data_7HFT
# 
_entry.id   7HFT 
# 
_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   7HFT         pdb_00007hft 10.2210/pdb7hft/pdb 
WWPDB D_1001407419 ?            ?                   
# 
_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                        7HFT 
_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 '4-[(2R)-2-tert-butylpyrrolidin-1-yl]-7H-pyrrolo[2,3-d]pyrimidine' 244.335   1   ?                      ? ? ? 
3 water       nat water                                                              18.015    408 ?                      ? ? ? 
# 
_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 '4-[(2R)-2-tert-butylpyrrolidin-1-yl]-7H-pyrrolo[2,3-d]pyrimidine' A1BBU 
3 water                                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BBU non-polymer         . '4-[(2R)-2-tert-butylpyrrolidin-1-yl]-7H-pyrrolo[2,3-d]pyrimidine' ? 'C14 H20 N4'     244.335 
ALA   'L-peptide linking' y ALANINE                                                            ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                           ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                         ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                    ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                           ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                          ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                    ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                            ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                          ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                              ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                         ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                            ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                             ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                         ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                      ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                            ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                             ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                          ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                           ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                             ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BBU 1   201 201  A1BBU LA1 A . 
D 3 HOH   1   301 36   HOH   HOH A . 
D 3 HOH   2   302 196  HOH   HOH A . 
D 3 HOH   3   303 292  HOH   HOH A . 
D 3 HOH   4   304 1309 HOH   HOH A . 
D 3 HOH   5   305 493  HOH   HOH A . 
D 3 HOH   6   306 93   HOH   HOH A . 
D 3 HOH   7   307 229  HOH   HOH A . 
D 3 HOH   8   308 393  HOH   HOH A . 
D 3 HOH   9   309 209  HOH   HOH A . 
D 3 HOH   10  310 661  HOH   HOH A . 
D 3 HOH   11  311 625  HOH   HOH A . 
D 3 HOH   12  312 109  HOH   HOH A . 
D 3 HOH   13  313 86   HOH   HOH A . 
D 3 HOH   14  314 964  HOH   HOH A . 
D 3 HOH   15  315 151  HOH   HOH A . 
D 3 HOH   16  316 630  HOH   HOH A . 
D 3 HOH   17  317 76   HOH   HOH A . 
D 3 HOH   18  318 136  HOH   HOH A . 
D 3 HOH   19  319 1295 HOH   HOH A . 
D 3 HOH   20  320 124  HOH   HOH A . 
D 3 HOH   21  321 236  HOH   HOH A . 
D 3 HOH   22  322 247  HOH   HOH A . 
D 3 HOH   23  323 105  HOH   HOH A . 
D 3 HOH   24  324 153  HOH   HOH A . 
D 3 HOH   25  325 8    HOH   HOH A . 
D 3 HOH   26  326 164  HOH   HOH A . 
D 3 HOH   27  327 225  HOH   HOH A . 
D 3 HOH   28  328 140  HOH   HOH A . 
D 3 HOH   29  329 15   HOH   HOH A . 
D 3 HOH   30  330 469  HOH   HOH A . 
D 3 HOH   31  331 337  HOH   HOH A . 
D 3 HOH   32  332 192  HOH   HOH A . 
D 3 HOH   33  333 1301 HOH   HOH A . 
D 3 HOH   34  334 396  HOH   HOH A . 
D 3 HOH   35  335 320  HOH   HOH A . 
D 3 HOH   36  336 662  HOH   HOH A . 
D 3 HOH   37  337 1300 HOH   HOH A . 
D 3 HOH   38  338 85   HOH   HOH A . 
D 3 HOH   39  339 241  HOH   HOH A . 
D 3 HOH   40  340 17   HOH   HOH A . 
D 3 HOH   41  341 42   HOH   HOH A . 
D 3 HOH   42  342 6    HOH   HOH A . 
D 3 HOH   43  343 2    HOH   HOH A . 
D 3 HOH   44  344 139  HOH   HOH A . 
D 3 HOH   45  345 281  HOH   HOH A . 
D 3 HOH   46  346 296  HOH   HOH A . 
D 3 HOH   47  347 1283 HOH   HOH A . 
D 3 HOH   48  348 102  HOH   HOH A . 
D 3 HOH   49  349 66   HOH   HOH A . 
D 3 HOH   50  350 19   HOH   HOH A . 
D 3 HOH   51  351 165  HOH   HOH A . 
D 3 HOH   52  352 405  HOH   HOH A . 
D 3 HOH   53  353 33   HOH   HOH A . 
D 3 HOH   54  354 92   HOH   HOH A . 
D 3 HOH   55  355 1290 HOH   HOH A . 
D 3 HOH   56  356 354  HOH   HOH A . 
D 3 HOH   57  357 57   HOH   HOH A . 
D 3 HOH   58  358 45   HOH   HOH A . 
D 3 HOH   59  359 56   HOH   HOH A . 
D 3 HOH   60  360 81   HOH   HOH A . 
D 3 HOH   61  361 162  HOH   HOH A . 
D 3 HOH   62  362 409  HOH   HOH A . 
D 3 HOH   63  363 21   HOH   HOH A . 
D 3 HOH   64  364 5    HOH   HOH A . 
D 3 HOH   65  365 155  HOH   HOH A . 
D 3 HOH   66  366 169  HOH   HOH A . 
D 3 HOH   67  367 18   HOH   HOH A . 
D 3 HOH   68  368 138  HOH   HOH A . 
D 3 HOH   69  369 939  HOH   HOH A . 
D 3 HOH   70  370 46   HOH   HOH A . 
D 3 HOH   71  371 39   HOH   HOH A . 
D 3 HOH   72  372 49   HOH   HOH A . 
D 3 HOH   73  373 27   HOH   HOH A . 
D 3 HOH   74  374 148  HOH   HOH A . 
D 3 HOH   75  375 186  HOH   HOH A . 
D 3 HOH   76  376 96   HOH   HOH A . 
D 3 HOH   77  377 154  HOH   HOH A . 
D 3 HOH   78  378 159  HOH   HOH A . 
D 3 HOH   79  379 1    HOH   HOH A . 
D 3 HOH   80  380 24   HOH   HOH A . 
D 3 HOH   81  381 134  HOH   HOH A . 
D 3 HOH   82  382 218  HOH   HOH A . 
D 3 HOH   83  383 26   HOH   HOH A . 
D 3 HOH   84  384 1275 HOH   HOH A . 
D 3 HOH   85  385 62   HOH   HOH A . 
D 3 HOH   86  386 78   HOH   HOH A . 
D 3 HOH   87  387 4    HOH   HOH A . 
D 3 HOH   88  388 199  HOH   HOH A . 
D 3 HOH   89  389 35   HOH   HOH A . 
D 3 HOH   90  390 461  HOH   HOH A . 
D 3 HOH   91  391 366  HOH   HOH A . 
D 3 HOH   92  392 1310 HOH   HOH A . 
D 3 HOH   93  393 83   HOH   HOH A . 
D 3 HOH   94  394 122  HOH   HOH A . 
D 3 HOH   95  395 1308 HOH   HOH A . 
D 3 HOH   96  396 67   HOH   HOH A . 
D 3 HOH   97  397 12   HOH   HOH A . 
D 3 HOH   98  398 7    HOH   HOH A . 
D 3 HOH   99  399 116  HOH   HOH A . 
D 3 HOH   100 400 333  HOH   HOH A . 
D 3 HOH   101 401 3    HOH   HOH A . 
D 3 HOH   102 402 303  HOH   HOH A . 
D 3 HOH   103 403 1315 HOH   HOH A . 
D 3 HOH   104 404 74   HOH   HOH A . 
D 3 HOH   105 405 58   HOH   HOH A . 
D 3 HOH   106 406 1296 HOH   HOH A . 
D 3 HOH   107 407 952  HOH   HOH A . 
D 3 HOH   108 408 121  HOH   HOH A . 
D 3 HOH   109 409 397  HOH   HOH A . 
D 3 HOH   110 410 156  HOH   HOH A . 
D 3 HOH   111 411 1279 HOH   HOH A . 
D 3 HOH   112 412 34   HOH   HOH A . 
D 3 HOH   113 413 132  HOH   HOH A . 
D 3 HOH   114 414 212  HOH   HOH A . 
D 3 HOH   115 415 278  HOH   HOH A . 
D 3 HOH   116 416 1068 HOH   HOH A . 
D 3 HOH   117 417 68   HOH   HOH A . 
D 3 HOH   118 418 195  HOH   HOH A . 
D 3 HOH   119 419 1134 HOH   HOH A . 
D 3 HOH   120 420 351  HOH   HOH A . 
D 3 HOH   121 421 25   HOH   HOH A . 
D 3 HOH   122 422 53   HOH   HOH A . 
D 3 HOH   123 423 1313 HOH   HOH A . 
D 3 HOH   124 424 95   HOH   HOH A . 
D 3 HOH   125 425 1289 HOH   HOH A . 
D 3 HOH   126 426 381  HOH   HOH A . 
D 3 HOH   127 427 51   HOH   HOH A . 
D 3 HOH   128 428 125  HOH   HOH A . 
D 3 HOH   129 429 123  HOH   HOH A . 
D 3 HOH   130 430 1222 HOH   HOH A . 
D 3 HOH   131 431 582  HOH   HOH A . 
D 3 HOH   132 432 115  HOH   HOH A . 
D 3 HOH   133 433 70   HOH   HOH A . 
D 3 HOH   134 434 1189 HOH   HOH A . 
D 3 HOH   135 435 1286 HOH   HOH A . 
D 3 HOH   136 436 944  HOH   HOH A . 
D 3 HOH   137 437 16   HOH   HOH A . 
D 3 HOH   138 438 40   HOH   HOH A . 
D 3 HOH   139 439 1238 HOH   HOH A . 
D 3 HOH   140 440 80   HOH   HOH A . 
D 3 HOH   141 441 73   HOH   HOH A . 
D 3 HOH   142 442 71   HOH   HOH A . 
D 3 HOH   143 443 188  HOH   HOH A . 
D 3 HOH   144 444 94   HOH   HOH A . 
D 3 HOH   145 445 1094 HOH   HOH A . 
D 3 HOH   146 446 104  HOH   HOH A . 
D 3 HOH   147 447 97   HOH   HOH A . 
D 3 HOH   148 448 576  HOH   HOH A . 
D 3 HOH   149 449 79   HOH   HOH A . 
D 3 HOH   150 450 107  HOH   HOH A . 
D 3 HOH   151 451 330  HOH   HOH A . 
D 3 HOH   152 452 1119 HOH   HOH A . 
D 3 HOH   153 453 509  HOH   HOH A . 
D 3 HOH   154 454 163  HOH   HOH A . 
D 3 HOH   155 455 726  HOH   HOH A . 
D 3 HOH   156 456 756  HOH   HOH A . 
D 3 HOH   157 457 408  HOH   HOH A . 
D 3 HOH   158 458 342  HOH   HOH A . 
D 3 HOH   159 459 1307 HOH   HOH A . 
D 3 HOH   160 460 361  HOH   HOH A . 
D 3 HOH   161 461 1284 HOH   HOH A . 
D 3 HOH   162 462 126  HOH   HOH A . 
D 3 HOH   163 463 63   HOH   HOH A . 
D 3 HOH   164 464 319  HOH   HOH A . 
D 3 HOH   165 465 370  HOH   HOH A . 
D 3 HOH   166 466 801  HOH   HOH A . 
D 3 HOH   167 467 1276 HOH   HOH A . 
D 3 HOH   168 468 280  HOH   HOH A . 
D 3 HOH   169 469 250  HOH   HOH A . 
D 3 HOH   170 470 556  HOH   HOH A . 
D 3 HOH   171 471 521  HOH   HOH A . 
D 3 HOH   172 472 1287 HOH   HOH A . 
D 3 HOH   173 473 1306 HOH   HOH A . 
D 3 HOH   174 474 267  HOH   HOH A . 
D 3 HOH   175 475 315  HOH   HOH A . 
D 3 HOH   176 476 919  HOH   HOH A . 
D 3 HOH   177 477 135  HOH   HOH A . 
D 3 HOH   178 478 711  HOH   HOH A . 
D 3 HOH   179 479 695  HOH   HOH A . 
D 3 HOH   180 480 224  HOH   HOH A . 
D 3 HOH   181 481 674  HOH   HOH A . 
D 3 HOH   182 482 202  HOH   HOH A . 
D 3 HOH   183 483 1314 HOH   HOH A . 
D 3 HOH   184 484 309  HOH   HOH A . 
D 3 HOH   185 485 1299 HOH   HOH A . 
D 3 HOH   186 486 318  HOH   HOH A . 
D 3 HOH   187 487 331  HOH   HOH A . 
D 3 HOH   188 488 805  HOH   HOH A . 
D 3 HOH   189 489 356  HOH   HOH A . 
D 3 HOH   190 490 263  HOH   HOH A . 
D 3 HOH   191 491 152  HOH   HOH A . 
D 3 HOH   192 492 941  HOH   HOH A . 
D 3 HOH   193 493 208  HOH   HOH A . 
D 3 HOH   194 494 1071 HOH   HOH A . 
D 3 HOH   195 495 180  HOH   HOH A . 
D 3 HOH   196 496 350  HOH   HOH A . 
D 3 HOH   197 497 326  HOH   HOH A . 
D 3 HOH   198 498 363  HOH   HOH A . 
D 3 HOH   199 499 371  HOH   HOH A . 
D 3 HOH   200 500 313  HOH   HOH A . 
D 3 HOH   201 501 376  HOH   HOH A . 
D 3 HOH   202 502 429  HOH   HOH A . 
D 3 HOH   203 503 185  HOH   HOH A . 
D 3 HOH   204 504 772  HOH   HOH A . 
D 3 HOH   205 505 1074 HOH   HOH A . 
D 3 HOH   206 506 346  HOH   HOH A . 
D 3 HOH   207 507 1292 HOH   HOH A . 
D 3 HOH   208 508 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 364  HOH   HOH B . 
E 3 HOH   3   203 900  HOH   HOH B . 
E 3 HOH   4   204 358  HOH   HOH B . 
E 3 HOH   5   205 1249 HOH   HOH B . 
E 3 HOH   6   206 549  HOH   HOH B . 
E 3 HOH   7   207 240  HOH   HOH B . 
E 3 HOH   8   208 120  HOH   HOH B . 
E 3 HOH   9   209 353  HOH   HOH B . 
E 3 HOH   10  210 264  HOH   HOH B . 
E 3 HOH   11  211 758  HOH   HOH B . 
E 3 HOH   12  212 743  HOH   HOH B . 
E 3 HOH   13  213 398  HOH   HOH B . 
E 3 HOH   14  214 50   HOH   HOH B . 
E 3 HOH   15  215 654  HOH   HOH B . 
E 3 HOH   16  216 452  HOH   HOH B . 
E 3 HOH   17  217 232  HOH   HOH B . 
E 3 HOH   18  218 276  HOH   HOH B . 
E 3 HOH   19  219 531  HOH   HOH B . 
E 3 HOH   20  220 75   HOH   HOH B . 
E 3 HOH   21  221 332  HOH   HOH B . 
E 3 HOH   22  222 131  HOH   HOH B . 
E 3 HOH   23  223 1312 HOH   HOH B . 
E 3 HOH   24  224 444  HOH   HOH B . 
E 3 HOH   25  225 205  HOH   HOH B . 
E 3 HOH   26  226 1140 HOH   HOH B . 
E 3 HOH   27  227 54   HOH   HOH B . 
E 3 HOH   28  228 272  HOH   HOH B . 
E 3 HOH   29  229 723  HOH   HOH B . 
E 3 HOH   30  230 343  HOH   HOH B . 
E 3 HOH   31  231 300  HOH   HOH B . 
E 3 HOH   32  232 129  HOH   HOH B . 
E 3 HOH   33  233 1    HOH   HOH B . 
E 3 HOH   34  234 82   HOH   HOH B . 
E 3 HOH   35  235 127  HOH   HOH B . 
E 3 HOH   36  236 128  HOH   HOH B . 
E 3 HOH   37  237 282  HOH   HOH B . 
E 3 HOH   38  238 110  HOH   HOH B . 
E 3 HOH   39  239 166  HOH   HOH B . 
E 3 HOH   40  240 69   HOH   HOH B . 
E 3 HOH   41  241 325  HOH   HOH B . 
E 3 HOH   42  242 52   HOH   HOH B . 
E 3 HOH   43  243 181  HOH   HOH B . 
E 3 HOH   44  244 133  HOH   HOH B . 
E 3 HOH   45  245 14   HOH   HOH B . 
E 3 HOH   46  246 9    HOH   HOH B . 
E 3 HOH   47  247 60   HOH   HOH B . 
E 3 HOH   48  248 1278 HOH   HOH B . 
E 3 HOH   49  249 391  HOH   HOH B . 
E 3 HOH   50  250 30   HOH   HOH B . 
E 3 HOH   51  251 31   HOH   HOH B . 
E 3 HOH   52  252 10   HOH   HOH B . 
E 3 HOH   53  253 144  HOH   HOH B . 
E 3 HOH   54  254 143  HOH   HOH B . 
E 3 HOH   55  255 47   HOH   HOH B . 
E 3 HOH   56  256 252  HOH   HOH B . 
E 3 HOH   57  257 302  HOH   HOH B . 
E 3 HOH   58  258 72   HOH   HOH B . 
E 3 HOH   59  259 172  HOH   HOH B . 
E 3 HOH   60  260 150  HOH   HOH B . 
E 3 HOH   61  261 175  HOH   HOH B . 
E 3 HOH   62  262 59   HOH   HOH B . 
E 3 HOH   63  263 103  HOH   HOH B . 
E 3 HOH   64  264 20   HOH   HOH B . 
E 3 HOH   65  265 243  HOH   HOH B . 
E 3 HOH   66  266 231  HOH   HOH B . 
E 3 HOH   67  267 11   HOH   HOH B . 
E 3 HOH   68  268 41   HOH   HOH B . 
E 3 HOH   69  269 347  HOH   HOH B . 
E 3 HOH   70  270 1106 HOH   HOH B . 
E 3 HOH   71  271 117  HOH   HOH B . 
E 3 HOH   72  272 84   HOH   HOH B . 
E 3 HOH   73  273 114  HOH   HOH B . 
E 3 HOH   74  274 271  HOH   HOH B . 
E 3 HOH   75  275 77   HOH   HOH B . 
E 3 HOH   76  276 61   HOH   HOH B . 
E 3 HOH   77  277 22   HOH   HOH B . 
E 3 HOH   78  278 106  HOH   HOH B . 
E 3 HOH   79  279 147  HOH   HOH B . 
E 3 HOH   80  280 242  HOH   HOH B . 
E 3 HOH   81  281 1066 HOH   HOH B . 
E 3 HOH   82  282 1305 HOH   HOH B . 
E 3 HOH   83  283 416  HOH   HOH B . 
E 3 HOH   84  284 287  HOH   HOH B . 
E 3 HOH   85  285 43   HOH   HOH B . 
E 3 HOH   86  286 1277 HOH   HOH B . 
E 3 HOH   87  287 13   HOH   HOH B . 
E 3 HOH   88  288 387  HOH   HOH B . 
E 3 HOH   89  289 235  HOH   HOH B . 
E 3 HOH   90  290 635  HOH   HOH B . 
E 3 HOH   91  291 137  HOH   HOH B . 
E 3 HOH   92  292 89   HOH   HOH B . 
E 3 HOH   93  293 299  HOH   HOH B . 
E 3 HOH   94  294 99   HOH   HOH B . 
E 3 HOH   95  295 141  HOH   HOH B . 
E 3 HOH   96  296 220  HOH   HOH B . 
E 3 HOH   97  297 297  HOH   HOH B . 
E 3 HOH   98  298 112  HOH   HOH B . 
E 3 HOH   99  299 316  HOH   HOH B . 
E 3 HOH   100 300 221  HOH   HOH B . 
E 3 HOH   101 301 88   HOH   HOH B . 
E 3 HOH   102 302 32   HOH   HOH B . 
E 3 HOH   103 303 216  HOH   HOH B . 
E 3 HOH   104 304 142  HOH   HOH B . 
E 3 HOH   105 305 1126 HOH   HOH B . 
E 3 HOH   106 306 160  HOH   HOH B . 
E 3 HOH   107 307 101  HOH   HOH B . 
E 3 HOH   108 308 311  HOH   HOH B . 
E 3 HOH   109 309 48   HOH   HOH B . 
E 3 HOH   110 310 118  HOH   HOH B . 
E 3 HOH   111 311 37   HOH   HOH B . 
E 3 HOH   112 312 215  HOH   HOH B . 
E 3 HOH   113 313 38   HOH   HOH B . 
E 3 HOH   114 314 182  HOH   HOH B . 
E 3 HOH   115 315 1274 HOH   HOH B . 
E 3 HOH   116 316 23   HOH   HOH B . 
E 3 HOH   117 317 341  HOH   HOH B . 
E 3 HOH   118 318 100  HOH   HOH B . 
E 3 HOH   119 319 177  HOH   HOH B . 
E 3 HOH   120 320 170  HOH   HOH B . 
E 3 HOH   121 321 44   HOH   HOH B . 
E 3 HOH   122 322 28   HOH   HOH B . 
E 3 HOH   123 323 1291 HOH   HOH B . 
E 3 HOH   124 324 161  HOH   HOH B . 
E 3 HOH   125 325 91   HOH   HOH B . 
E 3 HOH   126 326 704  HOH   HOH B . 
E 3 HOH   127 327 1285 HOH   HOH B . 
E 3 HOH   128 328 29   HOH   HOH B . 
E 3 HOH   129 329 1294 HOH   HOH B . 
E 3 HOH   130 330 98   HOH   HOH B . 
E 3 HOH   131 331 717  HOH   HOH B . 
E 3 HOH   132 332 334  HOH   HOH B . 
E 3 HOH   133 333 197  HOH   HOH B . 
E 3 HOH   134 334 55   HOH   HOH B . 
E 3 HOH   135 335 178  HOH   HOH B . 
E 3 HOH   136 336 65   HOH   HOH B . 
E 3 HOH   137 337 234  HOH   HOH B . 
E 3 HOH   138 338 339  HOH   HOH B . 
E 3 HOH   139 339 207  HOH   HOH B . 
E 3 HOH   140 340 445  HOH   HOH B . 
E 3 HOH   141 341 619  HOH   HOH B . 
E 3 HOH   142 342 960  HOH   HOH B . 
E 3 HOH   143 343 362  HOH   HOH B . 
E 3 HOH   144 344 1293 HOH   HOH B . 
E 3 HOH   145 345 463  HOH   HOH B . 
E 3 HOH   146 346 90   HOH   HOH B . 
E 3 HOH   147 347 191  HOH   HOH B . 
E 3 HOH   148 348 1304 HOH   HOH B . 
E 3 HOH   149 349 335  HOH   HOH B . 
E 3 HOH   150 350 623  HOH   HOH B . 
E 3 HOH   151 351 304  HOH   HOH B . 
E 3 HOH   152 352 203  HOH   HOH B . 
E 3 HOH   153 353 87   HOH   HOH B . 
E 3 HOH   154 354 1046 HOH   HOH B . 
E 3 HOH   155 355 290  HOH   HOH B . 
E 3 HOH   156 356 541  HOH   HOH B . 
E 3 HOH   157 357 1280 HOH   HOH B . 
E 3 HOH   158 358 1077 HOH   HOH B . 
E 3 HOH   159 359 389  HOH   HOH B . 
E 3 HOH   160 360 479  HOH   HOH B . 
E 3 HOH   161 361 718  HOH   HOH B . 
E 3 HOH   162 362 283  HOH   HOH B . 
E 3 HOH   163 363 1072 HOH   HOH B . 
E 3 HOH   164 364 1316 HOH   HOH B . 
E 3 HOH   165 365 898  HOH   HOH B . 
E 3 HOH   166 366 291  HOH   HOH B . 
E 3 HOH   167 367 340  HOH   HOH B . 
E 3 HOH   168 368 190  HOH   HOH B . 
E 3 HOH   169 369 667  HOH   HOH B . 
E 3 HOH   170 370 1303 HOH   HOH B . 
E 3 HOH   171 371 615  HOH   HOH B . 
E 3 HOH   172 372 373  HOH   HOH B . 
E 3 HOH   173 373 1163 HOH   HOH B . 
E 3 HOH   174 374 183  HOH   HOH B . 
E 3 HOH   175 375 310  HOH   HOH B . 
E 3 HOH   176 376 431  HOH   HOH B . 
E 3 HOH   177 377 149  HOH   HOH B . 
E 3 HOH   178 378 1173 HOH   HOH B . 
E 3 HOH   179 379 418  HOH   HOH B . 
E 3 HOH   180 380 1000 HOH   HOH B . 
E 3 HOH   181 381 1311 HOH   HOH B . 
E 3 HOH   182 382 176  HOH   HOH B . 
E 3 HOH   183 383 424  HOH   HOH B . 
E 3 HOH   184 384 470  HOH   HOH B . 
E 3 HOH   185 385 491  HOH   HOH B . 
E 3 HOH   186 386 1298 HOH   HOH B . 
E 3 HOH   187 387 981  HOH   HOH B . 
E 3 HOH   188 388 248  HOH   HOH B . 
E 3 HOH   189 389 265  HOH   HOH B . 
E 3 HOH   190 390 184  HOH   HOH B . 
E 3 HOH   191 391 360  HOH   HOH B . 
E 3 HOH   192 392 410  HOH   HOH B . 
E 3 HOH   193 393 355  HOH   HOH B . 
E 3 HOH   194 394 314  HOH   HOH B . 
E 3 HOH   195 395 274  HOH   HOH B . 
E 3 HOH   196 396 566  HOH   HOH B . 
E 3 HOH   197 397 157  HOH   HOH B . 
E 3 HOH   198 398 792  HOH   HOH B . 
E 3 HOH   199 399 321  HOH   HOH B . 
E 3 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HFT 
_cell.length_a           88.896 
_cell.length_b           88.896 
_cell.length_c           39.637 
_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                         7HFT 
_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          7HFT 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.16 
_exptl_crystal.density_percent_sol   43 
_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   2023-10-27 
_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                     7HFT 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.450 
_reflns.d_resolution_high            1.010 
_reflns.number_obs                   161611 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.113 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        6.900 
_reflns.B_iso_Wilson_estimate        12.200 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.123 
_reflns.pdbx_Rpim_I_all              0.048 
_reflns.pdbx_CC_half                 0.994 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1037394 
_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 1.010 1.030  ? 38792 7387 ? 2.119 ? ? ? 5.300 ? 0.400  ? ? ? ? ? ? 93.200 2.349 0.992 0.445 
1 2 5.530 44.450 ? 7361  1069 ? 0.087 ? ? ? 6.900 ? 19.000 ? ? ? ? ? ? 99.800 0.095 0.036 0.992 
# 
_refine.entry_id                                 7HFT 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0100 
_refine.ls_d_res_low                             44.4500 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.0100 
_refine.ls_number_reflns_obs                     160156 
_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                          0.1539 
_refine.ls_R_factor_R_work                       0.1531 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1690 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7734 
_refine.ls_number_reflns_R_work                  152422 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.4467 
_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                            0.1500 
_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                                67.540 
_refine.B_iso_min                                9.230 
_refine.pdbx_overall_phase_error                 21.1800 
_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                       1.0100 
_refine_hist.d_res_low                        44.4500 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.number_atoms_solvent             408 
_refine_hist.number_atoms_total               2988 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           19.77 
_refine_hist.pdbx_B_iso_mean_solvent          31.41 
_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 
1.0100 1.0200  30 73.0000  3740 . 0.4926 0.4982 . 205 0.0000 3945 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 99.0000  5114 . 0.4368 0.4445 . 209 0.0000 5323 . 'X-RAY DIFFRACTION' 
1.0300 1.0500  30 100.0000 5076 . 0.3942 0.3650 . 289 0.0000 5365 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5025 . 0.3691 0.3802 . 295 0.0000 5320 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5069 . 0.3718 0.3891 . 272 0.0000 5341 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5113 . 0.3564 0.3528 . 237 0.0000 5350 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5104 . 0.3162 0.3125 . 260 0.0000 5364 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5086 . 0.2758 0.2784 . 268 0.0000 5354 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5161 . 0.2340 0.2822 . 227 0.0000 5388 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5128 . 0.2072 0.2109 . 253 0.0000 5381 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5096 . 0.1754 0.1945 . 269 0.0000 5365 . 'X-RAY DIFFRACTION' 
1.1800 1.2000  30 100.0000 5114 . 0.1586 0.1983 . 249 0.0000 5363 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5058 . 0.1401 0.1655 . 281 0.0000 5339 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5153 . 0.1360 0.1485 . 239 0.0000 5392 . 'X-RAY DIFFRACTION' 
1.2500 1.2700  30 100.0000 5102 . 0.1429 0.1614 . 241 0.0000 5343 . 'X-RAY DIFFRACTION' 
1.2700 1.3000  30 100.0000 5120 . 0.1409 0.1621 . 251 0.0000 5371 . 'X-RAY DIFFRACTION' 
1.3000 1.3400  30 100.0000 5093 . 0.1433 0.1576 . 292 0.0000 5385 . 'X-RAY DIFFRACTION' 
1.3400 1.3700  30 100.0000 5145 . 0.1470 0.1724 . 274 0.0000 5419 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5154 . 0.1327 0.1800 . 227 0.0000 5381 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5093 . 0.1286 0.1533 . 269 0.0000 5362 . 'X-RAY DIFFRACTION' 
1.4600 1.5100  30 100.0000 5119 . 0.1210 0.1351 . 254 0.0000 5373 . 'X-RAY DIFFRACTION' 
1.5100 1.5700  30 100.0000 5148 . 0.1190 0.1363 . 266 0.0000 5414 . 'X-RAY DIFFRACTION' 
1.5700 1.6400  30 100.0000 5097 . 0.1184 0.1348 . 270 0.0000 5367 . 'X-RAY DIFFRACTION' 
1.6400 1.7300  30 100.0000 5218 . 0.1239 0.1458 . 226 0.0000 5444 . 'X-RAY DIFFRACTION' 
1.7300 1.8400  30 100.0000 5110 . 0.1304 0.1365 . 262 0.0000 5372 . 'X-RAY DIFFRACTION' 
1.8400 1.9800  30 100.0000 5145 . 0.1314 0.1314 . 283 0.0000 5428 . 'X-RAY DIFFRACTION' 
1.9800 2.1800  30 100.0000 5117 . 0.1387 0.1528 . 283 0.0000 5400 . 'X-RAY DIFFRACTION' 
2.1800 2.4900  30 100.0000 5194 . 0.1384 0.1451 . 265 0.0000 5459 . 'X-RAY DIFFRACTION' 
2.4900 3.1400  30 100.0000 5206 . 0.1524 0.1703 . 257 0.0000 5463 . 'X-RAY DIFFRACTION' 
3.1400 44.4500 30 100.0000 5324 . 0.1512 0.1761 . 261 0.0000 5585 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFT 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0006000' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFT 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HFT A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFT 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 7HFT SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFT MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFT SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFT MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D 
2 1 B,E   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HFT 
_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   HZ3 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    19 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OE2 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   GLU 
_pdbx_validate_close_contact.auth_seq_id_2    26 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   B 
_pdbx_validate_close_contact.dist             1.58 
# 
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  ? ? 56.27   -133.36 
2 1 PHE A 156 ? B -91.95  59.22   
3 1 ASP A 157 ? B -162.49 106.85  
4 1 SER A 167 ? B -104.20 41.05   
5 1 HIS B 86  ? ? 57.25   -126.96 
# 
_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 506 ? 5.97 . 
2 1 O ? A HOH 507 ? 6.04 . 
3 1 O ? A HOH 508 ? 7.57 . 
