211 0.3729 0.2320 -0.0317 0.0383  0.0186  29  LYS   A C   
818  O O   A LYS   A 29  ? 0.3486 0.4163 0.2363 -0.0674 0.0794  0.0172  29  LYS   A O   
819  O O   B LYS   A 29  ? 0.3221 0.3793 0.2405 -0.0314 0.0322  0.0237  29  LYS   A O   
820  C CB  A LYS   A 29  ? 0.3496 0.4374 0.2981 -0.0443 0.1098  0.0065  29  LYS   A CB  
821  C CB  B LYS   A 29  ? 0.3342 0.3955 0.3045 -0.0148 0.0604  0.0036  29  LYS   A CB  
822  C CG  A LYS   A 29  ? 0.3671 0.4561 0.3640 -0.0325 0.1118  0.0036  29  LYS   A CG  
823  C CG  B LYS   A 29  ? 0.3503 0.4097 0.3599 -0.0043 0.0662  -0.0004 29  LYS   A CG  
824  C CD  A LYS   A 29  ? 0.3826 0.4691 0.4228 -0.0251 0.1128  0.0016  29  LYS   A CD  
825  C CD  B LYS   A 29  ? 0.3633 0.4194 0.4113 0.0030  0.0685  0.0004  29  LYS   A CD  
826  C CE  A LYS   A 29  ? 0.3911 0.4764 0.4640 -0.0210 0.1144  0.0055  29  LYS   A CE  
827  C CE  B LYS   A 29  ? 0.3702 0.4264 0.4493 0.0063  0.0709  0.0023  29  LYS   A CE  
828  N NZ  A LYS   A 29  ? 0.3945 0.4802 0.4859 -0.0176 0.1100  0.0067  29  LYS   A NZ  
829  N NZ  B LYS   A 29  ? 0.3745 0.4304 0.4706 0.0068  0.0680  0.0046  29  LYS   A NZ  
856  N N   A VAL   A 30  ? 0.3270 0.3866 0.2093 -0.0879 0.0838  0.0314  30  VAL   A N   
857  N N   B VAL   A 30  ? 0.3205 0.3618 0.2349 -0.0395 0.0367  0.0297  30  VAL   A N   
858  C CA  A VAL   A 30  ? 0.3238 0.3702 0.2094 -0.1003 0.0494  0.0353  30  VAL   A CA  
859  C CA  B VAL   A 30  ? 0.3178 0.3508 0.2340 -0.0492 0.0133  0.0379  30  VAL   A CA  
860  C C   A VAL   A 30  ? 0.3222 0.3568 0.1716 -0.0992 0.0428  0.0413  30  VAL   A C   
861  C C   B VAL   A 30  ? 0.3166 0.3442 0.2193 -0.0476 0.0042  0.0366  30  VAL   A C   
862  O O   A VAL   A 30  ? 0.3239 0.3620 0.1816 -0.1014 0.0492  0.0425  30  VAL   A O   
863  O O   B VAL   A 30  ? 0.3142 0.3479 0.2283 -0.0505 0.0012  0.0363  30  VAL   A O   
864  C CB  A VAL   A 30  ? 0.3194 0.3633 0.2480 -0.1158 0.0376  0.0421  30  VAL   A CB  
865  C CB  B VAL   A 30  ? 0.3144 0.3432 0.2593 -0.0628 0.0068  0.0473  30  VAL   A CB  
866  C CG1 A VAL   A 30  ? 0.3261 0.3659 0.2712 -0.1154 0.0341  0.0479  30  VAL   A CG1 
867  C CG1 B VAL   A 30  ? 0.3196 0.3449 0.2778 -0.0650 0.0053  0.0493  30  VAL   A CG1 
868  C CG2 A VAL   A 30  ? 0.3123 0.3565 0.2723 -0.1289 0.0423  0.0446  30  VAL   A CG2 
869  C CG2 B VAL   A 30  ? 0.3095 0.3369 0.2710 -0.0707 0.0091  0.0556  30  VAL   A CG2 
888  N N   A LYS   A 31  ? 0.3144 0.3379 0.1506 -0.0982 0.0235  0.0403  31  LYS   A N   
889  N N   B LYS   A 31  ? 0.3177 0.3340 0.2196 -0.0440 -0.0115 0.0333  31  LYS   A N   
890  C CA  A LYS   A 31  ? 0.3207 0.3314 0.1723 -0.0878 -0.0033 0.0496  31  LYS   A CA  
891  C CA  B LYS   A 31  ? 0.3196 0.3304 0.2368 -0.0362 -0.0237 0.0298  31  LYS   A CA  
892  C C   A LYS   A 31  ? 0.2930 0.3034 0.1273 -0.0752 -0.0098 0.0761  31  LYS   A C   
893  C C   B LYS   A 31  ? 0.2942 0.3115 0.2033 -0.0273 -0.0171 0.0432  31  LYS   A C   
894  O O   A LYS   A 31  ? 0.3016 0.3175 0.1440 -0.0664 -0.0309 0.0869  31  LYS   A O   
895  O O   B LYS   A 31  ? 0.3020 0.3193 0.2150 -0.0223 -0.0199 0.0433  31  LYS   A O   
896  C CB  A LYS   A 31  ? 0.3545 0.3539 0.2776 -0.0779 -0.0209 0.0235  31  LYS   A CB  
897  C CB  B LYS   A 31  ? 0.3446 0.3482 0.3123 -0.0344 -0.0372 0.0119  31  LYS   A CB  
898  C CG  A LYS   A 31  ? 0.3880 0.3755 0.3970 -0.0643 -0.0370 0.0079  31  LYS   A CG  
899  C CG  B LYS   A 31  ? 0.3698 0.3673 0.3999 -0.0323 -0.0476 -0.0025 31  LYS   A CG  
900  C CD  A LYS   A 31  ? 0.4153 0.3918 0.4895 -0.0517 -0.0521 -0.0050 31  LYS   A CD  
901  C CD  B LYS   A 31  ? 0.3884 0.3813 0.4742 -0.0288 -0.0583 -0.0162 31  LYS   A CD  
902  C CE  A LYS   A 31  ? 0.4335 0.4040 0.5561 -0.0425 -0.0609 -0.0126 31  LYS   A CE  
903  C CE  B LYS   A 31  ? 0.4027 0.3929 0.5285 -0.0271 -0.0636 -0.0237 31  LYS   A CE  
904  N NZ  A LYS   A 31  ? 0.4430 0.4123 0.5869 -0.0370 -0.0649 -0.0156 31  LYS   A NZ  
905  N NZ  B LYS   A 31  ? 0.4131 0.4007 0.5554 -0.0259 -0.0624 -0.0278 31  LYS   A NZ  
932  N N   A PRO   A 32  ? 0.2638 0.2750 0.1289 -0.0864 -0.0067 0.0671  32  PRO   A N   
933  N N   B PRO   A 32  ? 0.2616 0.2846 0.1816 -0.0252 -0.0082 0.0403  32  PRO   A N   
934  C CA  A PRO   A 32  ? 0.2552 0.2592 0.1694 -0.0812 -0.0153 0.0632  32  PRO   A CA  
935  C CA  B PRO   A 32  ? 0.2452 0.2705 0.1795 -0.0182 -0.0048 0.0426  32  PRO   A CA  
936  C C   A PRO   A 32  ? 0.2495 0.2462 0.1871 -0.0709 -0.0217 0.0667  32  PRO   A C   
937  C C   B PRO   A 32  ? 0.2350 0.2594 0.1782 -0.0090 -0.0168 0.0479  32  PRO   A C   
938  O O   A PRO   A 32  ? 0.2497 0.2408 0.1828 -0.0746 -0.0201 0.0665  32  PRO   A O   
939  O O   B PRO   A 32  ? 0.2310 0.2548 0.1773 -0.0003 -0.0330 0.0424  32  PRO   A O   
940  C CB  A PRO   A 32  ? 0.2487 0.2601 0.1559 -0.0825 -0.0179 0.0512  32  PRO   A CB  
941  C CB  B PRO   A 32  ? 0.2402 0.2696 0.1667 -0.0171 -0.0012 0.0296  32  PRO   A CB  
942  C CG  A PRO   A 32  ? 0.2500 0.2667 0.1236 -0.0765 -0.0306 0.0381  32  PRO   A CG  
943  C CG  B PRO   A 32  ? 0.2439 0.2745 0.1570 -0.0172 -0.0068 0.0220  32  PRO   A CG  
944  C CD  A PRO   A 32  ? 0.2534 0.2683 0.1193 -0.0815 -0.0211 0.0471  32  PRO   A CD  
945  C CD  B PRO   A 32  ? 0.2501 0.2798 0.1585 -0.0214 -0.0050 0.0282  32  PRO   A CD  
960  N N   A THR   A 33  ? 0.2505 0.2410 0.1825 -0.0574 -0.0313 0.0757  33  THR   A N   
961  N N   B THR   A 33  ? 0.2359 0.2553 0.1905 -0.0132 -0.0187 0.0549  33  THR   A N   
962  C CA  A THR   A 33  ? 0.2517 0.2428 0.1830 -0.0439 -0.0510 0.0708  33  THR   A CA  
963  C CA  B THR   A 33  ? 0.2368 0.2491 0.1880 -0.0141 -0.0273 0.0555  33  THR   A CA  
964  C C   A THR   A 33  ? 0.2238 0.2303 0.1760 -0.0411 -0.0537 0.0632  33  THR   A C   
965  C C   B THR   A 33  ? 0.2147 0.2234 0.1751 -0.0266 -0.0313 0.0471  33  THR   A C   
966  O O   A THR   A 33  ? 0.2120 0.2271 0.1829 -0.0387 -0.0640 0.0646  33  THR   A O   
967  O O   B THR   A 33  ? 0.2044 0.2068 0.1822 -0.0246 -0.0220 0.0407  33  THR   A O   
968  C CB  A THR   A 33  ? 0.2787 0.2580 0.2228 -0.0333 -0.0479 0.0818  33  THR   A CB  
969  C CB  B THR   A 33  ? 0.2583 0.2669 0.2107 -0.0035 -0.0270 0.0739  33  THR   A CB  
970  O OG1 A THR   A 33  ? 0.2959 0.2689 0.2487 -0.0191 -0.0458 0.0918  33  THR   A OG1 
971  O OG1 B THR   A 33  ? 0.2709 0.2827 0.2260 0.0067  -0.0334 0.0843  33  THR   A OG1 
972  C CG2 A THR   A 33  ? 0.2849 0.2639 0.2415 -0.0279 -0.0496 0.0743  33  THR   A CG2 
973  C CG2 B THR   A 33  ? 0.2622 0.2683 0.2270 0.0029  -0.0263 0.0691  33  THR   A CG2 
988  N N   . VAL   A 34  ? 0.2055 0.2190 0.1590 -0.0407 -0.0326 0.0525  34  VAL   A N   
989  C CA  . VAL   A 34  ? 0.1817 0.1999 0.1559 -0.0298 -0.0197 0.0561  34  VAL   A CA  
990  C C   . VAL   A 34  ? 0.1681 0.1875 0.1655 -0.0298 -0.0139 0.0544  34  VAL   A C   
991  O O   . VAL   A 34  ? 0.1692 0.1937 0.1912 -0.0352 -0.0168 0.0446  34  VAL   A O   
992  C CB  . VAL   A 34  ? 0.1855 0.1985 0.1825 -0.0240 -0.0073 0.0484  34  VAL   A CB  
993  C CG1 . VAL   A 34  ? 0.1946 0.1988 0.1832 -0.0232 0.0011  0.0223  34  VAL   A CG1 
994  C CG2 . VAL   A 34  ? 0.1909 0.2181 0.2081 -0.0222 -0.0044 0.0570  34  VAL   A CG2 
1005 N N   . VAL   A 35  ? 0.1606 0.1777 0.1639 -0.0243 -0.0153 0.0425  35  VAL   A N   
1006 C CA  . VAL   A 35  ? 0.1531 0.1689 0.1664 -0.0248 0.0004  0.0283  35  VAL   A CA  
1007 C C   . VAL   A 35  ? 0.1502 0.1570 0.1507 -0.0175 0.0050  0.0196  35  VAL   A C   
1008 O O   . VAL   A 35  ? 0.1391 0.1716 0.1715 -0.0245 0.0120  0.0232  35  VAL   A O   
1009 C CB  . VAL   A 35  ? 0.1560 0.1744 0.1784 -0.0137 0.0083  0.0216  35  VAL   A CB  
1010 C CG1 . VAL   A 35  ? 0.1737 0.1828 0.1557 -0.0056 0.0093  0.0099  35  VAL   A CG1 
1011 C CG2 . VAL   A 35  ? 0.1543 0.1789 0.1945 -0.0124 0.0150  0.0042  35  VAL   A CG2 
1021 N N   . VAL   A 36  ? 0.1407 0.1514 0.1272 -0.0174 0.0009  0.0200  36  VAL   A N   
1022 C CA  . VAL   A 36  ? 0.1352 0.1381 0.1468 -0.0136 -0.0017 0.0138  36  VAL   A CA  
1023 C C   . VAL   A 36  ? 0.1270 0.1445 0.1703 -0.0176 0.0123  0.0189  36  VAL   A C   
1024 O O   . VAL   A 36  ? 0.1310 0.1423 0.1818 -0.0125 0.0163  0.0183  36  VAL   A O   
1025 C CB  . VAL   A 36  ? 0.1319 0.1340 0.1420 -0.0091 -0.0012 0.0281  36  VAL   A CB  
1026 C CG1 . VAL   A 36  ? 0.1380 0.1371 0.1683 -0.0151 0.0118  0.0115  36  VAL   A CG1 
1027 C CG2 . VAL   A 36  ? 0.1393 0.1467 0.1634 -0.0121 -0.0020 0.0307  36  VAL   A CG2 
1037 N N   . ASN   A 37  ? 0.1300 0.1304 0.1397 -0.0057 0.0066  0.0245  37  ASN   A N   
1038 C CA  . ASN   A 37  ? 0.1250 0.1277 0.1344 -0.0041 0.0088  0.0161  37  ASN   A CA  
1039 C C   . ASN   A 37  ? 0.1236 0.1288 0.1418 -0.0030 0.0110  0.0300  37  ASN   A C   
1040 O O   . ASN   A 37  ? 0.1404 0.1403 0.1329 0.0019  0.0111  0.0186  37  ASN   A O   
1041 C CB  . ASN   A 37  ? 0.1249 0.1296 0.1435 -0.0012 0.0054  0.0167  37  ASN   A CB  
1042 C CG  . ASN   A 37  ? 0.1280 0.1237 0.1612 0.0039  0.0149  0.0145  37  ASN   A CG  
1043 O OD1 . ASN   A 37  ? 0.1282 0.1314 0.1715 -0.0004 0.0095  0.0167  37  ASN   A OD1 
1044 N ND2 . ASN   A 37  ? 0.1328 0.1312 0.1685 -0.0009 0.0037  0.0256  37  ASN   A ND2 
1051 N N   A ALA   A 38  ? 0.1232 0.1306 0.1417 -0.0033 0.0159  0.0139  38  ALA   A N   
1052 N N   B ALA   A 38  ? 0.1290 0.1364 0.1602 -0.0039 0.0060  0.0194  38  ALA   A N   
1053 C CA  A ALA   A 38  ? 0.1309 0.1248 0.1419 -0.0047 0.0070  -0.0052 38  ALA   A CA  
1054 C CA  B ALA   A 38  ? 0.1386 0.1408 0.1701 -0.0042 0.0035  0.0052  38  ALA   A CA  
1055 C C   A ALA   A 38  ? 0.1244 0.1309 0.1478 -0.0072 -0.0017 -0.0030 38  ALA   A C   
1056 C C   B ALA   A 38  ? 0.1339 0.1379 0.1852 -0.0010 -0.0025 -0.0009 38  ALA   A C   
1057 O O   A ALA   A 38  ? 0.1232 0.1220 0.1372 -0.0121 -0.0072 0.0091  38  ALA   A O   
1058 O O   B ALA   A 38  ? 0.1335 0.1281 0.2037 0.0074  -0.0159 -0.0000 38  ALA   A O   
1059 C CB  A ALA   A 38  ? 0.1230 0.1269 0.1776 -0.0176 -0.0010 -0.0051 38  ALA   A CB  
1060 C CB  B ALA   A 38  ? 0.1418 0.1516 0.1898 -0.0094 0.0006  -0.0118 38  ALA   A CB  
1071 N N   A ALA   A 39  ? 0.1198 0.1302 0.1494 0.0025  0.0086  0.0087  39  ALA   A N   
1072 N N   B ALA   A 39  ? 0.1321 0.1460 0.1638 -0.0003 0.0068  0.0256  39  ALA   A N   
1073 C CA  A ALA   A 39  ? 0.1207 0.1217 0.1531 0.0039  0.0089  0.0215  39  ALA   A CA  
1074 C CA  B ALA   A 39  ? 0.1303 0.1445 0.1583 -0.0032 0.0042  0.0311  39  ALA   A CA  
1075 C C   A ALA   A 39  ? 0.1292 0.1245 0.1532 0.0014  -0.0005 -0.0019 39  ALA   A C   
1076 C C   B ALA   A 39  ? 0.1281 0.1343 0.1491 -0.0056 0.0166  0.0252  39  ALA   A C   
1077 O O   A ALA   A 39  ? 0.1458 0.1306 0.1598 -0.0023 -0.0007 -0.0053 39  ALA   A O   
1078 O O   B ALA   A 39  ? 0.1368 0.1364 0.1551 -0.0111 0.0226  0.0147  39  ALA   A O   
1079 C CB  A ALA   A 39  ? 0.1233 0.1187 0.1757 0.0018  -0.0035 0.0178  39  ALA   A CB  
1080 C CB  B ALA   A 39  ? 0.1470 0.1556 0.1773 -0.0041 -0.0113 0.0124  39  ALA   A CB  
1091 N N   A ASN   A 40  ? 0.1313 0.1305 0.1546 0.0011  0.0049  0.0072  40  ASN   A N   
1092 N N   B ASN   A 40  ? 0.1345 0.1299 0.1516 -0.0028 0.0309  0.0278  40  ASN   A N   
1093 C CA  A ASN   A 40  ? 0.1421 0.1329 0.1470 -0.0032 0.0069  0.0030  40  ASN   A CA  
1094 C CA  B ASN   A 40  ? 0.1427 0.1273 0.1565 -0.0012 0.0218  0.0254  40  ASN   A CA  
1095 C C   A ASN   A 40  ? 0.1416 0.1294 0.1411 -0.0028 0.0084  0.0105  40  ASN   A C   
1096 C C   B ASN   A 40  ? 0.1456 0.1216 0.1569 -0.0119 0.0231  0.0268  40  ASN   A C   
1097 O O   A ASN   A 40  ? 0.1391 0.1266 0.1404 -0.0012 0.0016  0.0042  40  ASN   A O   
1098 O O   B ASN   A 40  ? 0.1325 0.1222 0.1741 -0.0140 0.0175  0.0278  40  ASN   A O   
1099 C CB  A ASN   A 40  ? 0.1545 0.1412 0.1616 -0.0010 -0.0111 0.0047  40  ASN   A CB  
1100 C CB  B ASN   A 40  ? 0.1479 0.1349 0.1439 0.0019  0.0004  0.0276  40  ASN   A CB  
1101 C CG  A ASN   A 40  ? 0.1652 0.1375 0.2012 0.0064  -0.0084 0.0115  40  ASN   A CG  
1102 C CG  B ASN   A 40  ? 0.1507 0.1402 0.1561 0.0026  0.0006  0.0230  40  ASN   A CG  
1103 O OD1 A ASN   A 40  ? 0.1698 0.1270 0.1855 0.0057  -0.0057 0.0178  40  ASN   A OD1 
1104 O OD1 B ASN   A 40  ? 0.1532 0.1417 0.1407 -0.0031 0.0131  0.0193  40  ASN   A OD1 
1105 N ND2 A ASN   A 40  ? 0.1696 0.1466 0.2330 0.0070  -0.0173 -0.0050 40  ASN   A ND2 
1106 N ND2 B ASN   A 40  ? 0.1515 0.1463 0.2021 -0.0001 -0.0027 -0.0009 40  ASN   A ND2 
1119 N N   A VAL   A 41  ? 0.1477 0.1409 0.1439 -0.0021 0.0122  0.0122  41  VAL   A N   
1120 N N   B VAL   A 41  ? 0.1552 0.1259 0.1368 -0.0067 0.0242  0.0220  41  VAL   A N   
1121 C CA  A VAL   A 41  ? 0.1494 0.1369 0.1755 0.0044  0.0301  0.0155  41  VAL   A CA  
1122 C CA  B VAL   A 41  ? 0.1653 0.1283 0.1650 -0.0047 0.0464  0.0193  41  VAL   A CA  
1123 C C   A VAL   A 41  ? 0.1456 0.1387 0.1806 0.0017  0.0286  0.0195  41  VAL   A C   
1124 C C   B VAL   A 41  ? 0.1569 0.1275 0.1833 -0.0057 0.0382  0.0176  41  VAL   A C   
1125 O O   A VAL   A 41  ? 0.1442 0.1387 0.1960 0.0063  0.0264  0.0082  41  VAL   A O   
1126 O O   B VAL   A 41  ? 0.1614 0.1195 0.2071 -0.0043 0.0314  0.0023  41  VAL   A O   
1127 C CB  A VAL   A 41  ? 0.1640 0.1457 0.1878 0.0011  0.0423  0.0083  41  VAL   A CB  
1128 C CB  B VAL   A 41  ? 0.1852 0.1449 0.1732 -0.0084 0.0666  0.0106  41  VAL   A CB  
1129 C CG1 A VAL   A 41  ? 0.1565 0.1454 0.2032 0.0075  0.0275  0.0124  41  VAL   A CG1 
1130 C CG1 B VAL   A 41  ? 0.1968 0.1526 0.1957 -0.0092 0.0624  -0.0022 41  VAL   A CG1 
1131 C CG2 A VAL   A 41  ? 0.1897 0.1586 0.1970 -0.0144 0.0485  0.0013  41  VAL   A CG2 
1132 C CG2 B VAL   A 41  ? 0.2020 0.1539 0.1755 -0.0180 0.0715  0.0090  41  VAL   A CG2 
1151 N N   . TYR   A 42  ? 0.1424 0.1259 0.1771 -0.0052 0.0291  0.0256  42  TYR   A N   
1152 C CA  . TYR   A 42  ? 0.1433 0.1243 0.1952 -0.0022 0.0352  0.0213  42  TYR   A CA  
1153 C C   . TYR   A 42  ? 0.1374 0.1273 0.1916 -0.0010 0.0277  0.0316  42  TYR   A C   
1154 O O   . TYR   A 42  ? 0.1347 0.1307 0.1980 -0.0130 0.0165  0.0077  42  TYR   A O   
1155 C CB  . TYR   A 42  ? 0.1618 0.1302 0.1747 -0.0100 0.0295  0.0289  42  TYR   A CB  
1156 C CG  . TYR   A 42  ? 0.1737 0.1407 0.1763 -0.0006 0.0239  0.0338  42  TYR   A CG  
1157 C CD1 . TYR   A 42  ? 0.1864 0.1563 0.1933 -0.0148 0.0425  0.0307  42  TYR   A CD1 
1158 C CD2 . TYR   A 42  ? 0.1887 0.1705 0.2035 -0.0018 0.0108  0.0287  42  TYR   A CD2 
1159 C CE1 . TYR   A 42  ? 0.1988 0.1703 0.1903 -0.0094 0.0422  0.0317  42  TYR   A CE1 
1160 C CE2 . TYR   A 42  ? 0.2083 0.1811 0.2202 -0.0182 0.0189  0.0279  42  TYR   A CE2 
1161 C CZ  . TYR   A 42  ? 0.2195 0.1837 0.1908 -0.0179 0.0407  0.0342  42  TYR   A CZ  
1162 O OH  . TYR   A 42  ? 0.2453 0.2075 0.2177 -0.0291 0.0440  0.0192  42  TYR   A OH  
1173 N N   . LEU   A 43  ? 0.1388 0.1237 0.1719 -0.0008 0.0217  0.0154  43  LEU   A N   
1174 C CA  . LEU   A 43  ? 0.1311 0.1227 0.1583 -0.0090 0.0064  0.0104  43  LEU   A CA  
1175 C C   . LEU   A 43  ? 0.1302 0.1314 0.1593 -0.0105 0.0025  0.0084  43  LEU   A C   
1176 O O   . LEU   A 43  ? 0.1439 0.1340 0.1854 0.0033  -0.0098 0.0027  43  LEU   A O   
1177 C CB  . LEU   A 43  ? 0.1391 0.1284 0.1914 -0.0105 0.0024  0.0136  43  LEU   A CB  
1178 C CG  . LEU   A 43  ? 0.1384 0.1332 0.2029 -0.0039 0.0026  0.0152  43  LEU   A CG  
1179 C CD1 . LEU   A 43  ? 0.1415 0.1458 0.2114 -0.0072 -0.0088 0.0106  43  LEU   A CD1 
1180 C CD2 . LEU   A 43  ? 0.1600 0.1282 0.2115 -0.0037 0.0087  0.0325  43  LEU   A CD2 
1192 N N   A LYS   A 44  ? 0.1391 0.1287 0.1542 0.0000  0.0081  0.0115  44  LYS   A N   
1193 N N   B LYS   A 44  ? 0.1439 0.1413 0.1622 -0.0025 0.0018  0.0070  44  LYS   A N   
1194 C CA  A LYS   A 44  ? 0.1458 0.1282 0.1663 0.0022  0.0264  0.0210  44  LYS   A CA  
1195 C CA  B LYS   A 44  ? 0.1552 0.1540 0.1820 -0.0017 0.0080  0.0105  44  LYS   A CA  
1196 C C   A LYS   A 44  ? 0.1286 0.1244 0.1650 0.0062  0.0112  0.0137  44  LYS   A C   
1197 C C   B LYS   A 44  ? 0.1458 0.1536 0.1776 0.0013  -0.0031 0.0054  44  LYS   A C   
1198 O O   A LYS   A 44  ? 0.1357 0.1370 0.1816 0.0036  0.0104  -0.0051 44  LYS   A O   
1199 O O   B LYS   A 44  ? 0.1497 0.1604 0.1844 -0.0033 -0.0077 0.0020  44  LYS   A O   
1200 C CB  A LYS   A 44  ? 0.1802 0.1471 0.2063 0.0022  0.0388  0.0260  44  LYS   A CB  
1201 C CB  B LYS   A 44  ? 0.1809 0.1752 0.2210 -0.0017 0.0150  0.0155  44  LYS   A CB  
1202 C CG  A LYS   A 44  ? 0.2124 0.1754 0.2583 0.0004  0.0499  0.0232  44  LYS   A CG  
1203 C CG  B LYS   A 44  ? 0.2034 0.1994 0.2688 -0.0012 0.0189  0.0165  44  LYS   A CG  
1204 C CD  A LYS   A 44  ? 0.2514 0.2223 0.3331 -0.0105 0.0364  0.0180  44  LYS   A CD  
1205 C CD  B LYS   A 44  ? 0.2340 0.2343 0.3293 -0.0096 0.0083  0.0175  44  LYS   A CD  
1206 C CE  A LYS   A 44  ? 0.2749 0.2591 0.3818 -0.0180 0.0352  0.0147  44  LYS   A CE  
1207 C CE  B LYS   A 44  ? 0.2513 0.2627 0.3661 -0.0195 0.0022  0.0217  44  LYS   A CE  
1208 N NZ  A LYS   A 44  ? 0.2881 0.2812 0.4067 -0.0237 0.0353  0.0155  44  LYS   A NZ  
1209 N NZ  B LYS   A 44  ? 0.2653 0.2852 0.3902 -0.0282 0.0031  0.0269  44  LYS   A NZ  
1236 N N   A HIS   A 45  ? 0.1210 0.1225 0.1535 0.0033  0.0105  0.0188  45  HIS   A N   
1237 N N   B HIS   A 45  ? 0.1447 0.1542 0.1680 -0.0001 -0.0017 0.0016  45  HIS   A N   
1238 C CA  A HIS   A 45  ? 0.1203 0.1204 0.1674 -0.0016 -0.0007 0.0196  45  HIS   A CA  
1239 C CA  B HIS   A 45  ? 0.1479 0.1525 0.1801 0.0024  -0.0021 -0.0025 45  HIS   A CA  
1240 C C   A HIS   A 45  ? 0.1183 0.1317 0.1807 0.0006  0.0007  0.0221  45  HIS   A C   
1241 C C   B HIS   A 45  ? 0.1566 0.1564 0.1936 0.0074  0.0000  -0.0117 45  HIS   A C   
1242 O O   A HIS   A 45  ? 0.1255 0.1418 0.2062 -0.0010 0.0015  0.0192  45  HIS   A O   
1243 O O   B HIS   A 45  ? 0.1666 0.1582 0.2179 0.0137  0.0075  -0.0264 45  HIS   A O   
1244 C CB  A HIS   A 45  ? 0.1250 0.1137 0.1581 -0.0103 0.0049  0.0057  45  HIS   A CB  
1245 C CB  B HIS   A 45  ? 0.1430 0.1505 0.1694 0.0033  0.0055  -0.0016 45  HIS   A CB  
1246 C CG  A HIS   A 45  ? 0.1283 0.1133 0.1629 -0.0099 0.0018  0.0164  45  HIS   A CG  
1247 C CG  B HIS   A 45  ? 0.1288 0.1447 0.1632 0.0043  0.0046  0.0125  45  HIS   A CG  
1248 N ND1 A HIS   A 45  ? 0.1289 0.1252 0.1894 -0.0094 0.0105  0.0197  45  HIS   A ND1 
1249 N ND1 B HIS   A 45  ? 0.1193 0.1486 0.1670 0.0079  -0.0097 0.0249  45  HIS   A ND1 
1250 C CD2 A HIS   A 45  ? 0.1324 0.1241 0.1646 -0.0153 -0.0129 0.0242  45  HIS   A CD2 
1251 C CD2 B HIS   A 45  ? 0.1251 0.1421 0.1591 0.0054  -0.0036 0.0246  45  HIS   A CD2 
1252 C CE1 A HIS   A 45  ? 0.1344 0.1365 0.1663 -0.0172 0.0034  0.0290  45  HIS   A CE1 
1253 C CE1 B HIS   A 45  ? 0.1210 0.1475 0.1453 0.0009  -0.0195 0.0288  45  HIS   A CE1 
1254 N NE2 A HIS   A 45  ? 0.1381 0.1423 0.1628 -0.0123 0.0114  0.0381  45  HIS   A NE2 
1255 N NE2 B HIS   A 45  ? 0.1248 0.1489 0.1545 0.0067  -0.0105 0.0328  45  HIS   A NE2 
1270 N N   A GLY   A 46  ? 0.1425 0.1491 0.1918 0.0165  -0.0195 0.0370  46  GLY   A N   
1271 N N   B GLY   A 46  ? 0.1706 0.1687 0.1967 0.0127  -0.0077 0.0037  46  GLY   A N   
1272 C CA  A GLY   A 46  ? 0.1552 0.1639 0.2035 0.0260  -0.0168 0.0370  46  GLY   A CA  
1273 C CA  B GLY   A 46  ? 0.1644 0.1796 0.1881 0.0178  -0.0049 0.0144  46  GLY   A CA  
1274 C C   A GLY   A 46  ? 0.1674 0.1628 0.1957 0.0344  -0.0202 0.0349  46  GLY   A C   
1275 C C   B GLY   A 46  ? 0.1618 0.1782 0.1547 0.0234  0.0027  0.0172  46  GLY   A C   
1276 O O   A GLY   A 46  ? 0.1753 0.1615 0.1915 0.0306  -0.0322 0.0300  46  GLY   A O   
1277 O O   B GLY   A 46  ? 0.1628 0.1905 0.1396 0.0278  -0.0005 0.0055  46  GLY   A O   
1284 N N   A GLY   A 47  ? 0.1697 0.1696 0.1926 0.0414  -0.0165 0.0232  47  GLY   A N   
1285 N N   B GLY   A 47  ? 0.1685 0.1737 0.1545 0.0219  0.0029  0.0000  47  GLY   A N   
1286 C CA  A GLY   A 47  ? 0.1678 0.1751 0.1743 0.0442  -0.0152 0.0108  47  GLY   A CA  
1287 C CA  B GLY   A 47  ? 0.1648 0.1751 0.1695 0.0192  -0.0007 -0.0067 47  GLY   A CA  
1288 C C   A GLY   A 47  ? 0.1597 0.1715 0.1624 0.0374  -0.0249 0.0060  47  GLY   A C   
1289 C C   B GLY   A 47  ? 0.1546 0.1653 0.1481 0.0198  0.0050  -0.0090 47  GLY   A C   
1290 O O   A GLY   A 47  ? 0.1557 0.1622 0.1518 0.0379  -0.0199 0.0163  47  GLY   A O   
1291 O O   B GLY   A 47  ? 0.1501 0.1519 0.1399 0.0278  0.0032  0.0070  47  GLY   A O   
1298 N N   A GLY   A 48  ? 0.1477 0.1685 0.1645 0.0395  -0.0245 0.0010  48  GLY   A N   
1299 N N   B GLY   A 48  ? 0.1573 0.1650 0.1578 0.0160  0.0002  -0.0069 48  GLY   A N   
1300 C CA  A GLY   A 48  ? 0.1415 0.1621 0.1658 0.0139  -0.0162 -0.0053 48  GLY   A CA  
1301 C CA  B GLY   A 48  ? 0.1598 0.1519 0.1592 0.0131  0.0011  -0.0045 48  GLY   A CA  
1302 C C   A GLY   A 48  ? 0.1324 0.1576 0.1294 -0.0055 -0.0048 -0.0148 48  GLY   A C   
1303 C C   B GLY   A 48  ? 0.1563 0.1487 0.1501 0.0133  0.0081  -0.0103 48  GLY   A C   
1304 O O   A GLY   A 48  ? 0.1443 0.1614 0.1324 0.0024  -0.0117 -0.0145 48  GLY   A O   
1305 O O   B GLY   A 48  ? 0.1602 0.1438 0.1460 0.0205  0.0246  -0.0172 48  GLY   A O   
1312 N N   A VAL   A 49  ? 0.1242 0.1432 0.1417 -0.0099 0.0013  -0.0056 49  VAL   A N   
1313 N N   B VAL   A 49  ? 0.1514 0.1425 0.1422 0.0118  -0.0012 -0.0219 49  VAL   A N   
1314 C CA  A VAL   A 49  ? 0.1350 0.1414 0.1463 -0.0204 0.0078  0.0073  49  VAL   A CA  
1315 C CA  B VAL   A 49  ? 0.1527 0.1551 0.1605 0.0087  -0.0190 -0.0073 49  VAL   A CA  
1316 C C   A VAL   A 49  ? 0.1270 0.1337 0.1127 -0.0099 0.0106  0.0140  49  VAL   A C   
1317 C C   B VAL   A 49  ? 0.1461 0.1329 0.1524 0.0105  -0.0185 -0.0201 49  VAL   A C   
1318 O O   A VAL   A 49  ? 0.1323 0.1377 0.1004 -0.0171 0.0156  -0.0001 49  VAL   A O   
1319 O O   B VAL   A 49  ? 0.1465 0.1401 0.1366 0.0141  -0.0134 -0.0067 49  VAL   A O   
1320 C CB  A VAL   A 49  ? 0.1629 0.1334 0.1658 -0.0310 0.0093  -0.0083 49  VAL   A CB  
1321 C CB  B VAL   A 49  ? 0.1704 0.1815 0.2076 0.0061  -0.0198 0.0067  49  VAL   A CB  
1322 C CG1 A VAL   A 49  ? 0.1731 0.1274 0.2083 -0.0355 0.0091  -0.0081 49  VAL   A CG1 
1323 C CG1 B VAL   A 49  ? 0.1887 0.2032 0.2436 0.0015  0.0015  0.0218  49  VAL   A CG1 
1324 C CG2 A VAL   A 49  ? 0.1632 0.1285 0.2005 -0.0467 0.0039  0.0039  49  VAL   A CG2 
1325 C CG2 B VAL   A 49  ? 0.1698 0.1752 0.2068 0.0180  -0.0279 0.0165  49  VAL   A CG2 
1344 N N   A ALA   A 50  ? 0.1192 0.1337 0.1152 -0.0094 0.0088  0.0113  50  ALA   A N   
1345 N N   B ALA   A 50  ? 0.1501 0.1240 0.1499 0.0133  -0.0235 -0.0072 50  ALA   A N   
1346 C CA  A ALA   A 50  ? 0.1139 0.1407 0.1526 -0.0119 -0.0006 0.0112  50  ALA   A CA  
1347 C CA  B ALA   A 50  ? 0.1439 0.1241 0.1253 0.0073  -0.0144 -0.0134 50  ALA   A CA  
1348 C C   A ALA   A 50  ? 0.1093 0.1422 0.1290 -0.0075 0.0072  0.0177  50  ALA   A C   
1349 C C   B ALA   A 50  ? 0.1450 0.1210 0.0976 -0.0011 0.0032  -0.0087 50  ALA   A C   
1350 O O   A ALA   A 50  ? 0.1110 0.1386 0.1484 0.0001  -0.0007 0.0111  50  ALA   A O   
1351 O O   B ALA   A 50  ? 0.1479 0.1249 0.0812 -0.0049 0.0244  -0.0139 50  ALA   A O   
1352 C CB  A ALA   A 50  ? 0.1148 0.1448 0.1627 -0.0160 0.0088  0.0240  50  ALA   A CB  
1353 C CB  B ALA   A 50  ? 0.1456 0.1252 0.1136 0.0114  -0.0062 -0.0226 50  ALA   A CB  
1364 N N   A GLY   A 51  ? 0.1110 0.1416 0.1479 0.0010  -0.0072 0.0070  51  GLY   A N   
1365 N N   B GLY   A 51  ? 0.1497 0.1177 0.1491 0.0007  -0.0100 -0.0097 51  GLY   A N   
1366 C CA  A GLY   A 51  ? 0.1306 0.1348 0.1746 0.0039  -0.0107 0.0139  51  GLY   A CA  
1367 C CA  B GLY   A 51  ? 0.1576 0.1105 0.1398 0.0004  -0.0224 -0.0232 51  GLY   A CA  
1368 C C   A GLY   A 51  ? 0.1204 0.1366 0.1730 0.0077  -0.0003 -0.0075 51  GLY   A C   
1369 C C   B GLY   A 51  ? 0.1434 0.1208 0.1455 0.0072  -0.0124 -0.0165 51  GLY   A C   
1370 O O   A GLY   A 51  ? 0.1260 0.1497 0.1805 0.0054  -0.0171 -0.0139 51  GLY   A O   
1371 O O   B GLY   A 51  ? 0.1425 0.1333 0.1566 0.0071  -0.0069 -0.0310 51  GLY   A O   
1378 N N   A ALA   A 52  ? 0.1174 0.1495 0.1768 -0.0051 -0.0003 -0.0162 52  ALA   A N   
1379 N N   B ALA   A 52  ? 0.1396 0.1283 0.1426 0.0022  -0.0058 -0.0145 52  ALA   A N   
1380 C CA  A ALA   A 52  ? 0.1205 0.1598 0.1948 -0.0076 0.0034  -0.0248 52  ALA   A CA  
1381 C CA  B ALA   A 52  ? 0.1346 0.1434 0.1545 0.0005  0.0049  -0.0181 52  ALA   A CA  
1382 C C   A ALA   A 52  ? 0.1240 0.1572 0.1856 -0.0055 0.0165  -0.0044 52  ALA   A C   
1383 C C   B ALA   A 52  ? 0.1297 0.1441 0.1259 -0.0040 0.0153  -0.0214 52  ALA   A C   
1384 O O   A ALA   A 52  ? 0.1291 0.1682 0.2048 0.0051  0.0135  -0.0101 52  ALA   A O   
1385 O O   B ALA   A 52  ? 0.1338 0.1585 0.1212 -0.0034 0.0246  -0.0282 52  ALA   A O   
1386 C CB  A ALA   A 52  ? 0.1239 0.1769 0.2087 -0.0148 -0.0137 -0.0292 52  ALA   A CB  
1387 C CB  B ALA   A 52  ? 0.1346 0.1581 0.1675 0.0024  0.0069  -0.0137 52  ALA   A CB  
1398 N N   A LEU   A 53  ? 0.1226 0.1455 0.1733 -0.0082 0.0135  0.0046  53  LEU   A N   
1399 N N   B LEU   A 53  ? 0.1272 0.1399 0.1281 -0.0041 0.0047  -0.0194 53  LEU   A N   
1400 C CA  A LEU   A 53  ? 0.1365 0.1468 0.1862 -0.0089 0.0106  0.0090  53  LEU   A CA  
1401 C CA  B LEU   A 53  ? 0.1328 0.1447 0.1243 -0.0028 -0.0053 -0.0095 53  LEU   A CA  
1402 C C   A LEU   A 53  ? 0.1358 0.1524 0.1557 -0.0074 0.0145  0.0035  53  LEU   A C   
1403 C C   B LEU   A 53  ? 0.1312 0.1490 0.1158 0.0030  -0.0076 -0.0016 53  LEU   A C   
1404 O O   A LEU   A 53  ? 0.1377 0.1502 0.1632 -0.0149 0.0183  -0.0061 53  LEU   A O   
1405 O O   B LEU   A 53  ? 0.1349 0.1513 0.1373 0.0064  -0.0104 -0.0033 53  LEU   A O   
1406 C CB  A LEU   A 53  ? 0.1445 0.1417 0.2186 -0.0144 0.0158  0.0184  53  LEU   A CB  
1407 C CB  B LEU   A 53  ? 0.1342 0.1460 0.1232 -0.0096 -0.0035 -0.0096 53  LEU   A CB  
1408 C CG  A LEU   A 53  ? 0.1567 0.1440 0.2116 -0.0193 0.0002  0.0227  53  LEU   A CG  
1409 C CG  B LEU   A 53  ? 0.1384 0.1546 0.1205 -0.0122 -0.0047 -0.0086 53  LEU   A CG  
1410 C CD1 A LEU   A 53  ? 0.1489 0.1514 0.1940 -0.0167 -0.0068 0.0218  53  LEU   A CD1 
1411 C CD1 B LEU   A 53  ? 0.1454 0.1604 0.1481 -0.0186 -0.0051 -0.0138 53  LEU   A CD1 
1412 C CD2 A LEU   A 53  ? 0.1723 0.1592 0.2156 -0.0220 -0.0169 0.0230  53  LEU   A CD2 
1413 C CD2 B LEU   A 53  ? 0.1343 0.1659 0.1074 -0.0201 0.0046  0.0059  53  LEU   A CD2 
1436 N N   A ASN   A 54  ? 0.1239 0.1440 0.1616 -0.0084 0.0031  0.0025  54  ASN   A N   
1437 N N   B ASN   A 54  ? 0.1249 0.1446 0.1465 0.0009  -0.0085 -0.0050 54  ASN   A N   
1438 C CA  A ASN   A 54  ? 0.1197 0.1398 0.1710 -0.0033 -0.0039 0.0078  54  ASN   A CA  
1439 C CA  B ASN   A 54  ? 0.1229 0.1438 0.1647 -0.0029 -0.0076 -0.0032 54  ASN   A CA  
1440 C C   A ASN   A 54  ? 0.1281 0.1426 0.1541 -0.0081 0.0040  0.0093  54  ASN   A C   
1441 C C   B ASN   A 54  ? 0.1318 0.1476 0.1566 -0.0128 -0.0009 0.0062  54  ASN   A C   
1442 O O   A ASN   A 54  ? 0.1310 0.1479 0.1622 -0.0045 -0.0033 -0.0029 54  ASN   A O   
1443 O O   B ASN   A 54  ? 0.1378 0.1536 0.1653 -0.0178 -0.0082 0.0041  54  ASN   A O   
1444 C CB  A ASN   A 54  ? 0.1177 0.1395 0.1809 -0.0088 -0.0045 0.0152  54  ASN   A CB  
1445 C CB  B ASN   A 54  ? 0.1207 0.1453 0.1602 -0.0023 -0.0061 -0.0071 54  ASN   A CB  
1446 C CG  A ASN   A 54  ? 0.1218 0.1435 0.1841 -0.0108 -0.0080 0.0176  54  ASN   A CG  
1447 C CG  B ASN   A 54  ? 0.1246 0.1464 0.1556 -0.0006 -0.0037 -0.0221 54  ASN   A CG  
1448 O OD1 A ASN   A 54  ? 0.1171 0.1405 0.2077 -0.0128 -0.0068 0.0222  54  ASN   A OD1 
1449 O OD1 B ASN   A 54  ? 0.1202 0.1430 0.1451 0.0028  0.0002  -0.0439 54  ASN   A OD1 
1450 N ND2 A ASN   A 54  ? 0.1317 0.1558 0.1770 -0.0156 -0.0175 0.0291  54  ASN   A ND2 
1451 N ND2 B ASN   A 54  ? 0.1360 0.1569 0.1685 -0.0102 -0.0114 -0.0017 54  ASN   A ND2 
1464 N N   . LYS   A 55  ? 0.1315 0.1450 0.1604 -0.0054 -0.0040 -0.0022 55  LYS   A N   
1465 C CA  . LYS   A 55  ? 0.1426 0.1586 0.1806 0.0086  -0.0103 -0.0209 55  LYS   A CA  
1466 C C   . LYS   A 55  ? 0.1408 0.1643 0.1688 0.0018  0.0019  -0.0185 55  LYS   A C   
1467 O O   . LYS   A 55  ? 0.1508 0.1756 0.1705 0.0007  -0.0014 -0.0215 55  LYS   A O   
1468 C CB  . LYS   A 55  ? 0.1519 0.1740 0.2051 0.0201  -0.0026 -0.0298 55  LYS   A CB  
1469 C CG  . LYS   A 55  ? 0.1768 0.2132 0.2114 0.0444  -0.0289 -0.0396 55  LYS   A CG  
1470 C CD  . LYS   A 55  ? 0.2077 0.2475 0.2492 0.0602  -0.0291 -0.0327 55  LYS   A CD  
1471 C CE  . LYS   A 55  ? 0.2391 0.2728 0.2798 0.0757  -0.0252 -0.0280 55  LYS   A CE  
1472 N NZ  . LYS   A 55  ? 0.2479 0.3055 0.3032 0.0832  -0.0291 -0.0249 55  LYS   A NZ  
1487 N N   . ALA   A 56  ? 0.1440 0.1659 0.1761 -0.0074 0.0016  -0.0132 56  ALA   A N   
1488 C CA  . ALA   A 56  ? 0.1501 0.1911 0.1740 -0.0162 0.0059  -0.0178 56  ALA   A CA  
1489 C C   . ALA   A 56  ? 0.1591 0.1994 0.1627 -0.0097 0.0151  -0.0322 56  ALA   A C   
1490 O O   . ALA   A 56  ? 0.1616 0.2349 0.1605 0.0040  0.0131  -0.0213 56  ALA   A O   
1491 C CB  . ALA   A 56  ? 0.1619 0.2092 0.1741 -0.0201 0.0091  -0.0063 56  ALA   A CB  
1497 N N   . THR   A 57  ? 0.1446 0.1734 0.1533 -0.0150 0.0152  -0.0268 57  THR   A N   
1498 C CA  . THR   A 57  ? 0.1493 0.1716 0.1766 -0.0144 0.0056  -0.0102 57  THR   A CA  
1499 C C   . THR   A 57  ? 0.1522 0.1806 0.1645 -0.0034 0.0008  -0.0148 57  THR   A C   
1500 O O   . THR   A 57  ? 0.1494 0.1882 0.1756 -0.0157 -0.0068 -0.0251 57  THR   A O   
1501 C CB  . THR   A 57  ? 0.1422 0.1765 0.1634 -0.0117 0.0016  -0.0019 57  THR   A CB  
1502 O OG1 . THR   A 57  ? 0.1357 0.1684 0.1683 -0.0115 -0.0009 -0.0084 57  THR   A OG1 
1503 C CG2 . THR   A 57  ? 0.1533 0.1811 0.1481 -0.0043 0.0065  -0.0010 57  THR   A CG2 
1511 N N   . ASN   A 58  ? 0.1566 0.1716 0.1906 -0.0077 0.0095  -0.0239 58  ASN   A N   
1512 C CA  . ASN   A 58  ? 0.1734 0.1664 0.2178 -0.0123 0.0245  -0.0432 58  ASN   A CA  
1513 C C   . ASN   A 58  ? 0.1453 0.1582 0.2078 -0.0014 0.0080  -0.0343 58  ASN   A C   
1514 O O   . ASN   A 58  ? 0.1538 0.1637 0.2185 -0.0121 -0.0019 -0.0295 58  ASN   A O   
1515 C CB  . ASN   A 58  ? 0.2202 0.1873 0.2448 -0.0183 0.0417  -0.0631 58  ASN   A CB  
1516 C CG  . ASN   A 58  ? 0.2589 0.2117 0.3032 -0.0128 0.0353  -0.0265 58  ASN   A CG  
1517 O OD1 . ASN   A 58  ? 0.2879 0.2023 0.3334 0.0228  0.0784  -0.0194 58  ASN   A OD1 
1518 N ND2 . ASN   A 58  ? 0.2656 0.2206 0.3167 -0.0110 0.0133  -0.0220 58  ASN   A ND2 
1525 N N   . ASN   A 59  ? 0.1250 0.1482 0.1985 -0.0009 -0.0059 -0.0177 59  ASN   A N   
1526 C CA  . ASN   A 59  ? 0.1349 0.1360 0.1886 -0.0093 -0.0053 -0.0015 59  ASN   A CA  
1527 C C   . ASN   A 59  ? 0.1384 0.1429 0.1785 -0.0128 -0.0107 0.0031  59  ASN   A C   
1528 O O   . ASN   A 59  ? 0.1398 0.1437 0.1624 -0.0110 -0.0030 0.0024  59  ASN   A O   
1529 C CB  . ASN   A 59  ? 0.1436 0.1344 0.1911 -0.0012 -0.0131 -0.0129 59  ASN   A CB  
1530 C CG  . ASN   A 59  ? 0.1493 0.1388 0.1914 0.0023  -0.0247 0.0004  59  ASN   A CG  
1531 O OD1 . ASN   A 59  ? 0.1613 0.1486 0.1644 -0.0119 -0.0221 0.0002  59  ASN   A OD1 
1532 N ND2 . ASN   A 59  ? 0.1621 0.1451 0.2180 -0.0107 -0.0204 0.0123  59  ASN   A ND2 
1539 N N   . ALA   A 60  ? 0.1303 0.1509 0.1913 -0.0075 -0.0029 -0.0012 60  ALA   A N   
1540 C CA  . ALA   A 60  ? 0.1319 0.1529 0.1734 -0.0044 -0.0114 0.0018  60  ALA   A CA  
1541 C C   . ALA   A 60  ? 0.1358 0.1444 0.1850 -0.0059 -0.0050 -0.0004 60  ALA   A C   
1542 O O   . ALA   A 60  ? 0.1262 0.1428 0.1944 -0.0017 -0.0087 -0.0051 60  ALA   A O   
1543 C CB  . ALA   A 60  ? 0.1474 0.1535 0.1693 -0.0024 -0.0188 -0.0101 60  ALA   A CB  
1549 N N   . MET   A 61  ? 0.1250 0.1355 0.1786 -0.0080 0.0044  -0.0058 61  MET   A N   
1550 C CA  . MET   A 61  ? 0.1267 0.1338 0.1782 -0.0058 -0.0002 0.0088  61  MET   A CA  
1551 C C   . MET   A 61  ? 0.1250 0.1367 0.1788 -0.0122 -0.0044 -0.0025 61  MET   A C   
1552 O O   . MET   A 61  ? 0.1288 0.1409 0.1743 0.0005  0.0020  0.0096  61  MET   A O   
1553 C CB  . MET   A 61  ? 0.1386 0.1370 0.1693 -0.0068 0.0038  0.0030  61  MET   A CB  
1554 C CG  . MET   A 61  ? 0.1361 0.1404 0.1745 -0.0093 0.0007  0.0077  61  MET   A CG  
1555 S SD  . MET   A 61  ? 0.1377 0.1441 0.2173 -0.0130 -0.0005 -0.0136 61  MET   A SD  
1556 C CE  . MET   A 61  ? 0.1596 0.1530 0.2470 -0.0176 0.0212  -0.0089 61  MET   A CE  
1566 N N   . GLN   A 62  ? 0.1298 0.1331 0.1863 -0.0133 -0.0073 0.0018  62  GLN   A N   
1567 C CA  . GLN   A 62  ? 0.1328 0.1252 0.1871 -0.0081 0.0062  0.0088  62  GLN   A CA  
1568 C C   . GLN   A 62  ? 0.1323 0.1101 0.1930 -0.0007 0.0101  0.0056  62  GLN   A C   
1569 O O   . GLN   A 62  ? 0.1350 0.1335 0.1730 -0.0030 0.0091  -0.0016 62  GLN   A O   
1570 C CB  . GLN   A 62  ? 0.1261 0.1281 0.1963 -0.0129 0.0043  0.0055  62  GLN   A CB  
1571 C CG  . GLN   A 62  ? 0.1310 0.1246 0.1964 -0.0081 0.0158  0.0207  62  GLN   A CG  
1572 C CD  . GLN   A 62  ? 0.1388 0.1300 0.1794 -0.0007 0.0201  0.0056  62  GLN   A CD  
1573 O OE1 . GLN   A 62  ? 0.1341 0.1473 0.1979 0.0029  0.0069  0.0008  62  GLN   A OE1 
1574 N NE2 . GLN   A 62  ? 0.1492 0.1405 0.1851 0.0024  0.0077  -0.0013 62  GLN   A NE2 
1583 N N   . VAL   A 63  ? 0.1287 0.1288 0.2105 -0.0096 0.0109  -0.0156 63  VAL   A N   
1584 C CA  . VAL   A 63  ? 0.1314 0.1417 0.2249 -0.0092 -0.0024 -0.0140 63  VAL   A CA  
1585 C C   . VAL   A 63  ? 0.1211 0.1386 0.2031 -0.0149 -0.0053 -0.0209 63  VAL   A C   
1586 O O   . VAL   A 63  ? 0.1214 0.1396 0.2225 -0.0145 -0.0100 -0.0064 63  VAL   A O   
1587 C CB  . VAL   A 63  ? 0.1474 0.1552 0.2465 -0.0145 -0.0046 -0.0277 63  VAL   A CB  
1588 C CG1 . VAL   A 63  ? 0.1615 0.1742 0.2818 -0.0154 -0.0197 -0.0546 63  VAL   A CG1 
1589 C CG2 . VAL   A 63  ? 0.1543 0.1484 0.2632 -0.0119 0.0140  -0.0337 63  VAL   A CG2 
1599 N N   . GLU   A 64  ? 0.1295 0.1423 0.1765 -0.0045 -0.0102 -0.0132 64  GLU   A N   
1600 C CA  . GLU   A 64  ? 0.1285 0.1514 0.1920 -0.0044 -0.0173 0.0000  64  GLU   A CA  
1601 C C   . GLU   A 64  ? 0.1212 0.1390 0.1967 -0.0053 0.0046  0.0095  64  GLU   A C   
1602 O O   . GLU   A 64  ? 0.1264 0.1444 0.1943 -0.0010 0.0023  0.0003  64  GLU   A O   
1603 C CB  . GLU   A 64  ? 0.1396 0.1574 0.2000 -0.0073 0.0025  0.0053  64  GLU   A CB  
1604 C CG  . GLU   A 64  ? 0.1464 0.1580 0.2355 -0.0070 0.0015  0.0061  64  GLU   A CG  
1605 C CD  . GLU   A 64  ? 0.1576 0.1744 0.2319 -0.0177 0.0069  0.0084  64  GLU   A CD  
1606 O OE1 . GLU   A 64  ? 0.1582 0.1835 0.2332 -0.0245 0.0126  0.0090  64  GLU   A OE1 
1607 O OE2 . GLU   A 64  ? 0.1774 0.1717 0.2122 -0.0211 -0.0132 0.0129  64  GLU   A OE2 
1614 N N   . SER   A 65  ? 0.1182 0.1381 0.1784 0.0003  0.0034  0.0036  65  SER   A N   
1615 C CA  . SER   A 65  ? 0.1232 0.1309 0.1914 -0.0014 -0.0051 -0.0030 65  SER   A CA  
1616 C C   . SER   A 65  ? 0.1289 0.1368 0.1858 -0.0028 -0.0044 0.0008  65  SER   A C   
1617 O O   . SER   A 65  ? 0.1368 0.1412 0.2064 0.0004  0.0157  -0.0041 65  SER   A O   
1618 C CB  . SER   A 65  ? 0.1314 0.1359 0.2026 -0.0047 0.0016  0.0054  65  SER   A CB  
1619 O OG  . SER   A 65  ? 0.1273 0.1466 0.1740 -0.0119 0.0027  0.0165  65  SER   A OG  
1625 N N   . ASP   A 66  ? 0.1306 0.1381 0.1693 -0.0037 0.0052  -0.0005 66  ASP   A N   
1626 C CA  . ASP   A 66  ? 0.1386 0.1504 0.2017 0.0012  0.0153  0.0129  66  ASP   A CA  
1627 C C   . ASP   A 66  ? 0.1302 0.1487 0.2221 -0.0041 0.0059  0.0231  66  ASP   A C   
1628 O O   . ASP   A 66  ? 0.1380 0.1583 0.2244 -0.0027 0.0252  0.0226  66  ASP   A O   
1629 C CB  . ASP   A 66  ? 0.1466 0.1530 0.2405 0.0094  0.0136  0.0269  66  ASP   A CB  
1630 C CG  . ASP   A 66  ? 0.1743 0.1680 0.2672 0.0002  0.0023  0.0515  66  ASP   A CG  
1631 O OD1 . ASP   A 66  ? 0.1728 0.2042 0.2432 -0.0083 -0.0098 0.0565  66  ASP   A OD1 
1632 O OD2 . ASP   A 66  ? 0.1898 0.1839 0.3507 0.0179  -0.0086 0.0247  66  ASP   A OD2 
1637 N N   . ASP   A 67  ? 0.1296 0.1509 0.2241 -0.0054 0.0051  0.0234  67  ASP   A N   
1638 C CA  . ASP   A 67  ? 0.1282 0.1674 0.2338 -0.0029 0.0114  0.0218  67  ASP   A CA  
1639 C C   . ASP   A 67  ? 0.1312 0.1635 0.2277 -0.0013 0.0136  0.0229  67  ASP   A C   
1640 O O   . ASP   A 67  ? 0.1285 0.1694 0.2379 0.0024  0.0210  0.0267  67  ASP   A O   
1641 C CB  . ASP   A 67  ? 0.1391 0.1680 0.2619 -0.0073 -0.0106 0.0357  67  ASP   A CB  
1642 C CG  . ASP   A 67  ? 0.1405 0.1882 0.2977 -0.0110 -0.0221 0.0466  67  ASP   A CG  
1643 O OD1 . ASP   A 67  ? 0.1444 0.2101 0.3800 -0.0116 -0.0349 0.0568  67  ASP   A OD1 
1644 O OD2 . ASP   A 67  ? 0.1447 0.1968 0.2704 0.0048  -0.0122 0.0400  67  ASP   A OD2 
1649 N N   . TYR   A 68  ? 0.1410 0.1510 0.2223 0.0026  0.0256  0.0268  68  TYR   A N   
1650 C CA  . TYR   A 68  ? 0.1482 0.1455 0.2282 0.0011  0.0231  0.0223  68  TYR   A CA  
1651 C C   . TYR   A 68  ? 0.1404 0.1477 0.2237 0.0005  0.0268  0.0146  68  TYR   A C   
1652 O O   . TYR   A 68  ? 0.1484 0.1519 0.2219 0.0113  0.0206  0.0200  68  TYR   A O   
1653 C CB  . TYR   A 68  ? 0.1474 0.1396 0.2472 0.0061  0.0454  0.0229  68  TYR   A CB  
1654 C CG  . TYR   A 68  ? 0.1556 0.1543 0.2709 0.0058  0.0540  0.0285  68  TYR   A CG  
1655 C CD1 . TYR   A 68  ? 0.1641 0.1656 0.3039 -0.0214 0.0453  -0.0123 68  TYR   A CD1 
1656 C CD2 . TYR   A 68  ? 0.1817 0.1632 0.3017 0.0125  0.0643  0.0330  68  TYR   A CD2 
1657 C CE1 . TYR   A 68  ? 0.1748 0.1784 0.3475 -0.0258 0.0579  -0.0194 68  TYR   A CE1 
1658 C CE2 . TYR   A 68  ? 0.1846 0.1682 0.3351 -0.0053 0.0787  0.0064  68  TYR   A CE2 
1659 C CZ  . TYR   A 68  ? 0.1819 0.1757 0.3658 -0.0186 0.0660  -0.0230 68  TYR   A CZ  
1660 O OH  . TYR   A 68  ? 0.2074 0.1883 0.4064 -0.0148 0.0478  -0.0564 68  TYR   A OH  
1670 N N   . ILE   A 69  ? 0.1307 0.1378 0.2063 -0.0001 0.0218  0.0144  69  ILE   A N   
1671 C CA  . ILE   A 69  ? 0.1405 0.1470 0.1956 0.0018  0.0059  0.0038  69  ILE   A CA  
1672 C C   . ILE   A 69  ? 0.1452 0.1410 0.1948 0.0098  0.0178  0.0140  69  ILE   A C   
1673 O O   . ILE   A 69  ? 0.1499 0.1518 0.1866 0.0006  0.0165  0.0093  69  ILE   A O   
1674 C CB  . ILE   A 69  ? 0.1488 0.1665 0.2080 0.0054  0.0058  -0.0048 69  ILE   A CB  
1675 C CG1 . ILE   A 69  ? 0.1467 0.1767 0.2192 0.0127  0.0096  -0.0296 69  ILE   A CG1 
1676 C CG2 . ILE   A 69  ? 0.1675 0.1868 0.2429 0.0151  0.0025  -0.0087 69  ILE   A CG2 
1677 C CD1 . ILE   A 69  ? 0.1511 0.1905 0.2463 -0.0031 0.0097  -0.0381 69  ILE   A CD1 
1689 N N   . ALA   A 70  ? 0.1500 0.1473 0.2071 -0.0036 0.0253  0.0184  70  ALA   A N   
1690 C CA  . ALA   A 70  ? 0.1497 0.1643 0.2185 -0.0136 0.0280  0.0210  70  ALA   A CA  
1691 C C   . ALA   A 70  ? 0.1508 0.1740 0.2186 -0.0121 0.0328  0.0161  70  ALA   A C   
1692 O O   . ALA   A 70  ? 0.1673 0.2082 0.2512 0.0076  0.0524  0.0462  70  ALA   A O   
1693 C CB  . ALA   A 70  ? 0.1553 0.1571 0.2591 -0.0184 0.0329  0.0160  70  ALA   A CB  
1699 N N   . THR   A 71  ? 0.1438 0.1705 0.2053 -0.0000 0.0201  0.0278  71  THR   A N   
1700 C CA  . THR   A 71  ? 0.1540 0.1871 0.2571 0.0083  0.0146  0.0258  71  THR   A CA  
1701 C C   . THR   A 71  ? 0.1450 0.1833 0.2871 0.0135  0.0360  0.0298  71  THR   A C   