4 1 O ? B HOH 400 ? 6.37 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1 ? A SER 1 
2 1 Y 1 A MET 2 ? A MET 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BBU N2   N Y N 1   
A1BBU C3   C N N 2   
A1BBU C6   C N N 3   
A1BBU C9   C Y N 4   
A1BBU C12  C Y N 5   
A1BBU C14  C Y N 6   
A1BBU C1   C N N 7   
A1BBU C10  C Y N 8   
A1BBU C11  C Y N 9   
A1BBU C13  C Y N 10  
A1BBU C2   C N N 11  
A1BBU C4   C N N 12  
A1BBU C5   C N R 13  
A1BBU C7   C N N 14  
A1BBU C8   C N N 15  
A1BBU N1   N N N 16  
A1BBU N3   N Y N 17  
A1BBU N4   N Y N 18  
A1BBU H7   H N N 19  
A1BBU H6   H N N 20  
A1BBU H5   H N N 21  
A1BBU H12  H N N 22  
A1BBU H11  H N N 23  
A1BBU H19  H N N 24  
A1BBU H2   H N N 25  
A1BBU H3   H N N 26  
A1BBU H4   H N N 27  
A1BBU H17  H N N 28  
A1BBU H18  H N N 29  
A1BBU H8   H N N 30  
A1BBU H10  H N N 31  
A1BBU H9   H N N 32  
A1BBU H1   H N N 33  
A1BBU H13  H N N 34  
A1BBU H14  H N N 35  
A1BBU H16  H N N 36  
A1BBU H15  H N N 37  
A1BBU H20  H N N 38  
ALA   N    N N N 39  
ALA   CA   C N S 40  
ALA   C    C N N 41  
ALA   O    O N N 42  
ALA   CB   C N N 43  
ALA   OXT  O N N 44  
ALA   H    H N N 45  
ALA   H2   H N N 46  
ALA   HA   H N N 47  
ALA   HB1  H N N 48  
ALA   HB2  H N N 49  
ALA   HB3  H N N 50  
ALA   HXT  H N N 51  
ARG   N    N N N 52  
ARG   CA   C N S 53  
ARG   C    C N N 54  
ARG   O    O N N 55  
ARG   CB   C N N 56  
ARG   CG   C N N 57  
ARG   CD   C N N 58  
ARG   NE   N N N 59  
ARG   CZ   C N N 60  
ARG   NH1  N N N 61  
ARG   NH2  N N N 62  
ARG   OXT  O N N 63  
ARG   H    H N N 64  
ARG   H2   H N N 65  
ARG   HA   H N N 66  
ARG   HB2  H N N 67  
ARG   HB3  H N N 68  
ARG   HG2  H N N 69  
ARG   HG3  H N N 70  
ARG   HD2  H N N 71  
ARG   HD3  H N N 72  
ARG   HE   H N N 73  
ARG   HH11 H N N 74  
ARG   HH12 H N N 75  
ARG   HH21 H N N 76  
ARG   HH22 H N N 77  
ARG   HXT  H N N 78  
ASN   N    N N N 79  
ASN   CA   C N S 80  
ASN   C    C N N 81  
ASN   O    O N N 82  
ASN   CB   C N N 83  
ASN   CG   C N N 84  
ASN   OD1  O N N 85  
ASN   ND2  N N N 86  
ASN   OXT  O N N 87  
ASN   H    H N N 88  
ASN   H2   H N N 89  
ASN   HA   H N N 90  
ASN   HB2  H N N 91  
ASN   HB3  H N N 92  
ASN   HD21 H N N 93  
ASN   HD22 H N N 94  
ASN   HXT  H N N 95  
ASP   N    N N N 96  
ASP   CA   C N S 97  
ASP   C    C N N 98  
ASP   O    O N N 99  
ASP   CB   C N N 100 
ASP   CG   C N N 101 
ASP   OD1  O N N 102 
ASP   OD2  O N N 103 
ASP   OXT  O N N 104 
ASP   H    H N N 105 
ASP   H2   H N N 106 
ASP   HA   H N N 107 
ASP   HB2  H N N 108 
ASP   HB3  H N N 109 
ASP   HD2  H N N 110 
ASP   HXT  H N N 111 
CYS   N    N N N 112 
CYS   CA   C N R 113 
CYS   C    C N N 114 
CYS   O    O N N 115 
CYS   CB   C N N 116 
CYS   SG   S N N 117 
CYS   OXT  O N N 118 
CYS   H    H N N 119 
CYS   H2   H N N 120 
CYS   HA   H N N 121 
CYS   HB2  H N N 122 
CYS   HB3  H N N 123 
CYS   HG   H N N 124 
CYS   HXT  H N N 125 
GLN   N    N N N 126 
GLN   CA   C N S 127 
GLN   C    C N N 128 
GLN   O    O N N 129 
GLN   CB   C N N 130 
GLN   CG   C N N 131 
GLN   CD   C N N 132 
GLN   OE1  O N N 133 
GLN   NE2  N N N 134 
GLN   OXT  O N N 135 
GLN   H    H N N 136 
GLN   H2   H N N 137 
GLN   HA   H N N 138 
GLN   HB2  H N N 139 
GLN   HB3  H N N 140 
GLN   HG2  H N N 141 
GLN   HG3  H N N 142 
GLN   HE21 H N N 143 
GLN   HE22 H N N 144 
GLN   HXT  H N N 145 
GLU   N    N N N 146 
GLU   CA   C N S 147 
GLU   C    C N N 148 
GLU   O    O N N 149 
GLU   CB   C N N 150 
GLU   CG   C N N 151 
GLU   CD   C N N 152 
GLU   OE1  O N N 153 
GLU   OE2  O N N 154 
GLU   OXT  O N N 155 
GLU   H    H N N 156 
GLU   H2   H N N 157 
GLU   HA   H N N 158 
GLU   HB2  H N N 159 
GLU   HB3  H N N 160 
GLU   HG2  H N N 161 
GLU   HG3  H N N 162 
GLU   HE2  H N N 163 
GLU   HXT  H N N 164 
GLY   N    N N N 165 
GLY   CA   C N N 166 
GLY   C    C N N 167 
GLY   O    O N N 168 
GLY   OXT  O N N 169 
GLY   H    H N N 170 
GLY   H2   H N N 171 
GLY   HA2  H N N 172 
GLY   HA3  H N N 173 
GLY   HXT  H N N 174 
HIS   N    N N N 175 
HIS   CA   C N S 176 
HIS   C    C N N 177 
HIS   O    O N N 178 
HIS   CB   C N N 179 
HIS   CG   C Y N 180 
HIS   ND1  N Y N 181 
HIS   CD2  C Y N 182 
HIS   CE1  C Y N 183 
HIS   NE2  N Y N 184 
HIS   OXT  O N N 185 
HIS   H    H N N 186 
HIS   H2   H N N 187 
HIS   HA   H N N 188 
HIS   HB2  H N N 189 
HIS   HB3  H N N 190 
HIS   HD1  H N N 191 
HIS   HD2  H N N 192 
HIS   HE1  H N N 193 
HIS   HE2  H N N 194 
HIS   HXT  H N N 195 
HOH   O    O N N 196 
HOH   H1   H N N 197 
HOH   H2   H N N 198 
ILE   N    N N N 199 
ILE   CA   C N S 200 
ILE   C    C N N 201 
ILE   O    O N N 202 
ILE   CB   C N S 203 
ILE   CG1  C N N 204 
ILE   CG2  C N N 205 
ILE   CD1  C N N 206 
ILE   OXT  O N N 207 
ILE   H    H N N 208 
ILE   H2   H N N 209 
ILE   HA   H N N 210 
ILE   HB   H N N 211 
ILE   HG12 H N N 212 
ILE   HG13 H N N 213 
ILE   HG21 H N N 214 
ILE   HG22 H N N 215 
ILE   HG23 H N N 216 
ILE   HD11 H N N 217 
ILE   HD12 H N N 218 
ILE   HD13 H N N 219 
ILE   HXT  H N N 220 
LEU   N    N N N 221 
LEU   CA   C N S 222 
LEU   C    C N N 223 
LEU   O    O N N 224 
LEU   CB   C N N 225 
LEU   CG   C N N 226 
LEU   CD1  C N N 227 
LEU   CD2  C N N 228 
LEU   OXT  O N N 229 
LEU   H    H N N 230 
LEU   H2   H N N 231 
LEU   HA   H N N 232 
LEU   HB2  H N N 233 
LEU   HB3  H N N 234 
LEU   HG   H N N 235 
LEU   HD11 H N N 236 
LEU   HD12 H N N 237 
LEU   HD13 H N N 238 
LEU   HD21 H N N 239 
LEU   HD22 H N N 240 
LEU   HD23 H N N 241 
LEU   HXT  H N N 242 
LYS   N    N N N 243 
LYS   CA   C N S 244 
LYS   C    C N N 245 
LYS   O    O N N 246 
LYS   CB   C N N 247 
LYS   CG   C N N 248 
LYS   CD   C N N 249 
LYS   CE   C N N 250 
LYS   NZ   N N N 251 
LYS   OXT  O N N 252 
LYS   H    H N N 253 
LYS   H2   H N N 254 
LYS   HA   H N N 255 
LYS   HB2  H N N 256 
LYS   HB3  H N N 257 
LYS   HG2  H N N 258 
LYS   HG3  H N N 259 
LYS   HD2  H N N 260 
LYS   HD3  H N N 261 
LYS   HE2  H N N 262 
LYS   HE3  H N N 263 
LYS   HZ1  H N N 264 
LYS   HZ2  H N N 265 
LYS   HZ3  H N N 266 
LYS   HXT  H N N 267 
MET   N    N N N 268 
MET   CA   C N S 269 
MET   C    C N N 270 
MET   O    O N N 271 
MET   CB   C N N 272 
MET   CG   C N N 273 
MET   SD   S N N 274 
MET   CE   C N N 275 
MET   OXT  O N N 276 
MET   H    H N N 277 
MET   H2   H N N 278 
MET   HA   H N N 279 
MET   HB2  H N N 280 
MET   HB3  H N N 281 
MET   HG2  H N N 282 
MET   HG3  H N N 283 
MET   HE1  H N N 284 
MET   HE2  H N N 285 
MET   HE3  H N N 286 
MET   HXT  H N N 287 
PHE   N    N N N 288 
PHE   CA   C N S 289 
PHE   C    C N N 290 
PHE   O    O N N 291 
PHE   CB   C N N 292 
PHE   CG   C Y N 293 
PHE   CD1  C Y N 294 
PHE   CD2  C Y N 295 
PHE   CE1  C Y N 296 
PHE   CE2  C Y N 297 
PHE   CZ   C Y N 298 
PHE   OXT  O N N 299 
PHE   H    H N N 300 
PHE   H2   H N N 301 
PHE   HA   H N N 302 
PHE   HB2  H N N 303 
PHE   HB3  H N N 304 
PHE   HD1  H N N 305 
PHE   HD2  H N N 306 
PHE   HE1  H N N 307 
PHE   HE2  H N N 308 
PHE   HZ   H N N 309 
PHE   HXT  H N N 310 
PRO   N    N N N 311 
PRO   CA   C N S 312 
PRO   C    C N N 313 
PRO   O    O N N 314 
PRO   CB   C N N 315 
PRO   CG   C N N 316 
PRO   CD   C N N 317 
PRO   OXT  O N N 318 
PRO   H    H N N 319 
PRO   HA   H N N 320 
PRO   HB2  H N N 321 
PRO   HB3  H N N 322 
PRO   HG2  H N N 323 
PRO   HG3  H N N 324 
PRO   HD2  H N N 325 
PRO   HD3  H N N 326 
PRO   HXT  H N N 327 
SER   N    N N N 328 
SER   CA   C N S 329 
SER   C    C N N 330 
SER   O    O N N 331 
SER   CB   C N N 332 
SER   OG   O N N 333 
SER   OXT  O N N 334 
SER   H    H N N 335 
SER   H2   H N N 336 
SER   HA   H N N 337 
SER   HB2  H N N 338 
SER   HB3  H N N 339 
SER   HG   H N N 340 
SER   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 
A1BBU C1  C2   sing N N 1   
A1BBU C6  C7   sing N N 2   
A1BBU C6  C5   sing N N 3   
A1BBU C7  C8   sing N N 4   
A1BBU C2  C3   sing N N 5   
A1BBU C2  C5   sing N N 6   
A1BBU C2  C4   sing N N 7   
A1BBU C5  N1   sing N N 8   
A1BBU C8  N1   sing N N 9   
A1BBU N1  C9   sing N N 10  
A1BBU C9  N2   doub Y N 11  
A1BBU C9  C12  sing Y N 12  
A1BBU N2  C10  sing Y N 13  
A1BBU C13 C12  sing Y N 14  
A1BBU C13 C14  doub Y N 15  
A1BBU C12 C11  doub Y N 16  
A1BBU C14 N4   sing Y N 17  
A1BBU C10 N3   doub Y N 18  
A1BBU C11 N3   sing Y N 19  
A1BBU C11 N4   sing Y N 20  
A1BBU C3  H7   sing N N 21  
A1BBU C3  H6   sing N N 22  
A1BBU C3  H5   sing N N 23  
A1BBU C6  H12  sing N N 24  
A1BBU C6  H11  sing N N 25  
A1BBU C14 H19  sing N N 26  
A1BBU C1  H2   sing N N 27  
A1BBU C1  H3   sing N N 28  
A1BBU C1  H4   sing N N 29  
A1BBU C10 H17  sing N N 30  
A1BBU C13 H18  sing N N 31  
A1BBU C4  H8   sing N N 32  
A1BBU C4  H10  sing N N 33  
A1BBU C4  H9   sing N N 34  
A1BBU C5  H1   sing N N 35  
A1BBU C7  H13  sing N N 36  
A1BBU C7  H14  sing N N 37  
A1BBU C8  H16  sing N N 38  
A1BBU C8  H15  sing N N 39  
A1BBU N4  H20  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TYR   N   CA   sing N N 346 
TYR   N   H    sing N N 347 
TYR   N   H2   sing N N 348 
TYR   CA  C    sing N N 349 
TYR   CA  CB   sing N N 350 
TYR   CA  HA   sing N N 351 
TYR   C   O    doub N N 352 
TYR   C   OXT  sing N N 353 
TYR   CB  CG   sing N N 354 
TYR   CB  HB2  sing N N 355 
TYR   CB  HB3  sing N N 356 
TYR   CG  CD1  doub Y N 357 
TYR   CG  CD2  sing Y N 358 
TYR   CD1 CE1  sing Y N 359 
TYR   CD1 HD1  sing N N 360 
TYR   CD2 CE2  doub Y N 361 
TYR   CD2 HD2  sing N N 362 
TYR   CE1 CZ   doub Y N 363 
TYR   CE1 HE1  sing N N 364 
TYR   CE2 CZ   sing Y N 365 
TYR   CE2 HE2  sing N N 366 
TYR   CZ  OH   sing N N 367 
TYR   OH  HH   sing N N 368 
TYR   OXT HXT  sing N N 369 
VAL   N   CA   sing N N 370 
VAL   N   H    sing N N 371 
VAL   N   H2   sing N N 372 
VAL   CA  C    sing N N 373 
VAL   CA  CB   sing N N 374 
VAL   CA  HA   sing N N 375 
VAL   C   O    doub N N 376 
VAL   C   OXT  sing N N 377 
VAL   CB  CG1  sing N N 378 
VAL   CB  CG2  sing N N 379 
VAL   CB  HB   sing N N 380 
VAL   CG1 HG11 sing N N 381 
VAL   CG1 HG12 sing N N 382 
VAL   CG1 HG13 sing N N 383 
VAL   CG2 HG21 sing N N 384 
VAL   CG2 HG22 sing N N 385 
VAL   CG2 HG23 sing N N 386 
VAL   OXT HXT  sing N N 387 
# 
_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                    7HFT 
_atom_sites.fract_transf_matrix[1][1]   0.011249 
_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]   0.011249 
_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]   0.025229 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.753 -16.336 22.290  0.86 53.16 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.657 -16.294 22.404  0.14 51.82 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.786 -15.260 22.478  0.86 52.81 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.722 -15.194 22.603  0.14 51.59 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.437 -13.909 22.193  0.86 51.27 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.390 -13.864 22.278  0.14 50.58 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.552 -13.641 22.640  0.86 51.66 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.479 -13.569 22.773  0.14 50.94 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.169 -15.303 23.890  0.86 53.66 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.155 -15.192 24.035  0.14 52.12 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.159 -14.176 24.068  0.86 53.88 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.188 -14.030 24.220  0.14 52.27 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.516 -16.656 24.145  0.86 53.90 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.470 -16.515 24.338  0.14 52.27 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.064 -15.374 21.844  0.86 63.52 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.975 -15.300 21.996  0.14 62.05 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.871 -15.184 24.548  0.86 64.54 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.883 -15.081 24.665  0.14 62.69 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.656 -14.330 24.883  0.86 64.81 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.699 -14.157 25.048  0.14 62.87 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.633 -13.332 24.127  0.86 64.81 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.691 -13.201 24.258  0.14 62.87 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.558 -14.168 23.306  0.86 64.81 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.571 -14.011 23.472  0.14 62.87 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.076 -16.636 25.009  0.86 64.82 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.063 -16.465 25.217  0.14 62.87 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.865 -16.828 23.447  0.86 64.82 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.789 -16.679 23.667  0.14 62.87 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.200 -17.344 24.137  0.86 64.82 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.131 -17.225 24.320  0.14 62.87 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.733 -13.064 21.441  1.00 48.93 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.193 -11.722 21.105  1.00 44.62 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.056 -10.733 21.348  1.00 40.79 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.935 -11.115 21.699  1.00 40.27 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.748 -11.647 19.674  1.00 43.82 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.722 -12.012 18.625  1.00 42.93 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.607 -11.491 18.621  1.00 42.79 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.096 -12.914 17.720  1.00 42.60 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.965 -13.256 21.103  0.86 58.87 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.998 -13.283 21.050  0.14 58.87 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.917 -11.487 21.700  1.00 53.69 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 20.045 -10.739 19.497  1.00 52.74 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.494 -12.261 19.590  1.00 52.74 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.553 -13.156 17.098  1.00 51.27 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.886 -13.256 17.756  1.00 51.27 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.349 -9.447  21.157  1.00 37.16 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.446 -8.372  21.553  1.00 33.73 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.520 -7.903  20.433  1.00 29.12 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.775 -6.938  20.631  1.00 29.67 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.240 -7.189  22.117  1.00 35.20 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.121 -6.656  21.146  1.00 35.76 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 19.077 -9.171  20.791  1.00 44.74 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.886 -8.699  22.269  1.00 40.63 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.621 -6.496  22.397  1.00 42.39 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.761 -7.491  22.880  1.00 42.39 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.548 -6.005  21.469  1.00 43.06 ?  5   SER   A HG   1 
ATOM   57   N N    A PHE   A 1 6   ? 16.551 -8.545  19.266  0.86 25.56 ?  6   PHE   A N    1 
ATOM   58   N N    B PHE   A 1 6   ? 16.538 -8.559  19.278  0.14 27.18 ?  6   PHE   A N    1 
ATOM   59   C CA   A PHE   A 1 6   ? 15.652 -8.163  18.182  0.86 22.28 ?  6   PHE   A CA   1 
ATOM   60   C CA   B PHE   A 1 6   ? 15.567 -8.251  18.239  0.14 25.14 ?  6   PHE   A CA   1 
ATOM   61   C C    A PHE   A 1 6   ? 14.218 -8.529  18.547  0.86 22.59 ?  6   PHE   A C    1 
ATOM   62   C C    B PHE   A 1 6   ? 14.197 -8.770  18.655  0.14 24.33 ?  6   PHE   A C    1 
ATOM   63   O O    A PHE   A 1 6   ? 13.954 -9.644  19.000  0.86 23.77 ?  6   PHE   A O    1 
ATOM   64   O O    B PHE   A 1 6   ? 14.062 -9.925  19.073  0.14 24.61 ?  6   PHE   A O    1 
ATOM   65   C CB   A PHE   A 1 6   ? 16.048 -8.875  16.891  0.86 20.17 ?  6   PHE   A CB   1 
ATOM   66   C CB   B PHE   A 1 6   ? 15.986 -8.906  16.925  0.14 24.02 ?  6   PHE   A CB   1 
ATOM   67   C CG   A PHE   A 1 6   ? 17.308 -8.343  16.262  0.86 18.76 ?  6   PHE   A CG   1 
ATOM   68   C CG   B PHE   A 1 6   ? 17.313 -8.430  16.405  0.14 23.01 ?  6   PHE   A CG   1 
ATOM   69   C CD1  A PHE   A 1 6   ? 17.302 -7.149  15.559  0.86 18.43 ?  6   PHE   A CD1  1 
ATOM   70   C CD1  B PHE   A 1 6   ? 17.395 -7.295  15.614  0.14 22.57 ?  6   PHE   A CD1  1 
ATOM   71   C CD2  A PHE   A 1 6   ? 18.494 -9.051  16.361  0.86 18.81 ?  6   PHE   A CD2  1 
ATOM   72   C CD2  B PHE   A 1 6   ? 18.477 -9.119  16.701  0.14 22.64 ?  6   PHE   A CD2  1 
ATOM   73   C CE1  A PHE   A 1 6   ? 18.463 -6.664  14.978  0.86 18.62 ?  6   PHE   A CE1  1 
ATOM   74   C CE1  B PHE   A 1 6   ? 18.615 -6.855  15.132  0.14 22.34 ?  6   PHE   A CE1  1 
ATOM   75   C CE2  A PHE   A 1 6   ? 19.652 -8.580  15.781  0.86 18.87 ?  6   PHE   A CE2  1 
ATOM   76   C CE2  B PHE   A 1 6   ? 19.700 -8.685  16.221  0.14 22.35 ?  6   PHE   A CE2  1 
ATOM   77   C CZ   A PHE   A 1 6   ? 19.641 -7.383  15.088  0.86 18.59 ?  6   PHE   A CZ   1 
ATOM   78   C CZ   B PHE   A 1 6   ? 19.768 -7.551  15.435  0.14 22.27 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 17.076 -9.201  19.084  0.86 30.83 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 17.097 -9.179  19.075  0.14 32.77 ?  6   PHE   A H    1 
ATOM   81   H HA   A PHE   A 1 6   ? 15.700 -7.210  18.042  0.86 26.88 ?  6   PHE   A HA   1 
ATOM   82   H HA   B PHE   A 1 6   ? 15.514 -7.291  18.113  0.14 30.31 ?  6   PHE   A HA   1 
ATOM   83   H HB2  A PHE   A 1 6   ? 16.185 -9.820  17.085  0.86 24.35 ?  6   PHE   A HB2  1 
ATOM   84   H HB2  B PHE   A 1 6   ? 16.045 -9.865  17.062  0.14 28.97 ?  6   PHE   A HB2  1 
ATOM   85   H HB3  A PHE   A 1 6   ? 15.327 -8.778  16.250  0.86 24.35 ?  6   PHE   A HB3  1 
ATOM   86   H HB3  B PHE   A 1 6   ? 15.314 -8.711  16.254  0.14 28.97 ?  6   PHE   A HB3  1 
ATOM   87   H HD1  A PHE   A 1 6   ? 16.510 -6.665  15.485  0.86 22.26 ?  6   PHE   A HD1  1 
ATOM   88   H HD1  B PHE   A 1 6   ? 16.621 -6.824  15.408  0.14 27.24 ?  6   PHE   A HD1  1 
ATOM   89   H HD2  A PHE   A 1 6   ? 18.507 -9.856  16.828  0.86 22.71 ?  6   PHE   A HD2  1 
ATOM   90   H HD2  B PHE   A 1 6   ? 18.437 -9.883  17.229  0.14 27.31 ?  6   PHE   A HD2  1 
ATOM   91   H HE1  A PHE   A 1 6   ? 18.451 -5.858  14.510  0.86 22.50 ?  6   PHE   A HE1  1 
ATOM   92   H HE1  B PHE   A 1 6   ? 18.658 -6.091  14.602  0.14 26.96 ?  6   PHE   A HE1  1 
ATOM   93   H HE2  A PHE   A 1 6   ? 20.445 -9.059  15.859  0.86 22.80 ?  6   PHE   A HE2  1 
ATOM   94   H HE2  B PHE   A 1 6   ? 20.475 -9.156  16.427  0.14 26.97 ?  6   PHE   A HE2  1 
ATOM   95   H HZ   A PHE   A 1 6   ? 20.421 -7.056  14.697  0.86 22.46 ?  6   PHE   A HZ   1 
ATOM   96   H HZ   B PHE   A 1 6   ? 20.590 -7.257  15.111  0.14 26.88 ?  6   PHE   A HZ   1 
ATOM   97   N N    A SER   A 1 7   ? 13.286 -7.598  18.335  0.86 22.41 ?  7   SER   A N    1 
ATOM   98   N N    B SER   A 1 7   ? 13.178 -7.919  18.545  0.14 23.30 ?  7   SER   A N    1 
ATOM   99   C CA   A SER   A 1 7   ? 11.916 -7.752  18.809  0.86 23.41 ?  7   SER   A CA   1 
ATOM   100  C CA   B SER   A 1 7   ? 11.823 -8.302  18.911  0.14 22.34 ?  7   SER   A CA   1 
ATOM   101  C C    A SER   A 1 7   ? 10.921 -7.482  17.688  0.86 21.86 ?  7   SER   A C    1 
ATOM   102  C C    B SER   A 1 7   ? 10.841 -7.686  17.927  0.14 21.20 ?  7   SER   A C    1 
ATOM   103  O O    A SER   A 1 7   ? 11.128 -6.590  16.861  0.86 21.70 ?  7   SER   A O    1 
ATOM   104  O O    B SER   A 1 7   ? 11.119 -6.655  17.310  0.14 21.13 ?  7   SER   A O    1 
ATOM   105  C CB   A SER   A 1 7   ? 11.648 -6.800  19.982  0.86 25.44 ?  7   SER   A CB   1 
ATOM   106  C CB   B SER   A 1 7   ? 11.469 -7.874  20.343  0.14 22.56 ?  7   SER   A CB   1 
ATOM   107  O OG   A SER   A 1 7   ? 10.320 -6.931  20.450  0.86 27.40 ?  7   SER   A OG   1 
ATOM   108  O OG   B SER   A 1 7   ? 11.182 -6.488  20.412  0.14 22.69 ?  7   SER   A OG   1 
ATOM   109  H H    A SER   A 1 7   ? 13.427 -6.864  17.908  0.86 27.03 ?  7   SER   A H    1 
ATOM   110  H H    B SER   A 1 7   ? 13.247 -7.111  18.250  0.14 28.11 ?  7   SER   A H    1 
ATOM   111  H HA   A SER   A 1 7   ? 11.779 -8.659  19.120  0.86 28.24 ?  7   SER   A HA   1 
ATOM   112  H HA   B SER   A 1 7   ? 11.737 -9.265  18.858  0.14 26.96 ?  7   SER   A HA   1 
ATOM   113  H HB2  A SER   A 1 7   ? 12.258 -7.013  20.709  0.86 30.67 ?  7   SER   A HB2  1 
ATOM   114  H HB2  B SER   A 1 7   ? 10.695 -8.383  20.639  0.14 27.22 ?  7   SER   A HB2  1 
ATOM   115  H HB3  A SER   A 1 7   ? 11.793 -5.885  19.690  0.86 30.67 ?  7   SER   A HB3  1 
ATOM   116  H HB3  B SER   A 1 7   ? 12.225 -8.063  20.922  0.14 27.22 ?  7   SER   A HB3  1 
ATOM   117  H HG   A SER   A 1 7   ? 10.186 -6.403  21.090  0.86 33.02 ?  7   SER   A HG   1 
ATOM   118  H HG   B SER   A 1 7   ? 10.977 -6.279  21.199  0.14 27.37 ?  7   SER   A HG   1 
ATOM   119  N N    A GLY   A 1 8   ? 9.835  -8.257  17.667  0.86 21.10 ?  8   GLY   A N    1 
ATOM   120  N N    B GLY   A 1 8   ? 9.686  -8.332  17.787  0.14 20.16 ?  8   GLY   A N    1 
ATOM   121  C CA   A GLY   A 1 8   ? 8.745  -8.007  16.746  0.86 20.47 ?  8   GLY   A CA   1 
ATOM   122  C CA   B GLY   A 1 8   ? 8.676  -7.900  16.846  0.14 19.25 ?  8   GLY   A CA   1 
ATOM   123  C C    A GLY   A 1 8   ? 8.934  -8.525  15.339  0.86 19.39 ?  8   GLY   A C    1 
ATOM   124  C C    B GLY   A 1 8   ? 8.858  -8.414  15.438  0.14 18.20 ?  8   GLY   A C    1 
ATOM   125  O O    A GLY   A 1 8   ? 8.185  -8.113  14.445  0.86 20.20 ?  8   GLY   A O    1 
ATOM   126  O O    B GLY   A 1 8   ? 8.116  -7.993  14.543  0.14 18.28 ?  8   GLY   A O    1 
ATOM   127  H H    A GLY   A 1 8   ? 9.711  -8.933  18.183  0.86 25.47 ?  8   GLY   A H    1 
ATOM   128  H H    B GLY   A 1 8   ? 9.469  -9.034  18.233  0.14 24.33 ?  8   GLY   A H    1 
ATOM   129  H HA2  A GLY   A 1 8   ? 7.938  -8.411  17.101  0.86 24.71 ?  8   GLY   A HA2  1 
ATOM   130  H HA2  B GLY   A 1 8   ? 7.806  -8.189  17.163  0.14 23.25 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  A GLY   A 1 8   ? 8.597  -7.048  16.693  0.86 24.71 ?  8   GLY   A HA3  1 
ATOM   132  H HA3  B GLY   A 1 8   ? 8.675  -6.932  16.806  0.14 23.25 ?  8   GLY   A HA3  1 
ATOM   133  N N    A TYR   A 1 9   ? 9.900  -9.412  15.108  0.86 17.66 ?  9   TYR   A N    1 
ATOM   134  N N    B TYR   A 1 9   ? 9.816  -9.307  15.212  0.14 17.19 ?  9   TYR   A N    1 
ATOM   135  C CA   A TYR   A 1 9   ? 10.153 -9.951  13.779  0.86 16.25 ?  9   TYR   A CA   1 
ATOM   136  C CA   B TYR   A 1 9   ? 10.089 -9.835  13.886  0.14 16.19 ?  9   TYR   A CA   1 
ATOM   137  C C    A TYR   A 1 9   ? 9.278  -11.166 13.505  0.86 16.15 ?  9   TYR   A C    1 
ATOM   138  C C    B TYR   A 1 9   ? 9.216  -11.050 13.601  0.14 15.51 ?  9   TYR   A C    1 
ATOM   139  O O    A TYR   A 1 9   ? 9.007  -11.976 14.399  0.86 17.97 ?  9   TYR   A O    1 
ATOM   140  O O    B TYR   A 1 9   ? 8.805  -11.775 14.511  0.14 15.79 ?  9   TYR   A O    1 
ATOM   141  C CB   A TYR   A 1 9   ? 11.630 -10.347 13.612  0.86 16.43 ?  9   TYR   A CB   1 
ATOM   142  C CB   B TYR   A 1 9   ? 11.562 -10.233 13.763  0.14 16.23 ?  9   TYR   A CB   1 
ATOM   143  C CG   A TYR   A 1 9   ? 12.543 -9.150  13.444  0.86 16.35 ?  9   TYR   A CG   1 
ATOM   144  C CG   B TYR   A 1 9   ? 12.509 -9.060  13.637  0.14 16.18 ?  9   TYR   A CG   1 
ATOM   145  C CD1  A TYR   A 1 9   ? 12.871 -8.351  14.530  0.86 16.98 ?  9   TYR   A CD1  1 
ATOM   146  C CD1  B TYR   A 1 9   ? 12.788 -8.246  14.726  0.14 16.38 ?  9   TYR   A CD1  1 
ATOM   147  C CD2  A TYR   A 1 9   ? 13.045 -8.800  12.198  0.86 15.82 ?  9   TYR   A CD2  1 
ATOM   148  C CD2  B TYR   A 1 9   ? 13.128 -8.770  12.428  0.14 15.99 ?  9   TYR   A CD2  1 
ATOM   149  C CE1  A TYR   A 1 9   ? 13.671 -7.235  14.385  0.86 17.36 ?  9   TYR   A CE1  1 
ATOM   150  C CE1  B TYR   A 1 9   ? 13.651 -7.172  14.615  0.14 16.39 ?  9   TYR   A CE1  1 
ATOM   151  C CE2  A TYR   A 1 9   ? 13.847 -7.681  12.040  0.86 16.04 ?  9   TYR   A CE2  1 
ATOM   152  C CE2  B TYR   A 1 9   ? 13.990 -7.697  12.306  0.14 16.14 ?  9   TYR   A CE2  1 
ATOM   153  C CZ   A TYR   A 1 9   ? 14.164 -6.907  13.137  0.86 17.04 ?  9   TYR   A CZ   1 
ATOM   154  C CZ   B TYR   A 1 9   ? 14.251 -6.904  13.403  0.14 16.43 ?  9   TYR   A CZ   1 
ATOM   155  O OH   A TYR   A 1 9   ? 14.958 -5.797  12.979  0.86 18.00 ?  9   TYR   A OH   1 
ATOM   156  O OH   B TYR   A 1 9   ? 15.110 -5.837  13.288  0.14 16.79 ?  9   TYR   A OH   1 
ATOM   157  H H    A TYR   A 1 9   ? 10.431 -9.715  15.714  0.86 21.34 ?  9   TYR   A H    1 
ATOM   158  H H    B TYR   A 1 9   ? 10.332 -9.626  15.822  0.14 20.78 ?  9   TYR   A H    1 
ATOM   159  H HA   A TYR   A 1 9   ? 9.950  -9.270  13.118  0.86 19.65 ?  9   TYR   A HA   1 
ATOM   160  H HA   B TYR   A 1 9   ? 9.895  -9.159  13.222  0.14 19.57 ?  9   TYR   A HA   1 
ATOM   161  H HB2  A TYR   A 1 9   ? 11.916 -10.847 14.394  0.86 19.86 ?  9   TYR   A HB2  1 
ATOM   162  H HB2  B TYR   A 1 9   ? 11.818 -10.738 14.551  0.14 19.63 ?  9   TYR   A HB2  1 
ATOM   163  H HB3  A TYR   A 1 9   ? 11.706 -10.901 12.819  0.86 19.86 ?  9   TYR   A HB3  1 
ATOM   164  H HB3  B TYR   A 1 9   ? 11.667 -10.783 12.972  0.14 19.63 ?  9   TYR   A HB3  1 
ATOM   165  H HD1  A TYR   A 1 9   ? 12.525 -8.572  15.373  0.86 20.53 ?  9   TYR   A HD1  1 
ATOM   166  H HD1  B TYR   A 1 9   ? 12.383 -8.425  15.544  0.14 19.80 ?  9   TYR   A HD1  1 
ATOM   167  H HD2  A TYR   A 1 9   ? 12.830 -9.317  11.454  0.86 19.13 ?  9   TYR   A HD2  1 
ATOM   168  H HD2  B TYR   A 1 9   ? 12.955 -9.304  11.686  0.14 19.34 ?  9   TYR   A HD2  1 
ATOM   169  H HE1  A TYR   A 1 9   ? 13.876 -6.716  15.127  0.86 20.98 ?  9   TYR   A HE1  1 
ATOM   170  H HE1  B TYR   A 1 9   ? 13.827 -6.635  15.353  0.14 19.82 ?  9   TYR   A HE1  1 
ATOM   171  H HE2  A TYR   A 1 9   ? 14.185 -7.457  11.203  0.86 19.39 ?  9   TYR   A HE2  1 
ATOM   172  H HE2  B TYR   A 1 9   ? 14.400 -7.515  11.490  0.14 19.51 ?  9   TYR   A HE2  1 
ATOM   173  H HH   A TYR   A 1 9   ? 15.068 -5.424  13.725  0.86 21.75 ?  9   TYR   A HH   1 
ATOM   174  H HH   B TYR   A 1 9   ? 15.177 -5.442  14.027  0.14 20.30 ?  9   TYR   A HH   1 
ATOM   175  N N    A LEU   A 1 10  ? 8.848  -11.283 12.254  0.86 15.39 ?  10  LEU   A N    1 
ATOM   176  N N    B LEU   A 1 10  ? 8.929  -11.257 12.320  0.14 14.78 ?  10  LEU   A N    1 
ATOM   177  C CA   A LEU   A 1 10  ? 8.255  -12.508 11.747  0.86 15.73 ?  10  LEU   A CA   1 
ATOM   178  C CA   B LEU   A 1 10  ? 8.248  -12.453 11.847  0.14 14.27 ?  10  LEU   A CA   1 
ATOM   179  C C    A LEU   A 1 10  ? 9.381  -13.434 11.295  0.86 14.80 ?  10  LEU   A C    1 
ATOM   180  C C    B LEU   A 1 10  ? 9.284  -13.429 11.308  0.14 13.70 ?  10  LEU   A C    1 
ATOM   181  O O    A LEU   A 1 10  ? 10.362 -12.990 10.687  0.86 14.66 ?  10  LEU   A O    1 
ATOM   182  O O    B LEU   A 1 10  ? 10.104 -13.069 10.455  0.14 13.78 ?  10  LEU   A O    1 
ATOM   183  C CB   A LEU   A 1 10  ? 7.341  -12.166 10.567  0.86 17.25 ?  10  LEU   A CB   1 
ATOM   184  C CB   B LEU   A 1 10  ? 7.235  -12.113 10.752  0.14 14.39 ?  10  LEU   A CB   1 
ATOM   185  C CG   A LEU   A 1 10  ? 6.630  -13.343 9.896   0.86 19.43 ?  10  LEU   A CG   1 
ATOM   186  C CG   B LEU   A 1 10  ? 6.702  -13.323 9.975   0.14 14.65 ?  10  LEU   A CG   1 
ATOM   187  C CD1  A LEU   A 1 10  ? 5.530  -13.906 10.788  0.86 21.15 ?  10  LEU   A CD1  1 
ATOM   188  C CD1  B LEU   A 1 10  ? 5.185  -13.350 9.957   0.14 14.72 ?  10  LEU   A CD1  1 
ATOM   189  C CD2  A LEU   A 1 10  ? 6.093  -12.958 8.523   0.86 21.50 ?  10  LEU   A CD2  1 
ATOM   190  C CD2  B LEU   A 1 10  ? 7.260  -13.337 8.557   0.14 14.89 ?  10  LEU   A CD2  1 
ATOM   191  H H    A LEU   A 1 10  ? 8.907  -10.656 11.663  0.86 18.61 ?  10  LEU   A H    1 
ATOM   192  H H    B LEU   A 1 10  ? 9.119  -10.701 11.693  0.14 17.88 ?  10  LEU   A H    1 
ATOM   193  H HA   A LEU   A 1 10  ? 7.733  -12.942 12.444  0.86 19.03 ?  10  LEU   A HA   1 
ATOM   194  H HA   B LEU   A 1 10  ? 7.776  -12.874 12.584  0.14 17.27 ?  10  LEU   A HA   1 
ATOM   195  H HB2  A LEU   A 1 10  ? 6.654  -11.553 10.879  0.86 20.84 ?  10  LEU   A HB2  1 
ATOM   196  H HB2  B LEU   A 1 10  ? 6.473  -11.670 11.159  0.14 17.41 ?  10  LEU   A HB2  1 
ATOM   197  H HB3  A LEU   A 1 10  ? 7.876  -11.728 9.888   0.86 20.84 ?  10  LEU   A HB3  1 
ATOM   198  H HB3  B LEU   A 1 10  ? 7.658  -11.514 10.116  0.14 17.41 ?  10  LEU   A HB3  1 
ATOM   199  H HG   A LEU   A 1 10  ? 7.276  -14.052 9.765   0.86 23.46 ?  10  LEU   A HG   1 
ATOM   200  H HG   B LEU   A 1 10  ? 6.998  -14.137 10.411  0.14 17.73 ?  10  LEU   A HG   1 
ATOM   201  H HD11 A LEU   A 1 10  ? 5.133  -14.676 10.350  0.86 25.53 ?  10  LEU   A HD11 1 
ATOM   202  H HD11 B LEU   A 1 10  ? 4.892  -14.127 9.455   0.14 17.82 ?  10  LEU   A HD11 1 
ATOM   203  H HD12 A LEU   A 1 10  ? 5.914  -14.175 11.639  0.86 25.53 ?  10  LEU   A HD12 1 
ATOM   204  H HD12 B LEU   A 1 10  ? 4.863  -13.407 10.871  0.14 17.82 ?  10  LEU   A HD12 1 
ATOM   205  H HD13 A LEU   A 1 10  ? 4.856  -13.224 10.933  0.86 25.53 ?  10  LEU   A HD13 1 
ATOM   206  H HD13 B LEU   A 1 10  ? 4.860  -12.541 9.538   0.14 17.82 ?  10  LEU   A HD13 1 
ATOM   207  H HD21 A LEU   A 1 10  ? 5.650  -13.730 8.137   0.86 25.95 ?  10  LEU   A HD21 1 
ATOM   208  H HD21 B LEU   A 1 10  ? 6.882  -14.089 8.077   0.14 18.02 ?  10  LEU   A HD21 1 
ATOM   209  H HD22 A LEU   A 1 10  ? 5.465  -12.229 8.624   0.86 25.95 ?  10  LEU   A HD22 1 
ATOM   210  H HD22 B LEU   A 1 10  ? 7.019  -12.507 8.115   0.14 18.02 ?  10  LEU   A HD22 1 
ATOM   211  H HD23 A LEU   A 1 10  ? 6.835  -12.687 7.964   0.86 25.95 ?  10  LEU   A HD23 1 
ATOM   212  H HD23 B LEU   A 1 10  ? 8.227  -13.420 8.595   0.14 18.02 ?  10  LEU   A HD23 1 
ATOM   213  N N    A LYS   A 1 11  ? 9.257  -14.718 11.619  0.86 14.63 ?  11  LYS   A N    1 
ATOM   214  N N    B LYS   A 1 11  ? 9.240  -14.661 11.806  0.14 13.22 ?  11  LYS   A N    1 
ATOM   215  C CA   A LYS   A 1 11  ? 10.276 -15.704 11.289  0.86 14.66 ?  11  LYS   A CA   1 
ATOM   216  C CA   B LYS   A 1 11  ? 10.159 -15.692 11.352  0.14 12.78 ?  11  LYS   A CA   1 
ATOM   217  C C    A LYS   A 1 11  ? 9.930  -16.302 9.932   0.86 14.45 ?  11  LYS   A C    1 
ATOM   218  C C    B LYS   A 1 11  ? 9.775  -16.142 9.949   0.14 12.17 ?  11  LYS   A C    1 
ATOM   219  O O    A LYS   A 1 11  ? 8.876  -16.922 9.785   0.86 16.36 ?  11  LYS   A O    1 
ATOM   220  O O    B LYS   A 1 11  ? 8.607  -16.438 9.679   0.14 11.59 ?  11  LYS   A O    1 
ATOM   221  C CB   A LYS   A 1 11  ? 10.318 -16.775 12.381  0.86 14.34 ?  11  LYS   A CB   1 
ATOM   222  C CB   B LYS   A 1 11  ? 10.111 -16.875 12.317  0.14 12.95 ?  11  LYS   A CB   1 
ATOM   223  C CG   A LYS   A 1 11  ? 11.331 -17.889 12.175  0.86 14.73 ?  11  LYS   A CG   1 
ATOM   224  C CG   B LYS   A 1 11  ? 11.216 -17.899 12.131  0.14 13.31 ?  11  LYS   A CG   1 
ATOM   225  C CD   A LYS   A 1 11  ? 11.439 -18.729 13.450  0.86 15.04 ?  11  LYS   A CD   1 
ATOM   226  C CD   B LYS   A 1 11  ? 11.253 -18.856 13.315  0.14 13.67 ?  11  LYS   A CD   1 
ATOM   227  C CE   A LYS   A 1 11  ? 12.416 -19.891 13.314  0.86 15.38 ?  11  LYS   A CE   1 
ATOM   228  C CE   B LYS   A 1 11  ? 12.284 -19.954 13.126  0.14 13.78 ?  11  LYS   A CE   1 
ATOM   229  N NZ   A LYS   A 1 11  ? 13.800 -19.435 13.048  0.86 15.61 ?  11  LYS   A NZ   1 
ATOM   230  N NZ   B LYS   A 1 11  ? 13.651 -19.412 12.904  0.14 13.87 ?  11  LYS   A NZ   1 
ATOM   231  H H    A LYS   A 1 11  ? 8.572  -15.046 12.021  0.86 17.70 ?  11  LYS   A H    1 
ATOM   232  H H    B LYS   A 1 11  ? 8.685  -14.918 12.405  0.14 16.02 ?  11  LYS   A H    1 
ATOM   233  H HA   A LYS   A 1 11  ? 11.144 -15.269 11.232  0.86 17.74 ?  11  LYS   A HA   1 
ATOM   234  H HA   B LYS   A 1 11  ? 11.061 -15.341 11.330  0.14 15.49 ?  11  LYS   A HA   1 
ATOM   235  H HB2  A LYS   A 1 11  ? 10.530 -16.335 13.222  0.86 17.35 ?  11  LYS   A HB2  1 
ATOM   236  H HB2  B LYS   A 1 11  ? 10.176 -16.534 13.222  0.14 15.69 ?  11  LYS   A HB2  1 
ATOM   237  H HB3  A LYS   A 1 11  ? 9.440  -17.177 12.441  0.86 17.35 ?  11  LYS   A HB3  1 
ATOM   238  H HB3  B LYS   A 1 11  ? 9.264  -17.332 12.200  0.14 15.69 ?  11  LYS   A HB3  1 
ATOM   239  H HG2  A LYS   A 1 11  ? 11.037 -18.460 11.449  0.86 17.82 ?  11  LYS   A HG2  1 
ATOM   240  H HG2  B LYS   A 1 11  ? 11.051 -18.413 11.324  0.14 16.12 ?  11  LYS   A HG2  1 
ATOM   241  H HG3  A LYS   A 1 11  ? 12.199 -17.507 11.981  0.86 17.82 ?  11  LYS   A HG3  1 
ATOM   242  H HG3  B LYS   A 1 11  ? 12.073 -17.446 12.074  0.14 16.12 ?  11  LYS   A HG3  1 
ATOM   243  H HD2  A LYS   A 1 11  ? 11.739 -18.166 14.177  0.86 18.19 ?  11  LYS   A HD2  1 
ATOM   244  H HD2  B LYS   A 1 11  ? 11.480 -18.361 14.119  0.14 16.55 ?  11  LYS   A HD2  1 
ATOM   245  H HD3  A LYS   A 1 11  ? 10.563 -19.100 13.657  0.86 18.19 ?  11  LYS   A HD3  1 
ATOM   246  H HD3  B LYS   A 1 11  ? 10.382 -19.272 13.415  0.14 16.55 ?  11  LYS   A HD3  1 
ATOM   247  H HE2  A LYS   A 1 11  ? 12.423 -20.400 14.142  0.86 18.60 ?  11  LYS   A HE2  1 
ATOM   248  H HE2  B LYS   A 1 11  ? 12.306 -20.510 13.922  0.14 16.69 ?  11  LYS   A HE2  1 
ATOM   249  H HE3  A LYS   A 1 11  ? 12.140 -20.459 12.578  0.86 18.60 ?  11  LYS   A HE3  1 
ATOM   250  H HE3  B LYS   A 1 11  ? 12.041 -20.487 12.354  0.14 16.69 ?  11  LYS   A HE3  1 
ATOM   251  H HZ1  A LYS   A 1 11  ? 14.344 -20.137 12.971  0.86 18.88 ?  11  LYS   A HZ1  1 
ATOM   252  H HZ1  B LYS   A 1 11  ? 14.231 -20.080 12.813  0.14 16.79 ?  11  LYS   A HZ1  1 
ATOM   253  H HZ2  A LYS   A 1 11  ? 13.826 -18.967 12.291  0.86 18.88 ?  11  LYS   A HZ2  1 
ATOM   254  H HZ2  B LYS   A 1 11  ? 13.665 -18.915 12.166  0.14 16.79 ?  11  LYS   A HZ2  1 
ATOM   255  H HZ3  A LYS   A 1 11  ? 14.087 -18.921 13.715  0.86 18.88 ?  11  LYS   A HZ3  1 
ATOM   256  H HZ3  B LYS   A 1 11  ? 13.896 -18.910 13.596  0.14 16.79 ?  11  LYS   A HZ3  1 
ATOM   257  N N    A LEU   A 1 12  ? 10.797 -16.112 8.935   0.86 13.95 ?  12  LEU   A N    1 
ATOM   258  N N    B LEU   A 1 12  ? 10.757 -16.171 9.051   0.14 12.59 ?  12  LEU   A N    1 
ATOM   259  C CA   A LEU   A 1 12  ? 10.540 -16.697 7.620   0.86 14.31 ?  12  LEU   A CA   1 
ATOM   260  C CA   B LEU   A 1 12  ? 10.567 -16.648 7.686   0.14 13.32 ?  12  LEU   A CA   1 
ATOM   261  C C    A LEU   A 1 12  ? 11.124 -18.097 7.476   0.86 14.43 ?  12  LEU   A C    1 
ATOM   262  C C    B LEU   A 1 12  ? 11.157 -18.038 7.476   0.14 13.75 ?  12  LEU   A C    1 
ATOM   263  O O    A LEU   A 1 12  ? 10.501 -18.967 6.858   0.86 15.30 ?  12  LEU   A O    1 
ATOM   264  O O    B LEU   A 1 12  ? 10.503 -18.909 6.895   0.14 13.82 ?  12  LEU   A O    1 
ATOM   265  C CB   A LEU   A 1 12  ? 11.106 -15.809 6.508   0.86 15.17 ?  12  LEU   A CB   1 
ATOM   266  C CB   B LEU   A 1 12  ? 11.185 -15.660 6.687   0.14 13.71 ?  12  LEU   A CB   1 
ATOM   267  C CG   A LEU   A 1 12  ? 10.458 -14.432 6.346   0.86 16.26 ?  12  LEU   A CG   1 
ATOM   268  C CG   B LEU   A 1 12  ? 10.394 -14.380 6.388   0.14 13.95 ?  12  LEU   A CG   1 
ATOM   269  C CD1  A LEU   A 1 12  ? 11.188 -13.653 5.258   0.86 17.31 ?  12  LEU   A CD1  1 
ATOM   270  C CD1  B LEU   A 1 12  ? 11.214 -13.415 5.538   0.14 14.03 ?  12  LEU   A CD1  1 
ATOM   271  C CD2  A LEU   A 1 12  ? 8.970  -14.560 6.031   0.86 16.51 ?  12  LEU   A CD2  1 
ATOM   272  C CD2  B LEU   A 1 12  ? 9.083  -14.715 5.696   0.14 14.19 ?  12  LEU   A CD2  1 
ATOM   273  H H    A LEU   A 1 12  ? 11.533 -15.651 8.987   0.86 16.89 ?  12  LEU   A H    1 
ATOM   274  H H    B LEU   A 1 12  ? 11.559 -15.910 9.215   0.14 15.25 ?  12  LEU   A H    1 
ATOM   275  H HA   A LEU   A 1 12  ? 9.583  -16.757 7.493   0.86 17.33 ?  12  LEU   A HA   1 
ATOM   276  H HA   B LEU   A 1 12  ? 9.616  -16.700 7.507   0.14 16.13 ?  12  LEU   A HA   1 
ATOM   277  H HB2  A LEU   A 1 12  ? 12.050 -15.662 6.680   0.86 18.36 ?  12  LEU   A HB2  1 
ATOM   278  H HB2  B LEU   A 1 12  ? 12.050 -15.387 7.031   0.14 16.60 ?  12  LEU   A HB2  1 
ATOM   279  H HB3  A LEU   A 1 12  ? 11.004 -16.274 5.662   0.86 18.36 ?  12  LEU   A HB3  1 
ATOM   280  H HB3  B LEU   A 1 12  ? 11.308 -16.124 5.845   0.14 16.60 ?  12  LEU   A HB3  1 
ATOM   281  H HG   A LEU   A 1 12  ? 10.548 -13.940 7.175   0.86 19.66 ?  12  LEU   A HG   1 
ATOM   282  H HG   B LEU   A 1 12  ? 10.183 -13.930 7.221   0.14 16.89 ?  12  LEU   A HG   1 
ATOM   283  H HD11 A LEU   A 1 12  ? 10.777 -12.782 5.158   0.86 20.92 ?  12  LEU   A HD11 1 
ATOM   284  H HD11 B LEU   A 1 12  ? 10.690 -12.616 5.366   0.14 16.98 ?  12  LEU   A HD11 1 
ATOM   285  H HD12 A LEU   A 1 12  ? 12.121 -13.549 5.516   0.86 20.92 ?  12  LEU   A HD12 1 
ATOM   286  H HD12 B LEU   A 1 12  ? 12.024 -13.181 6.019   0.14 16.98 ?  12  LEU   A HD12 1 
ATOM   287  H HD13 A LEU   A 1 12  ? 11.133 -14.145 4.423   0.86 20.92 ?  12  LEU   A HD13 1 
ATOM   288  H HD13 B LEU   A 1 12  ? 11.441 -13.847 4.699   0.14 16.98 ?  12  LEU   A HD13 1 
ATOM   289  H HD21 A LEU   A 1 12  ? 8.623  -13.690 5.780   0.86 19.96 ?  12  LEU   A HD21 1 
ATOM   290  H HD21 B LEU   A 1 12  ? 8.674  -13.897 5.373   0.14 17.17 ?  12  LEU   A HD21 1 
ATOM   291  H HD22 A LEU   A 1 12  ? 8.856  -15.185 5.297   0.86 19.96 ?  12  LEU   A HD22 1 
ATOM   292  H HD22 B LEU   A 1 12  ? 9.264  -15.311 4.952   0.14 17.17 ?  12  LEU   A HD22 1 
ATOM   293  H HD23 A LEU   A 1 12  ? 8.508  -14.888 6.818   0.86 19.96 ?  12  LEU   A HD23 1 
ATOM   294  H HD23 B LEU   A 1 12  ? 8.494  -15.151 6.332   0.14 17.17 ?  12  LEU   A HD23 1 
ATOM   295  N N    A THR   A 1 13  ? 12.324 -18.315 8.006   0.86 14.06 ?  13  THR   A N    1 
ATOM   296  N N    B THR   A 1 13  ? 12.385 -18.260 7.937   0.14 14.08 ?  13  THR   A N    1 
ATOM   297  C CA   A THR   A 1 13  ? 13.021 -19.592 7.906   0.86 14.33 ?  13  THR   A CA   1 
ATOM   298  C CA   B THR   A 1 13  ? 13.036 -19.562 7.855   0.14 14.43 ?  13  THR   A CA   1 
ATOM   299  C C    A THR   A 1 13  ? 13.797 -19.813 9.197   0.86 14.09 ?  13  THR   A C    1 
ATOM   300  C C    B THR   A 1 13  ? 13.761 -19.820 9.171   0.14 14.57 ?  13  THR   A C    1 
ATOM   301  O O    A THR   A 1 13  ? 13.712 -19.024 10.145  0.86 14.11 ?  13  THR   A O    1 
ATOM   302  O O    B THR   A 1 13  ? 13.557 -19.120 10.168  0.14 14.61 ?  13  THR   A O    1 
ATOM   303  C CB   A THR   A 1 13  ? 13.988 -19.630 6.714   0.86 15.46 ?  13  THR   A CB   1 
ATOM   304  C CB   B THR   A 1 13  ? 14.009 -19.624 6.670   0.14 14.83 ?  13  THR   A CB   1 
ATOM   305  O OG1  A THR   A 1 13  ? 15.071 -18.733 6.968   0.86 15.42 ?  13  THR   A OG1  1 
ATOM   306  O OG1  B THR   A 1 13  ? 15.030 -18.636 6.842   0.14 15.04 ?  13  THR   A OG1  1 
ATOM   307  C CG2  A THR   A 1 13  ? 13.307 -19.255 5.401   0.86 17.02 ?  13  THR   A CG2  1 
ATOM   308  C CG2  B THR   A 1 13  ? 13.288 -19.383 5.354   0.14 15.14 ?  13  THR   A CG2  1 
ATOM   309  H H    A THR   A 1 13  ? 12.769 -17.718 8.432   0.86 17.02 ?  13  THR   A H    1 
ATOM   310  H H    B THR   A 1 13  ? 12.870 -17.653 8.303   0.14 17.04 ?  13  THR   A H    1 
ATOM   311  H HA   A THR   A 1 13  ? 12.374 -20.309 7.803   0.86 17.35 ?  13  THR   A HA   1 
ATOM   312  H HA   B THR   A 1 13  ? 12.366 -20.252 7.739   0.14 17.46 ?  13  THR   A HA   1 
ATOM   313  H HB   A THR   A 1 13  ? 14.338 -20.527 6.618   0.86 18.70 ?  13  THR   A HB   1 
ATOM   314  H HB   B THR   A 1 13  ? 14.415 -20.506 6.634   0.14 17.94 ?  13  THR   A HB   1 
ATOM   315  H HG1  A THR   A 1 13  ? 15.727 -19.154 7.277   0.86 18.65 ?  13  THR   A HG1  1 
ATOM   316  H HG1  B THR   A 1 13  ? 15.569 -18.667 6.201   0.14 18.20 ?  13  THR   A HG1  1 
ATOM   317  H HG21 A THR   A 1 13  ? 13.928 -19.381 4.661   0.86 20.57 ?  13  THR   A HG21 1 
ATOM   318  H HG21 B THR   A 1 13  ? 13.907 -19.498 4.615   0.14 18.32 ?  13  THR   A HG21 1 
ATOM   319  H HG22 A THR   A 1 13  ? 12.534 -19.823 5.256   0.86 20.57 ?  13  THR   A HG22 1 
ATOM   320  H HG22 B THR   A 1 13  ? 12.559 -20.013 5.255   0.14 18.32 ?  13  THR   A HG22 1 
ATOM   321  H HG23 A THR   A 1 13  ? 13.025 -18.331 5.421   0.86 20.57 ?  13  THR   A HG23 1 
ATOM   322  H HG23 B THR   A 1 13  ? 12.934 -18.481 5.331   0.14 18.32 ?  13  THR   A HG23 1 
ATOM   323  N N    A ASP   A 1 14  ? 14.593 -20.883 9.208   0.86 14.65 ?  14  ASP   A N    1 
ATOM   324  N N    B ASP   A 1 14  ? 14.628 -20.835 9.165   0.14 14.87 ?  14  ASP   A N    1 
ATOM   325  C CA   A ASP   A 1 14  ? 15.448 -21.164 10.352  0.86 15.44 ?  14  ASP   A CA   1 
ATOM   326  C CA   B ASP   A 1 14  ? 15.421 -21.155 10.343  0.14 15.16 ?  14  ASP   A CA   1 
ATOM   327  C C    A ASP   A 1 14  ? 16.270 -19.944 10.751  0.86 14.35 ?  14  ASP   A C    1 
ATOM   328  C C    B ASP   A 1 14  ? 16.368 -20.026 10.723  0.14 14.18 ?  14  ASP   A C    1 
ATOM   329  O O    A ASP   A 1 14  ? 16.474 -19.688 11.944  0.86 15.83 ?  14  ASP   A O    1 
ATOM   330  O O    B ASP   A 1 14  ? 16.754 -19.925 11.894  0.14 14.06 ?  14  ASP   A O    1 
ATOM   331  C CB   A ASP   A 1 14  ? 16.386 -22.324 10.022  0.86 18.75 ?  14  ASP   A CB   1 
ATOM   332  C CB   B ASP   A 1 14  ? 16.227 -22.430 10.091  0.14 16.70 ?  14  ASP   A CB   1 
ATOM   333  C CG   A ASP   A 1 14  ? 17.254 -22.696 11.192  0.86 23.23 ?  14  ASP   A CG   1 
ATOM   334  C CG   B ASP   A 1 14  ? 17.409 -22.562 11.027  0.14 18.12 ?  14  ASP   A CG   1 
ATOM   335  O OD1  A ASP   A 1 14  ? 16.701 -23.148 12.217  0.86 24.10 ?  14  ASP   A OD1  1 
ATOM   336  O OD1  B ASP   A 1 14  ? 17.190 -22.746 12.242  0.14 18.34 ?  14  ASP   A OD1  1 
ATOM   337  O OD2  A ASP   A 1 14  ? 18.480 -22.519 11.090  0.86 26.58 -1 14  ASP   A OD2  1 
ATOM   338  O OD2  B ASP   A 1 14  ? 18.557 -22.472 10.547  0.14 18.96 -1 14  ASP   A OD2  1 
ATOM   339  H H    A ASP   A 1 14  ? 14.664 -21.444 8.562   0.86 17.73 ?  14  ASP   A H    1 
ATOM   340  H H    B ASP   A 1 14  ? 14.777 -21.346 8.491   0.14 17.99 ?  14  ASP   A H    1 
ATOM   341  H HA   A ASP   A 1 14  ? 14.896 -21.428 11.107  0.86 18.68 ?  14  ASP   A HA   1 
ATOM   342  H HA   B ASP   A 1 14  ? 14.830 -21.319 11.094  0.14 18.34 ?  14  ASP   A HA   1 
ATOM   343  H HB2  A ASP   A 1 14  ? 15.852 -23.105 9.774   0.86 22.65 ?  14  ASP   A HB2  1 
ATOM   344  H HB2  B ASP   A 1 14  ? 15.653 -23.202 10.222  0.14 20.18 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  A ASP   A 1 14  ? 16.955 -22.073 9.277   0.86 22.65 ?  14  ASP   A HB3  1 