1702 O O   . THR   A 71  ? 0.1493 0.2098 0.3446 0.0090  0.0520  0.0120  71  THR   A O   
1703 C CB  . THR   A 71  ? 0.1851 0.2207 0.2874 0.0168  -0.0203 0.0316  71  THR   A CB  
1704 O OG1 . THR   A 71  ? 0.2178 0.2444 0.2872 0.0046  -0.0415 0.0258  71  THR   A OG1 
1705 C CG2 . THR   A 71  ? 0.1948 0.2382 0.3161 0.0247  -0.0365 0.0470  71  THR   A CG2 
1713 N N   . ASN   A 72  ? 0.1480 0.1694 0.2365 0.0146  0.0354  0.0380  72  ASN   A N   
1714 C CA  . ASN   A 72  ? 0.1506 0.1702 0.2668 0.0176  0.0445  0.0339  72  ASN   A CA  
1715 C C   . ASN   A 72  ? 0.1611 0.1608 0.2658 0.0126  0.0522  0.0253  72  ASN   A C   
1716 O O   . ASN   A 72  ? 0.1856 0.1533 0.2926 0.0121  0.0429  0.0082  72  ASN   A O   
1717 C CB  . ASN   A 72  ? 0.1769 0.1854 0.2643 0.0149  0.0369  0.0410  72  ASN   A CB  
1718 C CG  . ASN   A 72  ? 0.1988 0.2047 0.2771 0.0206  0.0303  0.0478  72  ASN   A CG  
1719 O OD1 . ASN   A 72  ? 0.2175 0.2357 0.3073 0.0237  0.0436  0.0497  72  ASN   A OD1 
1720 N ND2 . ASN   A 72  ? 0.2144 0.1957 0.2825 0.0565  0.0170  0.0406  72  ASN   A ND2 
1727 N N   . GLY   A 73  ? 0.1635 0.1657 0.2357 0.0059  0.0486  0.0175  73  GLY   A N   
1728 C CA  . GLY   A 73  ? 0.1643 0.1636 0.2223 -0.0019 0.0442  0.0256  73  GLY   A CA  
1729 C C   . GLY   A 73  ? 0.1690 0.1530 0.2060 0.0071  0.0506  0.0296  73  GLY   A C   
1730 O O   . GLY   A 73  ? 0.1666 0.1583 0.2077 0.0135  0.0322  0.0313  73  GLY   A O   
1734 N N   . PRO   A 74  ? 0.1844 0.1571 0.2060 -0.0057 0.0531  0.0097  74  PRO   A N   
1735 C CA  . PRO   A 74  ? 0.1802 0.1516 0.2327 -0.0028 0.0417  0.0071  74  PRO   A CA  
1736 C C   . PRO   A 74  ? 0.1704 0.1341 0.2295 -0.0029 0.0266  0.0049  74  PRO   A C   
1737 O O   . PRO   A 74  ? 0.1714 0.1380 0.2468 -0.0031 0.0331  -0.0027 74  PRO   A O   
1738 C CB  . PRO   A 74  ? 0.1987 0.1767 0.2378 -0.0060 0.0545  0.0043  74  PRO   A CB  
1739 C CG  . PRO   A 74  ? 0.2241 0.2169 0.2803 -0.0274 0.0369  -0.0032 74  PRO   A CG  
1740 C CD  . PRO   A 74  ? 0.2024 0.1890 0.2340 -0.0252 0.0269  -0.0068 74  PRO   A CD  
1748 N N   . LEU   A 75  ? 0.1664 0.1306 0.1918 -0.0008 0.0188  0.0057  75  LEU   A N   
1749 C CA  . LEU   A 75  ? 0.1594 0.1294 0.1952 0.0028  0.0137  0.0166  75  LEU   A CA  
1750 C C   . LEU   A 75  ? 0.1686 0.1454 0.1956 0.0117  0.0056  0.0112  75  LEU   A C   
1751 O O   . LEU   A 75  ? 0.2068 0.1625 0.1740 0.0182  0.0076  0.0095  75  LEU   A O   
1752 C CB  . LEU   A 75  ? 0.1642 0.1313 0.2056 -0.0038 0.0061  0.0183  75  LEU   A CB  
1753 C CG  . LEU   A 75  ? 0.1860 0.1628 0.2028 -0.0400 0.0064  0.0163  75  LEU   A CG  
1754 C CD1 . LEU   A 75  ? 0.2033 0.2156 0.2125 -0.0449 -0.0007 0.0035  75  LEU   A CD1 
1755 C CD2 . LEU   A 75  ? 0.2246 0.2069 0.2423 -0.0142 -0.0008 0.0276  75  LEU   A CD2 
1767 N N   . LYS   A 76  ? 0.1665 0.1438 0.2118 0.0001  0.0079  0.0015  76  LYS   A N   
1768 C CA  . LYS   A 76  ? 0.1657 0.1608 0.2164 -0.0043 0.0082  -0.0094 76  LYS   A CA  
1769 C C   . LYS   A 76  ? 0.1635 0.1437 0.1913 0.0026  0.0115  0.0091  76  LYS   A C   
1770 O O   . LYS   A 76  ? 0.1662 0.1347 0.1815 -0.0015 0.0175  0.0150  76  LYS   A O   
1771 C CB  . LYS   A 76  ? 0.1660 0.1810 0.2464 0.0022  0.0138  -0.0305 76  LYS   A CB  
1772 C CG  . LYS   A 76  ? 0.1782 0.1799 0.2880 0.0056  0.0034  -0.0309 76  LYS   A CG  
1773 C CD  . LYS   A 76  ? 0.1832 0.1752 0.3318 0.0099  -0.0182 -0.0274 76  LYS   A CD  
1774 C CE  . LYS   A 76  ? 0.2000 0.1977 0.3816 -0.0007 -0.0107 -0.0285 76  LYS   A CE  
1775 N NZ  . LYS   A 76  ? 0.2027 0.1857 0.4217 -0.0144 -0.0197 -0.0417 76  LYS   A NZ  
1789 N N   . VAL   A 77  ? 0.1727 0.1530 0.1856 -0.0010 0.0142  0.0124  77  VAL   A N   
1790 C CA  . VAL   A 77  ? 0.1716 0.1482 0.1743 0.0092  0.0076  0.0109  77  VAL   A CA  
1791 C C   . VAL   A 77  ? 0.1669 0.1469 0.1689 0.0065  0.0103  0.0055  77  VAL   A C   
1792 O O   . VAL   A 77  ? 0.1749 0.1565 0.1787 0.0130  0.0311  -0.0063 77  VAL   A O   
1793 C CB  . VAL   A 77  ? 0.1868 0.1685 0.1897 -0.0033 0.0137  0.0205  77  VAL   A CB  
1794 C CG1 . VAL   A 77  ? 0.1912 0.1828 0.2055 0.0011  0.0067  0.0058  77  VAL   A CG1 
1795 C CG2 . VAL   A 77  ? 0.2117 0.1810 0.2189 -0.0028 0.0017  0.0254  77  VAL   A CG2 
1805 N N   . GLY   A 78  ? 0.1603 0.1384 0.1645 0.0025  0.0185  0.0047  78  GLY   A N   
1806 C CA  . GLY   A 78  ? 0.1580 0.1373 0.1803 0.0027  0.0230  0.0052  78  GLY   A CA  
1807 C C   . GLY   A 78  ? 0.1465 0.1257 0.1840 0.0060  0.0166  0.0068  78  GLY   A C   
1808 O O   . GLY   A 78  ? 0.1460 0.1356 0.2116 -0.0024 0.0021  0.0257  78  GLY   A O   
1812 N N   . GLY   A 79  ? 0.1563 0.1294 0.1659 -0.0005 0.0098  0.0057  79  GLY   A N   
1813 C CA  . GLY   A 79  ? 0.1481 0.1361 0.1780 -0.0008 0.0124  0.0154  79  GLY   A CA  
1814 C C   . GLY   A 79  ? 0.1330 0.1354 0.1614 -0.0006 0.0035  0.0106  79  GLY   A C   
1815 O O   . GLY   A 79  ? 0.1398 0.1463 0.1838 0.0144  0.0105  0.0035  79  GLY   A O   
1819 N N   . SER   A 80  ? 0.1301 0.1414 0.1994 0.0048  0.0115  -0.0028 80  SER   A N   
1820 C CA  . SER   A 80  ? 0.1341 0.1359 0.1938 0.0038  0.0143  0.0053  80  SER   A CA  
1821 C C   . SER   A 80  ? 0.1305 0.1446 0.1812 -0.0034 0.0123  0.0085  80  SER   A C   
1822 O O   . SER   A 80  ? 0.1319 0.1638 0.2188 0.0064  0.0104  0.0016  80  SER   A O   
1823 C CB  . SER   A 80  ? 0.1556 0.1326 0.2158 -0.0025 0.0092  0.0099  80  SER   A CB  
1824 O OG  . SER   A 80  ? 0.1743 0.1377 0.2519 -0.0001 -0.0038 0.0262  80  SER   A OG  
1830 N N   . CYS   A 81  ? 0.1302 0.1364 0.1730 -0.0001 -0.0033 0.0165  81  CYS   A N   
1831 C CA  . CYS   A 81  ? 0.1269 0.1493 0.1914 -0.0046 0.0018  0.0169  81  CYS   A CA  
1832 C C   . CYS   A 81  ? 0.1283 0.1457 0.1943 -0.0096 0.0046  0.0296  81  CYS   A C   
1833 O O   . CYS   A 81  ? 0.1272 0.1751 0.1939 -0.0008 -0.0034 0.0392  81  CYS   A O   
1834 C CB  . CYS   A 81  ? 0.1366 0.1535 0.2049 -0.0112 -0.0060 0.0242  81  CYS   A CB  
1835 S SG  . CYS   A 81  ? 0.1491 0.1416 0.2042 -0.0140 0.0005  0.0175  81  CYS   A SG  
1841 N N   . VAL   A 82  ? 0.1346 0.1524 0.1899 -0.0015 -0.0106 0.0291  82  VAL   A N   
1842 C CA  . VAL   A 82  ? 0.1424 0.1626 0.1777 0.0010  -0.0113 0.0271  82  VAL   A CA  
1843 C C   . VAL   A 82  ? 0.1365 0.1674 0.1860 -0.0013 -0.0114 0.0306  82  VAL   A C   
1844 O O   . VAL   A 82  ? 0.1309 0.1683 0.2200 -0.0035 -0.0045 0.0133  82  VAL   A O   
1845 C CB  . VAL   A 82  ? 0.1739 0.1749 0.1941 -0.0033 -0.0073 0.0456  82  VAL   A CB  
1846 C CG1 . VAL   A 82  ? 0.1944 0.1855 0.2419 -0.0026 -0.0106 0.0418  82  VAL   A CG1 
1847 C CG2 . VAL   A 82  ? 0.1803 0.1760 0.2405 -0.0020 -0.0073 0.0482  82  VAL   A CG2 
1857 N N   . LEU   A 83  ? 0.1307 0.1630 0.1780 -0.0085 -0.0128 0.0129  83  LEU   A N   
1858 C CA  . LEU   A 83  ? 0.1351 0.1591 0.1670 -0.0149 -0.0062 0.0178  83  LEU   A CA  
1859 C C   . LEU   A 83  ? 0.1413 0.1647 0.1711 -0.0134 -0.0120 0.0292  83  LEU   A C   
1860 O O   . LEU   A 83  ? 0.1493 0.1688 0.1786 -0.0191 -0.0121 0.0335  83  LEU   A O   
1861 C CB  . LEU   A 83  ? 0.1471 0.1743 0.1818 -0.0135 -0.0141 0.0282  83  LEU   A CB  
1862 C CG  . LEU   A 83  ? 0.1548 0.1727 0.1963 -0.0118 0.0096  0.0133  83  LEU   A CG  
1863 C CD1 . LEU   A 83  ? 0.1660 0.1719 0.2232 -0.0202 0.0018  0.0238  83  LEU   A CD1 
1864 C CD2 . LEU   A 83  ? 0.1489 0.1887 0.2189 -0.0124 0.0221  0.0176  83  LEU   A CD2 
1876 N N   . SER   A 84  ? 0.1542 0.1638 0.1855 -0.0131 -0.0142 0.0244  84  SER   A N   
1877 C CA  . SER   A 84  ? 0.1695 0.1729 0.1740 -0.0128 -0.0166 0.0172  84  SER   A CA  
1878 C C   . SER   A 84  ? 0.1734 0.1715 0.1470 -0.0221 -0.0131 0.0184  84  SER   A C   
1879 O O   . SER   A 84  ? 0.1643 0.1868 0.1349 -0.0132 -0.0138 0.0159  84  SER   A O   
1880 C CB  . SER   A 84  ? 0.1751 0.1922 0.1875 -0.0044 -0.0131 0.0046  84  SER   A CB  
1881 O OG  . SER   A 84  ? 0.1784 0.2137 0.2046 -0.0142 -0.0282 -0.0157 84  SER   A OG  
1887 N N   . GLY   A 85  ? 0.1876 0.1840 0.1619 -0.0206 0.0052  0.0306  85  GLY   A N   
1888 C CA  . GLY   A 85  ? 0.1828 0.1937 0.1808 -0.0211 0.0081  0.0025  85  GLY   A CA  
1889 C C   . GLY   A 85  ? 0.1704 0.1983 0.1737 -0.0223 -0.0021 0.0073  85  GLY   A C   
1890 O O   . GLY   A 85  ? 0.1786 0.2123 0.2009 -0.0308 0.0038  -0.0078 85  GLY   A O   
1894 N N   . HIS   A 86  ? 0.1723 0.1918 0.1663 -0.0174 -0.0055 0.0167  86  HIS   A N   
1895 C CA  . HIS   A 86  ? 0.1884 0.1974 0.1623 -0.0189 -0.0097 0.0126  86  HIS   A CA  
1896 C C   . HIS   A 86  ? 0.2141 0.2134 0.1534 -0.0269 -0.0031 0.0122  86  HIS   A C   
1897 O O   . HIS   A 86  ? 0.2290 0.2385 0.1624 -0.0237 0.0081  0.0037  86  HIS   A O   
1898 C CB  . HIS   A 86  ? 0.1911 0.1938 0.1615 -0.0063 0.0076  0.0129  86  HIS   A CB  
1899 C CG  . HIS   A 86  ? 0.1844 0.1932 0.1670 -0.0030 -0.0010 0.0112  86  HIS   A CG  
1900 N ND1 . HIS   A 86  ? 0.1994 0.1910 0.2182 -0.0175 -0.0099 0.0120  86  HIS   A ND1 
1901 C CD2 . HIS   A 86  ? 0.1902 0.1859 0.1600 0.0085  0.0135  0.0102  86  HIS   A CD2 
1902 C CE1 . HIS   A 86  ? 0.1923 0.1854 0.2067 -0.0059 0.0112  0.0112  86  HIS   A CE1 
1903 N NE2 . HIS   A 86  ? 0.1885 0.1868 0.1791 0.0104  0.0138  0.0231  86  HIS   A NE2 
1911 N N   . ASN   A 87  ? 0.2289 0.2266 0.1685 -0.0179 0.0161  -0.0038 87  ASN   A N   
1912 C CA  . ASN   A 87  ? 0.2505 0.2381 0.1770 -0.0160 0.0361  -0.0106 87  ASN   A CA  
1913 C C   . ASN   A 87  ? 0.2469 0.2585 0.1946 -0.0285 0.0495  0.0049  87  ASN   A C   
1914 O O   . ASN   A 87  ? 0.2817 0.2855 0.2272 -0.0459 0.0925  -0.0106 87  ASN   A O   
1915 C CB  . ASN   A 87  ? 0.2706 0.2372 0.1894 -0.0032 0.0378  -0.0185 87  ASN   A CB  
1916 C CG  . ASN   A 87  ? 0.2852 0.2487 0.1943 0.0082  0.0485  -0.0065 87  ASN   A CG  
1917 O OD1 . ASN   A 87  ? 0.2989 0.2484 0.1938 0.0178  0.0495  0.0047  87  ASN   A OD1 
1918 N ND2 . ASN   A 87  ? 0.2911 0.2803 0.2208 0.0100  0.0409  0.0012  87  ASN   A ND2 
1925 N N   A LEU   A 88  ? 0.2170 0.2432 0.1796 -0.0359 0.0239  0.0096  88  LEU   A N   
1926 N N   B LEU   A 88  ? 0.2235 0.2482 0.1847 -0.0322 0.0388  0.0052  88  LEU   A N   
1927 C CA  A LEU   A 88  ? 0.1934 0.2350 0.1980 -0.0379 0.0231  0.0276  88  LEU   A CA  
1928 C CA  B LEU   A 88  ? 0.2048 0.2420 0.2013 -0.0313 0.0428  0.0167  88  LEU   A CA  
1929 C C   A LEU   A 88  ? 0.1873 0.2368 0.1981 -0.0318 0.0249  0.0358  88  LEU   A C   
1930 C C   B LEU   A 88  ? 0.1926 0.2397 0.1987 -0.0300 0.0353  0.0350  88  LEU   A C   
1931 O O   A LEU   A 88  ? 0.1966 0.2398 0.2267 -0.0232 0.0305  0.0446  88  LEU   A O   
1932 O O   B LEU   A 88  ? 0.1993 0.2418 0.2161 -0.0247 0.0428  0.0557  88  LEU   A O   
1933 C CB  A LEU   A 88  ? 0.1896 0.2396 0.2029 -0.0429 -0.0121 0.0399  88  LEU   A CB  
1934 C CB  B LEU   A 88  ? 0.2094 0.2484 0.2147 -0.0303 0.0323  0.0137  88  LEU   A CB  
1935 C CG  A LEU   A 88  ? 0.2088 0.2477 0.2125 -0.0435 -0.0173 0.0499  88  LEU   A CG  
1936 C CG  B LEU   A 88  ? 0.2222 0.2535 0.2246 -0.0275 0.0337  0.0090  88  LEU   A CG  
1937 C CD1 A LEU   A 88  ? 0.2256 0.2604 0.2280 -0.0395 -0.0209 0.0452  88  LEU   A CD1 
1938 C CD1 B LEU   A 88  ? 0.2325 0.2603 0.2352 -0.0241 0.0311  -0.0018 88  LEU   A CD1 
1939 C CD2 A LEU   A 88  ? 0.2211 0.2551 0.2460 -0.0400 -0.0064 0.0460  88  LEU   A CD2 
1940 C CD2 B LEU   A 88  ? 0.2289 0.2595 0.2344 -0.0236 0.0394  0.0023  88  LEU   A CD2 
1963 N N   . ALA   A 89  ? 0.1852 0.2357 0.1817 -0.0289 0.0184  0.0254  89  ALA   A N   
1964 C CA  . ALA   A 89  ? 0.1920 0.2348 0.1581 -0.0169 -0.0009 0.0206  89  ALA   A CA  
1965 C C   . ALA   A 89  ? 0.2066 0.2361 0.1654 -0.0144 -0.0140 0.0238  89  ALA   A C   
1966 O O   . ALA   A 89  ? 0.1995 0.2302 0.2009 -0.0244 -0.0078 -0.0022 89  ALA   A O   
1967 C CB  . ALA   A 89  ? 0.1889 0.2302 0.1453 -0.0190 -0.0018 0.0185  89  ALA   A CB  
1974 N N   . LYS   A 90  ? 0.2166 0.2517 0.1729 -0.0286 -0.0183 0.0287  90  LYS   A N   
1975 C CA  . LYS   A 90  ? 0.2180 0.2649 0.1885 -0.0187 -0.0386 0.0430  90  LYS   A CA  
1976 C C   . LYS   A 90  ? 0.1943 0.2482 0.1808 -0.0290 -0.0271 0.0229  90  LYS   A C   
1977 O O   . LYS   A 90  ? 0.1998 0.2652 0.2012 -0.0302 -0.0377 0.0013  90  LYS   A O   
1978 C CB  . LYS   A 90  ? 0.2428 0.3031 0.2093 -0.0125 -0.0487 0.0707  90  LYS   A CB  
1979 C CG  . LYS   A 90  ? 0.2928 0.3449 0.3097 -0.0112 -0.0416 0.0613  90  LYS   A CG  
1980 C CD  . LYS   A 90  ? 0.3352 0.3782 0.4050 -0.0150 -0.0290 0.0688  90  LYS   A CD  
1981 C CE  . LYS   A 90  ? 0.3646 0.3949 0.4840 -0.0189 -0.0181 0.0665  90  LYS   A CE  
1982 N NZ  . LYS   A 90  ? 0.4258 0.4258 0.5310 -0.0244 -0.0054 0.0565  90  LYS   A NZ  
1996 N N   . HIS   A 91  ? 0.1776 0.2155 0.1653 -0.0315 -0.0198 0.0360  91  HIS   A N   
1997 C CA  . HIS   A 91  ? 0.1690 0.1946 0.1593 -0.0202 -0.0149 0.0348  91  HIS   A CA  
1998 C C   . HIS   A 91  ? 0.1505 0.1819 0.1461 -0.0168 -0.0200 0.0335  91  HIS   A C   
1999 O O   . HIS   A 91  ? 0.1545 0.1941 0.1740 -0.0235 0.0030  0.0230  91  HIS   A O   
2000 C CB  . HIS   A 91  ? 0.1868 0.2169 0.2073 0.0032  -0.0377 0.0443  91  HIS   A CB  
2001 C CG  . HIS   A 91  ? 0.2406 0.2688 0.2741 0.0125  -0.0651 0.0236  91  HIS   A CG  
2002 N ND1 . HIS   A 91  ? 0.2535 0.2969 0.3071 0.0197  -0.0864 -0.0126 91  HIS   A ND1 
2003 C CD2 . HIS   A 91  ? 0.2688 0.2903 0.2955 0.0238  -0.0798 0.0301  91  HIS   A CD2 
2004 C CE1 . HIS   A 91  ? 0.2674 0.3091 0.3274 0.0263  -0.0864 -0.0044 91  HIS   A CE1 
2005 N NE2 . HIS   A 91  ? 0.2807 0.3087 0.3158 0.0307  -0.0909 0.0124  91  HIS   A NE2 
2013 N N   . CYS   A 92  ? 0.1447 0.1683 0.1607 -0.0185 -0.0169 0.0341  92  CYS   A N   
2014 C CA  . CYS   A 92  ? 0.1420 0.1607 0.1625 -0.0094 -0.0026 0.0284  92  CYS   A CA  
2015 C C   . CYS   A 92  ? 0.1396 0.1564 0.1679 -0.0134 -0.0025 0.0220  92  CYS   A C   
2016 O O   . CYS   A 92  ? 0.1411 0.1597 0.1751 -0.0159 0.0020  0.0163  92  CYS   A O   
2017 C CB  . CYS   A 92  ? 0.1397 0.1580 0.1723 -0.0066 -0.0104 0.0229  92  CYS   A CB  
2018 S SG  . CYS   A 92  ? 0.1480 0.1531 0.1548 -0.0138 -0.0050 0.0179  92  CYS   A SG  
2024 N N   . LEU   A 93  ? 0.1392 0.1427 0.1714 -0.0186 0.0093  0.0143  93  LEU   A N   
2025 C CA  . LEU   A 93  ? 0.1281 0.1420 0.1739 -0.0042 0.0013  0.0244  93  LEU   A CA  
2026 C C   . LEU   A 93  ? 0.1321 0.1297 0.1556 0.0011  0.0093  0.0107  93  LEU   A C   
2027 O O   . LEU   A 93  ? 0.1211 0.1384 0.1590 -0.0033 0.0004  0.0126  93  LEU   A O   
2028 C CB  . LEU   A 93  ? 0.1357 0.1386 0.1892 -0.0063 -0.0091 0.0290  93  LEU   A CB  
2029 C CG  . LEU   A 93  ? 0.1453 0.1434 0.2095 -0.0078 0.0040  0.0260  93  LEU   A CG  
2030 C CD1 . LEU   A 93  ? 0.1506 0.1498 0.2253 -0.0009 0.0130  0.0249  93  LEU   A CD1 
2031 C CD2 . LEU   A 93  ? 0.1575 0.1377 0.2272 -0.0135 -0.0117 0.0239  93  LEU   A CD2 
2043 N N   . HIS   A 94  ? 0.1266 0.1199 0.1567 -0.0056 0.0057  0.0190  94  HIS   A N   
2044 C CA  . HIS   A 94  ? 0.1158 0.1278 0.1675 -0.0013 0.0017  0.0192  94  HIS   A CA  
2045 C C   . HIS   A 94  ? 0.1207 0.1227 0.1674 -0.0057 -0.0012 0.0073  94  HIS   A C   
2046 O O   . HIS   A 94  ? 0.1271 0.1444 0.1958 0.0013  -0.0010 -0.0090 94  HIS   A O   
2047 C CB  . HIS   A 94  ? 0.1227 0.1244 0.1651 -0.0058 -0.0029 0.0238  94  HIS   A CB  
2048 C CG  . HIS   A 94  ? 0.1323 0.1232 0.1497 -0.0062 -0.0106 0.0224  94  HIS   A CG  
2049 N ND1 . HIS   A 94  ? 0.1276 0.1275 0.1665 -0.0036 -0.0053 0.0242  94  HIS   A ND1 
2050 C CD2 . HIS   A 94  ? 0.1373 0.1366 0.1726 -0.0163 -0.0127 0.0232  94  HIS   A CD2 
2051 C CE1 . HIS   A 94  ? 0.1314 0.1339 0.1705 -0.0080 -0.0199 0.0177  94  HIS   A CE1 
2052 N NE2 . HIS   A 94  ? 0.1412 0.1374 0.1709 -0.0162 -0.0086 0.0088  94  HIS   A NE2 
2060 N N   . VAL   A 95  ? 0.1189 0.1218 0.1553 -0.0039 0.0026  0.0054  95  VAL   A N   
2061 C CA  . VAL   A 95  ? 0.1253 0.1268 0.1671 -0.0064 0.0117  0.0125  95  VAL   A CA  
2062 C C   . VAL   A 95  ? 0.1311 0.1258 0.1511 -0.0119 0.0043  0.0184  95  VAL   A C   
2063 O O   . VAL   A 95  ? 0.1357 0.1351 0.1504 0.0086  0.0029  0.0138  95  VAL   A O   
2064 C CB  . VAL   A 95  ? 0.1214 0.1280 0.1796 -0.0123 0.0115  0.0127  95  VAL   A CB  
2065 C CG1 . VAL   A 95  ? 0.1404 0.1223 0.2058 -0.0147 -0.0004 0.0042  95  VAL   A CG1 
2066 C CG2 . VAL   A 95  ? 0.1351 0.1349 0.1775 -0.0167 0.0099  0.0315  95  VAL   A CG2 
2076 N N   . VAL   A 96  ? 0.1336 0.1266 0.1432 -0.0040 0.0028  0.0212  96  VAL   A N   
2077 C CA  . VAL   A 96  ? 0.1415 0.1280 0.1443 -0.0022 0.0043  0.0143  96  VAL   A CA  
2078 C C   . VAL   A 96  ? 0.1417 0.1366 0.1592 -0.0078 0.0019  0.0156  96  VAL   A C   
2079 O O   . VAL   A 96  ? 0.1476 0.1437 0.1719 -0.0045 0.0122  -0.0055 96  VAL   A O   
2080 C CB  . VAL   A 96  ? 0.1401 0.1352 0.1682 -0.0078 0.0104  0.0096  96  VAL   A CB  
2081 C CG1 . VAL   A 96  ? 0.1539 0.1461 0.1677 -0.0023 0.0215  0.0045  96  VAL   A CG1 
2082 C CG2 . VAL   A 96  ? 0.1376 0.1345 0.1873 -0.0115 0.0121  0.0118  96  VAL   A CG2 
2092 N N   A GLY   A 97  ? 0.1373 0.1320 0.1634 -0.0093 0.0110  0.0157  97  GLY   A N   
2093 N N   B GLY   A 97  ? 0.1408 0.1363 0.1589 -0.0040 -0.0002 0.0136  97  GLY   A N   
2094 C CA  A GLY   A 97  ? 0.1509 0.1421 0.1708 -0.0119 0.0050  0.0176  97  GLY   A CA  
2095 C CA  B GLY   A 97  ? 0.1506 0.1455 0.1659 -0.0053 -0.0081 0.0221  97  GLY   A CA  
2096 C C   A GLY   A 97  ? 0.1479 0.1537 0.1508 -0.0129 0.0149  0.0033  97  GLY   A C   
2097 C C   B GLY   A 97  ? 0.1491 0.1544 0.1605 -0.0037 -0.0053 0.0270  97  GLY   A C   
2098 O O   A GLY   A 97  ? 0.1556 0.1484 0.1581 -0.0096 0.0034  -0.0042 97  GLY   A O   
2099 O O   B GLY   A 97  ? 0.1528 0.1578 0.1886 -0.0012 -0.0103 0.0292  97  GLY   A O   
2106 N N   A PRO   A 98  ? 0.1492 0.1548 0.1552 -0.0030 0.0018  0.0029  98  PRO   A N   
2107 N N   B PRO   A 98  ? 0.1612 0.1546 0.1642 -0.0008 -0.0030 0.0387  98  PRO   A N   
2108 C CA  A PRO   A 98  ? 0.1543 0.1650 0.1667 0.0020  0.0021  -0.0057 98  PRO   A CA  
2109 C CA  B PRO   A 98  ? 0.1724 0.1655 0.1724 -0.0015 -0.0002 0.0140  98  PRO   A CA  
2110 C C   A PRO   A 98  ? 0.1502 0.1748 0.1487 0.0002  -0.0024 -0.0049 98  PRO   A C   
2111 C C   B PRO   A 98  ? 0.1885 0.1678 0.1508 0.0037  -0.0018 0.0188  98  PRO   A C   
2112 O O   A PRO   A 98  ? 0.1426 0.1668 0.1490 0.0010  0.0033  -0.0161 98  PRO   A O   
2113 O O   B PRO   A 98  ? 0.1880 0.1631 0.1533 0.0080  0.0082  0.0128  98  PRO   A O   
2114 C CB  A PRO   A 98  ? 0.1656 0.1676 0.1613 0.0091  0.0059  -0.0148 98  PRO   A CB  
2115 C CB  B PRO   A 98  ? 0.1774 0.1664 0.1808 0.0019  -0.0094 0.0084  98  PRO   A CB  
2116 C CG  A PRO   A 98  ? 0.1577 0.1630 0.1649 0.0137  0.0000  -0.0186 98  PRO   A CG  
2117 C CG  B PRO   A 98  ? 0.1792 0.1664 0.1913 -0.0002 -0.0093 0.0181  98  PRO   A CG  
2118 C CD  A PRO   A 98  ? 0.1488 0.1526 0.1691 0.0046  -0.0061 -0.0120 98  PRO   A CD  
2119 C CD  B PRO   A 98  ? 0.1667 0.1535 0.1777 -0.0004 -0.0132 0.0424  98  PRO   A CD  
2134 N N   A ASN   A 99  ? 0.1537 0.1901 0.1245 -0.0037 0.0001  0.0145  99  ASN   A N   
2135 N N   B ASN   A 99  ? 0.2099 0.1763 0.1360 0.0084  -0.0163 0.0344  99  ASN   A N   
2136 C CA  A ASN   A 99  ? 0.1671 0.2034 0.1266 -0.0109 0.0069  0.0188  99  ASN   A CA  
2137 C CA  B ASN   A 99  ? 0.2365 0.1844 0.1454 0.0044  -0.0169 0.0442  99  ASN   A CA  
2138 C C   A ASN   A 99  ? 0.1845 0.2201 0.1267 -0.0166 0.0073  0.0142  99  ASN   A C   
2139 C C   B ASN   A 99  ? 0.2545 0.1947 0.1483 0.0038  -0.0206 0.0490  99  ASN   A C   
2140 O O   A ASN   A 99  ? 0.1959 0.2343 0.1509 -0.0088 0.0002  0.0047  99  ASN   A O   
2141 O O   B ASN   A 99  ? 0.2506 0.1798 0.1547 0.0101  -0.0270 0.0472  99  ASN   A O   
2142 C CB  A ASN   A 99  ? 0.1553 0.2013 0.1272 -0.0130 0.0007  0.0243  99  ASN   A CB  
2143 C CB  B ASN   A 99  ? 0.2521 0.1888 0.1896 0.0003  -0.0162 0.0425  99  ASN   A CB  
2144 C CG  A ASN   A 99  ? 0.1593 0.2034 0.1363 -0.0070 -0.0237 0.0169  99  ASN   A CG  
2145 C CG  B ASN   A 99  ? 0.2664 0.1990 0.2258 -0.0073 -0.0168 0.0521  99  ASN   A CG  
2146 O OD1 A ASN   A 99  ? 0.1723 0.2093 0.1684 0.0075  -0.0197 -0.0057 99  ASN   A OD1 
2147 O OD1 B ASN   A 99  ? 0.2660 0.2033 0.2287 0.0013  -0.0134 0.0566  99  ASN   A OD1 
2148 N ND2 A ASN   A 99  ? 0.1648 0.1909 0.1518 -0.0069 -0.0348 0.0366  99  ASN   A ND2 
2149 N ND2 B ASN   A 99  ? 0.2774 0.2023 0.2678 -0.0107 -0.0325 0.0521  99  ASN   A ND2 
2162 N N   A VAL   A 100 ? 0.2054 0.2274 0.1512 -0.0286 -0.0184 0.0166  100 VAL   A N   
2163 N N   B VAL   A 100 ? 0.2745 0.2226 0.1719 0.0049  -0.0221 0.0509  100 VAL   A N   
2164 C CA  A VAL   A 100 ? 0.2290 0.2402 0.1734 -0.0299 -0.0259 0.0132  100 VAL   A CA  
2165 C CA  B VAL   A 100 ? 0.3001 0.2442 0.2069 0.0030  -0.0253 0.0410  100 VAL   A CA  
2166 C C   A VAL   A 100 ? 0.2346 0.2553 0.1533 -0.0399 -0.0153 0.0285  100 VAL   A C   
2167 C C   B VAL   A 100 ? 0.3112 0.2504 0.1988 0.0143  -0.0367 0.0396  100 VAL   A C   
2168 O O   A VAL   A 100 ? 0.2474 0.2588 0.1732 -0.0404 0.0085  0.0279  100 VAL   A O   
2169 O O   B VAL   A 100 ? 0.3145 0.2449 0.1992 0.0120  -0.0428 0.0320  100 VAL   A O   
2170 C CB  A VAL   A 100 ? 0.2509 0.2397 0.2204 -0.0312 -0.0300 -0.0006 100 VAL   A CB  
2171 C CB  B VAL   A 100 ? 0.3122 0.2595 0.2325 -0.0040 -0.0256 0.0274  100 VAL   A CB  
2172 C CG1 A VAL   A 100 ? 0.2522 0.2473 0.2373 -0.0332 -0.0156 -0.0042 100 VAL   A CG1 
2173 C CG1 B VAL   A 100 ? 0.3128 0.2618 0.2463 -0.0059 -0.0266 0.0185  100 VAL   A CG1 
2174 C CG2 A VAL   A 100 ? 0.2668 0.2387 0.2109 -0.0304 -0.0427 0.0041  100 VAL   A CG2 
2175 C CG2 B VAL   A 100 ? 0.3157 0.2668 0.2324 -0.0017 -0.0292 0.0194  100 VAL   A CG2 
2194 N N   A ASN   A 101 ? 0.2256 0.2656 0.1594 -0.0431 -0.0253 0.0514  101 ASN   A N   
2195 N N   B ASN   A 101 ? 0.3241 0.2649 0.2125 0.0202  -0.0376 0.0428  101 ASN   A N   
2196 C CA  A ASN   A 101 ? 0.2338 0.2818 0.1703 -0.0444 -0.0161 0.0759  101 ASN   A CA  
2197 C CA  B ASN   A 101 ? 0.3397 0.2822 0.2397 0.0319  -0.0312 0.0473  101 ASN   A CA  
2198 C C   A ASN   A 101 ? 0.2516 0.3103 0.1880 -0.0485 0.0001  0.1051  101 ASN   A C   
2199 C C   B ASN   A 101 ? 0.3600 0.3073 0.2583 0.0296  -0.0151 0.0561  101 ASN   A C   
2200 O O   A ASN   A 101 ? 0.2703 0.3138 0.2371 -0.0428 -0.0076 0.1021  101 ASN   A O   
2201 O O   B ASN   A 101 ? 0.3672 0.3087 0.2644 0.0292  -0.0233 0.0673  101 ASN   A O   
2202 C CB  A ASN   A 101 ? 0.2287 0.2726 0.1478 -0.0399 -0.0293 0.0631  101 ASN   A CB  
2203 C CB  B ASN   A 101 ? 0.3378 0.2772 0.2568 0.0362  -0.0293 0.0358  101 ASN   A CB  
2204 C CG  A ASN   A 101 ? 0.2201 0.2583 0.1522 -0.0320 -0.0342 0.0460  101 ASN   A CG  
2205 C CG  B ASN   A 101 ? 0.3400 0.2769 0.2749 0.0339  -0.0327 0.0301  101 ASN   A CG  
2206 O OD1 A ASN   A 101 ? 0.2027 0.2583 0.1771 -0.0157 -0.0286 0.0231  101 ASN   A OD1 
2207 O OD1 B ASN   A 101 ? 0.3456 0.2811 0.2971 0.0312  -0.0340 0.0382  101 ASN   A OD1 
2208 N ND2 A ASN   A 101 ? 0.2252 0.2540 0.1823 -0.0370 -0.0209 0.0371  101 ASN   A ND2 
2209 N ND2 B ASN   A 101 ? 0.3395 0.2732 0.2838 0.0340  -0.0231 0.0167  101 ASN   A ND2 
2222 N N   A LYS   A 102 ? 0.2485 0.3402 0.2127 -0.0584 0.0189  0.1174  102 LYS   A N   
2223 N N   B LYS   A 102 ? 0.3712 0.3313 0.2932 0.0299  0.0063  0.0506  102 LYS   A N   
2224 C CA  A LYS   A 102 ? 0.2568 0.3749 0.2166 -0.0552 0.0128  0.1075  102 LYS   A CA  
2225 C CA  B LYS   A 102 ? 0.3824 0.3553 0.3079 0.0261  0.0148  0.0507  102 LYS   A CA  
2226 C C   A LYS   A 102 ? 0.2675 0.4014 0.2178 -0.0413 0.0176  0.0888  102 LYS   A C   
2227 C C   B LYS   A 102 ? 0.3716 0.3581 0.2842 0.0308  0.0126  0.0707  102 LYS   A C   
2228 O O   A LYS   A 102 ? 0.2721 0.4117 0.2334 -0.0380 0.0177  0.0861  102 LYS   A O   
2229 O O   B LYS   A 102 ? 0.3751 0.3563 0.2918 0.0332  0.0180  0.0826  102 LYS   A O   
2230 C CB  A LYS   A 102 ? 0.2598 0.3795 0.2457 -0.0607 -0.0006 0.1046  102 LYS   A CB  
2231 C CB  B LYS   A 102 ? 0.4005 0.3749 0.3394 0.0207  0.0158  0.0315  102 LYS   A CB  
2232 C CG  A LYS   A 102 ? 0.2630 0.3807 0.2454 -0.0655 -0.0054 0.1080  102 LYS   A CG  
2233 C CG  B LYS   A 102 ? 0.4119 0.3893 0.3750 0.0165  0.0178  0.0139  102 LYS   A CG  
2234 C CD  A LYS   A 102 ? 0.2716 0.3793 0.2684 -0.0758 -0.0105 0.1064  102 LYS   A CD  
2235 C CD  B LYS   A 102 ? 0.4203 0.4004 0.4047 0.0126  0.0216  0.0049  102 LYS   A CD  
2236 C CE  A LYS   A 102 ? 0.2805 0.3776 0.2795 -0.0848 -0.0221 0.1069  102 LYS   A CE  
2237 C CE  B LYS   A 102 ? 0.4275 0.4081 0.4354 0.0074  0.0225  -0.0055 102 LYS   A CE  
2238 N NZ  A LYS   A 102 ? 0.2851 0.3724 0.2881 -0.0984 -0.0236 0.1038  102 LYS   A NZ  
2239 N NZ  B LYS   A 102 ? 0.4353 0.4128 0.4482 0.0041  0.0186  -0.0107 102 LYS   A NZ  
2266 N N   A GLY   A 103 ? 0.2732 0.4196 0.2365 -0.0271 0.0068  0.0609  103 GLY   A N   
2267 N N   B GLY   A 103 ? 0.3562 0.3643 0.2654 0.0367  0.0039  0.0623  103 GLY   A N   
2268 C CA  A GLY   A 103 ? 0.2838 0.4325 0.2520 -0.0158 0.0116  0.0405  103 GLY   A CA  
2269 C CA  B GLY   A 103 ? 0.3402 0.3663 0.2600 0.0448  -0.0075 0.0610  103 GLY   A CA  
2270 C C   A GLY   A 103 ? 0.2917 0.4452 0.2725 -0.0111 0.0231  0.0267  103 GLY   A C   
2271 C C   B GLY   A 103 ? 0.3268 0.3671 0.2453 0.0507  -0.0204 0.0558  103 GLY   A C   
2272 O O   A GLY   A 103 ? 0.3007 0.4530 0.3023 -0.0021 0.0293  0.0107  103 GLY   A O   
2273 O O   B GLY   A 103 ? 0.3320 0.3696 0.2468 0.0564  -0.0229 0.0553  103 GLY   A O   
2280 N N   A GLU   A 104 ? 0.2841 0.4456 0.2520 -0.0247 0.0300  0.0250  104 GLU   A N   
2281 N N   B GLU   A 104 ? 0.3042 0.3595 0.2213 0.0466  -0.0303 0.0677  104 GLU   A N   
2282 C CA  A GLU   A 104 ? 0.2750 0.4402 0.2496 -0.0422 0.0341  0.0239  104 GLU   A CA  
2283 C CA  B GLU   A 104 ? 0.2838 0.3535 0.2048 0.0364  -0.0333 0.0596  104 GLU   A CA  
2284 C C   A GLU   A 104 ? 0.2856 0.4468 0.2571 -0.0412 0.0305  0.0008  104 GLU   A C   
2285 C C   B GLU   A 104 ? 0.2707 0.3446 0.2091 0.0457  -0.0286 0.0385  104 GLU   A C   
2286 O O   A GLU   A 104 ? 0.2829 0.4473 0.2621 -0.0437 0.0206  -0.0039 104 GLU   A O   
2287 O O   B GLU   A 104 ? 0.2617 0.3357 0.2294 0.0489  -0.0282 0.0381  104 GLU   A O   
2288 C CB  A GLU   A 104 ? 0.2484 0.4259 0.2296 -0.0577 0.0333  0.0484  104 GLU   A CB  
2289 C CB  B GLU   A 104 ? 0.2810 0.3591 0.1991 0.0191  -0.0304 0.0687  104 GLU   A CB  
2290 C CG  A GLU   A 104 ? 0.2259 0.4097 0.2223 -0.0678 0.0214  0.0745  104 GLU   A CG  
2291 C CG  B GLU   A 104 ? 0.2807 0.3650 0.2069 0.0055  -0.0357 0.0781  104 GLU   A CG  
2292 C CD  A GLU   A 104 ? 0.1965 0.3914 0.2134 -0.0816 0.0159  0.0969  104 GLU   A CD  
2293 C CD  B GLU   A 104 ? 0.2794 0.3681 0.2255 -0.0026 -0.0410 0.0762  104 GLU   A CD  
2294 O OE1 A GLU   A 104 ? 0.1796 0.3707 0.1733 -0.0816 0.0021  0.1014  104 GLU   A OE1 
2295 O OE1 B GLU   A 104 ? 0.2783 0.3671 0.2290 -0.0031 -0.0508 0.0735  104 GLU   A OE1 
2296 O OE2 A GLU   A 104 ? 0.1980 0.3948 0.2496 -0.0820 0.0017  0.1072  104 GLU   A OE2 
2297 O OE2 B GLU   A 104 ? 0.2806 0.3721 0.2373 -0.0080 -0.0405 0.0781  104 GLU   A OE2 
2310 N N   A ASP   A 105 ? 0.2943 0.4495 0.2657 -0.0350 0.0374  -0.0254 105 ASP   A N   
2311 N N   B ASP   A 105 ? 0.2716 0.3475 0.2176 0.0455  -0.0218 0.0138  105 ASP   A N   
2312 C CA  A ASP   A 105 ? 0.3005 0.4519 0.2852 -0.0308 0.0387  -0.0502 105 ASP   A CA  
2313 C CA  B ASP   A 105 ? 0.2741 0.3499 0.2423 0.0458  -0.0039 -0.0208 105 ASP   A CA  
2314 C C   A ASP   A 105 ? 0.2763 0.4375 0.2501 -0.0458 0.0326  -0.0662 105 ASP   A C   
2315 C C   B ASP   A 105 ? 0.2778 0.3432 0.2208 0.0269  -0.0002 -0.0331 105 ASP   A C   
2316 O O   A ASP   A 105 ? 0.2655 0.4360 0.2201 -0.0473 0.0272  -0.0821 105 ASP   A O   
2317 O O   B ASP   A 105 ? 0.2704 0.3347 0.1692 0.0287  0.0041  -0.0445 105 ASP   A O   
2318 C CB  A ASP   A 105 ? 0.3263 0.4645 0.3414 -0.0140 0.0387  -0.0599 105 ASP   A CB  
2319 C CB  B ASP   A 105 ? 0.2762 0.3559 0.2933 0.0617  0.0102  -0.0412 105 ASP   A CB  
2320 C CG  A ASP   A 105 ? 0.3496 0.4739 0.3982 0.0001  0.0402  -0.0654 105 ASP   A CG  
2321 C CG  B ASP   A 105 ? 0.2811 0.3588 0.3341 0.0731  0.0191  -0.0572 105 ASP   A CG  
2322 O OD1 A ASP   A 105 ? 0.3580 0.4777 0.4062 -0.0011 0.0410  -0.0733 105 ASP   A OD1 
2323 O OD1 B ASP   A 105 ? 0.2859 0.3570 0.3347 0.0687  0.0218  -0.0688 105 ASP   A OD1 
2324 O OD2 A ASP   A 105 ? 0.3625 0.4779 0.4302 0.0106  0.0415  -0.0600 105 ASP   A OD2 
2325 O OD2 B ASP   A 105 ? 0.2764 0.3602 0.3605 0.0852  0.0266  -0.0591 105 ASP   A OD2 
2334 N N   A ILE   A 106 ? 0.2598 0.4217 0.2485 -0.0598 0.0162  -0.0692 106 ILE   A N   
2335 N N   B ILE   A 106 ? 0.2878 0.3448 0.2526 0.0080  -0.0102 -0.0379 106 ILE   A N   
2336 C CA  A ILE   A 106 ? 0.2376 0.3991 0.2520 -0.0774 -0.0053 -0.0802 106 ILE   A CA  
2337 C CA  B ILE   A 106 ? 0.2969 0.3470 0.2818 -0.0167 -0.0127 -0.0459 106 ILE   A CA  
2338 C C   A ILE   A 106 ? 0.2247 0.3698 0.2561 -0.0956 0.0088  -0.1053 106 ILE   A C   
2339 C C   B ILE   A 106 ? 0.2986 0.3422 0.2868 -0.0329 -0.0048 -0.0511 106 ILE   A C   
2340 O O   A ILE   A 106 ? 0.2041 0.3584 0.2592 -0.1030 0.0350  -0.1080 106 ILE   A O   
2341 O O   B ILE   A 106 ? 0.2951 0.3418 0.2847 -0.0343 -0.0015 -0.0494 106 ILE   A O   
2342 C CB  A ILE   A 106 ? 0.2391 0.4062 0.2864 -0.0672 -0.0288 -0.0510 106 ILE   A CB  
2343 C CB  B ILE   A 106 ? 0.3097 0.3583 0.3118 -0.0229 -0.0154 -0.0336 106 ILE   A CB  
2344 C CG1 A ILE   A 106 ? 0.2185 0.4102 0.3071 -0.0570 -0.0324 -0.0247 106 ILE   A CG1 
2345 C CG1 B ILE   A 106 ? 0.3159 0.3693 0.3331 -0.0253 -0.0106 -0.0201 106 ILE   A CG1 
2346 C CG2 A ILE   A 106 ? 0.2562 0.4066 0.3004 -0.0657 -0.0307 -0.0496 106 ILE   A CG2 
2347 C CG2 B ILE   A 106 ? 0.3150 0.3581 0.3215 -0.0245 -0.0187 -0.0348 106 ILE   A CG2 
2348 C CD1 A ILE   A 106 ? 0.2123 0.4090 0.3181 -0.0464 -0.0276 -0.0176 106 ILE   A CD1 
2349 C CD1 B ILE   A 106 ? 0.3229 0.3734 0.3460 -0.0248 -0.0037 -0.0213 106 ILE   A CD1 
2372 N N   A GLN   A 107 ? 0.2484 0.3568 0.2847 -0.0867 0.0197  -0.1138 107 GLN   A N   
2373 N N   B GLN   A 107 ? 0.3047 0.3346 0.3029 -0.0413 0.0083  -0.0590 107 GLN   A N   
2374 C CA  A GLN   A 107 ? 0.2751 0.3367 0.3487 -0.0692 0.0389  -0.1173 107 GLN   A CA  
2375 C CA  B GLN   A 107 ? 0.3102 0.3268 0.3555 -0.0478 0.0206  -0.0612 107 GLN   A CA  
2376 C C   A GLN   A 107 ? 0.2532 0.2940 0.3469 -0.0583 0.0614  -0.0894 107 GLN   A C   
2377 C C   B GLN   A 107 ? 0.2747 0.2906 0.3403 -0.0502 0.0487  -0.0650 107 GLN   A C   
2378 O O   A GLN   A 107 ? 0.2527 0.2886 0.3904 -0.0539 0.0710  -0.0912 107 GLN   A O   
2379 O O   B GLN   A 107 ? 0.2781 0.2895 0.3691 -0.0525 0.0502  -0.0665 107 GLN   A O   
2380 C CB  A GLN   A 107 ? 0.3141 0.3605 0.4263 -0.0675 0.0271  -0.1172 107 GLN   A CB  
2381 C CB  B GLN   A 107 ? 0.3432 0.3533 0.4206 -0.0539 0.0012  -0.0534 107 GLN   A CB  
2382 C CG  A GLN   A 107 ? 0.3497 0.3854 0.5164 -0.0633 0.0128  -0.1026 107 GLN   A CG  
2383 C CG  B GLN   A 107 ? 0.3740 0.3805 0.4901 -0.0550 -0.0172 -0.0393 107 GLN   A CG  
2384 C CD  A GLN   A 107 ? 0.3779 0.4044 0.5867 -0.0603 0.0068  -0.0868 107 GLN   A CD  
2385 C CD  B GLN   A 107 ? 0.3987 0.4050 0.5459 -0.0539 -0.0273 -0.0242 107 GLN   A CD  
2386 O OE1 A GLN   A 107 ? 0.3886 0.4143 0.6192 -0.0543 0.0074  -0.0775 107 GLN   A OE1 
2387 O OE1 B GLN   A 107 ? 0.4059 0.4142 0.5714 -0.0533 -0.0306 -0.0192 107 GLN   A OE1 
2388 N NE2 A GLN   A 107 ? 0.3870 0.4089 0.6128 -0.0647 0.0033  -0.0868 107 GLN   A NE2 
2389 N NE2 B GLN   A 107 ? 0.4102 0.4152 0.5671 -0.0540 -0.0329 -0.0214 107 GLN   A NE2 
2406 N N   . LEU   A 108 ? 0.2357 0.2555 0.2984 -0.0503 0.0620  -0.0748 108 LEU   A N   
2407 C CA  . LEU   A 108 ? 0.2059 0.2076 0.2457 -0.0213 0.0545  -0.0358 108 LEU   A CA  
2408 C C   . LEU   A 108 ? 0.1787 0.1620 0.2289 -0.0069 0.0393  0.0003  108 LEU   A C   
2409 O O   . LEU   A 108 ? 0.1739 0.1577 0.2579 0.0029  0.0401  0.0073  108 LEU   A O   
2410 C CB  . LEU   A 108 ? 0.2077 0.2167 0.2504 -0.0279 0.0571  -0.0328 108 LEU   A CB  
2411 C CG  . LEU   A 108 ? 0.2216 0.2388 0.2825 -0.0193 0.0629  -0.0388 108 LEU   A CG  
2412 C CD1 . LEU   A 108 ? 0.2414 0.2476 0.2865 -0.0270 0.0569  -0.0233 108 LEU   A CD1 
2413 C CD2 . LEU   A 108 ? 0.2272 0.2673 0.3237 -0.0115 0.0724  -0.0255 108 LEU   A CD2 
2426 N N   . LEU   A 109 ? 0.1706 0.1556 0.2166 0.0020  0.0239  0.0140  109 LEU   A N   
2427 C CA  . LEU   A 109 ? 0.1611 0.1450 0.2044 -0.0015 0.0149  0.0166  109 LEU   A CA  
2428 C C   . LEU   A 109 ? 0.1412 0.1400 0.2207 -0.0056 0.0115  0.0133  109 LEU   A C   
2429 O O   . LEU   A 109 ? 0.1491 0.1297 0.2489 -0.0029 -0.0011 0.0121  109 LEU   A O   
2430 C CB  . LEU   A 109 ? 0.1641 0.1595 0.2327 0.0061  0.0006  0.0265  109 LEU   A CB  
2431 C CG  . LEU   A 109 ? 0.1545 0.1661 0.2361 0.0032  0.0106  0.0328  109 LEU   A CG  
2432 C CD1 . LEU   A 109 ? 0.1613 0.1586 0.2527 0.0022  0.0113  0.0097  109 LEU   A CD1 
2433 C CD2 . LEU   A 109 ? 0.1518 0.1891 0.2780 0.0033  0.0030  0.0365  109 LEU   A CD2 
2445 N N   . LYS   A 110 ? 0.1522 0.1403 0.2286 -0.0049 -0.0015 0.0076  110 LYS   A N   
2446 C CA  . LYS   A 110 ? 0.1458 0.1362 0.2460 -0.0063 -0.0045 0.0055  110 LYS   A CA  
2447 C C   . LYS   A 110 ? 0.1448 0.1323 0.2341 -0.0042 -0.0012 0.0013  110 LYS   A C   
2448 O O   . LYS   A 110 ? 0.1417 0.1279 0.2504 -0.0087 0.0005  -0.0031 110 LYS   A O   
2449 C CB  . LYS   A 110 ? 0.1540 0.1427 0.2642 -0.0039 -0.0149 -0.0065 110 LYS   A CB  
2450 C CG  . LYS   A 110 ? 0.1600 0.1363 0.2887 0.0014  -0.0296 -0.0053 110 LYS   A CG  
2451 C CD  . LYS   A 110 ? 0.1612 0.1470 0.2778 -0.0042 -0.0160 -0.0158 110 LYS   A CD  
2452 C CE  . LYS   A 110 ? 0.1619 0.1538 0.2931 -0.0051 0.0061  -0.0176 110 LYS   A CE  
2453 N NZ  . LYS   A 110 ? 0.1754 0.1488 0.2987 -0.0137 0.0099  -0.0141 110 LYS   A NZ  
2467 N N   . SER   A 111 ? 0.1472 0.1378 0.2143 -0.0026 -0.0006 0.0000  111 SER   A N   
2468 C CA  . SER   A 111 ? 0.1396 0.1432 0.2209 -0.0008 0.0083  -0.0067 111 SER   A CA  
2469 C C   . SER   A 111 ? 0.1312 0.1330 0.2222 -0.0038 -0.0015 0.0075  111 SER   A C   
2470 O O   . SER   A 111 ? 0.1495 0.1257 0.2376 -0.0014 0.0071  0.0074  111 SER   A O   
2471 C CB  . SER   A 111 ? 0.1575 0.1647 0.2437 0.0033  0.0195  -0.0159 111 SER   A CB  
2472 O OG  . SER   A 111 ? 0.2079 0.1815 0.2325 0.0144  0.0163  -0.0135 111 SER   A OG  
2478 N N   . ALA   A 112 ? 0.1386 0.1328 0.2179 -0.0035 0.0072  0.0041  112 ALA   A N   
2479 C CA  . ALA   A 112 ? 0.1419 0.1306 0.2065 -0.0114 0.0107  -0.0046 112 ALA   A CA  
2480 C C   . ALA   A 112 ? 0.1323 0.1246 0.2317 -0.0035 0.0100  0.0075  112 ALA   A C   
2481 O O   . ALA   A 112 ? 0.1375 0.1211 0.2205 -0.0111 0.0186  0.0068  112 ALA   A O   
2482 C CB  . ALA   A 112 ? 0.1561 0.1340 0.2127 -0.0058 0.0138  0.0020  112 ALA   A CB  
2488 N N   . TYR   A 113 ? 0.1258 0.1308 0.2335 -0.0054 0.0064  0.0211  113 TYR   A N   
2489 C CA  . TYR   A 113 ? 0.1283 0.1249 0.2297 -0.0038 0.0153  0.0260  113 TYR   A CA  
2490 C C   . TYR   A 113 ? 0.1264 0.1269 0.2180 -0.0090 0.0043  0.0078  113 TYR   A C   
2491 O O   . TYR   A 113 ? 0.1324 0.1303 0.2287 -0.0084 0.0166  0.0109  113 TYR   A O   
2492 C CB  . TYR   A 113 ? 0.1256 0.1319 0.2414 -0.0078 0.0001  0.0267  113 TYR   A CB  
2493 C CG  . TYR   A 113 ? 0.1295 0.1380 0.2192 -0.0082 0.0144  0.0253  113 TYR   A CG  
2494 C CD1 . TYR   A 113 ? 0.1282 0.1457 0.2181 0.0001  0.0152  0.0259  113 TYR   A CD1 
2495 C CD2 . TYR   A 113 ? 0.1363 0.1417 0.2175 -0.0152 0.0006  0.0224  113 TYR   A CD2 
2496 C CE1 . TYR   A 113 ? 0.1332 0.1521 0.2143 -0.0078 0.0123  0.0299  113 TYR   A CE1 
2497 C CE2 . TYR   A 113 ? 0.1356 0.1520 0.2213 -0.0107 -0.0011 0.0366  113 TYR   A CE2 
2498 C CZ  . TYR   A 113 ? 0.1348 0.1530 0.2098 -0.0017 0.0124  0.0288  113 TYR   A CZ  
2499 O OH  . TYR   A 113 ? 0.1353 0.1616 0.2324 0.0139  0.0087  0.0171  113 TYR   A OH  
2509 N N   . GLU   A 114 ? 0.1277 0.1204 0.2355 0.0020  0.0105  0.0096  114 GLU   A N   
2510 C CA  . GLU   A 114 ? 0.1355 0.1232 0.2445 0.0005  0.0084  0.0188  114 GLU   A CA  
2511 C C   . GLU   A 114 ? 0.1295 0.1274 0.2312 -0.0027 0.0032  0.0151  114 GLU   A C   
2512 O O   . GLU   A 114 ? 0.1446 0.1271 0.2171 0.0014  0.0057  0.0131  114 GLU   A O   
2513 C CB  . GLU   A 114 ? 0.1408 0.1338 0.2231 0.0026  0.0127  0.0084  114 GLU   A CB  
2514 C CG  . GLU   A 114 ? 0.1447 0.1256 0.2530 0.0059  0.0032  -0.0024 114 GLU   A CG  
2515 C CD  . GLU   A 114 ? 0.1495 0.1230 0.2698 0.0027  0.0015  -0.0015 114 GLU   A CD  
2516 O OE1 . GLU   A 114 ? 0.1494 0.1306 0.2642 -0.0100 0.0075  -0.0109 114 GLU   A OE1 
2517 O OE2 . GLU   A 114 ? 0.1748 0.1377 0.2738 -0.0093 0.0064  -0.0144 114 GLU   A OE2 
2524 N N   . ASN   A 115 ? 0.1358 0.1270 0.2212 -0.0108 0.0108  0.0109  115 ASN   A N   
2525 C CA  . ASN   A 115 ? 0.1401 0.1315 0.2351 -0.0124 0.0102  0.0158  115 ASN   A CA  
2526 C C   . ASN   A 115 ? 0.1323 0.1295 0.2301 -0.0064 0.0043  0.0241  115 ASN   A C   
2527 O O   . ASN   A 115 ? 0.1348 0.1411 0.2159 -0.0066 0.0080  0.0207  115 ASN   A O   
2528 C CB  . ASN   A 115 ? 0.1472 0.1434 0.2074 -0.0130 0.0106  0.0139  115 ASN   A CB  
2529 C CG  . ASN   A 115 ? 0.1469 0.1511 0.2163 -0.0136 0.0219  0.0146  115 ASN   A CG  
2530 O OD1 . ASN   A 115 ? 0.1500 0.2458 0.2257 -0.0159 0.0279  0.0307  115 ASN   A OD1 
2531 N ND2 . ASN   A 115 ? 0.1479 0.1305 0.2238 -0.0135 0.0349  0.0169  115 ASN   A ND2 
2538 N N   . PHE   A 116 ? 0.1262 0.1238 0.2465 0.0021  0.0150  0.0214  116 PHE   A N   
2539 C CA  . PHE   A 116 ? 0.1292 0.1343 0.2269 -0.0020 0.0217  0.0178  116 PHE   A CA  
2540 C C   . PHE   A 116 ? 0.1312 0.1396 0.2226 -0.0125 0.0125  0.0160  116 PHE   A C   
2541 O O   . PHE   A 116 ? 0.1358 0.1479 0.2271 0.0026  0.0146  0.0365  116 PHE   A O   
2542 C CB  . PHE   A 116 ? 0.1329 0.1319 0.2359 -0.0071 0.0161  0.0225  116 PHE   A CB  
2543 C CG  . PHE   A 116 ? 0.1336 0.1258 0.2229 -0.0078 0.0182  0.0207  116 PHE   A CG  
2544 C CD1 . PHE   A 116 ? 0.1350 0.1270 0.2225 -0.0024 0.0135  0.0113  116 PHE   A CD1 
2545 C CD2 . PHE   A 116 ? 0.1416 0.1361 0.2190 -0.0077 0.0228  0.0250  116 PHE   A CD2 
2546 C CE1 . PHE   A 116 ? 0.1402 0.1340 0.2231 -0.0224 0.0111  0.0096  116 PHE   A CE1 
2547 C CE2 . PHE   A 116 ? 0.1381 0.1379 0.2394 -0.0000 0.0182  0.0166  116 PHE   A CE2 
2548 C CZ  . PHE   A 116 ? 0.1443 0.1209 0.2231 -0.0055 0.0111  0.0182  116 PHE   A CZ  
2558 N N   . ASN   A 117 ? 0.1330 0.1363 0.2226 -0.0093 0.0133  0.0286  117 ASN   A N   
2559 C CA  . ASN   A 117 ? 0.1354 0.1342 0.2588 -0.0047 0.0181  0.0331  117 ASN   A CA  
2560 C C   . ASN   A 117 ? 0.1347 0.1478 0.2643 -0.0021 0.0133  0.0382  117 ASN   A C   
2561 O O   . ASN   A 117 ? 0.1420 0.1577 0.2661 -0.0102 -0.0025 0.0414  117 ASN   A O   
2562 C CB  . ASN   A 117 ? 0.1368 0.1427 0.2455 -0.0025 0.0187  0.0337  117 ASN   A CB  
2563 C CG  . ASN   A 117 ? 0.1331 0.1371 0.2523 -0.0057 0.0194  0.0359  117 ASN   A CG  
2564 O OD1 . ASN   A 117 ? 0.1306 0.1621 0.2714 -0.0156 0.0093  0.0242  117 ASN   A OD1 