ATOM   346  H HB3  B ASP   A 1 14  ? 16.563 -22.421 9.181   0.14 20.18 ?  14  ASP   A HB3  1 
ATOM   347  N N    . ASN   A 1 15  ? 16.753 -19.177 9.768   1.00 13.85 ?  15  ASN   A N    1 
ATOM   348  C CA   . ASN   A 1 15  ? 17.739 -18.130 10.027  1.00 14.16 ?  15  ASN   A CA   1 
ATOM   349  C C    . ASN   A 1 15  ? 17.375 -16.730 9.537   1.00 14.58 ?  15  ASN   A C    1 
ATOM   350  O O    . ASN   A 1 15  ? 18.144 -15.794 9.787   1.00 16.30 ?  15  ASN   A O    1 
ATOM   351  C CB   . ASN   A 1 15  ? 19.110 -18.527 9.443   1.00 14.05 ?  15  ASN   A CB   1 
ATOM   352  C CG   . ASN   A 1 15  ? 19.097 -18.621 7.934   1.00 14.24 ?  15  ASN   A CG   1 
ATOM   353  O OD1  . ASN   A 1 15  ? 18.374 -19.441 7.360   1.00 15.61 ?  15  ASN   A OD1  1 
ATOM   354  N ND2  . ASN   A 1 15  ? 19.895 -17.776 7.279   1.00 14.44 ?  15  ASN   A ND2  1 
ATOM   355  H H    A ASN   A 1 15  ? 16.514 -19.241 8.948   0.86 16.77 ?  15  ASN   A H    1 
ATOM   356  H H    B ASN   A 1 15  ? 16.456 -19.194 8.963   0.14 16.77 ?  15  ASN   A H    1 
ATOM   357  H HA   . ASN   A 1 15  ? 17.866 -18.062 10.982  1.00 17.14 ?  15  ASN   A HA   1 
ATOM   358  H HB2  . ASN   A 1 15  ? 19.773 -17.855 9.697   1.00 17.01 ?  15  ASN   A HB2  1 
ATOM   359  H HB3  . ASN   A 1 15  ? 19.376 -19.392 9.790   1.00 17.01 ?  15  ASN   A HB3  1 
ATOM   360  H HD21 . ASN   A 1 15  ? 19.926 -17.786 6.417   1.00 17.48 ?  15  ASN   A HD21 1 
ATOM   361  H HD22 . ASN   A 1 15  ? 20.391 -17.213 7.711   1.00 17.48 ?  15  ASN   A HD22 1 
ATOM   362  N N    A VAL   A 1 16  ? 16.239 -16.547 8.864   0.86 14.57 ?  16  VAL   A N    1 
ATOM   363  N N    B VAL   A 1 16  ? 16.242 -16.556 8.865   0.14 14.13 ?  16  VAL   A N    1 
ATOM   364  C CA   A VAL   A 1 16  ? 15.852 -15.258 8.295   0.86 14.79 ?  16  VAL   A CA   1 
ATOM   365  C CA   B VAL   A 1 16  ? 15.848 -15.276 8.289   0.14 13.78 ?  16  VAL   A CA   1 
ATOM   366  C C    A VAL   A 1 16  ? 14.569 -14.769 8.959   0.86 13.91 ?  16  VAL   A C    1 
ATOM   367  C C    B VAL   A 1 16  ? 14.624 -14.758 9.031   0.14 13.38 ?  16  VAL   A C    1 
ATOM   368  O O    A VAL   A 1 16  ? 13.565 -15.491 9.011   0.86 13.97 ?  16  VAL   A O    1 
ATOM   369  O O    B VAL   A 1 16  ? 13.623 -15.471 9.170   0.14 13.37 ?  16  VAL   A O    1 
ATOM   370  C CB   A VAL   A 1 16  ? 15.689 -15.329 6.766   0.86 15.61 ?  16  VAL   A CB   1 
ATOM   371  C CB   B VAL   A 1 16  ? 15.569 -15.401 6.782   0.14 13.85 ?  16  VAL   A CB   1 
ATOM   372  C CG1  A VAL   A 1 16  ? 15.249 -13.969 6.210   0.86 16.17 ?  16  VAL   A CG1  1 
ATOM   373  C CG1  B VAL   A 1 16  ? 15.187 -14.048 6.202   0.14 14.05 ?  16  VAL   A CG1  1 
ATOM   374  C CG2  A VAL   A 1 16  ? 16.986 -15.781 6.105   0.86 16.26 ?  16  VAL   A CG2  1 
ATOM   375  C CG2  B VAL   A 1 16  ? 16.783 -15.976 6.062   0.14 13.91 ?  16  VAL   A CG2  1 
ATOM   376  H H    A VAL   A 1 16  ? 15.665 -17.168 8.729   0.86 17.63 ?  16  VAL   A H    1 
ATOM   377  H H    B VAL   A 1 16  ? 15.673 -17.183 8.728   0.14 17.11 ?  16  VAL   A H    1 
ATOM   378  H HA   A VAL   A 1 16  ? 16.553 -14.610 8.484   0.86 17.89 ?  16  VAL   A HA   1 
ATOM   379  H HA   B VAL   A 1 16  ? 16.566 -14.636 8.410   0.14 16.68 ?  16  VAL   A HA   1 
ATOM   380  H HB   A VAL   A 1 16  ? 15.001 -15.979 6.556   0.86 18.87 ?  16  VAL   A HB   1 
ATOM   381  H HB   B VAL   A 1 16  ? 14.824 -16.008 6.648   0.14 16.77 ?  16  VAL   A HB   1 
ATOM   382  H HG11 A VAL   A 1 16  ? 15.349 -13.982 5.247   0.86 19.55 ?  16  VAL   A HG11 1 
ATOM   383  H HG11 B VAL   A 1 16  ? 15.187 -14.111 5.235   0.14 17.01 ?  16  VAL   A HG11 1 
ATOM   384  H HG12 A VAL   A 1 16  ? 14.319 -13.820 6.445   0.86 19.55 ?  16  VAL   A HG12 1 
ATOM   385  H HG12 B VAL   A 1 16  ? 14.302 -13.806 6.518   0.14 17.01 ?  16  VAL   A HG12 1 
ATOM   386  H HG13 A VAL   A 1 16  ? 15.806 -13.278 6.595   0.86 19.55 ?  16  VAL   A HG13 1 
ATOM   387  H HG13 B VAL   A 1 16  ? 15.836 -13.388 6.491   0.14 17.01 ?  16  VAL   A HG13 1 
ATOM   388  H HG21 A VAL   A 1 16  ? 16.877 -15.745 5.142   0.86 19.66 ?  16  VAL   A HG21 1 
ATOM   389  H HG21 B VAL   A 1 16  ? 16.622 -15.956 5.106   0.14 16.84 ?  16  VAL   A HG21 1 
ATOM   390  H HG22 A VAL   A 1 16  ? 17.704 -15.191 6.379   0.86 19.66 ?  16  VAL   A HG22 1 
ATOM   391  H HG22 B VAL   A 1 16  ? 17.561 -15.438 6.278   0.14 16.84 ?  16  VAL   A HG22 1 
ATOM   392  H HG23 A VAL   A 1 16  ? 17.182 -16.690 6.382   0.86 19.66 ?  16  VAL   A HG23 1 
ATOM   393  H HG23 B VAL   A 1 16  ? 16.922 -16.890 6.355   0.14 16.84 ?  16  VAL   A HG23 1 
ATOM   394  N N    A TYR   A 1 17  ? 14.602 -13.509 9.403   0.86 13.84 ?  17  TYR   A N    1 
ATOM   395  N N    B TYR   A 1 17  ? 14.709 -13.516 9.502   0.14 13.13 ?  17  TYR   A N    1 
ATOM   396  C CA   A TYR   A 1 17  ? 13.526 -12.827 10.106  0.86 13.96 ?  17  TYR   A CA   1 
ATOM   397  C CA   B TYR   A 1 17  ? 13.608 -12.813 10.143  0.14 12.98 ?  17  TYR   A CA   1 
ATOM   398  C C    A TYR   A 1 17  ? 13.255 -11.497 9.412   0.86 14.32 ?  17  TYR   A C    1 
ATOM   399  C C    B TYR   A 1 17  ? 13.332 -11.518 9.385   0.14 12.77 ?  17  TYR   A C    1 
ATOM   400  O O    A TYR   A 1 17  ? 14.166 -10.902 8.837   0.86 13.85 ?  17  TYR   A O    1 
ATOM   401  O O    B TYR   A 1 17  ? 14.102 -11.110 8.512   0.14 12.82 ?  17  TYR   A O    1 
ATOM   402  C CB   A TYR   A 1 17  ? 13.946 -12.572 11.560  0.86 14.72 ?  17  TYR   A CB   1 
ATOM   403  C CB   B TYR   A 1 17  ? 13.928 -12.526 11.617  0.14 13.32 ?  17  TYR   A CB   1 
ATOM   404  C CG   A TYR   A 1 17  ? 14.155 -13.843 12.357  0.86 15.40 ?  17  TYR   A CG   1 
ATOM   405  C CG   B TYR   A 1 17  ? 14.087 -13.779 12.456  0.14 13.69 ?  17  TYR   A CG   1 
ATOM   406  C CD1  A TYR   A 1 17  ? 15.322 -14.587 12.246  0.86 16.22 ?  17  TYR   A CD1  1 
ATOM   407  C CD1  B TYR   A 1 17  ? 15.295 -14.465 12.498  0.14 13.81 ?  17  TYR   A CD1  1 
ATOM   408  C CD2  A TYR   A 1 17  ? 13.173 -14.310 13.213  0.86 15.85 ?  17  TYR   A CD2  1 
ATOM   409  C CD2  B TYR   A 1 17  ? 13.027 -14.278 13.201  0.14 14.12 ?  17  TYR   A CD2  1 
ATOM   410  C CE1  A TYR   A 1 17  ? 15.501 -15.764 12.968  0.86 16.37 ?  17  TYR   A CE1  1 
ATOM   411  C CE1  B TYR   A 1 17  ? 15.441 -15.614 13.260  0.14 14.08 ?  17  TYR   A CE1  1 
ATOM   412  C CE2  A TYR   A 1 17  ? 13.341 -15.491 13.941  0.86 16.41 ?  17  TYR   A CE2  1 
ATOM   413  C CE2  B TYR   A 1 17  ? 13.163 -15.426 13.965  0.14 14.33 ?  17  TYR   A CE2  1 
ATOM   414  C CZ   A TYR   A 1 17  ? 14.508 -16.212 13.817  0.86 16.39 ?  17  TYR   A CZ   1 
ATOM   415  C CZ   B TYR   A 1 17  ? 14.371 -16.089 13.991  0.14 14.32 ?  17  TYR   A CZ   1 
ATOM   416  O OH   A TYR   A 1 17  ? 14.676 -17.374 14.541  0.86 17.20 ?  17  TYR   A OH   1 
ATOM   417  O OH   B TYR   A 1 17  ? 14.507 -17.230 14.752  0.14 14.56 ?  17  TYR   A OH   1 
ATOM   418  H H    A TYR   A 1 17  ? 15.291 -12.992 9.286   0.86 16.75 ?  17  TYR   A H    1 
ATOM   419  H H    B TYR   A 1 17  ? 15.429 -13.046 9.458   0.14 15.90 ?  17  TYR   A H    1 
ATOM   420  H HA   A TYR   A 1 17  ? 12.724 -13.366 10.087  0.86 16.89 ?  17  TYR   A HA   1 
ATOM   421  H HA   B TYR   A 1 17  ? 12.815 -13.366 10.105  0.14 15.72 ?  17  TYR   A HA   1 
ATOM   422  H HB2  A TYR   A 1 17  ? 14.780 -12.079 11.563  0.86 17.81 ?  17  TYR   A HB2  1 
ATOM   423  H HB2  B TYR   A 1 17  ? 14.756 -12.026 11.667  0.14 16.13 ?  17  TYR   A HB2  1 
ATOM   424  H HB3  A TYR   A 1 17  ? 13.255 -12.057 11.995  0.86 17.81 ?  17  TYR   A HB3  1 
ATOM   425  H HB3  B TYR   A 1 17  ? 13.204 -12.004 11.995  0.14 16.13 ?  17  TYR   A HB3  1 
ATOM   426  H HD1  A TYR   A 1 17  ? 15.995 -14.297 11.674  0.86 19.61 ?  17  TYR   A HD1  1 
ATOM   427  H HD1  B TYR   A 1 17  ? 16.017 -14.149 12.005  0.14 16.72 ?  17  TYR   A HD1  1 
ATOM   428  H HD2  A TYR   A 1 17  ? 12.375 -13.838 13.303  0.86 19.17 ?  17  TYR   A HD2  1 
ATOM   429  H HD2  B TYR   A 1 17  ? 12.210 -13.835 13.186  0.14 17.09 ?  17  TYR   A HD2  1 
ATOM   430  H HE1  A TYR   A 1 17  ? 16.294 -16.248 12.883  0.86 19.79 ?  17  TYR   A HE1  1 
ATOM   431  H HE1  B TYR   A 1 17  ? 16.258 -16.063 13.277  0.14 17.04 ?  17  TYR   A HE1  1 
ATOM   432  H HE2  A TYR   A 1 17  ? 12.669 -15.788 14.514  0.86 19.84 ?  17  TYR   A HE2  1 
ATOM   433  H HE2  B TYR   A 1 17  ? 12.443 -15.748 14.460  0.14 17.35 ?  17  TYR   A HE2  1 
ATOM   434  H HH   A TYR   A 1 17  ? 15.447 -17.683 14.408  0.86 20.79 ?  17  TYR   A HH   1 
ATOM   435  H HH   B TYR   A 1 17  ? 13.750 -17.526 14.967  0.14 17.62 ?  17  TYR   A HH   1 
ATOM   436  N N    A ILE   A 1 18  ? 12.009 -11.010 9.469   0.86 14.27 ?  18  ILE   A N    1 
ATOM   437  N N    B ILE   A 1 18  ? 12.222 -10.859 9.722   0.14 12.52 ?  18  ILE   A N    1 
ATOM   438  C CA   A ILE   A 1 18  ? 11.625 -9.802  8.736   0.86 14.64 ?  18  ILE   A CA   1 
ATOM   439  C CA   B ILE   A 1 18  ? 11.812 -9.652  9.007   0.14 12.61 ?  18  ILE   A CA   1 
ATOM   440  C C    A ILE   A 1 18  ? 10.659 -8.948  9.553   0.86 15.23 ?  18  ILE   A C    1 
ATOM   441  C C    B ILE   A 1 18  ? 10.885 -8.831  9.889   0.14 12.85 ?  18  ILE   A C    1 
ATOM   442  O O    A ILE   A 1 18  ? 9.828  -9.463  10.306  0.86 15.45 ?  18  ILE   A O    1 
ATOM   443  O O    B ILE   A 1 18  ? 10.132 -9.373  10.702  0.14 12.96 ?  18  ILE   A O    1 
ATOM   444  C CB   A ILE   A 1 18  ? 11.050 -10.172 7.349   0.86 14.66 ?  18  ILE   A CB   1 
ATOM   445  C CB   B ILE   A 1 18  ? 11.166 -9.994  7.640   0.14 12.26 ?  18  ILE   A CB   1 
ATOM   446  C CG1  A ILE   A 1 18  ? 10.991 -8.954  6.429   0.86 15.50 ?  18  ILE   A CG1  1 
ATOM   447  C CG1  B ILE   A 1 18  ? 10.965 -8.724  6.806   0.14 12.29 ?  18  ILE   A CG1  1 
ATOM   448  C CG2  A ILE   A 1 18  ? 9.689  -10.869 7.481   0.86 15.67 ?  18  ILE   A CG2  1 
ATOM   449  C CG2  B ILE   A 1 18  ? 9.850  -10.737 7.832   0.14 12.49 ?  18  ILE   A CG2  1 
ATOM   450  C CD1  A ILE   A 1 18  ? 10.759 -9.324  4.993   0.86 16.87 ?  18  ILE   A CD1  1 
ATOM   451  C CD1  B ILE   A 1 18  ? 10.477 -8.997  5.401   0.14 12.40 ?  18  ILE   A CD1  1 
ATOM   452  H H    A ILE   A 1 18  ? 11.372 -11.375 9.919   0.86 17.27 ?  18  ILE   A H    1 
ATOM   453  H H    B ILE   A 1 18  ? 11.706 -11.086 10.369  0.14 15.18 ?  18  ILE   A H    1 
ATOM   454  H HA   A ILE   A 1 18  ? 12.431 -9.277  8.586   0.86 17.71 ?  18  ILE   A HA   1 
ATOM   455  H HA   B ILE   A 1 18  ? 12.597 -9.119  8.836   0.14 15.28 ?  18  ILE   A HA   1 
ATOM   456  H HB   A ILE   A 1 18  ? 11.664 -10.806 6.944   0.86 17.74 ?  18  ILE   A HB   1 
ATOM   457  H HB   B ILE   A 1 18  ? 11.775 -10.571 7.163   0.14 14.86 ?  18  ILE   A HB   1 
ATOM   458  H HG12 A ILE   A 1 18  ? 10.271 -8.377  6.708   0.86 18.75 ?  18  ILE   A HG12 1 
ATOM   459  H HG12 B ILE   A 1 18  ? 10.310 -8.157  7.240   0.14 14.90 ?  18  ILE   A HG12 1 
ATOM   460  H HG13 A ILE   A 1 18  ? 11.839 -8.479  6.475   0.86 18.75 ?  18  ILE   A HG13 1 
ATOM   461  H HG13 B ILE   A 1 18  ? 11.813 -8.253  6.737   0.14 14.90 ?  18  ILE   A HG13 1 
ATOM   462  H HG21 A ILE   A 1 18  ? 9.439  -11.229 6.614   0.86 18.96 ?  18  ILE   A HG21 1 
ATOM   463  H HG21 B ILE   A 1 18  ? 9.565  -11.096 6.976   0.14 15.14 ?  18  ILE   A HG21 1 
ATOM   464  H HG22 A ILE   A 1 18  ? 9.767  -11.587 8.126   0.86 18.96 ?  18  ILE   A HG22 1 
ATOM   465  H HG22 B ILE   A 1 18  ? 9.986  -11.460 8.463   0.14 15.14 ?  18  ILE   A HG22 1 
ATOM   466  H HG23 A ILE   A 1 18  ? 9.031  -10.224 7.775   0.86 18.96 ?  18  ILE   A HG23 1 
ATOM   467  H HG23 B ILE   A 1 18  ? 9.182  -10.122 8.172   0.14 15.14 ?  18  ILE   A HG23 1 
ATOM   468  H HD11 A ILE   A 1 18  ? 10.798 -8.520  4.451   0.86 20.39 ?  18  ILE   A HD11 1 
ATOM   469  H HD11 B ILE   A 1 18  ? 10.474 -8.166  4.900   0.14 15.03 ?  18  ILE   A HD11 1 
ATOM   470  H HD12 A ILE   A 1 18  ? 11.448 -9.946  4.710   0.86 20.39 ?  18  ILE   A HD12 1 
ATOM   471  H HD12 B ILE   A 1 18  ? 11.073 -9.636  4.979   0.14 15.03 ?  18  ILE   A HD12 1 
ATOM   472  H HD13 A ILE   A 1 18  ? 9.886  -9.736  4.912   0.86 20.39 ?  18  ILE   A HD13 1 
ATOM   473  H HD13 B ILE   A 1 18  ? 9.579  -9.361  5.444   0.14 15.03 ?  18  ILE   A HD13 1 
ATOM   474  N N    A LYS   A 1 19  ? 10.770 -7.625  9.388   0.86 15.95 ?  19  LYS   A N    1 
ATOM   475  N N    B LYS   A 1 19  ? 10.936 -7.509  9.711   0.14 13.28 ?  19  LYS   A N    1 
ATOM   476  C CA   A LYS   A 1 19  ? 9.967  -6.662  10.137  0.86 17.11 ?  19  LYS   A CA   1 
ATOM   477  C CA   B LYS   A 1 19  ? 10.120 -6.579  10.477  0.14 14.37 ?  19  LYS   A CA   1 
ATOM   478  C C    A LYS   A 1 19  ? 9.761  -5.401  9.303   0.86 16.65 ?  19  LYS   A C    1 
ATOM   479  C C    B LYS   A 1 19  ? 9.916  -5.310  9.661   0.14 14.92 ?  19  LYS   A C    1 
ATOM   480  O O    A LYS   A 1 19  ? 10.645 -4.996  8.542   0.86 16.71 ?  19  LYS   A O    1 
ATOM   481  O O    B LYS   A 1 19  ? 10.848 -4.829  9.010   0.14 14.87 ?  19  LYS   A O    1 
ATOM   482  C CB   A LYS   A 1 19  ? 10.681 -6.305  11.451  0.86 18.33 ?  19  LYS   A CB   1 
ATOM   483  C CB   B LYS   A 1 19  ? 10.799 -6.231  11.806  0.14 14.95 ?  19  LYS   A CB   1 
ATOM   484  C CG   A LYS   A 1 19  ? 9.954  -5.367  12.410  0.86 20.18 ?  19  LYS   A CG   1 
ATOM   485  C CG   B LYS   A 1 19  ? 9.992  -5.316  12.700  0.14 15.68 ?  19  LYS   A CG   1 
ATOM   486  C CD   A LYS   A 1 19  ? 10.868 -5.080  13.606  0.86 21.59 ?  19  LYS   A CD   1 
ATOM   487  C CD   B LYS   A 1 19  ? 10.802 -4.910  13.913  0.14 16.37 ?  19  LYS   A CD   1 
ATOM   488  C CE   A LYS   A 1 19  ? 10.260 -4.133  14.627  0.86 22.33 ?  19  LYS   A CE   1 
ATOM   489  C CE   B LYS   A 1 19  ? 10.004 -4.007  14.828  0.14 16.84 ?  19  LYS   A CE   1 
ATOM   490  N NZ   A LYS   A 1 19  ? 11.166 -3.961  15.803  0.86 22.49 ?  19  LYS   A NZ   1 
ATOM   491  N NZ   B LYS   A 1 19  ? 10.821 -3.550  15.980  0.14 17.06 ?  19  LYS   A NZ   1 
ATOM   492  H H    A LYS   A 1 19  ? 11.332 -7.257  8.841   0.86 19.28 ?  19  LYS   A H    1 
ATOM   493  H H    B LYS   A 1 19  ? 11.452 -7.122  9.141   0.14 16.09 ?  19  LYS   A H    1 
ATOM   494  H HA   A LYS   A 1 19  ? 9.107  -7.059  10.341  0.86 20.68 ?  19  LYS   A HA   1 
ATOM   495  H HA   B LYS   A 1 19  ? 9.256  -6.971  10.663  0.14 17.39 ?  19  LYS   A HA   1 
ATOM   496  H HB2  A LYS   A 1 19  ? 10.847 -7.130  11.935  0.86 22.14 ?  19  LYS   A HB2  1 
ATOM   497  H HB2  B LYS   A 1 19  ? 10.957 -7.052  12.297  0.14 18.09 ?  19  LYS   A HB2  1 
ATOM   498  H HB3  A LYS   A 1 19  ? 11.526 -5.889  11.229  0.86 22.14 ?  19  LYS   A HB3  1 
ATOM   499  H HB3  B LYS   A 1 19  ? 11.644 -5.791  11.621  0.14 18.09 ?  19  LYS   A HB3  1 
ATOM   500  H HG2  A LYS   A 1 19  ? 9.752  -4.529  11.964  0.86 24.36 ?  19  LYS   A HG2  1 
ATOM   501  H HG2  B LYS   A 1 19  ? 9.750  -4.513  12.213  0.14 18.96 ?  19  LYS   A HG2  1 
ATOM   502  H HG3  A LYS   A 1 19  ? 9.140  -5.788  12.733  0.86 24.36 ?  19  LYS   A HG3  1 
ATOM   503  H HG3  B LYS   A 1 19  ? 9.197  -5.782  13.003  0.14 18.96 ?  19  LYS   A HG3  1 
ATOM   504  H HD2  A LYS   A 1 19  ? 11.063 -5.917  14.058  0.86 26.06 ?  19  LYS   A HD2  1 
ATOM   505  H HD2  B LYS   A 1 19  ? 11.054 -5.705  14.409  0.14 19.79 ?  19  LYS   A HD2  1 
ATOM   506  H HD3  A LYS   A 1 19  ? 11.691 -4.682  13.283  0.86 26.06 ?  19  LYS   A HD3  1 
ATOM   507  H HD3  B LYS   A 1 19  ? 11.594 -4.431  13.622  0.14 19.79 ?  19  LYS   A HD3  1 
ATOM   508  H HE2  A LYS   A 1 19  ? 10.124 -3.263  14.218  0.86 26.94 ?  19  LYS   A HE2  1 
ATOM   509  H HE2  B LYS   A 1 19  ? 9.712  -3.227  14.331  0.14 20.36 ?  19  LYS   A HE2  1 
ATOM   510  H HE3  A LYS   A 1 19  ? 9.418  -4.493  14.943  0.86 26.94 ?  19  LYS   A HE3  1 
ATOM   511  H HE3  B LYS   A 1 19  ? 9.238  -4.495  15.169  0.14 20.36 ?  19  LYS   A HE3  1 
ATOM   512  H HZ1  A LYS   A 1 19  ? 10.795 -3.411  16.395  0.86 27.14 ?  19  LYS   A HZ1  1 
ATOM   513  H HZ1  B LYS   A 1 19  ? 10.337 -3.022  16.505  0.14 20.61 ?  19  LYS   A HZ1  1 
ATOM   514  H HZ2  A LYS   A 1 19  ? 11.314 -4.748  16.190  0.86 27.14 ?  19  LYS   A HZ2  1 
ATOM   515  H HZ2  B LYS   A 1 19  ? 11.100 -4.252  16.451  0.14 20.61 ?  19  LYS   A HZ2  1 
ATOM   516  H HZ3  A LYS   A 1 19  ? 11.944 -3.618  15.539  0.86 27.14 ?  19  LYS   A HZ3  1 
ATOM   517  H HZ3  B LYS   A 1 19  ? 11.531 -3.099  15.688  0.14 20.61 ?  19  LYS   A HZ3  1 
ATOM   518  N N    A ASN   A 1 20  ? 8.587  -4.779  9.448   0.86 18.06 ?  20  ASN   A N    1 
ATOM   519  N N    B ASN   A 1 20  ? 8.697  -4.773  9.700   0.14 15.79 ?  20  ASN   A N    1 
ATOM   520  C CA   A ASN   A 1 20  ? 8.351  -3.447  8.897   0.86 19.52 ?  20  ASN   A CA   1 
ATOM   521  C CA   B ASN   A 1 20  ? 8.371  -3.519  9.019   0.14 16.75 ?  20  ASN   A CA   1 
ATOM   522  C C    A ASN   A 1 20  ? 8.981  -2.451  9.860   0.86 20.27 ?  20  ASN   A C    1 
ATOM   523  C C    B ASN   A 1 20  ? 8.866  -2.364  9.881   0.14 16.81 ?  20  ASN   A C    1 
ATOM   524  O O    A ASN   A 1 20  ? 8.472  -2.237  10.965  0.86 20.93 ?  20  ASN   A O    1 
ATOM   525  O O    B ASN   A 1 20  ? 8.184  -1.930  10.812  0.14 17.02 ?  20  ASN   A O    1 
ATOM   526  C CB   A ASN   A 1 20  ? 6.852  -3.205  8.726   0.86 20.51 ?  20  ASN   A CB   1 
ATOM   527  C CB   B ASN   A 1 20  ? 6.870  -3.427  8.772   0.14 17.63 ?  20  ASN   A CB   1 
ATOM   528  C CG   A ASN   A 1 20  ? 6.516  -1.769  8.341   0.86 22.62 ?  20  ASN   A CG   1 
ATOM   529  C CG   B ASN   A 1 20  ? 6.417  -2.023  8.421   0.14 18.57 ?  20  ASN   A CG   1 
ATOM   530  O OD1  A ASN   A 1 20  ? 5.526  -1.219  8.812   0.86 25.29 ?  20  ASN   A OD1  1 
ATOM   531  O OD1  B ASN   A 1 20  ? 5.484  -1.495  9.026   0.14 19.43 ?  20  ASN   A OD1  1 
ATOM   532  N ND2  A ASN   A 1 20  ? 7.323  -1.165  7.482   0.86 23.45 ?  20  ASN   A ND2  1 
ATOM   533  N ND2  B ASN   A 1 20  ? 7.077  -1.409  7.443   0.14 18.72 ?  20  ASN   A ND2  1 
ATOM   534  H H    A ASN   A 1 20  ? 7.917  -5.115  9.867   0.86 21.82 ?  20  ASN   A H    1 
ATOM   535  H H    B ASN   A 1 20  ? 8.029  -5.126  10.112  0.14 19.10 ?  20  ASN   A H    1 
ATOM   536  H HA   A ASN   A 1 20  ? 8.787  -3.371  8.036   0.86 23.57 ?  20  ASN   A HA   1 
ATOM   537  H HA   B ASN   A 1 20  ? 8.827  -3.484  8.165   0.14 20.25 ?  20  ASN   A HA   1 
ATOM   538  H HB2  A ASN   A 1 20  ? 6.525  -3.785  8.026   0.86 24.76 ?  20  ASN   A HB2  1 
ATOM   539  H HB2  B ASN   A 1 20  ? 6.634  -4.007  8.033   0.14 21.31 ?  20  ASN   A HB2  1 
ATOM   540  H HB3  A ASN   A 1 20  ? 6.410  -3.412  9.565   0.86 24.76 ?  20  ASN   A HB3  1 
ATOM   541  H HB3  B ASN   A 1 20  ? 6.396  -3.703  9.572   0.14 21.31 ?  20  ASN   A HB3  1 
ATOM   542  H HD21 A ASN   A 1 20  ? 7.165  -0.351  7.250   0.86 28.29 ?  20  ASN   A HD21 1 
ATOM   543  H HD21 B ASN   A 1 20  ? 6.857  -0.611  7.208   0.14 22.61 ?  20  ASN   A HD21 1 
ATOM   544  H HD22 A ASN   A 1 20  ? 8.007  -1.577  7.170   0.86 28.29 ?  20  ASN   A HD22 1 
ATOM   545  H HD22 B ASN   A 1 20  ? 7.727  -1.809  7.046   0.14 22.61 ?  20  ASN   A HD22 1 
ATOM   546  N N    A ALA   A 1 21  ? 10.112 -1.869  9.465   0.86 20.34 ?  21  ALA   A N    1 
ATOM   547  N N    B ALA   A 1 21  ? 10.054 -1.854  9.564   0.14 16.55 ?  21  ALA   A N    1 
ATOM   548  C CA   A ALA   A 1 21  ? 10.835 -0.991  10.372  0.86 20.21 ?  21  ALA   A CA   1 
ATOM   549  C CA   B ALA   A 1 21  ? 10.670 -0.809  10.373  0.14 16.25 ?  21  ALA   A CA   1 
ATOM   550  C C    A ALA   A 1 21  ? 11.784 -0.107  9.585   0.86 20.03 ?  21  ALA   A C    1 
ATOM   551  C C    B ALA   A 1 21  ? 11.815 -0.179  9.595   0.14 15.71 ?  21  ALA   A C    1 
ATOM   552  O O    A ALA   A 1 21  ? 12.223 -0.466  8.489   0.86 19.97 ?  21  ALA   A O    1 
ATOM   553  O O    B ALA   A 1 21  ? 12.343 -0.764  8.645   0.14 15.20 ?  21  ALA   A O    1 
ATOM   554  C CB   A ALA   A 1 21  ? 11.618 -1.786  11.420  0.86 21.30 ?  21  ALA   A CB   1 
ATOM   555  C CB   B ALA   A 1 21  ? 11.185 -1.367  11.703  0.14 16.54 ?  21  ALA   A CB   1 
ATOM   556  H H    A ALA   A 1 21  ? 10.472 -1.957  8.688   0.86 24.55 ?  21  ALA   A H    1 
ATOM   557  H H    B ALA   A 1 21  ? 10.519 -2.094  8.882   0.14 20.01 ?  21  ALA   A H    1 
ATOM   558  H HA   A ALA   A 1 21  ? 10.199 -0.419  10.836  0.86 24.40 ?  21  ALA   A HA   1 
ATOM   559  H HA   B ALA   A 1 21  ? 10.013 -0.122  10.563  0.14 19.65 ?  21  ALA   A HA   1 
ATOM   560  H HB1  A ALA   A 1 21  ? 12.030 -1.163  12.037  0.86 25.71 ?  21  ALA   A HB1  1 
ATOM   561  H HB1  B ALA   A 1 21  ? 11.622 -0.655  12.195  0.14 19.99 ?  21  ALA   A HB1  1 
ATOM   562  H HB2  A ALA   A 1 21  ? 11.003 -2.366  11.899  0.86 25.71 ?  21  ALA   A HB2  1 
ATOM   563  H HB2  B ALA   A 1 21  ? 10.436 -1.713  12.212  0.14 19.99 ?  21  ALA   A HB2  1 
ATOM   564  H HB3  A ALA   A 1 21  ? 12.294 -2.315  10.974  0.86 25.71 ?  21  ALA   A HB3  1 
ATOM   565  H HB3  B ALA   A 1 21  ? 11.820 -2.078  11.521  0.14 19.99 ?  21  ALA   A HB3  1 
ATOM   566  N N    A ASP   A 1 22  ? 12.077 1.055   10.171  0.86 19.92 ?  22  ASP   A N    1 
ATOM   567  N N    B ASP   A 1 22  ? 12.187 1.030   10.018  0.14 15.65 ?  22  ASP   A N    1 
ATOM   568  C CA   A ASP   A 1 22  ? 13.113 1.964   9.700   0.86 19.54 ?  22  ASP   A CA   1 
ATOM   569  C CA   B ASP   A 1 22  ? 13.358 1.717   9.490   0.14 15.82 ?  22  ASP   A CA   1 
ATOM   570  C C    A ASP   A 1 22  ? 14.441 1.452   10.241  0.86 17.99 ?  22  ASP   A C    1 