2565 N ND2 . ASN   A 117 ? 0.1320 0.1332 0.2526 -0.0001 0.0094  0.0282  117 ASN   A ND2 
2572 N N   . GLN   A 118 ? 0.1330 0.1462 0.2589 -0.0062 0.0028  0.0346  118 GLN   A N   
2573 C CA  . GLN   A 118 ? 0.1406 0.1575 0.2671 -0.0072 0.0072  0.0314  118 GLN   A CA  
2574 C C   . GLN   A 118 ? 0.1468 0.1666 0.2678 -0.0101 0.0008  0.0430  118 GLN   A C   
2575 O O   . GLN   A 118 ? 0.1399 0.1982 0.2705 -0.0007 -0.0065 0.0231  118 GLN   A O   
2576 C CB  . GLN   A 118 ? 0.1362 0.1639 0.2850 0.0034  0.0228  0.0265  118 GLN   A CB  
2577 C CG  . GLN   A 118 ? 0.1289 0.1622 0.2960 0.0053  0.0138  0.0428  118 GLN   A CG  
2578 C CD  . GLN   A 118 ? 0.1356 0.1613 0.2969 -0.0014 0.0105  0.0312  118 GLN   A CD  
2579 O OE1 . GLN   A 118 ? 0.1345 0.1675 0.3087 0.0079  0.0139  0.0144  118 GLN   A OE1 
2580 N NE2 . GLN   A 118 ? 0.1437 0.1613 0.2839 0.0031  0.0080  0.0343  118 GLN   A NE2 
2589 N N   . HIS   A 119 ? 0.1465 0.1582 0.2510 -0.0033 0.0021  0.0453  119 HIS   A N   
2590 C CA  . HIS   A 119 ? 0.1540 0.1726 0.2398 -0.0062 0.0020  0.0510  119 HIS   A CA  
2591 C C   . HIS   A 119 ? 0.1637 0.1934 0.2309 -0.0099 0.0091  0.0599  119 HIS   A C   
2592 O O   . HIS   A 119 ? 0.1605 0.1925 0.2451 -0.0248 -0.0081 0.0614  119 HIS   A O   
2593 C CB  . HIS   A 119 ? 0.1576 0.1692 0.2382 -0.0086 0.0207  0.0468  119 HIS   A CB  
2594 C CG  . HIS   A 119 ? 0.1553 0.1764 0.2788 -0.0000 0.0192  0.0535  119 HIS   A CG  
2595 N ND1 . HIS   A 119 ? 0.1693 0.1950 0.3249 -0.0082 0.0059  0.0329  119 HIS   A ND1 
2596 C CD2 . HIS   A 119 ? 0.1662 0.1791 0.2861 0.0169  0.0403  0.0675  119 HIS   A CD2 
2597 C CE1 . HIS   A 119 ? 0.1684 0.1868 0.3302 -0.0100 0.0246  0.0541  119 HIS   A CE1 
2598 N NE2 . HIS   A 119 ? 0.1804 0.1868 0.3280 -0.0012 0.0474  0.0760  119 HIS   A NE2 
2606 N N   A GLU   A 120 ? 0.1610 0.1992 0.2297 -0.0066 -0.0049 0.0811  120 GLU   A N   
2607 N N   B GLU   A 120 ? 0.1801 0.2162 0.2377 -0.0083 0.0004  0.0694  120 GLU   A N   
2608 C CA  A GLU   A 120 ? 0.1806 0.2124 0.2601 0.0038  -0.0130 0.1209  120 GLU   A CA  
2609 C CA  B GLU   A 120 ? 0.2068 0.2413 0.2686 -0.0002 -0.0030 0.0897  120 GLU   A CA  
2610 C C   A GLU   A 120 ? 0.1603 0.2001 0.2536 -0.0091 0.0077  0.1179  120 GLU   A C   
2611 C C   B GLU   A 120 ? 0.1973 0.2399 0.2552 -0.0054 0.0003  0.0855  120 GLU   A C   
2612 O O   A GLU   A 120 ? 0.1549 0.1934 0.2537 -0.0143 0.0099  0.1259  120 GLU   A O   
2613 O O   B GLU   A 120 ? 0.2009 0.2459 0.2613 -0.0119 -0.0093 0.0764  120 GLU   A O   
2614 C CB  A GLU   A 120 ? 0.2366 0.2534 0.3151 0.0154  -0.0114 0.1456  120 GLU   A CB  
2615 C CB  B GLU   A 120 ? 0.2529 0.2746 0.3277 0.0053  0.0044  0.1069  120 GLU   A CB  
2616 C CG  A GLU   A 120 ? 0.2913 0.2927 0.4049 0.0299  -0.0114 0.1346  120 GLU   A CG  
2617 C CG  B GLU   A 120 ? 0.2989 0.3084 0.4066 0.0144  0.0056  0.1034  120 GLU   A CG  
2618 C CD  A GLU   A 120 ? 0.3389 0.3266 0.4857 0.0461  -0.0064 0.1169  120 GLU   A CD  
2619 C CD  B GLU   A 120 ? 0.3392 0.3386 0.4772 0.0253  0.0072  0.0927  120 GLU   A CD  
2620 O OE1 A GLU   A 120 ? 0.3817 0.3526 0.5149 0.0468  -0.0055 0.1079  120 GLU   A OE1 
2621 O OE1 B GLU   A 120 ? 0.3631 0.3595 0.4990 0.0274  0.0094  0.0885  120 GLU   A OE1 
2622 O OE2 A GLU   A 120 ? 0.3667 0.3406 0.5287 0.0467  -0.0056 0.1101  120 GLU   A OE2 
2623 O OE2 B GLU   A 120 ? 0.3704 0.3512 0.5157 0.0254  0.0055  0.0893  120 GLU   A OE2 
2636 N N   A VAL   A 121 ? 0.1627 0.2057 0.2203 -0.0107 0.0170  0.0980  121 VAL   A N   
2637 N N   B VAL   A 121 ? 0.1916 0.2368 0.2281 -0.0007 0.0062  0.0804  121 VAL   A N   
2638 C CA  A VAL   A 121 ? 0.1676 0.2133 0.1939 -0.0178 0.0304  0.0887  121 VAL   A CA  
2639 C CA  B VAL   A 121 ? 0.1856 0.2337 0.2101 -0.0001 0.0093  0.0721  121 VAL   A CA  
2640 C C   A VAL   A 121 ? 0.1592 0.1972 0.1821 -0.0257 0.0110  0.0599  121 VAL   A C   
2641 C C   B VAL   A 121 ? 0.1629 0.2070 0.1834 -0.0065 0.0057  0.0525  121 VAL   A C   
2642 O O   A VAL   A 121 ? 0.1616 0.1923 0.2190 -0.0382 -0.0009 0.0471  121 VAL   A O   
2643 O O   B VAL   A 121 ? 0.1493 0.1970 0.1446 -0.0066 0.0176  0.0420  121 VAL   A O   
2644 C CB  A VAL   A 121 ? 0.1964 0.2455 0.2251 -0.0114 0.0359  0.0898  121 VAL   A CB  
2645 C CB  B VAL   A 121 ? 0.2095 0.2599 0.2417 0.0079  0.0095  0.0746  121 VAL   A CB  
2646 C CG1 A VAL   A 121 ? 0.1987 0.2649 0.2344 -0.0042 0.0248  0.0793  121 VAL   A CG1 
2647 C CG1 B VAL   A 121 ? 0.2088 0.2744 0.2483 0.0130  0.0031  0.0737  121 VAL   A CG1 
2648 C CG2 A VAL   A 121 ? 0.2127 0.2557 0.2487 -0.0221 0.0329  0.0835  121 VAL   A CG2 
2649 C CG2 B VAL   A 121 ? 0.2242 0.2694 0.2604 0.0029  0.0114  0.0667  121 VAL   A CG2 
2668 N N   . LEU   A 122 ? 0.1473 0.1856 0.1854 -0.0207 0.0059  0.0507  122 LEU   A N   
2669 C CA  . LEU   A 122 ? 0.1601 0.1668 0.1800 -0.0218 0.0182  0.0560  122 LEU   A CA  
2670 C C   . LEU   A 122 ? 0.1503 0.1678 0.1931 -0.0251 0.0037  0.0509  122 LEU   A C   
2671 O O   . LEU   A 122 ? 0.1510 0.1730 0.2205 -0.0285 -0.0006 0.0503  122 LEU   A O   
2672 C CB  . LEU   A 122 ? 0.1806 0.1687 0.2336 -0.0070 0.0055  0.0604  122 LEU   A CB  
2673 C CG  . LEU   A 122 ? 0.1718 0.1742 0.2289 -0.0079 0.0213  0.0383  122 LEU   A CG  
2674 C CD1 . LEU   A 122 ? 0.1857 0.1734 0.2242 -0.0159 0.0234  0.0321  122 LEU   A CD1 
2675 C CD2 . LEU   A 122 ? 0.1706 0.1717 0.2176 -0.0010 0.0245  0.0416  122 LEU   A CD2 
2688 N N   A LEU   A 123 ? 0.1437 0.1632 0.1994 -0.0333 0.0100  0.0396  123 LEU   A N   
2689 N N   B LEU   A 123 ? 0.1464 0.1622 0.1938 -0.0227 -0.0007 0.0311  123 LEU   A N   
2690 C CA  A LEU   A 123 ? 0.1433 0.1666 0.1751 -0.0280 0.0121  0.0401  123 LEU   A CA  
2691 C CA  B LEU   A 123 ? 0.1467 0.1611 0.1759 -0.0100 -0.0107 0.0290  123 LEU   A CA  
2692 C C   A LEU   A 123 ? 0.1396 0.1536 0.1710 -0.0212 0.0125  0.0439  123 LEU   A C   
2693 C C   B LEU   A 123 ? 0.1401 0.1543 0.1634 -0.0058 -0.0022 0.0320  123 LEU   A C   
2694 O O   A LEU   A 123 ? 0.1339 0.1489 0.1840 -0.0219 0.0086  0.0409  123 LEU   A O   
2695 O O   B LEU   A 123 ? 0.1410 0.1534 0.1577 -0.0110 0.0116  0.0068  123 LEU   A O   
2696 C CB  A LEU   A 123 ? 0.1562 0.1809 0.1667 -0.0344 0.0293  0.0393  123 LEU   A CB  
2697 C CB  B LEU   A 123 ? 0.1565 0.1711 0.1776 -0.0116 -0.0201 0.0373  123 LEU   A CB  
2698 C CG  A LEU   A 123 ? 0.1564 0.1972 0.1732 -0.0210 0.0278  0.0230  123 LEU   A CG  
2699 C CG  B LEU   A 123 ? 0.1563 0.1821 0.1792 -0.0112 -0.0216 0.0372  123 LEU   A CG  
2700 C CD1 A LEU   A 123 ? 0.1613 0.2074 0.1811 -0.0134 0.0277  0.0163  123 LEU   A CD1 
2701 C CD1 B LEU   A 123 ? 0.1563 0.1893 0.2052 -0.0069 -0.0193 0.0267  123 LEU   A CD1 
2702 C CD2 A LEU   A 123 ? 0.1587 0.1970 0.1646 -0.0201 0.0273  0.0176  123 LEU   A CD2 
2703 C CD2 B LEU   A 123 ? 0.1666 0.1868 0.2137 -0.0083 -0.0209 0.0294  123 LEU   A CD2 
2726 N N   A ALA   A 124 ? 0.1433 0.1483 0.1542 -0.0275 0.0180  0.0356  124 ALA   A N   
2727 N N   B ALA   A 124 ? 0.1383 0.1454 0.1636 -0.0014 -0.0087 0.0440  124 ALA   A N   
2728 C CA  A ALA   A 124 ? 0.1355 0.1396 0.1601 -0.0284 0.0160  0.0232  124 ALA   A CA  
2729 C CA  B ALA   A 124 ? 0.1257 0.1366 0.1576 0.0067  0.0006  0.0365  124 ALA   A CA  
2730 C C   A ALA   A 124 ? 0.1330 0.1343 0.1497 -0.0158 0.0223  0.0161  124 ALA   A C   
2731 C C   B ALA   A 124 ? 0.1259 0.1367 0.1479 0.0036  0.0139  0.0122  124 ALA   A C   
2732 O O   A ALA   A 124 ? 0.1297 0.1244 0.1708 -0.0139 0.0220  0.0057  124 ALA   A O   
2733 O O   B ALA   A 124 ? 0.1256 0.1398 0.1409 -0.0035 0.0221  0.0126  124 ALA   A O   
2734 C CB  A ALA   A 124 ? 0.1466 0.1410 0.1844 -0.0251 0.0174  0.0171  124 ALA   A CB  
2735 C CB  B ALA   A 124 ? 0.1210 0.1309 0.1661 0.0168  -0.0038 0.0392  124 ALA   A CB  
2746 N N   A PRO   A 125 ? 0.1203 0.1251 0.1459 -0.0105 0.0116  0.0151  125 PRO   A N   
2747 N N   B PRO   A 125 ? 0.1291 0.1349 0.1296 0.0002  0.0076  0.0108  125 PRO   A N   
2748 C CA  A PRO   A 125 ? 0.1237 0.1284 0.1536 -0.0019 0.0112  0.0121  125 PRO   A CA  
2749 C CA  B PRO   A 125 ? 0.1464 0.1419 0.1651 -0.0021 0.0075  0.0063  125 PRO   A CA  
2750 C C   A PRO   A 125 ? 0.1114 0.1370 0.1342 -0.0074 0.0142  0.0140  125 PRO   A C   
2751 C C   B PRO   A 125 ? 0.1487 0.1458 0.1620 -0.0034 0.0088  -0.0024 125 PRO   A C   
2752 O O   A PRO   A 125 ? 0.1215 0.1452 0.1472 0.0050  0.0079  0.0139  125 PRO   A O   
2753 O O   B PRO   A 125 ? 0.1535 0.1391 0.1567 -0.0032 0.0246  0.0014  125 PRO   A O   
2754 C CB  A PRO   A 125 ? 0.1374 0.1194 0.1689 -0.0007 0.0207  0.0131  125 PRO   A CB  
2755 C CB  B PRO   A 125 ? 0.1493 0.1419 0.1560 0.0022  0.0220  0.0013  125 PRO   A CB  
2756 C CG  A PRO   A 125 ? 0.1391 0.1185 0.1514 -0.0076 0.0211  0.0110  125 PRO   A CG  
2757 C CG  B PRO   A 125 ? 0.1510 0.1446 0.1527 -0.0046 0.0207  -0.0011 125 PRO   A CG  
2758 C CD  A PRO   A 125 ? 0.1223 0.1211 0.1312 -0.0156 0.0218  0.0091  125 PRO   A CD  
2759 C CD  B PRO   A 125 ? 0.1339 0.1452 0.1538 -0.0070 0.0195  0.0065  125 PRO   A CD  
2774 N N   A LEU   A 126 ? 0.1088 0.1334 0.1652 -0.0017 0.0143  0.0123  126 LEU   A N   
2775 N N   B LEU   A 126 ? 0.1637 0.1577 0.1789 -0.0058 -0.0044 -0.0001 126 LEU   A N   
2776 C CA  A LEU   A 126 ? 0.1207 0.1333 0.1739 -0.0055 0.0048  0.0120  126 LEU   A CA  
2777 C CA  B LEU   A 126 ? 0.1707 0.1603 0.1957 -0.0104 0.0014  0.0021  126 LEU   A CA  
2778 C C   A LEU   A 126 ? 0.1279 0.1250 0.1794 -0.0098 0.0008  0.0015  126 LEU   A C   
2779 C C   B LEU   A 126 ? 0.1751 0.1559 0.2029 0.0020  0.0201  0.0054  126 LEU   A C   
2780 O O   A LEU   A 126 ? 0.1325 0.1130 0.1671 -0.0101 -0.0020 0.0014  126 LEU   A O   
2781 O O   B LEU   A 126 ? 0.1946 0.1541 0.2524 -0.0051 0.0386  0.0068  126 LEU   A O   
2782 C CB  A LEU   A 126 ? 0.1274 0.1366 0.1974 -0.0011 0.0055  0.0168  126 LEU   A CB  
2783 C CB  B LEU   A 126 ? 0.1742 0.1776 0.2170 -0.0244 -0.0015 0.0046  126 LEU   A CB  
2784 C CG  A LEU   A 126 ? 0.1305 0.1521 0.2063 -0.0006 0.0094  0.0255  126 LEU   A CG  
2785 C CG  B LEU   A 126 ? 0.1721 0.1885 0.2481 -0.0161 -0.0040 0.0146  126 LEU   A CG  
2786 C CD1 A LEU   A 126 ? 0.1317 0.1605 0.2051 -0.0083 0.0064  0.0470  126 LEU   A CD1 
2787 C CD1 B LEU   A 126 ? 0.1684 0.1867 0.2667 -0.0197 -0.0116 0.0146  126 LEU   A CD1 
2788 C CD2 A LEU   A 126 ? 0.1452 0.1543 0.2063 -0.0084 0.0063  0.0267  126 LEU   A CD2 
2789 C CD2 B LEU   A 126 ? 0.1684 0.1876 0.2544 -0.0139 -0.0035 0.0258  126 LEU   A CD2 
2812 N N   A LEU   A 127 ? 0.1279 0.1421 0.1784 -0.0032 0.0114  0.0078  127 LEU   A N   
2813 N N   B LEU   A 127 ? 0.1589 0.1546 0.1841 0.0097  0.0177  0.0264  127 LEU   A N   
2814 C CA  A LEU   A 127 ? 0.1287 0.1450 0.1726 -0.0010 0.0029  -0.0032 127 LEU   A CA  
2815 C CA  B LEU   A 127 ? 0.1503 0.1582 0.1800 0.0064  0.0002  0.0208  127 LEU   A CA  
2816 C C   A LEU   A 127 ? 0.1287 0.1391 0.1733 -0.0059 -0.0041 -0.0020 127 LEU   A C   
2817 C C   B LEU   A 127 ? 0.1472 0.1493 0.1804 0.0023  -0.0200 0.0168  127 LEU   A C   
2818 O O   A LEU   A 127 ? 0.1352 0.1418 0.1832 -0.0149 0.0042  0.0089  127 LEU   A O   
2819 O O   B LEU   A 127 ? 0.1493 0.1554 0.1716 -0.0048 -0.0275 0.0325  127 LEU   A O   
2820 C CB  A LEU   A 127 ? 0.1369 0.1410 0.1867 0.0084  0.0084  0.0055  127 LEU   A CB  
2821 C CB  B LEU   A 127 ? 0.1504 0.1711 0.1786 0.0055  0.0046  0.0143  127 LEU   A CB  
2822 C CG  A LEU   A 127 ? 0.1428 0.1480 0.1844 0.0082  -0.0127 0.0123  127 LEU   A CG  
2823 C CG  B LEU   A 127 ? 0.1525 0.1838 0.1721 0.0060  -0.0069 0.0251  127 LEU   A CG  
2824 C CD1 A LEU   A 127 ? 0.1470 0.1435 0.2016 0.0043  -0.0089 0.0085  127 LEU   A CD1 
2825 C CD1 B LEU   A 127 ? 0.1530 0.1913 0.1934 0.0103  0.0049  0.0356  127 LEU   A CD1 
2826 C CD2 A LEU   A 127 ? 0.1572 0.1487 0.2071 0.0200  -0.0161 0.0228  127 LEU   A CD2 
2827 C CD2 B LEU   A 127 ? 0.1621 0.1927 0.1799 0.0039  -0.0204 0.0188  127 LEU   A CD2 
2850 N N   A SER   A 128 ? 0.1353 0.1407 0.1739 -0.0130 0.0036  0.0106  128 SER   A N   
2851 N N   B SER   A 128 ? 0.1513 0.1452 0.1866 -0.0061 -0.0143 0.0102  128 SER   A N   
2852 C CA  A SER   A 128 ? 0.1462 0.1380 0.1721 -0.0066 -0.0009 0.0062  128 SER   A CA  
2853 C CA  B SER   A 128 ? 0.1546 0.1380 0.1820 0.0009  -0.0106 0.0107  128 SER   A CA  
2854 C C   A SER   A 128 ? 0.1514 0.1435 0.1532 -0.0033 0.0019  0.0099  128 SER   A C   
2855 C C   B SER   A 128 ? 0.1588 0.1449 0.1804 0.0074  -0.0178 0.0164  128 SER   A C   
2856 O O   A SER   A 128 ? 0.1634 0.1628 0.1605 -0.0033 0.0188  -0.0030 128 SER   A O   
2857 O O   B SER   A 128 ? 0.1545 0.1481 0.1887 0.0108  -0.0106 0.0189  128 SER   A O   
2858 C CB  A SER   A 128 ? 0.1436 0.1408 0.1825 -0.0043 -0.0012 0.0004  128 SER   A CB  
2859 C CB  B SER   A 128 ? 0.1485 0.1412 0.1840 -0.0021 -0.0038 0.0153  128 SER   A CB  
2860 O OG  A SER   A 128 ? 0.1501 0.1427 0.1937 -0.0020 -0.0082 -0.0200 128 SER   A OG  
2861 O OG  B SER   A 128 ? 0.1398 0.1511 0.1817 0.0016  0.0060  0.0208  128 SER   A OG  
2872 N N   A ALA   A 129 ? 0.1510 0.1450 0.1588 -0.0028 0.0038  0.0193  129 ALA   A N   
2873 N N   B ALA   A 129 ? 0.1634 0.1587 0.1702 0.0111  -0.0233 0.0035  129 ALA   A N   
2874 C CA  A ALA   A 129 ? 0.1387 0.1503 0.1359 0.0002  0.0075  0.0247  129 ALA   A CA  
2875 C CA  B ALA   A 129 ? 0.1634 0.1676 0.1597 0.0130  -0.0239 -0.0046 129 ALA   A CA  
2876 C C   A ALA   A 129 ? 0.1428 0.1535 0.1206 -0.0024 0.0036  0.0073  129 ALA   A C   
2877 C C   B ALA   A 129 ? 0.1807 0.1778 0.1693 0.0209  -0.0140 -0.0065 129 ALA   A C   
2878 O O   A ALA   A 129 ? 0.1479 0.1572 0.1405 -0.0112 0.0041  0.0108  129 ALA   A O   
2879 O O   B ALA   A 129 ? 0.1808 0.1764 0.1575 0.0232  -0.0167 -0.0057 129 ALA   A O   
2880 C CB  A ALA   A 129 ? 0.1346 0.1710 0.1491 0.0044  0.0023  0.0383  129 ALA   A CB  
2881 C CB  B ALA   A 129 ? 0.1601 0.1803 0.1489 0.0146  -0.0203 -0.0220 129 ALA   A CB  
2892 N N   A GLY   A 130 ? 0.1447 0.1515 0.1171 -0.0005 -0.0009 0.0053  130 GLY   A N   
2893 N N   B GLY   A 130 ? 0.1976 0.1881 0.1748 0.0152  -0.0014 -0.0125 130 GLY   A N   
2894 C CA  A GLY   A 130 ? 0.1598 0.1450 0.1240 0.0101  0.0086  0.0012  130 GLY   A CA  
2895 C CA  B GLY   A 130 ? 0.2114 0.1913 0.1873 0.0129  -0.0138 -0.0053 130 GLY   A CA  
2896 C C   A GLY   A 130 ? 0.1587 0.1298 0.1109 0.0081  0.0133  -0.0081 130 GLY   A C   
2897 C C   B GLY   A 130 ? 0.2174 0.1922 0.1902 0.0087  -0.0247 0.0020  130 GLY   A C   
2898 O O   A GLY   A 130 ? 0.1552 0.1317 0.1259 0.0031  0.0067  -0.0009 130 GLY   A O   
2899 O O   B GLY   A 130 ? 0.2146 0.1934 0.1885 0.0114  -0.0373 0.0097  130 GLY   A O   
2906 N N   A ILE   A 131 ? 0.1762 0.1256 0.1261 -0.0034 0.0098  -0.0034 131 ILE   A N   
2907 N N   B ILE   A 131 ? 0.2259 0.1957 0.2065 0.0009  -0.0176 0.0004  131 ILE   A N   
2908 C CA  A ILE   A 131 ? 0.1904 0.1271 0.1272 -0.0071 -0.0065 -0.0031 131 ILE   A CA  
2909 C CA  B ILE   A 131 ? 0.2320 0.1967 0.2153 -0.0049 -0.0070 -0.0027 131 ILE   A CA  
2910 C C   A ILE   A 131 ? 0.1713 0.1286 0.1103 -0.0064 -0.0026 0.0141  131 ILE   A C   
2911 C C   B ILE   A 131 ? 0.2181 0.2013 0.2165 0.0029  -0.0022 0.0025  131 ILE   A C   
2912 O O   A ILE   A 131 ? 0.1783 0.1324 0.1165 -0.0050 -0.0012 0.0176  131 ILE   A O   
2913 O O   B ILE   A 131 ? 0.2230 0.2149 0.2235 0.0122  0.0091  0.0073  131 ILE   A O   
2914 C CB  A ILE   A 131 ? 0.2246 0.1430 0.1429 -0.0113 -0.0074 -0.0050 131 ILE   A CB  
2915 C CB  B ILE   A 131 ? 0.2487 0.2044 0.2329 -0.0156 -0.0004 -0.0133 131 ILE   A CB  
2916 C CG1 A ILE   A 131 ? 0.2336 0.1815 0.1644 -0.0248 -0.0130 -0.0227 131 ILE   A CG1 
2917 C CG1 B ILE   A 131 ? 0.2532 0.2209 0.2445 -0.0181 -0.0030 -0.0155 131 ILE   A CG1 
2918 C CG2 A ILE   A 131 ? 0.2488 0.1310 0.1720 -0.0114 0.0209  -0.0140 131 ILE   A CG2 
2919 C CG2 B ILE   A 131 ? 0.2583 0.2002 0.2429 -0.0198 0.0103  -0.0090 131 ILE   A CG2 
2920 C CD1 A ILE   A 131 ? 0.2391 0.2005 0.1960 -0.0258 -0.0055 -0.0304 131 ILE   A CD1 
2921 C CD1 B ILE   A 131 ? 0.2575 0.2293 0.2509 -0.0188 -0.0067 -0.0146 131 ILE   A CD1 
2944 N N   A PHE   A 132 ? 0.1517 0.1278 0.1162 -0.0128 0.0161  0.0123  132 PHE   A N   
2945 N N   B PHE   A 132 ? 0.2060 0.1951 0.2077 -0.0014 -0.0072 0.0029  132 PHE   A N   
2946 C CA  A PHE   A 132 ? 0.1581 0.1359 0.1389 -0.0146 0.0147  -0.0135 132 PHE   A CA  
2947 C CA  B PHE   A 132 ? 0.1925 0.1948 0.1986 -0.0028 -0.0123 0.0076  132 PHE   A CA  
2948 C C   A PHE   A 132 ? 0.1637 0.1593 0.1268 -0.0148 0.0107  0.0025  132 PHE   A C   
2949 C C   B PHE   A 132 ? 0.1913 0.2034 0.1986 0.0058  -0.0067 0.0123  132 PHE   A C   
2950 O O   A PHE   A 132 ? 0.1739 0.1826 0.1464 -0.0048 0.0068  -0.0012 132 PHE   A O   
2951 O O   B PHE   A 132 ? 0.2022 0.2180 0.1982 0.0084  0.0080  0.0098  132 PHE   A O   
2952 C CB  A PHE   A 132 ? 0.1658 0.1276 0.1311 -0.0111 0.0078  -0.0175 132 PHE   A CB  
2953 C CB  B PHE   A 132 ? 0.1766 0.1843 0.1730 -0.0110 -0.0120 0.0258  132 PHE   A CB  
2954 C CG  A PHE   A 132 ? 0.1641 0.1351 0.1411 -0.0028 -0.0056 -0.0158 132 PHE   A CG  
2955 C CG  B PHE   A 132 ? 0.1760 0.1857 0.1876 -0.0053 -0.0194 0.0209  132 PHE   A CG  
2956 C CD1 A PHE   A 132 ? 0.1693 0.1496 0.1449 0.0076  -0.0149 -0.0214 132 PHE   A CD1 
2957 C CD1 B PHE   A 132 ? 0.1813 0.1907 0.2020 0.0029  -0.0262 0.0132  132 PHE   A CD1 
2958 C CD2 A PHE   A 132 ? 0.1623 0.1439 0.1672 0.0036  -0.0041 -0.0131 132 PHE   A CD2 
2959 C CD2 B PHE   A 132 ? 0.1728 0.1942 0.2000 -0.0045 -0.0249 0.0244  132 PHE   A CD2 
2960 C CE1 A PHE   A 132 ? 0.1754 0.1604 0.1806 0.0058  -0.0296 -0.0097 132 PHE   A CE1 
2961 C CE1 B PHE   A 132 ? 0.1874 0.1939 0.2154 0.0004  -0.0355 0.0040  132 PHE   A CE1 
2962 C CE2 A PHE   A 132 ? 0.1649 0.1519 0.1778 0.0035  -0.0060 -0.0043 132 PHE   A CE2 
2963 C CE2 B PHE   A 132 ? 0.1748 0.1977 0.2189 -0.0076 -0.0261 0.0227  132 PHE   A CE2 
2964 C CZ  A PHE   A 132 ? 0.1738 0.1535 0.1749 0.0031  -0.0174 0.0014  132 PHE   A CZ  
2965 C CZ  B PHE   A 132 ? 0.1836 0.1943 0.2182 -0.0072 -0.0359 0.0139  132 PHE   A CZ  
2984 N N   A GLY   A 133 ? 0.1607 0.1686 0.1077 -0.0131 -0.0064 0.0105  133 GLY   A N   
2985 N N   B GLY   A 133 ? 0.1872 0.1959 0.1990 0.0039  -0.0069 0.0173  133 GLY   A N   
2986 C CA  A GLY   A 133 ? 0.1741 0.1777 0.1309 -0.0145 -0.0019 0.0115  133 GLY   A CA  
2987 C CA  B GLY   A 133 ? 0.1844 0.1948 0.1992 0.0007  -0.0223 0.0026  133 GLY   A CA  
2988 C C   A GLY   A 133 ? 0.1843 0.1902 0.1600 -0.0190 -0.0305 -0.0016 133 GLY   A C   
2989 C C   B GLY   A 133 ? 0.1769 0.2033 0.2001 -0.0054 -0.0336 -0.0202 133 GLY   A C   
2990 O O   A GLY   A 133 ? 0.1937 0.2052 0.1825 -0.0267 -0.0491 -0.0133 133 GLY   A O   
2991 O O   B GLY   A 133 ? 0.1711 0.2169 0.2097 -0.0049 -0.0554 -0.0275 133 GLY   A O   
2998 N N   A ALA   A 134 ? 0.1874 0.1751 0.1487 -0.0125 -0.0147 -0.0087 134 ALA   A N   
2999 N N   B ALA   A 134 ? 0.1752 0.1922 0.1830 -0.0034 -0.0033 -0.0290 134 ALA   A N   
3000 C CA  A ALA   A 134 ? 0.1877 0.1766 0.1588 -0.0072 -0.0211 -0.0040 134 ALA   A CA  
3001 C CA  B ALA   A 134 ? 0.1716 0.1975 0.1905 -0.0054 -0.0141 -0.0242 134 ALA   A CA  
3002 C C   A ALA   A 134 ? 0.1901 0.1825 0.1855 -0.0078 -0.0121 0.0166  134 ALA   A C   
3003 C C   B ALA   A 134 ? 0.1732 0.1996 0.1869 -0.0113 -0.0183 -0.0084 134 ALA   A C   
3004 O O   A ALA   A 134 ? 0.2026 0.1852 0.2066 -0.0052 0.0078  0.0254  134 ALA   A O   
3005 O O   B ALA   A 134 ? 0.1835 0.1979 0.1893 -0.0188 -0.0037 -0.0017 134 ALA   A O   
3006 C CB  A ALA   A 134 ? 0.1932 0.1714 0.1809 -0.0003 -0.0336 -0.0190 134 ALA   A CB  
3007 C CB  B ALA   A 134 ? 0.1757 0.1945 0.2201 -0.0025 -0.0172 -0.0346 134 ALA   A CB  
3018 N N   A ASP   A 135 ? 0.1942 0.1918 0.1901 -0.0182 -0.0133 0.0258  135 ASP   A N   
3019 N N   B ASP   A 135 ? 0.1823 0.2050 0.1994 -0.0078 -0.0351 0.0015  135 ASP   A N   
3020 C CA  A ASP   A 135 ? 0.1894 0.2015 0.2163 -0.0274 -0.0289 0.0267  135 ASP   A CA  
3021 C CA  B ASP   A 135 ? 0.1860 0.2125 0.2202 -0.0105 -0.0358 0.0226  135 ASP   A CA  
3022 C C   A ASP   A 135 ? 0.1761 0.1860 0.2209 -0.0235 -0.0222 0.0214  135 ASP   A C   
3023 C C   B ASP   A 135 ? 0.1774 0.2022 0.2178 -0.0067 -0.0206 0.0342  135 ASP   A C   
3024 O O   A ASP   A 135 ? 0.1742 0.1766 0.2029 -0.0269 -0.0232 0.0160  135 ASP   A O   
3025 O O   B ASP   A 135 ? 0.1754 0.1980 0.2149 -0.0050 -0.0136 0.0438  135 ASP   A O   
3026 C CB  A ASP   A 135 ? 0.2096 0.2292 0.2491 -0.0441 -0.0526 0.0303  135 ASP   A CB  
3027 C CB  B ASP   A 135 ? 0.2052 0.2317 0.2554 -0.0278 -0.0479 0.0302  135 ASP   A CB  
3028 C CG  A ASP   A 135 ? 0.2225 0.2466 0.2902 -0.0599 -0.0563 0.0317  135 ASP   A CG  
3029 C CG  B ASP   A 135 ? 0.2209 0.2472 0.2962 -0.0363 -0.0502 0.0329  135 ASP   A CG  
3030 O OD1 A ASP   A 135 ? 0.2145 0.2565 0.2873 -0.0730 -0.0497 0.0651  135 ASP   A OD1 
3031 O OD1 B ASP   A 135 ? 0.2265 0.2491 0.3230 -0.0301 -0.0441 0.0439  135 ASP   A OD1 
3032 O OD2 A ASP   A 135 ? 0.2470 0.2595 0.3402 -0.0540 -0.0386 0.0269  135 ASP   A OD2 
3033 O OD2 B ASP   A 135 ? 0.2291 0.2610 0.3179 -0.0432 -0.0556 0.0337  135 ASP   A OD2 
3042 N N   A PRO   A 136 ? 0.1593 0.1859 0.2457 -0.0029 -0.0116 0.0315  136 PRO   A N   
3043 N N   B PRO   A 136 ? 0.1661 0.1960 0.2273 0.0006  -0.0115 0.0391  136 PRO   A N   
3044 C CA  A PRO   A 136 ? 0.1557 0.1785 0.2515 -0.0001 -0.0061 0.0140  136 PRO   A CA  
3045 C CA  B PRO   A 136 ? 0.1680 0.1876 0.2252 -0.0010 -0.0080 0.0133  136 PRO   A CA  
3046 C C   A PRO   A 136 ? 0.1418 0.1686 0.2192 0.0037  -0.0014 0.0105  136 PRO   A C   
3047 C C   B PRO   A 136 ? 0.1572 0.1858 0.2095 -0.0045 -0.0092 -0.0041 136 PRO   A C   
3048 O O   A PRO   A 136 ? 0.1351 0.1497 0.1926 0.0057  0.0115  0.0149  136 PRO   A O   
3049 O O   B PRO   A 136 ? 0.1456 0.1882 0.1914 -0.0095 -0.0128 -0.0084 136 PRO   A O   
3050 C CB  A PRO   A 136 ? 0.1721 0.1842 0.2704 0.0073  -0.0012 0.0136  136 PRO   A CB  
3051 C CB  B PRO   A 136 ? 0.1800 0.1892 0.2367 0.0053  -0.0027 0.0168  136 PRO   A CB  
3052 C CG  A PRO   A 136 ? 0.1826 0.1934 0.2897 0.0089  0.0081  0.0258  136 PRO   A CG  
3053 C CG  B PRO   A 136 ? 0.1885 0.1971 0.2480 0.0113  0.0059  0.0232  136 PRO   A CG  
3054 C CD  A PRO   A 136 ? 0.1702 0.1917 0.2628 0.0060  0.0078  0.0399  136 PRO   A CD  
3055 C CD  B PRO   A 136 ? 0.1757 0.1940 0.2385 0.0040  0.0033  0.0452  136 PRO   A CD  
3070 N N   A ILE   A 137 ? 0.1442 0.1791 0.2246 0.0035  -0.0041 0.0211  137 ILE   A N   
3071 N N   B ILE   A 137 ? 0.1585 0.1933 0.2078 -0.0111 -0.0071 -0.0016 137 ILE   A N   
3072 C CA  A ILE   A 137 ? 0.1473 0.1933 0.2190 -0.0066 -0.0072 0.0217  137 ILE   A CA  
3073 C CA  B ILE   A 137 ? 0.1624 0.2011 0.2019 -0.0208 -0.0129 -0.0017 137 ILE   A CA  
3074 C C   A ILE   A 137 ? 0.1459 0.1839 0.1994 -0.0099 -0.0105 0.0187  137 ILE   A C   
3075 C C   B ILE   A 137 ? 0.1663 0.1932 0.2074 -0.0226 -0.0116 -0.0016 137 ILE   A C   
3076 O O   A ILE   A 137 ? 0.1461 0.1782 0.1931 -0.0166 -0.0173 0.0237  137 ILE   A O   
3077 O O   B ILE   A 137 ? 0.1772 0.1843 0.2108 -0.0287 -0.0160 -0.0109 137 ILE   A O   
3078 C CB  A ILE   A 137 ? 0.1505 0.2188 0.2242 -0.0128 -0.0200 0.0171  137 ILE   A CB  
3079 C CB  B ILE   A 137 ? 0.1690 0.2219 0.1893 -0.0199 -0.0220 -0.0003 137 ILE   A CB  
3080 C CG1 A ILE   A 137 ? 0.1573 0.2448 0.2285 -0.0018 -0.0162 0.0226  137 ILE   A CG1 
3081 C CG1 B ILE   A 137 ? 0.1805 0.2445 0.2010 -0.0012 -0.0252 -0.0057 137 ILE   A CG1 
3082 C CG2 A ILE   A 137 ? 0.1661 0.2221 0.2209 -0.0236 -0.0382 0.0067  137 ILE   A CG2 
3083 C CG2 B ILE   A 137 ? 0.1750 0.2202 0.1783 -0.0321 -0.0209 0.0055  137 ILE   A CG2 
3084 C CD1 A ILE   A 137 ? 0.1719 0.2604 0.2416 0.0052  -0.0129 0.0176  137 ILE   A CD1 
3085 C CD1 B ILE   A 137 ? 0.1923 0.2564 0.2079 0.0090  -0.0245 -0.0189 137 ILE   A CD1 
3108 N N   A HIS   A 138 ? 0.1464 0.1934 0.2129 -0.0132 0.0053  0.0123  138 HIS   A N   
3109 N N   B HIS   A 138 ? 0.1560 0.2013 0.2111 -0.0190 0.0007  -0.0011 138 HIS   A N   
3110 C CA  A HIS   A 138 ? 0.1500 0.1972 0.2113 -0.0126 0.0112  0.0208  138 HIS   A CA  
3111 C CA  B HIS   A 138 ? 0.1524 0.2050 0.2287 -0.0180 -0.0001 0.0028  138 HIS   A CA  
3112 C C   A HIS   A 138 ? 0.1486 0.1866 0.2169 -0.0127 0.0045  0.0345  138 HIS   A C   
3113 C C   B HIS   A 138 ? 0.1440 0.1955 0.2320 -0.0122 -0.0049 0.0166  138 HIS   A C   
3114 O O   A HIS   A 138 ? 0.1643 0.1874 0.2263 -0.0166 0.0040  0.0327  138 HIS   A O   
3115 O O   B HIS   A 138 ? 0.1429 0.2010 0.2343 -0.0116 -0.0023 0.0129  138 HIS   A O   
3116 C CB  A HIS   A 138 ? 0.1571 0.2164 0.2134 -0.0082 0.0039  0.0114  138 HIS   A CB  
3117 C CB  B HIS   A 138 ? 0.1707 0.2245 0.2375 -0.0229 -0.0180 -0.0051 138 HIS   A CB  
3118 C CG  A HIS   A 138 ? 0.1705 0.2289 0.2305 -0.0052 -0.0069 -0.0099 138 HIS   A CG  
3119 C CG  B HIS   A 138 ? 0.1842 0.2362 0.2450 -0.0295 -0.0139 -0.0147 138 HIS   A CG  
3120 N ND1 A HIS   A 138 ? 0.1868 0.2377 0.2606 -0.0019 0.0116  -0.0228 138 HIS   A ND1 
3121 N ND1 B HIS   A 138 ? 0.1948 0.2468 0.2663 -0.0293 0.0004  -0.0194 138 HIS   A ND1 
3122 C CD2 A HIS   A 138 ? 0.1706 0.2384 0.2388 0.0017  -0.0057 -0.0102 138 HIS   A CD2 
3123 C CD2 B HIS   A 138 ? 0.1887 0.2451 0.2543 -0.0222 -0.0188 -0.0131 138 HIS   A CD2 
3124 C CE1 A HIS   A 138 ? 0.1910 0.2404 0.2716 0.0096  0.0125  -0.0236 138 HIS   A CE1 
3125 C CE1 B HIS   A 138 ? 0.2017 0.2529 0.2773 -0.0204 -0.0008 -0.0137 138 HIS   A CE1 
3126 N NE2 A HIS   A 138 ? 0.1859 0.2442 0.2578 0.0071  0.0105  -0.0197 138 HIS   A NE2 
3127 N NE2 B HIS   A 138 ? 0.1980 0.2527 0.2705 -0.0167 -0.0070 -0.0143 138 HIS   A NE2 
3142 N N   . SER   A 139 ? 0.1377 0.1810 0.2220 -0.0107 -0.0024 0.0302  139 SER   A N   
3143 C CA  . SER   A 139 ? 0.1348 0.1729 0.2336 -0.0086 0.0032  0.0303  139 SER   A CA  
3144 C C   . SER   A 139 ? 0.1339 0.1620 0.2250 -0.0078 0.0032  0.0244  139 SER   A C   
3145 O O   . SER   A 139 ? 0.1349 0.1628 0.2283 -0.0098 -0.0048 0.0335  139 SER   A O   
3146 C CB  . SER   A 139 ? 0.1258 0.1738 0.2359 -0.0121 -0.0045 0.0353  139 SER   A CB  
3147 O OG  . SER   A 139 ? 0.1439 0.1756 0.2376 -0.0239 -0.0082 0.0419  139 SER   A OG  
3154 N N   A LEU   A 140 ? 0.1268 0.1598 0.2177 -0.0064 0.0082  0.0433  140 LEU   A N   
3155 N N   B LEU   A 140 ? 0.1386 0.1676 0.2211 -0.0119 -0.0000 0.0326  140 LEU   A N   
3156 C CA  A LEU   A 140 ? 0.1233 0.1550 0.2218 -0.0087 0.0106  0.0356  140 LEU   A CA  
3157 C CA  B LEU   A 140 ? 0.1435 0.1648 0.2205 -0.0171 -0.0059 0.0179  140 LEU   A CA  
3158 C C   A LEU   A 140 ? 0.1192 0.1637 0.2092 -0.0182 0.0062  0.0424  140 LEU   A C   
3159 C C   B LEU   A 140 ? 0.1471 0.1705 0.2237 -0.0204 -0.0108 0.0098  140 LEU   A C   
3160 O O   A LEU   A 140 ? 0.1220 0.1650 0.2288 -0.0089 -0.0068 0.0342  140 LEU   A O   
3161 O O   B LEU   A 140 ? 0.1522 0.1701 0.2455 -0.0202 -0.0140 0.0049  140 LEU   A O   
3162 C CB  A LEU   A 140 ? 0.1282 0.1618 0.2399 -0.0148 0.0027  0.0311  140 LEU   A CB  
3163 C CB  B LEU   A 140 ? 0.1514 0.1623 0.2169 -0.0213 0.0009  0.0148  140 LEU   A CB  
3164 C CG  A LEU   A 140 ? 0.1320 0.1669 0.2564 -0.0140 0.0053  0.0499  140 LEU   A CG  
3165 C CG  B LEU   A 140 ? 0.1532 0.1622 0.2123 -0.0234 0.0147  0.0332  140 LEU   A CG  
3166 C CD1 A LEU   A 140 ? 0.1298 0.1379 0.2453 -0.0099 -0.0099 0.0647  140 LEU   A CD1 
3167 C CD1 B LEU   A 140 ? 0.1569 0.1567 0.2144 -0.0305 0.0244  0.0318  140 LEU   A CD1 
3168 C CD2 A LEU   A 140 ? 0.1386 0.1832 0.2735 -0.0118 -0.0003 0.0411  140 LEU   A CD2 
3169 C CD2 B LEU   A 140 ? 0.1480 0.1630 0.2059 -0.0187 0.0177  0.0525  140 LEU   A CD2 
3192 N N   A ARG   A 141 ? 0.1312 0.1749 0.1970 -0.0149 0.0001  0.0341  141 ARG   A N   
3193 N N   B ARG   A 141 ? 0.1559 0.1744 0.2227 -0.0174 -0.0160 0.0020  141 ARG   A N   
3194 C CA  A ARG   A 141 ? 0.1435 0.1859 0.2077 -0.0264 -0.0079 0.0198  141 ARG   A CA  
3195 C CA  B ARG   A 141 ? 0.1777 0.1840 0.2388 -0.0112 -0.0113 -0.0081 141 ARG   A CA  
3196 C C   A ARG   A 141 ? 0.1432 0.1672 0.1915 -0.0254 -0.0173 0.0125  141 ARG   A C   
3197 C C   B ARG   A 141 ? 0.1678 0.1759 0.2339 -0.0072 -0.0043 -0.0104 141 ARG   A C   
3198 O O   A ARG   A 141 ? 0.1382 0.1590 0.1790 -0.0279 -0.0150 0.0068  141 ARG   A O   
3199 O O   B ARG   A 141 ? 0.1531 0.1711 0.2093 -0.0058 -0.0061 -0.0288 141 ARG   A O   
3200 C CB  A ARG   A 141 ? 0.1606 0.2081 0.2110 -0.0397 0.0013  0.0181  141 ARG   A CB  
3201 C CB  B ARG   A 141 ? 0.2091 0.1980 0.2528 -0.0085 -0.0141 -0.0160 141 ARG   A CB  
3202 C CG  A ARG   A 141 ? 0.1826 0.2342 0.2258 -0.0550 0.0147  0.0261  141 ARG   A CG  
3203 C CG  B ARG   A 141 ? 0.2375 0.2086 0.2632 -0.0126 -0.0112 -0.0129 141 ARG   A CG  
3204 C CD  A ARG   A 141 ? 0.2205 0.2642 0.2564 -0.0574 -0.0002 0.0195  141 ARG   A CD  
3205 C CD  B ARG   A 141 ? 0.2552 0.2174 0.2772 -0.0188 -0.0101 0.0042  141 ARG   A CD  
3206 N NE  A ARG   A 141 ? 0.2241 0.2937 0.2789 -0.0569 -0.0106 0.0287  141 ARG   A NE  
3207 N NE  B ARG   A 141 ? 0.2554 0.2148 0.2893 -0.0189 -0.0147 0.0399  141 ARG   A NE  
3208 C CZ  A ARG   A 141 ? 0.2190 0.3035 0.2713 -0.0707 -0.0293 0.0436  141 ARG   A CZ  
3209 C CZ  B ARG   A 141 ? 0.2696 0.2382 0.2877 -0.0085 -0.0286 0.0493  141 ARG   A CZ  
3210 N NH1 A ARG   A 141 ? 0.2027 0.3076 0.2511 -0.0838 -0.0179 0.0376  141 ARG   A NH1 
3211 N NH1 B ARG   A 141 ? 0.2703 0.2473 0.2876 -0.0075 -0.0407 0.0499  141 ARG   A NH1 
3212 N NH2 A ARG   A 141 ? 0.2234 0.3042 0.2907 -0.0663 -0.0432 0.0463  141 ARG   A NH2 
3213 N NH2 B ARG   A 141 ? 0.2764 0.2468 0.2979 -0.0068 -0.0415 0.0507  141 ARG   A NH2 
3240 N N   A VAL   A 142 ? 0.1381 0.1576 0.2173 -0.0220 -0.0036 0.0087  142 VAL   A N   
3241 N N   B VAL   A 142 ? 0.1577 0.1702 0.2512 -0.0070 0.0050  -0.0007 142 VAL   A N   
3242 C CA  A VAL   A 142 ? 0.1432 0.1555 0.2292 -0.0180 0.0122  0.0014  142 VAL   A CA  
3243 C CA  B VAL   A 142 ? 0.1537 0.1623 0.2412 -0.0040 0.0137  -0.0023 142 VAL   A CA  
3244 C C   A VAL   A 142 ? 0.1300 0.1503 0.2347 -0.0157 0.0046  0.0043  142 VAL   A C   
3245 C C   B VAL   A 142 ? 0.1367 0.1551 0.2348 -0.0098 0.0049  0.0030  142 VAL   A C   
3246 O O   A VAL   A 142 ? 0.1343 0.1532 0.2600 -0.0055 0.0130  0.0124  142 VAL   A O   
3247 O O   B VAL   A 142 ? 0.1389 0.1584 0.2497 -0.0060 0.0088  0.0092  142 VAL   A O   
3248 C CB  A VAL   A 142 ? 0.1452 0.1605 0.2452 -0.0203 0.0109  0.0096  142 VAL   A CB  
3249 C CB  B VAL   A 142 ? 0.1574 0.1657 0.2473 0.0014  0.0154  0.0093  142 VAL   A CB  
3250 C CG1 A VAL   A 142 ? 0.1437 0.1541 0.2477 -0.0237 0.0200  0.0183  142 VAL   A CG1 
3251 C CG1 B VAL   A 142 ? 0.1593 0.1652 0.2492 0.0018  0.0155  0.0145  142 VAL   A CG1 
3252 C CG2 A VAL   A 142 ? 0.1581 0.1689 0.2523 -0.0184 0.0204  0.0044  142 VAL   A CG2 
3253 C CG2 B VAL   A 142 ? 0.1643 0.1706 0.2432 0.0129  0.0283  0.0140  142 VAL   A CG2 
3272 N N   . CYS   A 143 ? 0.1368 0.1485 0.2334 -0.0153 0.0047  0.0056  143 CYS   A N   
3273 C CA  . CYS   A 143 ? 0.1350 0.1536 0.2508 -0.0119 -0.0008 0.0207  143 CYS   A CA  
3274 C C   . CYS   A 143 ? 0.1353 0.1552 0.2609 -0.0121 -0.0021 0.0337  143 CYS   A C   
3275 O O   . CYS   A 143 ? 0.1339 0.1571 0.2532 -0.0086 -0.0010 0.0334  143 CYS   A O   
3276 C CB  . CYS   A 143 ? 0.1449 0.1559 0.2548 -0.0058 0.0210  0.0354  143 CYS   A CB  
3277 S SG  . CYS   A 143 ? 0.1648 0.1680 0.2380 0.0034  0.0094  0.0216  143 CYS   A SG  
3284 N N   . VAL   A 144 ? 0.1331 0.1587 0.2765 -0.0123 -0.0037 0.0386  144 VAL   A N   
3285 C CA  . VAL   A 144 ? 0.1421 0.1670 0.3101 -0.0131 0.0129  0.0453  144 VAL   A CA  
3286 C C   . VAL   A 144 ? 0.1455 0.1531 0.3095 -0.0220 -0.0131 0.0343  144 VAL   A C   
3287 O O   . VAL   A 144 ? 0.1663 0.1614 0.3102 -0.0133 -0.0110 0.0422  144 VAL   A O   
3288 C CB  . VAL   A 144 ? 0.1672 0.1973 0.3633 -0.0038 0.0266  0.0537  144 VAL   A CB  
3289 C CG1 . VAL   A 144 ? 0.1885 0.2189 0.3950 -0.0143 0.0082  0.0481  144 VAL   A CG1 
3290 C CG2 . VAL   A 144 ? 0.1543 0.2085 0.3570 -0.0029 0.0228  0.0814  144 VAL   A CG2 
3300 N N   . ASP   A 145 ? 0.1530 0.1450 0.3178 -0.0156 -0.0016 0.0195  145 ASP   A N   
3301 C CA  . ASP   A 145 ? 0.1669 0.1553 0.3252 -0.0191 -0.0091 0.0133  145 ASP   A CA  
3302 C C   . ASP   A 145 ? 0.1659 0.1516 0.3244 -0.0092 -0.0061 0.0063  145 ASP   A C   
3303 O O   . ASP   A 145 ? 0.1782 0.1598 0.3553 -0.0143 -0.0108 -0.0240 145 ASP   A O   
3304 C CB  . ASP   A 145 ? 0.1870 0.1857 0.3470 -0.0306 -0.0266 0.0162  145 ASP   A CB  
3305 C CG  . ASP   A 145 ? 0.2119 0.2250 0.3752 -0.0454 -0.0396 0.0245  145 ASP   A CG  
3306 O OD1 . ASP   A 145 ? 0.2086 0.2405 0.3937 -0.0626 -0.0319 0.0284  145 ASP   A OD1 
3307 O OD2 . ASP   A 145 ? 0.2276 0.2443 0.3816 -0.0564 -0.0566 0.0137  145 ASP   A OD2 
3312 N N   . THR   A 146 ? 0.1446 0.1452 0.2746 -0.0147 -0.0017 0.0143  146 THR   A N   
3313 C CA  . THR   A 146 ? 0.1440 0.1442 0.2695 -0.0090 0.0012  0.0071  146 THR   A CA  
3314 C C   . THR   A 146 ? 0.1385 0.1434 0.2702 -0.0048 0.0089  0.0220  146 THR   A C   
3315 O O   . THR   A 146 ? 0.1509 0.1551 0.2815 0.0042  -0.0019 0.0200  146 THR   A O   
3316 C CB  . THR   A 146 ? 0.1341 0.1458 0.2716 -0.0045 0.0013  0.0125  146 THR   A CB  
3317 O OG1 . THR   A 146 ? 0.1432 0.1640 0.2788 -0.0057 0.0045  0.0094  146 THR   A OG1 
3318 C CG2 . THR   A 146 ? 0.1316 0.1505 0.3044 -0.0046 -0.0037 0.0090  146 THR   A CG2 
3326 N N   . VAL   A 147 ? 0.1387 0.1471 0.2648 -0.0005 0.0115  0.0253  147 VAL   A N   
3327 C CA  . VAL   A 147 ? 0.1359 0.1514 0.2720 -0.0130 0.0342  0.0370  147 VAL   A CA  
3328 C C   . VAL   A 147 ? 0.1360 0.1471 0.2797 -0.0114 0.0162  0.0467  147 VAL   A C   
3329 O O   . VAL   A 147 ? 0.1392 0.1537 0.2861 -0.0180 0.0039  0.0425  147 VAL   A O   
3330 C CB  . VAL   A 147 ? 0.1451 0.1508 0.2623 -0.0197 0.0236  0.0245  147 VAL   A CB  
3331 C CG1 . VAL   A 147 ? 0.1796 0.1539 0.2666 -0.0120 0.0147  0.0337  147 VAL   A CG1 
3332 C CG2 . VAL   A 147 ? 0.1491 0.1544 0.2722 -0.0149 0.0205  0.0163  147 VAL   A CG2 
3342 N N   . ARG   A 148 ? 0.1335 0.1488 0.2856 -0.0116 0.0183  0.0601  148 ARG   A N   
3343 C CA  . ARG   A 148 ? 0.1389 0.1547 0.2790 -0.0133 0.0126  0.0649  148 ARG   A CA  
3344 C C   . ARG   A 148 ? 0.1567 0.1541 0.2881 -0.0160 0.0116  0.0756  148 ARG   A C   
3345 O O   . ARG   A 148 ? 0.1863 0.1694 0.2985 -0.0221 0.0276  0.0655  148 ARG   A O   
3346 C CB  . ARG   A 148 ? 0.1520 0.1596 0.3059 -0.0025 0.0285  0.0571  148 ARG   A CB  
3347 C CG  . ARG   A 148 ? 0.1724 0.1579 0.3376 -0.0027 0.0422  0.0523  148 ARG   A CG  
3348 C CD  . ARG   A 148 ? 0.1867 0.1513 0.3538 -0.0050 0.0492  0.0717  148 ARG   A CD  
3349 N NE  . ARG   A 148 ? 0.1866 0.1555 0.3583 0.0103  0.0554  0.0753  148 ARG   A NE  
3350 C CZ  . ARG   A 148 ? 0.1820 0.1478 0.3332 0.0070  0.0501  0.0652  148 ARG   A CZ  
3351 N NH1 . ARG   A 148 ? 0.1877 0.1445 0.3480 -0.0054 0.0515  0.0360  148 ARG   A NH1 
3352 N NH2 . ARG   A 148 ? 0.1686 0.1695 0.3415 0.0163  0.0514  0.0598  148 ARG   A NH2 
3366 N N   . THR   A 149 ? 0.1570 0.1672 0.2883 -0.0156 -0.0018 0.0690  149 THR   A N   
3367 C CA  . THR   A 149 ? 0.1591 0.1749 0.2857 -0.0129 -0.0051 0.0634  149 THR   A CA  
3368 C C   . THR   A 149 ? 0.1544 0.1740 0.2783 -0.0189 0.0063  0.0702  149 THR   A C   
3369 O O   . THR   A 149 ? 0.1545 0.1784 0.2800 -0.0189 0.0131  0.0661  149 THR   A O   
3370 C CB  . THR   A 149 ? 0.1498 0.1821 0.2841 -0.0231 0.0002  0.0539  149 THR   A CB  
3371 O OG1 . THR   A 149 ? 0.1548 0.1651 0.2862 -0.0211 0.0058  0.0584  149 THR   A OG1 
3372 C CG2 . THR   A 149 ? 0.1501 0.1842 0.2752 -0.0098 -0.0159 0.0329  149 THR   A CG2 
3380 N N   . ASN   A 150 ? 0.1455 0.1801 0.2713 -0.0148 -0.0105 0.0871  150 ASN   A N   
3381 C CA  . ASN   A 150 ? 0.1624 0.1877 0.2715 -0.0184 -0.0007 0.0754  150 ASN   A CA  
3382 C C   . ASN   A 150 ? 0.1474 0.1762 0.2684 -0.0237 -0.0033 0.0613  150 ASN   A C   
3383 O O   . ASN   A 150 ? 0.1555 0.1865 0.2744 -0.0212 -0.0165 0.0613  150 ASN   A O   
3384 C CB  . ASN   A 150 ? 0.2102 0.2090 0.2964 -0.0237 0.0171  0.0833  150 ASN   A CB  
3385 C CG  . ASN   A 150 ? 0.2706 0.2396 0.3617 -0.0316 0.0055  0.0852  150 ASN   A CG  
3386 O OD1 . ASN   A 150 ? 0.2961 0.2470 0.3674 -0.0398 0.0084  0.1026  150 ASN   A OD1 
3387 N ND2 . ASN   A 150 ? 0.3104 0.2614 0.4024 -0.0235 -0.0032 0.0717  150 ASN   A ND2 
3394 N N   . VAL   A 151 ? 0.1417 0.1595 0.2531 -0.0229 -0.0062 0.0603  151 VAL   A N   
3395 C CA  . VAL   A 151 ? 0.1511 0.1664 0.2439 -0.0188 0.0076  0.0616  151 VAL   A CA  
3396 C C   . VAL   A 151 ? 0.1411 0.1645 0.2487 -0.0295 0.0031  0.0586  151 VAL   A C   
3397 O O   . VAL   A 151 ? 0.1547 0.1697 0.2860 -0.0213 0.0021  0.0504  151 VAL   A O   
3398 C CB  . VAL   A 151 ? 0.1772 0.1884 0.2555 -0.0076 0.0087  0.0569  151 VAL   A CB  
3399 C CG1 . VAL   A 151 ? 0.1722 0.2086 0.2829 -0.0158 0.0037  0.0508  151 VAL   A CG1 
3400 C CG2 . VAL   A 151 ? 0.1935 0.1873 0.2436 -0.0044 0.0150  0.0561  151 VAL   A CG2 
3410 N N   A TYR   A 152 ? 0.1376 0.1646 0.2489 -0.0319 -0.0097 0.0642  152 TYR   A N   
3411 N N   B TYR   A 152 ? 0.1422 0.1744 0.2389 -0.0281 -0.0092 0.0562  152 TYR   A N   
3412 C CA  A TYR   A 152 ? 0.1406 0.1742 0.2243 -0.0256 -0.0059 0.0655  152 TYR   A CA  
3413 C CA  B TYR   A 152 ? 0.1451 0.1881 0.2113 -0.0234 -0.0039 0.0536  152 TYR   A CA  
3414 C C   A TYR   A 152 ? 0.1416 0.1555 0.2058 -0.0228 0.0133  0.0496  152 TYR   A C   
3415 C C   B TYR   A 152 ? 0.1373 0.1824 0.1791 -0.0208 0.0077  0.0444  152 TYR   A C   
3416 O O   A TYR   A 152 ? 0.1471 0.1465 0.2011 -0.0280 0.0242  0.0434  152 TYR   A O   
3417 O O   B TYR   A 152 ? 0.1426 0.1778 0.1759 -0.0143 0.0055  0.0433  152 TYR   A O   
3418 C CB  A TYR   A 152 ? 0.1544 0.1927 0.2234 -0.0268 0.0115  0.0788  152 TYR   A CB  
3419 C CB  B TYR   A 152 ? 0.1611 0.2029 0.2126 -0.0201 0.0070  0.0609  152 TYR   A CB  
3420 C CG  A TYR   A 152 ? 0.1688 0.2119 0.2148 -0.0287 0.0185  0.0868  152 TYR   A CG  
3421 C CG  B TYR   A 152 ? 0.1803 0.2219 0.2135 -0.0190 0.0217  0.0675  152 TYR   A CG  
3422 C CD1 A TYR   A 152 ? 0.1890 0.2327 0.2383 -0.0206 0.0166  0.0845  152 TYR   A CD1 
3423 C CD1 B TYR   A 152 ? 0.1981 0.2369 0.2255 -0.0140 0.0300  0.0739  152 TYR   A CD1 
3424 C CD2 A TYR   A 152 ? 0.1750 0.2167 0.2182 -0.0388 0.0146  0.0729  152 TYR   A CD2 
3425 C CD2 B TYR   A 152 ? 0.1880 0.2285 0.2074 -0.0243 0.0201  0.0606  152 TYR   A CD2 
3426 C CE1 A TYR   A 152 ? 0.2150 0.2466 0.2462 -0.0157 0.0065  0.0944  152 TYR   A CE1 
3427 C CE1 B TYR   A 152 ? 0.2229 0.2515 0.2409 -0.0112 0.0201  0.0798  152 TYR   A CE1 
3428 C CE2 A TYR   A 152 ? 0.1986 0.2290 0.2305 -0.0407 0.0183  0.0734  152 TYR   A CE2 
3429 C CE2 B TYR   A 152 ? 0.2122 0.2457 0.2222 -0.0256 0.0269  0.0666  152 TYR   A CE2 
3430 C CZ  A TYR   A 152 ? 0.2241 0.2427 0.2346 -0.0258 0.0075  0.1010  152 TYR   A CZ  
3431 C CZ  B TYR   A 152 ? 0.2329 0.2538 0.2341 -0.0194 0.0243  0.0894  152 TYR   A CZ  