ATOM   571  C C    B ASP   A 1 22  ? 14.611 1.091   10.089  0.14 15.44 ?  22  ASP   A C    1 
ATOM   572  O O    A ASP   A 1 22  ? 14.652 1.439   11.457  0.86 18.56 ?  22  ASP   A O    1 
ATOM   573  O O    B ASP   A 1 22  ? 14.709 0.923   11.309  0.14 15.33 ?  22  ASP   A O    1 
ATOM   574  C CB   A ASP   A 1 22  ? 12.820 3.356   10.253  0.86 21.88 ?  22  ASP   A CB   1 
ATOM   575  C CB   B ASP   A 1 22  ? 13.281 3.199   9.864   0.14 16.35 ?  22  ASP   A CB   1 
ATOM   576  C CG   A ASP   A 1 22  ? 13.784 4.409   9.748   0.86 24.02 ?  22  ASP   A CG   1 
ATOM   577  C CG   B ASP   A 1 22  ? 14.405 4.023   9.267   0.14 16.65 ?  22  ASP   A CG   1 
ATOM   578  O OD1  A ASP   A 1 22  ? 14.874 4.060   9.261   0.86 24.00 ?  22  ASP   A OD1  1 
ATOM   579  O OD1  B ASP   A 1 22  ? 15.368 3.436   8.734   0.14 16.48 ?  22  ASP   A OD1  1 
ATOM   580  O OD2  A ASP   A 1 22  ? 13.453 5.607   9.860   0.86 26.00 -1 22  ASP   A OD2  1 
ATOM   581  O OD2  B ASP   A 1 22  ? 14.329 5.268   9.337   0.14 17.04 -1 22  ASP   A OD2  1 
ATOM   582  H H    A ASP   A 1 22  ? 11.657 1.352   10.869  0.86 24.05 ?  22  ASP   A H    1 
ATOM   583  H H    B ASP   A 1 22  ? 11.763 1.479   10.618  0.14 18.93 ?  22  ASP   A H    1 
ATOM   584  H HA   A ASP   A 1 22  ? 13.133 1.983   8.731   0.86 23.59 ?  22  ASP   A HA   1 
ATOM   585  H HA   B ASP   A 1 22  ? 13.393 1.633   8.523   0.14 19.13 ?  22  ASP   A HA   1 
ATOM   586  H HB2  A ASP   A 1 22  ? 11.916 3.609   10.004  0.86 26.41 ?  22  ASP   A HB2  1 
ATOM   587  H HB2  B ASP   A 1 22  ? 12.429 3.557   9.565   0.14 19.77 ?  22  ASP   A HB2  1 
ATOM   588  H HB3  A ASP   A 1 22  ? 12.895 3.326   11.223  0.86 26.41 ?  22  ASP   A HB3  1 
ATOM   589  H HB3  B ASP   A 1 22  ? 13.360 3.284   10.822  0.14 19.77 ?  22  ASP   A HB3  1 
ATOM   590  N N    A ILE   A 1 23  ? 15.333 1.017   9.345   0.86 17.47 ?  23  ILE   A N    1 
ATOM   591  N N    B ILE   A 1 23  ? 15.569 0.736   9.228   0.14 15.40 ?  23  ILE   A N    1 
ATOM   592  C CA   A ILE   A 1 23  ? 16.600 0.422   9.766   0.86 16.50 ?  23  ILE   A CA   1 
ATOM   593  C CA   B ILE   A 1 23  ? 16.795 0.106   9.709   0.14 15.55 ?  23  ILE   A CA   1 
ATOM   594  C C    A ILE   A 1 23  ? 17.404 1.375   10.643  0.86 16.53 ?  23  ILE   A C    1 
ATOM   595  C C    B ILE   A 1 23  ? 17.566 1.054   10.615  0.14 16.18 ?  23  ILE   A C    1 
ATOM   596  O O    A ILE   A 1 23  ? 18.133 0.935   11.540  0.86 16.58 ?  23  ILE   A O    1 
ATOM   597  O O    B ILE   A 1 23  ? 18.285 0.616   11.521  0.14 16.12 ?  23  ILE   A O    1 
ATOM   598  C CB   A ILE   A 1 23  ? 17.391 -0.084  8.539   0.86 15.78 ?  23  ILE   A CB   1 
ATOM   599  C CB   B ILE   A 1 23  ? 17.651 -0.407  8.532   0.14 15.07 ?  23  ILE   A CB   1 
ATOM   600  C CG1  A ILE   A 1 23  ? 18.554 -0.974  8.981   0.86 15.73 ?  23  ILE   A CG1  1 
ATOM   601  C CG1  B ILE   A 1 23  ? 18.740 -1.351  9.048   0.14 14.88 ?  23  ILE   A CG1  1 
ATOM   602  C CG2  A ILE   A 1 23  ? 17.865 1.082   7.667   0.86 16.07 ?  23  ILE   A CG2  1 
ATOM   603  C CG2  B ILE   A 1 23  ? 18.268 0.753   7.757   0.14 14.99 ?  23  ILE   A CG2  1 
ATOM   604  C CD1  A ILE   A 1 23  ? 19.271 -1.665  7.828   0.86 16.23 ?  23  ILE   A CD1  1 
ATOM   605  C CD1  B ILE   A 1 23  ? 19.650 -1.884  7.968   0.14 14.75 ?  23  ILE   A CD1  1 
ATOM   606  H H    A ILE   A 1 23  ? 15.217 1.044   8.500   0.86 21.11 ?  23  ILE   A H    1 
ATOM   607  H H    B ILE   A 1 23  ? 15.532 0.848   8.381   0.14 18.63 ?  23  ILE   A H    1 
ATOM   608  H HA   A ILE   A 1 23  ? 16.402 -0.355  10.310  0.86 19.94 ?  23  ILE   A HA   1 
ATOM   609  H HA   B ILE   A 1 23  ? 16.548 -0.665  10.239  0.14 18.81 ?  23  ILE   A HA   1 
ATOM   610  H HB   A ILE   A 1 23  ? 16.791 -0.627  8.007   0.86 19.08 ?  23  ILE   A HB   1 
ATOM   611  H HB   B ILE   A 1 23  ? 17.078 -0.906  7.930   0.14 18.23 ?  23  ILE   A HB   1 
ATOM   612  H HG12 A ILE   A 1 23  ? 19.206 -0.435  9.452   0.86 19.02 ?  23  ILE   A HG12 1 
ATOM   613  H HG12 B ILE   A 1 23  ? 19.290 -0.876  9.689   0.14 18.00 ?  23  ILE   A HG12 1 
ATOM   614  H HG13 A ILE   A 1 23  ? 18.213 -1.668  9.569   0.86 19.02 ?  23  ILE   A HG13 1 
ATOM   615  H HG13 B ILE   A 1 23  ? 18.316 -2.111  9.477   0.14 18.00 ?  23  ILE   A HG13 1 
ATOM   616  H HG21 A ILE   A 1 23  ? 18.221 0.730   6.836   0.86 19.43 ?  23  ILE   A HG21 1 
ATOM   617  H HG21 B ILE   A 1 23  ? 18.599 0.424   6.904   0.14 18.13 ?  23  ILE   A HG21 1 
ATOM   618  H HG22 A ILE   A 1 23  ? 17.106 1.660   7.478   0.86 19.43 ?  23  ILE   A HG22 1 
ATOM   619  H HG22 B ILE   A 1 23  ? 17.589 1.427   7.606   0.14 18.13 ?  23  ILE   A HG22 1 
ATOM   620  H HG23 A ILE   A 1 23  ? 18.547 1.578   8.139   0.86 19.43 ?  23  ILE   A HG23 1 
ATOM   621  H HG23 B ILE   A 1 23  ? 18.999 1.127   8.272   0.14 18.13 ?  23  ILE   A HG23 1 
ATOM   622  H HD11 A ILE   A 1 23  ? 19.935 -2.270  8.187   0.86 19.62 ?  23  ILE   A HD11 1 
ATOM   623  H HD11 B ILE   A 1 23  ? 20.204 -2.585  8.343   0.14 17.85 ?  23  ILE   A HD11 1 
ATOM   624  H HD12 A ILE   A 1 23  ? 18.619 -2.157  7.304   0.86 19.62 ?  23  ILE   A HD12 1 
ATOM   625  H HD12 B ILE   A 1 23  ? 19.107 -2.238  7.247   0.14 17.85 ?  23  ILE   A HD12 1 
ATOM   626  H HD13 A ILE   A 1 23  ? 19.697 -0.990  7.276   0.86 19.62 ?  23  ILE   A HD13 1 
ATOM   627  H HD13 B ILE   A 1 23  ? 20.207 -1.161  7.640   0.14 17.85 ?  23  ILE   A HD13 1 
ATOM   628  N N    A VAL   A 1 24  ? 17.271 2.684   10.422  0.86 17.76 ?  24  VAL   A N    1 
ATOM   629  N N    B VAL   A 1 24  ? 17.428 2.362   10.393  0.14 17.23 ?  24  VAL   A N    1 
ATOM   630  C CA   A VAL   A 1 24  ? 17.960 3.658   11.268  0.86 18.94 ?  24  VAL   A CA   1 
ATOM   631  C CA   B VAL   A 1 24  ? 18.083 3.338   11.257  0.14 18.24 ?  24  VAL   A CA   1 
ATOM   632  C C    A VAL   A 1 24  ? 17.458 3.560   12.701  0.86 19.44 ?  24  VAL   A C    1 
ATOM   633  C C    B VAL   A 1 24  ? 17.493 3.291   12.660  0.14 19.00 ?  24  VAL   A C    1 
ATOM   634  O O    A VAL   A 1 24  ? 18.246 3.491   13.654  0.86 19.75 ?  24  VAL   A O    1 
ATOM   635  O O    B VAL   A 1 24  ? 18.223 3.334   13.657  0.14 19.09 ?  24  VAL   A O    1 
ATOM   636  C CB   A VAL   A 1 24  ? 17.775 5.078   10.703  0.86 19.92 ?  24  VAL   A CB   1 
ATOM   637  C CB   B VAL   A 1 24  ? 17.980 4.743   10.637  0.14 18.62 ?  24  VAL   A CB   1 
ATOM   638  C CG1  A VAL   A 1 24  ? 18.271 6.129   11.696  0.86 20.98 ?  24  VAL   A CG1  1 
ATOM   639  C CG1  B VAL   A 1 24  ? 18.622 5.775   11.550  0.14 19.06 ?  24  VAL   A CG1  1 
ATOM   640  C CG2  A VAL   A 1 24  ? 18.483 5.210   9.367   0.86 20.95 ?  24  VAL   A CG2  1 
ATOM   641  C CG2  B VAL   A 1 24  ? 18.624 4.766   9.257   0.14 18.67 ?  24  VAL   A CG2  1 
ATOM   642  H H    A VAL   A 1 24  ? 16.799 3.028   9.796   0.86 21.46 ?  24  VAL   A H    1 
ATOM   643  H H    B VAL   A 1 24  ? 16.971 2.705   9.752   0.14 20.83 ?  24  VAL   A H    1 
ATOM   644  H HA   A VAL   A 1 24  ? 18.908 3.463   11.273  0.86 22.87 ?  24  VAL   A HA   1 
ATOM   645  H HA   B VAL   A 1 24  ? 19.023 3.115   11.325  0.14 22.03 ?  24  VAL   A HA   1 
ATOM   646  H HB   A VAL   A 1 24  ? 16.828 5.235   10.552  0.86 24.06 ?  24  VAL   A HB   1 
ATOM   647  H HB   B VAL   A 1 24  ? 17.045 4.977   10.534  0.14 22.49 ?  24  VAL   A HB   1 
ATOM   648  H HG11 A VAL   A 1 24  ? 18.404 6.965   11.225  0.86 25.33 ?  24  VAL   A HG11 1 
ATOM   649  H HG11 B VAL   A 1 24  ? 18.723 6.606   11.061  0.14 23.02 ?  24  VAL   A HG11 1 
ATOM   650  H HG12 A VAL   A 1 24  ? 17.607 6.244   12.393  0.86 25.33 ?  24  VAL   A HG12 1 
ATOM   651  H HG12 B VAL   A 1 24  ? 18.051 5.913   12.322  0.14 23.02 ?  24  VAL   A HG12 1 
ATOM   652  H HG13 A VAL   A 1 24  ? 19.109 5.826   12.078  0.86 25.33 ?  24  VAL   A HG13 1 
ATOM   653  H HG13 B VAL   A 1 24  ? 19.490 5.449   11.832  0.14 23.02 ?  24  VAL   A HG13 1 
ATOM   654  H HG21 A VAL   A 1 24  ? 18.333 6.102   9.015   0.86 25.29 ?  24  VAL   A HG21 1 
ATOM   655  H HG21 B VAL   A 1 24  ? 18.138 5.391   8.699   0.14 22.55 ?  24  VAL   A HG21 1 
ATOM   656  H HG22 A VAL   A 1 24  ? 19.433 5.063   9.498   0.86 25.29 ?  24  VAL   A HG22 1 
ATOM   657  H HG22 B VAL   A 1 24  ? 19.545 5.052   9.346   0.14 22.55 ?  24  VAL   A HG22 1 
ATOM   658  H HG23 A VAL   A 1 24  ? 18.129 4.548   8.752   0.86 25.29 ?  24  VAL   A HG23 1 
ATOM   659  H HG23 B VAL   A 1 24  ? 18.586 3.880   8.864   0.14 22.55 ?  24  VAL   A HG23 1 
ATOM   660  N N    A GLU   A 1 25  ? 16.135 3.564   12.874  0.86 20.70 ?  25  GLU   A N    1 
ATOM   661  N N    B GLU   A 1 25  ? 16.164 3.203   12.762  0.14 19.82 ?  25  GLU   A N    1 
ATOM   662  C CA   A GLU   A 1 25  ? 15.561 3.490   14.214  0.86 22.24 ?  25  GLU   A CA   1 
ATOM   663  C CA   B GLU   A 1 25  ? 15.530 3.137   14.074  0.14 20.83 ?  25  GLU   A CA   1 
ATOM   664  C C    A GLU   A 1 25  ? 15.807 2.124   14.844  0.86 21.36 ?  25  GLU   A C    1 
ATOM   665  C C    B GLU   A 1 25  ? 15.740 1.780   14.734  0.14 20.55 ?  25  GLU   A C    1 
ATOM   666  O O    A GLU   A 1 25  ? 16.078 2.031   16.046  0.86 21.94 ?  25  GLU   A O    1 
ATOM   667  O O    B GLU   A 1 25  ? 15.822 1.699   15.964  0.14 20.67 ?  25  GLU   A O    1 
ATOM   668  C CB   A GLU   A 1 25  ? 14.067 3.824   14.163  0.86 25.00 ?  25  GLU   A CB   1 
ATOM   669  C CB   B GLU   A 1 25  ? 14.041 3.470   13.959  0.14 22.04 ?  25  GLU   A CB   1 
ATOM   670  C CG   A GLU   A 1 25  ? 13.784 5.266   13.756  0.86 28.36 ?  25  GLU   A CG   1 
ATOM   671  C CG   B GLU   A 1 25  ? 13.772 4.911   13.556  0.14 23.31 ?  25  GLU   A CG   1 
ATOM   672  C CD   A GLU   A 1 25  ? 14.526 6.270   14.624  0.86 31.46 ?  25  GLU   A CD   1 
ATOM   673  C CD   B GLU   A 1 25  ? 14.326 5.904   14.554  0.14 24.35 ?  25  GLU   A CD   1 
ATOM   674  O OE1  A GLU   A 1 25  ? 14.586 6.067   15.857  0.86 32.55 ?  25  GLU   A OE1  1 
ATOM   675  O OE1  B GLU   A 1 25  ? 14.287 5.610   15.768  0.14 24.61 ?  25  GLU   A OE1  1 
ATOM   676  O OE2  A GLU   A 1 25  ? 15.071 7.249   14.072  0.86 32.79 -1 25  GLU   A OE2  1 
ATOM   677  O OE2  B GLU   A 1 25  ? 14.806 6.975   14.127  0.14 24.79 -1 25  GLU   A OE2  1 
ATOM   678  H H    A GLU   A 1 25  ? 15.554 3.611   12.241  0.86 24.98 ?  25  GLU   A H    1 
ATOM   679  H H    B GLU   A 1 25  ? 15.620 3.187   12.096  0.14 23.93 ?  25  GLU   A H    1 
ATOM   680  H HA   A GLU   A 1 25  ? 15.989 4.148   14.778  0.86 26.83 ?  25  GLU   A HA   1 
ATOM   681  H HA   B GLU   A 1 25  ? 15.938 3.802   14.646  0.14 25.14 ?  25  GLU   A HA   1 
ATOM   682  H HB2  A GLU   A 1 25  ? 13.630 3.245   13.516  0.86 30.15 ?  25  GLU   A HB2  1 
ATOM   683  H HB2  B GLU   A 1 25  ? 13.639 2.896   13.289  0.14 26.59 ?  25  GLU   A HB2  1 
ATOM   684  H HB3  A GLU   A 1 25  ? 13.676 3.686   15.041  0.86 30.15 ?  25  GLU   A HB3  1 
ATOM   685  H HB3  B GLU   A 1 25  ? 13.618 3.319   14.819  0.14 26.59 ?  25  GLU   A HB3  1 
ATOM   686  H HG2  A GLU   A 1 25  ? 14.078 5.401   12.842  0.86 34.18 ?  25  GLU   A HG2  1 
ATOM   687  H HG2  B GLU   A 1 25  ? 14.181 5.081   12.692  0.14 28.12 ?  25  GLU   A HG2  1 
ATOM   688  H HG3  A GLU   A 1 25  ? 12.826 5.433   13.822  0.86 34.18 ?  25  GLU   A HG3  1 
ATOM   689  H HG3  B GLU   A 1 25  ? 12.816 5.057   13.506  0.14 28.12 ?  25  GLU   A HG3  1 
ATOM   690  N N    A GLU   A 1 26  ? 15.745 1.056   14.045  0.86 20.56 ?  26  GLU   A N    1 
ATOM   691  N N    B GLU   A 1 26  ? 15.828 0.708   13.942  0.14 20.37 ?  26  GLU   A N    1 
ATOM   692  C CA   A GLU   A 1 26  ? 16.067 -0.273  14.561  0.86 20.24 ?  26  GLU   A CA   1 
ATOM   693  C CA   B GLU   A 1 26  ? 16.170 -0.593  14.509  0.14 20.27 ?  26  GLU   A CA   1 
ATOM   694  C C    A GLU   A 1 26  ? 17.499 -0.320  15.081  0.86 19.04 ?  26  GLU   A C    1 
ATOM   695  C C    B GLU   A 1 26  ? 17.602 -0.617  15.027  0.14 20.39 ?  26  GLU   A C    1 
ATOM   696  O O    A GLU   A 1 26  ? 17.759 -0.831  16.177  0.86 19.30 ?  26  GLU   A O    1 
ATOM   697  O O    B GLU   A 1 26  ? 17.897 -1.325  15.996  0.14 20.32 ?  26  GLU   A O    1 
ATOM   698  C CB   A GLU   A 1 26  ? 15.883 -1.322  13.461  0.86 21.87 ?  26  GLU   A CB   1 
ATOM   699  C CB   B GLU   A 1 26  ? 15.967 -1.693  13.466  0.14 20.18 ?  26  GLU   A CB   1 
ATOM   700  C CG   A GLU   A 1 26  ? 14.509 -1.954  13.363  0.86 24.04 ?  26  GLU   A CG   1 
ATOM   701  C CG   B GLU   A 1 26  ? 14.515 -1.920  13.075  0.14 20.05 ?  26  GLU   A CG   1 
ATOM   702  C CD   A GLU   A 1 26  ? 14.113 -2.715  14.619  0.86 24.73 ?  26  GLU   A CD   1 
ATOM   703  C CD   B GLU   A 1 26  ? 13.724 -2.666  14.134  0.14 19.82 ?  26  GLU   A CD   1 
ATOM   704  O OE1  A GLU   A 1 26  ? 14.577 -3.860  14.859  0.86 25.07 ?  26  GLU   A OE1  1 
ATOM   705  O OE1  B GLU   A 1 26  ? 14.114 -3.799  14.490  0.14 20.19 ?  26  GLU   A OE1  1 
ATOM   706  O OE2  A GLU   A 1 26  ? 13.316 -2.148  15.374  0.86 25.88 -1 26  GLU   A OE2  1 
ATOM   707  O OE2  B GLU   A 1 26  ? 12.708 -2.116  14.607  0.14 19.19 -1 26  GLU   A OE2  1 
ATOM   708  H H    A GLU   A 1 26  ? 15.527 1.077   13.215  0.86 24.82 ?  26  GLU   A H    1 
ATOM   709  H H    B GLU   A 1 26  ? 15.690 0.707   13.094  0.14 24.59 ?  26  GLU   A H    1 
ATOM   710  H HA   A GLU   A 1 26  ? 15.470 -0.484  15.294  0.86 24.43 ?  26  GLU   A HA   1 
ATOM   711  H HA   B GLU   A 1 26  ? 15.579 -0.776  15.254  0.14 24.48 ?  26  GLU   A HA   1 
ATOM   712  H HB2  A GLU   A 1 26  ? 16.070 -0.903  12.606  0.86 26.39 ?  26  GLU   A HB2  1 
ATOM   713  H HB2  B GLU   A 1 26  ? 16.455 -1.455  12.662  0.14 24.37 ?  26  GLU   A HB2  1 
ATOM   714  H HB3  A GLU   A 1 26  ? 16.519 -2.036  13.616  0.86 26.39 ?  26  GLU   A HB3  1 
ATOM   715  H HB3  B GLU   A 1 26  ? 16.312 -2.527  13.823  0.14 24.37 ?  26  GLU   A HB3  1 
ATOM   716  H HG2  A GLU   A 1 26  ? 13.853 -1.251  13.213  0.86 28.99 ?  26  GLU   A HG2  1 
ATOM   717  H HG2  B GLU   A 1 26  ? 14.088 -1.061  12.937  0.14 24.21 ?  26  GLU   A HG2  1 
ATOM   718  H HG3  A GLU   A 1 26  ? 14.494 -2.578  12.622  0.86 28.99 ?  26  GLU   A HG3  1 
ATOM   719  H HG3  B GLU   A 1 26  ? 14.486 -2.443  12.261  0.14 24.21 ?  26  GLU   A HG3  1 
ATOM   720  N N    A ALA   A 1 27  ? 18.447 0.204   14.300  0.86 17.73 ?  27  ALA   A N    1 
ATOM   721  N N    B ALA   A 1 27  ? 18.503 0.144   14.400  0.14 20.68 ?  27  ALA   A N    1 
ATOM   722  C CA   A ALA   A 1 27  ? 19.843 0.169   14.722  0.86 17.56 ?  27  ALA   A CA   1 
ATOM   723  C CA   B ALA   A 1 27  ? 19.887 0.180   14.859  0.14 21.20 ?  27  ALA   A CA   1 
ATOM   724  C C    A ALA   A 1 27  ? 20.047 0.952   16.013  0.86 18.82 ?  27  ALA   A C    1 
ATOM   725  C C    B ALA   A 1 27  ? 20.044 1.044   16.106  0.14 22.20 ?  27  ALA   A C    1 
ATOM   726  O O    A ALA   A 1 27  ? 20.721 0.480   16.936  0.86 18.83 ?  27  ALA   A O    1 
ATOM   727  O O    B ALA   A 1 27  ? 20.754 0.660   17.042  0.14 22.07 ?  27  ALA   A O    1 
ATOM   728  C CB   A ALA   A 1 27  ? 20.742 0.711   13.608  0.86 16.88 ?  27  ALA   A CB   1 
ATOM   729  C CB   B ALA   A 1 27  ? 20.802 0.678   13.738  0.14 21.00 ?  27  ALA   A CB   1 
ATOM   730  H H    A ALA   A 1 27  ? 18.305 0.582   13.536  0.86 21.43 ?  27  ALA   A H    1 
ATOM   731  H H    B ALA   A 1 27  ? 18.340 0.635   13.712  0.14 24.96 ?  27  ALA   A H    1 
ATOM   732  H HA   A ALA   A 1 27  ? 20.093 -0.752  14.882  0.86 21.22 ?  27  ALA   A HA   1 
ATOM   733  H HA   B ALA   A 1 27  ? 20.162 -0.721  15.084  0.14 25.59 ?  27  ALA   A HA   1 
ATOM   734  H HB1  A ALA   A 1 27  ? 21.667 0.677   13.904  0.86 20.41 ?  27  ALA   A HB1  1 
ATOM   735  H HB1  B ALA   A 1 27  ? 21.718 0.691   14.060  0.14 25.34 ?  27  ALA   A HB1  1 
ATOM   736  H HB2  A ALA   A 1 27  ? 20.633 0.162   12.813  0.86 20.41 ?  27  ALA   A HB2  1 
ATOM   737  H HB2  B ALA   A 1 27  ? 20.730 0.076   12.979  0.14 25.34 ?  27  ALA   A HB2  1 
ATOM   738  H HB3  A ALA   A 1 27  ? 20.493 1.627   13.411  0.86 20.41 ?  27  ALA   A HB3  1 
ATOM   739  H HB3  B ALA   A 1 27  ? 20.530 1.571   13.478  0.14 25.34 ?  27  ALA   A HB3  1 
ATOM   740  N N    A LYS   A 1 28  ? 19.458 2.147   16.106  0.86 20.59 ?  28  LYS   A N    1 
ATOM   741  N N    B LYS   A 1 28  ? 19.389 2.208   16.141  0.14 23.41 ?  28  LYS   A N    1 
ATOM   742  C CA   A LYS   A 1 28  ? 19.614 2.948   17.316  0.86 23.65 ?  28  LYS   A CA   1 
ATOM   743  C CA   B LYS   A 1 28  ? 19.485 3.071   17.315  0.14 24.78 ?  28  LYS   A CA   1 
ATOM   744  C C    A LYS   A 1 28  ? 19.076 2.225   18.546  0.86 24.80 ?  28  LYS   A C    1 
ATOM   745  C C    B LYS   A 1 28  ? 18.928 2.394   18.559  0.14 25.06 ?  28  LYS   A C    1 
ATOM   746  O O    A LYS   A 1 28  ? 19.642 2.344   19.639  0.86 26.62 ?  28  LYS   A O    1 
ATOM   747  O O    B LYS   A 1 28  ? 19.338 2.721   19.678  0.14 25.35 ?  28  LYS   A O    1 
ATOM   748  C CB   A LYS   A 1 28  ? 18.953 4.316   17.141  0.86 25.79 ?  28  LYS   A CB   1 
ATOM   749  C CB   B LYS   A 1 28  ? 18.759 4.395   17.069  0.14 25.78 ?  28  LYS   A CB   1 
ATOM   750  C CG   A LYS   A 1 28  ? 19.765 5.258   16.266  0.86 27.86 ?  28  LYS   A CG   1 
ATOM   751  C CG   B LYS   A 1 28  ? 19.533 5.363   16.192  0.14 26.72 ?  28  LYS   A CG   1 
ATOM   752  C CD   A LYS   A 1 28  ? 19.249 6.683   16.324  0.86 30.60 ?  28  LYS   A CD   1 
ATOM   753  C CD   B LYS   A 1 28  ? 19.111 6.806   16.430  0.14 27.78 ?  28  LYS   A CD   1 
ATOM   754  C CE   A LYS   A 1 28  ? 17.942 6.823   15.577  0.86 32.30 ?  28  LYS   A CE   1 
ATOM   755  C CE   B LYS   A 1 28  ? 17.748 7.103   15.832  0.14 28.47 ?  28  LYS   A CE   1 
ATOM   756  N NZ   A LYS   A 1 28  ? 17.486 8.240   15.545  0.86 33.44 ?  28  LYS   A NZ   1 
ATOM   757  N NZ   B LYS   A 1 28  ? 17.762 8.384   15.071  0.14 28.91 ?  28  LYS   A NZ   1 
ATOM   758  H H    A LYS   A 1 28  ? 18.979 2.510   15.492  0.86 24.85 ?  28  LYS   A H    1 
ATOM   759  H H    B LYS   A 1 28  ? 18.897 2.514   15.509  0.14 28.24 ?  28  LYS   A H    1 
ATOM   760  H HA   A LYS   A 1 28  ? 20.556 3.098   17.469  0.86 28.52 ?  28  LYS   A HA   1 
ATOM   761  H HA   B LYS   A 1 28  ? 20.417 3.269   17.484  0.14 29.88 ?  28  LYS   A HA   1 
ATOM   762  H HB2  A LYS   A 1 28  ? 18.085 4.200   16.727  0.86 31.10 ?  28  LYS   A HB2  1 
ATOM   763  H HB2  B LYS   A 1 28  ? 17.912 4.212   16.634  0.14 31.08 ?  28  LYS   A HB2  1 
ATOM   764  H HB3  A LYS   A 1 28  ? 18.852 4.733   18.012  0.86 31.10 ?  28  LYS   A HB3  1 
ATOM   765  H HB3  B LYS   A 1 28  ? 18.602 4.828   17.924  0.14 31.08 ?  28  LYS   A HB3  1 
ATOM   766  H HG2  A LYS   A 1 28  ? 20.688 5.259   16.567  0.86 33.58 ?  28  LYS   A HG2  1 
ATOM   767  H HG2  B LYS   A 1 28  ? 20.479 5.289   16.391  0.14 32.22 ?  28  LYS   A HG2  1 
ATOM   768  H HG3  A LYS   A 1 28  ? 19.716 4.958   15.344  0.86 33.58 ?  28  LYS   A HG3  1 
ATOM   769  H HG3  B LYS   A 1 28  ? 19.371 5.149   15.259  0.14 32.22 ?  28  LYS   A HG3  1 
ATOM   770  H HD2  A LYS   A 1 28  ? 19.100 6.933   17.250  0.86 36.86 ?  28  LYS   A HD2  1 
ATOM   771  H HD2  B LYS   A 1 28  ? 19.066 6.973   17.386  0.14 33.48 ?  28  LYS   A HD2  1 
ATOM   772  H HD3  A LYS   A 1 28  ? 19.899 7.278   15.917  0.86 36.86 ?  28  LYS   A HD3  1 
ATOM   773  H HD3  B LYS   A 1 28  ? 19.758 7.400   16.019  0.14 33.48 ?  28  LYS   A HD3  1 
ATOM   774  H HE2  A LYS   A 1 28  ? 18.063 6.521   14.663  0.86 38.91 ?  28  LYS   A HE2  1 
ATOM   775  H HE2  B LYS   A 1 28  ? 17.498 6.390   15.225  0.14 34.31 ?  28  LYS   A HE2  1 
ATOM   776  H HE3  A LYS   A 1 28  ? 17.261 6.294   16.020  0.86 38.91 ?  28  LYS   A HE3  1 
ATOM   777  H HE3  B LYS   A 1 28  ? 17.094 7.181   16.546  0.14 34.31 ?  28  LYS   A HE3  1 
ATOM   778  H HZ1  A LYS   A 1 28  ? 16.718 8.302   15.101  0.86 40.28 ?  28  LYS   A HZ1  1 
ATOM   779  H HZ1  B LYS   A 1 28  ? 16.958 8.543   14.727  0.14 34.84 ?  28  LYS   A HZ1  1 
ATOM   780  H HZ2  A LYS   A 1 28  ? 17.368 8.540   16.374  0.86 40.28 ?  28  LYS   A HZ2  1 
ATOM   781  H HZ2  B LYS   A 1 28  ? 17.985 9.056   15.611  0.14 34.84 ?  28  LYS   A HZ2  1 
ATOM   782  H HZ3  A LYS   A 1 28  ? 18.096 8.746   15.139  0.86 40.28 ?  28  LYS   A HZ3  1 
ATOM   783  H HZ3  B LYS   A 1 28  ? 18.356 8.337   14.409  0.14 34.84 ?  28  LYS   A HZ3  1 
ATOM   784  N N    . LYS   A 1 29  ? 17.995 1.459   18.390  1.00 25.14 ?  29  LYS   A N    1 
ATOM   785  C CA   . LYS   A 1 29  ? 17.417 0.749   19.528  1.00 27.31 ?  29  LYS   A CA   1 
ATOM   786  C C    . LYS   A 1 29  ? 18.244 -0.474  19.916  1.00 26.84 ?  29  LYS   A C    1 
ATOM   787  O O    . LYS   A 1 29  ? 18.542 -0.682  21.099  1.00 28.02 ?  29  LYS   A O    1 
ATOM   788  C CB   . LYS   A 1 29  ? 15.985 0.319   19.192  1.00 30.51 ?  29  LYS   A CB   1 
ATOM   789  C CG   . LYS   A 1 29  ? 15.250 -0.365  20.333  1.00 33.82 ?  29  LYS   A CG   1 
ATOM   790  C CD   . LYS   A 1 29  ? 14.857 0.631   21.409  1.00 37.03 ?  29  LYS   A CD   1 
ATOM   791  C CE   . LYS   A 1 29  ? 14.011 -0.020  22.491  1.00 39.21 ?  29  LYS   A CE   1 
ATOM   792  N NZ   . LYS   A 1 29  ? 13.588 0.962   23.527  1.00 40.53 ?  29  LYS   A NZ   1 
ATOM   793  H H    A LYS   A 1 29  ? 17.583 1.329   17.644  0.86 30.32 ?  29  LYS   A H    1 
ATOM   794  H H    B LYS   A 1 29  ? 17.670 1.223   17.628  0.14 30.32 ?  29  LYS   A H    1 
ATOM   795  H HA   . LYS   A 1 29  ? 17.380 1.345   20.293  1.00 32.92 ?  29  LYS   A HA   1 