3432 O OH  A TYR   A 152 ? 0.2535 0.2662 0.2625 -0.0156 0.0143  0.1145  152 TYR   A OH  
3433 O OH  B TYR   A 152 ? 0.2599 0.2744 0.2674 -0.0155 0.0302  0.1022  152 TYR   A OH  
3452 N N   A LEU   A 153 ? 0.1423 0.1497 0.2147 -0.0236 0.0121  0.0423  153 LEU   A N   
3453 N N   B LEU   A 153 ? 0.1288 0.1805 0.1899 -0.0296 0.0114  0.0392  153 LEU   A N   
3454 C CA  A LEU   A 153 ? 0.1416 0.1375 0.2300 -0.0091 0.0171  0.0465  153 LEU   A CA  
3455 C CA  B LEU   A 153 ? 0.1253 0.1736 0.1944 -0.0226 0.0064  0.0361  153 LEU   A CA  
3456 C C   A LEU   A 153 ? 0.1445 0.1369 0.2145 -0.0079 0.0291  0.0417  153 LEU   A C   
3457 C C   B LEU   A 153 ? 0.1266 0.1794 0.1912 -0.0118 0.0124  0.0440  153 LEU   A C   
3458 O O   A LEU   A 153 ? 0.1484 0.1523 0.2251 -0.0136 0.0447  0.0364  153 LEU   A O   
3459 O O   B LEU   A 153 ? 0.1325 0.1930 0.1904 -0.0168 0.0120  0.0465  153 LEU   A O   
3460 C CB  A LEU   A 153 ? 0.1369 0.1301 0.2417 -0.0112 0.0131  0.0435  153 LEU   A CB  
3461 C CB  B LEU   A 153 ? 0.1240 0.1737 0.2023 -0.0222 0.0056  0.0387  153 LEU   A CB  
3462 C CG  A LEU   A 153 ? 0.1403 0.1399 0.2225 -0.0112 0.0143  0.0336  153 LEU   A CG  
3463 C CG  B LEU   A 153 ? 0.1378 0.1837 0.1945 -0.0163 0.0051  0.0403  153 LEU   A CG  
3464 C CD1 A LEU   A 153 ? 0.1528 0.1349 0.2195 -0.0118 0.0022  0.0274  153 LEU   A CD1 
3465 C CD1 B LEU   A 153 ? 0.1551 0.1875 0.1961 -0.0099 0.0069  0.0487  153 LEU   A CD1 
3466 C CD2 A LEU   A 153 ? 0.1299 0.1406 0.2009 -0.0068 0.0098  -0.0003 153 LEU   A CD2 
3467 C CD2 B LEU   A 153 ? 0.1328 0.1854 0.1850 -0.0161 -0.0097 0.0308  153 LEU   A CD2 
3490 N N   A ALA   A 154 ? 0.1457 0.1332 0.2254 -0.0050 0.0356  0.0475  154 ALA   A N   
3491 N N   B ALA   A 154 ? 0.1256 0.1759 0.1967 -0.0084 0.0292  0.0411  154 ALA   A N   
3492 C CA  A ALA   A 154 ? 0.1614 0.1386 0.2284 0.0018  0.0380  0.0468  154 ALA   A CA  
3493 C CA  B ALA   A 154 ? 0.1335 0.1695 0.1994 -0.0045 0.0369  0.0453  154 ALA   A CA  
3494 C C   A ALA   A 154 ? 0.1556 0.1400 0.2255 0.0110  0.0347  0.0389  154 ALA   A C   
3495 C C   B ALA   A 154 ? 0.1285 0.1557 0.1945 -0.0047 0.0333  0.0450  154 ALA   A C   
3496 O O   A ALA   A 154 ? 0.1546 0.1412 0.2408 0.0037  0.0298  0.0371  154 ALA   A O   
3497 O O   B ALA   A 154 ? 0.1317 0.1550 0.1868 -0.0082 0.0196  0.0457  154 ALA   A O   
3498 C CB  A ALA   A 154 ? 0.1749 0.1452 0.2320 0.0057  0.0341  0.0394  154 ALA   A CB  
3499 C CB  B ALA   A 154 ? 0.1395 0.1788 0.1989 0.0001  0.0457  0.0420  154 ALA   A CB  
3510 N N   A VAL   A 155 ? 0.1472 0.1339 0.1931 0.0293  0.0183  0.0600  155 VAL   A N   
3511 N N   B VAL   A 155 ? 0.1166 0.1391 0.1915 0.0006  0.0377  0.0623  155 VAL   A N   
3512 C CA  A VAL   A 155 ? 0.1579 0.1518 0.2094 0.0355  0.0032  0.0508  155 VAL   A CA  
3513 C CA  B VAL   A 155 ? 0.1376 0.1534 0.2287 -0.0103 0.0457  0.0587  155 VAL   A CA  
3514 C CA  T VAL   A 155 ? 0.1744 0.1787 0.2252 -0.0162 0.0152  0.0439  155 VAL   A CA  
3515 C C   A VAL   A 155 ? 0.1602 0.1681 0.2249 0.0419  0.0012  0.0422  155 VAL   A C   
3516 C C   B VAL   A 155 ? 0.1479 0.1663 0.2398 -0.0051 0.0469  0.0615  155 VAL   A C   
3517 C C   T VAL   A 155 ? 0.1733 0.1801 0.2251 -0.0073 0.0177  0.0438  155 VAL   A C   
3518 O O   A VAL   A 155 ? 0.1582 0.1754 0.2364 0.0440  -0.0013 0.0360  155 VAL   A O   
3519 O O   B VAL   A 155 ? 0.1439 0.1737 0.2327 0.0012  0.0587  0.0683  155 VAL   A O   
3520 O O   T VAL   A 155 ? 0.1652 0.1854 0.2213 -0.0069 0.0203  0.0370  155 VAL   A O   
3521 C CB  A VAL   A 155 ? 0.1650 0.1512 0.2132 0.0434  -0.0184 0.0473  155 VAL   A CB  
3522 C CB  B VAL   A 155 ? 0.1484 0.1592 0.2531 0.0046  0.0283  0.0405  155 VAL   A CB  
3523 C CB  T VAL   A 155 ? 0.1779 0.1795 0.2289 -0.0142 -0.0037 0.0366  155 VAL   A CB  
3524 C CG1 A VAL   A 155 ? 0.1752 0.1530 0.2156 0.0397  -0.0279 0.0450  155 VAL   A CG1 
3525 C CG1 B VAL   A 155 ? 0.1586 0.1558 0.2554 0.0050  0.0159  0.0473  155 VAL   A CG1 
3526 C CG1 T VAL   A 155 ? 0.1873 0.1809 0.2285 -0.0123 -0.0128 0.0345  155 VAL   A CG1 
3527 C CG2 A VAL   A 155 ? 0.1654 0.1525 0.2186 0.0476  -0.0342 0.0480  155 VAL   A CG2 
3528 C CG2 B VAL   A 155 ? 0.1583 0.1661 0.2700 0.0138  0.0062  0.0353  155 VAL   A CG2 
3529 C CG2 T VAL   A 155 ? 0.1750 0.1804 0.2291 -0.0184 -0.0140 0.0361  155 VAL   A CG2 
3555 N N   A PHE   A 156 ? 0.1655 0.1747 0.2336 0.0455  0.0105  0.0493  156 PHE   A N   
3556 N N   B PHE   A 156 ? 0.1656 0.1694 0.2633 -0.0016 0.0455  0.0711  156 PHE   A N   
3557 N N   T PHE   A 156 ? 0.1842 0.1741 0.2307 0.0014  0.0229  0.0588  156 PHE   A N   
3558 C CA  A PHE   A 156 ? 0.1794 0.1773 0.2490 0.0516  0.0176  0.0489  156 PHE   A CA  
3559 C CA  B PHE   A 156 ? 0.1991 0.1806 0.2713 -0.0012 0.0350  0.0683  156 PHE   A CA  
3560 C CA  T PHE   A 156 ? 0.2051 0.1696 0.2263 0.0066  0.0233  0.0606  156 PHE   A CA  
3561 C C   A PHE   A 156 ? 0.1792 0.1801 0.2460 0.0575  0.0278  0.0409  156 PHE   A C   
3562 C C   B PHE   A 156 ? 0.1976 0.1939 0.2727 0.0038  0.0484  0.0772  156 PHE   A C   
3563 C C   T PHE   A 156 ? 0.2041 0.1837 0.2301 0.0104  0.0365  0.0521  156 PHE   A C   
3564 O O   A PHE   A 156 ? 0.1793 0.1851 0.2544 0.0483  0.0399  0.0277  156 PHE   A O   
3565 O O   B PHE   A 156 ? 0.2029 0.2020 0.2802 0.0003  0.0508  0.0627  156 PHE   A O   
3566 O O   T PHE   A 156 ? 0.2118 0.1903 0.2414 0.0148  0.0392  0.0352  156 PHE   A O   
3567 C CB  A PHE   A 156 ? 0.1911 0.1870 0.2605 0.0477  0.0098  0.0596  156 PHE   A CB  
3568 C CB  B PHE   A 156 ? 0.2239 0.1872 0.2823 -0.0014 0.0139  0.0490  156 PHE   A CB  
3569 C CB  T PHE   A 156 ? 0.2199 0.1539 0.2134 0.0089  0.0107  0.0714  156 PHE   A CB  
3570 C CG  A PHE   A 156 ? 0.2034 0.1929 0.2783 0.0462  0.0059  0.0541  156 PHE   A CG  
3571 C CG  B PHE   A 156 ? 0.2505 0.2077 0.3058 0.0036  -0.0009 0.0316  156 PHE   A CG  
3572 C CG  T PHE   A 156 ? 0.2347 0.1455 0.1972 0.0141  0.0033  0.0884  156 PHE   A CG  
3573 C CD1 A PHE   A 156 ? 0.2054 0.1959 0.2720 0.0469  0.0128  0.0526  156 PHE   A CD1 
3574 C CD1 B PHE   A 156 ? 0.2618 0.2204 0.3172 0.0103  -0.0135 0.0238  156 PHE   A CD1 
3575 C CD1 T PHE   A 156 ? 0.2387 0.1466 0.2058 0.0176  -0.0029 0.0804  156 PHE   A CD1 
3576 C CD2 A PHE   A 156 ? 0.2090 0.2002 0.2879 0.0463  0.0018  0.0482  156 PHE   A CD2 
3577 C CD2 B PHE   A 156 ? 0.2676 0.2228 0.3161 0.0055  -0.0046 0.0295  156 PHE   A CD2 
3578 C CD2 T PHE   A 156 ? 0.2466 0.1465 0.2094 0.0153  0.0055  0.0901  156 PHE   A CD2 
3579 C CE1 A PHE   A 156 ? 0.2065 0.1985 0.2792 0.0470  0.0103  0.0568  156 PHE   A CE1 
3580 C CE1 B PHE   A 156 ? 0.2720 0.2274 0.3298 0.0123  -0.0178 0.0230  156 PHE   A CE1 
3581 C CE1 T PHE   A 156 ? 0.2441 0.1514 0.2205 0.0220  -0.0145 0.0761  156 PHE   A CE1 
3582 C CE2 A PHE   A 156 ? 0.2112 0.2055 0.2924 0.0475  0.0019  0.0480  156 PHE   A CE2 
3583 C CE2 B PHE   A 156 ? 0.2762 0.2311 0.3245 0.0091  -0.0152 0.0269  156 PHE   A CE2 
3584 C CE2 T PHE   A 156 ? 0.2528 0.1487 0.2264 0.0167  -0.0059 0.0737  156 PHE   A CE2 
3585 C CZ  A PHE   A 156 ? 0.2099 0.2055 0.2870 0.0488  0.0060  0.0539  156 PHE   A CZ  
3586 C CZ  B PHE   A 156 ? 0.2756 0.2310 0.3270 0.0076  -0.0183 0.0246  156 PHE   A CZ  
3587 C CZ  T PHE   A 156 ? 0.2496 0.1500 0.2280 0.0159  -0.0138 0.0729  156 PHE   A CZ  
3615 N N   A ASP   A 157 ? 0.1783 0.1778 0.2306 0.0738  0.0216  0.0431  157 ASP   A N   
3616 N N   B ASP   A 157 ? 0.1860 0.2102 0.2733 0.0111  0.0422  0.0952  157 ASP   A N   
3617 N N   T ASP   A 157 ? 0.1922 0.1926 0.2251 0.0145  0.0297  0.0561  157 ASP   A N   
3618 C CA  A ASP   A 157 ? 0.1927 0.1934 0.2311 0.0687  0.0233  0.0588  157 ASP   A CA  
3619 C CA  B ASP   A 157 ? 0.1820 0.2368 0.2634 0.0212  0.0360  0.1036  157 ASP   A CA  
3620 C CA  T ASP   A 157 ? 0.1904 0.2098 0.2194 0.0141  0.0303  0.0637  157 ASP   A CA  
3621 C C   A ASP   A 157 ? 0.1878 0.2074 0.2355 0.0622  0.0222  0.0708  157 ASP   A C   
3622 C C   B ASP   A 157 ? 0.1705 0.2653 0.2576 0.0384  0.0454  0.1000  157 ASP   A C   
3623 C C   T ASP   A 157 ? 0.1884 0.2285 0.2272 0.0189  0.0312  0.0672  157 ASP   A C   
3624 O O   A ASP   A 157 ? 0.1866 0.2079 0.2313 0.0574  0.0150  0.0730  157 ASP   A O   
3625 O O   B ASP   A 157 ? 0.1616 0.2673 0.2546 0.0381  0.0462  0.0974  157 ASP   A O   
3626 O O   T ASP   A 157 ? 0.1863 0.2292 0.2278 0.0176  0.0280  0.0672  157 ASP   A O   
3627 C CB  A ASP   A 157 ? 0.2107 0.1962 0.2401 0.0738  0.0250  0.0491  157 ASP   A CB  
3628 C CB  B ASP   A 157 ? 0.1888 0.2321 0.2827 0.0267  0.0220  0.1085  157 ASP   A CB  
3629 C CB  T ASP   A 157 ? 0.1919 0.2057 0.2151 0.0153  0.0316  0.0566  157 ASP   A CB  
3630 C CG  A ASP   A 157 ? 0.2248 0.2018 0.2658 0.0758  0.0216  0.0485  157 ASP   A CG  
3631 C CG  B ASP   A 157 ? 0.1851 0.2256 0.3157 0.0343  0.0153  0.1000  157 ASP   A CG  
3632 C CG  T ASP   A 157 ? 0.1873 0.1990 0.2210 0.0170  0.0325  0.0478  157 ASP   A CG  
3633 O OD1 A ASP   A 157 ? 0.2332 0.2015 0.2690 0.0789  0.0195  0.0446  157 ASP   A OD1 
3634 O OD1 B ASP   A 157 ? 0.1815 0.2231 0.3517 0.0314  0.0199  0.0987  157 ASP   A OD1 
3635 O OD1 T ASP   A 157 ? 0.1873 0.1977 0.2561 0.0145  0.0264  0.0259  157 ASP   A OD1 
3636 O OD2 A ASP   A 157 ? 0.2238 0.2028 0.2876 0.0725  0.0260  0.0622  157 ASP   A OD2 
3637 O OD2 B ASP   A 157 ? 0.1956 0.2280 0.3236 0.0379  -0.0047 0.0965  157 ASP   A OD2 
3638 O OD2 T ASP   A 157 ? 0.1846 0.1940 0.2110 0.0232  0.0308  0.0584  157 ASP   A OD2 
3651 N N   A LYS   A 158 ? 0.1915 0.2255 0.2488 0.0564  0.0277  0.0756  158 LYS   A N   
3652 N N   B LYS   A 158 ? 0.1825 0.2917 0.2524 0.0451  0.0467  0.1001  158 LYS   A N   
3653 N N   T LYS   A 158 ? 0.1950 0.2456 0.2348 0.0190  0.0380  0.0706  158 LYS   A N   
3654 C CA  A LYS   A 158 ? 0.1930 0.2423 0.2666 0.0520  0.0341  0.0696  158 LYS   A CA  
3655 C CA  B LYS   A 158 ? 0.1961 0.3120 0.2563 0.0474  0.0356  0.1031  158 LYS   A CA  
3656 C CA  T LYS   A 158 ? 0.1988 0.2593 0.2485 0.0187  0.0423  0.0669  158 LYS   A CA  
3657 C C   A LYS   A 158 ? 0.1810 0.2443 0.2639 0.0477  0.0316  0.0657  158 LYS   A C   
3658 C C   B LYS   A 158 ? 0.1783 0.3167 0.2439 0.0547  0.0289  0.1193  158 LYS   A C   
3659 C C   T LYS   A 158 ? 0.1904 0.2495 0.2459 0.0116  0.0393  0.0617  158 LYS   A C   
3660 O O   A LYS   A 158 ? 0.1772 0.2508 0.2714 0.0418  0.0374  0.0649  158 LYS   A O   
3661 O O   B LYS   A 158 ? 0.1694 0.3214 0.2411 0.0475  0.0382  0.1200  158 LYS   A O   
3662 O O   T LYS   A 158 ? 0.1862 0.2475 0.2553 0.0063  0.0402  0.0594  158 LYS   A O   
3663 C CB  A LYS   A 158 ? 0.2077 0.2520 0.2997 0.0481  0.0484  0.0599  158 LYS   A CB  
3664 C CB  B LYS   A 158 ? 0.2234 0.3213 0.2864 0.0390  0.0182  0.0939  158 LYS   A CB  
3665 C CB  T LYS   A 158 ? 0.2125 0.2757 0.2788 0.0224  0.0523  0.0630  158 LYS   A CB  
3666 C CG  A LYS   A 158 ? 0.2222 0.2618 0.3292 0.0463  0.0566  0.0559  158 LYS   A CG  
3667 C CG  B LYS   A 158 ? 0.2541 0.3320 0.3323 0.0299  0.0031  0.0794  158 LYS   A CG  
3668 C CG  T LYS   A 158 ? 0.2263 0.2887 0.3119 0.0288  0.0567  0.0674  158 LYS   A CG  
3669 C CD  A LYS   A 158 ? 0.2313 0.2710 0.3468 0.0444  0.0681  0.0581  158 LYS   A CD  
3670 C CD  B LYS   A 158 ? 0.2724 0.3421 0.3748 0.0230  -0.0155 0.0679  158 LYS   A CD  
3671 C CD  T LYS   A 158 ? 0.2414 0.3019 0.3443 0.0366  0.0571  0.0734  158 LYS   A CD  
3672 C CE  A LYS   A 158 ? 0.2355 0.2734 0.3509 0.0377  0.0777  0.0703  158 LYS   A CE  
3673 C CE  B LYS   A 158 ? 0.2811 0.3475 0.4059 0.0142  -0.0221 0.0638  158 LYS   A CE  
3674 C CE  T LYS   A 158 ? 0.2522 0.3070 0.3702 0.0390  0.0563  0.0768  158 LYS   A CE  
3675 N NZ  A LYS   A 158 ? 0.2349 0.2720 0.3524 0.0297  0.0851  0.0829  158 LYS   A NZ  
3676 N NZ  B LYS   A 158 ? 0.2822 0.3502 0.4227 0.0044  -0.0164 0.0587  158 LYS   A NZ  
3677 N NZ  T LYS   A 158 ? 0.2589 0.3095 0.3835 0.0427  0.0535  0.0748  158 LYS   A NZ  
3717 N N   A ASN   A 159 ? 0.1773 0.2390 0.2588 0.0427  0.0214  0.0586  159 ASN   A N   
3718 N N   B ASN   A 159 ? 0.1769 0.3186 0.2447 0.0630  0.0220  0.1174  159 ASN   A N   
3719 N N   T ASN   A 159 ? 0.1928 0.2457 0.2465 0.0090  0.0323  0.0517  159 ASN   A N   
3720 C CA  A ASN   A 159 ? 0.1724 0.2342 0.2512 0.0324  0.0092  0.0537  159 ASN   A CA  
3721 C CA  B ASN   A 159 ? 0.1821 0.3213 0.2630 0.0598  0.0117  0.1057  159 ASN   A CA  
3722 C CA  T ASN   A 159 ? 0.1985 0.2442 0.2544 0.0044  0.0210  0.0463  159 ASN   A CA  
3723 C C   A ASN   A 159 ? 0.1597 0.2224 0.2293 0.0249  0.0026  0.0496  159 ASN   A C   
3724 C C   B ASN   A 159 ? 0.1751 0.3188 0.2497 0.0416  0.0121  0.0881  159 ASN   A C   
3725 C C   T ASN   A 159 ? 0.2042 0.2409 0.2521 -0.0024 0.0231  0.0370  159 ASN   A C   
3726 O O   A ASN   A 159 ? 0.1410 0.2072 0.2125 0.0270  -0.0243 0.0336  159 ASN   A O   
3727 O O   B ASN   A 159 ? 0.1676 0.3285 0.2564 0.0351  0.0080  0.0677  159 ASN   A O   
3728 O O   T ASN   A 159 ? 0.1987 0.2283 0.2476 -0.0096 0.0136  0.0126  159 ASN   A O   
3729 C CB  A ASN   A 159 ? 0.1834 0.2426 0.2721 0.0258  0.0056  0.0594  159 ASN   A CB  
3730 C CB  B ASN   A 159 ? 0.1976 0.3234 0.3001 0.0669  0.0157  0.1164  159 ASN   A CB  
3731 C CB  T ASN   A 159 ? 0.2024 0.2490 0.2735 0.0048  0.0132  0.0568  159 ASN   A CB  
3732 C CG  A ASN   A 159 ? 0.1949 0.2500 0.2998 0.0213  0.0161  0.0620  159 ASN   A CG  
3733 C CG  B ASN   A 159 ? 0.2161 0.3249 0.3416 0.0626  0.0290  0.1128  159 ASN   A CG  
3734 C CG  T ASN   A 159 ? 0.2087 0.2535 0.2976 0.0057  0.0217  0.0663  159 ASN   A CG  
3735 O OD1 A ASN   A 159 ? 0.1955 0.2603 0.3165 0.0219  0.0279  0.0704  159 ASN   A OD1 
3736 O OD1 B ASN   A 159 ? 0.2238 0.3315 0.3668 0.0640  0.0453  0.1064  159 ASN   A OD1 
3737 O OD1 T ASN   A 159 ? 0.2063 0.2643 0.3177 0.0079  0.0353  0.0743  159 ASN   A OD1 
3738 N ND2 A ASN   A 159 ? 0.2006 0.2493 0.3023 0.0199  0.0133  0.0576  159 ASN   A ND2 
3739 N ND2 B ASN   A 159 ? 0.2252 0.3254 0.3526 0.0570  0.0235  0.1120  159 ASN   A ND2 
3740 N ND2 T ASN   A 159 ? 0.2138 0.2518 0.2941 0.0070  0.0154  0.0663  159 ASN   A ND2 
3759 N N   A LEU   A 160 ? 0.1607 0.2171 0.2257 0.0238  0.0170  0.0552  160 LEU   A N   
3760 N N   B LEU   A 160 ? 0.1651 0.2975 0.2326 0.0314  0.0107  0.0988  160 LEU   A N   
3761 N N   T LEU   A 160 ? 0.2110 0.2444 0.2612 0.0017  0.0344  0.0446  160 LEU   A N   
3762 C CA  A LEU   A 160 ? 0.1623 0.2105 0.2104 0.0169  0.0266  0.0573  160 LEU   A CA  
3763 C CA  B LEU   A 160 ? 0.1579 0.2772 0.2256 0.0191  0.0167  0.0919  160 LEU   A CA  
3764 C CA  T LEU   A 160 ? 0.2187 0.2437 0.2581 0.0014  0.0423  0.0511  160 LEU   A CA  
3765 C C   A LEU   A 160 ? 0.1458 0.1984 0.1859 0.0059  0.0281  0.0672  160 LEU   A C   
3766 C C   B LEU   A 160 ? 0.1324 0.2635 0.2213 0.0149  0.0124  0.0759  160 LEU   A C   
3767 O O   A LEU   A 160 ? 0.1274 0.1941 0.1495 0.0021  0.0335  0.0687  160 LEU   A O   
3768 O O   B LEU   A 160 ? 0.1228 0.2608 0.2342 0.0143  0.0190  0.0736  160 LEU   A O   
3769 C CB  A LEU   A 160 ? 0.1726 0.2170 0.2286 0.0202  0.0320  0.0506  160 LEU   A CB  
3770 C CB  B LEU   A 160 ? 0.1688 0.2704 0.2172 0.0115  0.0227  0.0906  160 LEU   A CB  
3771 C CB  T LEU   A 160 ? 0.2226 0.2457 0.2592 0.0004  0.0464  0.0546  160 LEU   A CB  
3772 C CG  A LEU   A 160 ? 0.1816 0.2215 0.2534 0.0236  0.0326  0.0394  160 LEU   A CG  
3773 C CG  B LEU   A 160 ? 0.1820 0.2736 0.2470 0.0007  0.0257  0.0810  160 LEU   A CG  
3774 C CG  T LEU   A 160 ? 0.2273 0.2493 0.2729 -0.0011 0.0455  0.0498  160 LEU   A CG  
3775 C CD1 A LEU   A 160 ? 0.1878 0.2239 0.2611 0.0282  0.0370  0.0279  160 LEU   A CD1 
3776 C CD1 B LEU   A 160 ? 0.1887 0.2797 0.2527 0.0040  0.0332  0.0801  160 LEU   A CD1 
3777 C CD1 T LEU   A 160 ? 0.2329 0.2526 0.2795 0.0033  0.0461  0.0410  160 LEU   A CD1 
3778 C CD2 A LEU   A 160 ? 0.1838 0.2229 0.2543 0.0246  0.0349  0.0331  160 LEU   A CD2 
3779 C CD2 B LEU   A 160 ? 0.1938 0.2741 0.2575 -0.0098 0.0276  0.0813  160 LEU   A CD2 
3780 C CD2 T LEU   A 160 ? 0.2269 0.2502 0.2706 -0.0039 0.0499  0.0494  160 LEU   A CD2 
3813 N N   A TYR   A 161 ? 0.1621 0.1969 0.2249 0.0020  0.0231  0.0730  161 TYR   A N   
3814 N N   B TYR   A 161 ? 0.1397 0.2522 0.2081 0.0118  0.0186  0.0603  161 TYR   A N   
3815 C CA  A TYR   A 161 ? 0.1573 0.2164 0.2211 -0.0100 0.0231  0.0543  161 TYR   A CA  
3816 C CA  B TYR   A 161 ? 0.1450 0.2485 0.1922 -0.0026 0.0229  0.0682  161 TYR   A CA  
3817 C C   A TYR   A 161 ? 0.1616 0.2497 0.2389 -0.0246 0.0113  0.0565  161 TYR   A C   
3818 C C   B TYR   A 161 ? 0.1466 0.2681 0.2065 -0.0129 0.0115  0.0668  161 TYR   A C   
3819 O O   A TYR   A 161 ? 0.1572 0.2539 0.2233 -0.0251 0.0137  0.0577  161 TYR   A O   
3820 O O   B TYR   A 161 ? 0.1403 0.2664 0.1879 -0.0220 0.0017  0.0667  161 TYR   A O   
3821 C CB  A TYR   A 161 ? 0.1669 0.2144 0.2274 -0.0033 0.0329  0.0413  161 TYR   A CB  
3822 C CB  B TYR   A 161 ? 0.1566 0.2361 0.1958 -0.0056 0.0267  0.0656  161 TYR   A CB  
3823 C CG  A TYR   A 161 ? 0.1581 0.2062 0.2380 0.0023  0.0231  0.0418  161 TYR   A CG  
3824 C CG  B TYR   A 161 ? 0.1533 0.2233 0.1956 -0.0066 0.0255  0.0672  161 TYR   A CG  
3825 C CD1 A TYR   A 161 ? 0.1513 0.1903 0.2397 0.0022  0.0153  0.0412  161 TYR   A CD1 
3826 C CD1 B TYR   A 161 ? 0.1495 0.2149 0.2154 -0.0095 0.0092  0.0580  161 TYR   A CD1 
3827 C CD2 A TYR   A 161 ? 0.1558 0.2133 0.2608 0.0117  0.0185  0.0455  161 TYR   A CD2 
3828 C CD2 B TYR   A 161 ? 0.1504 0.2239 0.2193 0.0011  0.0214  0.0652  161 TYR   A CD2 
3829 C CE1 A TYR   A 161 ? 0.1511 0.1888 0.2381 0.0021  -0.0046 0.0447  161 TYR   A CE1 
3830 C CE1 B TYR   A 161 ? 0.1474 0.2101 0.2018 -0.0056 -0.0057 0.0637  161 TYR   A CE1 
3831 C CE2 A TYR   A 161 ? 0.1570 0.2072 0.2637 0.0052  0.0080  0.0547  161 TYR   A CE2 
3832 C CE2 B TYR   A 161 ? 0.1475 0.2180 0.2136 -0.0060 0.0114  0.0748  161 TYR   A CE2 
3833 C CZ  A TYR   A 161 ? 0.1619 0.1946 0.2459 0.0034  -0.0013 0.0562  161 TYR   A CZ  
3834 C CZ  B TYR   A 161 ? 0.1566 0.2127 0.2029 -0.0076 0.0010  0.0733  161 TYR   A CZ  
3835 O OH  A TYR   A 161 ? 0.1774 0.1901 0.2729 0.0036  -0.0112 0.0655  161 TYR   A OH  
3836 O OH  B TYR   A 161 ? 0.1789 0.2143 0.2268 -0.0122 0.0077  0.0726  161 TYR   A OH  
3855 N N   A ASP   A 162 ? 0.1556 0.2785 0.2496 -0.0222 0.0215  0.0602  162 ASP   A N   
3856 N N   B ASP   A 162 ? 0.1410 0.2879 0.2246 -0.0098 0.0215  0.0682  162 ASP   A N   
3857 C CA  A ASP   A 162 ? 0.1536 0.3056 0.2271 -0.0124 0.0272  0.0573  162 ASP   A CA  
3858 C CA  B ASP   A 162 ? 0.1454 0.3116 0.2380 -0.0061 0.0195  0.0674  162 ASP   A CA  
3859 C C   A ASP   A 162 ? 0.1426 0.3100 0.2115 -0.0133 0.0278  0.0457  162 ASP   A C   
3860 C C   B ASP   A 162 ? 0.1443 0.3165 0.2251 -0.0136 0.0118  0.0676  162 ASP   A C   
3861 O O   A ASP   A 162 ? 0.1522 0.3122 0.2178 -0.0053 0.0191  0.0360  162 ASP   A O   
3862 O O   B ASP   A 162 ? 0.1449 0.3200 0.2162 -0.0121 -0.0163 0.0718  162 ASP   A O   
3863 C CB  A ASP   A 162 ? 0.1647 0.3233 0.2180 -0.0064 0.0426  0.0605  162 ASP   A CB  
3864 C CB  B ASP   A 162 ? 0.1539 0.3265 0.2546 0.0082  0.0278  0.0789  162 ASP   A CB  
3865 C CG  A ASP   A 162 ? 0.1858 0.3438 0.2333 -0.0029 0.0462  0.0687  162 ASP   A CG  
3866 C CG  B ASP   A 162 ? 0.1656 0.3378 0.2684 0.0147  0.0228  0.0986  162 ASP   A CG  
3867 O OD1 A ASP   A 162 ? 0.1950 0.3554 0.2384 -0.0035 0.0393  0.0701  162 ASP   A OD1 
3868 O OD1 B ASP   A 162 ? 0.1650 0.3386 0.2759 0.0111  0.0220  0.1138  162 ASP   A OD1 
3869 O OD2 A ASP   A 162 ? 0.1971 0.3500 0.2503 0.0051  0.0485  0.0746  162 ASP   A OD2 
3870 O OD2 B ASP   A 162 ? 0.1746 0.3464 0.2792 0.0249  0.0364  0.1024  162 ASP   A OD2 
3879 N N   A LYS   A 163 ? 0.1532 0.3222 0.2126 -0.0060 0.0240  0.0344  163 LYS   A N   
3880 N N   B LYS   A 163 ? 0.1597 0.3237 0.2318 -0.0093 0.0109  0.0604  163 LYS   A N   
3881 C CA  A LYS   A 163 ? 0.1589 0.3260 0.2296 -0.0114 0.0089  0.0327  163 LYS   A CA  
3882 C CA  B LYS   A 163 ? 0.1719 0.3218 0.2402 -0.0156 0.0108  0.0466  163 LYS   A CA  
3883 C C   A LYS   A 163 ? 0.1603 0.3064 0.2161 -0.0100 0.0123  0.0395  163 LYS   A C   
3884 C C   B LYS   A 163 ? 0.1746 0.3063 0.2014 -0.0279 0.0068  0.0378  163 LYS   A C   
3885 O O   A LYS   A 163 ? 0.1509 0.3044 0.2129 -0.0121 -0.0028 0.0352  163 LYS   A O   
3886 O O   B LYS   A 163 ? 0.1803 0.3167 0.1936 -0.0350 0.0041  0.0486  163 LYS   A O   
3887 C CB  A LYS   A 163 ? 0.1877 0.3490 0.2703 0.0027  0.0043  0.0317  163 LYS   A CB  
3888 C CB  B LYS   A 163 ? 0.1987 0.3317 0.2893 -0.0068 0.0209  0.0574  163 LYS   A CB  
3889 C CG  A LYS   A 163 ? 0.2127 0.3687 0.3306 0.0027  -0.0004 0.0319  163 LYS   A CG  
3890 C CG  B LYS   A 163 ? 0.2288 0.3398 0.3376 -0.0126 0.0300  0.0705  163 LYS   A CG  
3891 C CD  A LYS   A 163 ? 0.2446 0.3876 0.3881 0.0020  -0.0029 0.0346  163 LYS   A CD  
3892 C CD  B LYS   A 163 ? 0.2504 0.3482 0.3815 -0.0178 0.0414  0.0731  163 LYS   A CD  
3893 C CE  A LYS   A 163 ? 0.2587 0.4000 0.4367 -0.0051 0.0027  0.0329  163 LYS   A CE  
3894 C CE  B LYS   A 163 ? 0.2683 0.3568 0.4196 -0.0216 0.0431  0.0713  163 LYS   A CE  
3895 N NZ  A LYS   A 163 ? 0.2695 0.4087 0.4608 -0.0133 0.0062  0.0336  163 LYS   A NZ  
3896 N NZ  B LYS   A 163 ? 0.2773 0.3617 0.4485 -0.0232 0.0383  0.0647  163 LYS   A NZ  
3923 N N   A LEU   A 164 ? 0.1493 0.2768 0.2020 -0.0093 0.0088  0.0434  164 LEU   A N   
3924 N N   B LEU   A 164 ? 0.1552 0.2719 0.1723 -0.0380 0.0016  0.0194  164 LEU   A N   
3925 C CA  A LEU   A 164 ? 0.1542 0.2513 0.1619 -0.0213 0.0136  0.0250  164 LEU   A CA  
3926 C CA  B LEU   A 164 ? 0.1592 0.2544 0.1801 -0.0420 0.0032  0.0091  164 LEU   A CA  
3927 C C   A LEU   A 164 ? 0.1645 0.2350 0.1648 -0.0295 0.0063  0.0130  164 LEU   A C   
3928 C C   B LEU   A 164 ? 0.1638 0.2544 0.1919 -0.0403 0.0044  0.0056  164 LEU   A C   
3929 O O   A LEU   A 164 ? 0.1627 0.2265 0.1409 -0.0365 0.0215  0.0079  164 LEU   A O   
3930 O O   B LEU   A 164 ? 0.1649 0.2571 0.2057 -0.0455 0.0105  -0.0190 164 LEU   A O   
3931 C CB  A LEU   A 164 ? 0.1506 0.2396 0.1478 -0.0202 0.0138  0.0178  164 LEU   A CB  
3932 C CB  B LEU   A 164 ? 0.1627 0.2412 0.1771 -0.0372 0.0013  0.0046  164 LEU   A CB  
3933 C CG  A LEU   A 164 ? 0.1619 0.2292 0.1644 -0.0147 0.0174  0.0224  164 LEU   A CG  
3934 C CG  B LEU   A 164 ? 0.1622 0.2314 0.1853 -0.0312 0.0020  0.0067  164 LEU   A CG  
3935 C CD1 A LEU   A 164 ? 0.1495 0.2274 0.1481 -0.0090 0.0304  0.0183  164 LEU   A CD1 
3936 C CD1 B LEU   A 164 ? 0.1560 0.2271 0.1947 -0.0288 0.0061  0.0096  164 LEU   A CD1 
3937 C CD2 A LEU   A 164 ? 0.1761 0.2243 0.1637 -0.0279 0.0049  0.0360  164 LEU   A CD2 
3938 C CD2 B LEU   A 164 ? 0.1715 0.2303 0.1862 -0.0336 0.0068  0.0006  164 LEU   A CD2 
3961 N N   A VAL   A 165 ? 0.1543 0.2310 0.1538 -0.0284 0.0083  0.0264  165 VAL   A N   
3962 N N   B VAL   A 165 ? 0.1620 0.2513 0.1899 -0.0308 0.0108  0.0196  165 VAL   A N   
3963 C CA  A VAL   A 165 ? 0.1583 0.2308 0.1550 -0.0195 0.0263  0.0412  165 VAL   A CA  
3964 C CA  B VAL   A 165 ? 0.1677 0.2533 0.1971 -0.0317 0.0170  0.0237  165 VAL   A CA  
3965 C C   A VAL   A 165 ? 0.1573 0.2285 0.1677 -0.0188 0.0332  0.0330  165 VAL   A C   
3966 C C   B VAL   A 165 ? 0.1756 0.2675 0.2309 -0.0341 0.0029  0.0213  165 VAL   A C   
3967 O O   A VAL   A 165 ? 0.1566 0.2231 0.1960 -0.0180 0.0264  0.0317  165 VAL   A O   
3968 O O   B VAL   A 165 ? 0.1724 0.2656 0.2452 -0.0355 0.0222  0.0190  165 VAL   A O   
3969 C CB  A VAL   A 165 ? 0.1784 0.2342 0.1527 -0.0142 0.0311  0.0356  165 VAL   A CB  
3970 C CB  B VAL   A 165 ? 0.1778 0.2494 0.1920 -0.0294 0.0272  0.0242  165 VAL   A CB  
3971 C CG1 A VAL   A 165 ? 0.1807 0.2429 0.1564 -0.0099 0.0429  0.0263  165 VAL   A CG1 
3972 C CG1 B VAL   A 165 ? 0.1826 0.2492 0.2064 -0.0310 0.0264  0.0230  165 VAL   A CG1 
3973 C CG2 A VAL   A 165 ? 0.1974 0.2365 0.1561 -0.0125 0.0180  0.0449  165 VAL   A CG2 
3974 C CG2 B VAL   A 165 ? 0.1846 0.2537 0.1917 -0.0170 0.0310  0.0188  165 VAL   A CG2 
3993 N N   A SER   A 166 ? 0.1480 0.2394 0.1686 -0.0137 0.0328  0.0142  166 SER   A N   
3994 N N   B SER   A 166 ? 0.1794 0.2783 0.2482 -0.0338 -0.0227 0.0187  166 SER   A N   
3995 C CA  A SER   A 166 ? 0.1548 0.2524 0.1668 -0.0153 0.0232  0.0134  166 SER   A CA  
3996 C CA  B SER   A 166 ? 0.1960 0.2940 0.2748 -0.0324 -0.0337 0.0187  166 SER   A CA  
3997 C C   A SER   A 166 ? 0.1545 0.2703 0.1814 -0.0086 0.0087  -0.0049 166 SER   A C   
3998 C C   B SER   A 166 ? 0.2271 0.3119 0.2942 -0.0323 -0.0391 0.0070  166 SER   A C   
3999 O O   A SER   A 166 ? 0.1627 0.2902 0.2163 -0.0192 0.0061  -0.0206 166 SER   A O   
4000 O O   B SER   A 166 ? 0.2319 0.3182 0.3108 -0.0322 -0.0516 -0.0008 166 SER   A O   
4001 C CB  A SER   A 166 ? 0.1734 0.2564 0.2093 -0.0118 0.0038  0.0191  166 SER   A CB  
4002 C CB  B SER   A 166 ? 0.1876 0.2959 0.2928 -0.0246 -0.0335 0.0296  166 SER   A CB  
4003 O OG  A SER   A 166 ? 0.1934 0.2704 0.2531 -0.0130 0.0042  0.0272  166 SER   A OG  
4004 O OG  B SER   A 166 ? 0.1793 0.2995 0.3151 -0.0156 -0.0299 0.0335  166 SER   A OG  
4015 N N   A SER   A 167 ? 0.1533 0.2702 0.1821 0.0134  0.0051  0.0054  167 SER   A N   
4016 N N   B SER   A 167 ? 0.2479 0.3203 0.2914 -0.0307 -0.0353 0.0008  167 SER   A N   
4017 C CA  A SER   A 167 ? 0.1769 0.2707 0.1724 0.0226  -0.0059 0.0064  167 SER   A CA  
4018 C CA  B SER   A 167 ? 0.2790 0.3296 0.2996 -0.0244 -0.0296 -0.0123 167 SER   A CA  
4019 C C   A SER   A 167 ? 0.1791 0.2711 0.1639 0.0236  0.0366  0.0095  167 SER   A C   
4020 C C   B SER   A 167 ? 0.3031 0.3359 0.3288 -0.0182 -0.0188 -0.0234 167 SER   A C   
4021 O O   A SER   A 167 ? 0.1970 0.2700 0.1789 0.0289  0.0177  0.0171  167 SER   A O   
4022 O O   B SER   A 167 ? 0.3110 0.3372 0.3328 -0.0140 -0.0117 -0.0272 167 SER   A O   
4023 C CB  A SER   A 167 ? 0.1835 0.2752 0.1872 0.0293  -0.0076 0.0212  167 SER   A CB  
4024 C CB  B SER   A 167 ? 0.2837 0.3316 0.2761 -0.0205 -0.0256 -0.0048 167 SER   A CB  
4025 O OG  A SER   A 167 ? 0.1880 0.2839 0.1994 0.0325  0.0001  0.0209  167 SER   A OG  
4026 O OG  B SER   A 167 ? 0.2857 0.3367 0.2630 -0.0162 -0.0214 -0.0026 167 SER   A OG  
4037 N N   A PHE   A 168 ? 0.1621 0.2660 0.1798 0.0299  0.0367  0.0179  168 PHE   A N   
4038 N N   B PHE   A 168 ? 0.3157 0.3401 0.3473 -0.0140 -0.0157 -0.0255 168 PHE   A N   
4039 C CA  A PHE   A 168 ? 0.1552 0.2646 0.1967 0.0258  0.0314  0.0235  168 PHE   A CA  
4040 C CA  B PHE   A 168 ? 0.3267 0.3452 0.3662 -0.0133 -0.0111 -0.0297 168 PHE   A CA  
4041 C C   A PHE   A 168 ? 0.1549 0.2668 0.2000 0.0220  0.0468  0.0284  168 PHE   A C   
4042 C C   B PHE   A 168 ? 0.3460 0.3594 0.4179 -0.0104 -0.0051 -0.0374 168 PHE   A C   
4043 O O   A PHE   A 168 ? 0.1711 0.2740 0.2666 0.0082  0.0624  0.0390  168 PHE   A O   
4044 O O   B PHE   A 168 ? 0.3502 0.3588 0.4378 -0.0083 0.0019  -0.0301 168 PHE   A O   
4045 C CB  A PHE   A 168 ? 0.1510 0.2558 0.1788 0.0162  0.0180  0.0125  168 PHE   A CB  
4046 C CB  B PHE   A 168 ? 0.3195 0.3364 0.3347 -0.0182 -0.0091 -0.0233 168 PHE   A CB  
4047 C CG  A PHE   A 168 ? 0.1463 0.2499 0.1580 0.0038  0.0041  0.0205  168 PHE   A CG  
4048 C CG  B PHE   A 168 ? 0.3108 0.3260 0.3057 -0.0232 -0.0066 -0.0262 168 PHE   A CG  
4049 C CD1 A PHE   A 168 ? 0.1496 0.2441 0.1545 0.0010  -0.0009 0.0344  168 PHE   A CD1 
4050 C CD1 B PHE   A 168 ? 0.3062 0.3238 0.2947 -0.0257 -0.0090 -0.0278 168 PHE   A CD1 
4051 C CD2 A PHE   A 168 ? 0.1399 0.2456 0.1635 -0.0035 0.0170  0.0259  168 PHE   A CD2 
4052 C CD2 B PHE   A 168 ? 0.3049 0.3199 0.2849 -0.0262 -0.0048 -0.0275 168 PHE   A CD2 
4053 C CE1 A PHE   A 168 ? 0.1423 0.2378 0.1518 0.0043  0.0045  0.0493  168 PHE   A CE1 
4054 C CE1 B PHE   A 168 ? 0.3019 0.3203 0.2833 -0.0276 -0.0111 -0.0274 168 PHE   A CE1 
4055 C CE2 A PHE   A 168 ? 0.1456 0.2344 0.1716 -0.0039 0.0181  0.0349  168 PHE   A CE2 
4056 C CE2 B PHE   A 168 ? 0.3017 0.3156 0.2753 -0.0294 -0.0050 -0.0244 168 PHE   A CE2 
4057 C CZ  A PHE   A 168 ? 0.1417 0.2305 0.1738 0.0007  0.0089  0.0370  168 PHE   A CZ  
4058 C CZ  B PHE   A 168 ? 0.3000 0.3187 0.2702 -0.0301 -0.0085 -0.0230 168 PHE   A CZ  
4077 N N   A LEU   A 169 ? 0.1830 0.2609 0.2117 0.0050  0.0434  0.0224  169 LEU   A N   
4078 N N   B LEU   A 169 ? 0.3610 0.3738 0.4394 -0.0053 -0.0003 -0.0513 169 LEU   A N   
4079 C CA  A LEU   A 169 ? 0.2202 0.2646 0.2515 0.0115  0.0231  0.0331  169 LEU   A CA  
4080 C CA  B LEU   A 169 ? 0.3759 0.3866 0.4617 -0.0028 0.0097  -0.0572 169 LEU   A CA  
4081 C C   A LEU   A 169 ? 0.2215 0.2545 0.2634 0.0049  0.0234  0.0453  169 LEU   A C   
4082 C C   B LEU   A 169 ? 0.3813 0.3887 0.4838 -0.0025 0.0183  -0.0585 169 LEU   A C   
4083 O O   A LEU   A 169 ? 0.2263 0.2626 0.2853 0.0090  0.0188  0.0343  169 LEU   A O   
4084 O O   B LEU   A 169 ? 0.3774 0.3888 0.4917 -0.0035 0.0257  -0.0569 169 LEU   A O   
4085 C CB  A LEU   A 169 ? 0.2453 0.2768 0.2708 0.0098  0.0067  0.0276  169 LEU   A CB  
4086 C CB  B LEU   A 169 ? 0.3871 0.3976 0.4549 -0.0020 0.0101  -0.0563 169 LEU   A CB  
4087 C CG  A LEU   A 169 ? 0.2707 0.2872 0.3062 0.0064  0.0016  0.0103  169 LEU   A CG  
4088 C CG  B LEU   A 169 ? 0.3983 0.4043 0.4489 -0.0022 0.0111  -0.0571 169 LEU   A CG  
4089 C CD1 A LEU   A 169 ? 0.2862 0.2861 0.3130 0.0043  -0.0048 0.0030  169 LEU   A CD1 
4090 C CD1 B LEU   A 169 ? 0.4045 0.4065 0.4514 -0.0053 0.0100  -0.0583 169 LEU   A CD1 
4091 C CD2 A LEU   A 169 ? 0.2724 0.2948 0.3087 0.0024  0.0028  0.0073  169 LEU   A CD2 
4092 C CD2 B LEU   A 169 ? 0.3994 0.4062 0.4482 0.0004  0.0119  -0.0598 169 LEU   A CD2 
4093 O OXT A LEU   A 169 ? 0.2192 0.2525 0.2644 -0.0186 0.0290  0.0577  169 LEU   A OXT 
4094 O OXT B LEU   A 169 ? 0.3895 0.3925 0.4921 -0.0003 0.0217  -0.0569 169 LEU   A OXT 
4117 N N   A SER   B 1   ? 0.3731 0.3527 0.3502 -0.0997 -0.0835 0.0354  1   SER   B N   
4118 N N   B SER   B 1   ? 0.3344 0.3187 0.3499 -0.1058 -0.0570 0.0252  1   SER   B N   
4119 C CA  A SER   B 1   ? 0.3681 0.3572 0.3605 -0.1033 -0.0860 0.0335  1   SER   B CA  
4120 C CA  B SER   B 1   ? 0.3274 0.3233 0.3482 -0.1078 -0.0595 0.0249  1   SER   B CA  
4121 C C   A SER   B 1   ? 0.3487 0.3579 0.3613 -0.1013 -0.0878 0.0435  1   SER   B C   
4122 C C   B SER   B 1   ? 0.3073 0.3262 0.3394 -0.1054 -0.0678 0.0422  1   SER   B C   
4123 O O   A SER   B 1   ? 0.3582 0.3584 0.3571 -0.0912 -0.0776 0.0510  1   SER   B O   
4124 O O   B SER   B 1   ? 0.3153 0.3282 0.3362 -0.0953 -0.0526 0.0477  1   SER   B O   
4125 C CB  A SER   B 1   ? 0.3765 0.3563 0.3853 -0.1071 -0.0823 0.0163  1   SER   B CB  
4126 C CB  B SER   B 1   ? 0.3350 0.3187 0.3682 -0.1111 -0.0516 -0.0001 1   SER   B CB  
4127 O OG  A SER   B 1   ? 0.3873 0.3643 0.4166 -0.1062 -0.0660 0.0043  1   SER   B OG  
4128 O OG  B SER   B 1   ? 0.3455 0.3236 0.3926 -0.1104 -0.0429 -0.0191 1   SER   B OG  
4143 N N   A MET   B 2   ? 0.3276 0.3576 0.3699 -0.1054 -0.0809 0.0644  2   MET   B N   
4144 N N   B MET   B 2   ? 0.2880 0.3265 0.3345 -0.1088 -0.0723 0.0763  2   MET   B N   
4145 C CA  A MET   B 2   ? 0.3107 0.3598 0.3851 -0.0926 -0.0767 0.0851  2   MET   B CA  
4146 C CA  B MET   B 2   ? 0.2771 0.3328 0.3366 -0.0910 -0.0802 0.1090  2   MET   B CA  
4147 C C   A MET   B 2   ? 0.2655 0.3367 0.3548 -0.0799 -0.0868 0.1159  2   MET   B C   
4148 C C   B MET   B 2   ? 0.2481 0.3212 0.3276 -0.0772 -0.0910 0.1300  2   MET   B C   
4149 O O   A MET   B 2   ? 0.2656 0.3466 0.3516 -0.0681 -0.1055 0.1174  2   MET   B O   
4150 O O   B MET   B 2   ? 0.2466 0.3271 0.3145 -0.0630 -0.1149 0.1365  2   MET   B O   
4151 C CB  A MET   B 2   ? 0.3422 0.3900 0.4525 -0.0775 -0.0561 0.0677  2   MET   B CB  
4152 C CB  B MET   B 2   ? 0.3001 0.3579 0.3634 -0.0714 -0.0713 0.1115  2   MET   B CB  
4153 C CG  A MET   B 2   ? 0.3689 0.4136 0.5292 -0.0586 -0.0366 0.0553  2   MET   B CG  
4154 C CG  B MET   B 2   ? 0.3199 0.3779 0.3887 -0.0470 -0.0648 0.1191  2   MET   B CG  
4155 S SD  A MET   B 2   ? 0.3920 0.4328 0.5993 -0.0410 -0.0193 0.0440  2   MET   B SD  
4156 S SD  B MET   B 2   ? 0.3375 0.3963 0.4091 -0.0228 -0.0656 0.1259  2   MET   B SD  
4157 C CE  A MET   B 2   ? 0.3883 0.4302 0.6014 -0.0430 -0.0101 0.0389  2   MET   B CE  
4158 C CE  B MET   B 2   ? 0.3342 0.3942 0.4141 -0.0222 -0.0581 0.1180  2   MET   B CE  
4177 N N   . VAL   B 3   ? 0.2292 0.3047 0.3188 -0.0791 -0.0782 0.1438  3   VAL   B N   
4178 C CA  . VAL   B 3   ? 0.2161 0.2669 0.3091 -0.0654 -0.0780 0.1251  3   VAL   B CA  
4179 C C   . VAL   B 3   ? 0.1982 0.2632 0.2801 -0.0568 -0.0732 0.1087  3   VAL   B C   
4180 O O   . VAL   B 3   ? 0.1943 0.2842 0.2864 -0.0667 -0.0628 0.1150  3   VAL   B O   
4181 C CB  . VAL   B 3   ? 0.2315 0.2542 0.3738 -0.0695 -0.0730 0.0984  3   VAL   B CB  
4182 C CG1 . VAL   B 3   ? 0.2394 0.2410 0.3981 -0.0765 -0.0817 0.0910  3   VAL   B CG1 
4183 C CG2 . VAL   B 3   ? 0.2335 0.2542 0.3829 -0.0625 -0.0534 0.1113  3   VAL   B CG2 
4194 N N   . ASN   B 4   ? 0.1909 0.2338 0.2453 -0.0624 -0.0624 0.0864  4   ASN   B N   
4195 C CA  . ASN   B 4   ? 0.1950 0.2334 0.2162 -0.0598 -0.0657 0.0636  4   ASN   B CA  
4196 C C   . ASN   B 4   ? 0.1991 0.2468 0.2177 -0.0590 -0.0544 0.0401  4   ASN   B C   
4197 O O   . ASN   B 4   ? 0.2004 0.2499 0.2261 -0.0611 -0.0404 0.0313  4   ASN   B O   
4198 C CB  . ASN   B 4   ? 0.2020 0.2261 0.1996 -0.0575 -0.0697 0.0608  4   ASN   B CB  
4199 C CG  . ASN   B 4   ? 0.2080 0.2076 0.2112 -0.0574 -0.0667 0.0363  4   ASN   B CG  
4200 O OD1 . ASN   B 4   ? 0.2108 0.1921 0.2135 -0.0591 -0.0594 0.0373  4   ASN   B OD1 
4201 N ND2 . ASN   B 4   ? 0.2294 0.2126 0.1994 -0.0398 -0.0483 0.0284  4   ASN   B ND2 
4208 N N   . SER   B 5   ? 0.2099 0.2665 0.2154 -0.0652 -0.0439 0.0299  5   SER   B N   
4209 C CA  . SER   B 5   ? 0.2442 0.3027 0.2371 -0.0577 -0.0188 0.0397  5   SER   B CA  
4210 C C   . SER   B 5   ? 0.2713 0.3134 0.2727 -0.0773 0.0046  0.0398  5   SER   B C   
4211 O O   . SER   B 5   ? 0.2862 0.3093 0.3580 -0.0660 0.0433  0.0296  5   SER   B O   
4212 C CB  . SER   B 5   ? 0.2603 0.3264 0.2723 -0.0410 0.0008  0.0537  5   SER   B CB  
4213 O OG  . SER   B 5   ? 0.2912 0.3585 0.3331 -0.0252 0.0009  0.0567  5   SER   B OG  
4219 N N   . PHE   B 6   ? 0.2965 0.3346 0.2657 -0.0934 0.0253  0.0445  6   PHE   B N   
4220 C CA  . PHE   B 6   ? 0.3163 0.3395 0.2322 -0.1121 0.0304  0.0236  6   PHE   B CA  
4221 C C   . PHE   B 6   ? 0.3681 0.3685 0.2893 -0.1174 0.0654  -0.0185 6   PHE   B C   
4222 O O   . PHE   B 6   ? 0.3772 0.4026 0.3238 -0.1086 0.0527  -0.0302 6   PHE   B O   
4223 C CB  . PHE   B 6   ? 0.2856 0.3170 0.2217 -0.1017 0.0095  0.0270  6   PHE   B CB  
4224 C CG  . PHE   B 6   ? 0.2408 0.2787 0.2095 -0.0935 -0.0122 0.0304  6   PHE   B CG  
4225 C CD1 . PHE   B 6   ? 0.2339 0.2484 0.1944 -0.0831 -0.0336 0.0252  6   PHE   B CD1 
4226 C CD2 . PHE   B 6   ? 0.2111 0.2755 0.1937 -0.0722 -0.0187 0.0605  6   PHE   B CD2 
4227 C CE1 . PHE   B 6   ? 0.2283 0.2241 0.1860 -0.0674 -0.0336 0.0291  6   PHE   B CE1 
4228 C CE2 . PHE   B 6   ? 0.2122 0.2628 0.2253 -0.0565 -0.0050 0.0542  6   PHE   B CE2 
4229 C CZ  . PHE   B 6   ? 0.2201 0.2360 0.2140 -0.0530 -0.0299 0.0386  6   PHE   B CZ  
4239 N N   A SER   B 7   ? 0.3940 0.3548 0.3013 -0.1291 0.0827  -0.0445 7   SER   B N   
4240 N N   B SER   B 7   ? 0.3896 0.3586 0.3018 -0.1268 0.0807  -0.0406 7   SER   B N   
4241 C CA  A SER   B 7   ? 0.4217 0.3659 0.3449 -0.1268 0.0982  -0.0469 7   SER   B CA  
4242 C CA  B SER   B 7   ? 0.4144 0.3634 0.3388 -0.1267 0.0944  -0.0451 7   SER   B CA  
4243 C C   A SER   B 7   ? 0.4239 0.3574 0.3428 -0.1345 0.1148  -0.0620 7   SER   B C   
4244 C C   B SER   B 7   ? 0.4198 0.3571 0.3419 -0.1335 0.1109  -0.0594 7   SER   B C   
4245 O O   A SER   B 7   ? 0.4337 0.3553 0.3587 -0.1407 0.1265  -0.0659 7   SER   B O   
4246 O O   B SER   B 7   ? 0.4291 0.3553 0.3562 -0.1398 0.1200  -0.0607 7   SER   B O   
4247 C CB  A SER   B 7   ? 0.4389 0.3824 0.3944 -0.1200 0.1045  -0.0397 7   SER   B CB  
4248 C CB  B SER   B 7   ? 0.4288 0.3693 0.3771 -0.1226 0.0992  -0.0381 7   SER   B CB  
4249 O OG  A SER   B 7   ? 0.4513 0.3965 0.4326 -0.1170 0.1035  -0.0428 7   SER   B OG  
4250 O OG  B SER   B 7   ? 0.4393 0.3715 0.4014 -0.1218 0.0996  -0.0386 7   SER   B OG  
4261 N N   . GLY   B 8   ? 0.4192 0.3546 0.3347 -0.1258 0.1162  -0.0693 8   GLY   B N   
4262 C CA  . GLY   B 8   ? 0.4041 0.3399 0.3389 -0.1107 0.1257  -0.0773 8   GLY   B CA  
4263 C C   . GLY   B 8   ? 0.3858 0.3097 0.3271 -0.1068 0.1389  -0.0711 8   GLY   B C   
4264 O O   . GLY   B 8   ? 0.3996 0.3189 0.3619 -0.0949 0.1400  -0.0918 8   GLY   B O   
4269 N N   . TYR   B 9   ? 0.3722 0.2815 0.3111 -0.0975 0.1070  -0.0727 9   TYR   B N   
4270 C CA  . TYR   B 9   ? 0.3519 0.2502 0.2815 -0.0831 0.0809  -0.0696 9   TYR   B CA  
4271 C C   . TYR   B 9   ? 0.3356 0.2480 0.2644 -0.0775 0.0514  -0.0631 9   TYR   B C   
4272 O O   . TYR   B 9   ? 0.3378 0.2611 0.3242 -0.0779 0.0479  -0.0464 9   TYR   B O   
4273 C CB  . TYR   B 9   ? 0.3455 0.2236 0.2854 -0.0817 0.0737  -0.0620 9   TYR   B CB  
4274 C CG  . TYR   B 9   ? 0.3332 0.2048 0.2833 -0.0950 0.0620  -0.0621 9   TYR   B CG  
4275 C CD1 . TYR   B 9   ? 0.3271 0.2119 0.2831 -0.1046 0.0770  -0.0603 9   TYR   B CD1 
4276 C CD2 . TYR   B 9   ? 0.3232 0.2046 0.2680 -0.0916 0.0442  -0.0579 9   TYR   B CD2 
4277 C CE1 . TYR   B 9   ? 0.3207 0.2190 0.2742 -0.1086 0.0819  -0.0712 9   TYR   B CE1 
4278 C CE2 . TYR   B 9   ? 0.3197 0.2082 0.2748 -0.0917 0.0587  -0.0481 9   TYR   B CE2 
4279 C CZ  . TYR   B 9   ? 0.3168 0.2239 0.2727 -0.0982 0.0690  -0.0749 9   TYR   B CZ  
4280 O OH  . TYR   B 9   ? 0.3079 0.2387 0.3021 -0.1020 0.0634  -0.0843 9   TYR   B OH  
4290 N N   . LEU   B 10  ? 0.3195 0.2272 0.2390 -0.0817 0.0325  -0.0527 10  LEU   B N   
4291 C CA  . LEU   B 10  ? 0.3192 0.2247 0.2479 -0.1017 -0.0110 -0.0435 10  LEU   B CA  
4292 C C   . LEU   B 10  ? 0.2962 0.2304 0.2419 -0.0958 -0.0367 -0.0372 10  LEU   B C   
4293 O O   . LEU   B 10  ? 0.2677 0.2371 0.2372 -0.0743 -0.0351 -0.0209 10  LEU   B O   
4294 C CB  . LEU   B 10  ? 0.3454 0.2224 0.2611 -0.1016 -0.0336 -0.0167 10  LEU   B CB  
4295 C CG  . LEU   B 10  ? 0.3628 0.2258 0.2894 -0.0996 -0.0667 -0.0035 10  LEU   B CG  
4296 C CD1 . LEU   B 10  ? 0.3754 0.2333 0.3098 -0.0918 -0.0581 0.0023  10  LEU   B CD1 
4297 C CD2 . LEU   B 10  ? 0.3643 0.2315 0.3058 -0.1016 -0.0577 0.0178  10  LEU   B CD2 
4309 N N   . LYS   B 11  ? 0.3163 0.2550 0.2259 -0.0877 -0.0482 -0.0365 11  LYS   B N   
4310 C CA  . LYS   B 11  ? 0.3321 0.2801 0.2819 -0.0745 -0.0485 -0.0346 11  LYS   B CA  
4311 C C   . LYS   B 11  ? 0.3051 0.2513 0.2958 -0.0882 -0.0525 -0.0475 11  LYS   B C   
4312 O O   . LYS   B 11  ? 0.3271 0.2702 0.3317 -0.0992 -0.0581 -0.0753 11  LYS   B O   
4313 C CB  . LYS   B 11  ? 0.3736 0.3296 0.3537 -0.0520 -0.0380 -0.0381 11  LYS   B CB  
4314 C CG  . LYS   B 11  ? 0.4091 0.3644 0.4444 -0.0385 -0.0439 -0.0468 11  LYS   B CG  
4315 C CD  . LYS   B 11  ? 0.4337 0.3886 0.5140 -0.0289 -0.0455 -0.0585 11  LYS   B CD  