ATOM   796  H HB2  . LYS   A 1 29  ? 15.472 1.105   18.948  1.00 36.76 ?  29  LYS   A HB2  1 
ATOM   797  H HB3  . LYS   A 1 29  ? 16.011 -0.301  18.449  1.00 36.76 ?  29  LYS   A HB3  1 
ATOM   798  H HG2  . LYS   A 1 29  ? 14.441 -0.777  19.991  1.00 40.74 ?  29  LYS   A HG2  1 
ATOM   799  H HG3  . LYS   A 1 29  ? 15.821 -1.040  20.736  1.00 40.74 ?  29  LYS   A HG3  1 
ATOM   800  H HD2  . LYS   A 1 29  ? 15.658 0.988   21.824  1.00 44.58 ?  29  LYS   A HD2  1 
ATOM   801  H HD3  . LYS   A 1 29  ? 14.339 1.346   21.008  1.00 44.58 ?  29  LYS   A HD3  1 
ATOM   802  H HE2  . LYS   A 1 29  ? 13.213 -0.399  22.088  1.00 47.20 ?  29  LYS   A HE2  1 
ATOM   803  H HE3  . LYS   A 1 29  ? 14.528 -0.716  22.926  1.00 47.20 ?  29  LYS   A HE3  1 
ATOM   804  H HZ1  . LYS   A 1 29  ? 13.094 0.557   24.147  1.00 48.79 ?  29  LYS   A HZ1  1 
ATOM   805  H HZ2  . LYS   A 1 29  ? 14.303 1.321   23.916  1.00 48.79 ?  29  LYS   A HZ2  1 
ATOM   806  H HZ3  . LYS   A 1 29  ? 13.105 1.610   23.152  1.00 48.79 ?  29  LYS   A HZ3  1 
ATOM   807  N N    . VAL   A 1 30  ? 18.605 -1.300  18.935  1.00 25.38 ?  30  VAL   A N    1 
ATOM   808  C CA   . VAL   A 1 30  ? 19.245 -2.579  19.222  1.00 24.54 ?  30  VAL   A CA   1 
ATOM   809  C C    . VAL   A 1 30  ? 20.752 -2.436  19.432  1.00 23.21 ?  30  VAL   A C    1 
ATOM   810  O O    . VAL   A 1 30  ? 21.342 -3.174  20.228  1.00 23.81 ?  30  VAL   A O    1 
ATOM   811  C CB   . VAL   A 1 30  ? 18.917 -3.570  18.090  1.00 25.17 ?  30  VAL   A CB   1 
ATOM   812  C CG1  . VAL   A 1 30  ? 19.685 -4.872  18.266  1.00 25.65 ?  30  VAL   A CG1  1 
ATOM   813  C CG2  . VAL   A 1 30  ? 17.417 -3.835  18.029  1.00 26.03 ?  30  VAL   A CG2  1 
ATOM   814  H H    . VAL   A 1 30  ? 18.478 -1.149  18.097  1.00 30.61 ?  30  VAL   A H    1 
ATOM   815  H HA   . VAL   A 1 30  ? 18.861 -2.937  20.037  1.00 29.60 ?  30  VAL   A HA   1 
ATOM   816  H HB   . VAL   A 1 30  ? 19.183 -3.182  17.243  1.00 30.36 ?  30  VAL   A HB   1 
ATOM   817  H HG11 . VAL   A 1 30  ? 19.292 -5.547  17.690  1.00 30.93 ?  30  VAL   A HG11 1 
ATOM   818  H HG12 . VAL   A 1 30  ? 20.611 -4.728  18.021  1.00 30.93 ?  30  VAL   A HG12 1 
ATOM   819  H HG13 . VAL   A 1 30  ? 19.621 -5.151  19.191  1.00 30.93 ?  30  VAL   A HG13 1 
ATOM   820  H HG21 . VAL   A 1 30  ? 17.240 -4.492  17.337  1.00 31.39 ?  30  VAL   A HG21 1 
ATOM   821  H HG22 . VAL   A 1 30  ? 17.121 -4.174  18.889  1.00 31.39 ?  30  VAL   A HG22 1 
ATOM   822  H HG23 . VAL   A 1 30  ? 16.958 -3.006  17.824  1.00 31.39 ?  30  VAL   A HG23 1 
ATOM   823  N N    . LYS   A 1 31  ? 21.395 -1.501  18.742  1.00 21.50 ?  31  LYS   A N    1 
ATOM   824  C CA   . LYS   A 1 31  ? 22.851 -1.409  18.689  1.00 22.39 ?  31  LYS   A CA   1 
ATOM   825  C C    . LYS   A 1 31  ? 23.454 -2.767  18.315  1.00 19.92 ?  31  LYS   A C    1 
ATOM   826  O O    . LYS   A 1 31  ? 24.238 -3.337  19.080  1.00 21.28 ?  31  LYS   A O    1 
ATOM   827  C CB   . LYS   A 1 31  ? 23.441 -0.890  19.991  1.00 27.85 ?  31  LYS   A CB   1 
ATOM   828  C CG   . LYS   A 1 31  ? 22.785 0.380   20.508  1.00 34.09 ?  31  LYS   A CG   1 
ATOM   829  C CD   . LYS   A 1 31  ? 23.808 1.473   20.786  1.00 39.04 ?  31  LYS   A CD   1 
ATOM   830  C CE   . LYS   A 1 31  ? 23.226 2.560   21.680  1.00 42.36 ?  31  LYS   A CE   1 
ATOM   831  N NZ   . LYS   A 1 31  ? 21.990 3.171   21.116  1.00 43.99 ?  31  LYS   A NZ   1 
ATOM   832  H H    . LYS   A 1 31  ? 21.001 -0.887  18.291  1.00 25.94 ?  31  LYS   A H    1 
ATOM   833  H HA   . LYS   A 1 31  ? 23.094 -0.783  17.999  1.00 27.02 ?  31  LYS   A HA   1 
ATOM   834  H HB2  . LYS   A 1 31  ? 23.329 -1.580  20.650  1.00 33.56 ?  31  LYS   A HB2  1 
ATOM   835  H HB3  . LYS   A 1 31  ? 24.390 -0.712  19.864  1.00 33.56 ?  31  LYS   A HB3  1 
ATOM   836  H HG2  . LYS   A 1 31  ? 22.162 0.712   19.842  1.00 41.06 ?  31  LYS   A HG2  1 
ATOM   837  H HG3  . LYS   A 1 31  ? 22.317 0.187   21.336  1.00 41.06 ?  31  LYS   A HG3  1 
ATOM   838  H HD2  . LYS   A 1 31  ? 24.577 1.088   21.236  1.00 47.00 ?  31  LYS   A HD2  1 
ATOM   839  H HD3  . LYS   A 1 31  ? 24.079 1.880   19.947  1.00 47.00 ?  31  LYS   A HD3  1 
ATOM   840  H HE2  . LYS   A 1 31  ? 23.002 2.172   22.540  1.00 50.98 ?  31  LYS   A HE2  1 
ATOM   841  H HE3  . LYS   A 1 31  ? 23.884 3.263   21.793  1.00 50.98 ?  31  LYS   A HE3  1 
ATOM   842  H HZ1  . LYS   A 1 31  ? 21.690 3.808   21.660  1.00 52.94 ?  31  LYS   A HZ1  1 
ATOM   843  H HZ2  . LYS   A 1 31  ? 22.163 3.529   20.320  1.00 52.94 ?  31  LYS   A HZ2  1 
ATOM   844  H HZ3  . LYS   A 1 31  ? 21.358 2.551   21.023  1.00 52.94 ?  31  LYS   A HZ3  1 
ATOM   845  N N    . PRO   A 1 32  ? 23.093 -3.306  17.158  1.00 17.84 ?  32  PRO   A N    1 
ATOM   846  C CA   . PRO   A 1 32  ? 23.569 -4.638  16.784  1.00 18.54 ?  32  PRO   A CA   1 
ATOM   847  C C    . PRO   A 1 32  ? 25.069 -4.647  16.567  1.00 18.35 ?  32  PRO   A C    1 
ATOM   848  O O    . PRO   A 1 32  ? 25.704 -3.614  16.349  1.00 18.36 ?  32  PRO   A O    1 
ATOM   849  C CB   . PRO   A 1 32  ? 22.831 -4.910  15.471  1.00 18.87 ?  32  PRO   A CB   1 
ATOM   850  C CG   . PRO   A 1 32  ? 22.617 -3.535  14.889  1.00 17.36 ?  32  PRO   A CG   1 
ATOM   851  C CD   . PRO   A 1 32  ? 22.325 -2.672  16.075  1.00 17.18 ?  32  PRO   A CD   1 
ATOM   852  H HA   . PRO   A 1 32  ? 23.327 -5.302  17.446  1.00 22.39 ?  32  PRO   A HA   1 
ATOM   853  H HB2  . PRO   A 1 32  ? 23.381 -5.454  14.881  1.00 22.80 ?  32  PRO   A HB2  1 
ATOM   854  H HB3  . PRO   A 1 32  ? 21.984 -5.350  15.652  1.00 22.80 ?  32  PRO   A HB3  1 
ATOM   855  H HG2  . PRO   A 1 32  ? 23.418 -3.248  14.435  1.00 20.99 ?  32  PRO   A HG2  1 
ATOM   856  H HG3  . PRO   A 1 32  ? 21.859 -3.559  14.281  1.00 20.99 ?  32  PRO   A HG3  1 
ATOM   857  H HD2  . PRO   A 1 32  ? 22.641 -1.773  15.912  1.00 20.76 ?  32  PRO   A HD2  1 
ATOM   858  H HD3  . PRO   A 1 32  ? 21.378 -2.691  16.278  1.00 20.76 ?  32  PRO   A HD3  1 
ATOM   859  N N    . THR   A 1 33  ? 25.632 -5.854  16.607  1.00 18.40 ?  33  THR   A N    1 
ATOM   860  C CA   . THR   A 1 33  ? 27.042 -6.009  16.278  1.00 18.40 ?  33  THR   A CA   1 
ATOM   861  C C    . THR   A 1 33  ? 27.326 -5.537  14.857  1.00 16.43 ?  33  THR   A C    1 
ATOM   862  O O    . THR   A 1 33  ? 28.352 -4.890  14.607  1.00 16.75 ?  33  THR   A O    1 
ATOM   863  C CB   . THR   A 1 33  ? 27.465 -7.467  16.475  1.00 19.99 ?  33  THR   A CB   1 
ATOM   864  O OG1  . THR   A 1 33  ? 27.173 -7.861  17.819  1.00 21.85 ?  33  THR   A OG1  1 
ATOM   865  C CG2  . THR   A 1 33  ? 28.959 -7.642  16.224  1.00 20.57 ?  33  THR   A CG2  1 
ATOM   866  H H    . THR   A 1 33  ? 25.231 -6.590  16.810  1.00 22.22 ?  33  THR   A H    1 
ATOM   867  H HA   . THR   A 1 33  ? 27.573 -5.470  16.881  1.00 22.23 ?  33  THR   A HA   1 
ATOM   868  H HB   . THR   A 1 33  ? 26.983 -8.044  15.860  1.00 24.13 ?  33  THR   A HB   1 
ATOM   869  H HG1  . THR   A 1 33  ? 27.601 -7.377  18.362  1.00 26.37 ?  33  THR   A HG1  1 
ATOM   870  H HG21 . THR   A 1 33  ? 29.242 -8.530  16.497  1.00 24.83 ?  33  THR   A HG21 1 
ATOM   871  H HG22 . THR   A 1 33  ? 29.153 -7.528  15.281  1.00 24.83 ?  33  THR   A HG22 1 
ATOM   872  H HG23 . THR   A 1 33  ? 29.458 -6.984  16.732  1.00 24.83 ?  33  THR   A HG23 1 
ATOM   873  N N    . VAL   A 1 34  ? 26.427 -5.848  13.918  1.00 14.92 ?  34  VAL   A N    1 
ATOM   874  C CA   . VAL   A 1 34  ? 26.600 -5.505  12.509  1.00 13.63 ?  34  VAL   A CA   1 
ATOM   875  C C    . VAL   A 1 34  ? 25.294 -4.947  11.955  1.00 13.15 ?  34  VAL   A C    1 
ATOM   876  O O    . VAL   A 1 34  ? 24.255 -5.619  12.013  1.00 13.89 ?  34  VAL   A O    1 
ATOM   877  C CB   . VAL   A 1 34  ? 27.041 -6.711  11.658  1.00 14.30 ?  34  VAL   A CB   1 
ATOM   878  C CG1  . VAL   A 1 34  ? 27.191 -6.298  10.198  1.00 14.51 ?  34  VAL   A CG1  1 
ATOM   879  C CG2  . VAL   A 1 34  ? 28.334 -7.324  12.196  1.00 15.74 ?  34  VAL   A CG2  1 
ATOM   880  H H    . VAL   A 1 34  ? 25.695 -6.274  14.079  1.00 18.06 ?  34  VAL   A H    1 
ATOM   881  H HA   . VAL   A 1 34  ? 27.277 -4.815  12.429  1.00 16.51 ?  34  VAL   A HA   1 
ATOM   882  H HB   . VAL   A 1 34  ? 26.350 -7.389  11.702  1.00 17.31 ?  34  VAL   A HB   1 
ATOM   883  H HG11 . VAL   A 1 34  ? 27.693 -6.979  9.727   1.00 17.56 ?  34  VAL   A HG11 1 
ATOM   884  H HG12 . VAL   A 1 34  ? 26.313 -6.198  9.799   1.00 17.56 ?  34  VAL   A HG12 1 
ATOM   885  H HG13 . VAL   A 1 34  ? 27.670 -5.451  10.157  1.00 17.56 ?  34  VAL   A HG13 1 
ATOM   886  H HG21 . VAL   A 1 34  ? 28.596 -8.059  11.617  1.00 19.04 ?  34  VAL   A HG21 1 
ATOM   887  H HG22 . VAL   A 1 34  ? 29.026 -6.646  12.204  1.00 19.04 ?  34  VAL   A HG22 1 
ATOM   888  H HG23 . VAL   A 1 34  ? 28.178 -7.652  13.095  1.00 19.04 ?  34  VAL   A HG23 1 
ATOM   889  N N    . VAL   A 1 35  ? 25.349 -3.732  11.403  1.00 12.62 ?  35  VAL   A N    1 
ATOM   890  C CA   . VAL   A 1 35  ? 24.308 -3.214  10.524  1.00 12.20 ?  35  VAL   A CA   1 
ATOM   891  C C    . VAL   A 1 35  ? 24.853 -3.207  9.104   1.00 11.64 ?  35  VAL   A C    1 
ATOM   892  O O    . VAL   A 1 35  ? 25.997 -2.799  8.876   1.00 12.48 ?  35  VAL   A O    1 
ATOM   893  C CB   . VAL   A 1 35  ? 23.785 -1.821  10.943  1.00 12.91 ?  35  VAL   A CB   1 
ATOM   894  C CG1  . VAL   A 1 35  ? 24.853 -0.729  10.819  1.00 13.65 ?  35  VAL   A CG1  1 
ATOM   895  C CG2  . VAL   A 1 35  ? 22.545 -1.453  10.121  1.00 13.63 ?  35  VAL   A CG2  1 
ATOM   896  H H    . VAL   A 1 35  ? 25.991 -3.174  11.527  1.00 15.29 ?  35  VAL   A H    1 
ATOM   897  H HA   . VAL   A 1 35  ? 23.550 -3.822  10.546  1.00 14.79 ?  35  VAL   A HA   1 
ATOM   898  H HB   . VAL   A 1 35  ? 23.511 -1.856  11.869  1.00 15.64 ?  35  VAL   A HB   1 
ATOM   899  H HG11 . VAL   A 1 35  ? 24.509 0.104   11.188  1.00 16.53 ?  35  VAL   A HG11 1 
ATOM   900  H HG12 . VAL   A 1 35  ? 25.645 -0.998  11.314  1.00 16.53 ?  35  VAL   A HG12 1 
ATOM   901  H HG13 . VAL   A 1 35  ? 25.082 -0.598  9.883   1.00 16.53 ?  35  VAL   A HG13 1 
ATOM   902  H HG21 . VAL   A 1 35  ? 22.193 -0.611  10.438  1.00 16.50 ?  35  VAL   A HG21 1 
ATOM   903  H HG22 . VAL   A 1 35  ? 22.802 -1.372  9.184   1.00 16.50 ?  35  VAL   A HG22 1 
ATOM   904  H HG23 . VAL   A 1 35  ? 21.885 -2.154  10.220  1.00 16.50 ?  35  VAL   A HG23 1 
ATOM   905  N N    . VAL   A 1 36  ? 24.038 -3.663  8.153   1.00 10.98 ?  36  VAL   A N    1 
ATOM   906  C CA   . VAL   A 1 36  ? 24.408 -3.669  6.743   1.00 10.87 ?  36  VAL   A CA   1 
ATOM   907  C C    . VAL   A 1 36  ? 23.952 -2.369  6.090   1.00 11.33 ?  36  VAL   A C    1 
ATOM   908  O O    . VAL   A 1 36  ? 22.795 -1.955  6.240   1.00 11.99 ?  36  VAL   A O    1 
ATOM   909  C CB   . VAL   A 1 36  ? 23.801 -4.884  6.019   1.00 10.95 ?  36  VAL   A CB   1 
ATOM   910  C CG1  . VAL   A 1 36  ? 24.057 -4.798  4.530   1.00 11.38 ?  36  VAL   A CG1  1 
ATOM   911  C CG2  . VAL   A 1 36  ? 24.342 -6.198  6.589   1.00 12.01 ?  36  VAL   A CG2  1 
ATOM   912  H H    . VAL   A 1 36  ? 23.248 -3.990  8.304   1.00 13.32 ?  36  VAL   A H    1 
ATOM   913  H HA   . VAL   A 1 36  ? 25.376 -3.731  6.671   1.00 13.19 ?  36  VAL   A HA   1 
ATOM   914  H HB   . VAL   A 1 36  ? 22.843 -4.878  6.150   1.00 13.29 ?  36  VAL   A HB   1 
ATOM   915  H HG11 . VAL   A 1 36  ? 23.917 -5.673  4.134   1.00 13.80 ?  36  VAL   A HG11 1 
ATOM   916  H HG12 . VAL   A 1 36  ? 23.444 -4.157  4.136   1.00 13.80 ?  36  VAL   A HG12 1 
ATOM   917  H HG13 . VAL   A 1 36  ? 24.974 -4.515  4.381   1.00 13.80 ?  36  VAL   A HG13 1 
ATOM   918  H HG21 . VAL   A 1 36  ? 23.942 -6.943  6.106   1.00 14.56 ?  36  VAL   A HG21 1 
ATOM   919  H HG22 . VAL   A 1 36  ? 25.307 -6.221  6.480   1.00 14.56 ?  36  VAL   A HG22 1 
ATOM   920  H HG23 . VAL   A 1 36  ? 24.114 -6.258  7.529   1.00 14.56 ?  36  VAL   A HG23 1 
ATOM   921  N N    . ASN   A 1 37  ? 24.857 -1.747  5.338   1.00 10.58 ?  37  ASN   A N    1 
ATOM   922  C CA   . ASN   A 1 37  ? 24.521 -0.622  4.481   1.00 10.49 ?  37  ASN   A CA   1 
ATOM   923  C C    . ASN   A 1 37  ? 24.377 -1.080  3.039   1.00 10.48 ?  37  ASN   A C    1 
ATOM   924  O O    . ASN   A 1 37  ? 25.160 -1.907  2.551   1.00 11.16 ?  37  ASN   A O    1 
ATOM   925  C CB   . ASN   A 1 37  ? 25.603 0.454   4.561   1.00 10.77 ?  37  ASN   A CB   1 
ATOM   926  C CG   . ASN   A 1 37  ? 25.273 1.665   3.715   1.00 11.20 ?  37  ASN   A CG   1 
ATOM   927  O OD1  . ASN   A 1 37  ? 24.097 2.017   3.553   1.00 11.80 ?  37  ASN   A OD1  1 
ATOM   928  N ND2  . ASN   A 1 37  ? 26.298 2.326   3.192   1.00 11.61 ?  37  ASN   A ND2  1 
ATOM   929  H H    . ASN   A 1 37  ? 25.693 -1.964  5.314   1.00 12.84 ?  37  ASN   A H    1 
ATOM   930  H HA   . ASN   A 1 37  ? 23.685 -0.234  4.774   1.00 12.74 ?  37  ASN   A HA   1 
ATOM   931  H HB2  . ASN   A 1 37  ? 25.695 0.747   5.485   1.00 13.07 ?  37  ASN   A HB2  1 
ATOM   932  H HB3  . ASN   A 1 37  ? 26.448 0.083   4.251   1.00 13.07 ?  37  ASN   A HB3  1 
ATOM   933  H HD21 . ASN   A 1 37  ? 26.155 3.020   2.701   1.00 14.08 ?  37  ASN   A HD21 1 
ATOM   934  H HD22 . ASN   A 1 37  ? 27.100 2.063   3.328   1.00 14.08 ?  37  ASN   A HD22 1 
ATOM   935  N N    A ALA   A 1 38  ? 23.377 -0.507  2.360   0.86 11.32 ?  38  ALA   A N    1 
ATOM   936  N N    B ALA   A 1 38  ? 23.370 -0.545  2.353   0.14 10.97 ?  38  ALA   A N    1 
ATOM   937  C CA   A ALA   A 1 38  ? 23.168 -0.649  0.919   0.86 11.14 ?  38  ALA   A CA   1 
ATOM   938  C CA   B ALA   A 1 38  ? 23.191 -0.800  0.924   0.14 11.45 ?  38  ALA   A CA   1 
ATOM   939  C C    A ALA   A 1 38  ? 24.087 0.332   0.194   0.86 11.38 ?  38  ALA   A C    1 
ATOM   940  C C    B ALA   A 1 38  ? 23.956 0.284   0.175   0.14 11.58 ?  38  ALA   A C    1 
ATOM   941  O O    A ALA   A 1 38  ? 23.684 1.417   -0.236  0.86 11.44 ?  38  ALA   A O    1 
ATOM   942  O O    B ALA   A 1 38  ? 23.422 1.347   -0.145  0.14 11.41 ?  38  ALA   A O    1 
ATOM   943  C CB   A ALA   A 1 38  ? 21.703 -0.389  0.580   0.86 12.69 ?  38  ALA   A CB   1 
ATOM   944  C CB   B ALA   A 1 38  ? 21.711 -0.807  0.568   0.14 12.00 ?  38  ALA   A CB   1 
ATOM   945  H H    A ALA   A 1 38  ? 22.795 0.003   2.735   0.86 13.73 ?  38  ALA   A H    1 
ATOM   946  H H    B ALA   A 1 38  ? 22.772 -0.027  2.697   0.14 13.31 ?  38  ALA   A H    1 
ATOM   947  H HA   A ALA   A 1 38  ? 23.398 -1.549  0.646   0.86 13.52 ?  38  ALA   A HA   1 
ATOM   948  H HA   B ALA   A 1 38  ? 23.569 -1.667  0.701   0.14 13.89 ?  38  ALA   A HA   1 
ATOM   949  H HB1  A ALA   A 1 38  ? 21.577 -0.494  -0.375  0.86 15.37 ?  38  ALA   A HB1  1 
ATOM   950  H HB1  B ALA   A 1 38  ? 21.624 -0.855  -0.395  0.14 14.54 ?  38  ALA   A HB1  1 
ATOM   951  H HB2  A ALA   A 1 38  ? 21.151 -1.031  1.058   0.86 15.37 ?  38  ALA   A HB2  1 
ATOM   952  H HB2  B ALA   A 1 38  ? 21.285 -1.576  0.981   0.14 14.54 ?  38  ALA   A HB2  1 
ATOM   953  H HB3  A ALA   A 1 38  ? 21.470 0.511   0.850   0.86 15.37 ?  38  ALA   A HB3  1 
ATOM   954  H HB3  B ALA   A 1 38  ? 21.306 0.012   0.893   0.14 14.54 ?  38  ALA   A HB3  1 
ATOM   955  N N    A ALA   A 1 39  ? 25.351 -0.057  0.069   0.86 10.96 ?  39  ALA   A N    1 
ATOM   956  N N    B ALA   A 1 39  ? 25.229 0.017   -0.103  0.14 11.80 ?  39  ALA   A N    1 
ATOM   957  C CA   A ALA   A 1 39  ? 26.406 0.815   -0.418  0.86 10.83 ?  39  ALA   A CA   1 
ATOM   958  C CA   B ALA   A 1 39  ? 26.145 1.021   -0.621  0.14 12.14 ?  39  ALA   A CA   1 
ATOM   959  C C    A ALA   A 1 39  ? 26.520 0.769   -1.939  0.86 10.78 ?  39  ALA   A C    1 
ATOM   960  C C    B ALA   A 1 39  ? 26.428 0.795   -2.102  0.14 11.83 ?  39  ALA   A C    1 
ATOM   961  O O    A ALA   A 1 39  ? 26.002 -0.134  -2.602  0.86 11.30 ?  39  ALA   A O    1 
ATOM   962  O O    B ALA   A 1 39  ? 26.117 -0.253  -2.673  0.14 11.82 ?  39  ALA   A O    1 
ATOM   963  C CB   A ALA   A 1 39  ? 27.734 0.402   0.212   0.86 11.18 ?  39  ALA   A CB   1 
ATOM   964  C CB   B ALA   A 1 39  ? 27.459 1.001   0.168   0.14 12.61 ?  39  ALA   A CB   1 
ATOM   965  H H    A ALA   A 1 39  ? 25.630 -0.853  0.267   0.86 13.31 ?  39  ALA   A H    1 
ATOM   966  H H    B ALA   A 1 39  ? 25.590 -0.760  0.005   0.14 14.31 ?  39  ALA   A H    1 
ATOM   967  H HA   A ALA   A 1 39  ? 26.206 1.727   -0.155  0.86 13.15 ?  39  ALA   A HA   1 
ATOM   968  H HA   B ALA   A 1 39  ? 25.743 1.896   -0.510  0.14 14.71 ?  39  ALA   A HA   1 
ATOM   969  H HB1  A ALA   A 1 39  ? 28.429 0.991   -0.114  0.86 13.56 ?  39  ALA   A HB1  1 
ATOM   970  H HB1  B ALA   A 1 39  ? 28.045 1.689   -0.183  0.14 15.28 ?  39  ALA   A HB1  1 
ATOM   971  H HB2  A ALA   A 1 39  ? 27.658 0.481   1.178   0.86 13.56 ?  39  ALA   A HB2  1 
ATOM   972  H HB2  B ALA   A 1 39  ? 27.269 1.172   1.103   0.14 15.28 ?  39  ALA   A HB2  1 
ATOM   973  H HB3  A ALA   A 1 39  ? 27.926 -0.514  -0.031  0.86 13.56 ?  39  ALA   A HB3  1 
ATOM   974  H HB3  B ALA   A 1 39  ? 27.872 0.129   0.069   0.14 15.28 ?  39  ALA   A HB3  1 
ATOM   975  N N    A ASN   A 1 40  ? 27.205 1.774   -2.488  0.86 11.02 ?  40  ASN   A N    1 
ATOM   976  N N    B ASN   A 1 40  ? 27.032 1.809   -2.720  0.14 11.70 ?  40  ASN   A N    1 
ATOM   977  C CA   A ASN   A 1 40  ? 27.734 1.737   -3.846  0.86 11.26 ?  40  ASN   A CA   1 
ATOM   978  C CA   B ASN   A 1 40  ? 27.540 1.713   -4.078  0.14 11.51 ?  40  ASN   A CA   1 
ATOM   979  C C    A ASN   A 1 40  ? 29.262 1.637   -3.793  0.86 10.79 ?  40  ASN   A C    1 
ATOM   980  C C    B ASN   A 1 40  ? 29.053 1.510   -4.045  0.14 11.31 ?  40  ASN   A C    1 
ATOM   981  O O    A ASN   A 1 40  ? 29.866 1.752   -2.724  0.86 10.89 ?  40  ASN   A O    1 
ATOM   982  O O    B ASN   A 1 40  ? 29.680 1.470   -2.984  0.14 11.32 ?  40  ASN   A O    1 
ATOM   983  C CB   A ASN   A 1 40  ? 27.235 2.926   -4.688  0.86 12.27 ?  40  ASN   A CB   1 
ATOM   984  C CB   B ASN   A 1 40  ? 27.147 2.939   -4.909  0.14 11.46 ?  40  ASN   A CB   1 
ATOM   985  C CG   A ASN   A 1 40  ? 27.611 4.277   -4.104  0.86 13.85 ?  40  ASN   A CG   1 
ATOM   986  C CG   B ASN   A 1 40  ? 27.500 4.247   -4.231  0.14 11.34 ?  40  ASN   A CG   1 
ATOM   987  O OD1  A ASN   A 1 40  ? 28.783 4.532   -3.791  0.86 14.80 ?  40  ASN   A OD1  1 
ATOM   988  O OD1  B ASN   A 1 40  ? 28.676 4.590   -4.091  0.14 11.28 ?  40  ASN   A OD1  1 
ATOM   989  N ND2  A ASN   A 1 40  ? 26.615 5.149   -3.957  0.86 14.62 ?  40  ASN   A ND2  1 
ATOM   990  N ND2  B ASN   A 1 40  ? 26.480 4.992   -3.820  0.14 11.55 ?  40  ASN   A ND2  1 
ATOM   991  H H    A ASN   A 1 40  ? 27.383 2.504   -2.080  0.86 13.37 ?  40  ASN   A H    1 
ATOM   992  H H    B ASN   A 1 40  ? 27.165 2.575   -2.353  0.14 14.19 ?  40  ASN   A H    1 
ATOM   993  H HA   A ASN   A 1 40  ? 27.409 0.927   -4.279  0.86 13.66 ?  40  ASN   A HA   1 
ATOM   994  H HA   B ASN   A 1 40  ? 27.156 0.933   -4.505  0.14 13.97 ?  40  ASN   A HA   1 
ATOM   995  H HB2  A ASN   A 1 40  ? 27.613 2.859   -5.582  0.86 14.87 ?  40  ASN   A HB2  1 
ATOM   996  H HB2  B ASN   A 1 40  ? 27.613 2.909   -5.758  0.14 13.90 ?  40  ASN   A HB2  1 
ATOM   997  H HB3  A ASN   A 1 40  ? 26.264 2.882   -4.746  0.86 14.87 ?  40  ASN   A HB3  1 
ATOM   998  H HB3  B ASN   A 1 40  ? 26.189 2.924   -5.056  0.14 13.90 ?  40  ASN   A HB3  1 
ATOM   999  H HD21 A ASN   A 1 40  ? 26.773 5.929   -3.637  0.86 17.70 ?  40  ASN   A HD21 1 
ATOM   1000 H HD21 B ASN   A 1 40  ? 26.627 5.743   -3.430  0.14 14.00 ?  40  ASN   A HD21 1 
ATOM   1001 H HD22 A ASN   A 1 40  ? 25.813 4.926   -4.176  0.86 17.70 ?  40  ASN   A HD22 1 
ATOM   1002 H HD22 B ASN   A 1 40  ? 25.673 4.721   -3.943  0.14 14.00 ?  40  ASN   A HD22 1 
ATOM   1003 N N    A VAL   A 1 41  ? 29.880 1.384   -4.952  0.86 11.37 ?  41  VAL   A N    1 
ATOM   1004 N N    B VAL   A 1 41  ? 29.646 1.370   -5.232  0.14 11.35 ?  41  VAL   A N    1 
ATOM   1005 C CA   A VAL   A 1 41  ? 31.310 1.071   -4.977  0.86 11.78 ?  41  VAL   A CA   1 
ATOM   1006 C CA   B VAL   A 1 41  ? 31.071 1.054   -5.302  0.14 11.29 ?  41  VAL   A CA   1 
ATOM   1007 C C    A VAL   A 1 41  ? 32.169 2.225   -4.500  0.86 12.19 ?  41  VAL   A C    1 
ATOM   1008 C C    B VAL   A 1 41  ? 31.933 2.202   -4.791  0.14 11.53 ?  41  VAL   A C    1 
ATOM   1009 O O    A VAL   A 1 41  ? 33.317 2.005   -4.093  0.86 12.73 ?  41  VAL   A O    1 
ATOM   1010 O O    B VAL   A 1 41  ? 33.054 1.976   -4.319  0.14 11.60 ?  41  VAL   A O    1 
ATOM   1011 C CB   A VAL   A 1 41  ? 31.806 0.580   -6.357  0.86 12.59 ?  41  VAL   A CB   1 
ATOM   1012 C CB   B VAL   A 1 41  ? 31.476 0.619   -6.722  0.14 11.31 ?  41  VAL   A CB   1 
ATOM   1013 C CG1  A VAL   A 1 41  ? 31.098 -0.697  -6.756  0.86 13.62 ?  41  VAL   A CG1  1 
ATOM   1014 C CG1  B VAL   A 1 41  ? 30.795 -0.686  -7.086  0.14 11.63 ?  41  VAL   A CG1  1 
ATOM   1015 C CG2  A VAL   A 1 41  ? 31.668 1.656   -7.432  0.86 13.43 ?  41  VAL   A CG2  1 
ATOM   1016 C CG2  B VAL   A 1 41  ? 31.153 1.710   -7.734  0.14 11.16 ?  41  VAL   A CG2  1 
ATOM   1017 H H    A VAL   A 1 41  ? 29.501 1.374   -5.725  0.86 13.80 ?  41  VAL   A H    1 
ATOM   1018 H H    B VAL   A 1 41  ? 29.245 1.437   -5.990  0.14 13.76 ?  41  VAL   A H    1 
ATOM   1019 H HA   A VAL   A 1 41  ? 31.465 0.340   -4.358  0.86 14.28 ?  41  VAL   A HA   1 
ATOM   1020 H HA   B VAL   A 1 41  ? 31.232 0.299   -4.718  0.14 13.70 ?  41  VAL   A HA   1 
ATOM   1021 H HB   A VAL   A 1 41  ? 32.752 0.366   -6.285  0.86 15.26 ?  41  VAL   A HB   1 
ATOM   1022 H HB   B VAL   A 1 41  ? 32.433 0.465   -6.739  0.14 13.72 ?  41  VAL   A HB   1 
ATOM   1023 H HG11 A VAL   A 1 41  ? 31.438 -0.996  -7.613  0.86 16.49 ?  41  VAL   A HG11 1 
ATOM   1024 H HG11 B VAL   A 1 41  ? 31.025 -0.917  -7.998  0.14 14.10 ?  41  VAL   A HG11 1 
ATOM   1025 H HG12 A VAL   A 1 41  ? 31.263 -1.374  -6.079  0.86 16.49 ?  41  VAL   A HG12 1 
ATOM   1026 H HG12 B VAL   A 1 41  ? 31.102 -1.380  -6.480  0.14 14.10 ?  41  VAL   A HG12 1 
ATOM   1027 H HG13 A VAL   A 1 41  ? 30.146 -0.521  -6.820  0.86 16.49 ?  41  VAL   A HG13 1 
ATOM   1028 H HG13 B VAL   A 1 41  ? 29.836 -0.577  -7.002  0.14 14.10 ?  41  VAL   A HG13 1 
ATOM   1029 H HG21 A VAL   A 1 41  ? 31.899 1.274   -8.297  0.86 16.26 ?  41  VAL   A HG21 1 
ATOM   1030 H HG21 B VAL   A 1 41  ? 31.475 1.432   -8.605  0.14 13.54 ?  41  VAL   A HG21 1 
ATOM   1031 H HG22 A VAL   A 1 41  ? 30.756 1.977   -7.446  0.86 16.26 ?  41  VAL   A HG22 1 
ATOM   1032 H HG22 B VAL   A 1 41  ? 30.194 1.844   -7.763  0.14 13.54 ?  41  VAL   A HG22 1 
ATOM   1033 H HG23 A VAL   A 1 41  ? 32.275 2.388   -7.228  0.86 16.26 ?  41  VAL   A HG23 1 
ATOM   1034 H HG23 B VAL   A 1 41  ? 31.596 2.529   -7.464  0.14 13.54 ?  41  VAL   A HG23 1 
ATOM   1035 N N    A TYR   A 1 42  ? 31.650 3.455   -4.557  0.86 11.79 ?  42  TYR   A N    1 
ATOM   1036 N N    B TYR   A 1 42  ? 31.448 3.440   -4.877  0.14 11.82 ?  42  TYR   A N    1 
ATOM   1037 C CA   A TYR   A 1 42  ? 32.379 4.652   -4.147  0.86 11.97 ?  42  TYR   A CA   1 
ATOM   1038 C CA   B TYR   A 1 42  ? 32.224 4.602   -4.460  0.14 12.24 ?  42  TYR   A CA   1 
ATOM   1039 C C    A TYR   A 1 42  ? 32.122 5.020   -2.695  0.86 11.05 ?  42  TYR   A C    1 
ATOM   1040 C C    B TYR   A 1 42  ? 31.955 5.012   -3.018  0.14 12.11 ?  42  TYR   A C    1 
ATOM   1041 O O    A TYR   A 1 42  ? 32.698 5.994   -2.202  0.86 11.87 ?  42  TYR   A O    1 
ATOM   1042 O O    B TYR   A 1 42  ? 32.498 6.025   -2.567  0.14 11.97 ?  42  TYR   A O    1 
ATOM   1043 C CB   A TYR   A 1 42  ? 32.030 5.845   -5.064  0.86 12.94 ?  42  TYR   A CB   1 
ATOM   1044 C CB   B TYR   A 1 42  ? 31.945 5.791   -5.385  0.14 12.92 ?  42  TYR   A CB   1 
ATOM   1045 C CG   A TYR   A 1 42  ? 32.219 5.533   -6.538  0.86 14.17 ?  42  TYR   A CG   1 
ATOM   1046 C CG   B TYR   A 1 42  ? 32.119 5.471   -6.849  0.14 13.60 ?  42  TYR   A CG   1 
ATOM   1047 C CD1  A TYR   A 1 42  ? 33.486 5.335   -7.074  0.86 14.90 ?  42  TYR   A CD1  1 
ATOM   1048 C CD1  B TYR   A 1 42  ? 33.383 5.319   -7.402  0.14 13.78 ?  42  TYR   A CD1  1 
ATOM   1049 C CD2  A TYR   A 1 42  ? 31.130 5.414   -7.389  0.86 15.62 ?  42  TYR   A CD2  1 
ATOM   1050 C CD2  B TYR   A 1 42  ? 31.018 5.322   -7.679  0.14 14.04 ?  42  TYR   A CD2  1 
ATOM   1051 C CE1  A TYR   A 1 42  ? 33.660 5.030   -8.417  0.86 15.75 ?  42  TYR   A CE1  1 
ATOM   1052 C CE1  B TYR   A 1 42  ? 33.543 5.024   -8.743  0.14 14.18 ?  42  TYR   A CE1  1 
ATOM   1053 C CE2  A TYR   A 1 42  ? 31.295 5.119   -8.734  0.86 16.63 ?  42  TYR   A CE2  1 
ATOM   1054 C CE2  B TYR   A 1 42  ? 31.168 5.029   -9.019  0.14 14.54 ?  42  TYR   A CE2  1 
ATOM   1055 C CZ   A TYR   A 1 42  ? 32.564 4.928   -9.242  0.86 16.64 ?  42  TYR   A CZ   1 
ATOM   1056 C CZ   B TYR   A 1 42  ? 32.432 4.881   -9.547  0.14 14.61 ?  42  TYR   A CZ   1 
ATOM   1057 O OH   A TYR   A 1 42  ? 32.720 4.628   -10.576 0.86 18.46 ?  42  TYR   A OH   1 
ATOM   1058 O OH   B TYR   A 1 42  ? 32.583 4.588   -10.883 0.14 15.12 ?  42  TYR   A OH   1 
ATOM   1059 H H    A TYR   A 1 42  ? 30.858 3.622   -4.845  0.86 14.30 ?  42  TYR   A H    1 
ATOM   1060 H H    B TYR   A 1 42  ? 30.663 3.633   -5.173  0.14 14.33 ?  42  TYR   A H    1 
ATOM   1061 H HA   A TYR   A 1 42  ? 33.330 4.485   -4.244  0.86 14.51 ?  42  TYR   A HA   1 
ATOM   1062 H HA   B TYR   A 1 42  ? 33.167 4.388   -4.536  0.14 14.84 ?  42  TYR   A HA   1 
ATOM   1063 H HB2  A TYR   A 1 42  ? 31.100 6.091   -4.928  0.86 15.68 ?  42  TYR   A HB2  1 
ATOM   1064 H HB2  B TYR   A 1 42  ? 31.031 6.085   -5.250  0.14 15.65 ?  42  TYR   A HB2  1 
ATOM   1065 H HB3  A TYR   A 1 42  ? 32.604 6.598   -4.844  0.86 15.68 ?  42  TYR   A HB3  1 
ATOM   1066 H HB3  B TYR   A 1 42  ? 32.559 6.510   -5.163  0.14 15.65 ?  42  TYR   A HB3  1 
ATOM   1067 H HD1  A TYR   A 1 42  ? 34.229 5.399   -6.522  0.86 18.02 ?  42  TYR   A HD1  1 
ATOM   1068 H HD1  B TYR   A 1 42  ? 34.134 5.413   -6.860  0.14 16.69 ?  42  TYR   A HD1  1 
ATOM   1069 H HD2  A TYR   A 1 42  ? 30.272 5.547   -7.052  0.86 18.89 ?  42  TYR   A HD2  1 
ATOM   1070 H HD2  B TYR   A 1 42  ? 30.163 5.422   -7.324  0.14 16.99 ?  42  TYR   A HD2  1 
ATOM   1071 H HE1  A TYR   A 1 42  ? 34.513 4.900   -8.764  0.86 19.05 ?  42  TYR   A HE1  1 
ATOM   1072 H HE1  B TYR   A 1 42  ? 34.395 4.924   -9.100  0.14 17.16 ?  42  TYR   A HE1  1 
ATOM   1073 H HE2  A TYR   A 1 42  ? 30.551 5.049   -9.292  0.86 20.10 ?  42  TYR   A HE2  1 
ATOM   1074 H HE2  B TYR   A 1 42  ? 30.419 4.934   -9.561  0.14 17.59 ?  42  TYR   A HE2  1 
ATOM   1075 H HH   A TYR   A 1 42  ? 33.534 4.527   -10.760 0.86 22.30 ?  42  TYR   A HH   1 
ATOM   1076 H HH   B TYR   A 1 42  ? 33.399 4.524   -11.069 0.14 18.29 ?  42  TYR   A HH   1 
ATOM   1077 N N    A LEU   A 1 43  ? 31.276 4.258   -2.008  0.86 11.34 ?  43  LEU   A N    1 
ATOM   1078 N N    B LEU   A 1 43  ? 31.132 4.256   -2.294  0.14 12.33 ?  43  LEU   A N    1 
ATOM   1079 C CA   A LEU   A 1 43  ? 30.820 4.594   -0.659  0.86 10.75 ?  43  LEU   A CA   1 
ATOM   1080 C CA   B LEU   A 1 43  ? 30.758 4.583   -0.917  0.14 12.53 ?  43  LEU   A CA   1 
ATOM   1081 C C    A LEU   A 1 43  ? 30.342 6.042   -0.560  0.86 10.93 ?  43  LEU   A C    1 
ATOM   1082 C C    B LEU   A 1 43  ? 30.270 6.025   -0.796  0.14 13.21 ?  43  LEU   A C    1 
ATOM   1083 O O    A LEU   A 1 43  ? 30.589 6.735   0.427   0.86 12.15 ?  43  LEU   A O    1 
ATOM   1084 O O    B LEU   A 1 43  ? 30.608 6.742   0.148   0.14 13.06 ?  43  LEU   A O    1 
ATOM   1085 C CB   A LEU   A 1 43  ? 31.870 4.271   0.407   0.86 11.64 ?  43  LEU   A CB   1 
ATOM   1086 C CB   B LEU   A 1 43  ? 31.890 4.292   0.072   0.14 12.50 ?  43  LEU   A CB   1 
ATOM   1087 C CG   A LEU   A 1 43  ? 32.374 2.820   0.494   0.86 11.82 ?  43  LEU   A CG   1 
ATOM   1088 C CG   B LEU   A 1 43  ? 32.354 2.838   0.206   0.14 12.48 ?  43  LEU   A CG   1 
ATOM   1089 C CD1  A LEU   A 1 43  ? 33.413 2.716   1.603   0.86 12.46 ?  43  LEU   A CD1  1 
ATOM   1090 C CD1  B LEU   A 1 43  ? 33.443 2.733   1.265   0.14 12.40 ?  43  LEU   A CD1  1 
ATOM   1091 C CD2  A LEU   A 1 43  ? 31.247 1.821   0.715   0.86 12.47 ?  43  LEU   A CD2  1 
ATOM   1092 C CD2  B LEU   A 1 43  ? 31.190 1.912   0.536   0.14 12.60 ?  43  LEU   A CD2  1 
ATOM   1093 H H    A LEU   A 1 43  ? 30.937 3.515   -2.307  0.86 13.76 ?  43  LEU   A H    1 
ATOM   1094 H H    B LEU   A 1 43  ? 30.768 3.536   -2.584  0.14 14.95 ?  43  LEU   A H    1 
ATOM   1095 H HA   A LEU   A 1 43  ? 30.050 4.031   -0.460  0.86 13.05 ?  43  LEU   A HA   1 
ATOM   1096 H HA   B LEU   A 1 43  ? 30.016 4.011   -0.672  0.14 15.18 ?  43  LEU   A HA   1 
ATOM   1097 H HB2  A LEU   A 1 43  ? 32.643 4.832   0.249   0.86 14.12 ?  43  LEU   A HB2  1 
ATOM   1098 H HB2  B LEU   A 1 43  ? 32.662 4.813   -0.190  0.14 15.15 ?  43  LEU   A HB2  1 
ATOM   1099 H HB3  A LEU   A 1 43  ? 31.491 4.487   1.276   0.86 14.12 ?  43  LEU   A HB3  1 
ATOM   1100 H HB3  B LEU   A 1 43  ? 31.597 4.575   0.954   0.14 15.15 ?  43  LEU   A HB3  1 
ATOM   1101 H HG   A LEU   A 1 43  ? 32.812 2.593   -0.340  0.86 14.33 ?  43  LEU   A HG   1 
ATOM   1102 H HG   B LEU   A 1 43  ? 32.734 2.550   -0.638  0.14 15.12 ?  43  LEU   A HG   1 
ATOM   1103 H HD11 A LEU   A 1 43  ? 33.728 1.800   1.655   0.86 15.11 ?  43  LEU   A HD11 1 
ATOM   1104 H HD11 B LEU   A 1 43  ? 33.728 1.809   1.338   0.14 15.02 ?  43  LEU   A HD11 1 
ATOM   1105 H HD12 A LEU   A 1 43  ? 34.151 3.311   1.401   0.86 15.11 ?  43  LEU   A HD12 1 
ATOM   1106 H HD12 B LEU   A 1 43  ? 34.192 3.292   1.005   0.14 15.02 ?  43  LEU   A HD12 1 
ATOM   1107 H HD13 A LEU   A 1 43  ? 33.002 2.972   2.445   0.86 15.11 ?  43  LEU   A HD13 1 
ATOM   1108 H HD13 B LEU   A 1 43  ? 33.085 3.036   2.116   0.14 15.02 ?  43  LEU   A HD13 1 
ATOM   1109 H HD21 A LEU   A 1 43  ? 31.630 0.937   0.826   0.86 15.12 ?  43  LEU   A HD21 1 
ATOM   1110 H HD21 B LEU   A 1 43  ? 31.537 1.032   0.751   0.14 15.27 ?  43  LEU   A HD21 1 
ATOM   1111 H HD22 A LEU   A 1 43  ? 30.756 2.073   1.512   0.86 15.12 ?  43  LEU   A HD22 1 
ATOM   1112 H HD22 B LEU   A 1 43  ? 30.707 2.272   1.296   0.14 15.27 ?  43  LEU   A HD22 1 
ATOM   1113 H HD23 A LEU   A 1 43  ? 30.661 1.835   -0.056  0.86 15.12 ?  43  LEU   A HD23 1 
ATOM   1114 H HD23 B LEU   A 1 43  ? 30.602 1.857   -0.234  0.14 15.27 ?  43  LEU   A HD23 1 
ATOM   1115 N N    A LYS   A 1 44  ? 29.620 6.488   -1.587  0.86 11.26 ?  44  LYS   A N    1 
ATOM   1116 N N    B LYS   A 1 44  ? 29.466 6.456   -1.766  0.14 14.06 ?  44  LYS   A N    1 
ATOM   1117 C CA   A LYS   A 1 44  ? 28.978 7.801   -1.589  0.86 11.71 ?  44  LYS   A CA   1 
ATOM   1118 C CA   B LYS   A 1 44  ? 28.813 7.763   -1.728  0.14 14.93 ?  44  LYS   A CA   1 
ATOM   1119 C C    A LYS   A 1 44  ? 27.550 7.605   -1.089  0.86 10.97 ?  44  LYS   A C    1 
ATOM   1120 C C    B LYS   A 1 44  ? 27.402 7.561   -1.190  0.14 14.00 ?  44  LYS   A C    1 
ATOM   1121 O O    A LYS   A 1 44  ? 26.690 7.087   -1.804  0.86 12.28 ?  44  LYS   A O    1 
ATOM   1122 O O    B LYS   A 1 44  ? 26.502 7.126   -1.913  0.14 14.01 ?  44  LYS   A O    1 
ATOM   1123 C CB   A LYS   A 1 44  ? 29.007 8.415   -2.983  0.86 14.21 ?  44  LYS   A CB   1 
ATOM   1124 C CB   B LYS   A 1 44  ? 28.808 8.410   -3.110  0.14 17.04 ?  44  LYS   A CB   1 
ATOM   1125 C CG   A LYS   A 1 44  ? 30.368 8.923   -3.419  0.86 18.10 ?  44  LYS   A CG   1 
ATOM   1126 C CG   B LYS   A 1 44  ? 30.174 8.900   -3.573  0.14 19.16 ?  44  LYS   A CG   1 
ATOM   1127 C CD   A LYS   A 1 44  ? 31.031 9.813   -2.369  0.86 23.87 ?  44  LYS   A CD   1 
ATOM   1128 C CD   B LYS   A 1 44  ? 30.851 9.765   -2.516  0.14 21.28 ?  44  LYS   A CD   1 
ATOM   1129 C CE   A LYS   A 1 44  ? 32.345 10.379  -2.881  0.86 27.30 ?  44  LYS   A CE   1 
ATOM   1130 C CE   B LYS   A 1 44  ? 32.198 10.272  -2.988  0.14 22.76 ?  44  LYS   A CE   1 
ATOM   1131 N NZ   A LYS   A 1 44  ? 33.232 10.851  -1.781  0.86 29.12 ?  44  LYS   A NZ   1 
ATOM   1132 N NZ   B LYS   A 1 44  ? 32.947 10.960  -1.900  0.14 23.58 ?  44  LYS   A NZ   1 
ATOM   1133 H H    A LYS   A 1 44  ? 29.482 6.035   -2.305  0.86 13.66 ?  44  LYS   A H    1 
ATOM   1134 H H    B LYS   A 1 44  ? 29.285 6.003   -2.473  0.14 17.02 ?  44  LYS   A H    1 
ATOM   1135 H HA   A LYS   A 1 44  ? 29.431 8.384   -0.959  0.86 14.20 ?  44  LYS   A HA   1 
ATOM   1136 H HA   B LYS   A 1 44  ? 29.274 8.339   -1.101  0.14 18.06 ?  44  LYS   A HA   1 
ATOM   1137 H HB2  A LYS   A 1 44  ? 28.722 7.743   -3.622  0.86 17.21 ?  44  LYS   A HB2  1 
ATOM   1138 H HB2  B LYS   A 1 44  ? 28.493 7.760   -3.759  0.14 20.60 ?  44  LYS   A HB2  1 
ATOM   1139 H HB3  A LYS   A 1 44  ? 28.389 9.164   -3.001  0.86 17.21 ?  44  LYS   A HB3  1 
ATOM   1140 H HB3  B LYS   A 1 44  ? 28.210 9.174   -3.097  0.14 20.60 ?  44  LYS   A HB3  1 
ATOM   1141 H HG2  A LYS   A 1 44  ? 30.952 8.170   -3.588  0.86 21.87 ?  44  LYS   A HG2  1 
ATOM   1142 H HG2  B LYS   A 1 44  ? 30.744 8.136   -3.752  0.14 23.14 ?  44  LYS   A HG2  1 
ATOM   1143 H HG3  A LYS   A 1 44  ? 30.264 9.451   -4.231  0.86 21.87 ?  44  LYS   A HG3  1 
ATOM   1144 H HG3  B LYS   A 1 44  ? 30.067 9.434   -4.378  0.14 23.14 ?  44  LYS   A HG3  1 
ATOM   1145 H HD2  A LYS   A 1 44  ? 30.434 10.544  -2.146  0.86 28.80 ?  44  LYS   A HD2  1 
ATOM   1146 H HD2  B LYS   A 1 44  ? 30.280 10.524  -2.310  0.14 25.69 ?  44  LYS   A HD2  1 
ATOM   1147 H HD3  A LYS   A 1 44  ? 31.225 9.282   -1.579  0.86 28.80 ?  44  LYS   A HD3  1 
ATOM   1148 H HD3  B LYS   A 1 44  ? 31.009 9.238   -1.717  0.14 25.69 ?  44  LYS   A HD3  1 
ATOM   1149 H HE2  A LYS   A 1 44  ? 32.818 9.687   -3.370  0.86 32.90 ?  44  LYS   A HE2  1 
ATOM   1150 H HE2  B LYS   A 1 44  ? 32.730 9.519   -3.292  0.14 27.46 ?  44  LYS   A HE2  1 
ATOM   1151 H HE3  A LYS   A 1 44  ? 32.158 11.130  -3.463  0.86 32.90 ?  44  LYS   A HE3  1 
ATOM   1152 H HE3  B LYS   A 1 44  ? 32.064 10.902  -3.710  0.14 27.46 ?  44  LYS   A HE3  1 
ATOM   1153 H HZ1  A LYS   A 1 44  ? 33.987 11.177  -2.119  0.86 35.10 ?  44  LYS   A HZ1  1 
ATOM   1154 H HZ1  B LYS   A 1 44  ? 33.733 11.245  -2.206  0.14 28.45 ?  44  LYS   A HZ1  1 
ATOM   1155 H HZ2  A LYS   A 1 44  ? 32.822 11.494  -1.318  0.86 35.10 ?  44  LYS   A HZ2  1 
ATOM   1156 H HZ2  B LYS   A 1 44  ? 32.482 11.658  -1.603  0.14 28.45 ?  44  LYS   A HZ2  1 
ATOM   1157 H HZ3  A LYS   A 1 44  ? 33.423 10.179  -1.233  0.86 35.10 ?  44  LYS   A HZ3  1 
ATOM   1158 H HZ3  B LYS   A 1 44  ? 33.088 10.399  -1.223  0.14 28.45 ?  44  LYS   A HZ3  1 
ATOM   1159 N N    A HIS   A 1 45  ? 27.305 8.003   0.154   0.86 11.09 ?  45  HIS   A N    1 
ATOM   1160 N N    B HIS   A 1 45  ? 27.215 7.884   0.087   0.14 13.29 ?  45  HIS   A N    1 
ATOM   1161 C CA   A HIS   A 1 45  ? 26.070 7.646   0.849   0.86 11.27 ?  45  HIS   A CA   1 
ATOM   1162 C CA   B HIS   A 1 45  ? 25.944 7.662   0.772   0.14 12.61 ?  45  HIS   A CA   1 
ATOM   1163 C C    A HIS   A 1 45  ? 25.036 8.766   0.699   0.86 11.94 ?  45  HIS   A C    1 
ATOM   1164 C C    B HIS   A 1 45  ? 25.042 8.854   0.485   0.14 12.42 ?  45  HIS   A C    1 
ATOM   1165 O O    A HIS   A 1 45  ? 24.687 9.469   1.646   0.86 12.93 ?  45  HIS   A O    1 
ATOM   1166 O O    B HIS   A 1 45  ? 25.060 9.864   1.189   0.14 12.62 ?  45  HIS   A O    1 
ATOM   1167 C CB   A HIS   A 1 45  ? 26.366 7.360   2.309   0.86 10.86 ?  45  HIS   A CB   1 
ATOM   1168 C CB   B HIS   A 1 45  ? 26.176 7.472   2.264   0.14 11.93 ?  45  HIS   A CB   1 
ATOM   1169 C CG   A HIS   A 1 45  ? 27.486 6.394   2.519   0.86 10.87 ?  45  HIS   A CG   1 
ATOM   1170 C CG   B HIS   A 1 45  ? 27.324 6.567   2.579   0.14 10.99 ?  45  HIS   A CG   1 
ATOM   1171 N ND1  A HIS   A 1 45  ? 27.473 5.106   2.018   0.86 11.46 ?  45  HIS   A ND1  1 
ATOM   1172 N ND1  B HIS   A 1 45  ? 27.408 5.278   2.097   0.14 10.87 ?  45  HIS   A ND1  1 
ATOM   1173 C CD2  A HIS   A 1 45  ? 28.660 6.536   3.181   0.86 11.13 ?  45  HIS   A CD2  1 
ATOM   1174 C CD2  B HIS   A 1 45  ? 28.440 6.767   3.318   0.14 10.42 ?  45  HIS   A CD2  1 
ATOM   1175 C CE1  A HIS   A 1 45  ? 28.593 4.500   2.371   0.86 11.14 ?  45  HIS   A CE1  1 
ATOM   1176 C CE1  B HIS   A 1 45  ? 28.526 4.722   2.530   0.14 10.14 ?  45  HIS   A CE1  1 
ATOM   1177 N NE2  A HIS   A 1 45  ? 29.329 5.342   3.077   0.86 11.15 ?  45  HIS   A NE2  1 
ATOM   1178 N NE2  B HIS   A 1 45  ? 29.170 5.604   3.274   0.14 10.07 ?  45  HIS   A NE2  1 
ATOM   1179 H H    A HIS   A 1 45  ? 27.844 8.487   0.627   0.86 13.45 ?  45  HIS   A H    1 
ATOM   1180 H H    B HIS   A 1 45  ? 27.819 8.244   0.586   0.14 16.10 ?  45  HIS   A H    1 
ATOM   1181 H HA   A HIS   A 1 45  ? 25.704 6.844   0.451   0.86 13.67 ?  45  HIS   A HA   1 
ATOM   1182 H HA   B HIS   A 1 45  ? 25.524 6.864   0.422   0.14 15.28 ?  45  HIS   A HA   1 
ATOM   1183 H HB2  A HIS   A 1 45  ? 26.597 8.188   2.755   0.86 13.18 ?  45  HIS   A HB2  1 
ATOM   1184 H HB2  B HIS   A 1 45  ? 26.359 8.333   2.669   0.14 14.46 ?  45  HIS   A HB2  1 
ATOM   1185 H HB3  A HIS   A 1 45  ? 25.568 6.981   2.720   0.86 13.18 ?  45  HIS   A HB3  1 
ATOM   1186 H HB3  B HIS   A 1 45  ? 25.378 7.084   2.659   0.14 14.46 ?  45  HIS   A HB3  1 
ATOM   1187 H HD2  A HIS   A 1 45  ? 28.959 7.300   3.625   0.86 13.50 ?  45  HIS   A HD2  1 
ATOM   1188 H HD2  B HIS   A 1 45  ? 28.670 7.545   3.773   0.14 12.66 ?  45  HIS   A HD2  1 
ATOM   1189 H HE1  A HIS   A 1 45  ? 28.825 3.622   2.167   0.86 13.52 ?  45  HIS   A HE1  1 
ATOM   1190 H HE1  B HIS   A 1 45  ? 28.811 3.856   2.344   0.14 12.31 ?  45  HIS   A HE1  1 
ATOM   1191 H HE2  A HIS   A 1 45  ? 30.106 5.170   3.413   0.86 13.53 ?  45  HIS   A HE2  1 
ATOM   1192 H HE2  B HIS   A 1 45  ? 29.924 5.472   3.665   0.14 12.23 ?  45  HIS   A HE2  1 
ATOM   1193 N N    A GLY   A 1 46  ? 24.528 8.905   -0.522  0.86 13.17 ?  46  GLY   A N    1 
ATOM   1194 N N    B GLY   A 1 46  ? 24.246 8.733   -0.574  0.14 12.14 ?  46  GLY   A N    1 
ATOM   1195 C CA   A GLY   A 1 46  ? 23.717 10.064  -0.855  0.86 14.08 ?  46  GLY   A CA   1 
ATOM   1196 C CA   B GLY   A 1 46  ? 23.383 9.815   -0.999  0.14 12.02 ?  46  GLY   A CA   1 
ATOM   1197 C C    A GLY   A 1 46  ? 22.229 9.944   -0.597  0.86 13.87 ?  46  GLY   A C    1 
ATOM   1198 C C    B GLY   A 1 46  ? 21.957 9.704   -0.498  0.14 11.88 ?  46  GLY   A C    1 
ATOM   1199 O O    A GLY   A 1 46  ? 21.564 10.942  -0.298  0.86 15.34 ?  46  GLY   A O    1 
ATOM   1200 O O    B GLY   A 1 46  ? 21.384 10.696  -0.037  0.14 12.17 ?  46  GLY   A O    1 
ATOM   1201 H H    A GLY   A 1 46  ? 24.623 8.341   -1.162  0.86 15.96 ?  46  GLY   A H    1 
ATOM   1202 H H    B GLY   A 1 46  ? 24.199 8.030   -1.068  0.14 14.72 ?  46  GLY   A H    1 
ATOM   1203 H HA2  A GLY   A 1 46  ? 24.035 10.826  -0.348  0.86 17.05 ?  46  GLY   A HA2  1 
ATOM   1204 H HA2  B GLY   A 1 46  ? 23.742 10.656  -0.676  0.14 14.58 ?  46  GLY   A HA2  1 
ATOM   1205 H HA3  A GLY   A 1 46  ? 23.823 10.261  -1.795  0.86 17.05 ?  46  GLY   A HA3  1 
ATOM   1206 H HA3  B GLY   A 1 46  ? 23.373 9.847   -1.969  0.14 14.58 ?  46  GLY   A HA3  1 
ATOM   1207 N N    A GLY   A 1 47  ? 21.692 8.737   -0.737  0.86 13.75 ?  47  GLY   A N    1 
ATOM   1208 N N    B GLY   A 1 47  ? 21.371 8.513   -0.570  0.14 11.69 ?  47  GLY   A N    1 
ATOM   1209 C CA   A GLY   A 1 47  ? 20.256 8.537   -0.703  0.86 14.24 ?  47  GLY   A CA   1 
ATOM   1210 C CA   B GLY   A 1 47  ? 19.975 8.368   -0.229  0.14 11.23 ?  47  GLY   A CA   1 
ATOM   1211 C C    A GLY   A 1 47  ? 19.933 7.099   -0.356  0.86 13.09 ?  47  GLY   A C    1 
ATOM   1212 C C    B GLY   A 1 47  ? 19.621 6.939   0.116   0.14 10.41 ?  47  GLY   A C    1 
ATOM   1213 O O    A GLY   A 1 47  ? 20.818 6.271   -0.123  0.86 13.34 ?  47  GLY   A O    1 
ATOM   1214 O O    B GLY   A 1 47  ? 20.486 6.063   0.191   0.14 10.13 ?  47  GLY   A O    1 
ATOM   1215 H H    A GLY   A 1 47  ? 22.136 8.013   -0.840  0.86 16.64 ?  47  GLY   A H    1 
ATOM   1216 H H    B GLY   A 1 47  ? 21.764 7.778   -0.800  0.14 14.18 ?  47  GLY   A H    1 
ATOM   1217 H HA2  A GLY   A 1 47  ? 19.844 9.120   -0.040  0.86 17.23 ?  47  GLY   A HA2  1 
ATOM   1218 H HA2  B GLY   A 1 47  ? 19.769 8.928   0.536   0.14 13.62 ?  47  GLY   A HA2  1 
ATOM   1219 H HA3  A GLY   A 1 47  ? 19.871 8.745   -1.574  0.86 17.23 ?  47  GLY   A HA3  1 
ATOM   1220 H HA3  B GLY   A 1 47  ? 19.425 8.651   -0.976  0.14 13.62 ?  47  GLY   A HA3  1 
ATOM   1221 N N    A GLY   A 1 48  ? 18.637 6.801   -0.350  0.86 13.08 ?  48  GLY   A N    1 
ATOM   1222 N N    B GLY   A 1 48  ? 18.326 6.714   0.326   0.14 10.32 ?  48  GLY   A N    1 
ATOM   1223 C CA   A GLY   A 1 48  ? 18.202 5.475   0.031   0.86 12.91 ?  48  GLY   A CA   1 
ATOM   1224 C CA   B GLY   A 1 48  ? 17.877 5.394   0.731   0.14 9.79  ?  48  GLY   A CA   1 
ATOM   1225 C C    A GLY   A 1 48  ? 18.622 5.147   1.452   0.86 11.94 ?  48  GLY   A C    1 
ATOM   1226 C C    B GLY   A 1 48  ? 18.486 5.009   2.064   0.14 9.86  ?  48  GLY   A C    1 
ATOM   1227 O O    A GLY   A 1 48  ? 18.774 6.027   2.311   0.86 12.64 ?  48  GLY   A O    1 
ATOM   1228 O O    B GLY   A 1 48  ? 18.631 5.834   2.975   0.14 9.58  ?  48  GLY   A O    1 
ATOM   1229 H H    A GLY   A 1 48  ? 17.999 7.340   -0.555  0.86 15.85 ?  48  GLY   A H    1 
ATOM   1230 H H    B GLY   A 1 48  ? 17.696 7.300   0.244   0.14 12.54 ?  48  GLY   A H    1 
ATOM   1231 H HA2  A GLY   A 1 48  ? 17.240 5.404   -0.035  0.86 15.64 ?  48  GLY   A HA2  1 
ATOM   1232 H HA2  B GLY   A 1 48  ? 16.906 5.383   0.800   0.14 11.90 ?  48  GLY   A HA2  1 
ATOM   1233 H HA3  A GLY   A 1 48  ? 18.603 4.813   -0.564  0.86 15.64 ?  48  GLY   A HA3  1 
ATOM   1234 H HA3  B GLY   A 1 48  ? 18.144 4.739   0.065   0.14 11.90 ?  48  GLY   A HA3  1 
ATOM   1235 N N    A VAL   A 1 49  ? 18.826 3.849   1.700   0.86 12.29 ?  49  VAL   A N    1 
ATOM   1236 N N    B VAL   A 1 49  ? 18.864 3.734   2.179   0.14 9.70  ?  49  VAL   A N    1 
ATOM   1237 C CA   A VAL   A 1 49  ? 19.289 3.393   3.009   0.86 12.16 ?  49  VAL   A CA   1 
ATOM   1238 C CA   B VAL   A 1 49  ? 19.502 3.250   3.401   0.14 9.94  ?  49  VAL   A CA   1 
ATOM   1239 C C    A VAL   A 1 49  ? 20.610 4.065   3.388   0.86 11.29 ?  49  VAL   A C    1 
ATOM   1240 C C    B VAL   A 1 49  ? 20.810 3.991   3.654   0.14 9.66  ?  49  VAL   A C    1 
ATOM   1241 O O    A VAL   A 1 49  ? 20.800 4.484   4.537   0.86 11.64 ?  49  VAL   A O    1 
ATOM   1242 O O    B VAL   A 1 49  ? 21.105 4.388   4.789   0.14 9.48  ?  49  VAL   A O    1 
ATOM   1243 C CB   A VAL   A 1 49  ? 19.401 1.856   3.029   0.86 13.30 ?  49  VAL   A CB   1 
ATOM   1244 C CB   B VAL   A 1 49  ? 19.706 1.724   3.323   0.14 10.31 ?  49  VAL   A CB   1 
ATOM   1245 C CG1  A VAL   A 1 49  ? 20.157 1.379   4.277   0.86 14.06 ?  49  VAL   A CG1  1 