4316 C CE  . LYS   B 11  ? 0.4527 0.4069 0.5661 -0.0201 -0.0358 -0.0613 11  LYS   B CE  
4317 N NZ  . LYS   B 11  ? 0.4631 0.4181 0.5990 -0.0133 -0.0294 -0.0556 11  LYS   B NZ  
4331 N N   . LEU   B 12  ? 0.2608 0.2263 0.2765 -0.0745 -0.0519 -0.0444 12  LEU   B N   
4332 C CA  . LEU   B 12  ? 0.2471 0.1970 0.2961 -0.0596 -0.0359 -0.0329 12  LEU   B CA  
4333 C C   . LEU   B 12  ? 0.2372 0.1985 0.3115 -0.0638 -0.0567 -0.0251 12  LEU   B C   
4334 O O   . LEU   B 12  ? 0.2421 0.1924 0.3419 -0.0723 -0.0721 -0.0230 12  LEU   B O   
4335 C CB  . LEU   B 12  ? 0.2507 0.1719 0.2981 -0.0441 -0.0200 -0.0207 12  LEU   B CB  
4336 C CG  . LEU   B 12  ? 0.2527 0.1651 0.2894 -0.0501 -0.0096 -0.0264 12  LEU   B CG  
4337 C CD1 . LEU   B 12  ? 0.2620 0.1701 0.2845 -0.0342 -0.0039 -0.0109 12  LEU   B CD1 
4338 C CD2 . LEU   B 12  ? 0.2624 0.1792 0.2788 -0.0550 -0.0177 -0.0420 12  LEU   B CD2 
4350 N N   . THR   B 13  ? 0.2325 0.2018 0.3103 -0.0586 -0.0547 -0.0418 13  THR   B N   
4351 C CA  . THR   B 13  ? 0.2348 0.2110 0.3035 -0.0676 -0.0699 -0.0209 13  THR   B CA  
4352 C C   . THR   B 13  ? 0.2830 0.2331 0.3243 -0.0833 -0.0897 -0.0131 13  THR   B C   
4353 O O   . THR   B 13  ? 0.3043 0.2276 0.3486 -0.0823 -0.0578 -0.0138 13  THR   B O   
4354 C CB  . THR   B 13  ? 0.2143 0.2092 0.3144 -0.0594 -0.0608 -0.0076 13  THR   B CB  
4355 O OG1 . THR   B 13  ? 0.2003 0.2005 0.3080 -0.0489 -0.0510 -0.0138 13  THR   B OG1 
4356 C CG2 . THR   B 13  ? 0.2184 0.2151 0.2994 -0.0502 -0.0759 -0.0009 13  THR   B CG2 
4364 N N   A ASP   B 14  ? 0.2976 0.2504 0.3280 -0.0908 -0.1121 -0.0052 14  ASP   B N   
4365 N N   B ASP   B 14  ? 0.2964 0.2484 0.3257 -0.0876 -0.1031 -0.0007 14  ASP   B N   
4366 C CA  A ASP   B 14  ? 0.3092 0.2657 0.3542 -0.0912 -0.1115 0.0140  14  ASP   B CA  
4367 C CA  B ASP   B 14  ? 0.3058 0.2614 0.3451 -0.0863 -0.1007 0.0194  14  ASP   B CA  
4368 C C   A ASP   B 14  ? 0.2964 0.2473 0.3259 -0.0939 -0.1046 0.0153  14  ASP   B C   
4369 C C   B ASP   B 14  ? 0.2927 0.2420 0.3217 -0.0898 -0.1000 0.0216  14  ASP   B C   
4370 O O   A ASP   B 14  ? 0.3228 0.2651 0.3364 -0.0921 -0.0950 0.0225  14  ASP   B O   
4371 O O   B ASP   B 14  ? 0.3150 0.2490 0.3321 -0.0896 -0.0904 0.0348  14  ASP   B O   
4372 C CB  A ASP   B 14  ? 0.3317 0.2994 0.4218 -0.0825 -0.1108 0.0192  14  ASP   B CB  
4373 C CB  B ASP   B 14  ? 0.3264 0.2934 0.4005 -0.0749 -0.0929 0.0271  14  ASP   B CB  
4374 C CG  A ASP   B 14  ? 0.3513 0.3254 0.4840 -0.0744 -0.1087 0.0049  14  ASP   B CG  
4375 C CG  B ASP   B 14  ? 0.3435 0.3193 0.4513 -0.0634 -0.0862 0.0171  14  ASP   B CG  
4376 O OD1 A ASP   B 14  ? 0.3544 0.3319 0.4986 -0.0784 -0.1124 -0.0057 14  ASP   B OD1 
4377 O OD1 B ASP   B 14  ? 0.3452 0.3279 0.4659 -0.0600 -0.0819 0.0095  14  ASP   B OD1 
4378 O OD2 A ASP   B 14  ? 0.3612 0.3378 0.5155 -0.0704 -0.1053 0.0043  14  ASP   B OD2 
4379 O OD2 B ASP   B 14  ? 0.3527 0.3294 0.4775 -0.0624 -0.0867 0.0170  14  ASP   B OD2 
4388 N N   . ASN   B 15  ? 0.2627 0.2203 0.3062 -0.0781 -0.1097 0.0189  15  ASN   B N   
4389 C CA  . ASN   B 15  ? 0.2114 0.1825 0.2857 -0.0514 -0.0866 0.0153  15  ASN   B CA  
4390 C C   . ASN   B 15  ? 0.1908 0.1678 0.2686 -0.0321 -0.0620 0.0083  15  ASN   B C   
4391 O O   . ASN   B 15  ? 0.1912 0.1534 0.2680 -0.0350 -0.0671 -0.0015 15  ASN   B O   
4392 C CB  . ASN   B 15  ? 0.2053 0.1757 0.3035 -0.0283 -0.0838 0.0125  15  ASN   B CB  
4393 C CG  . ASN   B 15  ? 0.1858 0.1703 0.3345 -0.0291 -0.0549 0.0135  15  ASN   B CG  
4394 O OD1 . ASN   B 15  ? 0.1925 0.2006 0.3585 -0.0506 -0.0570 0.0205  15  ASN   B OD1 
4395 N ND2 . ASN   B 15  ? 0.1837 0.1508 0.3014 -0.0196 -0.0228 -0.0033 15  ASN   B ND2 
4403 N N   . VAL   B 16  ? 0.1903 0.1557 0.2600 -0.0369 -0.0648 0.0008  16  VAL   B N   
4404 C CA  . VAL   B 16  ? 0.1937 0.1592 0.2492 -0.0332 -0.0522 -0.0242 16  VAL   B CA  
4405 C C   . VAL   B 16  ? 0.1980 0.1719 0.2391 -0.0374 -0.0437 -0.0151 16  VAL   B C   
4406 O O   . VAL   B 16  ? 0.1951 0.1846 0.2513 -0.0380 -0.0422 -0.0289 16  VAL   B O   
4407 C CB  . VAL   B 16  ? 0.1965 0.1635 0.2707 -0.0196 -0.0339 -0.0186 16  VAL   B CB  
4408 C CG1 . VAL   B 16  ? 0.1978 0.1582 0.2690 -0.0070 -0.0362 -0.0090 16  VAL   B CG1 
4409 C CG2 . VAL   B 16  ? 0.1973 0.1723 0.2830 -0.0114 -0.0212 -0.0199 16  VAL   B CG2 
4419 N N   . TYR   B 17  ? 0.2038 0.1799 0.2427 -0.0393 -0.0379 -0.0148 17  TYR   B N   
4420 C CA  . TYR   B 17  ? 0.2121 0.2008 0.2357 -0.0514 -0.0458 0.0040  17  TYR   B CA  
4421 C C   . TYR   B 17  ? 0.1987 0.1699 0.2371 -0.0529 -0.0322 -0.0114 17  TYR   B C   
4422 O O   . TYR   B 17  ? 0.1909 0.1694 0.2550 -0.0419 -0.0382 -0.0318 17  TYR   B O   
4423 C CB  . TYR   B 17  ? 0.2520 0.2506 0.2702 -0.0438 -0.0490 0.0440  17  TYR   B CB  
4424 C CG  . TYR   B 17  ? 0.2861 0.3096 0.3398 -0.0324 -0.0676 0.0577  17  TYR   B CG  
4425 C CD1 . TYR   B 17  ? 0.3063 0.3301 0.3654 -0.0306 -0.0788 0.0653  17  TYR   B CD1 
4426 C CD2 . TYR   B 17  ? 0.3041 0.3393 0.3742 -0.0193 -0.0876 0.0587  17  TYR   B CD2 
4427 C CE1 . TYR   B 17  ? 0.3251 0.3528 0.3971 -0.0194 -0.0955 0.0630  17  TYR   B CE1 
4428 C CE2 . TYR   B 17  ? 0.3204 0.3574 0.4007 -0.0022 -0.1123 0.0732  17  TYR   B CE2 
4429 C CZ  . TYR   B 17  ? 0.3342 0.3643 0.4136 -0.0032 -0.1137 0.0665  17  TYR   B CZ  
4430 O OH  . TYR   B 17  ? 0.3507 0.3792 0.4360 0.0087  -0.1175 0.0597  17  TYR   B OH  
4440 N N   . ILE   B 18  ? 0.2140 0.1752 0.2246 -0.0470 -0.0131 -0.0176 18  ILE   B N   
4441 C CA  . ILE   B 18  ? 0.2215 0.1690 0.2356 -0.0484 -0.0089 -0.0330 18  ILE   B CA  
4442 C C   . ILE   B 18  ? 0.2278 0.1691 0.2220 -0.0598 0.0071  -0.0454 18  ILE   B C   
4443 O O   . ILE   B 18  ? 0.2478 0.1920 0.2348 -0.0539 0.0120  -0.0577 18  ILE   B O   
4444 C CB  . ILE   B 18  ? 0.2285 0.1641 0.2310 -0.0549 -0.0148 -0.0200 18  ILE   B CB  
4445 C CG1 . ILE   B 18  ? 0.2281 0.1743 0.2435 -0.0544 -0.0141 -0.0192 18  ILE   B CG1 
4446 C CG2 . ILE   B 18  ? 0.2343 0.1709 0.2199 -0.0568 -0.0207 -0.0216 18  ILE   B CG2 
4447 C CD1 . ILE   B 18  ? 0.2364 0.2031 0.2715 -0.0457 -0.0167 0.0109  18  ILE   B CD1 
4459 N N   . LYS   B 19  ? 0.2280 0.1735 0.2374 -0.0376 0.0401  -0.0469 19  LYS   B N   
4460 C CA  . LYS   B 19  ? 0.2249 0.1792 0.2686 -0.0426 0.0318  -0.0572 19  LYS   B CA  
4461 C C   . LYS   B 19  ? 0.2089 0.1756 0.2927 -0.0326 0.0412  -0.0690 19  LYS   B C   
4462 O O   . LYS   B 19  ? 0.2015 0.1746 0.2694 -0.0253 0.0274  -0.0599 19  LYS   B O   
4463 C CB  . LYS   B 19  ? 0.2485 0.2079 0.2740 -0.0438 0.0536  -0.0551 19  LYS   B CB  
4464 C CG  . LYS   B 19  ? 0.2811 0.2290 0.3074 -0.0555 0.0610  -0.0544 19  LYS   B CG  
4465 C CD  . LYS   B 19  ? 0.3171 0.2619 0.3305 -0.0652 0.0737  -0.0483 19  LYS   B CD  
4466 C CE  . LYS   B 19  ? 0.3533 0.2890 0.3470 -0.0722 0.0651  -0.0439 19  LYS   B CE  
4467 N NZ  . LYS   B 19  ? 0.3809 0.3061 0.3558 -0.0766 0.0752  -0.0372 19  LYS   B NZ  
4481 N N   . ASN   B 20  ? 0.2114 0.1861 0.3220 -0.0366 0.0574  -0.0766 20  ASN   B N   
4482 C CA  . ASN   B 20  ? 0.2103 0.1987 0.3513 -0.0298 0.0494  -0.0977 20  ASN   B CA  
4483 C C   . ASN   B 20  ? 0.2104 0.2257 0.3438 -0.0275 0.0626  -0.1020 20  ASN   B C   
4484 O O   . ASN   B 20  ? 0.2327 0.2641 0.3599 -0.0435 0.0584  -0.0924 20  ASN   B O   
4485 C CB  . ASN   B 20  ? 0.2411 0.2041 0.3822 -0.0013 0.0357  -0.0956 20  ASN   B CB  
4486 C CG  . ASN   B 20  ? 0.2744 0.2130 0.4051 0.0356  0.0374  -0.1085 20  ASN   B CG  
4487 O OD1 . ASN   B 20  ? 0.3153 0.2443 0.4318 0.0564  0.0325  -0.1129 20  ASN   B OD1 
4488 N ND2 . ASN   B 20  ? 0.2564 0.2105 0.3971 0.0336  0.0360  -0.1059 20  ASN   B ND2 
4495 N N   . ALA   B 21  ? 0.2125 0.2110 0.3468 -0.0340 0.0738  -0.0852 21  ALA   B N   
4496 C CA  . ALA   B 21  ? 0.2301 0.2155 0.3529 -0.0306 0.0645  -0.0708 21  ALA   B CA  
4497 C C   . ALA   B 21  ? 0.2264 0.1839 0.3264 -0.0232 0.0680  -0.0626 21  ALA   B C   
4498 O O   . ALA   B 21  ? 0.2361 0.1762 0.3239 -0.0346 0.0527  -0.0524 21  ALA   B O   
4499 C CB  . ALA   B 21  ? 0.2512 0.2443 0.3775 -0.0509 0.0550  -0.0432 21  ALA   B CB  
4505 N N   . ASP   B 22  ? 0.2123 0.1725 0.3144 -0.0234 0.0529  -0.0463 22  ASP   B N   
4506 C CA  . ASP   B 22  ? 0.2116 0.1614 0.3055 -0.0135 0.0323  -0.0237 22  ASP   B CA  
4507 C C   . ASP   B 22  ? 0.1995 0.1605 0.2663 -0.0205 0.0239  -0.0135 22  ASP   B C   
4508 O O   . ASP   B 22  ? 0.1968 0.1638 0.2662 -0.0159 0.0143  -0.0138 22  ASP   B O   
4509 C CB  . ASP   B 22  ? 0.2176 0.1705 0.3420 -0.0111 0.0214  -0.0111 22  ASP   B CB  
4510 C CG  . ASP   B 22  ? 0.2164 0.1915 0.3819 -0.0001 0.0025  -0.0078 22  ASP   B CG  
4511 O OD1 . ASP   B 22  ? 0.2215 0.1808 0.3744 0.0020  -0.0204 0.0061  22  ASP   B OD1 
4512 O OD2 . ASP   B 22  ? 0.2217 0.2203 0.4368 0.0090  -0.0104 -0.0239 22  ASP   B OD2 
4517 N N   . ILE   B 23  ? 0.1942 0.1513 0.2361 -0.0141 0.0022  0.0163  23  ILE   B N   
4518 C CA  . ILE   B 23  ? 0.1853 0.1490 0.2243 -0.0186 -0.0014 0.0044  23  ILE   B CA  
4519 C C   . ILE   B 23  ? 0.1739 0.1482 0.2052 -0.0160 -0.0086 0.0011  23  ILE   B C   
4520 O O   . ILE   B 23  ? 0.1669 0.1458 0.2109 -0.0142 -0.0107 0.0058  23  ILE   B O   
4521 C CB  . ILE   B 23  ? 0.1763 0.1525 0.2468 -0.0233 -0.0086 0.0199  23  ILE   B CB  
4522 C CG1 . ILE   B 23  ? 0.1765 0.1678 0.2587 -0.0113 0.0011  0.0302  23  ILE   B CG1 
4523 C CG2 . ILE   B 23  ? 0.1805 0.1751 0.2449 -0.0193 -0.0156 0.0083  23  ILE   B CG2 
4524 C CD1 . ILE   B 23  ? 0.1765 0.1752 0.2567 -0.0146 -0.0002 0.0294  23  ILE   B CD1 
4536 N N   . VAL   B 24  ? 0.1788 0.1463 0.2140 -0.0117 -0.0148 0.0112  24  VAL   B N   
4537 C CA  . VAL   B 24  ? 0.1782 0.1535 0.2512 -0.0113 -0.0220 0.0049  24  VAL   B CA  
4538 C C   . VAL   B 24  ? 0.1783 0.1618 0.2526 -0.0169 -0.0093 0.0010  24  VAL   B C   
4539 O O   . VAL   B 24  ? 0.1704 0.1760 0.2637 -0.0169 -0.0022 0.0152  24  VAL   B O   
4540 C CB  . VAL   B 24  ? 0.1853 0.1674 0.2649 -0.0033 -0.0233 -0.0047 24  VAL   B CB  
4541 C CG1 . VAL   B 24  ? 0.1751 0.1739 0.2934 -0.0153 -0.0249 -0.0030 24  VAL   B CG1 
4542 C CG2 . VAL   B 24  ? 0.1947 0.1993 0.2481 0.0116  -0.0215 -0.0139 24  VAL   B CG2 
4552 N N   A GLU   B 25  ? 0.1930 0.1769 0.2554 -0.0167 -0.0047 0.0009  25  GLU   B N   
4553 N N   B GLU   B 25  ? 0.1943 0.1793 0.2551 -0.0180 -0.0017 0.0021  25  GLU   B N   
4554 C CA  A GLU   B 25  ? 0.2100 0.2075 0.2676 -0.0119 0.0053  -0.0065 25  GLU   B CA  
4555 C CA  B GLU   B 25  ? 0.2108 0.2081 0.2685 -0.0140 0.0113  -0.0026 25  GLU   B CA  
4556 C C   A GLU   B 25  ? 0.2020 0.2029 0.2331 -0.0195 0.0069  -0.0072 25  GLU   B C   
4557 C C   B GLU   B 25  ? 0.2049 0.2058 0.2436 -0.0181 0.0114  0.0018  25  GLU   B C   
4558 O O   A GLU   B 25  ? 0.2004 0.2159 0.2455 -0.0182 0.0169  -0.0037 25  GLU   B O   
4559 O O   B GLU   B 25  ? 0.2047 0.2158 0.2504 -0.0164 0.0188  0.0020  25  GLU   B O   
4560 C CB  A GLU   B 25  ? 0.2433 0.2512 0.3344 0.0045  0.0114  -0.0091 25  GLU   B CB  
4561 C CB  B GLU   B 25  ? 0.2388 0.2457 0.3243 -0.0012 0.0192  -0.0079 25  GLU   B CB  
4562 C CG  A GLU   B 25  ? 0.2804 0.2976 0.4087 0.0096  0.0016  -0.0101 25  GLU   B CG  
4563 C CG  B GLU   B 25  ? 0.2696 0.2848 0.3881 0.0022  0.0136  -0.0113 25  GLU   B CG  
4564 C CD  A GLU   B 25  ? 0.3130 0.3412 0.4658 0.0055  -0.0052 -0.0065 25  GLU   B CD  
4565 C CD  B GLU   B 25  ? 0.2965 0.3196 0.4368 -0.0027 0.0107  -0.0125 25  GLU   B CD  
4566 O OE1 A GLU   B 25  ? 0.3282 0.3661 0.4891 0.0079  0.0018  -0.0017 25  GLU   B OE1 
4567 O OE1 B GLU   B 25  ? 0.3088 0.3400 0.4576 0.0002  0.0164  -0.0144 25  GLU   B OE1 
4568 O OE2 A GLU   B 25  ? 0.3223 0.3532 0.4924 0.0043  -0.0130 -0.0086 25  GLU   B OE2 
4569 O OE2 B GLU   B 25  ? 0.3047 0.3308 0.4592 -0.0048 0.0067  -0.0126 25  GLU   B OE2 
4582 N N   A GLU   B 26  ? 0.1989 0.1826 0.2081 -0.0321 0.0088  -0.0032 26  GLU   B N   
4583 N N   B GLU   B 26  ? 0.2003 0.1913 0.2282 -0.0271 0.0111  0.0133  26  GLU   B N   
4584 C CA  A GLU   B 26  ? 0.2067 0.1973 0.2181 -0.0378 -0.0007 0.0011  26  GLU   B CA  
4585 C CA  B GLU   B 26  ? 0.2022 0.2011 0.2394 -0.0334 0.0032  0.0206  26  GLU   B CA  
4586 C C   A GLU   B 26  ? 0.1909 0.1954 0.2041 -0.0335 0.0064  0.0091  26  GLU   B C   
4587 C C   B GLU   B 26  ? 0.1873 0.1975 0.2126 -0.0335 0.0106  0.0187  26  GLU   B C   
4588 O O   A GLU   B 26  ? 0.2066 0.2130 0.2166 -0.0307 0.0061  0.0088  26  GLU   B O   
4589 O O   B GLU   B 26  ? 0.1986 0.2136 0.2193 -0.0338 0.0120  0.0170  26  GLU   B O   
4590 C CB  A GLU   B 26  ? 0.2347 0.2086 0.2259 -0.0398 0.0170  0.0188  26  GLU   B CB  
4591 C CB  B GLU   B 26  ? 0.2213 0.2108 0.2644 -0.0355 0.0120  0.0428  26  GLU   B CB  
4592 C CG  A GLU   B 26  ? 0.2692 0.2314 0.2516 -0.0367 0.0291  0.0026  26  GLU   B CG  
4593 C CG  B GLU   B 26  ? 0.2442 0.2324 0.3047 -0.0349 0.0195  0.0351  26  GLU   B CG  
4594 C CD  A GLU   B 26  ? 0.2916 0.2398 0.2604 -0.0509 0.0370  -0.0233 26  GLU   B CD  
4595 C CD  B GLU   B 26  ? 0.2501 0.2337 0.3275 -0.0471 0.0181  0.0309  26  GLU   B CD  
4596 O OE1 A GLU   B 26  ? 0.3045 0.2349 0.2416 -0.0589 0.0642  -0.0365 26  GLU   B OE1 
4597 O OE1 B GLU   B 26  ? 0.2571 0.2439 0.3533 -0.0601 0.0476  0.0187  26  GLU   B OE1 
4598 O OE2 A GLU   B 26  ? 0.2938 0.2518 0.2807 -0.0499 0.0432  0.0026  26  GLU   B OE2 
4599 O OE2 B GLU   B 26  ? 0.2440 0.2242 0.3205 -0.0440 0.0085  0.0272  26  GLU   B OE2 
4612 N N   . ALA   B 27  ? 0.1748 0.1856 0.1981 -0.0327 0.0101  0.0208  27  ALA   B N   
4613 C CA  . ALA   B 27  ? 0.1662 0.1797 0.2098 -0.0242 -0.0105 0.0262  27  ALA   B CA  
4614 C C   . ALA   B 27  ? 0.1723 0.1912 0.2358 -0.0198 0.0016  0.0362  27  ALA   B C   
4615 O O   . ALA   B 27  ? 0.1809 0.1978 0.2272 -0.0100 0.0033  0.0414  27  ALA   B O   
4616 C CB  . ALA   B 27  ? 0.1804 0.1572 0.2190 -0.0273 -0.0058 0.0225  27  ALA   B CB  
4623 N N   . LYS   B 28  ? 0.1687 0.2091 0.2799 -0.0255 0.0030  0.0573  28  LYS   B N   
4624 C CA  . LYS   B 28  ? 0.1820 0.2534 0.3071 -0.0199 0.0414  0.0841  28  LYS   B CA  
4625 C C   . LYS   B 28  ? 0.2145 0.2697 0.2971 -0.0160 0.0506  0.0781  28  LYS   B C   
4626 O O   . LYS   B 28  ? 0.2340 0.2730 0.3099 -0.0122 0.0605  0.0782  28  LYS   B O   
4627 C CB  . LYS   B 28  ? 0.2019 0.2940 0.3477 -0.0065 0.0646  0.0934  28  LYS   B CB  
4628 C CG  . LYS   B 28  ? 0.2297 0.3453 0.3948 0.0026  0.0739  0.1137  28  LYS   B CG  
4629 C CD  . LYS   B 28  ? 0.2608 0.3953 0.4579 0.0097  0.0798  0.1169  28  LYS   B CD  
4630 C CE  . LYS   B 28  ? 0.3194 0.4357 0.5010 0.0185  0.0731  0.1204  28  LYS   B CE  
4631 N NZ  . LYS   B 28  ? 0.3695 0.4939 0.5332 0.0302  0.0734  0.1261  28  LYS   B NZ  
4645 N N   A LYS   B 29  ? 0.2342 0.2895 0.2988 -0.0064 0.0476  0.0594  29  LYS   B N   
4646 N N   B LYS   B 29  ? 0.2358 0.2894 0.3003 -0.0086 0.0447  0.0614  29  LYS   B N   
4647 C CA  A LYS   B 29  ? 0.2667 0.3150 0.3135 -0.0035 0.0429  0.0558  29  LYS   B CA  
4648 C CA  B LYS   B 29  ? 0.2655 0.3122 0.3147 -0.0049 0.0403  0.0565  29  LYS   B CA  
4649 C C   A LYS   B 29  ? 0.2591 0.3180 0.2856 -0.0065 0.0284  0.0657  29  LYS   B C   
4650 C C   B LYS   B 29  ? 0.2593 0.3130 0.2862 -0.0055 0.0317  0.0657  29  LYS   B C   
4651 O O   A LYS   B 29  ? 0.2721 0.3412 0.3057 -0.0038 0.0253  0.0682  29  LYS   B O   
4652 O O   B LYS   B 29  ? 0.2735 0.3280 0.2962 0.0001  0.0351  0.0697  29  LYS   B O   
4653 C CB  A LYS   B 29  ? 0.3129 0.3397 0.3739 0.0023  0.0397  0.0428  29  LYS   B CB  
4654 C CB  B LYS   B 29  ? 0.3065 0.3357 0.3717 -0.0006 0.0350  0.0423  29  LYS   B CB  
4655 C CG  A LYS   B 29  ? 0.3480 0.3579 0.4349 0.0056  0.0393  0.0355  29  LYS   B CG  
4656 C CG  B LYS   B 29  ? 0.3376 0.3530 0.4289 0.0022  0.0318  0.0340  29  LYS   B CG  
4657 C CD  A LYS   B 29  ? 0.3761 0.3723 0.4862 0.0059  0.0437  0.0274  29  LYS   B CD  
4658 C CD  B LYS   B 29  ? 0.3614 0.3668 0.4774 0.0028  0.0326  0.0251  29  LYS   B CD  
4659 C CE  A LYS   B 29  ? 0.3970 0.3835 0.5246 0.0054  0.0500  0.0221  29  LYS   B CE  
4660 C CE  B LYS   B 29  ? 0.3798 0.3771 0.5140 0.0026  0.0356  0.0188  29  LYS   B CE  
4661 N NZ  A LYS   B 29  ? 0.4110 0.3932 0.5425 0.0063  0.0545  0.0175  29  LYS   B NZ  
4662 N NZ  B LYS   B 29  ? 0.3909 0.3856 0.5305 0.0031  0.0390  0.0135  29  LYS   B NZ  
4689 N N   . VAL   B 30  ? 0.2361 0.3014 0.2683 -0.0174 0.0228  0.0621  30  VAL   B N   
4690 C CA  . VAL   B 30  ? 0.2178 0.2815 0.2949 -0.0299 -0.0153 0.0664  30  VAL   B CA  
4691 C C   . VAL   B 30  ? 0.1961 0.2706 0.2759 -0.0310 -0.0181 0.0930  30  VAL   B C   
4692 O O   . VAL   B 30  ? 0.2149 0.2876 0.2805 -0.0263 -0.0174 0.1103  30  VAL   B O   
4693 C CB  . VAL   B 30  ? 0.2238 0.2773 0.3435 -0.0465 -0.0371 0.0628  30  VAL   B CB  
4694 C CG1 . VAL   B 30  ? 0.2393 0.2924 0.3359 -0.0427 -0.0394 0.0499  30  VAL   B CG1 
4695 C CG2 . VAL   B 30  ? 0.2387 0.2749 0.3678 -0.0579 -0.0396 0.0444  30  VAL   B CG2 
4706 N N   A LYS   B 31  ? 0.1849 0.2461 0.2941 -0.0440 -0.0148 0.0981  31  LYS   B N   
4707 N N   B LYS   B 31  ? 0.1941 0.2524 0.2875 -0.0381 -0.0191 0.0864  31  LYS   B N   
4708 C CA  A LYS   B 31  ? 0.1738 0.2414 0.3187 -0.0479 -0.0104 0.0989  31  LYS   B CA  
4709 C CA  B LYS   B 31  ? 0.1939 0.2460 0.3017 -0.0392 -0.0226 0.0799  31  LYS   B CA  
4710 C C   A LYS   B 31  ? 0.1723 0.2070 0.2850 -0.0450 -0.0329 0.0904  31  LYS   B C   
4711 C C   B LYS   B 31  ? 0.1862 0.2076 0.2706 -0.0415 -0.0414 0.0746  31  LYS   B C   
4712 O O   A LYS   B 31  ? 0.1657 0.2149 0.2997 -0.0441 -0.0324 0.1002  31  LYS   B O   
4713 O O   B LYS   B 31  ? 0.1839 0.2109 0.2722 -0.0432 -0.0467 0.0764  31  LYS   B O   
4714 C CB  A LYS   B 31  ? 0.1776 0.2821 0.3747 -0.0389 0.0258  0.1106  31  LYS   B CB  
4715 C CB  B LYS   B 31  ? 0.2075 0.2839 0.3481 -0.0283 -0.0007 0.0778  31  LYS   B CB  
4716 C CG  A LYS   B 31  ? 0.2015 0.3162 0.4147 -0.0330 0.0344  0.1077  31  LYS   B CG  
4717 C CG  B LYS   B 31  ? 0.2277 0.3120 0.3833 -0.0241 0.0049  0.0684  31  LYS   B CG  
4718 C CD  A LYS   B 31  ? 0.2313 0.3520 0.4559 -0.0249 0.0238  0.0937  31  LYS   B CD  
4719 C CD  B LYS   B 31  ? 0.2505 0.3414 0.4194 -0.0234 -0.0006 0.0578  31  LYS   B CD  
4720 C CE  A LYS   B 31  ? 0.2520 0.3730 0.4891 -0.0189 0.0129  0.0803  31  LYS   B CE  
4721 C CE  B LYS   B 31  ? 0.2702 0.3634 0.4502 -0.0232 -0.0052 0.0512  31  LYS   B CE  
4722 N NZ  A LYS   B 31  ? 0.2727 0.3849 0.5057 -0.0106 0.0061  0.0647  31  LYS   B NZ  
4723 N NZ  B LYS   B 31  ? 0.2888 0.3775 0.4641 -0.0186 -0.0112 0.0398  31  LYS   B NZ  
4750 N N   . PRO   B 32  ? 0.1821 0.1707 0.2435 -0.0439 -0.0513 0.0661  32  PRO   B N   
4751 C CA  . PRO   B 32  ? 0.2004 0.1616 0.2150 -0.0381 -0.0518 0.0329  32  PRO   B CA  
4752 C C   . PRO   B 32  ? 0.2139 0.1501 0.1949 -0.0419 -0.0675 0.0393  32  PRO   B C   
4753 O O   . PRO   B 32  ? 0.2188 0.1559 0.2482 -0.0458 -0.0816 0.0301  32  PRO   B O   
4754 C CB  . PRO   B 32  ? 0.2142 0.1596 0.2101 -0.0369 -0.0327 0.0134  32  PRO   B CB  
4755 C CG  . PRO   B 32  ? 0.2238 0.1500 0.2173 -0.0287 -0.0516 0.0223  32  PRO   B CG  
4756 C CD  . PRO   B 32  ? 0.2059 0.1576 0.2373 -0.0256 -0.0732 0.0288  32  PRO   B CD  
4764 N N   . THR   B 33  ? 0.2170 0.1432 0.1973 -0.0407 -0.0597 0.0304  33  THR   B N   
4765 C CA  . THR   B 33  ? 0.2143 0.1490 0.1810 -0.0364 -0.0587 0.0409  33  THR   B CA  
4766 C C   . THR   B 33  ? 0.2183 0.1395 0.1744 -0.0407 -0.0503 0.0242  33  THR   B C   
4767 O O   . THR   B 33  ? 0.2401 0.1430 0.1869 -0.0479 -0.0558 0.0115  33  THR   B O   
4768 C CB  . THR   B 33  ? 0.2233 0.1619 0.1998 -0.0225 -0.0651 0.0395  33  THR   B CB  
4769 O OG1 . THR   B 33  ? 0.2114 0.1700 0.2064 -0.0302 -0.0638 0.0421  33  THR   B OG1 
4770 C CG2 . THR   B 33  ? 0.2526 0.1616 0.2190 -0.0097 -0.0582 0.0357  33  THR   B CG2 
4778 N N   . VAL   B 34  ? 0.1982 0.1400 0.1732 -0.0383 -0.0471 0.0195  34  VAL   B N   
4779 C CA  . VAL   B 34  ? 0.1812 0.1404 0.1812 -0.0336 -0.0498 0.0116  34  VAL   B CA  
4780 C C   . VAL   B 34  ? 0.1665 0.1314 0.1765 -0.0316 -0.0272 0.0111  34  VAL   B C   
4781 O O   . VAL   B 34  ? 0.1815 0.1432 0.1716 -0.0310 -0.0432 0.0125  34  VAL   B O   
4782 C CB  . VAL   B 34  ? 0.1907 0.1491 0.2096 -0.0085 -0.0483 0.0196  34  VAL   B CB  
4783 C CG1 . VAL   B 34  ? 0.1837 0.1617 0.2019 0.0014  -0.0223 0.0155  34  VAL   B CG1 
4784 C CG2 . VAL   B 34  ? 0.1960 0.1536 0.2291 -0.0095 -0.0495 0.0234  34  VAL   B CG2 
4794 N N   . VAL   B 35  ? 0.1506 0.1325 0.1567 -0.0290 -0.0171 0.0077  35  VAL   B N   
4795 C CA  . VAL   B 35  ? 0.1508 0.1273 0.1574 -0.0212 -0.0118 0.0065  35  VAL   B CA  
4796 C C   . VAL   B 35  ? 0.1446 0.1246 0.1430 -0.0181 -0.0176 0.0072  35  VAL   B C   
4797 O O   . VAL   B 35  ? 0.1481 0.1326 0.1442 -0.0215 -0.0064 -0.0040 35  VAL   B O   
4798 C CB  . VAL   B 35  ? 0.1532 0.1460 0.1649 -0.0234 -0.0055 0.0011  35  VAL   B CB  
4799 C CG1 . VAL   B 35  ? 0.1482 0.1569 0.1934 -0.0242 0.0016  -0.0027 35  VAL   B CG1 
4800 C CG2 . VAL   B 35  ? 0.1534 0.1488 0.1799 -0.0156 -0.0040 0.0023  35  VAL   B CG2 
4810 N N   . VAL   B 36  ? 0.1390 0.1268 0.1600 -0.0191 -0.0133 0.0196  36  VAL   B N   
4811 C CA  . VAL   B 36  ? 0.1343 0.1171 0.1523 -0.0189 -0.0123 -0.0008 36  VAL   B CA  
4812 C C   . VAL   B 36  ? 0.1333 0.1261 0.1490 -0.0139 -0.0057 0.0034  36  VAL   B C   
4813 O O   . VAL   B 36  ? 0.1408 0.1391 0.1575 -0.0146 -0.0090 -0.0039 36  VAL   B O   
4814 C CB  . VAL   B 36  ? 0.1336 0.1269 0.1617 -0.0161 -0.0120 0.0008  36  VAL   B CB  
4815 C CG1 . VAL   B 36  ? 0.1355 0.1387 0.1713 -0.0206 -0.0095 -0.0005 36  VAL   B CG1 
4816 C CG2 . VAL   B 36  ? 0.1410 0.1391 0.1786 -0.0183 -0.0172 -0.0034 36  VAL   B CG2 
4826 N N   . ASN   B 37  ? 0.1393 0.1319 0.1543 0.0010  -0.0093 0.0031  37  ASN   B N   
4827 C CA  . ASN   B 37  ? 0.1375 0.1324 0.1750 -0.0019 -0.0154 0.0119  37  ASN   B CA  
4828 C C   . ASN   B 37  ? 0.1329 0.1362 0.1837 -0.0010 -0.0171 0.0003  37  ASN   B C   
4829 O O   . ASN   B 37  ? 0.1419 0.1446 0.1616 0.0012  -0.0034 0.0058  37  ASN   B O   
4830 C CB  . ASN   B 37  ? 0.1381 0.1345 0.1611 -0.0048 -0.0271 0.0095  37  ASN   B CB  
4831 C CG  . ASN   B 37  ? 0.1415 0.1358 0.1785 -0.0067 -0.0121 0.0049  37  ASN   B CG  
4832 O OD1 . ASN   B 37  ? 0.1454 0.1443 0.1860 0.0087  -0.0191 -0.0003 37  ASN   B OD1 
4833 N ND2 . ASN   B 37  ? 0.1515 0.1315 0.1658 0.0044  -0.0158 0.0111  37  ASN   B ND2 
4840 N N   . ALA   B 38  ? 0.1488 0.1310 0.1678 0.0047  -0.0063 0.0097  38  ALA   B N   
4841 C CA  . ALA   B 38  ? 0.1550 0.1398 0.1828 -0.0006 -0.0023 0.0099  38  ALA   B CA  
4842 C C   . ALA   B 38  ? 0.1491 0.1383 0.1721 0.0020  0.0021  0.0152  38  ALA   B C   
4843 O O   . ALA   B 38  ? 0.1731 0.1447 0.1671 0.0049  0.0010  0.0135  38  ALA   B O   
4844 C CB  . ALA   B 38  ? 0.1758 0.1457 0.1911 -0.0095 0.0184  0.0106  38  ALA   B CB  
4850 N N   . ALA   B 39  ? 0.1494 0.1285 0.1764 0.0076  -0.0056 0.0091  39  ALA   B N   
4851 C CA  . ALA   B 39  ? 0.1554 0.1415 0.1829 0.0038  -0.0051 0.0059  39  ALA   B CA  
4852 C C   . ALA   B 39  ? 0.1544 0.1510 0.1699 0.0079  -0.0065 0.0013  39  ALA   B C   
4853 O O   . ALA   B 39  ? 0.1686 0.1558 0.1681 -0.0048 -0.0045 0.0088  39  ALA   B O   
4854 C CB  . ALA   B 39  ? 0.1494 0.1413 0.1859 -0.0086 0.0015  0.0053  39  ALA   B CB  
4860 N N   . ASN   B 40  ? 0.1628 0.1690 0.1735 -0.0048 0.0012  -0.0012 40  ASN   B N   
4861 C CA  . ASN   B 40  ? 0.1718 0.1720 0.1961 0.0010  -0.0010 0.0039  40  ASN   B CA  
4862 C C   . ASN   B 40  ? 0.1769 0.1718 0.1657 0.0054  -0.0027 0.0082  40  ASN   B C   
4863 O O   . ASN   B 40  ? 0.1752 0.1642 0.1489 0.0066  -0.0016 0.0029  40  ASN   B O   
4864 C CB  . ASN   B 40  ? 0.1851 0.1700 0.1994 0.0046  -0.0070 0.0206  40  ASN   B CB  
4865 C CG  . ASN   B 40  ? 0.1955 0.1706 0.2313 0.0058  -0.0197 0.0250  40  ASN   B CG  
4866 O OD1 . ASN   B 40  ? 0.2009 0.1700 0.3105 -0.0004 -0.0356 0.0356  40  ASN   B OD1 
4867 N ND2 . ASN   B 40  ? 0.2003 0.1718 0.2384 0.0058  -0.0158 0.0260  40  ASN   B ND2 
4874 N N   . VAL   B 41  ? 0.1854 0.1696 0.1630 0.0144  0.0102  0.0072  41  VAL   B N   
4875 C CA  . VAL   B 41  ? 0.1940 0.1839 0.1608 0.0052  -0.0016 -0.0027 41  VAL   B CA  
4876 C C   . VAL   B 41  ? 0.1937 0.1800 0.1610 0.0106  -0.0092 -0.0036 41  VAL   B C   
4877 O O   . VAL   B 41  ? 0.1928 0.1809 0.1718 0.0128  -0.0123 -0.0058 41  VAL   B O   
4878 C CB  . VAL   B 41  ? 0.2111 0.2057 0.1865 -0.0004 0.0223  -0.0199 41  VAL   B CB  
4879 C CG1 . VAL   B 41  ? 0.2047 0.2092 0.1858 -0.0073 0.0287  -0.0304 41  VAL   B CG1 
4880 C CG2 . VAL   B 41  ? 0.2279 0.2164 0.2019 -0.0108 0.0285  -0.0131 41  VAL   B CG2 
4890 N N   . TYR   B 42  ? 0.2034 0.1833 0.1487 0.0160  -0.0183 0.0070  42  TYR   B N   
4891 C CA  . TYR   B 42  ? 0.2042 0.1895 0.1539 0.0218  -0.0272 -0.0033 42  TYR   B CA  
4892 C C   . TYR   B 42  ? 0.1856 0.1718 0.1661 0.0200  -0.0214 -0.0096 42  TYR   B C   
4893 O O   . TYR   B 42  ? 0.1812 0.1785 0.2251 0.0100  -0.0207 -0.0101 42  TYR   B O   
4894 C CB  . TYR   B 42  ? 0.2279 0.2141 0.1911 0.0211  -0.0270 0.0065  42  TYR   B CB  
4895 C CG  . TYR   B 42  ? 0.2323 0.2340 0.1772 0.0089  -0.0292 0.0162  42  TYR   B CG  
4896 C CD1 . TYR   B 42  ? 0.2227 0.2330 0.1775 0.0025  -0.0242 0.0068  42  TYR   B CD1 
4897 C CD2 . TYR   B 42  ? 0.2522 0.2495 0.2215 0.0145  -0.0221 0.0222  42  TYR   B CD2 
4898 C CE1 . TYR   B 42  ? 0.2323 0.2536 0.1747 0.0031  -0.0297 0.0039  42  TYR   B CE1 
4899 C CE2 . TYR   B 42  ? 0.2536 0.2624 0.2043 0.0207  0.0041  0.0341  42  TYR   B CE2 
4900 C CZ  . TYR   B 42  ? 0.2597 0.2787 0.1882 0.0250  0.0053  0.0039  42  TYR   B CZ  
4901 O OH  . TYR   B 42  ? 0.2875 0.3149 0.2402 0.0428  0.0117  0.0153  42  TYR   B OH  
4911 N N   . LEU   B 43  ? 0.1790 0.1530 0.1517 0.0100  -0.0153 -0.0153 43  LEU   B N   
4912 C CA  . LEU   B 43  ? 0.1766 0.1536 0.1539 0.0047  -0.0245 -0.0007 43  LEU   B CA  
4913 C C   . LEU   B 43  ? 0.1756 0.1566 0.1450 0.0044  -0.0236 0.0007  43  LEU   B C   
4914 O O   . LEU   B 43  ? 0.1728 0.1623 0.1877 0.0118  -0.0245 0.0071  43  LEU   B O   
4915 C CB  . LEU   B 43  ? 0.1696 0.1480 0.1694 0.0040  -0.0310 -0.0014 43  LEU   B CB  
4916 C CG  . LEU   B 43  ? 0.1788 0.1440 0.1876 -0.0009 -0.0374 -0.0027 43  LEU   B CG  
4917 C CD1 . LEU   B 43  ? 0.1867 0.1457 0.2267 0.0039  -0.0400 -0.0071 43  LEU   B CD1 
4918 C CD2 . LEU   B 43  ? 0.1813 0.1529 0.1846 -0.0080 -0.0448 -0.0056 43  LEU   B CD2 
4930 N N   . LYS   B 44  ? 0.1747 0.1587 0.1689 0.0084  -0.0191 -0.0103 44  LYS   B N   
4931 C CA  . LYS   B 44  ? 0.1861 0.1690 0.1685 0.0091  -0.0172 -0.0029 44  LYS   B CA  
4932 C C   . LYS   B 44  ? 0.1800 0.1602 0.1654 0.0128  -0.0147 0.0005  44  LYS   B C   
4933 O O   . LYS   B 44  ? 0.1937 0.1630 0.1958 0.0023  -0.0127 0.0027  44  LYS   B O   
4934 C CB  . LYS   B 44  ? 0.2130 0.1809 0.1838 0.0223  -0.0336 0.0025  44  LYS   B CB  
4935 C CG  . LYS   B 44  ? 0.2578 0.2127 0.2079 0.0153  -0.0601 0.0138  44  LYS   B CG  
4936 C CD  . LYS   B 44  ? 0.2987 0.2379 0.2798 -0.0109 -0.0733 0.0085  44  LYS   B CD  
4937 C CE  . LYS   B 44  ? 0.3335 0.2718 0.3342 -0.0237 -0.0727 0.0178  44  LYS   B CE  
4938 N NZ  . LYS   B 44  ? 0.3505 0.2806 0.3474 -0.0244 -0.0744 0.0294  44  LYS   B NZ  
4952 N N   . HIS   B 45  ? 0.1742 0.1701 0.1452 0.0039  -0.0137 0.0064  45  HIS   B N   
4953 C CA  . HIS   B 45  ? 0.1679 0.1605 0.1494 0.0066  -0.0137 0.0090  45  HIS   B CA  
4954 C C   . HIS   B 45  ? 0.1876 0.1746 0.2213 0.0200  -0.0221 0.0045  45  HIS   B C   
4955 O O   . HIS   B 45  ? 0.2043 0.2055 0.2739 0.0482  -0.0014 0.0046  45  HIS   B O   
4956 C CB  . HIS   B 45  ? 0.1630 0.1626 0.1708 0.0072  -0.0084 -0.0062 45  HIS   B CB  
4957 C CG  . HIS   B 45  ? 0.1670 0.1573 0.1638 -0.0041 -0.0175 0.0011  45  HIS   B CG  
4958 N ND1 . HIS   B 45  ? 0.1766 0.1504 0.1727 -0.0014 -0.0215 -0.0024 45  HIS   B ND1 
4959 C CD2 . HIS   B 45  ? 0.1768 0.1659 0.1676 -0.0065 -0.0336 0.0034  45  HIS   B CD2 
4960 C CE1 . HIS   B 45  ? 0.1837 0.1412 0.1804 -0.0051 -0.0319 -0.0115 45  HIS   B CE1 
4961 N NE2 . HIS   B 45  ? 0.1866 0.1583 0.1758 0.0015  -0.0259 -0.0084 45  HIS   B NE2 
4969 N N   A GLY   B 46  ? 0.2032 0.1735 0.2503 0.0180  -0.0404 0.0115  46  GLY   B N   
4970 N N   B GLY   B 46  ? 0.2047 0.1822 0.2388 0.0209  -0.0397 0.0149  46  GLY   B N   
4971 C CA  A GLY   B 46  ? 0.2166 0.1831 0.2943 0.0163  -0.0498 0.0149  46  GLY   B CA  
4972 C CA  B GLY   B 46  ? 0.2180 0.1952 0.2659 0.0199  -0.0517 0.0215  46  GLY   B CA  
4973 C C   A GLY   B 46  ? 0.2170 0.1914 0.3236 0.0237  -0.0419 0.0125  46  GLY   B C   
4974 C C   B GLY   B 46  ? 0.2196 0.2043 0.2852 0.0244  -0.0490 0.0273  46  GLY   B C   
4975 O O   A GLY   B 46  ? 0.2233 0.1941 0.4021 0.0290  -0.0149 -0.0159 46  GLY   B O   
4976 O O   B GLY   B 46  ? 0.2269 0.2152 0.3123 0.0287  -0.0373 0.0331  46  GLY   B O   
4983 N N   . GLY   B 47  ? 0.2191 0.2089 0.2966 0.0074  -0.0298 0.0076  47  GLY   B N   
4984 C CA  . GLY   B 47  ? 0.2072 0.1816 0.2720 0.0059  -0.0202 0.0035  47  GLY   B CA  
4985 C C   . GLY   B 47  ? 0.1855 0.1661 0.2326 0.0037  -0.0013 0.0095  47  GLY   B C   
4986 O O   . GLY   B 47  ? 0.1951 0.1451 0.2211 0.0022  -0.0119 0.0101  47  GLY   B O   
4991 N N   . GLY   B 48  ? 0.1690 0.1557 0.2401 0.0001  -0.0134 0.0185  48  GLY   B N   
4992 C CA  . GLY   B 48  ? 0.1642 0.1452 0.2253 -0.0077 -0.0114 0.0157  48  GLY   B CA  
4993 C C   . GLY   B 48  ? 0.1529 0.1413 0.2123 0.0014  0.0002  0.0058  48  GLY   B C   
4994 O O   . GLY   B 48  ? 0.1472 0.1494 0.2396 0.0049  -0.0061 0.0055  48  GLY   B O   
4998 N N   . VAL   B 49  ? 0.1551 0.1516 0.1970 0.0182  -0.0119 0.0036  49  VAL   B N   
4999 C CA  . VAL   B 49  ? 0.1552 0.1574 0.1980 0.0156  -0.0204 -0.0086 49  VAL   B CA  
5000 C C   . VAL   B 49  ? 0.1462 0.1493 0.1838 0.0122  -0.0199 -0.0053 49  VAL   B C   
5001 O O   . VAL   B 49  ? 0.1593 0.1540 0.1870 -0.0008 -0.0098 -0.0045 49  VAL   B O   
5002 C CB  . VAL   B 49  ? 0.1584 0.1722 0.2249 0.0020  -0.0311 0.0028  49  VAL   B CB  
5003 C CG1 . VAL   B 49  ? 0.1595 0.1840 0.2205 0.0067  -0.0331 0.0116  49  VAL   B CG1 
5004 C CG2 . VAL   B 49  ? 0.1833 0.1950 0.2557 -0.0126 -0.0473 -0.0072 49  VAL   B CG2 
5014 N N   . ALA   B 50  ? 0.1522 0.1415 0.1774 0.0061  -0.0138 0.0058  50  ALA   B N   
5015 C CA  . ALA   B 50  ? 0.1534 0.1393 0.1784 0.0089  -0.0092 0.0002  50  ALA   B CA  
5016 C C   . ALA   B 50  ? 0.1554 0.1436 0.1828 0.0013  -0.0084 -0.0038 50  ALA   B C   
5017 O O   . ALA   B 50  ? 0.1565 0.1428 0.1697 0.0013  -0.0033 -0.0042 50  ALA   B O   
5018 C CB  . ALA   B 50  ? 0.1641 0.1392 0.1670 -0.0007 -0.0169 0.0055  50  ALA   B CB  
5024 N N   . GLY   B 51  ? 0.1488 0.1524 0.1969 0.0048  -0.0144 0.0098  51  GLY   B N   
5025 C CA  . GLY   B 51  ? 0.1529 0.1588 0.2295 0.0175  -0.0152 0.0057  51  GLY   B CA  
5026 C C   . GLY   B 51  ? 0.1481 0.1592 0.2204 0.0189  -0.0115 0.0065  51  GLY   B C   
5027 O O   . GLY   B 51  ? 0.1498 0.1687 0.2289 0.0088  -0.0115 -0.0096 51  GLY   B O   
5031 N N   . ALA   B 52  ? 0.1495 0.1486 0.1963 0.0146  -0.0059 0.0055  52  ALA   B N   
5032 C CA  . ALA   B 52  ? 0.1535 0.1554 0.1975 0.0118  -0.0019 -0.0075 52  ALA   B CA  
5033 C C   . ALA   B 52  ? 0.1408 0.1495 0.1768 0.0079  -0.0108 -0.0072 52  ALA   B C   
5034 O O   . ALA   B 52  ? 0.1451 0.1602 0.2188 0.0070  -0.0075 -0.0003 52  ALA   B O   
5035 C CB  . ALA   B 52  ? 0.1722 0.1576 0.2080 0.0105  0.0021  -0.0139 52  ALA   B CB  
5041 N N   . LEU   B 53  ? 0.1436 0.1498 0.1649 0.0133  -0.0052 0.0007  53  LEU   B N   
5042 C CA  . LEU   B 53  ? 0.1459 0.1610 0.1739 0.0095  -0.0158 -0.0049 53  LEU   B CA  
5043 C C   . LEU   B 53  ? 0.1552 0.1516 0.1696 0.0075  -0.0036 0.0090  53  LEU   B C   
5044 O O   . LEU   B 53  ? 0.1621 0.1588 0.1731 -0.0004 0.0045  0.0109  53  LEU   B O   
5045 C CB  . LEU   B 53  ? 0.1461 0.1650 0.1879 0.0094  -0.0105 0.0024  53  LEU   B CB  
5046 C CG  . LEU   B 53  ? 0.1443 0.1692 0.1841 0.0022  -0.0033 0.0147  53  LEU   B CG  
5047 C CD1 . LEU   B 53  ? 0.1518 0.1924 0.2114 0.0069  -0.0091 0.0057  53  LEU   B CD1 
5048 C CD2 . LEU   B 53  ? 0.1594 0.2027 0.2070 -0.0047 -0.0105 -0.0134 53  LEU   B CD2 
5060 N N   . ASN   B 54  ? 0.1539 0.1383 0.1619 0.0005  -0.0114 0.0114  54  ASN   B N   
5061 C CA  . ASN   B 54  ? 0.1573 0.1575 0.1920 -0.0009 0.0008  0.0078  54  ASN   B CA  
5062 C C   . ASN   B 54  ? 0.1516 0.1601 0.2062 -0.0012 0.0117  0.0025  54  ASN   B C   
5063 O O   . ASN   B 54  ? 0.1498 0.1602 0.1952 -0.0022 0.0046  0.0025  54  ASN   B O   
5064 C CB  . ASN   B 54  ? 0.1595 0.1757 0.1937 0.0091  0.0031  0.0135  54  ASN   B CB  
5065 C CG  . ASN   B 54  ? 0.1588 0.1807 0.1949 0.0074  -0.0135 0.0032  54  ASN   B CG  
5066 O OD1 . ASN   B 54  ? 0.1487 0.1766 0.2055 0.0043  -0.0101 -0.0118 54  ASN   B OD1 
5067 N ND2 . ASN   B 54  ? 0.1751 0.1970 0.2201 0.0041  -0.0396 0.0012  54  ASN   B ND2 
5074 N N   . LYS   B 55  ? 0.1492 0.1669 0.2238 0.0057  0.0005  0.0023  55  LYS   B N   
5075 C CA  . LYS   B 55  ? 0.1484 0.1807 0.2433 0.0114  0.0089  -0.0051 55  LYS   B CA  
5076 C C   . LYS   B 55  ? 0.1462 0.1744 0.2492 0.0105  0.0143  -0.0088 55  LYS   B C   
5077 O O   . LYS   B 55  ? 0.1478 0.1880 0.2630 0.0134  0.0055  -0.0010 55  LYS   B O   
5078 C CB  . LYS   B 55  ? 0.1655 0.1957 0.2783 0.0238  0.0127  -0.0074 55  LYS   B CB  
5079 C CG  . LYS   B 55  ? 0.2096 0.2283 0.3389 0.0248  0.0244  0.0055  55  LYS   B CG  
5080 C CD  . LYS   B 55  ? 0.2577 0.2606 0.4099 0.0425  0.0432  0.0176  55  LYS   B CD  
5081 C CE  . LYS   B 55  ? 0.2922 0.2881 0.4731 0.0538  0.0604  0.0237  55  LYS   B CE  
5082 N NZ  . LYS   B 55  ? 0.3085 0.3104 0.5122 0.0537  0.0411  0.0473  55  LYS   B NZ  
5096 N N   . ALA   B 56  ? 0.1475 0.1775 0.2362 0.0015  0.0076  -0.0028 56  ALA   B N   
5097 C CA  . ALA   B 56  ? 0.1565 0.1919 0.2323 -0.0028 0.0107  -0.0035 56  ALA   B CA  
5098 C C   . ALA   B 56  ? 0.1600 0.1936 0.2123 -0.0026 0.0223  -0.0035 56  ALA   B C   
5099 O O   . ALA   B 56  ? 0.1704 0.2001 0.2305 -0.0047 0.0369  -0.0017 56  ALA   B O   
5100 C CB  . ALA   B 56  ? 0.1731 0.2094 0.2288 -0.0051 -0.0017 0.0040  56  ALA   B CB  
5106 N N   . THR   B 57  ? 0.1489 0.1823 0.2165 -0.0051 0.0236  -0.0085 57  THR   B N   
5107 C CA  . THR   B 57  ? 0.1546 0.1808 0.2296 -0.0074 0.0161  -0.0065 57  THR   B CA  
5108 C C   . THR   B 57  ? 0.1546 0.1943 0.2422 0.0000  0.0180  0.0071  57  THR   B C   
5109 O O   . THR   B 57  ? 0.1671 0.1936 0.2309 -0.0192 0.0161  -0.0059 57  THR   B O   
5110 C CB  . THR   B 57  ? 0.1679 0.1648 0.2000 -0.0028 0.0091  -0.0051 57  THR   B CB  
5111 O OG1 . THR   B 57  ? 0.1651 0.1605 0.2203 -0.0082 0.0032  0.0031  57  THR   B OG1 
5112 C CG2 . THR   B 57  ? 0.1674 0.1673 0.1933 -0.0032 0.0154  -0.0059 57  THR   B CG2 
5120 N N   . ASN   B 58  ? 0.1396 0.2146 0.2508 -0.0103 0.0198  -0.0155 58  ASN   B N   
5121 C CA  . ASN   B 58  ? 0.1624 0.2582 0.2936 -0.0273 0.0394  -0.0025 58  ASN   B CA  
5122 C C   . ASN   B 58  ? 0.1491 0.2372 0.2569 -0.0212 -0.0090 0.0057  58  ASN   B C   
5123 O O   . ASN   B 58  ? 0.1598 0.2437 0.2655 -0.0272 -0.0116 -0.0099 58  ASN   B O   
5124 C CB  . ASN   B 58  ? 0.2417 0.3276 0.3872 -0.0407 0.0902  -0.0013 58  ASN   B CB  
5125 C CG  . ASN   B 58  ? 0.3857 0.4303 0.5234 -0.0479 0.1035  0.0215  58  ASN   B CG  
5126 O OD1 . ASN   B 58  ? 0.4044 0.4327 0.5732 -0.0481 0.1011  0.0293  58  ASN   B OD1 
5127 N ND2 . ASN   B 58  ? 0.5308 0.5308 0.5717 -0.0554 0.1119  0.0310  58  ASN   B ND2 
5134 N N   . ASN   B 59  ? 0.1544 0.2176 0.2344 -0.0126 -0.0146 0.0051  59  ASN   B N   
5135 C CA  . ASN   B 59  ? 0.1589 0.2134 0.2200 -0.0110 -0.0199 0.0043  59  ASN   B CA  
5136 C C   . ASN   B 59  ? 0.1527 0.1990 0.2177 -0.0158 -0.0177 -0.0099 59  ASN   B C   
5137 O O   . ASN   B 59  ? 0.1589 0.1988 0.2125 -0.0148 -0.0171 -0.0012 59  ASN   B O   
5138 C CB  . ASN   B 59  ? 0.1632 0.2280 0.2418 -0.0101 -0.0331 0.0055  59  ASN   B CB  
5139 C CG  . ASN   B 59  ? 0.1725 0.2475 0.2526 -0.0088 -0.0516 0.0110  59  ASN   B CG  
5140 O OD1 . ASN   B 59  ? 0.1794 0.2463 0.2531 -0.0063 -0.0418 0.0158  59  ASN   B OD1 
5141 N ND2 . ASN   B 59  ? 0.1857 0.2586 0.2510 -0.0156 -0.0496 0.0083  59  ASN   B ND2 
5148 N N   . ALA   B 60  ? 0.1533 0.1889 0.2302 -0.0187 0.0139  -0.0105 60  ALA   B N   
5149 C CA  . ALA   B 60  ? 0.1646 0.1823 0.2273 -0.0223 0.0116  -0.0079 60  ALA   B CA  
5150 C C   . ALA   B 60  ? 0.1690 0.1678 0.1951 -0.0191 -0.0048 -0.0039 60  ALA   B C   
5151 O O   . ALA   B 60  ? 0.1739 0.1681 0.2062 -0.0243 0.0003  -0.0084 60  ALA   B O   
5152 C CB  . ALA   B 60  ? 0.1793 0.1792 0.2588 -0.0267 0.0131  -0.0061 60  ALA   B CB  
5158 N N   . MET   B 61  ? 0.1580 0.1544 0.1895 -0.0119 0.0021  -0.0066 61  MET   B N   
5159 C CA  . MET   B 61  ? 0.1488 0.1562 0.1890 -0.0087 -0.0078 -0.0030 61  MET   B CA  
5160 C C   . MET   B 61  ? 0.1548 0.1557 0.1919 -0.0110 -0.0175 0.0004  61  MET   B C   
5161 O O   . MET   B 61  ? 0.1564 0.1549 0.1768 -0.0015 -0.0064 -0.0144 61  MET   B O   
5162 C CB  . MET   B 61  ? 0.1422 0.1571 0.1980 -0.0033 -0.0068 -0.0001 61  MET   B CB  
5163 C CG  . MET   B 61  ? 0.1440 0.1542 0.1923 0.0045  -0.0157 0.0004  61  MET   B CG  
5164 S SD  . MET   B 61  ? 0.1528 0.1528 0.2069 -0.0054 -0.0141 -0.0137 61  MET   B SD  
5165 C CE  . MET   B 61  ? 0.1641 0.1770 0.2217 -0.0025 -0.0088 -0.0310 61  MET   B CE  
5175 N N   . GLN   B 62  ? 0.1529 0.1696 0.1630 -0.0086 -0.0217 0.0090  62  GLN   B N   
5176 C CA  . GLN   B 62  ? 0.1584 0.1625 0.1714 0.0013  -0.0308 -0.0009 62  GLN   B CA  
5177 C C   . GLN   B 62  ? 0.1574 0.1623 0.1977 -0.0022 -0.0292 -0.0079 62  GLN   B C   
5178 O O   . GLN   B 62  ? 0.1680 0.1709 0.1935 -0.0035 -0.0264 -0.0209 62  GLN   B O   
5179 C CB  . GLN   B 62  ? 0.1632 0.1652 0.1862 0.0019  -0.0228 0.0090  62  GLN   B CB  
5180 C CG  . GLN   B 62  ? 0.1683 0.1706 0.2001 -0.0012 -0.0363 -0.0028 62  GLN   B CG  
5181 C CD  . GLN   B 62  ? 0.1705 0.1724 0.1927 0.0038  -0.0320 0.0014  62  GLN   B CD  
5182 O OE1 . GLN   B 62  ? 0.1677 0.1682 0.2045 0.0024  -0.0312 -0.0053 62  GLN   B OE1 
5183 N NE2 . GLN   B 62  ? 0.1772 0.1777 0.1785 0.0085  -0.0297 -0.0090 62  GLN   B NE2 
5192 N N   . VAL   B 63  ? 0.1593 0.1622 0.2009 -0.0098 -0.0255 -0.0171 63  VAL   B N   
5193 C CA  . VAL   B 63  ? 0.1717 0.1762 0.2366 -0.0128 -0.0305 -0.0095 63  VAL   B CA  
5194 C C   . VAL   B 63  ? 0.1713 0.1674 0.2090 -0.0223 -0.0427 -0.0236 63  VAL   B C   
5195 O O   . VAL   B 63  ? 0.1845 0.1593 0.2075 -0.0187 -0.0471 -0.0134 63  VAL   B O   
5196 C CB  . VAL   B 63  ? 0.1659 0.1936 0.2735 -0.0192 -0.0239 -0.0192 63  VAL   B CB  
5197 C CG1 . VAL   B 63  ? 0.1739 0.1991 0.2877 -0.0225 -0.0188 -0.0254 63  VAL   B CG1 
5198 C CG2 . VAL   B 63  ? 0.1575 0.2156 0.2887 -0.0137 -0.0226 -0.0207 63  VAL   B CG2 
5208 N N   . GLU   B 64  ? 0.1633 0.1574 0.2076 -0.0075 -0.0344 -0.0193 64  GLU   B N   
5209 C CA  . GLU   B 64  ? 0.1664 0.1491 0.2008 -0.0162 -0.0359 -0.0059 64  GLU   B CA  
5210 C C   . GLU   B 64  ? 0.1693 0.1433 0.1963 -0.0106 -0.0371 -0.0183 64  GLU   B C   
5211 O O   . GLU   B 64  ? 0.1731 0.1535 0.1798 -0.0116 -0.0286 -0.0200 64  GLU   B O   
5212 C CB  . GLU   B 64  ? 0.1669 0.1596 0.2061 -0.0215 -0.0311 0.0043  64  GLU   B CB  
5213 C CG  . GLU   B 64  ? 0.1825 0.1616 0.2168 -0.0271 -0.0348 -0.0152 64  GLU   B CG  
5214 C CD  . GLU   B 64  ? 0.1830 0.1687 0.2316 -0.0389 -0.0357 0.0043  64  GLU   B CD  
5215 O OE1 . GLU   B 64  ? 0.1853 0.1860 0.2426 -0.0292 -0.0257 -0.0153 64  GLU   B OE1 
5216 O OE2 . GLU   B 64  ? 0.1994 0.1792 0.2239 -0.0388 -0.0463 0.0025  64  GLU   B OE2 
5223 N N   . SER   B 65  ? 0.1639 0.1469 0.1816 -0.0130 -0.0262 -0.0159 65  SER   B N   
5224 C CA  . SER   B 65  ? 0.1656 0.1511 0.1885 0.0031  -0.0171 -0.0128 65  SER   B CA  
5225 C C   . SER   B 65  ? 0.1750 0.1521 0.1801 0.0015  -0.0250 -0.0133 65  SER   B C   
5226 O O   . SER   B 65  ? 0.1730 0.1592 0.1701 0.0012  -0.0179 -0.0253 65  SER   B O   
5227 C CB  . SER   B 65  ? 0.1648 0.1457 0.2003 -0.0122 -0.0139 -0.0047 65  SER   B CB  
5228 O OG  . SER   B 65  ? 0.1697 0.1472 0.1858 -0.0107 -0.0169 -0.0144 65  SER   B OG  
5234 N N   . ASP   B 66  ? 0.1799 0.1630 0.1685 -0.0034 -0.0293 -0.0162 66  ASP   B N   
5235 C CA  . ASP   B 66  ? 0.1876 0.1656 0.1713 0.0045  -0.0392 -0.0133 66  ASP   B CA  
5236 C C   . ASP   B 66  ? 0.1988 0.1723 0.1838 -0.0022 -0.0395 -0.0210 66  ASP   B C   
5237 O O   . ASP   B 66  ? 0.2037 0.1726 0.1863 0.0012  -0.0289 -0.0310 66  ASP   B O   
5238 C CB  . ASP   B 66  ? 0.1984 0.1833 0.2154 0.0127  -0.0621 -0.0233 66  ASP   B CB  
5239 C CG  . ASP   B 66  ? 0.2218 0.2024 0.2169 0.0233  -0.0663 -0.0047 66  ASP   B CG  
5240 O OD1 . ASP   B 66  ? 0.2500 0.2064 0.2436 0.0191  -0.0632 0.0024  66  ASP   B OD1 
5241 O OD2 . ASP   B 66  ? 0.2410 0.2254 0.2876 0.0364  -0.0567 -0.0010 66  ASP   B OD2 
5246 N N   . ASP   B 67  ? 0.1918 0.1618 0.1635 -0.0112 -0.0395 -0.0242 67  ASP   B N   
5247 C CA  . ASP   B 67  ? 0.2007 0.1593 0.1976 -0.0161 -0.0443 -0.0148 67  ASP   B CA  
5248 C C   . ASP   B 67  ? 0.1952 0.1628 0.2031 -0.0029 -0.0360 -0.0164 67  ASP   B C   
5249 O O   . ASP   B 67  ? 0.1992 0.1709 0.1969 -0.0011 -0.0130 -0.0322 67  ASP   B O   
5250 C CB  . ASP   B 67  ? 0.2197 0.1671 0.2275 -0.0197 -0.0493 -0.0081 67  ASP   B CB  
5251 C CG  . ASP   B 67  ? 0.2538 0.1723 0.2324 -0.0156 -0.0743 -0.0043 67  ASP   B CG  
5252 O OD1 . ASP   B 67  ? 0.2825 0.1880 0.2357 -0.0157 -0.0729 -0.0051 67  ASP   B OD1 
5253 O OD2 . ASP   B 67  ? 0.2671 0.1870 0.2410 0.0017  -0.0731 0.0034  67  ASP   B OD2 
5258 N N   . TYR   B 68  ? 0.1914 0.1626 0.2042 -0.0025 -0.0441 -0.0256 68  TYR   B N   
5259 C CA  . TYR   B 68  ? 0.1848 0.1728 0.2363 0.0111  -0.0441 -0.0287 68  TYR   B CA  
5260 C C   . TYR   B 68  ? 0.1752 0.1666 0.1990 0.0057  -0.0363 -0.0271 68  TYR   B C   
5261 O O   . TYR   B 68  ? 0.1906 0.1761 0.2049 0.0109  -0.0277 -0.0515 68  TYR   B O   
5262 C CB  . TYR   B 68  ? 0.1881 0.1918 0.2200 0.0119  -0.0539 -0.0460 68  TYR   B CB  
5263 C CG  . TYR   B 68  ? 0.2049 0.2172 0.2194 0.0187  -0.0404 -0.0623 68  TYR   B CG  
5264 C CD1 . TYR   B 68  ? 0.2079 0.2212 0.2478 0.0047  -0.0389 -0.0788 68  TYR   B CD1 
5265 C CD2 . TYR   B 68  ? 0.2067 0.2456 0.2402 0.0262  -0.0617 -0.0581 68  TYR   B CD2 
5266 C CE1 . TYR   B 68  ? 0.2099 0.2450 0.2731 0.0055  -0.0271 -0.0825 68  TYR   B CE1 
5267 C CE2 . TYR   B 68  ? 0.1982 0.2514 0.2730 0.0222  -0.0442 -0.0866 68  TYR   B CE2 
5268 C CZ  . TYR   B 68  ? 0.1945 0.2543 0.2832 0.0125  -0.0295 -0.0843 68  TYR   B CZ  
5269 O OH  . TYR   B 68  ? 0.1904 0.2733 0.3264 -0.0005 -0.0296 -0.0562 68  TYR   B OH  
5279 N N   . ILE   B 69  ? 0.1741 0.1681 0.1945 0.0014  -0.0336 -0.0295 69  ILE   B N   
5280 C CA  . ILE   B 69  ? 0.1851 0.1732 0.2122 -0.0023 -0.0222 -0.0327 69  ILE   B CA  
5281 C C   . ILE   B 69  ? 0.1831 0.1690 0.2013 0.0077  -0.0346 -0.0295 69  ILE   B C   
5282 O O   . ILE   B 69  ? 0.1956 0.1885 0.1783 0.0118  -0.0251 -0.0328 69  ILE   B O   
5283 C CB  . ILE   B 69  ? 0.1927 0.1700 0.2264 0.0011  0.0090  -0.0297 69  ILE   B CB  
5284 C CG1 . ILE   B 69  ? 0.1894 0.1786 0.2430 -0.0061 0.0165  -0.0319 69  ILE   B CG1 
5285 C CG2 . ILE   B 69  ? 0.2079 0.1768 0.2395 -0.0054 0.0053  -0.0324 69  ILE   B CG2 
5286 C CD1 . ILE   B 69  ? 0.1899 0.1879 0.2644 -0.0151 0.0161  -0.0304 69  ILE   B CD1 
5298 N N   . ALA   B 70  ? 0.1802 0.1647 0.2131 0.0086  -0.0344 -0.0228 70  ALA   B N   
5299 C CA  . ALA   B 70  ? 0.1828 0.1702 0.1945 0.0050  -0.0473 -0.0289 70  ALA   B CA  
5300 C C   . ALA   B 70  ? 0.1955 0.1689 0.2058 0.0014  -0.0456 -0.0401 70  ALA   B C   
5301 O O   . ALA   B 70  ? 0.2100 0.1693 0.2204 0.0075  -0.0369 -0.0377 70  ALA   B O   
5302 C CB  . ALA   B 70  ? 0.1789 0.1863 0.1923 0.0048  -0.0436 -0.0377 70  ALA   B CB  
5308 N N   . THR   B 71  ? 0.2060 0.1679 0.2004 0.0065  -0.0531 -0.0385 71  THR   B N   
5309 C CA  . THR   B 71  ? 0.2113 0.1727 0.2179 0.0101  -0.0612 -0.0400 71  THR   B CA  
5310 C C   . THR   B 71  ? 0.2012 0.1796 0.2648 0.0247  -0.0601 -0.0520 71  THR   B C   
5311 O O   . THR   B 71  ? 0.2123 0.1866 0.2990 0.0356  -0.0547 -0.0643 71  THR   B O   
5312 C CB  . THR   B 71  ? 0.2345 0.1936 0.2545 0.0029  -0.0699 -0.0160 71  THR   B CB  
5313 O OG1 . THR   B 71  ? 0.2476 0.2169 0.2904 -0.0153 -0.0674 0.0055  71  THR   B OG1 
5314 C CG2 . THR   B 71  ? 0.2505 0.1883 0.2712 0.0021  -0.0568 -0.0158 71  THR   B CG2 
5322 N N   . ASN   B 72  ? 0.1942 0.1878 0.2632 0.0168  -0.0672 -0.0590 72  ASN   B N   
5323 C CA  . ASN   B 72  ? 0.1902 0.2017 0.2651 0.0131  -0.0516 -0.0800 72  ASN   B CA  
5324 C C   . ASN   B 72  ? 0.1884 0.2166 0.2621 -0.0016 -0.0278 -0.0760 72  ASN   B C   
5325 O O   . ASN   B 72  ? 0.1948 0.2272 0.3154 0.0018  -0.0120 -0.0823 72  ASN   B O   
5326 C CB  . ASN   B 72  ? 0.1928 0.2178 0.2810 0.0111  -0.0690 -0.0614 72  ASN   B CB  
5327 C CG  . ASN   B 72  ? 0.2138 0.2298 0.2768 0.0225  -0.0708 -0.0362 72  ASN   B CG  
5328 O OD1 . ASN   B 72  ? 0.2428 0.2538 0.2754 0.0099  -0.0489 -0.0473 72  ASN   B OD1 
5329 N ND2 . ASN   B 72  ? 0.2211 0.2370 0.3235 0.0381  -0.0598 0.0081  72  ASN   B ND2 
5336 N N   . GLY   B 73  ? 0.1920 0.2144 0.2499 -0.0072 -0.0281 -0.0763 73  GLY   B N   
5337 C CA  . GLY   B 73  ? 0.1878 0.2216 0.2156 -0.0039 -0.0141 -0.0684 73  GLY   B CA  
5338 C C   . GLY   B 73  ? 0.1843 0.2122 0.1832 0.0050  -0.0205 -0.0593 73  GLY   B C   
5339 O O   . GLY   B 73  ? 0.1825 0.1975 0.1873 0.0087  -0.0207 -0.0496 73  GLY   B O   
5343 N N   . PRO   B 74  ? 0.1824 0.2177 0.1769 0.0018  -0.0236 -0.0380 74  PRO   B N   
5344 C CA  . PRO   B 74  ? 0.1818 0.2121 0.1588 0.0107  -0.0155 -0.0235 74  PRO   B CA  
5345 C C   . PRO   B 74  ? 0.1671 0.1987 0.1811 0.0059  -0.0181 -0.0159 74  PRO   B C   
5346 O O   . PRO   B 74  ? 0.1674 0.2047 0.2350 0.0045  -0.0050 -0.0292 74  PRO   B O   
5347 C CB  . PRO   B 74  ? 0.1966 0.2237 0.1772 0.0121  -0.0169 -0.0144 74  PRO   B CB  
5348 C CG  . PRO   B 74  ? 0.2150 0.2365 0.2090 0.0098  -0.0088 -0.0156 74  PRO   B CG  
5349 C CD  . PRO   B 74  ? 0.2109 0.2279 0.1980 0.0107  -0.0157 -0.0246 74  PRO   B CD  
5357 N N   . LEU   B 75  ? 0.1672 0.1885 0.1634 0.0059  -0.0232 -0.0180 75  LEU   B N   
5358 C CA  . LEU   B 75  ? 0.1754 0.1823 0.1664 0.0013  -0.0246 -0.0048 75  LEU   B CA  
5359 C C   . LEU   B 75  ? 0.1760 0.1969 0.1612 0.0055  -0.0075 -0.0073 75  LEU   B C   
5360 O O   . LEU   B 75  ? 0.1874 0.2144 0.1697 0.0049  -0.0069 -0.0072 75  LEU   B O   
5361 C CB  . LEU   B 75  ? 0.1785 0.1891 0.1472 -0.0124 -0.0277 0.0028  75  LEU   B CB  
5362 C CG  . LEU   B 75  ? 0.2089 0.2062 0.1839 -0.0337 -0.0092 0.0109  75  LEU   B CG  
5363 C CD1 . LEU   B 75  ? 0.2418 0.2236 0.1954 -0.0448 0.0092  -0.0074 75  LEU   B CD1 
5364 C CD2 . LEU   B 75  ? 0.2483 0.2316 0.2506 -0.0270 0.0038  0.0193  75  LEU   B CD2 
5376 N N   . LYS   B 76  ? 0.1785 0.2222 0.2003 -0.0007 -0.0049 0.0168  76  LYS   B N   
5377 C CA  . LYS   B 76  ? 0.1880 0.2269 0.2367 -0.0157 0.0195  0.0127  76  LYS   B CA  
5378 C C   . LYS   B 76  ? 0.1745 0.2099 0.2125 -0.0068 0.0163  0.0444  76  LYS   B C   
5379 O O   . LYS   B 76  ? 0.1798 0.1869 0.2060 -0.0010 0.0054  0.0276  76  LYS   B O   
5380 C CB  . LYS   B 76  ? 0.1994 0.2280 0.2774 -0.0185 0.0439  -0.0185 76  LYS   B CB  
5381 C CG  . LYS   B 76  ? 0.2016 0.2452 0.3102 -0.0087 0.0409  -0.0186 76  LYS   B CG  
5382 C CD  . LYS   B 76  ? 0.2038 0.2541 0.3349 -0.0021 0.0417  -0.0381 76  LYS   B CD  
5383 C CE  . LYS   B 76  ? 0.2192 0.2703 0.3875 0.0012  0.0187  -0.0466 76  LYS   B CE  
5384 N NZ  . LYS   B 76  ? 0.2181 0.2727 0.4102 -0.0036 -0.0084 -0.0663 76  LYS   B NZ  
5398 N N   . VAL   B 77  ? 0.1858 0.2212 0.2153 -0.0026 0.0193  0.0449  77  VAL   B N   
5399 C CA  . VAL   B 77  ? 0.1938 0.2118 0.2185 0.0039  0.0247  0.0659  77  VAL   B CA  
5400 C C   . VAL   B 77  ? 0.1767 0.1957 0.1885 0.0059  0.0382  0.0489  77  VAL   B C   
5401 O O   . VAL   B 77  ? 0.1824 0.1949 0.1978 0.0147  0.0352  0.0336  77  VAL   B O   
5402 C CB  . VAL   B 77  ? 0.2071 0.2146 0.2610 0.0130  0.0291  0.0813  77  VAL   B CB  
5403 C CG1 . VAL   B 77  ? 0.2094 0.2031 0.2918 0.0086  0.0206  0.0875  77  VAL   B CG1 
5404 C CG2 . VAL   B 77  ? 0.2262 0.2349 0.2651 0.0061  0.0115  0.0770  77  VAL   B CG2 
5414 N N   . GLY   B 78  ? 0.1633 0.1764 0.1893 0.0053  0.0225  0.0310  78  GLY   B N   
5415 C CA  . GLY   B 78  ? 0.1661 0.1716 0.1892 0.0036  0.0318  0.0298  78  GLY   B CA  
5416 C C   . GLY   B 78  ? 0.1667 0.1666 0.1891 0.0105  0.0228  0.0313  78  GLY   B C   
5417 O O   . GLY   B 78  ? 0.1614 0.1655 0.2016 0.0142  0.0159  0.0315  78  GLY   B O   
5421 N N   . GLY   B 79  ? 0.1545 0.1693 0.1984 0.0020  0.0093  0.0206  79  GLY   B N   
5422 C CA  . GLY   B 79  ? 0.1579 0.1557 0.2146 0.0064  0.0040  0.0235  79  GLY   B CA  
5423 C C   . GLY   B 79  ? 0.1480 0.1516 0.1984 0.0116  0.0081  0.0161  79  GLY   B C   
5424 O O   . GLY   B 79  ? 0.1572 0.1524 0.2033 0.0102  0.0178  0.0264  79  GLY   B O   
5428 N N   . SER   B 80  ? 0.1478 0.1474 0.2037 0.0123  0.0161  0.0181  80  SER   B N   
5429 C CA  . SER   B 80  ? 0.1456 0.1440 0.1878 0.0027  0.0056  0.0114  80  SER   B CA  
5430 C C   . SER   B 80  ? 0.1494 0.1421 0.1741 0.0107  -0.0023 0.0097  80  SER   B C   
5431 O O   . SER   B 80  ? 0.1575 0.1470 0.2104 0.0107  0.0029  -0.0019 80  SER   B O   
5432 C CB  . SER   B 80  ? 0.1472 0.1502 0.1996 -0.0012 0.0105  0.0099  80  SER   B CB  
5433 O OG  . SER   B 80  ? 0.1540 0.1634 0.2285 -0.0050 -0.0030 0.0170  80  SER   B OG  
5439 N N   . CYS   B 81  ? 0.1439 0.1314 0.1824 0.0021  -0.0063 0.0004  81  CYS   B N   
5440 C CA  . CYS   B 81  ? 0.1441 0.1257 0.1959 0.0053  -0.0061 0.0047  81  CYS   B CA  
5441 C C   . CYS   B 81  ? 0.1435 0.1251 0.1762 0.0003  -0.0059 0.0031  81  CYS   B C   
5442 O O   . CYS   B 81  ? 0.1682 0.1231 0.1936 0.0078  -0.0045 0.0037  81  CYS   B O   
5443 C CB  . CYS   B 81  ? 0.1578 0.1420 0.1990 -0.0037 -0.0069 0.0079  81  CYS   B CB  
5444 S SG  . CYS   B 81  ? 0.1661 0.1633 0.2004 -0.0034 -0.0218 -0.0076 81  CYS   B SG  
5450 N N   . VAL   B 82  ? 0.1527 0.1271 0.1890 -0.0001 -0.0034 0.0021  82  VAL   B N   
5451 C CA  . VAL   B 82  ? 0.1585 0.1300 0.1885 -0.0090 -0.0090 0.0033  82  VAL   B CA  
5452 C C   . VAL   B 82  ? 0.1681 0.1287 0.1968 -0.0071 -0.0112 0.0023  82  VAL   B C   
5453 O O   . VAL   B 82  ? 0.1719 0.1317 0.2054 -0.0085 -0.0175 -0.0127 82  VAL   B O   
5454 C CB  . VAL   B 82  ? 0.1630 0.1546 0.2103 -0.0031 -0.0183 0.0131  82  VAL   B CB  
5455 C CG1 . VAL   B 82  ? 0.1893 0.1828 0.2134 0.0001  -0.0121 0.0314  82  VAL   B CG1 
5456 C CG2 . VAL   B 82  ? 0.1761 0.1666 0.2238 -0.0065 -0.0342 0.0147  82  VAL   B CG2 
5466 N N   . LEU   B 83  ? 0.1524 0.1285 0.1762 -0.0113 -0.0170 -0.0107 83  LEU   B N   
5467 C CA  . LEU   B 83  ? 0.1473 0.1384 0.1820 -0.0122 -0.0184 -0.0111 83  LEU   B CA  
5468 C C   . LEU   B 83  ? 0.1464 0.1340 0.1968 -0.0178 -0.0229 0.0068  83  LEU   B C   
5469 O O   . LEU   B 83  ? 0.1517 0.1417 0.1533 -0.0222 -0.0150 0.0090  83  LEU   B O   
5470 C CB  . LEU   B 83  ? 0.1528 0.1467 0.1885 -0.0111 -0.0230 -0.0112 83  LEU   B CB  
5471 C CG  . LEU   B 83  ? 0.1728 0.1716 0.1742 -0.0147 -0.0195 -0.0082 83  LEU   B CG  
5472 C CD1 . LEU   B 83  ? 0.1912 0.1790 0.1758 -0.0115 -0.0278 -0.0052 83  LEU   B CD1 
5473 C CD2 . LEU   B 83  ? 0.1975 0.1723 0.2012 -0.0076 -0.0295 -0.0250 83  LEU   B CD2 
5485 N N   . SER   B 84  ? 0.1583 0.1401 0.2145 -0.0267 -0.0233 0.0077  84  SER   B N   
5486 C CA  . SER   B 84  ? 0.1599 0.1650 0.1994 -0.0281 -0.0112 0.0222  84  SER   B CA  
5487 C C   . SER   B 84  ? 0.1474 0.1787 0.1462 -0.0265 -0.0235 0.0115  84  SER   B C   
5488 O O   . SER   B 84  ? 0.1550 0.1678 0.1264 -0.0185 -0.0108 0.0005  84  SER   B O   
5489 C CB  . SER   B 84  ? 0.1736 0.1724 0.2332 -0.0315 0.0069  0.0196  84  SER   B CB  
5490 O OG  . SER   B 84  ? 0.1744 0.1873 0.2744 -0.0424 -0.0007 0.0225  84  SER   B OG  
5496 N N   . GLY   B 85  ? 0.1565 0.1908 0.1554 -0.0246 -0.0201 0.0229  85  GLY   B N   
5497 C CA  . GLY   B 85  ? 0.1536 0.1960 0.1845 -0.0376 -0.0053 -0.0002 85  GLY   B CA  
5498 C C   . GLY   B 85  ? 0.1524 0.1892 0.1778 -0.0379 -0.0069 0.0078  85  GLY   B C   
5499 O O   . GLY   B 85  ? 0.1611 0.1870 0.1680 -0.0470 0.0006  -0.0081 85  GLY   B O   
5503 N N   . HIS   B 86  ? 0.1492 0.1714 0.1804 -0.0322 -0.0177 0.0172  86  HIS   B N   
5504 C CA  . HIS   B 86  ? 0.1563 0.1783 0.1782 -0.0307 -0.0176 0.0178  86  HIS   B CA  
5505 C C   . HIS   B 86  ? 0.1596 0.1911 0.1754 -0.0412 -0.0025 0.0387  86  HIS   B C   
5506 O O   . HIS   B 86  ? 0.1787 0.2057 0.1669 -0.0410 0.0006  0.0313  86  HIS   B O   
5507 C CB  . HIS   B 86  ? 0.1655 0.1847 0.1984 -0.0236 -0.0228 0.0041  86  HIS   B CB  
5508 C CG  . HIS   B 86  ? 0.1665 0.1899 0.1900 -0.0112 -0.0263 0.0062  86  HIS   B CG  
5509 N ND1 . HIS   B 86  ? 0.1738 0.2115 0.2195 -0.0164 -0.0339 -0.0137 86  HIS   B ND1 
5510 C CD2 . HIS   B 86  ? 0.1685 0.1884 0.1941 -0.0018 -0.0203 0.0031  86  HIS   B CD2 
5511 C CE1 . HIS   B 86  ? 0.1882 0.2017 0.2013 -0.0071 -0.0075 -0.0417 86  HIS   B CE1 
5512 N NE2 . HIS   B 86  ? 0.1831 0.1954 0.1809 0.0079  -0.0107 -0.0127 86  HIS   B NE2 
5520 N N   . ASN   B 87  ? 0.1600 0.1925 0.1925 -0.0282 0.0073  0.0235  87  ASN   B N   
5521 C CA  . ASN   B 87  ? 0.1637 0.2062 0.2077 -0.0273 0.0277  0.0203  87  ASN   B CA  
5522 C C   . ASN   B 87  ? 0.1821 0.1908 0.2161 -0.0288 0.0359  0.0117  87  ASN   B C   
5523 O O   . ASN   B 87  ? 0.2127 0.2003 0.2366 -0.0282 0.0506  0.0121  87  ASN   B O   
5524 C CB  . ASN   B 87  ? 0.1682 0.2452 0.2268 -0.0252 0.0254  0.0146  87  ASN   B CB  
5525 C CG  . ASN   B 87  ? 0.1761 0.2636 0.2330 0.0029  0.0297  0.0398  87  ASN   B CG  
5526 O OD1 . ASN   B 87  ? 0.1643 0.2552 0.2129 0.0074  0.0501  0.0531  87  ASN   B OD1 
5527 N ND2 . ASN   B 87  ? 0.2132 0.2684 0.2753 0.0092  0.0354  0.0282  87  ASN   B ND2 
5534 N N   . LEU   B 88  ? 0.1700 0.1820 0.1802 -0.0311 0.0146  0.0070  88  LEU   B N   
5535 C CA  . LEU   B 88  ? 0.1821 0.1725 0.1821 -0.0369 0.0046  0.0040  88  LEU   B CA  
5536 C C   . LEU   B 88  ? 0.1801 0.1573 0.1888 -0.0436 -0.0064 0.0029  88  LEU   B C   
5537 O O   . LEU   B 88  ? 0.2054 0.1628 0.2275 -0.0237 -0.0238 0.0012  88  LEU   B O   
5538 C CB  . LEU   B 88  ? 0.2017 0.1788 0.1931 -0.0494 0.0037  0.0100  88  LEU   B CB  
5539 C CG  . LEU   B 88  ? 0.2427 0.2024 0.2202 -0.0428 -0.0216 0.0235  88  LEU   B CG  
5540 C CD1 . LEU   B 88  ? 0.2564 0.2344 0.2342 -0.0521 -0.0177 0.0490  88  LEU   B CD1 
5541 C CD2 . LEU   B 88  ? 0.2822 0.2262 0.2715 -0.0026 -0.0452 0.0003  88  LEU   B CD2 
5553 N N   . ALA   B 89  ? 0.1698 0.1609 0.1529 -0.0400 0.0221  0.0030  89  ALA   B N   
5554 C CA  . ALA   B 89  ? 0.1626 0.1601 0.1392 -0.0396 0.0060  0.0173  89  ALA   B CA  
5555 C C   . ALA   B 89  ? 0.1732 0.1623 0.1603 -0.0443 0.0097  0.0116  89  ALA   B C   
5556 O O   . ALA   B 89  ? 0.1569 0.1704 0.1839 -0.0418 0.0077  -0.0270 89  ALA   B O   
5557 C CB  . ALA   B 89  ? 0.1560 0.1641 0.1446 -0.0393 0.0051  0.0134  89  ALA   B CB  
5563 N N   . LYS   B 90  ? 0.2085 0.1507 0.1698 -0.0423 -0.0122 0.0192  90  LYS   B N   
5564 C CA  . LYS   B 90  ? 0.2197 0.1496 0.1574 -0.0428 -0.0202 0.0127  90  LYS   B CA  
5565 C C   . LYS   B 90  ? 0.1991 0.1433 0.1540 -0.0437 -0.0192 0.0044  90  LYS   B C   
5566 O O   . LYS   B 90  ? 0.2096 0.1601 0.1697 -0.0527 -0.0005 0.0041  90  LYS   B O   
5567 C CB  . LYS   B 90  ? 0.2321 0.1567 0.1946 -0.0358 -0.0199 0.0197  90  LYS   B CB  
5568 C CG  . LYS   B 90  ? 0.2246 0.1708 0.2028 -0.0193 0.0071  0.0190  90  LYS   B CG  
5569 C CD  . LYS   B 90  ? 0.2550 0.1911 0.2485 -0.0042 0.0229  -0.0017 90  LYS   B CD  
5570 C CE  . LYS   B 90  ? 0.2687 0.2045 0.2857 -0.0116 0.0417  -0.0113 90  LYS   B CE  
5571 N NZ  . LYS   B 90  ? 0.2697 0.1941 0.2717 -0.0259 0.0690  -0.0165 90  LYS   B NZ  
5585 N N   . HIS   B 91  ? 0.1770 0.1379 0.1471 -0.0343 -0.0206 0.0116  91  HIS   B N   
5586 C CA  . HIS   B 91  ? 0.1617 0.1328 0.1760 -0.0257 -0.0235 0.0113  91  HIS   B CA  
5587 C C   . HIS   B 91  ? 0.1549 0.1357 0.1564 -0.0273 -0.0053 0.0252  91  HIS   B C   
5588 O O   . HIS   B 91  ? 0.1670 0.1341 0.1478 -0.0227 -0.0233 0.0039  91  HIS   B O   
5589 C CB  . HIS   B 91  ? 0.1736 0.1335 0.2244 -0.0125 -0.0230 0.0132  91  HIS   B CB  
5590 C CG  . HIS   B 91  ? 0.2161 0.1623 0.2835 0.0039  0.0028  0.0244  91  HIS   B CG  
5591 N ND1 . HIS   B 91  ? 0.2438 0.1714 0.3384 0.0029  0.0177  0.0090  91  HIS   B ND1 
5592 C CD2 . HIS   B 91  ? 0.2277 0.1928 0.3248 0.0189  -0.0042 0.0637  91  HIS   B CD2 
5593 C CE1 . HIS   B 91  ? 0.2474 0.1854 0.3624 0.0193  0.0212  0.0176  91  HIS   B CE1 
5594 N NE2 . HIS   B 91  ? 0.2448 0.1964 0.3613 0.0311  0.0103  0.0698  91  HIS   B NE2 
5602 N N   . CYS   B 92  ? 0.1470 0.1349 0.1482 -0.0275 -0.0164 0.0102  92  CYS   B N   
5603 C CA  . CYS   B 92  ? 0.1492 0.1350 0.1258 -0.0205 -0.0038 0.0048  92  CYS   B CA  
5604 C C   . CYS   B 92  ? 0.1381 0.1283 0.1442 -0.0210 -0.0080 0.0024  92  CYS   B C   
5605 O O   . CYS   B 92  ? 0.1546 0.1389 0.1530 -0.0159 -0.0054 -0.0033 92  CYS   B O   
5606 C CB  . CYS   B 92  ? 0.1522 0.1382 0.1452 -0.0111 -0.0022 -0.0018 92  CYS   B CB  
5607 S SG  . CYS   B 92  ? 0.1498 0.1436 0.1467 -0.0118 -0.0090 0.0049  92  CYS   B SG  
5613 N N   . LEU   B 93  ? 0.1332 0.1277 0.1451 -0.0112 -0.0079 -0.0012 93  LEU   B N   
5614 C CA  . LEU   B 93  ? 0.1338 0.1279 0.1470 -0.0035 -0.0188 0.0126  93  LEU   B CA  
5615 C C   . LEU   B 93  ? 0.1320 0.1263 0.1419 -0.0083 -0.0046 0.0155  93  LEU   B C   
5616 O O   . LEU   B 93  ? 0.1433 0.1245 0.1538 -0.0078 -0.0083 0.0006  93  LEU   B O   
5617 C CB  . LEU   B 93  ? 0.1440 0.1270 0.1809 -0.0008 -0.0092 0.0140  93  LEU   B CB  
5618 C CG  . LEU   B 93  ? 0.1340 0.1418 0.1923 -0.0035 -0.0080 0.0112  93  LEU   B CG  
5619 C CD1 . LEU   B 93  ? 0.1404 0.1529 0.1980 0.0107  -0.0068 -0.0019 93  LEU   B CD1 
5620 C CD2 . LEU   B 93  ? 0.1376 0.1439 0.1886 0.0029  -0.0232 0.0001  93  LEU   B CD2 
5632 N N   . HIS   B 94  ? 0.1441 0.1253 0.1236 -0.0061 -0.0170 0.0151  94  HIS   B N   
5633 C CA  . HIS   B 94  ? 0.1415 0.1244 0.1483 -0.0048 -0.0124 0.0085  94  HIS   B CA  
5634 C C   . HIS   B 94  ? 0.1454 0.1265 0.1795 0.0004  -0.0047 0.0123  94  HIS   B C   
5635 O O   . HIS   B 94  ? 0.1436 0.1376 0.2133 -0.0066 0.0179  -0.0005 94  HIS   B O   
5636 C CB  . HIS   B 94  ? 0.1399 0.1288 0.1773 0.0007  -0.0152 -0.0037 94  HIS   B CB  
5637 C CG  . HIS   B 94  ? 0.1382 0.1285 0.1715 -0.0087 -0.0209 -0.0027 94  HIS   B CG  
5638 N ND1 . HIS   B 94  ? 0.1454 0.1388 0.1596 -0.0066 -0.0202 -0.0068 94  HIS   B ND1 
5639 C CD2 . HIS   B 94  ? 0.1421 0.1346 0.1654 -0.0023 -0.0227 0.0017  94  HIS   B CD2 
5640 C CE1 . HIS   B 94  ? 0.1497 0.1341 0.1626 -0.0090 -0.0148 0.0088  94  HIS   B CE1 
5641 N NE2 . HIS   B 94  ? 0.1410 0.1432 0.1644 -0.0177 -0.0223 0.0040  94  HIS   B NE2 
5649 N N   . VAL   B 95  ? 0.1358 0.1202 0.1720 0.0030  -0.0013 0.0138  95  VAL   B N   
5650 C CA  . VAL   B 95  ? 0.1308 0.1411 0.1721 -0.0002 0.0051  0.0225  95  VAL   B CA  
5651 C C   . VAL   B 95  ? 0.1387 0.1336 0.1731 0.0026  0.0081  0.0184  95  VAL   B C   
5652 O O   . VAL   B 95  ? 0.1449 0.1300 0.1925 0.0075  -0.0006 0.0108  95  VAL   B O   
5653 C CB  . VAL   B 95  ? 0.1349 0.1391 0.1707 -0.0017 -0.0120 0.0146  95  VAL   B CB  
5654 C CG1 . VAL   B 95  ? 0.1475 0.1533 0.2072 -0.0056 0.0051  0.0219  95  VAL   B CG1 
5655 C CG2 . VAL   B 95  ? 0.1398 0.1397 0.1767 0.0064  -0.0016 0.0077  95  VAL   B CG2 
5665 N N   . VAL   B 96  ? 0.1489 0.1342 0.1726 0.0054  0.0080  0.0275  96  VAL   B N   
5666 C CA  . VAL   B 96  ? 0.1577 0.1431 0.1882 0.0103  0.0086  0.0266  96  VAL   B CA  
5667 C C   . VAL   B 96  ? 0.1676 0.1493 0.2030 0.0058  0.0145  0.0323  96  VAL   B C   
5668 O O   . VAL   B 96  ? 0.1730 0.1590 0.1987 0.0020  0.0195  0.0056  96  VAL   B O   
5669 C CB  . VAL   B 96  ? 0.1659 0.1671 0.1894 0.0093  0.0070  0.0215  96  VAL   B CB  
5670 C CG1 . VAL   B 96  ? 0.1669 0.1805 0.1770 0.0215  0.0095  0.0167  96  VAL   B CG1 
5671 C CG2 . VAL   B 96  ? 0.1733 0.1679 0.1981 0.0048  0.0085  0.0105  96  VAL   B CG2 
5681 N N   . GLY   B 97  ? 0.1746 0.1531 0.1765 0.0018  -0.0047 0.0316  97  GLY   B N   
5682 C CA  . GLY   B 97  ? 0.1971 0.1559 0.1954 0.0018  0.0050  0.0375  97  GLY   B CA  
5683 C C   . GLY   B 97  ? 0.2240 0.1702 0.2059 0.0031  0.0185  0.0282  97  GLY   B C   
5684 O O   . GLY   B 97  ? 0.2443 0.1724 0.1900 0.0017  -0.0009 0.0239  97  GLY   B O   
5688 N N   . PRO   B 98  ? 0.2443 0.1700 0.2026 0.0067  0.0428  0.0385  98  PRO   B N   
5689 C CA  . PRO   B 98  ? 0.2635 0.1967 0.2126 0.0210  0.0562  0.0438  98  PRO   B CA  
5690 C C   . PRO   B 98  ? 0.2775 0.1958 0.1923 0.0422  0.0676  0.0497  98  PRO   B C   
5691 O O   . PRO   B 98  ? 0.2613 0.1896 0.2297 0.0345  0.0559  0.0524  98  PRO   B O   
5692 C CB  . PRO   B 98  ? 0.2536 0.2049 0.2419 0.0168  0.0718  0.0573  98  PRO   B CB  
5693 C CG  . PRO   B 98  ? 0.2446 0.1958 0.2543 0.0104  0.0562  0.0679  98  PRO   B CG  
5694 C CD  . PRO   B 98  ? 0.2298 0.1720 0.2483 0.0085  0.0503  0.0524  98  PRO   B CD  
5702 N N   . ASN   B 99  ? 0.2969 0.2183 0.2123 0.0651  0.0723  0.0484  99  ASN   B N   
5703 C CA  . ASN   B 99  ? 0.3252 0.2295 0.2220 0.0794  0.0622  0.0776  99  ASN   B CA  
5704 C C   . ASN   B 99  ? 0.3463 0.2714 0.2533 0.0874  0.0755  0.1098  99  ASN   B C   
5705 O O   . ASN   B 99  ? 0.3610 0.2977 0.2574 0.0901  0.0623  0.1125  99  ASN   B O   
5706 C CB  . ASN   B 99  ? 0.3416 0.2237 0.2117 0.0816  0.0463  0.0624  99  ASN   B CB  
5707 C CG  . ASN   B 99  ? 0.3497 0.2297 0.2288 0.0777  0.0374  0.0455  99  ASN   B CG  
5708 O OD1 . ASN   B 99  ? 0.3469 0.2263 0.2570 0.0800  0.0482  0.0562  99  ASN   B OD1 
5709 N ND2 . ASN   B 99  ? 0.3464 0.2330 0.2290 0.0843  0.0177  0.0428  99  ASN   B ND2 
5716 N N   . VAL   B 100 ? 0.3654 0.2875 0.3145 0.0763  0.0958  0.1193  100 VAL   B N   
5717 C CA  . VAL   B 100 ? 0.3977 0.3158 0.3792 0.0606  0.0889  0.1424  100 VAL   B CA  
5718 C C   . VAL   B 100 ? 0.4259 0.3327 0.3722 0.0651  0.0831  0.1624  100 VAL   B C   
5719 O O   . VAL   B 100 ? 0.4323 0.3507 0.3782 0.0601  0.1008  0.1480  100 VAL   B O   
5720 C CB  . VAL   B 100 ? 0.4018 0.3253 0.4492 0.0296  0.0890  0.1561  100 VAL   B CB  
5721 C CG1 . VAL   B 100 ? 0.4085 0.3294 0.4777 0.0121  0.0824  0.1486  100 VAL   B CG1 
5722 C CG2 . VAL   B 100 ? 0.3976 0.3322 0.4546 0.0272  0.0925  0.1671  100 VAL   B CG2 
5732 N N   . ASN   B 101 ? 0.4474 0.3362 0.3629 0.0763  0.0556  0.1747  101 ASN   B N   
5733 C CA  . ASN   B 101 ? 0.4750 0.3463 0.3673 0.0777  0.0363  0.1809  101 ASN   B CA  
5734 C C   . ASN   B 101 ? 0.5141 0.3891 0.3757 0.0720  0.0199  0.1783  101 ASN   B C   
5735 O O   . ASN   B 101 ? 0.5147 0.3997 0.4099 0.0784  0.0222  0.1482  101 ASN   B O   
5736 C CB  . ASN   B 101 ? 0.4665 0.3249 0.3585 0.0740  0.0437  0.1543  101 ASN   B CB  
5737 C CG  . ASN   B 101 ? 0.4551 0.3037 0.3559 0.0692  0.0403  0.1400  101 ASN   B CG  
5738 O OD1 . ASN   B 101 ? 0.4565 0.2994 0.3974 0.0666  0.0554  0.1277  101 ASN   B OD1 
5739 N ND2 . ASN   B 101 ? 0.4428 0.2946 0.3474 0.0624  0.0343  0.1267  101 ASN   B ND2 
5746 N N   . LYS   B 102 ? 0.5508 0.4310 0.4022 0.0560  0.0166  0.1640  102 LYS   B N   
5747 C CA  . LYS   B 102 ? 0.5833 0.4752 0.4378 0.0380  0.0180  0.1421  102 LYS   B CA  
5748 C C   . LYS   B 102 ? 0.5766 0.4785 0.4237 0.0367  0.0212  0.1503  102 LYS   B C   
5749 O O   . LYS   B 102 ? 0.5867 0.4855 0.4246 0.0346  0.0090  0.1502  102 LYS   B O   
5750 C CB  . LYS   B 102 ? 0.6147 0.5129 0.4981 0.0251  0.0276  0.0997  102 LYS   B CB  
5751 C CG  . LYS   B 102 ? 0.6397 0.5446 0.5753 0.0171  0.0325  0.0557  102 LYS   B CG  
5752 C CD  . LYS   B 102 ? 0.6597 0.5687 0.6300 0.0106  0.0371  0.0206  102 LYS   B CD  
5753 C CE  . LYS   B 102 ? 0.6736 0.5862 0.6881 0.0045  0.0428  -0.0032 102 LYS   B CE  
5754 N NZ  . LYS   B 102 ? 0.6821 0.5950 0.7170 0.0011  0.0466  -0.0182 102 LYS   B NZ  
5768 N N   . GLY   B 103 ? 0.5573 0.4746 0.4108 0.0347  0.0404  0.1415  103 GLY   B N   
5769 C CA  . GLY   B 103 ? 0.5385 0.4681 0.4280 0.0303  0.0619  0.1213  103 GLY   B CA  
5770 C C   . GLY   B 103 ? 0.5176 0.4576 0.4264 0.0237  0.0802  0.0979  103 GLY   B C   
5771 O O   . GLY   B 103 ? 0.5237 0.4642 0.4302 0.0184  0.0823  0.0964  103 GLY   B O   
5775 N N   A GLU   B 104 ? 0.5018 0.4472 0.4133 0.0257  0.0944  0.0828  104 GLU   B N   
5776 N N   B GLU   B 104 ? 0.5043 0.4497 0.4203 0.0215  0.0818  0.0811  104 GLU   B N   
5777 C CA  A GLU   B 104 ? 0.4840 0.4353 0.4056 0.0330  0.1005  0.0643  104 GLU   B CA  
5778 C CA  B GLU   B 104 ? 0.4893 0.4401 0.4168 0.0233  0.0778  0.0609  104 GLU   B CA  
5779 C C   A GLU   B 104 ? 0.4770 0.4313 0.4102 0.0162  0.1343  0.0642  104 GLU   B C   
5780 C C   B GLU   B 104 ? 0.4813 0.4368 0.4230 0.0124  0.0987  0.0564  104 GLU   B C   
5781 O O   A GLU   B 104 ? 0.4715 0.4293 0.4248 0.0141  0.1403  0.0681  104 GLU   B O   
5782 O O   B GLU   B 104 ? 0.4768 0.4348 0.4366 0.0111  0.1021  0.0577  104 GLU   B O   
5783 C CB  A GLU   B 104 ? 0.4751 0.4241 0.3910 0.0560  0.0684  0.0399  104 GLU   B CB  
5784 C CB  B GLU   B 104 ? 0.4836 0.4314 0.4039 0.0349  0.0505  0.0415  104 GLU   B CB  
5785 C CG  A GLU   B 104 ? 0.4648 0.4123 0.3754 0.0745  0.0295  0.0134  104 GLU   B CG  
5786 C CG  B GLU   B 104 ? 0.4763 0.4220 0.3908 0.0427  0.0188  0.0206  104 GLU   B CG  
5787 C CD  A GLU   B 104 ? 0.4533 0.4000 0.3555 0.0867  0.0021  -0.0064 104 GLU   B CD  
5788 C CD  B GLU   B 104 ? 0.4684 0.4119 0.3751 0.0454  -0.0025 0.0039  104 GLU   B CD  
5789 O OE1 A GLU   B 104 ? 0.4380 0.3877 0.3290 0.0949  0.0038  -0.0146 104 GLU   B OE1 
5790 O OE1 B GLU   B 104 ? 0.4585 0.4044 0.3600 0.0457  -0.0021 -0.0017 104 GLU   B OE1 
5791 O OE2 A GLU   B 104 ? 0.4564 0.4008 0.3526 0.0881  -0.0167 -0.0184 104 GLU   B OE2 
5792 O OE2 B GLU   B 104 ? 0.4702 0.4105 0.3727 0.0466  -0.0167 -0.0059 104 GLU   B OE2 
5805 N N   A ASP   B 105 ? 0.4716 0.4284 0.4128 0.0049  0.1615  0.0579  105 ASP   B N   
5806 N N   B ASP   B 105 ? 0.4757 0.4349 0.4260 0.0047  0.1151  0.0495  105 ASP   B N   
5807 C CA  A ASP   B 105 ? 0.4678 0.4244 0.4251 -0.0049 0.1861  0.0401  105 ASP   B CA  
5808 C CA  B ASP   B 105 ? 0.4709 0.4313 0.4318 -0.0020 0.1309  0.0346  105 ASP   B CA  
5809 C C   A ASP   B 105 ? 0.4447 0.3958 0.3885 -0.0204 0.2054  0.0379  105 ASP   B C   
5810 C C   B ASP   B 105 ? 0.4544 0.4113 0.4031 -0.0125 0.1385  0.0278  105 ASP   B C   
5811 O O   A ASP   B 105 ? 0.4333 0.3901 0.3653 -0.0148 0.2307  0.0428  105 ASP   B O   
5812 O O   B ASP   B 105 ? 0.4501 0.4082 0.3911 -0.0092 0.1478  0.0304  105 ASP   B O   
5813 C CB  A ASP   B 105 ? 0.4785 0.4425 0.4856 0.0034  0.1935  0.0231  105 ASP   B CB  
5814 C CB  B ASP   B 105 ? 0.4761 0.4434 0.4775 0.0038  0.1399  0.0251  105 ASP   B CB  
5815 C CG  A ASP   B 105 ? 0.4838 0.4536 0.5385 0.0081  0.1950  0.0127  105 ASP   B CG  
5816 C CG  B ASP   B 105 ? 0.4776 0.4500 0.5148 0.0068  0.1440  0.0209  105 ASP   B CG  
5817 O OD1 A ASP   B 105 ? 0.4802 0.4558 0.5450 0.0032  0.2072  0.0190  105 ASP   B OD1 
5818 O OD1 B ASP   B 105 ? 0.4755 0.4506 0.5230 0.0042  0.1500  0.0255  105 ASP   B OD1 
5819 O OD2 A ASP   B 105 ? 0.4872 0.4584 0.5726 0.0157  0.1843  0.0024  105 ASP   B OD2 
5820 O OD2 B ASP   B 105 ? 0.4768 0.4540 0.5349 0.0103  0.1418  0.0174  105 ASP   B OD2 
5829 N N   A ILE   B 106 ? 0.4320 0.3708 0.3959 -0.0359 0.1865  0.0341  106 ILE   B N   
5830 N N   B ILE   B 106 ? 0.4414 0.3927 0.3997 -0.0217 0.1288  0.0209  106 ILE   B N   
5831 C CA  A ILE   B 106 ? 0.4102 0.3447 0.3889 -0.0547 0.1915  0.0291  106 ILE   B CA  
5832 C CA  B ILE   B 106 ? 0.4240 0.3751 0.3920 -0.0297 0.1283  0.0106  106 ILE   B CA  
5833 C C   A ILE   B 106 ? 0.3814 0.3344 0.3759 -0.0562 0.1940  0.0209  106 ILE   B C   
5834 C C   B ILE   B 106 ? 0.3998 0.3647 0.3822 -0.0299 0.1299  0.0019  106 ILE   B C   
5835 O O   A ILE   B 106 ? 0.3735 0.3174 0.3831 -0.0668 0.1976  0.0250  106 ILE   B O   
5836 O O   B ILE   B 106 ? 0.3961 0.3564 0.3849 -0.0356 0.1296  -0.0007 106 ILE   B O   
5837 C CB  A ILE   B 106 ? 0.4210 0.3331 0.3947 -0.0684 0.1837  0.0341  106 ILE   B CB  
5838 C CB  B ILE   B 106 ? 0.4313 0.3711 0.3947 -0.0358 0.1242  0.0102  106 ILE   B CB  
5839 C CG1 A ILE   B 106 ? 0.4277 0.3276 0.4010 -0.0714 0.1696  0.0280  106 ILE   B CG1 
5840 C CG1 B ILE   B 106 ? 0.4384 0.3699 0.3990 -0.0362 0.1128  0.0053  106 ILE   B CG1 
5841 C CG2 A ILE   B 106 ? 0.4227 0.3354 0.4108 -0.0699 0.1850  0.0365  106 ILE   B CG2 
5842 C CG2 B ILE   B 106 ? 0.4310 0.3734 0.4059 -0.0356 0.1274  0.0111  106 ILE   B CG2 
5843 C CD1 A ILE   B 106 ? 0.4322 0.3283 0.3902 -0.0716 0.1660  0.0257  106 ILE   B CD1 
5844 C CD1 B ILE   B 106 ? 0.4433 0.3713 0.3956 -0.0353 0.1077  0.0020  106 ILE   B CD1 
5867 N N   A GLN   B 107 ? 0.3623 0.3425 0.3789 -0.0549 0.1837  0.0246  107 GLN   B N   
5868 N N   B GLN   B 107 ? 0.3803 0.3646 0.3877 -0.0290 0.1255  0.0043  107 GLN   B N   
5869 C CA  A GLN   B 107 ? 0.3455 0.3490 0.3979 -0.0462 0.1489  0.0189  107 GLN   B CA  
5870 C CA  B GLN   B 107 ? 0.3606 0.3620 0.3999 -0.0256 0.1102  0.0059  107 GLN   B CA  
5871 C C   A GLN   B 107 ? 0.3140 0.3251 0.3676 -0.0261 0.1230  0.0053  107 GLN   B C   
5872 C C   B GLN   B 107 ? 0.3242 0.3342 0.3674 -0.0152 0.1053  0.0010  107 GLN   B C   
5873 O O   A GLN   B 107 ? 0.3004 0.3250 0.3823 -0.0160 0.1006  -0.0126 107 GLN   B O   
5874 O O   B GLN   B 107 ? 0.3158 0.3363 0.3772 -0.0089 0.0901  -0.0096 107 GLN   B O   
5875 C CB  A GLN   B 107 ? 0.3729 0.3833 0.4609 -0.0470 0.1183  0.0176  107 GLN   B CB  
5876 C CB  B GLN   B 107 ? 0.3835 0.3888 0.4521 -0.0276 0.0891  0.0068  107 GLN   B CB  
5877 C CG  A GLN   B 107 ? 0.3993 0.4108 0.5234 -0.0419 0.0848  0.0146  107 GLN   B CG  
5878 C CG  B GLN   B 107 ? 0.4047 0.4106 0.5062 -0.0251 0.0653  0.0060  107 GLN   B CG  
5879 C CD  A GLN   B 107 ? 0.4189 0.4301 0.5716 -0.0383 0.0604  0.0144  107 GLN   B CD  
5880 C CD  B GLN   B 107 ? 0.4210 0.4259 0.5483 -0.0231 0.0471  0.0070  107 GLN   B CD  
5881 O OE1 A GLN   B 107 ? 0.4241 0.4375 0.5890 -0.0320 0.0552  0.0128  107 GLN   B OE1 
5882 O OE1 B GLN   B 107 ? 0.4249 0.4320 0.5617 -0.0190 0.0440  0.0068  107 GLN   B OE1 
5883 N NE2 A GLN   B 107 ? 0.4289 0.4358 0.5883 -0.0376 0.0509  0.0179  107 GLN   B NE2 
5884 N NE2 B GLN   B 107 ? 0.4295 0.4305 0.5638 -0.0226 0.0403  0.0096  107 GLN   B NE2 
5901 N N   . LEU   B 108 ? 0.2928 0.3071 0.3343 -0.0029 0.1056  0.0078  108 LEU   B N   
5902 C CA  . LEU   B 108 ? 0.2580 0.2673 0.2794 0.0141  0.0795  0.0346  108 LEU   B CA  
5903 C C   . LEU   B 108 ? 0.2055 0.2116 0.2796 0.0087  0.0484  0.0371  108 LEU   B C   
5904 O O   . LEU   B 108 ? 0.1980 0.1892 0.2616 0.0171  0.0481  0.0398  108 LEU   B O   
5905 C CB  . LEU   B 108 ? 0.2698 0.2824 0.2556 0.0201  0.0788  0.0597  108 LEU   B CB  
5906 C CG  . LEU   B 108 ? 0.2844 0.3144 0.2716 0.0273  0.0659  0.0366  108 LEU   B CG  
5907 C CD1 . LEU   B 108 ? 0.2956 0.3306 0.2557 0.0231  0.0671  0.0371  108 LEU   B CD1 
5908 C CD2 . LEU   B 108 ? 0.2933 0.3245 0.2797 0.0398  0.0480  0.0173  108 LEU   B CD2 
5921 N N   . LEU   B 109 ? 0.1812 0.1889 0.2751 0.0019  0.0388  0.0207  109 LEU   B N   
5922 C CA  . LEU   B 109 ? 0.1647 0.1574 0.2868 0.0010  0.0404  0.0289  109 LEU   B CA  
5923 C C   . LEU   B 109 ? 0.1538 0.1413 0.2902 0.0003  0.0478  0.0149  109 LEU   B C   
5924 O O   . LEU   B 109 ? 0.1597 0.1347 0.2649 -0.0013 0.0439  0.0249  109 LEU   B O   
5925 C CB  . LEU   B 109 ? 0.1707 0.1481 0.3032 0.0020  0.0257  0.0471  109 LEU   B CB  
5926 C CG  . LEU   B 109 ? 0.1657 0.1439 0.3010 -0.0041 0.0311  0.0341  109 LEU   B CG  
5927 C CD1 . LEU   B 109 ? 0.1672 0.1566 0.2914 0.0059  0.0170  0.0362  109 LEU   B CD1 
5928 C CD2 . LEU   B 109 ? 0.1766 0.1428 0.3120 0.0008  0.0237  0.0221  109 LEU   B CD2 
5940 N N   . LYS   B 110 ? 0.1559 0.1441 0.2698 -0.0042 0.0390  0.0221  110 LYS   B N   
5941 C CA  . LYS   B 110 ? 0.1456 0.1427 0.2777 -0.0064 0.0273  0.0196  110 LYS   B CA  
5942 C C   . LYS   B 110 ? 0.1451 0.1427 0.2814 -0.0054 0.0312  0.0112  110 LYS   B C   
5943 O O   . LYS   B 110 ? 0.1442 0.1443 0.2732 -0.0084 0.0198  -0.0003 110 LYS   B O   
5944 C CB  . LYS   B 110 ? 0.1501 0.1417 0.2994 -0.0004 0.0324  0.0235  110 LYS   B CB  
5945 C CG  . LYS   B 110 ? 0.1515 0.1486 0.3074 -0.0013 0.0158  0.0182  110 LYS   B CG  
5946 C CD  . LYS   B 110 ? 0.1551 0.1445 0.3269 -0.0006 0.0148  0.0229  110 LYS   B CD  
5947 C CE  . LYS   B 110 ? 0.1568 0.1621 0.3472 0.0058  0.0197  0.0055  110 LYS   B CE  
5948 N NZ  . LYS   B 110 ? 0.1576 0.1739 0.3403 0.0024  0.0113  0.0071  110 LYS   B NZ  
5962 N N   . SER   B 111 ? 0.1521 0.1447 0.2826 -0.0008 0.0201  0.0202  111 SER   B N   
5963 C CA  . SER   B 111 ? 0.1551 0.1439 0.2706 0.0060  0.0250  0.0216  111 SER   B CA  
5964 C C   . SER   B 111 ? 0.1514 0.1346 0.2639 0.0012  0.0221  0.0116  111 SER   B C   
5965 O O   . SER   B 111 ? 0.1467 0.1389 0.2791 0.0010  0.0193  0.0063  111 SER   B O   
5966 C CB  . SER   B 111 ? 0.1622 0.1738 0.2887 0.0064  0.0487  0.0258  111 SER   B CB  
5967 O OG  . SER   B 111 ? 0.1779 0.2065 0.3022 0.0089  0.0508  0.0399  111 SER   B OG  
5973 N N   . ALA   B 112 ? 0.1449 0.1438 0.2545 0.0048  0.0264  0.0211  112 ALA   B N   
5974 C CA  . ALA   B 112 ? 0.1476 0.1507 0.2364 0.0009  0.0135  0.0051  112 ALA   B CA  
5975 C C   . ALA   B 112 ? 0.1438 0.1416 0.2271 0.0014  -0.0026 -0.0010 112 ALA   B C   
5976 O O   . ALA   B 112 ? 0.1411 0.1390 0.2365 -0.0046 0.0096  0.0010  112 ALA   B O   
5977 C CB  . ALA   B 112 ? 0.1408 0.1530 0.2529 0.0056  0.0185  0.0115  112 ALA   B CB  
5983 N N   . TYR   B 113 ? 0.1403 0.1316 0.2455 -0.0032 0.0061  -0.0046 113 TYR   B N   
5984 C CA  . TYR   B 113 ? 0.1356 0.1302 0.2495 -0.0049 0.0098  -0.0132 113 TYR   B CA  
5985 C C   . TYR   B 113 ? 0.1310 0.1323 0.2408 -0.0125 0.0182  -0.0050 113 TYR   B C   
5986 O O   . TYR   B 113 ? 0.1323 0.1303 0.2185 -0.0071 0.0043  -0.0024 113 TYR   B O   
5987 C CB  . TYR   B 113 ? 0.1380 0.1196 0.2532 -0.0008 0.0111  0.0097  113 TYR   B CB  
5988 C CG  . TYR   B 113 ? 0.1391 0.1260 0.2623 -0.0077 0.0039  0.0091  113 TYR   B CG  
5989 C CD1 . TYR   B 113 ? 0.1439 0.1345 0.2785 -0.0091 0.0115  0.0179  113 TYR   B CD1 
5990 C CD2 . TYR   B 113 ? 0.1467 0.1268 0.2773 -0.0053 0.0102  0.0072  113 TYR   B CD2 
5991 C CE1 . TYR   B 113 ? 0.1474 0.1356 0.2536 -0.0032 0.0134  0.0108  113 TYR   B CE1 
5992 C CE2 . TYR   B 113 ? 0.1544 0.1233 0.2767 -0.0005 0.0076  0.0223  113 TYR   B CE2 
5993 C CZ  . TYR   B 113 ? 0.1418 0.1216 0.2686 0.0053  0.0023  0.0206  113 TYR   B CZ  
5994 O OH  . TYR   B 113 ? 0.1560 0.1277 0.2942 0.0129  0.0227  0.0128  113 TYR   B OH  
6004 N N   . GLU   B 114 ? 0.1306 0.1224 0.2502 -0.0078 0.0117  0.0040  114 GLU   B N   
6005 C CA  . GLU   B 114 ? 0.1262 0.1228 0.2442 0.0069  0.0001  0.0081  114 GLU   B CA  
6006 C C   . GLU   B 114 ? 0.1312 0.1201 0.2443 -0.0018 0.0084  0.0035  114 GLU   B C   
6007 O O   . GLU   B 114 ? 0.1346 0.1255 0.2523 0.0028  -0.0037 0.0089  114 GLU   B O   
6008 C CB  . GLU   B 114 ? 0.1304 0.1331 0.2726 0.0010  0.0147  0.0009  114 GLU   B CB  
6009 C CG  . GLU   B 114 ? 0.1337 0.1305 0.2820 -0.0035 0.0050  0.0066  114 GLU   B CG  
6010 C CD  . GLU   B 114 ? 0.1318 0.1345 0.2716 -0.0055 0.0091  0.0132  114 GLU   B CD  
6011 O OE1 . GLU   B 114 ? 0.1263 0.1438 0.2639 -0.0124 0.0165  0.0058  114 GLU   B OE1 
6012 O OE2 . GLU   B 114 ? 0.1324 0.1554 0.2661 -0.0180 0.0129  0.0036  114 GLU   B OE2 
6019 N N   . ASN   B 115 ? 0.1307 0.1126 0.2403 -0.0004 -0.0082 0.0032  115 ASN   B N   
6020 C CA  . ASN   B 115 ? 0.1286 0.1252 0.2092 -0.0112 -0.0019 0.0083  115 ASN   B CA  
6021 C C   . ASN   B 115 ? 0.1292 0.1197 0.2244 -0.0102 -0.0034 -0.0091 115 ASN   B C   
6022 O O   . ASN   B 115 ? 0.1437 0.1213 0.2155 -0.0123 0.0043  -0.0010 115 ASN   B O   
6023 C CB  . ASN   B 115 ? 0.1421 0.1375 0.2331 -0.0102 -0.0001 0.0042  115 ASN   B CB  
6024 C CG  . ASN   B 115 ? 0.1537 0.1448 0.2240 -0.0015 -0.0046 0.0016  115 ASN   B CG  
6025 O OD1 . ASN   B 115 ? 0.1908 0.1582 0.2337 -0.0045 0.0155  -0.0056 115 ASN   B OD1 
6026 N ND2 . ASN   B 115 ? 0.1509 0.1520 0.2154 -0.0120 -0.0019 0.0096  115 ASN   B ND2 
6033 N N   . PHE   B 116 ? 0.1286 0.1229 0.2223 -0.0052 -0.0023 -0.0005 116 PHE   B N   
6034 C CA  . PHE   B 116 ? 0.1408 0.1323 0.2253 -0.0103 -0.0047 0.0018  116 PHE   B CA  
6035 C C   . PHE   B 116 ? 0.1361 0.1208 0.2172 -0.0122 -0.0132 0.0089  116 PHE   B C   
6036 O O   . PHE   B 116 ? 0.1445 0.1313 0.2272 -0.0042 -0.0114 0.0114  116 PHE   B O   
6037 C CB  . PHE   B 116 ? 0.1372 0.1244 0.2026 -0.0085 -0.0183 0.0010  116 PHE   B CB  
6038 C CG  . PHE   B 116 ? 0.1319 0.1224 0.2195 -0.0156 -0.0083 0.0053  116 PHE   B CG  
6039 C CD1 . PHE   B 116 ? 0.1383 0.1270 0.2359 -0.0073 -0.0049 0.0043  116 PHE   B CD1 
6040 C CD2 . PHE   B 116 ? 0.1405 0.1312 0.2211 -0.0132 -0.0030 -0.0046 116 PHE   B CD2 
6041 C CE1 . PHE   B 116 ? 0.1424 0.1348 0.2160 -0.0083 -0.0169 0.0109  116 PHE   B CE1 
6042 C CE2 . PHE   B 116 ? 0.1369 0.1291 0.2252 -0.0064 0.0015  0.0040  116 PHE   B CE2 
6043 C CZ  . PHE   B 116 ? 0.1305 0.1400 0.2243 -0.0079 -0.0092 0.0015  116 PHE   B CZ  
6053 N N   . ASN   B 117 ? 0.1321 0.1249 0.2294 -0.0054 -0.0116 0.0076  117 ASN   B N   
6054 C CA  . ASN   B 117 ? 0.1463 0.1267 0.2440 0.0011  -0.0180 0.0061  117 ASN   B CA  
6055 C C   . ASN   B 117 ? 0.1499 0.1308 0.2678 0.0005  -0.0235 0.0066  117 ASN   B C   
6056 O O   . ASN   B 117 ? 0.1501 0.1303 0.3010 -0.0067 -0.0360 0.0138  117 ASN   B O   
6057 C CB  . ASN   B 117 ? 0.1472 0.1273 0.2325 0.0017  -0.0167 -0.0001 117 ASN   B CB  
6058 C CG  . ASN   B 117 ? 0.1386 0.1286 0.2563 0.0061  -0.0125 -0.0091 117 ASN   B CG  
6059 O OD1 . ASN   B 117 ? 0.1561 0.1315 0.2782 -0.0140 -0.0071 -0.0070 117 ASN   B OD1 
6060 N ND2 . ASN   B 117 ? 0.1389 0.1339 0.2386 -0.0022 -0.0090 -0.0150 117 ASN   B ND2 
6067 N N   . GLN   B 118 ? 0.1445 0.1245 0.2414 -0.0125 -0.0125 0.0066  118 GLN   B N   
6068 C CA  . GLN   B 118 ? 0.1512 0.1308 0.2587 -0.0013 -0.0172 0.0047  118 GLN   B CA  
6069 C C   . GLN   B 118 ? 0.1475 0.1240 0.2683 0.0013  -0.0183 0.0087  118 GLN   B C   
6070 O O   . GLN   B 118 ? 0.1687 0.1244 0.3021 -0.0070 -0.0046 0.0028  118 GLN   B O   
6071 C CB  . GLN   B 118 ? 0.1556 0.1397 0.2522 -0.0049 -0.0138 0.0007  118 GLN   B CB  
6072 C CG  . GLN   B 118 ? 0.1610 0.1379 0.2506 0.0062  -0.0199 -0.0179 118 GLN   B CG  
6073 C CD  . GLN   B 118 ? 0.1595 0.1267 0.2581 0.0064  -0.0173 -0.0092 118 GLN   B CD  
6074 O OE1 . GLN   B 118 ? 0.1711 0.1286 0.2872 0.0081  -0.0049 0.0023  118 GLN   B OE1 
6075 N NE2 . GLN   B 118 ? 0.1728 0.1321 0.2604 -0.0005 -0.0100 -0.0003 118 GLN   B NE2 
6084 N N   . HIS   B 119 ? 0.1599 0.1303 0.2063 -0.0075 -0.0222 0.0126  119 HIS   B N   
6085 C CA  . HIS   B 119 ? 0.1673 0.1385 0.2146 -0.0013 -0.0299 0.0080  119 HIS   B CA  
6086 C C   . HIS   B 119 ? 0.1787 0.1446 0.1976 -0.0069 -0.0495 0.0094  119 HIS   B C   
6087 O O   . HIS   B 119 ? 0.1856 0.1409 0.2289 -0.0285 -0.0312 0.0018  119 HIS   B O   
6088 C CB  . HIS   B 119 ? 0.1749 0.1498 0.2004 -0.0020 -0.0282 0.0064  119 HIS   B CB  
6089 C CG  . HIS   B 119 ? 0.1799 0.1736 0.2165 0.0091  -0.0416 -0.0103 119 HIS   B CG  
6090 N ND1 . HIS   B 119 ? 0.1810 0.1838 0.2562 -0.0003 -0.0461 -0.0282 119 HIS   B ND1 
6091 C CD2 . HIS   B 119 ? 0.1931 0.1918 0.2250 0.0382  -0.0495 -0.0180 119 HIS   B CD2 
6092 C CE1 . HIS   B 119 ? 0.2009 0.1999 0.2627 0.0127  -0.0544 -0.0412 119 HIS   B CE1 
6093 N NE2 . HIS   B 119 ? 0.2054 0.2108 0.2411 0.0284  -0.0504 -0.0382 119 HIS   B NE2 
6101 N N   A GLU   B 120 ? 0.1986 0.1505 0.2029 -0.0142 -0.0539 0.0159  120 GLU   B N   
6102 N N   B GLU   B 120 ? 0.1980 0.1532 0.2039 -0.0098 -0.0507 0.0158  120 GLU   B N   
6103 C CA  A GLU   B 120 ? 0.2231 0.1609 0.2287 -0.0117 -0.0575 0.0355  120 GLU   B CA  
6104 C CA  B GLU   B 120 ? 0.2203 0.1629 0.2264 -0.0062 -0.0541 0.0329  120 GLU   B CA  
6105 C C   A GLU   B 120 ? 0.2026 0.1526 0.2121 -0.0200 -0.0570 0.0285  120 GLU   B C   
6106 C C   B GLU   B 120 ? 0.2014 0.1535 0.2108 -0.0169 -0.0526 0.0255  120 GLU   B C   
6107 O O   A GLU   B 120 ? 0.1978 0.1626 0.2098 -0.0175 -0.0612 0.0120  120 GLU   B O   
6108 O O   B GLU   B 120 ? 0.1972 0.1604 0.2084 -0.0153 -0.0513 0.0098  120 GLU   B O   
6109 C CB  A GLU   B 120 ? 0.2692 0.1922 0.2883 -0.0014 -0.0675 0.0500  120 GLU   B CB  
6110 C CB  B GLU   B 120 ? 0.2619 0.1898 0.2810 0.0079  -0.0654 0.0487  120 GLU   B CB  
6111 C CG  A GLU   B 120 ? 0.3061 0.2406 0.3736 0.0054  -0.0769 0.0513  120 GLU   B CG  
6112 C CG  B GLU   B 120 ? 0.2964 0.2340 0.3590 0.0164  -0.0727 0.0515  120 GLU   B CG  
6113 C CD  A GLU   B 120 ? 0.3308 0.2801 0.4492 0.0077  -0.0805 0.0604  120 GLU   B CD  
6114 C CD  B GLU   B 120 ? 0.3286 0.2750 0.4315 0.0193  -0.0638 0.0569  120 GLU   B CD  
6115 O OE1 A GLU   B 120 ? 0.3533 0.3000 0.4849 0.0062  -0.0675 0.0711  120 GLU   B OE1 
6116 O OE1 B GLU   B 120 ? 0.3520 0.2897 0.4661 0.0207  -0.0546 0.0600  120 GLU   B OE1 
6117 O OE2 A GLU   B 120 ? 0.3437 0.2970 0.4910 0.0055  -0.0806 0.0530  120 GLU   B OE2 
6118 O OE2 B GLU   B 120 ? 0.3369 0.2935 0.4615 0.0162  -0.0643 0.0617  120 GLU   B OE2 
6131 N N   . VAL   B 121 ? 0.1881 0.1454 0.1969 -0.0238 -0.0450 0.0221  121 VAL   B N   
6132 C CA  . VAL   B 121 ? 0.1773 0.1588 0.1655 -0.0230 -0.0350 0.0249  121 VAL   B CA  
6133 C C   . VAL   B 121 ? 0.1751 0.1548 0.1973 -0.0275 -0.0299 0.0238  121 VAL   B C   
6134 O O   . VAL   B 121 ? 0.1845 0.1492 0.1983 -0.0383 -0.0458 0.0228  121 VAL   B O   
6135 C CB  . VAL   B 121 ? 0.2051 0.1983 0.1988 -0.0148 -0.0348 0.0149  121 VAL   B CB  
6136 C CG1 . VAL   B 121 ? 0.2096 0.2123 0.2434 -0.0277 -0.0182 0.0068  121 VAL   B CG1 
6137 C CG2 . VAL   B 121 ? 0.2344 0.2207 0.2085 -0.0033 -0.0274 0.0071  121 VAL   B CG2 
6148 N N   . LEU   B 122 ? 0.1637 0.1484 0.1829 -0.0195 -0.0289 0.0107  122 LEU   B N   
6149 C CA  . LEU   B 122 ? 0.1546 0.1557 0.1770 -0.0258 -0.0258 0.0159  122 LEU   B CA  
6150 C C   . LEU   B 122 ? 0.1556 0.1393 0.1889 -0.0321 -0.0237 0.0167  122 LEU   B C   
6151 O O   . LEU   B 122 ? 0.1633 0.1410 0.2035 -0.0355 -0.0349 0.0106  122 LEU   B O   
6152 C CB  . LEU   B 122 ? 0.1812 0.1666 0.2168 -0.0054 -0.0266 0.0213  122 LEU   B CB  
6153 C CG  . LEU   B 122 ? 0.1698 0.1737 0.2278 -0.0145 -0.0153 0.0181  122 LEU   B CG  
6154 C CD1 . LEU   B 122 ? 0.1661 0.1982 0.2274 -0.0258 -0.0179 0.0192  122 LEU   B CD1 
6155 C CD2 . LEU   B 122 ? 0.1743 0.1669 0.2026 -0.0108 -0.0059 0.0051  122 LEU   B CD2 
6167 N N   . LEU   B 123 ? 0.1568 0.1286 0.1589 -0.0272 -0.0241 0.0157  123 LEU   B N   
6168 C CA  . LEU   B 123 ? 0.1603 0.1346 0.1618 -0.0321 -0.0244 0.0003  123 LEU   B CA  
6169 C C   . LEU   B 123 ? 0.1555 0.1322 0.1642 -0.0291 -0.0169 0.0073  123 LEU   B C   
6170 O O   . LEU   B 123 ? 0.1621 0.1375 0.1526 -0.0298 -0.0148 -0.0022 123 LEU   B O   
6171 C CB  . LEU   B 123 ? 0.1693 0.1300 0.1741 -0.0308 -0.0182 -0.0023 123 LEU   B CB  
6172 C CG  . LEU   B 123 ? 0.1632 0.1403 0.1913 -0.0201 -0.0139 0.0078  123 LEU   B CG  
6173 C CD1 . LEU   B 123 ? 0.1758 0.1463 0.2072 -0.0201 -0.0067 -0.0106 123 LEU   B CD1 
6174 C CD2 . LEU   B 123 ? 0.1741 0.1562 0.2068 -0.0144 -0.0071 0.0180  123 LEU   B CD2 
6186 N N   . ALA   B 124 ? 0.1500 0.1289 0.1693 -0.0202 -0.0211 0.0029  124 ALA   B N   
6187 C CA  . ALA   B 124 ? 0.1395 0.1262 0.1882 -0.0181 -0.0263 -0.0003 124 ALA   B CA  
6188 C C   . ALA   B 124 ? 0.1387 0.1280 0.1728 -0.0186 -0.0132 0.0123  124 ALA   B C   
6189 O O   . ALA   B 124 ? 0.1477 0.1308 0.1825 -0.0177 -0.0153 0.0044  124 ALA   B O   
6190 C CB  . ALA   B 124 ? 0.1518 0.1273 0.2060 -0.0097 -0.0197 0.0031  124 ALA   B CB  
6196 N N   . PRO   B 125 ? 0.1399 0.1304 0.1784 -0.0158 -0.0276 0.0164  125 PRO   B N   
6197 C CA  . PRO   B 125 ? 0.1523 0.1278 0.1914 -0.0212 -0.0187 0.0182  125 PRO   B CA  
6198 C C   . PRO   B 125 ? 0.1480 0.1316 0.2322 -0.0135 -0.0065 0.0200  125 PRO   B C   
6199 O O   . PRO   B 125 ? 0.1476 0.1330 0.2354 -0.0146 -0.0041 0.0220  125 PRO   B O   
6200 C CB  . PRO   B 125 ? 0.1536 0.1540 0.2072 -0.0208 -0.0254 0.0266  125 PRO   B CB  
6201 C CG  . PRO   B 125 ? 0.1589 0.1588 0.2054 -0.0243 -0.0237 0.0184  125 PRO   B CG  
6202 C CD  . PRO   B 125 ? 0.1575 0.1390 0.1853 -0.0302 -0.0190 0.0106  125 PRO   B CD  
6210 N N   . LEU   B 126 ? 0.1462 0.1265 0.2490 -0.0151 0.0159  0.0270  126 LEU   B N   
6211 C CA  . LEU   B 126 ? 0.1522 0.1403 0.2474 -0.0140 0.0077  0.0264  126 LEU   B CA  
6212 C C   . LEU   B 126 ? 0.1519 0.1463 0.2413 -0.0032 0.0064  0.0245  126 LEU   B C   
6213 O O   . LEU   B 126 ? 0.1737 0.1811 0.2567 0.0154  -0.0113 -0.0026 126 LEU   B O   
6214 C CB  . LEU   B 126 ? 0.1761 0.1389 0.2636 -0.0210 0.0155  0.0206  126 LEU   B CB  
6215 C CG  . LEU   B 126 ? 0.1920 0.1518 0.2786 -0.0257 0.0189  -0.0047 126 LEU   B CG  
6216 C CD1 . LEU   B 126 ? 0.2132 0.1639 0.3315 -0.0213 0.0196  -0.0142 126 LEU   B CD1 
6217 C CD2 . LEU   B 126 ? 0.1928 0.1664 0.2854 -0.0336 0.0073  -0.0154 126 LEU   B CD2 
6229 N N   . LEU   B 127 ? 0.1523 0.1287 0.2527 0.0006  0.0168  0.0145  127 LEU   B N   
6230 C CA  . LEU   B 127 ? 0.1587 0.1403 0.2508 -0.0052 0.0241  0.0185  127 LEU   B CA  
6231 C C   . LEU   B 127 ? 0.1513 0.1349 0.2542 -0.0023 0.0100  0.0287  127 LEU   B C   
6232 O O   . LEU   B 127 ? 0.1542 0.1446 0.2609 -0.0152 0.0106  0.0232  127 LEU   B O   
6233 C CB  . LEU   B 127 ? 0.1729 0.1380 0.2711 -0.0026 0.0234  0.0200  127 LEU   B CB  
6234 C CG  . LEU   B 127 ? 0.1828 0.1394 0.2692 0.0022  0.0359  0.0236  127 LEU   B CG  
6235 C CD1 . LEU   B 127 ? 0.1929 0.1400 0.2831 0.0134  0.0159  0.0117  127 LEU   B CD1 
6236 C CD2 . LEU   B 127 ? 0.1861 0.1526 0.2932 -0.0104 0.0370  0.0346  127 LEU   B CD2 
6248 N N   . SER   B 128 ? 0.1501 0.1399 0.2601 -0.0041 0.0024  0.0196  128 SER   B N   
6249 C CA  . SER   B 128 ? 0.1695 0.1433 0.2555 0.0020  -0.0074 0.0281  128 SER   B CA  
6250 C C   . SER   B 128 ? 0.1790 0.1457 0.2991 0.0056  -0.0330 0.0200  128 SER   B C   
6251 O O   . SER   B 128 ? 0.1976 0.1504 0.3305 -0.0021 -0.0299 0.0425  128 SER   B O   
6252 C CB  . SER   B 128 ? 0.1826 0.1441 0.2594 -0.0021 0.0084  0.0438  128 SER   B CB  
6253 O OG  . SER   B 128 ? 0.1871 0.1610 0.2519 0.0019  0.0102  0.0473  128 SER   B OG  
6259 N N   . ALA   B 129 ? 0.1970 0.1552 0.3141 0.0222  -0.0163 0.0084  129 ALA   B N   
6260 C CA  . ALA   B 129 ? 0.2152 0.1592 0.3398 0.0314  -0.0096 -0.0055 129 ALA   B CA  
6261 C C   . ALA   B 129 ? 0.1987 0.1516 0.3243 0.0199  0.0047  0.0077  129 ALA   B C   
6262 O O   . ALA   B 129 ? 0.1883 0.1604 0.3219 0.0200  -0.0094 0.0125  129 ALA   B O   
6263 C CB  . ALA   B 129 ? 0.2385 0.1809 0.3552 0.0344  0.0028  -0.0060 129 ALA   B CB  
6269 N N   . GLY   B 130 ? 0.1913 0.1539 0.3280 0.0243  0.0151  -0.0010 130 GLY   B N   
6270 C CA  . GLY   B 130 ? 0.1956 0.1633 0.3442 0.0258  0.0366  0.0007  130 GLY   B CA  
6271 C C   . GLY   B 130 ? 0.2054 0.1705 0.3206 0.0098  0.0224  0.0084  130 GLY   B C   
6272 O O   . GLY   B 130 ? 0.2105 0.1841 0.3219 0.0147  0.0083  0.0190  130 GLY   B O   
6276 N N   . ILE   B 131 ? 0.2073 0.1794 0.3166 0.0207  0.0096  0.0068  131 ILE   B N   
6277 C CA  . ILE   B 131 ? 0.2280 0.1943 0.3177 0.0102  0.0006  0.0198  131 ILE   B CA  
6278 C C   . ILE   B 131 ? 0.2399 0.1889 0.2894 0.0090  0.0102  0.0236  131 ILE   B C   
6279 O O   . ILE   B 131 ? 0.2698 0.2144 0.3012 0.0142  -0.0128 0.0254  131 ILE   B O   
6280 C CB  . ILE   B 131 ? 0.2264 0.2256 0.3615 0.0090  -0.0152 0.0234  131 ILE   B CB  
6281 C CG1 . ILE   B 131 ? 0.2352 0.2414 0.3786 -0.0115 -0.0168 0.0274  131 ILE   B CG1 
6282 C CG2 . ILE   B 131 ? 0.2267 0.2432 0.3820 0.0236  -0.0228 0.0156  131 ILE   B CG2 
6283 C CD1 . ILE   B 131 ? 0.2434 0.2573 0.4007 -0.0227 -0.0333 0.0321  131 ILE   B CD1 
6295 N N   . PHE   B 132 ? 0.2275 0.1680 0.2707 0.0058  0.0272  0.0210  132 PHE   B N   
6296 C CA  . PHE   B 132 ? 0.2338 0.1702 0.2653 0.0066  0.0484  0.0138  132 PHE   B CA  
6297 C C   . PHE   B 132 ? 0.2482 0.1869 0.2927 0.0105  0.0572  0.0186  132 PHE   B C   
6298 O O   . PHE   B 132 ? 0.2674 0.2146 0.3183 0.0058  0.0760  0.0277  132 PHE   B O   
6299 C CB  . PHE   B 132 ? 0.2173 0.1706 0.2503 0.0049  0.0506  0.0078  132 PHE   B CB  
6300 C CG  . PHE   B 132 ? 0.2089 0.1722 0.2409 0.0118  0.0323  0.0173  132 PHE   B CG  
6301 C CD1 . PHE   B 132 ? 0.2227 0.1692 0.2755 0.0108  0.0368  0.0256  132 PHE   B CD1 
6302 C CD2 . PHE   B 132 ? 0.2085 0.1742 0.2307 0.0192  0.0252  0.0331  132 PHE   B CD2 
6303 C CE1 . PHE   B 132 ? 0.2334 0.1747 0.2961 0.0020  0.0092  0.0317  132 PHE   B CE1 
6304 C CE2 . PHE   B 132 ? 0.2234 0.1780 0.2407 0.0168  0.0101  0.0319  132 PHE   B CE2 
6305 C CZ  . PHE   B 132 ? 0.2308 0.1811 0.2752 0.0043  -0.0076 0.0429  132 PHE   B CZ  
6315 N N   . GLY   B 133 ? 0.2485 0.1760 0.2956 -0.0028 0.0295  0.0468  133 GLY   B N   
6316 C CA  . GLY   B 133 ? 0.2586 0.1915 0.3187 -0.0227 0.0283  0.0512  133 GLY   B CA  
6317 C C   . GLY   B 133 ? 0.2637 0.1996 0.3307 -0.0330 0.0365  0.0551  133 GLY   B C   
6318 O O   . GLY   B 133 ? 0.2834 0.2148 0.3531 -0.0468 0.0315  0.0658  133 GLY   B O   
6322 N N   . ALA   B 134 ? 0.2451 0.2002 0.3080 -0.0348 0.0361  0.0391  134 ALA   B N   
6323 C CA  . ALA   B 134 ? 0.2400 0.1983 0.3094 -0.0288 0.0496  0.0242  134 ALA   B CA  
6324 C C   . ALA   B 134 ? 0.2450 0.1822 0.3124 -0.0300 0.0446  0.0487  134 ALA   B C   
6325 O O   . ALA   B 134 ? 0.2497 0.1994 0.3290 -0.0170 0.0319  0.0490  134 ALA   B O   
6326 C CB  . ALA   B 134 ? 0.2357 0.2036 0.3077 -0.0177 0.0442  0.0149  134 ALA   B CB  
6332 N N   . ASP   B 135 ? 0.2657 0.1789 0.3159 -0.0261 0.0312  0.0423  135 ASP   B N   
6333 C CA  . ASP   B 135 ? 0.2823 0.1727 0.3355 -0.0196 0.0119  0.0489  135 ASP   B CA  
6334 C C   . ASP   B 135 ? 0.2547 0.1576 0.3179 -0.0091 -0.0032 0.0442  135 ASP   B C   
6335 O O   . ASP   B 135 ? 0.2411 0.1489 0.3387 -0.0105 -0.0005 0.0386  135 ASP   B O   
6336 C CB  . ASP   B 135 ? 0.3219 0.1815 0.3631 -0.0325 0.0051  0.0495  135 ASP   B CB  
6337 C CG  . ASP   B 135 ? 0.3487 0.1786 0.4016 -0.0576 0.0038  0.0403  135 ASP   B CG  
6338 O OD1 . ASP   B 135 ? 0.3646 0.1642 0.4064 -0.0354 -0.0191 0.0294  135 ASP   B OD1 
6339 O OD2 . ASP   B 135 ? 0.3674 0.2151 0.4572 -0.0716 0.0202  0.0367  135 ASP   B OD2 
6344 N N   . PRO   B 136 ? 0.2392 0.1622 0.3297 0.0185  -0.0251 0.0264  136 PRO   B N   
6345 C CA  . PRO   B 136 ? 0.2127 0.1522 0.3381 0.0142  -0.0270 0.0078  136 PRO   B CA  
6346 C C   . PRO   B 136 ? 0.1923 0.1336 0.3470 0.0102  -0.0117 0.0028  136 PRO   B C   
6347 O O   . PRO   B 136 ? 0.1720 0.1383 0.3382 0.0076  0.0003  0.0097  136 PRO   B O   
6348 C CB  . PRO   B 136 ? 0.2186 0.1744 0.3311 0.0212  -0.0311 -0.0034 136 PRO   B CB  
6349 C CG  . PRO   B 136 ? 0.2436 0.1930 0.3591 0.0277  -0.0139 0.0031  136 PRO   B CG  
6350 C CD  . PRO   B 136 ? 0.2484 0.1810 0.3525 0.0387  -0.0104 0.0160  136 PRO   B CD  
6358 N N   . ILE   B 137 ? 0.2066 0.1326 0.3583 0.0117  -0.0101 -0.0003 137 ILE   B N   
6359 C CA  . ILE   B 137 ? 0.2105 0.1237 0.3615 -0.0005 -0.0014 -0.0053 137 ILE   B CA  
6360 C C   . ILE   B 137 ? 0.1986 0.1355 0.3562 -0.0091 0.0144  0.0054  137 ILE   B C   
6361 O O   . ILE   B 137 ? 0.1866 0.1441 0.3446 -0.0136 0.0108  0.0077  137 ILE   B O   
6362 C CB  . ILE   B 137 ? 0.2336 0.1376 0.4043 -0.0060 -0.0033 0.0018  137 ILE   B CB  
6363 C CG1 . ILE   B 137 ? 0.2454 0.1579 0.4466 0.0050  0.0046  -0.0154 137 ILE   B CG1 
6364 C CG2 . ILE   B 137 ? 0.2419 0.1452 0.4243 -0.0359 -0.0002 0.0100  137 ILE   B CG2 
6365 C CD1 . ILE   B 137 ? 0.2639 0.1896 0.4805 0.0112  0.0030  -0.0022 137 ILE   B CD1 
6377 N N   . HIS   B 138 ? 0.2063 0.1378 0.3520 -0.0026 0.0265  0.0209  138 HIS   B N   
6378 C CA  . HIS   B 138 ? 0.2179 0.1476 0.3471 -0.0024 0.0317  0.0244  138 HIS   B CA  
6379 C C   . HIS   B 138 ? 0.1966 0.1393 0.3294 -0.0042 0.0312  0.0356  138 HIS   B C   
6380 O O   . HIS   B 138 ? 0.1824 0.1476 0.3484 -0.0025 0.0406  0.0412  138 HIS   B O   
6381 C CB  . HIS   B 138 ? 0.2516 0.1657 0.3563 -0.0140 0.0566  0.0273  138 HIS   B CB  
6382 C CG  . HIS   B 138 ? 0.2749 0.1773 0.3696 -0.0193 0.0859  0.0457  138 HIS   B CG  
6383 N ND1 . HIS   B 138 ? 0.2838 0.2012 0.3998 -0.0160 0.0961  0.0318  138 HIS   B ND1 
6384 C CD2 . HIS   B 138 ? 0.2882 0.1949 0.3555 -0.0217 0.0961  0.0418  138 HIS   B CD2 
6385 C CE1 . HIS   B 138 ? 0.2843 0.2067 0.3883 -0.0152 0.0978  0.0321  138 HIS   B CE1 
6386 N NE2 . HIS   B 138 ? 0.2912 0.1981 0.3686 -0.0118 0.1005  0.0277  138 HIS   B NE2 
6394 N N   . SER   B 139 ? 0.1929 0.1284 0.3304 0.0031  0.0234  0.0201  139 SER   B N   
6395 C CA  . SER   B 139 ? 0.1917 0.1304 0.3102 0.0027  0.0297  0.0104  139 SER   B CA  
6396 C C   . SER   B 139 ? 0.1605 0.1256 0.3090 0.0046  0.0165  0.0072  139 SER   B C   
6397 O O   . SER   B 139 ? 0.1645 0.1265 0.3126 -0.0048 0.0032  0.0131  139 SER   B O   
6398 C CB  . SER   B 139 ? 0.1926 0.1337 0.3136 0.0012  0.0162  0.0077  139 SER   B CB  
6399 O OG  . SER   B 139 ? 0.1891 0.1250 0.3186 0.0015  -0.0120 0.0224  139 SER   B OG  
6405 N N   . LEU   B 140 ? 0.1632 0.1178 0.2979 -0.0069 0.0128  0.0067  140 LEU   B N   
6406 C CA  . LEU   B 140 ? 0.1593 0.1232 0.3003 -0.0075 0.0066  0.0043  140 LEU   B CA  
6407 C C   . LEU   B 140 ? 0.1528 0.1258 0.3153 -0.0049 0.0038  -0.0069 140 LEU   B C   
6408 O O   . LEU   B 140 ? 0.1499 0.1306 0.3138 -0.0019 -0.0039 0.0092  140 LEU   B O   
6409 C CB  . LEU   B 140 ? 0.1593 0.1244 0.2897 -0.0091 0.0093  -0.0086 140 LEU   B CB  
6410 C CG  . LEU   B 140 ? 0.1633 0.1251 0.2950 -0.0121 0.0007  0.0107  140 LEU   B CG  
6411 C CD1 . LEU   B 140 ? 0.1791 0.1368 0.3145 -0.0131 0.0220  0.0013  140 LEU   B CD1 
6412 C CD2 . LEU   B 140 ? 0.1863 0.1410 0.2879 -0.0117 -0.0055 -0.0015 140 LEU   B CD2 
6424 N N   . ARG   B 141 ? 0.1464 0.1316 0.3095 -0.0055 0.0093  -0.0006 141 ARG   B N   
6425 C CA  . ARG   B 141 ? 0.1536 0.1296 0.3681 -0.0141 0.0238  -0.0025 141 ARG   B CA  
6426 C C   . ARG   B 141 ? 0.1467 0.1282 0.3693 -0.0172 0.0115  -0.0059 141 ARG   B C   
6427 O O   . ARG   B 141 ? 0.1458 0.1283 0.3704 -0.0140 -0.0007 -0.0153 141 ARG   B O   
6428 C CB  . ARG   B 141 ? 0.1680 0.1413 0.3777 -0.0284 0.0362  -0.0054 141 ARG   B CB  
6429 C CG  . ARG   B 141 ? 0.1984 0.1730 0.3822 -0.0250 0.0308  0.0023  141 ARG   B CG  
6430 C CD  . ARG   B 141 ? 0.2425 0.1919 0.3783 -0.0204 0.0199  -0.0138 141 ARG   B CD  
6431 N NE  . ARG   B 141 ? 0.2582 0.1917 0.3639 -0.0289 0.0203  -0.0288 141 ARG   B NE  
6432 C CZ  . ARG   B 141 ? 0.2670 0.1802 0.3452 -0.0256 0.0221  -0.0287 141 ARG   B CZ  
6433 N NH1 . ARG   B 141 ? 0.2910 0.1571 0.3400 -0.0257 0.0241  -0.0184 141 ARG   B NH1 
6434 N NH2 . ARG   B 141 ? 0.2592 0.1955 0.3394 -0.0177 -0.0085 -0.0238 141 ARG   B NH2 
6448 N N   . VAL   B 142 ? 0.1587 0.1253 0.3367 -0.0154 0.0152  -0.0076 142 VAL   B N   
6449 C CA  . VAL   B 142 ? 0.1463 0.1241 0.3184 -0.0086 0.0167  -0.0057 142 VAL   B CA  
6450 C C   . VAL   B 142 ? 0.1388 0.1285 0.3225 -0.0068 0.0038  -0.0049 142 VAL   B C   
6451 O O   . VAL   B 142 ? 0.1475 0.1301 0.3292 0.0033  0.0042  -0.0027 142 VAL   B O   
6452 C CB  . VAL   B 142 ? 0.1608 0.1351 0.3205 -0.0012 0.0220  -0.0005 142 VAL   B CB  
6453 C CG1 . VAL   B 142 ? 0.1568 0.1430 0.3219 0.0056  0.0291  -0.0008 142 VAL   B CG1 
6454 C CG2 . VAL   B 142 ? 0.1879 0.1417 0.3328 -0.0005 0.0063  0.0100  142 VAL   B CG2 
6464 N N   . CYS   B 143 ? 0.1389 0.1277 0.3145 -0.0032 0.0098  -0.0015 143 CYS   B N   
6465 C CA  . CYS   B 143 ? 0.1365 0.1243 0.3121 -0.0126 0.0038  -0.0021 143 CYS   B CA  
6466 C C   . CYS   B 143 ? 0.1373 0.1232 0.3072 -0.0089 -0.0068 0.0028  143 CYS   B C   
6467 O O   . CYS   B 143 ? 0.1418 0.1337 0.2925 -0.0033 -0.0129 -0.0020 143 CYS   B O   
6468 C CB  . CYS   B 143 ? 0.1538 0.1382 0.2888 -0.0083 0.0012  0.0029  143 CYS   B CB  
6469 S SG  . CYS   B 143 ? 0.1497 0.1533 0.2691 -0.0038 -0.0023 0.0046  143 CYS   B SG  
6475 N N   . VAL   B 144 ? 0.1403 0.1284 0.3347 -0.0125 -0.0119 -0.0120 144 VAL   B N   
6476 C CA  . VAL   B 144 ? 0.1503 0.1331 0.3463 -0.0129 -0.0234 -0.0175 144 VAL   B CA  
6477 C C   . VAL   B 144 ? 0.1442 0.1373 0.3613 -0.0090 -0.0226 0.0024  144 VAL   B C   
6478 O O   . VAL   B 144 ? 0.1534 0.1581 0.3665 -0.0015 -0.0259 0.0149  144 VAL   B O   
6479 C CB  . VAL   B 144 ? 0.1678 0.1617 0.3922 -0.0150 -0.0204 -0.0344 144 VAL   B CB  
6480 C CG1 . VAL   B 144 ? 0.1962 0.2097 0.4141 -0.0115 -0.0129 -0.0314 144 VAL   B CG1 
6481 C CG2 . VAL   B 144 ? 0.1841 0.1688 0.3840 -0.0027 -0.0272 -0.0475 144 VAL   B CG2 
6491 N N   . ASP   B 145 ? 0.1445 0.1361 0.3489 -0.0074 -0.0166 -0.0117 145 ASP   B N   
6492 C CA  . ASP   B 145 ? 0.1454 0.1402 0.3705 -0.0038 0.0019  -0.0002 145 ASP   B CA  
6493 C C   . ASP   B 145 ? 0.1431 0.1462 0.3518 -0.0059 -0.0017 -0.0082 145 ASP   B C   
6494 O O   . ASP   B 145 ? 0.1471 0.1622 0.4119 -0.0122 -0.0026 -0.0287 145 ASP   B O   
6495 C CB  . ASP   B 145 ? 0.1531 0.1446 0.4193 -0.0177 0.0190  0.0044  145 ASP   B CB  
6496 C CG  . ASP   B 145 ? 0.1671 0.1536 0.4680 -0.0189 0.0262  -0.0009 145 ASP   B CG  
6497 O OD1 . ASP   B 145 ? 0.1701 0.1580 0.4827 -0.0151 -0.0191 -0.0172 145 ASP   B OD1 
6498 O OD2 . ASP   B 145 ? 0.1928 0.1618 0.5133 -0.0329 0.0530  0.0032  145 ASP   B OD2 
6503 N N   . THR   B 146 ? 0.1362 0.1354 0.3160 -0.0082 -0.0080 0.0011  146 THR   B N   
6504 C CA  . THR   B 146 ? 0.1472 0.1284 0.3056 -0.0110 -0.0059 0.0003  146 THR   B CA  
6505 C C   . THR   B 146 ? 0.1452 0.1281 0.2979 -0.0085 -0.0110 0.0046  146 THR   B C   
6506 O O   . THR   B 146 ? 0.1397 0.1264 0.3156 -0.0072 -0.0044 0.0077  146 THR   B O   
6507 C CB  . THR   B 146 ? 0.1483 0.1297 0.3169 -0.0090 0.0120  -0.0052 146 THR   B CB  
6508 O OG1 . THR   B 146 ? 0.1549 0.1313 0.3164 -0.0054 0.0122  0.0138  146 THR   B OG1 
6509 C CG2 . THR   B 146 ? 0.1572 0.1392 0.3123 -0.0053 0.0015  0.0005  146 THR   B CG2 
6517 N N   . VAL   B 147 ? 0.1566 0.1290 0.2749 -0.0076 0.0007  0.0019  147 VAL   B N   
6518 C CA  . VAL   B 147 ? 0.1537 0.1250 0.2792 -0.0099 -0.0157 0.0068  147 VAL   B CA  
6519 C C   . VAL   B 147 ? 0.1487 0.1276 0.2843 -0.0173 -0.0198 -0.0059 147 VAL   B C   
6520 O O   . VAL   B 147 ? 0.1600 0.1398 0.2963 -0.0171 -0.0423 -0.0049 147 VAL   B O   
6521 C CB  . VAL   B 147 ? 0.1476 0.1399 0.2648 -0.0096 -0.0152 0.0045  147 VAL   B CB  
6522 C CG1 . VAL   B 147 ? 0.1469 0.1558 0.2254 -0.0102 -0.0091 0.0099  147 VAL   B CG1 
6523 C CG2 . VAL   B 147 ? 0.1484 0.1352 0.2612 -0.0098 -0.0107 -0.0081 147 VAL   B CG2 
6533 N N   . ARG   B 148 ? 0.1466 0.1305 0.2741 -0.0103 -0.0229 -0.0142 148 ARG   B N   
6534 C CA  . ARG   B 148 ? 0.1465 0.1460 0.2709 -0.0070 -0.0383 -0.0088 148 ARG   B CA  
6535 C C   . ARG   B 148 ? 0.1541 0.1519 0.2421 -0.0087 -0.0512 0.0024  148 ARG   B C   
6536 O O   . ARG   B 148 ? 0.1744 0.1821 0.2647 -0.0290 -0.0620 0.0106  148 ARG   B O   
6537 C CB  . ARG   B 148 ? 0.1524 0.1580 0.2673 -0.0020 -0.0422 -0.0106 148 ARG   B CB  
6538 C CG  . ARG   B 148 ? 0.1555 0.1726 0.2725 -0.0059 -0.0329 -0.0284 148 ARG   B CG  
6539 C CD  . ARG   B 148 ? 0.1631 0.1860 0.2851 0.0129  -0.0282 -0.0413 148 ARG   B CD  
6540 N NE  . ARG   B 148 ? 0.1701 0.1856 0.2918 0.0227  -0.0474 -0.0368 148 ARG   B NE  
6541 C CZ  . ARG   B 148 ? 0.1587 0.1775 0.2843 0.0167  -0.0335 -0.0316 148 ARG   B CZ  
6542 N NH1 . ARG   B 148 ? 0.1501 0.1758 0.2788 0.0010  -0.0139 -0.0328 148 ARG   B NH1 
6543 N NH2 . ARG   B 148 ? 0.1805 0.1572 0.2826 0.0204  -0.0302 -0.0225 148 ARG   B NH2 
6557 N N   . THR   B 149 ? 0.1644 0.1365 0.2538 -0.0109 -0.0458 -0.0036 149 THR   B N   
6558 C CA  . THR   B 149 ? 0.1679 0.1471 0.2411 -0.0129 -0.0447 0.0083  149 THR   B CA  
6559 C C   . THR   B 149 ? 0.1708 0.1440 0.2273 -0.0169 -0.0494 0.0084  149 THR   B C   
6560 O O   . THR   B 149 ? 0.1793 0.1441 0.2399 -0.0203 -0.0279 0.0060  149 THR   B O   
6561 C CB  . THR   B 149 ? 0.1717 0.1460 0.2639 -0.0143 -0.0398 0.0092  149 THR   B CB  
6562 O OG1 . THR   B 149 ? 0.1694 0.1513 0.2522 -0.0214 -0.0465 0.0159  149 THR   B OG1 
6563 C CG2 . THR   B 149 ? 0.1867 0.1497 0.2669 -0.0074 -0.0241 0.0129  149 THR   B CG2 
6571 N N   . ASN   B 150 ? 0.1791 0.1502 0.2116 -0.0228 -0.0504 0.0128  150 ASN   B N   
6572 C CA  . ASN   B 150 ? 0.1888 0.1670 0.1980 -0.0243 -0.0392 0.0057  150 ASN   B CA  
6573 C C   . ASN   B 150 ? 0.1717 0.1562 0.2126 -0.0215 -0.0418 0.0001  150 ASN   B C   
6574 O O   . ASN   B 150 ? 0.1807 0.1521 0.2391 -0.0321 -0.0447 -0.0069 150 ASN   B O   
6575 C CB  . ASN   B 150 ? 0.2130 0.2053 0.2101 -0.0264 -0.0512 0.0104  150 ASN   B CB  
6576 C CG  . ASN   B 150 ? 0.2404 0.2472 0.2610 -0.0274 -0.0620 0.0364  150 ASN   B CG  
6577 O OD1 . ASN   B 150 ? 0.2490 0.2708 0.2688 -0.0368 -0.0779 0.0372  150 ASN   B OD1 
6578 N ND2 . ASN   B 150 ? 0.2528 0.2674 0.3014 -0.0185 -0.0686 0.0685  150 ASN   B ND2 
6585 N N   . VAL   B 151 ? 0.1668 0.1518 0.2119 -0.0230 -0.0446 0.0060  151 VAL   B N   
6586 C CA  . VAL   B 151 ? 0.1713 0.1516 0.2157 -0.0291 -0.0378 0.0035  151 VAL   B CA  
6587 C C   . VAL   B 151 ? 0.1755 0.1453 0.2175 -0.0359 -0.0452 -0.0064 151 VAL   B C   
6588 O O   . VAL   B 151 ? 0.1871 0.1563 0.2358 -0.0342 -0.0339 -0.0096 151 VAL   B O   
6589 C CB  . VAL   B 151 ? 0.1849 0.1608 0.2290 -0.0163 -0.0283 0.0065  151 VAL   B CB  
6590 C CG1 . VAL   B 151 ? 0.1839 0.1650 0.2677 -0.0210 -0.0265 0.0025  151 VAL   B CG1 
6591 C CG2 . VAL   B 151 ? 0.1937 0.1724 0.1937 -0.0019 -0.0315 0.0077  151 VAL   B CG2 
6601 N N   . TYR   B 152 ? 0.1714 0.1382 0.1986 -0.0265 -0.0416 0.0004  152 TYR   B N   
6602 C CA  . TYR   B 152 ? 0.1786 0.1578 0.1870 -0.0334 -0.0287 -0.0020 152 TYR   B CA  
6603 C C   . TYR   B 152 ? 0.1723 0.1422 0.1994 -0.0264 -0.0187 -0.0051 152 TYR   B C   
6604 O O   . TYR   B 152 ? 0.1689 0.1482 0.1964 -0.0265 -0.0233 0.0062  152 TYR   B O   
6605 C CB  . TYR   B 152 ? 0.1963 0.1710 0.1885 -0.0388 -0.0269 0.0082  152 TYR   B CB  
6606 C CG  . TYR   B 152 ? 0.2141 0.1771 0.1895 -0.0521 -0.0260 0.0075  152 TYR   B CG  
6607 C CD1 . TYR   B 152 ? 0.2222 0.1920 0.1862 -0.0449 -0.0425 0.0094  152 TYR   B CD1 
6608 C CD2 . TYR   B 152 ? 0.2374 0.1975 0.1927 -0.0514 -0.0286 -0.0067 152 TYR   B CD2 
6609 C CE1 . TYR   B 152 ? 0.2447 0.2149 0.2053 -0.0389 -0.0449 0.0141  152 TYR   B CE1 
6610 C CE2 . TYR   B 152 ? 0.2473 0.2247 0.1856 -0.0514 -0.0341 -0.0034 152 TYR   B CE2 
6611 C CZ  . TYR   B 152 ? 0.2457 0.2387 0.1698 -0.0449 -0.0585 0.0183  152 TYR   B CZ  
6612 O OH  . TYR   B 152 ? 0.2624 0.2757 0.2345 -0.0274 -0.0495 0.0284  152 TYR   B OH  
6622 N N   . LEU   B 153 ? 0.1741 0.1349 0.2029 -0.0325 -0.0158 -0.0006 153 LEU   B N   
6623 C CA  . LEU   B 153 ? 0.1750 0.1343 0.1979 -0.0279 -0.0151 -0.0051 153 LEU   B CA  
6624 C C   . LEU   B 153 ? 0.1725 0.1301 0.1997 -0.0296 -0.0141 -0.0196 153 LEU   B C   
6625 O O   . LEU   B 153 ? 0.1718 0.1554 0.2112 -0.0144 -0.0052 -0.0313 153 LEU   B O   
6626 C CB  . LEU   B 153 ? 0.1730 0.1267 0.2009 -0.0303 -0.0136 -0.0062 153 LEU   B CB  
6627 C CG  . LEU   B 153 ? 0.1646 0.1375 0.2411 -0.0269 -0.0043 -0.0038 153 LEU   B CG  
6628 C CD1 . LEU   B 153 ? 0.1733 0.1545 0.2467 -0.0263 -0.0009 0.0157  153 LEU   B CD1 
6629 C CD2 . LEU   B 153 ? 0.1576 0.1510 0.2550 -0.0294 0.0069  0.0120  153 LEU   B CD2 
6641 N N   . ALA   B 154 ? 0.1627 0.1334 0.2129 -0.0106 -0.0108 -0.0208 154 ALA   B N   
6642 C CA  . ALA   B 154 ? 0.1733 0.1474 0.2448 -0.0038 -0.0029 -0.0216 154 ALA   B CA  
6643 C C   . ALA   B 154 ? 0.1860 0.1536 0.2612 -0.0005 -0.0177 -0.0287 154 ALA   B C   
6644 O O   . ALA   B 154 ? 0.2324 0.1507 0.2811 0.0070  -0.0125 -0.0112 154 ALA   B O   
6645 C CB  . ALA   B 154 ? 0.1694 0.1598 0.2614 -0.0041 0.0053  -0.0270 154 ALA   B CB  
6651 N N   . VAL   B 155 ? 0.1469 0.1467 0.2723 -0.0082 0.0088  -0.0140 155 VAL   B N   
6652 C CA  . VAL   B 155 ? 0.1469 0.1415 0.3011 -0.0051 -0.0146 -0.0101 155 VAL   B CA  
6653 C C   . VAL   B 155 ? 0.1460 0.1411 0.2773 -0.0083 -0.0095 -0.0273 155 VAL   B C   
6654 O O   . VAL   B 155 ? 0.1723 0.1595 0.2979 0.0024  -0.0134 -0.0517 155 VAL   B O   
6655 C CB  . VAL   B 155 ? 0.1519 0.1534 0.3254 -0.0107 -0.0318 0.0077  155 VAL   B CB  
6656 C CG1 . VAL   B 155 ? 0.1640 0.1503 0.3245 -0.0170 -0.0277 0.0080  155 VAL   B CG1 
6657 C CG2 . VAL   B 155 ? 0.1469 0.1710 0.3446 -0.0117 -0.0244 0.0424  155 VAL   B CG2 
6667 N N   . PHE   B 156 ? 0.1389 0.1512 0.3073 -0.0045 0.0041  -0.0251 156 PHE   B N   
6668 C CA  . PHE   B 156 ? 0.1445 0.1511 0.3399 0.0017  -0.0018 -0.0349 156 PHE   B CA  
6669 C C   . PHE   B 156 ? 0.1455 0.1687 0.3732 0.0100  -0.0142 -0.0433 156 PHE   B C   
6670 O O   . PHE   B 156 ? 0.1667 0.1929 0.3850 0.0208  -0.0002 -0.0402 156 PHE   B O   
6671 C CB  . PHE   B 156 ? 0.1513 0.1435 0.3317 -0.0044 -0.0062 -0.0237 156 PHE   B CB  
6672 C CG  . PHE   B 156 ? 0.1587 0.1623 0.3415 -0.0054 -0.0134 0.0037  156 PHE   B CG  
6673 C CD1 . PHE   B 156 ? 0.1617 0.1938 0.3737 0.0062  -0.0004 0.0389  156 PHE   B CD1 
6674 C CD2 . PHE   B 156 ? 0.1662 0.1822 0.3290 0.0074  -0.0123 0.0023  156 PHE   B CD2 
6675 C CE1 . PHE   B 156 ? 0.1641 0.2126 0.3718 0.0033  -0.0006 0.0339  156 PHE   B CE1 
6676 C CE2 . PHE   B 156 ? 0.1657 0.2027 0.3563 0.0120  -0.0179 0.0007  156 PHE   B CE2 
6677 C CZ  . PHE   B 156 ? 0.1563 0.2110 0.3732 0.0112  -0.0249 0.0109  156 PHE   B CZ  
6687 N N   . ASP   B 157 ? 0.1487 0.1593 0.3994 0.0155  -0.0243 -0.0199 157 ASP   B N   
6688 C CA  . ASP   B 157 ? 0.1596 0.1730 0.4244 0.0118  -0.0296 -0.0242 157 ASP   B CA  
6689 C C   . ASP   B 157 ? 0.1658 0.1747 0.4227 0.0110  -0.0251 -0.0520 157 ASP   B C   
6690 O O   . ASP   B 157 ? 0.1519 0.1656 0.4050 0.0046  -0.0241 -0.0323 157 ASP   B O   
6691 C CB  . ASP   B 157 ? 0.1846 0.1936 0.4296 0.0051  -0.0617 -0.0117 157 ASP   B CB  
6692 C CG  . ASP   B 157 ? 0.2260 0.2113 0.4515 0.0011  -0.0489 -0.0145 157 ASP   B CG  
6693 O OD1 . ASP   B 157 ? 0.2372 0.2052 0.4681 0.0123  -0.0308 -0.0111 157 ASP   B OD1 
6694 O OD2 . ASP   B 157 ? 0.2634 0.2297 0.4782 0.0015  -0.0329 -0.0162 157 ASP   B OD2 
6699 N N   A LYS   B 158 ? 0.1689 0.1982 0.4206 0.0099  -0.0158 -0.0752 158 LYS   B N   
6700 N N   B LYS   B 158 ? 0.1724 0.1986 0.4130 0.0123  -0.0172 -0.0718 158 LYS   B N   
6701 C CA  A LYS   B 158 ? 0.1887 0.2111 0.4204 0.0047  -0.0075 -0.1005 158 LYS   B CA  
6702 C CA  B LYS   B 158 ? 0.1921 0.2130 0.4103 0.0103  -0.0087 -0.0927 158 LYS   B CA  
6703 C C   A LYS   B 158 ? 0.1885 0.1992 0.4375 0.0068  -0.0172 -0.0966 158 LYS   B C   
6704 C C   B LYS   B 158 ? 0.1911 0.2011 0.4281 0.0099  -0.0166 -0.0912 158 LYS   B C   
6705 O O   A LYS   B 158 ? 0.1841 0.1964 0.4532 -0.0019 -0.0174 -0.1000 158 LYS   B O   
6706 O O   B LYS   B 158 ? 0.1882 0.1990 0.4369 0.0025  -0.0175 -0.0918 158 LYS   B O   
6707 C CB  A LYS   B 158 ? 0.2187 0.2497 0.4172 0.0026  0.0006  -0.1044 158 LYS   B CB  
6708 C CB  B LYS   B 158 ? 0.2207 0.2479 0.4029 0.0133  -0.0012 -0.0947 158 LYS   B CB  
6709 C CG  A LYS   B 158 ? 0.2555 0.2861 0.4166 0.0052  0.0045  -0.1093 158 LYS   B CG  
6710 C CG  B LYS   B 158 ? 0.2538 0.2791 0.4009 0.0185  0.0042  -0.0989 158 LYS   B CG  
6711 C CD  A LYS   B 158 ? 0.2815 0.3204 0.4228 0.0024  0.0071  -0.1022 158 LYS   B CD  
6712 C CD  B LYS   B 158 ? 0.2793 0.3089 0.4076 0.0165  0.0074  -0.0938 158 LYS   B CD  
6713 C CE  A LYS   B 158 ? 0.3002 0.3397 0.4264 0.0036  0.0091  -0.0948 158 LYS   B CE  
6714 C CE  B LYS   B 158 ? 0.2976 0.3278 0.4124 0.0173  0.0104  -0.0873 158 LYS   B CE  
6715 N NZ  A LYS   B 158 ? 0.3006 0.3458 0.4265 -0.0001 0.0073  -0.0908 158 LYS   B NZ  
6716 N NZ  B LYS   B 158 ? 0.3009 0.3348 0.4155 0.0152  0.0119  -0.0838 158 LYS   B NZ  
6743 N N   . ASN   B 159 ? 0.1895 0.1883 0.4559 0.0113  -0.0244 -0.0806 159 ASN   B N   
6744 C CA  . ASN   B 159 ? 0.2094 0.1800 0.4758 0.0195  -0.0397 -0.0618 159 ASN   B CA  
6745 C C   . ASN   B 159 ? 0.1863 0.1605 0.4721 0.0147  -0.0685 -0.0467 159 ASN   B C   
6746 O O   . ASN   B 159 ? 0.1873 0.1534 0.4904 -0.0028 -0.0691 -0.0291 159 ASN   B O   
6747 C CB  . ASN   B 159 ? 0.2361 0.1981 0.5019 0.0288  -0.0416 -0.0504 159 ASN   B CB  
6748 C CG  . ASN   B 159 ? 0.2647 0.2265 0.5170 0.0290  -0.0523 -0.0477 159 ASN   B CG  
6749 O OD1 . ASN   B 159 ? 0.2795 0.2314 0.5196 0.0401  -0.0549 -0.0499 159 ASN   B OD1 
6750 N ND2 . ASN   B 159 ? 0.2648 0.2373 0.5405 0.0247  -0.0582 -0.0447 159 ASN   B ND2 
6758 N N   . LEU   B 160 ? 0.1738 0.1659 0.4587 0.0065  -0.0574 -0.0423 160 LEU   B N   
6759 C CA  . LEU   B 160 ? 0.1721 0.1625 0.4258 0.0068  -0.0553 -0.0189 160 LEU   B CA  
6760 C C   . LEU   B 160 ? 0.1626 0.1491 0.4087 -0.0001 -0.0298 -0.0282 160 LEU   B C   
6761 O O   . LEU   B 160 ? 0.1474 0.1564 0.4079 -0.0039 -0.0418 -0.0232 160 LEU   B O   
6762 C CB  . LEU   B 160 ? 0.1731 0.1716 0.3864 0.0071  -0.0640 -0.0053 160 LEU   B CB  
6763 C CG  . LEU   B 160 ? 0.1662 0.1839 0.3623 0.0112  -0.0481 0.0028  160 LEU   B CG  
6764 C CD1 . LEU   B 160 ? 0.1858 0.2060 0.3739 -0.0057 -0.0345 0.0085  160 LEU   B CD1 
6765 C CD2 . LEU   B 160 ? 0.1685 0.1917 0.3462 0.0170  -0.0251 -0.0123 160 LEU   B CD2 
6777 N N   . TYR   B 161 ? 0.1620 0.1552 0.4098 -0.0039 0.0046  -0.0499 161 TYR   B N   
6778 C CA  . TYR   B 161 ? 0.1752 0.1554 0.3956 -0.0138 0.0211  -0.0499 161 TYR   B CA  
6779 C C   . TYR   B 161 ? 0.1828 0.1547 0.3913 -0.0135 0.0298  -0.0404 161 TYR   B C   
6780 O O   . TYR   B 161 ? 0.1866 0.1527 0.3844 -0.0230 0.0267  -0.0281 161 TYR   B O   
6781 C CB  . TYR   B 161 ? 0.1917 0.1717 0.3753 -0.0224 0.0324  -0.0647 161 TYR   B CB  
6782 C CG  . TYR   B 161 ? 0.2326 0.1771 0.3627 -0.0331 0.0384  -0.0728 161 TYR   B CG  
6783 C CD1 . TYR   B 161 ? 0.2372 0.1719 0.3634 -0.0459 0.0493  -0.0656 161 TYR   B CD1 
6784 C CD2 . TYR   B 161 ? 0.2554 0.1818 0.3599 -0.0356 0.0257  -0.0702 161 TYR   B CD2 
6785 C CE1 . TYR   B 161 ? 0.2632 0.1960 0.3722 -0.0472 0.0477  -0.0550 161 TYR   B CE1 
6786 C CE2 . TYR   B 161 ? 0.2801 0.1987 0.3541 -0.0424 0.0386  -0.0588 161 TYR   B CE2 
6787 C CZ  . TYR   B 161 ? 0.2840 0.2020 0.3665 -0.0568 0.0289  -0.0464 161 TYR   B CZ  
6788 O OH  . TYR   B 161 ? 0.3159 0.2227 0.4007 -0.0533 0.0284  -0.0460 161 TYR   B OH  
6798 N N   . ASP   B 162 ? 0.1875 0.1558 0.4003 -0.0169 0.0040  -0.0639 162 ASP   B N   
6799 C CA  . ASP   B 162 ? 0.1868 0.1578 0.4137 -0.0072 -0.0094 -0.0570 162 ASP   B CA  
6800 C C   . ASP   B 162 ? 0.1845 0.1526 0.4141 -0.0070 -0.0114 -0.0463 162 ASP   B C   
6801 O O   . ASP   B 162 ? 0.1833 0.1626 0.4368 -0.0152 -0.0471 -0.0352 162 ASP   B O   
6802 C CB  . ASP   B 162 ? 0.2015 0.1714 0.4368 -0.0012 -0.0126 -0.0766 162 ASP   B CB  
6803 C CG  . ASP   B 162 ? 0.2116 0.2019 0.4571 0.0044  -0.0065 -0.0980 162 ASP   B CG  
6804 O OD1 . ASP   B 162 ? 0.2195 0.2266 0.4611 -0.0032 -0.0006 -0.1036 162 ASP   B OD1 
6805 O OD2 . ASP   B 162 ? 0.2219 0.2254 0.4714 0.0199  0.0159  -0.0827 162 ASP   B OD2 
6810 N N   . LYS   B 163 ? 0.1802 0.1396 0.3902 -0.0049 -0.0284 -0.0275 163 LYS   B N   
6811 C CA  . LYS   B 163 ? 0.1855 0.1461 0.3875 -0.0142 -0.0235 -0.0047 163 LYS   B CA  
6812 C C   . LYS   B 163 ? 0.1634 0.1482 0.3778 -0.0143 -0.0253 -0.0011 163 LYS   B C   
6813 O O   . LYS   B 163 ? 0.1556 0.1607 0.4031 -0.0242 -0.0375 0.0056  163 LYS   B O   
6814 C CB  . LYS   B 163 ? 0.2313 0.1787 0.4043 -0.0008 -0.0376 0.0168  163 LYS   B CB  
6815 C CG  . LYS   B 163 ? 0.2992 0.2497 0.4510 0.0020  -0.0301 0.0160  163 LYS   B CG  
6816 C CD  . LYS   B 163 ? 0.3508 0.2958 0.4974 -0.0064 -0.0222 0.0126  163 LYS   B CD  
6817 C CE  . LYS   B 163 ? 0.4127 0.3538 0.5345 -0.0105 -0.0144 0.0184  163 LYS   B CE  
6818 N NZ  . LYS   B 163 ? 0.4549 0.3824 0.5485 -0.0159 -0.0145 0.0207  163 LYS   B NZ  
6832 N N   . LEU   B 164 ? 0.1556 0.1347 0.3458 -0.0118 -0.0258 -0.0087 164 LEU   B N   
6833 C CA  . LEU   B 164 ? 0.1556 0.1382 0.3263 -0.0087 -0.0281 -0.0097 164 LEU   B CA  
6834 C C   . LEU   B 164 ? 0.1665 0.1444 0.3457 -0.0137 -0.0408 0.0018  164 LEU   B C   
6835 O O   . LEU   B 164 ? 0.1674 0.1654 0.3800 -0.0151 -0.0430 0.0033  164 LEU   B O   
6836 C CB  . LEU   B 164 ? 0.1440 0.1388 0.3212 -0.0099 -0.0164 -0.0033 164 LEU   B CB  
6837 C CG  . LEU   B 164 ? 0.1596 0.1539 0.3204 -0.0104 -0.0174 0.0113  164 LEU   B CG  
6838 C CD1 . LEU   B 164 ? 0.1702 0.1575 0.3177 -0.0201 -0.0194 -0.0053 164 LEU   B CD1 
6839 C CD2 . LEU   B 164 ? 0.1757 0.1901 0.3371 -0.0126 -0.0113 0.0017  164 LEU   B CD2 
6851 N N   . VAL   B 165 ? 0.2049 0.1508 0.3558 -0.0248 -0.0508 -0.0015 165 VAL   B N   
6852 C CA  . VAL   B 165 ? 0.2469 0.1647 0.3680 -0.0385 -0.0681 -0.0014 165 VAL   B CA  
6853 C C   . VAL   B 165 ? 0.2806 0.1816 0.3988 -0.0417 -0.1030 -0.0027 165 VAL   B C   
6854 O O   . VAL   B 165 ? 0.3086 0.1930 0.4164 -0.0441 -0.1098 -0.0069 165 VAL   B O   
6855 C CB  . VAL   B 165 ? 0.2768 0.1835 0.3523 -0.0223 -0.0393 -0.0139 165 VAL   B CB  
6856 C CG1 . VAL   B 165 ? 0.2972 0.1939 0.3788 -0.0268 -0.0310 -0.0083 165 VAL   B CG1 
6857 C CG2 . VAL   B 165 ? 0.2709 0.1807 0.3402 -0.0119 -0.0179 -0.0202 165 VAL   B CG2 
6867 N N   . SER   B 166 ? 0.2839 0.1705 0.4426 -0.0421 -0.1176 -0.0226 166 SER   B N   
6868 C CA  . SER   B 166 ? 0.2775 0.1709 0.4825 -0.0410 -0.0996 -0.0285 166 SER   B CA  
6869 C C   . SER   B 166 ? 0.2557 0.1726 0.5056 -0.0431 -0.0905 0.0029  166 SER   B C   
6870 O O   . SER   B 166 ? 0.2609 0.2004 0.5394 -0.0624 -0.1058 -0.0228 166 SER   B O   
6871 C CB  . SER   B 166 ? 0.2742 0.1781 0.5020 -0.0338 -0.0887 -0.0351 166 SER   B CB  
6872 O OG  . SER   B 166 ? 0.2527 0.1778 0.5263 -0.0316 -0.0877 -0.0145 166 SER   B OG  
6878 N N   . SER   B 167 ? 0.2277 0.1663 0.4756 -0.0457 -0.0958 0.0428  167 SER   B N   
6879 C CA  . SER   B 167 ? 0.2248 0.1843 0.4644 -0.0314 -0.0720 0.0554  167 SER   B CA  
6880 C C   . SER   B 167 ? 0.2080 0.1944 0.4376 -0.0495 -0.0684 0.0670  167 SER   B C   
6881 O O   . SER   B 167 ? 0.2011 0.2121 0.4387 -0.0547 -0.0766 0.0664  167 SER   B O   
6882 C CB  . SER   B 167 ? 0.2168 0.1824 0.4724 -0.0292 -0.0475 0.0577  167 SER   B CB  
6883 O OG  . SER   B 167 ? 0.2087 0.1896 0.4796 -0.0259 -0.0174 0.0540  167 SER   B OG  
6889 N N   . PHE   B 168 ? 0.2098 0.1926 0.4222 -0.0459 -0.0441 0.0696  168 PHE   B N   
6890 C CA  . PHE   B 168 ? 0.2077 0.1917 0.3749 -0.0485 -0.0344 0.0401  168 PHE   B CA  
6891 C C   . PHE   B 168 ? 0.1757 0.1787 0.3270 -0.0299 -0.0190 0.0083  168 PHE   B C   
6892 O O   . PHE   B 168 ? 0.2060 0.1620 0.3141 -0.0085 -0.0162 -0.0030 168 PHE   B O   
6893 C CB  . PHE   B 168 ? 0.2322 0.1980 0.3797 -0.0579 -0.0432 0.0507  168 PHE   B CB  
6894 C CG  . PHE   B 168 ? 0.2598 0.1824 0.3651 -0.0646 -0.0482 0.0181  168 PHE   B CG  
6895 C CD1 . PHE   B 168 ? 0.2899 0.1811 0.3795 -0.0681 -0.0533 0.0110  168 PHE   B CD1 
6896 C CD2 . PHE   B 168 ? 0.2501 0.1714 0.3546 -0.0669 -0.0483 0.0127  168 PHE   B CD2 
6897 C CE1 . PHE   B 168 ? 0.3051 0.1802 0.3455 -0.0585 -0.0396 0.0351  168 PHE   B CE1 
6898 C CE2 . PHE   B 168 ? 0.2831 0.1792 0.3656 -0.0459 -0.0467 0.0091  168 PHE   B CE2 
6899 C CZ  . PHE   B 168 ? 0.2993 0.1739 0.3625 -0.0390 -0.0481 0.0407  168 PHE   B CZ  
6909 N N   . LEU   B 169 ? 0.1939 0.1911 0.3268 -0.0063 0.0050  0.0047  169 LEU   B N   
6910 C CA  . LEU   B 169 ? 0.2245 0.2224 0.3568 -0.0068 0.0042  -0.0224 169 LEU   B CA  
6911 C C   . LEU   B 169 ? 0.2669 0.2471 0.4013 0.0103  0.0055  -0.0537 169 LEU   B C   
6912 O O   . LEU   B 169 ? 0.2941 0.2666 0.4466 0.0097  0.0058  -0.0721 169 LEU   B O   
6913 C CB  . LEU   B 169 ? 0.2482 0.2602 0.3569 -0.0156 0.0006  0.0092  169 LEU   B CB  
6914 C CG  . LEU   B 169 ? 0.2929 0.3000 0.3850 -0.0043 0.0115  0.0134  169 LEU   B CG  
6915 C CD1 . LEU   B 169 ? 0.3152 0.3183 0.3944 -0.0111 0.0055  0.0299  169 LEU   B CD1 
6916 C CD2 . LEU   B 169 ? 0.2852 0.3067 0.3811 0.0163  0.0360  0.0011  169 LEU   B CD2 
6917 O OXT . LEU   B 169 ? 0.2886 0.2611 0.4020 0.0386  0.0207  -0.0547 169 LEU   B OXT 
6929 C C1  T TFA   C .   ? 0.1367 0.1483 0.1370 -0.0126 0.0245  0.0198  201 TFA   A C1  
6930 C C2  T TFA   C .   ? 0.1529 0.1713 0.1791 -0.0177 0.0105  -0.0087 201 TFA   A C2  
6931 O O   T TFA   C .   ? 0.1248 0.1279 0.1274 -0.0106 0.0168  0.0262  201 TFA   A O   
6932 F F1  T TFA   C .   ? 0.1604 0.1772 0.2353 -0.0059 -0.0045 -0.0267 201 TFA   A F1  
6933 F F2  T TFA   C .   ? 0.1594 0.1679 0.1729 -0.0284 0.0230  0.0125  201 TFA   A F2  
6934 F F3  T TFA   C .   ? 0.1665 0.1986 0.2189 -0.0210 0.0297  -0.0228 201 TFA   A F3  
6935 O OXT T TFA   C .   ? 0.1189 0.1502 0.1353 0.0084  0.0442  0.0339  201 TFA   A OXT 
6936 N N2  B A1A85 D .   ? 0.2325 0.2155 0.2517 0.0204  0.0238  0.0150  202 A1A85 A N2  
6937 C C3  B A1A85 D .   ? 0.2619 0.2294 0.3053 0.0077  0.0317  0.0130  202 A1A85 A C3  
6938 C C6  B A1A85 D .   ? 0.2325 0.2097 0.2255 0.0240  0.0113  0.0114  202 A1A85 A C6  
6939 C C9  B A1A85 D .   ? 0.2106 0.2141 0.2306 0.0009  0.0160  0.0192  202 A1A85 A C9  
6940 C C1  B A1A85 D .   ? 0.2695 0.2295 0.2993 -0.0030 0.0505  0.0049  202 A1A85 A C1  
6941 C C10 B A1A85 D .   ? 0.1978 0.1983 0.2161 -0.0021 -0.0146 0.0247  202 A1A85 A C10 
6942 C C11 B A1A85 D .   ? 0.2548 0.2036 0.2774 0.0063  0.0637  0.0230  202 A1A85 A C11 
6943 C C2  B A1A85 D .   ? 0.2698 0.2336 0.2989 0.0023  0.0427  0.0039  202 A1A85 A C2  
6944 C C4  B A1A85 D .   ? 0.2595 0.2232 0.2952 0.0154  0.0285  0.0255  202 A1A85 A C4  
6945 C C5  B A1A85 D .   ? 0.2363 0.2150 0.2546 0.0200  0.0310  0.0254  202 A1A85 A C5  
6946 C C7  B A1A85 D .   ? 0.2181 0.2025 0.2137 0.0157  -0.0033 0.0314  202 A1A85 A C7  
6947 C C8  B A1A85 D .   ? 0.2202 0.2116 0.2277 0.0157  0.0143  0.0244  202 A1A85 A C8  
6948 N N1  B A1A85 D .   ? 0.2506 0.2146 0.2756 0.0152  0.0419  0.0320  202 A1A85 A N1  
6949 N N3  B A1A85 D .   ? 0.2317 0.2031 0.2023 0.0163  0.0083  0.0229  202 A1A85 A N3  
6950 N N4  B A1A85 D .   ? 0.2024 0.1919 0.2143 0.0088  -0.0328 0.0435  202 A1A85 A N4  
6951 O O1  B A1A85 D .   ? 0.2841 0.2394 0.3235 -0.0148 0.0448  -0.0113 202 A1A85 A O1  
6966 O O   . HOH   E .   ? 0.4644 0.4026 0.4869 0.0036  0.1576  -0.0041 301 HOH   A O   
6967 O O   . HOH   E .   ? 0.2529 0.2229 0.3963 -0.0185 -0.0575 0.0175  302 HOH   A O   
6968 O O   A HOH   E .   ? 0.3582 0.6080 0.4568 -0.0848 -0.0106 0.1287  303 HOH   A O   
6969 O O   . HOH   E .   ? 0.6905 0.5343 0.5760 -0.0977 0.2045  0.2046  304 HOH   A O   
6970 O O   . HOH   E .   ? 0.8023 0.6009 0.3935 -0.1829 -0.0170 0.2243  305 HOH   A O   
6971 O O   . HOH   E .   ? 0.3624 0.2814 0.5101 -0.0421 -0.1794 0.1256  306 HOH   A O   
6972 O O   . HOH   E .   ? 0.5337 0.7969 0.5672 -0.0067 0.0522  -0.0284 307 HOH   A O   
6973 O O   . HOH   E .   ? 0.2979 0.7218 0.6307 -0.0469 -0.0905 0.2379  308 HOH   A O   
6974 O O   . HOH   E .   ? 0.6681 0.6547 0.6666 -0.1437 -0.1343 -0.0961 309 HOH   A O   
6975 O O   . HOH   E .   ? 0.3960 0.3733 0.4037 -0.1340 -0.0060 0.1270  310 HOH   A O   
6976 O O   . HOH   E .   ? 0.4833 0.2427 0.7180 -0.0269 0.0594  -0.0622 311 HOH   A O   
6977 O O   . HOH   E .   ? 1.1525 1.1466 0.9085 0.0627  -0.0339 -0.0532 312 HOH   A O   
6978 O O   . HOH   E .   ? 0.6697 0.4755 0.3398 0.1976  -0.1353 0.0424  313 HOH   A O   
6979 O O   . HOH   E .   ? 0.2964 0.4423 0.1785 -0.0777 0.0315  0.0460  314 HOH   A O   
6980 O O   . HOH   E .   ? 0.6243 0.6340 0.3810 -0.0489 -0.0700 0.0963  315 HOH   A O   
6981 O O   . HOH   E .   ? 0.2093 0.5321 0.3815 0.1321  0.0229  0.0930  316 HOH   A O   
6982 O O   . HOH   E .   ? 0.4983 0.2303 0.6946 0.0760  -0.0504 -0.0282 317 HOH   A O   
6983 O O   . HOH   E .   ? 0.2831 0.2518 0.3152 -0.0241 0.0169  -0.0301 318 HOH   A O   
6984 O O   . HOH   E .   ? 0.1864 0.1844 0.3043 -0.0291 0.0031  0.0558  319 HOH   A O   
6985 O O   A HOH   E .   ? 0.1397 0.1928 0.2272 0.0442  0.0442  0.0548  320 HOH   A O   
6986 O O   . HOH   E .   ? 0.2662 0.4239 0.4476 0.0547  -0.0662 0.0558  321 HOH   A O   
6987 O O   . HOH   E .   ? 0.2336 0.1825 0.2912 0.0378  -0.0315 -0.0077 322 HOH   A O   
6988 O O   . HOH   E .   ? 0.5587 0.4494 0.5582 0.0236  -0.0103 0.0276  323 HOH   A O   
6989 O O   . HOH   E .   ? 0.5531 0.3589 0.3915 -0.0903 -0.1651 0.0403  324 HOH   A O   
6990 O O   . HOH   E .   ? 0.1991 0.2777 0.2832 -0.0101 0.0367  0.0669  325 HOH   A O   
6991 O O   . HOH   E .   ? 0.2554 0.2243 0.2332 -0.0617 0.0033  0.0489  326 HOH   A O   
6992 O O   . HOH   E .   ? 0.2194 0.2006 0.3904 -0.0520 0.0238  -0.0207 327 HOH   A O   
6993 O O   . HOH   E .   ? 0.2853 0.2011 0.3018 0.0062  0.0150  0.0290  328 HOH   A O   
6994 O O   . HOH   E .   ? 0.2234 0.3031 0.5045 0.0132  0.1175  0.1571  329 HOH   A O   
6995 O O   . HOH   E .   ? 0.2028 0.1904 0.2547 0.0198  -0.0206 0.0373  330 HOH   A O   
6996 O O   . HOH   E .   ? 0.5291 0.7201 0.4100 0.2123  -0.0364 -0.0170 331 HOH   A O   
6997 O O   . HOH   E .   ? 0.5186 0.6132 0.4828 0.0265  0.2851  -0.0867 332 HOH   A O   
6998 O O   . HOH   E .   ? 0.3973 0.3568 0.5036 -0.0157 0.2069  0.0869  333 HOH   A O   
6999 O O   . HOH   E .   ? 0.2316 0.4098 0.4611 -0.0572 -0.0893 0.1621  334 HOH   A O   
7000 O O   . HOH   E .   ? 0.2156 0.3901 0.4381 -0.0557 0.0379  -0.0923 335 HOH   A O   
7001 O O   . HOH   E .   ? 0.6477 0.6600 0.5007 0.0237  0.0161  -0.1357 336 HOH   A O   
7002 O O   B HOH   E .   ? 0.2579 0.1716 0.3181 -0.0054 -0.0041 0.0221  337 HOH   A O   
7003 O O   A HOH   E .   ? 0.2116 0.4083 0.4948 0.0511  0.0223  0.0400  338 HOH   A O   
7004 O O   . HOH   E .   ? 0.4653 0.4682 0.5630 -0.0071 0.0947  0.2565  339 HOH   A O   
7005 O O   . HOH   E .   ? 0.2509 0.3463 0.3486 -0.0381 0.0722  -0.0282 340 HOH   A O   
7006 O O   . HOH   E .   ? 0.2055 0.2052 0.3206 -0.0081 0.0084  -0.0527 341 HOH   A O   
7007 O O   . HOH   E .   ? 0.4798 0.5295 0.5858 0.1716  0.0661  -0.1168 342 HOH   A O   
7008 O O   . HOH   E .   ? 0.2408 0.4099 0.3593 0.0794  -0.0499 -0.0332 343 HOH   A O   
7009 O O   . HOH   E .   ? 0.4216 0.7016 0.4571 -0.0953 -0.0421 0.1653  344 HOH   A O   
7010 O O   . HOH   E .   ? 0.1936 0.2745 0.4246 0.0114  0.0710  -0.0837 345 HOH   A O   
7011 O O   . HOH   E .   ? 0.3307 0.3696 0.5636 -0.0914 -0.1341 -0.0958 346 HOH   A O   
7012 O O   . HOH   E .   ? 0.4453 0.5763 0.3845 0.0707  -0.0458 0.1401  347 HOH   A O   
7013 O O   . HOH   E .   ? 0.2337 0.2081 0.3355 0.0252  0.0218  0.0336  348 HOH   A O   
7014 O O   . HOH   E .   ? 0.1525 0.2273 0.2561 0.0018  -0.0104 0.0392  349 HOH   A O   
7015 O O   . HOH   E .   ? 0.5350 0.3900 0.4700 -0.1928 -0.1464 0.2031  350 HOH   A O   
7016 O O   . HOH   E .   ? 0.3929 0.4344 0.4869 0.1938  0.1082  0.0248  351 HOH   A O   
7017 O O   . HOH   E .   ? 0.2662 0.3368 0.4746 -0.0471 -0.0524 -0.0592 352 HOH   A O   
7018 O O   . HOH   E .   ? 0.5814 0.4632 0.4161 -0.1489 -0.0834 0.1794  353 HOH   A O   
7019 O O   . HOH   E .   ? 0.3137 0.4448 0.2793 -0.0272 0.0329  0.0218  354 HOH   A O   
7020 O O   . HOH   E .   ? 0.2085 0.2156 0.4695 0.0175  0.0991  -0.0173 355 HOH   A O   
7021 O O   . HOH   E .   ? 0.5245 0.5975 0.4210 -0.1546 0.1567  0.0855  356 HOH   A O   
7022 O O   . HOH   E .   ? 0.1679 0.1794 0.2895 0.0136  -0.0314 -0.0300 357 HOH   A O   
7023 O O   . HOH   E .   ? 0.3570 0.4270 0.2540 -0.1537 -0.0186 -0.0588 358 HOH   A O   
7024 O O   A HOH   E .   ? 0.1617 0.2046 0.2497 -0.0022 0.0302  0.0361  359 HOH   A O   
7025 O O   . HOH   E .   ? 0.4876 0.2082 0.4573 0.0311  -0.1289 0.0176  360 HOH   A O   
7026 O O   . HOH   E .   ? 0.1406 0.1361 0.1843 -0.0079 0.0110  0.0131  361 HOH   A O   
7027 O O   . HOH   E .   ? 0.4181 0.2212 0.3186 0.1034  0.0458  0.0297  362 HOH   A O   
7028 O O   . HOH   E .   ? 0.1814 0.2471 0.2442 -0.0304 -0.0125 0.0823  363 HOH   A O   
7029 O O   . HOH   E .   ? 0.6115 0.6024 0.8528 -0.1118 -0.0260 0.1633  364 HOH   A O   
7030 O O   . HOH   E .   ? 0.3875 0.3144 0.3846 -0.1016 -0.0091 -0.0275 365 HOH   A O   
7031 O O   . HOH   E .   ? 0.1678 0.1392 0.3051 -0.0074 0.0165  -0.0102 366 HOH   A O   
7032 O O   . HOH   E .   ? 0.6872 0.4546 0.6652 -0.0687 -0.1395 -0.0200 367 HOH   A O   
7033 O O   . HOH   E .   ? 0.2003 0.2575 0.2920 -0.0374 -0.0585 0.0791  368 HOH   A O   
7034 O O   . HOH   E .   ? 0.1584 0.1945 0.3057 0.0026  -0.0012 0.0193  369 HOH   A O   
7035 O O   . HOH   E .   ? 0.1918 0.2916 0.3268 0.0461  0.0498  0.1125  370 HOH   A O   
7036 O O   . HOH   E .   ? 0.1542 0.1737 0.1794 -0.0078 -0.0130 0.0030  371 HOH   A O   
7037 O O   . HOH   E .   ? 0.2336 0.1890 0.3362 -0.0117 -0.0732 -0.0140 372 HOH   A O   
7038 O O   . HOH   E .   ? 0.3574 0.3115 0.3610 -0.0079 -0.0304 0.1216  373 HOH   A O   
7039 O O   T HOH   E .   ? 0.1003 0.1274 0.3284 -0.0032 0.0163  0.0603  374 HOH   A O   
7040 O O   . HOH   E .   ? 0.4517 0.2439 0.5056 -0.1187 0.0686  0.0526  375 HOH   A O   
7041 O O   . HOH   E .   ? 0.4057 0.7824 0.5927 -0.0724 -0.1714 0.0858  376 HOH   A O   
7042 O O   . HOH   E .   ? 0.5961 0.5082 0.3909 0.1155  -0.0086 0.1956  377 HOH   A O   
7043 O O   . HOH   E .   ? 0.6008 0.3482 0.5417 0.1494  -0.0501 -0.0119 378 HOH   A O   
7044 O O   . HOH   E .   ? 0.2244 0.2202 0.2430 -0.0019 0.0132  0.0040  379 HOH   A O   
7045 O O   . HOH   E .   ? 0.3298 0.3022 0.2379 0.0144  0.0653  -0.0045 380 HOH   A O   
7046 O O   . HOH   E .   ? 0.2730 0.4065 0.4173 -0.0272 0.0597  0.0038  381 HOH   A O   
7047 O O   . HOH   E .   ? 0.3881 0.6096 0.5690 0.1380  0.1903  0.0586  382 HOH   A O   
7048 O O   . HOH   E .   ? 0.1938 0.1890 0.3464 0.0123  -0.0355 -0.0092 383 HOH   A O   
7049 O O   . HOH   E .   ? 0.1926 0.2013 0.2846 -0.0297 0.0061  0.0417  384 HOH   A O   
7050 O O   . HOH   E .   ? 0.2308 0.2325 0.3616 0.0019  -0.0341 0.0605  385 HOH   A O   
7051 O O   . HOH   E .   ? 0.2745 0.4895 0.3886 0.0202  0.0703  0.2272  386 HOH   A O   
7052 O O   . HOH   E .   ? 0.2004 0.2161 0.3612 -0.0011 -0.0319 0.0309  387 HOH   A O   
7053 O O   . HOH   E .   ? 0.3491 0.4209 0.4304 -0.0996 0.1478  0.0121  388 HOH   A O   
7054 O O   . HOH   E .   ? 0.3301 0.2523 0.4097 -0.0941 0.0882  -0.0100 389 HOH   A O   
7055 O O   . HOH   E .   ? 0.1690 0.1945 0.2433 0.0223  -0.0419 -0.0596 390 HOH   A O   
7056 O O   . HOH   E .   ? 0.4117 0.2714 0.5434 -0.0976 0.0024  -0.0025 391 HOH   A O   
7057 O O   . HOH   E .   ? 0.3280 0.4063 0.4035 -0.1647 0.1232  -0.0411 392 HOH   A O   
7058 O O   . HOH   E .   ? 0.3694 0.7275 0.3072 0.1624  0.0480  -0.1075 393 HOH   A O   
7059 O O   . HOH   E .   ? 0.5852 0.5930 0.5677 0.1795  -0.1195 -0.1373 394 HOH   A O   
7060 O O   . HOH   E .   ? 0.2593 0.3200 0.3940 -0.0032 -0.0240 -0.0931 395 HOH   A O   
7061 O O   A HOH   E .   ? 0.2782 0.1887 0.2645 0.0018  0.0194  0.0250  396 HOH   A O   
7062 O O   . HOH   E .   ? 0.2163 0.2385 0.3457 -0.0155 -0.0399 0.1010  397 HOH   A O   
7063 O O   . HOH   E .   ? 0.2873 0.4032 0.4500 -0.0141 0.1339  -0.0590 398 HOH   A O   
7064 O O   . HOH   E .   ? 0.2104 0.1698 0.2050 -0.0089 0.0179  0.0334  399 HOH   A O   
7065 O O   . HOH   E .   ? 0.1397 0.1570 0.2431 -0.0023 -0.0144 0.0054  400 HOH   A O   
7066 O O   A HOH   E .   ? 0.1140 0.3224 0.2428 -0.0000 0.0257  0.0688  401 HOH   A O   
7067 O O   . HOH   E .   ? 0.9507 0.4210 0.5213 -0.0525 0.1658  0.1638  402 HOH   A O   
7068 O O   A HOH   E .   ? 0.3154 0.3056 0.3588 0.0776  0.0741  0.0608  403 HOH   A O   
7069 O O   . HOH   E .   ? 0.1753 0.2657 0.3121 -0.0253 0.0488  0.0813  404 HOH   A O   
7070 O O   . HOH   E .   ? 0.1654 0.1761 0.3951 -0.0020 -0.0125 0.0305  405 HOH   A O   
7071 O O   . HOH   E .   ? 0.3013 0.2828 0.2667 -0.0629 -0.1051 0.0595  406 HOH   A O   
7072 O O   . HOH   E .   ? 0.5439 0.4737 0.2372 -0.1197 0.0648  0.0668  407 HOH   A O   
7073 O O   . HOH   E .   ? 0.1865 0.1981 0.3884 0.0306  0.0811  0.0959  408 HOH   A O   
7074 O O   . HOH   E .   ? 0.2646 0.1961 0.3783 0.0026  -0.0516 0.0212  409 HOH   A O   
7075 O O   . HOH   E .   ? 0.3093 0.3237 0.2568 -0.0425 -0.0766 0.0382  410 HOH   A O   
7076 O O   . HOH   E .   ? 0.1668 0.2115 0.3204 -0.0170 -0.0064 0.0161  411 HOH   A O   
7077 O O   . HOH   E .   ? 0.1807 0.1416 0.2014 -0.0201 0.0153  -0.0017 412 HOH   A O   
7078 O O   . HOH   E .   ? 0.6145 0.4705 0.6696 0.0430  0.1421  -0.1784 413 HOH   A O   
7079 O O   . HOH   E .   ? 0.6585 0.3799 0.5620 0.1578  -0.1187 0.1544  414 HOH   A O   
7080 O O   . HOH   E .   ? 0.2666 0.6793 0.2117 -0.0014 0.0463  0.0461  415 HOH   A O   
7081 O O   . HOH   E .   ? 0.2041 0.2978 0.3020 -0.0204 -0.0559 0.0794  416 HOH   A O   
7082 O O   . HOH   E .   ? 0.4336 0.7262 0.3491 -0.0940 -0.0136 0.1489  417 HOH   A O   
7083 O O   . HOH   E .   ? 0.5008 0.2682 0.3267 -0.1144 0.0466  0.0019  418 HOH   A O   
7084 O O   . HOH   E .   ? 0.4294 0.6186 0.3528 0.2885  -0.0102 -0.0796 419 HOH   A O   
7085 O O   . HOH   E .   ? 0.2090 0.1984 0.3096 0.0249  -0.0676 0.0154  420 HOH   A O   
7086 O O   . HOH   E .   ? 0.7154 0.9445 0.5661 0.2358  -0.1338 0.2745  421 HOH   A O   
7087 O O   . HOH   E .   ? 0.2663 0.2225 0.2883 -0.0504 0.0051  0.0635  422 HOH   A O   
7088 O O   . HOH   E .   ? 0.1941 0.2759 0.4692 -0.0109 -0.0144 0.0480  423 HOH   A O   
7089 O O   . HOH   E .   ? 0.3279 0.1348 0.2571 0.0007  -0.0753 0.0163  424 HOH   A O   
7090 O O   . HOH   E .   ? 0.2455 0.3983 0.3165 0.1532  0.0135  0.0350  425 HOH   A O   
7091 O O   . HOH   E .   ? 0.3014 0.3584 0.7478 -0.0139 0.0622  -0.0788 426 HOH   A O   
7092 O O   . HOH   E .   ? 0.5822 0.6269 0.6040 -0.0333 0.1440  0.0989  427 HOH   A O   
7093 O O   A HOH   E .   ? 0.1531 0.1356 0.1764 0.0122  0.0109  0.0032  428 HOH   A O   
7094 O O   A HOH   E .   ? 0.1827 0.1846 0.3183 -0.0154 0.0412  0.0000  429 HOH   A O   
7095 O O   . HOH   E .   ? 0.2062 0.2332 0.3482 0.0041  -0.0158 -0.0241 430 HOH   A O   
7096 O O   . HOH   E .   ? 0.5060 0.6552 0.7384 -0.0676 -0.1190 0.2315  431 HOH   A O   
7097 O O   B HOH   E .   ? 0.2373 0.2635 0.4859 -0.0148 0.0495  0.1552  432 HOH   A O   
7098 O O   . HOH   E .   ? 0.4336 0.2524 0.5864 -0.0944 -0.2884 0.1228  433 HOH   A O   
7099 O O   . HOH   E .   ? 0.3581 0.4152 0.2774 -0.0492 -0.0768 0.0438  434 HOH   A O   
7100 O O   . HOH   E .   ? 0.5309 0.5269 0.6111 -0.1271 -0.0959 -0.1165 435 HOH   A O   
7101 O O   . HOH   E .   ? 0.6410 0.7531 0.7326 -0.1093 -0.0417 -0.0510 436 HOH   A O   
7102 O O   . HOH   E .   ? 0.6154 0.7074 0.4432 0.0912  0.2913  -0.0238 437 HOH   A O   
7103 O O   . HOH   E .   ? 0.7068 0.5541 0.7751 0.0520  -0.0803 0.1951  438 HOH   A O   
7104 O O   . HOH   E .   ? 0.6199 0.5163 0.4125 -0.0204 -0.1449 0.0208  439 HOH   A O   
7105 O O   . HOH   E .   ? 0.2904 0.1736 0.3484 0.0114  0.0111  -0.0041 440 HOH   A O   
7106 O O   . HOH   E .   ? 0.1913 0.2187 0.5198 -0.0115 -0.0615 0.0630  441 HOH   A O   
7107 O O   . HOH   E .   ? 0.3832 0.3196 0.2521 -0.0996 0.0159  0.0583  442 HOH   A O   
7108 O O   . HOH   E .   ? 0.4296 0.3978 0.3469 0.2420  -0.0491 -0.0448 443 HOH   A O   
7109 O O   . HOH   E .   ? 0.3385 0.4025 0.6860 -0.0466 0.1451  -0.2110 444 HOH   A O   
7110 O O   . HOH   E .   ? 0.7778 0.6864 0.7443 0.0607  -0.0685 -0.0736 445 HOH   A O   
7111 O O   A HOH   E .   ? 0.2864 0.2047 0.2584 -0.0340 -0.0082 0.0698  446 HOH   A O   
7112 O O   . HOH   E .   ? 0.2286 0.2123 0.3652 0.0074  0.0116  0.0338  447 HOH   A O   
7113 O O   . HOH   E .   ? 0.2371 0.2910 0.3434 0.0037  -0.0063 -0.0399 448 HOH   A O   
7114 O O   . HOH   E .   ? 0.6983 0.6899 0.8016 -0.1372 -0.0051 -0.1368 449 HOH   A O   
7115 O O   . HOH   E .   ? 0.6649 0.7170 0.5017 -0.0770 0.0999  0.1460  450 HOH   A O   
7116 O O   . HOH   E .   ? 0.4438 0.3343 0.4303 0.0501  0.0153  0.0134  451 HOH   A O   
7117 O O   . HOH   E .   ? 0.5137 0.5470 0.5550 0.2721  -0.0955 0.1054  452 HOH   A O   
7118 O O   . HOH   E .   ? 0.4134 0.5124 0.4644 0.0004  0.1483  0.0052  453 HOH   A O   
7119 O O   . HOH   E .   ? 0.7709 0.8164 0.4978 0.1247  -0.0076 -0.0834 454 HOH   A O   
7120 O O   . HOH   E .   ? 0.4915 0.6728 0.4995 0.0709  0.0403  0.1194  455 HOH   A O   
7121 O O   B HOH   E .   ? 0.1727 0.2462 0.2757 -0.0281 -0.0492 -0.0767 456 HOH   A O   
7122 O O   . HOH   E .   ? 0.2816 0.2539 0.4509 -0.0426 0.0177  -0.0530 457 HOH   A O   
7123 O O   . HOH   E .   ? 0.3939 0.6965 0.4408 -0.1161 -0.1019 0.2379  458 HOH   A O   
7124 O O   . HOH   E .   ? 0.3490 0.3016 0.7519 0.0590  -0.2054 -0.0850 459 HOH   A O   
7125 O O   . HOH   E .   ? 0.4509 0.5569 0.4645 0.0663  -0.0599 -0.0589 460 HOH   A O   
7126 O O   . HOH   E .   ? 0.3896 0.5681 0.5726 -0.1306 0.0808  -0.1349 461 HOH   A O   
7127 O O   . HOH   E .   ? 0.4454 0.5295 0.5303 0.0340  -0.0262 0.1192  462 HOH   A O   
7128 O O   . HOH   E .   ? 0.7248 0.4000 0.7069 0.1171  -0.0409 0.2599  463 HOH   A O   
7129 O O   . HOH   E .   ? 0.2722 0.4874 0.4938 0.0397  -0.0147 -0.2087 464 HOH   A O   
7130 O O   . HOH   E .   ? 0.3452 0.3033 0.4207 -0.1222 0.0508  -0.0573 465 HOH   A O   
7131 O O   . HOH   E .   ? 0.6153 0.5328 0.4708 0.1133  -0.1120 -0.0850 466 HOH   A O   
7132 O O   . HOH   E .   ? 0.4370 0.4632 0.5166 -0.0716 0.0143  0.0268  467 HOH   A O   
7133 O O   . HOH   E .   ? 0.5573 0.5043 0.5609 -0.0188 0.1034  0.0266  468 HOH   A O   
7134 O O   . HOH   E .   ? 0.2750 0.1887 0.2946 0.0190  -0.0762 -0.0259 469 HOH   A O   
7135 O O   . HOH   E .   ? 0.7546 0.7210 0.5902 0.0740  0.1326  0.2648  470 HOH   A O   
7136 O O   . HOH   E .   ? 0.2777 0.2761 0.2947 0.0340  -0.0212 -0.0080 471 HOH   A O   
7137 O O   . HOH   E .   ? 0.3813 0.3390 0.4555 0.0689  0.1333  0.0600  472 HOH   A O   
7138 O O   . HOH   E .   ? 0.6820 0.6454 0.4890 0.1979  -0.1463 -0.0735 473 HOH   A O   
7139 O O   . HOH   E .   ? 0.5398 0.2933 0.4161 -0.1072 -0.1301 0.0511  474 HOH   A O   
7140 O O   . HOH   E .   ? 0.5225 0.3959 0.6054 -0.1969 -0.1272 0.0808  475 HOH   A O   
7141 O O   . HOH   E .   ? 0.4418 0.4581 0.5988 -0.1970 -0.0162 -0.0416 476 HOH   A O   
7142 O O   . HOH   E .   ? 0.4596 0.5265 0.3243 0.0275  -0.0131 -0.0338 477 HOH   A O   
7143 O O   . HOH   E .   ? 0.7432 0.6361 0.7843 -0.0370 0.0971  -0.0965 478 HOH   A O   
7144 O O   . HOH   E .   ? 0.5708 0.4571 0.5446 -0.0003 -0.0455 -0.1154 479 HOH   A O   
7145 O O   . HOH   E .   ? 0.3035 0.3907 0.5584 -0.0322 0.1062  -0.0832 480 HOH   A O   
7146 O O   . HOH   E .   ? 0.4471 0.4106 0.5241 -0.0556 -0.0637 0.1876  481 HOH   A O   
7147 O O   . HOH   E .   ? 0.4759 0.4130 0.3069 -0.0883 0.1626  -0.0850 482 HOH   A O   
7148 O O   . HOH   E .   ? 0.4403 0.5789 0.3576 -0.0274 -0.0064 -0.0431 483 HOH   A O   
7149 O O   . HOH   E .   ? 0.7989 0.4130 0.3644 0.0019  -0.1401 0.0485  484 HOH   A O   
7150 O O   . HOH   E .   ? 0.3805 0.2548 0.6277 -0.0008 0.0078  0.1199  485 HOH   A O   
7151 O O   . HOH   E .   ? 0.3580 0.4871 0.5085 0.0096  0.1674  0.1259  486 HOH   A O   
7152 O O   . HOH   E .   ? 0.2869 0.2502 0.7423 -0.0093 -0.1222 0.0395  487 HOH   A O   
7153 O O   . HOH   E .   ? 0.5764 0.6965 0.7147 0.0210  0.1491  -0.1220 488 HOH   A O   
7154 O O   . HOH   E .   ? 0.6479 0.4908 0.5268 -0.1178 -0.0518 -0.0619 489 HOH   A O   
7155 O O   . HOH   E .   ? 0.2676 0.5411 0.3895 0.0928  0.0783  0.2474  490 HOH   A O   
7156 O O   . HOH   E .   ? 0.5971 0.6921 0.7391 0.1651  -0.0873 0.0574  491 HOH   A O   
7157 O O   . HOH   E .   ? 0.7129 0.7427 0.4921 -0.1095 0.1063  0.1740  492 HOH   A O   
7158 O O   . HOH   E .   ? 0.7383 0.3975 0.4224 -0.0273 0.0689  -0.0029 493 HOH   A O   
7159 O O   . HOH   E .   ? 0.5444 0.5484 0.5125 0.0897  -0.0473 -0.0941 494 HOH   A O   
7160 O O   . HOH   E .   ? 0.5068 0.3285 0.4977 0.0081  0.2107  0.0310  495 HOH   A O   
7161 O O   B HOH   E .   ? 0.2694 0.4081 0.3377 0.0579  0.0748  0.0155  496 HOH   A O   
7162 O O   . HOH   E .   ? 0.2802 0.5182 0.3378 0.1371  -0.0224 0.0848  497 HOH   A O   
7163 O O   . HOH   E .   ? 0.4177 0.8139 0.6196 -0.0944 -0.0430 0.2149  498 HOH   A O   
7164 O O   . HOH   E .   ? 0.3194 0.4246 0.5305 0.0743  -0.0330 -0.0051 499 HOH   A O   
7165 O O   . HOH   E .   ? 0.6034 0.2947 0.5616 0.0686  -0.1885 0.0648  500 HOH   A O   
7166 O O   . HOH   E .   ? 0.2991 0.4691 0.3821 0.0114  -0.0572 -0.0340 501 HOH   A O   
7167 O O   . HOH   E .   ? 0.7096 0.2782 0.4843 -0.0914 0.0877  0.0259  502 HOH   A O   
7168 O O   . HOH   E .   ? 0.6101 0.8384 0.4930 0.1491  -0.0575 0.1463  503 HOH   A O   
7169 O O   . HOH   E .   ? 0.3335 0.2443 0.5848 0.0100  0.0184  0.0570  504 HOH   A O   
7170 O O   . HOH   E .   ? 0.5717 0.7225 0.6232 0.3379  0.0165  0.1949  505 HOH   A O   
7171 O O   T HOH   E .   ? 0.1306 0.1213 0.2595 -0.0070 -0.0164 0.0547  506 HOH   A O   
7172 O O   . HOH   E .   ? 0.5910 0.6527 0.4852 -0.0666 -0.1070 -0.1320 507 HOH   A O   
7173 O O   A HOH   E .   ? 0.3884 0.6697 0.3375 0.2597  -0.0466 0.0391  508 HOH   A O   
7174 O O   . HOH   E .   ? 0.3482 0.7430 0.5161 0.0883  0.0532  -0.1042 509 HOH   A O   
7175 O O   . HOH   E .   ? 0.4935 0.7438 0.5168 -0.0534 -0.0732 0.1495  510 HOH   A O   
7176 O O   . HOH   E .   ? 0.5830 0.5813 0.5473 0.1450  0.0886  0.1861  511 HOH   A O   
7177 O O   . HOH   E .   ? 0.3012 0.4916 0.6736 0.0126  -0.0789 0.2985  512 HOH   A O   
7178 O O   . HOH   F .   ? 0.2289 0.2577 0.3475 -0.0102 0.0712  0.0253  201 HOH   B O   
7179 O O   . HOH   F .   ? 0.7554 0.3603 0.4290 0.0577  0.0246  -0.0041 202 HOH   B O   
7180 O O   . HOH   F .   ? 0.5567 0.3432 0.4799 -0.0010 0.0410  -0.1820 203 HOH   B O   
7181 O O   . HOH   F .   ? 0.3309 0.3783 0.6500 -0.0302 -0.0028 -0.0246 204 HOH   B O   
7182 O O   . HOH   F .   ? 0.3694 0.2490 0.6188 -0.0331 0.2264  0.0187  205 HOH   B O   
7183 O O   . HOH   F .   ? 0.3481 0.4103 0.3185 -0.0239 -0.0297 -0.1178 206 HOH   B O   
7184 O O   . HOH   F .   ? 0.4285 0.4224 0.5380 -0.0932 -0.0191 -0.1439 207 HOH   B O   
7185 O O   . HOH   F .   ? 0.2873 0.6906 0.4295 0.0226  0.0042  0.2371  208 HOH   B O   
7186 O O   . HOH   F .   ? 0.4620 0.5778 0.3521 0.2623  -0.0313 0.0469  209 HOH   B O   
7187 O O   . HOH   F .   ? 0.3143 0.2029 0.6402 0.0021  0.2092  0.0454  210 HOH   B O   
7188 O O   . HOH   F .   ? 0.4277 0.4113 0.3915 -0.0002 -0.1335 0.0508  211 HOH   B O   
7189 O O   . HOH   F .   ? 0.4774 0.6240 0.4745 0.2731  -0.1353 0.0213  212 HOH   B O   
7190 O O   . HOH   F .   ? 0.1666 0.2085 0.3616 -0.0177 -0.0107 0.0082  213 HOH   B O   
7191 O O   . HOH   F .   ? 0.2036 0.2339 0.3235 0.0059  0.0140  -0.0384 214 HOH   B O   
7192 O O   . HOH   F .   ? 0.3109 0.5720 0.5357 -0.0469 0.1512  -0.1916 215 HOH   B O   
7193 O O   . HOH   F .   ? 0.4966 0.6799 0.4227 0.1825  0.0612  0.0643  216 HOH   B O   
7194 O O   . HOH   F .   ? 0.3690 0.5175 0.6054 0.2302  0.0821  -0.0169 217 HOH   B O   
7195 O O   . HOH   F .   ? 0.2633 0.2835 0.6046 0.0533  -0.0693 0.0415  218 HOH   B O   
7196 O O   . HOH   F .   ? 0.3670 0.2977 0.4831 0.0623  -0.0226 0.0025  219 HOH   B O   
7197 O O   . HOH   F .   ? 0.7230 0.4580 0.4062 -0.1016 -0.0208 0.0957  220 HOH   B O   
7198 O O   . HOH   F .   ? 0.1649 0.1637 0.2723 -0.0162 -0.0019 0.0002  221 HOH   B O   
7199 O O   . HOH   F .   ? 0.6610 0.6265 0.6252 0.1442  0.1554  -0.0379 222 HOH   B O   
7200 O O   . HOH   F .   ? 0.1793 0.2292 0.3847 -0.0160 0.0165  -0.0055 223 HOH   B O   
7201 O O   . HOH   F .   ? 0.2423 0.2391 0.4346 -0.0402 -0.0011 -0.0431 224 HOH   B O   
7202 O O   . HOH   F .   ? 0.5069 0.4857 0.6149 0.0462  -0.1702 -0.0818 225 HOH   B O   
7203 O O   . HOH   F .   ? 0.2391 0.2999 0.3972 -0.0737 0.0337  -0.0314 226 HOH   B O   
7204 O O   . HOH   F .   ? 0.5447 0.2303 0.3388 -0.0071 -0.1002 0.0091  227 HOH   B O   
7205 O O   . HOH   F .   ? 0.3570 0.2780 0.4608 0.0664  -0.0402 -0.0434 228 HOH   B O   
7206 O O   . HOH   F .   ? 0.3935 0.1761 0.2572 0.0157  -0.0800 -0.0044 229 HOH   B O   
7207 O O   . HOH   F .   ? 0.4693 0.4800 0.4155 0.0301  0.0755  -0.1686 230 HOH   B O   
7208 O O   . HOH   F .   ? 0.2331 0.2021 0.2970 -0.0352 0.0891  -0.0113 231 HOH   B O   
7209 O O   . HOH   F .   ? 0.3405 0.4229 0.2459 -0.0033 0.0517  0.0427  232 HOH   B O   
7210 O O   . HOH   F .   ? 0.2309 0.3737 0.3144 -0.0156 -0.0311 0.0649  233 HOH   B O   
7211 O O   . HOH   F .   ? 0.5895 0.3490 0.4074 -0.2516 -0.0458 0.0427  234 HOH   B O   
7212 O O   . HOH   F .   ? 0.2233 0.1362 0.3751 0.0096  -0.0693 -0.0108 235 HOH   B O   
7213 O O   . HOH   F .   ? 0.3712 0.2678 0.4734 0.0447  -0.0890 -0.1231 236 HOH   B O   
7214 O O   . HOH   F .   ? 0.1558 0.1505 0.1775 -0.0076 -0.0090 -0.0034 237 HOH   B O   
7215 O O   . HOH   F .   ? 0.2545 0.2079 0.3131 0.0749  -0.0857 -0.0651 238 HOH   B O   
7216 O O   . HOH   F .   ? 0.5876 0.3000 0.3738 -0.1529 -0.0266 -0.0110 239 HOH   B O   
7217 O O   . HOH   F .   ? 0.2784 0.2296 0.3358 0.0595  0.0522  -0.0140 240 HOH   B O   
7218 O O   . HOH   F .   ? 0.3036 0.3394 0.2982 -0.0762 0.0031  -0.0122 241 HOH   B O   
7219 O O   . HOH   F .   ? 0.7396 0.5632 0.4719 0.2259  0.0144  -0.0943 242 HOH   B O   
7220 O O   . HOH   F .   ? 0.3561 0.4575 0.3368 -0.0335 -0.0968 0.0430  243 HOH   B O   
7221 O O   . HOH   F .   ? 0.2549 0.5699 0.6000 0.1354  -0.0828 -0.1109 244 HOH   B O   
7222 O O   . HOH   F .   ? 0.1631 0.1582 0.3096 -0.0050 -0.0007 -0.0157 245 HOH   B O   
7223 O O   . HOH   F .   ? 0.4774 0.4116 0.6992 0.0092  -0.1259 0.2691  246 HOH   B O   
7224 O O   . HOH   F .   ? 0.2165 0.1665 0.2553 -0.0268 -0.0534 0.0311  247 HOH   B O   
7225 O O   . HOH   F .   ? 0.4461 0.2982 0.2558 0.0361  0.0710  0.0471  248 HOH   B O   
7226 O O   . HOH   F .   ? 0.3035 0.1823 0.6733 -0.0061 -0.1127 -0.0362 249 HOH   B O   
7227 O O   . HOH   F .   ? 0.1553 0.1405 0.2064 -0.0011 -0.0207 0.0028  250 HOH   B O   
7228 O O   . HOH   F .   ? 0.4087 0.5358 0.6158 -0.1999 0.0088  0.1192  251 HOH   B O   
7229 O O   . HOH   F .   ? 0.2661 0.2900 0.3556 0.0350  0.0192  -0.1082 252 HOH   B O   
7230 O O   . HOH   F .   ? 0.4410 0.4431 0.4545 0.1808  -0.0575 -0.1311 253 HOH   B O   
7231 O O   . HOH   F .   ? 0.6980 0.6860 0.3915 -0.0003 -0.0114 0.0518  254 HOH   B O   
7232 O O   . HOH   F .   ? 0.2605 0.3841 0.3678 -0.0572 -0.0934 -0.0338 255 HOH   B O   
7233 O O   . HOH   F .   ? 0.2274 0.2013 0.2479 -0.0342 -0.0648 0.0264  256 HOH   B O   
7234 O O   . HOH   F .   ? 0.3583 0.2344 0.2183 0.0138  -0.0340 -0.0103 257 HOH   B O   
7235 O O   . HOH   F .   ? 0.2475 0.3393 0.2269 -0.0620 0.0357  0.0592  258 HOH   B O   
7236 O O   . HOH   F .   ? 0.4600 0.4446 0.3381 0.0278  -0.0088 -0.0262 259 HOH   B O   
7237 O O   . HOH   F .   ? 0.1519 0.1821 0.2575 -0.0064 0.0066  0.0151  260 HOH   B O   
7238 O O   . HOH   F .   ? 0.3872 0.4111 0.6675 -0.0237 0.1219  -0.0099 261 HOH   B O   
7239 O O   . HOH   F .   ? 0.2287 0.2039 0.3978 -0.0030 -0.0474 -0.0154 262 HOH   B O   
7240 O O   . HOH   F .   ? 0.5147 0.3850 0.4337 -0.1535 0.0231  -0.1222 263 HOH   B O   
7241 O O   . HOH   F .   ? 0.1734 0.1781 0.3665 -0.0246 -0.0191 0.0092  264 HOH   B O   
7242 O O   . HOH   F .   ? 0.4866 0.3054 0.4973 0.0462  0.0087  -0.0729 265 HOH   B O   
7243 O O   . HOH   F .   ? 0.3153 0.3688 0.3563 -0.0871 -0.0187 -0.0396 266 HOH   B O   
7244 O O   . HOH   F .   ? 0.2580 0.2771 0.2921 -0.0590 -0.1000 0.0232  267 HOH   B O   
7245 O O   . HOH   F .   ? 0.2932 0.3903 0.4036 0.0033  0.1226  0.0134  268 HOH   B O   
7246 O O   . HOH   F .   ? 0.1942 0.1830 0.1968 -0.0473 -0.0516 0.0107  269 HOH   B O   
7247 O O   . HOH   F .   ? 0.4232 0.2434 0.4388 -0.0300 -0.0781 -0.0164 270 HOH   B O   
7248 O O   . HOH   F .   ? 0.3019 0.2260 0.5140 0.0096  0.0399  0.0724  271 HOH   B O   
7249 O O   . HOH   F .   ? 0.2333 0.2737 0.2530 -0.0452 -0.0664 -0.0260 272 HOH   B O   
7250 O O   . HOH   F .   ? 0.2485 0.2593 0.2423 -0.0057 -0.0034 -0.0171 273 HOH   B O   
7251 O O   . HOH   F .   ? 0.2018 0.1476 0.3819 -0.0115 -0.0388 -0.0224 274 HOH   B O   
7252 O O   . HOH   F .   ? 0.2892 0.4614 0.6870 -0.0437 0.0261  -0.1174 275 HOH   B O   
7253 O O   . HOH   F .   ? 0.2173 0.5511 0.5287 -0.0189 -0.0203 -0.1104 276 HOH   B O   
7254 O O   . HOH   F .   ? 0.2434 0.3244 0.3611 -0.0255 0.0355  -0.0886 277 HOH   B O   
7255 O O   . HOH   F .   ? 0.3606 0.3233 0.3581 -0.0672 -0.0046 -0.0660 278 HOH   B O   
7256 O O   . HOH   F .   ? 0.2788 0.2121 0.3170 -0.0614 0.0207  -0.0051 279 HOH   B O   
7257 O O   . HOH   F .   ? 0.2078 0.1646 0.2768 -0.0234 -0.0066 0.0175  280 HOH   B O   
7258 O O   . HOH   F .   ? 0.5655 0.3897 0.3846 0.2594  0.1294  0.1004  281 HOH   B O   
7259 O O   . HOH   F .   ? 0.2582 0.3980 0.2633 0.1175  -0.0270 -0.0325 282 HOH   B O   
7260 O O   . HOH   F .   ? 0.1753 0.1760 0.4133 -0.0121 -0.0038 0.0014  283 HOH   B O   
7261 O O   . HOH   F .   ? 0.1762 0.1604 0.2419 0.0011  0.0143  0.0093  284 HOH   B O   
7262 O O   . HOH   F .   ? 0.2204 0.2467 0.5605 -0.0526 -0.0053 0.1430  285 HOH   B O   
7263 O O   . HOH   F .   ? 0.1860 0.2245 0.3688 0.0236  0.0128  0.0156  286 HOH   B O   
7264 O O   . HOH   F .   ? 0.3773 0.2764 0.2540 0.0069  -0.0738 0.0115  287 HOH   B O   
7265 O O   . HOH   F .   ? 0.2670 0.2770 0.3247 -0.0158 -0.0774 0.0437  288 HOH   B O   
7266 O O   . HOH   F .   ? 0.4900 0.5555 0.5802 0.0545  -0.1768 0.0353  289 HOH   B O   
7267 O O   . HOH   F .   ? 0.1784 0.1989 0.2023 -0.0165 -0.0160 0.0077  290 HOH   B O   
7268 O O   . HOH   F .   ? 0.3553 0.3233 0.3473 -0.0628 0.0176  -0.1548 291 HOH   B O   
7269 O O   . HOH   F .   ? 0.2787 0.7903 0.7333 0.1704  -0.0432 -0.0985 292 HOH   B O   
7270 O O   . HOH   F .   ? 0.2998 0.4891 0.5033 -0.1091 -0.1088 0.0530  293 HOH   B O   
7271 O O   . HOH   F .   ? 0.3955 0.2324 0.4782 -0.1003 -0.2114 0.1274  294 HOH   B O   
7272 O O   . HOH   F .   ? 0.7890 0.6803 0.3696 0.0704  0.0062  0.0419  295 HOH   B O   
7273 O O   . HOH   F .   ? 0.5265 0.6457 0.4890 0.3144  -0.0342 0.0154  296 HOH   B O   
7274 O O   . HOH   F .   ? 0.5055 0.3918 0.2525 0.1129  -0.0805 0.0469  297 HOH   B O   
7275 O O   . HOH   F .   ? 0.1830 0.3872 0.5690 0.0413  -0.0188 -0.1712 298 HOH   B O   
7276 O O   . HOH   F .   ? 0.5066 0.5336 0.2936 0.0252  0.1151  0.1328  299 HOH   B O   
7277 O O   . HOH   F .   ? 0.2337 0.3518 0.4941 -0.0292 -0.0500 -0.0202 300 HOH   B O   
7278 O O   . HOH   F .   ? 0.2196 0.3510 0.6449 0.0713  -0.0533 -0.1426 301 HOH   B O   
7279 O O   . HOH   F .   ? 0.2782 0.7079 0.2675 0.0885  -0.0537 -0.0553 302 HOH   B O   
7280 O O   . HOH   F .   ? 0.4957 0.3058 0.2547 -0.1695 0.0584  -0.0201 303 HOH   B O   
7281 O O   . HOH   F .   ? 0.5117 0.4089 0.4501 -0.1001 0.0129  0.1593  304 HOH   B O   
7282 O O   . HOH   F .   ? 0.3534 0.3144 0.5932 -0.0557 -0.0787 0.1471  305 HOH   B O   
7283 O O   . HOH   F .   ? 0.5455 0.6991 0.3022 -0.0264 -0.0718 0.0093  306 HOH   B O   
7284 O O   . HOH   F .   ? 0.5643 0.2723 0.3483 0.0253  -0.0093 0.0888  307 HOH   B O   
7285 O O   . HOH   F .   ? 0.3473 0.1985 0.4305 0.0711  0.1222  0.0244  308 HOH   B O   
7286 O O   . HOH   F .   ? 0.1854 0.1799 0.3057 0.0111  -0.0100 0.0274  309 HOH   B O   
7287 O O   . HOH   F .   ? 0.2159 0.1649 0.3899 0.0347  -0.0914 0.0146  310 HOH   B O   
7288 O O   . HOH   F .   ? 0.3940 0.4119 0.4447 -0.1630 0.1431  -0.0427 311 HOH   B O   
7289 O O   . HOH   F .   ? 0.2315 0.1989 0.2324 -0.0081 0.0263  0.0245  312 HOH   B O   
7290 O O   . HOH   F .   ? 0.2290 0.6245 0.5741 -0.0743 -0.0121 0.0461  313 HOH   B O   
7291 O O   . HOH   F .   ? 0.1685 0.1532 0.4037 0.0053  -0.0007 0.0169  314 HOH   B O   
7292 O O   . HOH   F .   ? 0.2851 0.1527 0.3337 -0.0197 -0.0418 0.0398  315 HOH   B O   
7293 O O   . HOH   F .   ? 0.1774 0.2810 0.2926 -0.0140 -0.0148 0.0766  316 HOH   B O   
7294 O O   . HOH   F .   ? 0.3307 0.2936 0.4156 -0.0435 0.1465  -0.0897 317 HOH   B O   
7295 O O   . HOH   F .   ? 0.2493 0.1698 0.3126 -0.0310 -0.0417 -0.0102 318 HOH   B O   
7296 O O   . HOH   F .   ? 0.5212 0.7023 0.4956 0.1599  -0.1005 0.1342  319 HOH   B O   
7297 O O   . HOH   F .   ? 0.5003 0.4865 0.2788 0.0283  -0.0349 -0.0803 320 HOH   B O   
7298 O O   . HOH   F .   ? 0.4372 0.2329 0.3051 0.1468  0.1136  0.0379  321 HOH   B O   
7299 O O   . HOH   F .   ? 0.1852 0.1907 0.3545 0.0218  0.0454  0.0163  322 HOH   B O   
7300 O O   . HOH   F .   ? 0.1703 0.1663 0.3754 -0.0117 -0.0171 -0.0122 323 HOH   B O   
7301 O O   . HOH   F .   ? 0.6296 0.5037 0.7410 0.1917  -0.1235 0.1316  324 HOH   B O   
7302 O O   . HOH   F .   ? 0.3027 0.2137 0.5157 -0.0036 -0.0182 0.0691  325 HOH   B O   
7303 O O   . HOH   F .   ? 0.3444 0.2494 0.2995 0.0336  -0.0295 0.0178  326 HOH   B O   
7304 O O   . HOH   F .   ? 0.1663 0.1958 0.3460 -0.0171 -0.0203 -0.0048 327 HOH   B O   
7305 O O   . HOH   F .   ? 0.3616 0.4779 0.8842 -0.0040 -0.0813 0.2376  328 HOH   B O   
7306 O O   . HOH   F .   ? 0.4876 0.5112 0.2319 0.1528  -0.0543 0.0090  329 HOH   B O   
7307 O O   . HOH   F .   ? 0.8378 0.2259 0.4249 0.0484  -0.1100 -0.0378 330 HOH   B O   
7308 O O   . HOH   F .   ? 0.1944 0.3006 0.4017 0.0438  -0.0393 -0.0796 331 HOH   B O   
7309 O O   . HOH   F .   ? 0.5582 0.3686 0.4739 -0.0334 0.0722  -0.1585 332 HOH   B O   
7310 O O   . HOH   F .   ? 0.2957 0.3583 0.6339 -0.0710 -0.1759 0.2044  333 HOH   B O   
7311 O O   . HOH   F .   ? 0.4472 0.4412 0.5740 0.0739  -0.0038 0.0460  334 HOH   B O   
7312 O O   . HOH   F .   ? 0.4647 0.3348 0.5632 0.1237  0.2246  0.1722  335 HOH   B O   
7313 O O   . HOH   F .   ? 0.5669 0.4229 0.4622 0.1080  0.1604  0.1766  336 HOH   B O   
7314 O O   . HOH   F .   ? 0.6624 0.4647 0.5413 0.1025  0.1998  0.0111  337 HOH   B O   
7315 O O   . HOH   F .   ? 0.1924 0.1471 0.2992 0.0062  -0.0336 0.0177  338 HOH   B O   
7316 O O   . HOH   F .   ? 0.3421 0.5739 0.4625 -0.1218 -0.1034 -0.0148 339 HOH   B O   
7317 O O   . HOH   F .   ? 0.6251 0.4414 0.5802 -0.0806 -0.1222 -0.1636 340 HOH   B O   
7318 O O   . HOH   F .   ? 0.6065 0.6333 0.5734 -0.1023 -0.0801 0.1469  341 HOH   B O   
7319 O O   . HOH   F .   ? 0.4837 0.7689 0.4155 -0.0798 -0.1097 0.1958  342 HOH   B O   
7320 O O   . HOH   F .   ? 0.5234 0.3490 0.3687 0.0478  -0.1042 -0.1096 343 HOH   B O   
7321 O O   . HOH   F .   ? 0.3769 0.5597 0.7642 0.0029  -0.0868 0.0294  344 HOH   B O   
7322 O O   . HOH   F .   ? 0.2609 0.2094 0.4083 0.0278  -0.0787 -0.0399 345 HOH   B O   
7323 O O   . HOH   F .   ? 0.4759 0.6219 0.5533 -0.1125 -0.0004 0.1058  346 HOH   B O   
7324 O O   . HOH   F .   ? 0.2244 0.2257 0.4255 -0.0107 0.0855  -0.0105 347 HOH   B O   
7325 O O   . HOH   F .   ? 0.6093 0.5150 0.4067 0.0334  -0.1253 -0.0311 348 HOH   B O   
7326 O O   . HOH   F .   ? 0.3644 0.4313 0.5538 -0.1460 0.0015  -0.0554 349 HOH   B O   
7327 O O   . HOH   F .   ? 0.2360 0.6547 0.3736 0.1390  -0.0647 -0.1532 350 HOH   B O   
7328 O O   . HOH   F .   ? 0.4552 0.5865 0.7053 0.0168  0.0534  -0.0765 351 HOH   B O   
7329 O O   . HOH   F .   ? 0.2964 0.2388 0.5265 -0.0361 -0.0842 -0.0688 352 HOH   B O   
7330 O O   . HOH   F .   ? 0.4315 0.6255 0.6217 -0.0103 -0.1211 0.0414  353 HOH   B O   
7331 O O   . HOH   F .   ? 0.2531 0.4442 0.5606 -0.0070 0.0261  -0.0148 354 HOH   B O   
7332 O O   . HOH   F .   ? 0.5146 0.5800 0.5240 0.2170  -0.1176 0.1236  355 HOH   B O   
7333 O O   . HOH   F .   ? 0.4286 0.2320 0.3321 -0.0841 0.0610  -0.0750 356 HOH   B O   
7334 O O   . HOH   F .   ? 0.4629 0.2877 0.5882 -0.0879 0.0801  0.0744  357 HOH   B O   
7335 O O   . HOH   F .   ? 0.5198 0.3748 0.4873 0.0249  0.1160  -0.0816 358 HOH   B O   
7336 O O   . HOH   F .   ? 0.4155 0.2650 0.3822 -0.1160 -0.0078 -0.0432 359 HOH   B O   
7337 O O   . HOH   F .   ? 0.4767 0.4699 0.6086 -0.0092 0.0516  0.1502  360 HOH   B O   
7338 O O   . HOH   F .   ? 0.5791 0.3558 0.4942 -0.0067 -0.1758 -0.0864 361 HOH   B O   
7339 O O   . HOH   F .   ? 0.2358 0.4138 0.6954 -0.0949 -0.0750 -0.0573 362 HOH   B O   
7340 O O   . HOH   F .   ? 0.4898 0.6596 0.3420 0.2034  -0.0046 0.0081  363 HOH   B O   
7341 O O   . HOH   F .   ? 0.6538 0.2629 0.3596 -0.0453 -0.0029 0.0451  364 HOH   B O   
7342 O O   . HOH   F .   ? 0.6373 0.5725 0.5639 -0.0036 0.0505  0.0694  365 HOH   B O   
7343 O O   . HOH   F .   ? 0.5615 0.6261 0.5149 -0.1111 -0.0563 -0.1160 366 HOH   B O   
7344 O O   . HOH   F .   ? 0.3167 0.3425 0.5111 0.0548  -0.1264 -0.0174 367 HOH   B O   
7345 O O   . HOH   F .   ? 0.5518 0.3140 0.5320 -0.1596 -0.0579 0.0049  368 HOH   B O   
7346 O O   . HOH   F .   ? 0.5014 0.6199 0.3752 0.2046  -0.1493 0.0242  369 HOH   B O   
7347 O O   . HOH   F .   ? 0.6255 0.4928 0.4576 0.1206  -0.0168 0.0451  370 HOH   B O   
7348 O O   . HOH   F .   ? 0.3774 0.5447 0.5571 0.2048  0.0902  0.1664  371 HOH   B O   
7349 O O   . HOH   F .   ? 0.3959 0.3357 0.3687 0.0684  -0.0759 -0.0133 372 HOH   B O   
7350 O O   . HOH   F .   ? 0.4433 0.5481 0.5272 -0.0509 -0.0210 0.0327  373 HOH   B O   
7351 O O   . HOH   F .   ? 0.7921 0.7385 0.5090 0.1572  -0.1367 -0.0165 374 HOH   B O   
7352 O O   . HOH   F .   ? 0.6762 0.4212 0.3401 -0.0963 -0.1066 -0.0595 375 HOH   B O   
7353 O O   . HOH   F .   ? 0.5947 0.7451 0.4495 -0.1532 0.0194  -0.1504 376 HOH   B O   
7354 O O   . HOH   F .   ? 0.3847 0.6144 0.5787 0.0882  0.0125  0.0232  377 HOH   B O   
7355 O O   . HOH   F .   ? 0.2307 0.4200 0.4808 0.0271  -0.0468 -0.0687 378 HOH   B O   
7356 O O   . HOH   F .   ? 0.4878 0.6986 0.6189 0.0960  0.0099  0.2526  379 HOH   B O   
7357 O O   . HOH   F .   ? 0.4193 0.6879 0.2949 -0.1017 0.0254  0.0658  380 HOH   B O   
7358 O O   . HOH   F .   ? 0.7072 0.3842 0.5177 -0.0229 -0.1260 0.0105  381 HOH   B O   
7359 O O   . HOH   F .   ? 0.3124 0.2790 0.3445 -0.0039 0.0448  0.0155  382 HOH   B O   
7360 O O   . HOH   F .   ? 0.6128 0.7530 0.7283 -0.0657 0.1702  0.1967  383 HOH   B O   
7361 O O   . HOH   F .   ? 0.6768 0.3936 0.4150 0.0339  0.0191  -0.0839 384 HOH   B O   
7362 O O   . HOH   F .   ? 0.4459 0.7744 0.5525 0.1078  0.1129  0.1001  385 HOH   B O   
7363 O O   . HOH   F .   ? 0.7716 0.6485 0.4829 0.2684  0.0828  -0.0190 386 HOH   B O   
7364 O O   . HOH   F .   ? 0.2483 0.4658 0.4347 -0.0718 -0.0909 -0.0535 387 HOH   B O   
7365 O O   . HOH   F .   ? 0.5031 0.4781 0.4601 0.0168  0.0734  -0.0450 388 HOH   B O   
7366 O O   . HOH   F .   ? 0.6582 0.5205 0.6190 -0.0856 0.0995  -0.0234 389 HOH   B O   
7367 O O   . HOH   F .   ? 0.4939 0.3420 0.5171 -0.1770 0.0131  0.0478  390 HOH   B O   
7368 O O   . HOH   F .   ? 0.4332 0.2645 0.3815 0.0925  -0.0580 0.0155  391 HOH   B O   
7369 O O   . HOH   F .   ? 0.5488 0.4484 0.5201 0.0619  0.1016  0.0304  392 HOH   B O   
7370 O O   . HOH   F .   ? 0.2690 0.4222 0.7212 -0.1139 -0.0702 -0.0149 393 HOH   B O   
7371 O O   . HOH   F .   ? 0.3548 0.2415 0.5431 -0.0135 0.0522  0.0805  394 HOH   B O   
7372 O O   . HOH   F .   ? 0.2141 0.2782 0.5596 -0.0624 -0.0667 -0.0005 395 HOH   B O   
7373 O O   . HOH   F .   ? 0.4410 0.6558 0.5098 0.0829  0.0039  -0.1215 396 HOH   B O   
7374 O O   . HOH   F .   ? 0.4886 0.4869 0.4998 0.0241  0.1168  0.1082  397 HOH   B O   
7375 O O   . HOH   F .   ? 0.3430 0.4077 0.4597 -0.0077 0.0258  -0.0580 398 HOH   B O   
7376 O O   . HOH   F .   ? 0.5687 0.4384 0.3353 -0.2482 -0.0552 0.0892  399 HOH   B O   
7377 O O   . HOH   F .   ? 0.5521 0.6408 0.7247 0.0127  -0.1565 0.1325  400 HOH   B O   
7378 O O   . HOH   F .   ? 0.6331 0.5710 0.3690 0.1663  0.0346  -0.0434 401 HOH   B O   
# 