ATOM   1246 C CG1  B VAL   A 1 49  ? 20.701 1.264   4.372   0.14 9.94  ?  49  VAL   A CG1  1 
ATOM   1247 C CG2  A VAL   A 1 49  ? 18.021 1.222   2.955   0.86 15.27 ?  49  VAL   A CG2  1 
ATOM   1248 C CG2  B VAL   A 1 49  ? 18.383 0.998   3.496   0.14 10.76 ?  49  VAL   A CG2  1 
ATOM   1249 H H    A VAL   A 1 49  ? 18.700 3.213   1.132   0.86 14.90 ?  49  VAL   A H    1 
ATOM   1250 H H    B VAL   A 1 49  ? 18.766 3.140   1.568   0.14 11.79 ?  49  VAL   A H    1 
ATOM   1251 H HA   A VAL   A 1 49  ? 18.636 3.640   3.677   0.86 14.74 ?  49  VAL   A HA   1 
ATOM   1252 H HA   B VAL   A 1 49  ? 18.918 3.431   4.151   0.14 12.07 ?  49  VAL   A HA   1 
ATOM   1253 H HB   A VAL   A 1 49  ? 19.907 1.560   2.255   0.86 16.11 ?  49  VAL   A HB   1 
ATOM   1254 H HB   B VAL   A 1 49  ? 20.060 1.495   2.448   0.14 12.52 ?  49  VAL   A HB   1 
ATOM   1255 H HG11 A VAL   A 1 49  ? 19.981 0.434   4.411   0.86 17.02 ?  49  VAL   A HG11 1 
ATOM   1256 H HG11 B VAL   A 1 49  ? 20.633 0.302   4.472   0.14 12.07 ?  49  VAL   A HG11 1 
ATOM   1257 H HG12 A VAL   A 1 49  ? 21.106 1.524   4.153   0.86 17.02 ?  49  VAL   A HG12 1 
ATOM   1258 H HG12 B VAL   A 1 49  ? 21.597 1.497   4.084   0.14 12.07 ?  49  VAL   A HG12 1 
ATOM   1259 H HG13 A VAL   A 1 49  ? 19.840 1.882   5.046   0.86 17.02 ?  49  VAL   A HG13 1 
ATOM   1260 H HG13 B VAL   A 1 49  ? 20.495 1.697   5.213   0.14 12.07 ?  49  VAL   A HG13 1 
ATOM   1261 H HG21 A VAL   A 1 49  ? 18.115 0.256   2.972   0.86 18.47 ?  49  VAL   A HG21 1 
ATOM   1262 H HG21 B VAL   A 1 49  ? 18.450 0.382   4.240   0.14 13.06 ?  49  VAL   A HG21 1 
ATOM   1263 H HG22 A VAL   A 1 49  ? 17.501 1.518   3.717   0.86 18.47 ?  49  VAL   A HG22 1 
ATOM   1264 H HG22 B VAL   A 1 49  ? 17.691 1.652   3.672   0.14 13.06 ?  49  VAL   A HG22 1 
ATOM   1265 H HG23 A VAL   A 1 49  ? 17.596 1.500   2.131   0.86 18.47 ?  49  VAL   A HG23 1 
ATOM   1266 H HG23 B VAL   A 1 49  ? 18.179 0.514   2.680   0.14 13.06 ?  49  VAL   A HG23 1 
ATOM   1267 N N    A ALA   A 1 50  ? 21.561 4.130   2.447   0.86 11.18 ?  50  ALA   A N    1 
ATOM   1268 N N    B ALA   A 1 50  ? 21.610 4.191   2.604   0.14 9.70  ?  50  ALA   A N    1 
ATOM   1269 C CA   A ALA   A 1 50  ? 22.879 4.682   2.760   0.86 11.43 ?  50  ALA   A CA   1 
ATOM   1270 C CA   B ALA   A 1 50  ? 22.921 4.812   2.776   0.14 9.51  ?  50  ALA   A CA   1 
ATOM   1271 C C    A ALA   A 1 50  ? 22.786 6.141   3.188   0.86 10.84 ?  50  ALA   A C    1 
ATOM   1272 C C    B ALA   A 1 50  ? 22.788 6.248   3.266   0.14 9.34  ?  50  ALA   A C    1 
ATOM   1273 O O    A ALA   A 1 50  ? 23.420 6.552   4.167   0.86 11.66 ?  50  ALA   A O    1 
ATOM   1274 O O    B ALA   A 1 50  ? 23.428 6.644   4.247   0.14 9.23  ?  50  ALA   A O    1 
ATOM   1275 C CB   A ALA   A 1 50  ? 23.802 4.545   1.551   0.86 11.42 ?  50  ALA   A CB   1 
ATOM   1276 C CB   B ALA   A 1 50  ? 23.700 4.755   1.460   0.14 9.29  ?  50  ALA   A CB   1 
ATOM   1277 H H    A ALA   A 1 50  ? 21.466 3.874   1.632   0.86 13.57 ?  50  ALA   A H    1 
ATOM   1278 H H    B ALA   A 1 50  ? 21.414 3.987   1.791   0.14 11.79 ?  50  ALA   A H    1 
ATOM   1279 H HA   A ALA   A 1 50  ? 23.266 4.183   3.496   0.86 13.86 ?  50  ALA   A HA   1 
ATOM   1280 H HA   B ALA   A 1 50  ? 23.419 4.316   3.440   0.14 11.56 ?  50  ALA   A HA   1 
ATOM   1281 H HB1  A ALA   A 1 50  ? 24.670 4.915   1.774   0.86 13.85 ?  50  ALA   A HB1  1 
ATOM   1282 H HB1  B ALA   A 1 50  ? 24.577 5.148   1.595   0.14 11.30 ?  50  ALA   A HB1  1 
ATOM   1283 H HB2  A ALA   A 1 50  ? 23.887 3.608   1.324   0.86 13.85 ?  50  ALA   A HB2  1 
ATOM   1284 H HB2  B ALA   A 1 50  ? 23.794 3.827   1.189   0.14 11.30 ?  50  ALA   A HB2  1 
ATOM   1285 H HB3  A ALA   A 1 50  ? 23.416 5.034   0.806   0.86 13.85 ?  50  ALA   A HB3  1 
ATOM   1286 H HB3  B ALA   A 1 50  ? 23.215 5.249   0.781   0.14 11.30 ?  50  ALA   A HB3  1 
ATOM   1287 N N    A GLY   A 1 51  ? 22.017 6.941   2.452   0.86 11.47 ?  51  GLY   A N    1 
ATOM   1288 N N    B GLY   A 1 51  ? 21.958 7.045   2.591   0.14 10.09 ?  51  GLY   A N    1 
ATOM   1289 C CA   A GLY   A 1 51  ? 21.860 8.334   2.832   0.86 11.82 ?  51  GLY   A CA   1 
ATOM   1290 C CA   B GLY   A 1 51  ? 21.789 8.428   3.003   0.14 10.39 ?  51  GLY   A CA   1 
ATOM   1291 C C    A GLY   A 1 51  ? 21.257 8.482   4.213   0.86 11.48 ?  51  GLY   A C    1 
ATOM   1292 C C    B GLY   A 1 51  ? 21.203 8.547   4.396   0.14 10.89 ?  51  GLY   A C    1 
ATOM   1293 O O    A GLY   A 1 51  ? 21.651 9.367   4.977   0.86 12.53 ?  51  GLY   A O    1 
ATOM   1294 O O    B GLY   A 1 51  ? 21.599 9.420   5.174   0.14 11.27 ?  51  GLY   A O    1 
ATOM   1295 H H    A GLY   A 1 51  ? 21.588 6.704   1.747   0.86 13.91 ?  51  GLY   A H    1 
ATOM   1296 H H    B GLY   A 1 51  ? 21.490 6.808   1.909   0.14 12.26 ?  51  GLY   A H    1 
ATOM   1297 H HA2  A GLY   A 1 51  ? 22.724 8.774   2.824   0.86 14.33 ?  51  GLY   A HA2  1 
ATOM   1298 H HA2  B GLY   A 1 51  ? 22.651 8.874   2.993   0.14 12.62 ?  51  GLY   A HA2  1 
ATOM   1299 H HA3  A GLY   A 1 51  ? 21.280 8.782   2.195   0.86 14.33 ?  51  GLY   A HA3  1 
ATOM   1300 H HA3  B GLY   A 1 51  ? 21.204 8.881   2.373   0.14 12.62 ?  51  GLY   A HA3  1 
ATOM   1301 N N    A ALA   A 1 52  ? 20.288 7.620   4.547   0.86 11.72 ?  52  ALA   A N    1 
ATOM   1302 N N    B ALA   A 1 52  ? 20.257 7.667   4.734   0.14 11.19 ?  52  ALA   A N    1 
ATOM   1303 C CA   A ALA   A 1 52  ? 19.651 7.672   5.859   0.86 12.46 ?  52  ALA   A CA   1 
ATOM   1304 C CA   B ALA   A 1 52  ? 19.642 7.720   6.057   0.14 11.53 ?  52  ALA   A CA   1 
ATOM   1305 C C    A ALA   A 1 52  ? 20.610 7.257   6.974   0.86 11.84 ?  52  ALA   A C    1 
ATOM   1306 C C    B ALA   A 1 52  ? 20.609 7.251   7.140   0.14 11.20 ?  52  ALA   A C    1 
ATOM   1307 O O    A ALA   A 1 52  ? 20.687 7.919   8.015   0.86 13.02 ?  52  ALA   A O    1 
ATOM   1308 O O    B ALA   A 1 52  ? 20.669 7.844   8.224   0.14 11.31 ?  52  ALA   A O    1 
ATOM   1309 C CB   A ALA   A 1 52  ? 18.393 6.801   5.858   0.86 14.12 ?  52  ALA   A CB   1 
ATOM   1310 C CB   B ALA   A 1 52  ? 18.357 6.892   6.073   0.14 12.20 ?  52  ALA   A CB   1 
ATOM   1311 H H    A ALA   A 1 52  ? 20.003 6.987   4.038   0.86 14.22 ?  52  ALA   A H    1 
ATOM   1312 H H    B ALA   A 1 52  ? 19.962 7.041   4.221   0.14 13.58 ?  52  ALA   A H    1 
ATOM   1313 H HA   A ALA   A 1 52  ? 19.385 8.583   6.033   0.86 15.10 ?  52  ALA   A HA   1 
ATOM   1314 H HA   B ALA   A 1 52  ? 19.405 8.639   6.249   0.14 13.98 ?  52  ALA   A HA   1 
ATOM   1315 H HB1  A ALA   A 1 52  ? 17.977 6.853   6.736   0.86 17.10 ?  52  ALA   A HB1  1 
ATOM   1316 H HB1  B ALA   A 1 52  ? 17.962 6.946   6.958   0.14 14.78 ?  52  ALA   A HB1  1 
ATOM   1317 H HB2  A ALA   A 1 52  ? 17.780 7.141   5.185   0.86 17.10 ?  52  ALA   A HB2  1 
ATOM   1318 H HB2  B ALA   A 1 52  ? 17.741 7.254   5.415   0.14 14.78 ?  52  ALA   A HB2  1 
ATOM   1319 H HB3  A ALA   A 1 52  ? 18.635 5.888   5.659   0.86 17.10 ?  52  ALA   A HB3  1 
ATOM   1320 H HB3  B ALA   A 1 52  ? 18.569 5.972   5.858   0.14 14.78 ?  52  ALA   A HB3  1 
ATOM   1321 N N    A LEU   A 1 53  ? 21.338 6.153   6.790   0.86 11.85 ?  53  LEU   A N    1 
ATOM   1322 N N    B LEU   A 1 53  ? 21.371 6.187   6.873   0.14 11.21 ?  53  LEU   A N    1 
ATOM   1323 C CA   A LEU   A 1 53  ? 22.301 5.736   7.808   0.86 11.92 ?  53  LEU   A CA   1 
ATOM   1324 C CA   B LEU   A 1 53  ? 22.374 5.745   7.838   0.14 11.46 ?  53  LEU   A CA   1 
ATOM   1325 C C    A LEU   A 1 53  ? 23.360 6.809   8.009   0.86 10.81 ?  53  LEU   A C    1 
ATOM   1326 C C    B LEU   A 1 53  ? 23.431 6.821   8.050   0.14 11.41 ?  53  LEU   A C    1 
ATOM   1327 O O    A LEU   A 1 53  ? 23.693 7.168   9.144   0.86 12.20 ?  53  LEU   A O    1 
ATOM   1328 O O    B LEU   A 1 53  ? 23.786 7.145   9.189   0.14 11.62 ?  53  LEU   A O    1 
ATOM   1329 C CB   A LEU   A 1 53  ? 22.950 4.397   7.432   0.86 12.27 ?  53  LEU   A CB   1 
ATOM   1330 C CB   B LEU   A 1 53  ? 23.026 4.436   7.379   0.14 11.66 ?  53  LEU   A CB   1 
ATOM   1331 C CG   A LEU   A 1 53  ? 22.074 3.135   7.465   0.86 12.90 ?  53  LEU   A CG   1 
ATOM   1332 C CG   B LEU   A 1 53  ? 22.265 3.114   7.538   0.14 11.87 ?  53  LEU   A CG   1 
ATOM   1333 C CD1  A LEU   A 1 53  ? 22.797 1.955   6.829   0.86 13.51 ?  53  LEU   A CD1  1 
ATOM   1334 C CD1  B LEU   A 1 53  ? 23.131 1.946   7.075   0.14 11.94 ?  53  LEU   A CD1  1 
ATOM   1335 C CD2  A LEU   A 1 53  ? 21.656 2.788   8.879   0.86 15.10 ?  53  LEU   A CD2  1 
ATOM   1336 C CD2  B LEU   A 1 53  ? 21.809 2.896   8.971   0.14 12.44 ?  53  LEU   A CD2  1 
ATOM   1337 H H    A LEU   A 1 53  ? 21.292 5.631   6.100   0.86 14.37 ?  53  LEU   A H    1 
ATOM   1338 H H    B LEU   A 1 53  ? 21.325 5.713   6.156   0.14 13.59 ?  53  LEU   A H    1 
ATOM   1339 H HA   A LEU   A 1 53  ? 21.834 5.613   8.648   0.86 14.46 ?  53  LEU   A HA   1 
ATOM   1340 H HA   B LEU   A 1 53  ? 21.940 5.586   8.689   0.14 13.90 ?  53  LEU   A HA   1 
ATOM   1341 H HB2  A LEU   A 1 53  ? 23.302 4.477   6.531   0.86 14.87 ?  53  LEU   A HB2  1 
ATOM   1342 H HB2  B LEU   A 1 53  ? 23.228 4.524   6.436   0.14 14.14 ?  53  LEU   A HB2  1 
ATOM   1343 H HB3  A LEU   A 1 53  ? 23.688 4.242   8.045   0.86 14.87 ?  53  LEU   A HB3  1 
ATOM   1344 H HB3  B LEU   A 1 53  ? 23.856 4.335   7.870   0.14 14.14 ?  53  LEU   A HB3  1 
ATOM   1345 H HG   A LEU   A 1 53  ? 21.272 3.303   6.944   0.86 15.63 ?  53  LEU   A HG   1 
ATOM   1346 H HG   B LEU   A 1 53  ? 21.478 3.134   6.974   0.14 14.39 ?  53  LEU   A HG   1 
ATOM   1347 H HD11 A LEU   A 1 53  ? 22.217 1.179   6.863   0.86 16.36 ?  53  LEU   A HD11 1 
ATOM   1348 H HD11 B LEU   A 1 53  ? 22.633 1.119   7.183   0.14 14.48 ?  53  LEU   A HD11 1 
ATOM   1349 H HD12 A LEU   A 1 53  ? 23.007 2.172   5.907   0.86 16.36 ?  53  LEU   A HD12 1 
ATOM   1350 H HD12 B LEU   A 1 53  ? 23.361 2.072   6.141   0.14 14.48 ?  53  LEU   A HD12 1 
ATOM   1351 H HD13 A LEU   A 1 53  ? 23.612 1.783   7.324   0.86 16.36 ?  53  LEU   A HD13 1 
ATOM   1352 H HD13 B LEU   A 1 53  ? 23.938 1.917   7.614   0.14 14.48 ?  53  LEU   A HD13 1 
ATOM   1353 H HD21 A LEU   A 1 53  ? 21.130 1.970   8.861   0.86 18.27 ?  53  LEU   A HD21 1 
ATOM   1354 H HD21 B LEU   A 1 53  ? 21.371 2.032   9.035   0.14 15.08 ?  53  LEU   A HD21 1 
ATOM   1355 H HD22 A LEU   A 1 53  ? 22.447 2.660   9.423   0.86 18.27 ?  53  LEU   A HD22 1 
ATOM   1356 H HD22 B LEU   A 1 53  ? 22.581 2.918   9.554   0.14 15.08 ?  53  LEU   A HD22 1 
ATOM   1357 H HD23 A LEU   A 1 53  ? 21.120 3.513   9.239   0.86 18.27 ?  53  LEU   A HD23 1 
ATOM   1358 H HD23 B LEU   A 1 53  ? 21.186 3.597   9.217   0.14 15.08 ?  53  LEU   A HD23 1 
ATOM   1359 N N    A ASN   A 1 54  ? 23.886 7.353   6.911   0.86 10.81 ?  54  ASN   A N    1 
ATOM   1360 N N    B ASN   A 1 54  ? 23.942 7.396   6.959   0.14 11.57 ?  54  ASN   A N    1 
ATOM   1361 C CA   A ASN   A 1 54  ? 24.937 8.351   7.048   0.86 10.67 ?  54  ASN   A CA   1 
ATOM   1362 C CA   B ASN   A 1 54  ? 24.991 8.403   7.086   0.14 11.64 ?  54  ASN   A CA   1 
ATOM   1363 C C    A ASN   A 1 54  ? 24.433 9.590   7.790   0.86 11.27 ?  54  ASN   A C    1 
ATOM   1364 C C    B ASN   A 1 54  ? 24.468 9.670   7.751   0.14 11.66 ?  54  ASN   A C    1 
ATOM   1365 O O    A ASN   A 1 54  ? 25.116 10.122  8.675   0.86 11.88 ?  54  ASN   A O    1 
ATOM   1366 O O    B ASN   A 1 54  ? 25.181 10.302  8.540   0.14 11.59 ?  54  ASN   A O    1 
ATOM   1367 C CB   A ASN   A 1 54  ? 25.496 8.732   5.684   0.86 10.98 ?  54  ASN   A CB   1 
ATOM   1368 C CB   B ASN   A 1 54  ? 25.597 8.723   5.721   0.14 11.87 ?  54  ASN   A CB   1 
ATOM   1369 C CG   A ASN   A 1 54  ? 26.515 9.826   5.798   0.86 11.61 ?  54  ASN   A CG   1 
ATOM   1370 C CG   B ASN   A 1 54  ? 26.583 9.870   5.784   0.14 12.14 ?  54  ASN   A CG   1 
ATOM   1371 O OD1  A ASN   A 1 54  ? 27.512 9.678   6.520   0.86 11.53 ?  54  ASN   A OD1  1 
ATOM   1372 O OD1  B ASN   A 1 54  ? 27.685 9.725   6.314   0.14 12.45 ?  54  ASN   A OD1  1 
ATOM   1373 N ND2  A ASN   A 1 54  ? 26.273 10.947  5.131   0.86 12.36 ?  54  ASN   A ND2  1 
ATOM   1374 N ND2  B ASN   A 1 54  ? 26.191 11.022  5.250   0.14 12.13 ?  54  ASN   A ND2  1 
ATOM   1375 H H    A ASN   A 1 54  ? 23.651 7.166   6.104   0.86 13.12 ?  54  ASN   A H    1 
ATOM   1376 H H    B ASN   A 1 54  ? 23.698 7.224   6.153   0.14 14.03 ?  54  ASN   A H    1 
ATOM   1377 H HA   A ASN   A 1 54  ? 25.654 7.968   7.568   0.86 12.95 ?  54  ASN   A HA   1 
ATOM   1378 H HA   B ASN   A 1 54  ? 25.693 8.046   7.648   0.14 14.12 ?  54  ASN   A HA   1 
ATOM   1379 H HB2  A ASN   A 1 54  ? 25.922 7.951   5.286   0.86 13.32 ?  54  ASN   A HB2  1 
ATOM   1380 H HB2  B ASN   A 1 54  ? 26.067 7.940   5.395   0.14 14.39 ?  54  ASN   A HB2  1 
ATOM   1381 H HB3  A ASN   A 1 54  ? 24.776 9.043   5.114   0.86 13.32 ?  54  ASN   A HB3  1 
ATOM   1382 H HB3  B ASN   A 1 54  ? 24.887 8.968   5.109   0.14 14.39 ?  54  ASN   A HB3  1 
ATOM   1383 H HD21 A ASN   A 1 54  ? 26.835 11.600  5.174   0.86 14.97 ?  54  ASN   A HD21 1 
ATOM   1384 H HD21 B ASN   A 1 54  ? 26.715 11.704  5.268   0.14 14.70 ?  54  ASN   A HD21 1 
ATOM   1385 H HD22 A ASN   A 1 54  ? 25.567 11.017  4.653   0.86 14.97 ?  54  ASN   A HD22 1 
ATOM   1386 H HD22 B ASN   A 1 54  ? 25.416 11.085  4.885   0.14 14.70 ?  54  ASN   A HD22 1 
ATOM   1387 N N    . LYS   A 1 55  ? 23.229 10.063  7.444   1.00 11.91 ?  55  LYS   A N    1 
ATOM   1388 C CA   . LYS   A 1 55  ? 22.645 11.219  8.117   1.00 12.42 ?  55  LYS   A CA   1 
ATOM   1389 C C    . LYS   A 1 55  ? 22.551 10.979  9.619   1.00 12.63 ?  55  LYS   A C    1 
ATOM   1390 O O    . LYS   A 1 55  ? 22.840 11.876  10.423  1.00 13.63 ?  55  LYS   A O    1 
ATOM   1391 C CB   . LYS   A 1 55  ? 21.269 11.522  7.511   1.00 13.33 ?  55  LYS   A CB   1 
ATOM   1392 C CG   . LYS   A 1 55  ? 20.521 12.677  8.160   1.00 15.01 ?  55  LYS   A CG   1 
ATOM   1393 C CD   . LYS   A 1 55  ? 19.199 12.941  7.427   1.00 15.97 ?  55  LYS   A CD   1 
ATOM   1394 C CE   . LYS   A 1 55  ? 18.384 14.050  8.069   1.00 18.06 ?  55  LYS   A CE   1 
ATOM   1395 N NZ   . LYS   A 1 55  ? 17.049 14.200  7.415   1.00 18.75 ?  55  LYS   A NZ   1 
ATOM   1396 H H    A LYS   A 1 55  ? 22.724 9.722   6.834   0.86 14.44 ?  55  LYS   A H    1 
ATOM   1397 H H    B LYS   A 1 55  ? 22.710 9.678   6.872   0.14 14.44 ?  55  LYS   A H    1 
ATOM   1398 H HA   . LYS   A 1 55  ? 23.213 11.988  7.974   1.00 15.05 ?  55  LYS   A HA   1 
ATOM   1399 H HB2  . LYS   A 1 55  ? 21.388 11.744  6.575   1.00 16.14 ?  55  LYS   A HB2  1 
ATOM   1400 H HB3  . LYS   A 1 55  ? 20.713 10.731  7.591   1.00 16.14 ?  55  LYS   A HB3  1 
ATOM   1401 H HG2  . LYS   A 1 55  ? 20.316 12.450  9.083   1.00 18.16 ?  55  LYS   A HG2  1 
ATOM   1402 H HG3  . LYS   A 1 55  ? 21.063 13.477  8.120   1.00 18.16 ?  55  LYS   A HG3  1 
ATOM   1403 H HD2  . LYS   A 1 55  ? 19.393 13.202  6.513   1.00 19.31 ?  55  LYS   A HD2  1 
ATOM   1404 H HD3  . LYS   A 1 55  ? 18.664 12.132  7.434   1.00 19.31 ?  55  LYS   A HD3  1 
ATOM   1405 H HE2  . LYS   A 1 55  ? 18.238 13.841  9.005   1.00 21.82 ?  55  LYS   A HE2  1 
ATOM   1406 H HE3  . LYS   A 1 55  ? 18.858 14.890  7.982   1.00 21.82 ?  55  LYS   A HE3  1 
ATOM   1407 H HZ1  . LYS   A 1 55  ? 16.491 14.638  7.957   1.00 22.65 ?  55  LYS   A HZ1  1 
ATOM   1408 H HZ2  . LYS   A 1 55  ? 17.128 14.660  6.657   1.00 22.65 ?  55  LYS   A HZ2  1 
ATOM   1409 H HZ3  . LYS   A 1 55  ? 16.702 13.400  7.236   1.00 22.65 ?  55  LYS   A HZ3  1 
ATOM   1410 N N    . ALA   A 1 56  ? 22.169 9.764   10.017  1.00 13.03 ?  56  ALA   A N    1 
ATOM   1411 C CA   . ALA   A 1 56  ? 22.049 9.435   11.431  1.00 14.19 ?  56  ALA   A CA   1 
ATOM   1412 C C    . ALA   A 1 56  ? 23.394 9.471   12.158  1.00 13.60 ?  56  ALA   A C    1 
ATOM   1413 O O    . ALA   A 1 56  ? 23.413 9.660   13.376  1.00 14.93 ?  56  ALA   A O    1 
ATOM   1414 C CB   . ALA   A 1 56  ? 21.369 8.070   11.598  1.00 14.89 ?  56  ALA   A CB   1 
ATOM   1415 H H    . ALA   A 1 56  ? 21.973 9.118   9.486   1.00 15.79 ?  56  ALA   A H    1 
ATOM   1416 H HA   . ALA   A 1 56  ? 21.477 10.087  11.855  1.00 17.18 ?  56  ALA   A HA   1 
ATOM   1417 H HB1  . ALA   A 1 56  ? 21.297 7.863   12.545  1.00 18.01 ?  56  ALA   A HB1  1 
ATOM   1418 H HB2  . ALA   A 1 56  ? 20.483 8.108   11.202  1.00 18.01 ?  56  ALA   A HB2  1 
ATOM   1419 H HB3  . ALA   A 1 56  ? 21.900 7.391   11.152  1.00 18.01 ?  56  ALA   A HB3  1 
ATOM   1420 N N    . THR   A 1 57  ? 24.512 9.285   11.442  1.00 12.89 ?  57  THR   A N    1 
ATOM   1421 C CA   . THR   A 1 57  ? 25.855 9.415   12.018  1.00 12.89 ?  57  THR   A CA   1 
ATOM   1422 C C    . THR   A 1 57  ? 26.405 10.834  11.948  1.00 13.20 ?  57  THR   A C    1 
ATOM   1423 O O    . THR   A 1 57  ? 27.588 11.040  12.239  1.00 13.78 ?  57  THR   A O    1 
ATOM   1424 C CB   . THR   A 1 57  ? 26.864 8.465   11.343  1.00 12.78 ?  57  THR   A CB   1 
ATOM   1425 O OG1  . THR   A 1 57  ? 27.249 8.967   10.050  1.00 12.72 ?  57  THR   A OG1  1 
ATOM   1426 C CG2  . THR   A 1 57  ? 26.327 7.043   11.228  1.00 12.85 ?  57  THR   A CG2  1 
ATOM   1427 H H    . THR   A 1 57  ? 24.514 9.058   10.606  1.00 15.62 ?  57  THR   A H    1 
ATOM   1428 H HA   . THR   A 1 57  ? 25.810 9.155   12.952  1.00 15.61 ?  57  THR   A HA   1 
ATOM   1429 H HB   . THR   A 1 57  ? 27.660 8.414   11.903  1.00 15.48 ?  57  THR   A HB   1 
ATOM   1430 H HG1  . THR   A 1 57  ? 26.569 9.032   9.563   1.00 15.41 ?  57  THR   A HG1  1 
ATOM   1431 H HG21 . THR   A 1 57  ? 26.951 6.484   10.731  1.00 15.57 ?  57  THR   A HG21 1 
ATOM   1432 H HG22 . THR   A 1 57  ? 26.200 6.655   12.109  1.00 15.57 ?  57  THR   A HG22 1 
ATOM   1433 H HG23 . THR   A 1 57  ? 25.476 7.038   10.764  1.00 15.57 ?  57  THR   A HG23 1 
ATOM   1434 N N    . ASN   A 1 58  ? 25.596 11.807  11.545  1.00 13.28 ?  58  ASN   A N    1 
ATOM   1435 C CA   . ASN   A 1 58  ? 26.058 13.185  11.460  1.00 14.28 ?  58  ASN   A CA   1 
ATOM   1436 C C    . ASN   A 1 58  ? 27.200 13.319  10.447  1.00 13.06 ?  58  ASN   A C    1 
ATOM   1437 O O    . ASN   A 1 58  ? 28.090 14.158  10.597  1.00 13.85 ?  58  ASN   A O    1 
ATOM   1438 C CB   . ASN   A 1 58  ? 26.443 13.709  12.858  1.00 16.56 ?  58  ASN   A CB   1 
ATOM   1439 C CG   . ASN   A 1 58  ? 26.851 15.170  12.866  1.00 20.35 ?  58  ASN   A CG   1 
ATOM   1440 O OD1  . ASN   A 1 58  ? 26.208 16.004  12.234  1.00 22.31 ?  58  ASN   A OD1  1 
ATOM   1441 N ND2  . ASN   A 1 58  ? 27.921 15.492  13.607  1.00 21.62 ?  58  ASN   A ND2  1 
ATOM   1442 H H    . ASN   A 1 58  ? 24.775 11.681  11.309  1.00 16.09 ?  58  ASN   A H    1 
ATOM   1443 H HA   . ASN   A 1 58  ? 25.320 13.721  11.145  1.00 17.28 ?  58  ASN   A HA   1 
ATOM   1444 H HB2  . ASN   A 1 58  ? 25.676 13.609  13.453  1.00 20.02 ?  58  ASN   A HB2  1 
ATOM   1445 H HB3  . ASN   A 1 58  ? 27.186 13.191  13.202  1.00 20.02 ?  58  ASN   A HB3  1 
ATOM   1446 H HD21 . ASN   A 1 58  ? 28.190 16.309  13.645  1.00 26.10 ?  58  ASN   A HD21 1 
ATOM   1447 H HD22 . ASN   A 1 58  ? 28.342 14.881  14.042  1.00 26.10 ?  58  ASN   A HD22 1 
ATOM   1448 N N    . ASN   A 1 59  ? 27.169 12.507  9.391   1.00 12.31 ?  59  ASN   A N    1 
ATOM   1449 C CA   . ASN   A 1 59  ? 28.140 12.474  8.289   1.00 12.06 ?  59  ASN   A CA   1 
ATOM   1450 C C    . ASN   A 1 59  ? 29.460 11.794  8.671   1.00 11.83 ?  59  ASN   A C    1 
ATOM   1451 O O    . ASN   A 1 59  ? 30.382 11.763  7.841   1.00 12.32 ?  59  ASN   A O    1 
ATOM   1452 C CB   . ASN   A 1 59  ? 28.436 13.860  7.684   1.00 12.30 ?  59  ASN   A CB   1 
ATOM   1453 C CG   . ASN   A 1 59  ? 28.787 13.795  6.215   1.00 12.60 ?  59  ASN   A CG   1 
ATOM   1454 O OD1  . ASN   A 1 59  ? 28.076 13.177  5.422   1.00 12.96 ?  59  ASN   A OD1  1 
ATOM   1455 N ND2  . ASN   A 1 59  ? 29.872 14.465  5.834   1.00 13.35 ?  59  ASN   A ND2  1 
ATOM   1456 H H    . ASN   A 1 59  ? 26.552 11.917  9.274   1.00 14.92 ?  59  ASN   A H    1 
ATOM   1457 H HA   . ASN   A 1 59  ? 27.762 11.946  7.575   1.00 14.62 ?  59  ASN   A HA   1 
ATOM   1458 H HB2  . ASN   A 1 59  ? 27.656 14.425  7.771   1.00 14.91 ?  59  ASN   A HB2  1 
ATOM   1459 H HB3  . ASN   A 1 59  ? 29.191 14.264  8.144   1.00 14.91 ?  59  ASN   A HB3  1 
ATOM   1460 H HD21 . ASN   A 1 59  ? 30.117 14.464  5.007   1.00 16.17 ?  59  ASN   A HD21 1 
ATOM   1461 H HD22 . ASN   A 1 59  ? 30.350 14.890  6.415   1.00 16.17 ?  59  ASN   A HD22 1 
ATOM   1462 N N    . ALA   A 1 60  ? 29.589 11.246  9.877   1.00 11.71 ?  60  ALA   A N    1 
ATOM   1463 C CA   . ALA   A 1 60  ? 30.831 10.570  10.233  1.00 12.13 ?  60  ALA   A CA   1 
ATOM   1464 C C    . ALA   A 1 60  ? 31.064 9.333   9.368   1.00 12.16 ?  60  ALA   A C    1 
ATOM   1465 O O    . ALA   A 1 60  ? 32.211 9.006   9.038   1.00 12.62 ?  60  ALA   A O    1 
ATOM   1466 C CB   . ALA   A 1 60  ? 30.814 10.193  11.712  1.00 12.64 ?  60  ALA   A CB   1 
ATOM   1467 H H    . ALA   A 1 60  ? 28.995 11.254  10.493  1.00 14.21 ?  60  ALA   A H    1 
ATOM   1468 H HA   . ALA   A 1 60  ? 31.578 11.178  10.091  1.00 14.70 ?  60  ALA   A HA   1 
ATOM   1469 H HB1  . ALA   A 1 60  ? 31.641 9.747   11.940  1.00 15.31 ?  60  ALA   A HB1  1 
ATOM   1470 H HB2  . ALA   A 1 60  ? 30.718 11.004  12.243  1.00 15.31 ?  60  ALA   A HB2  1 
ATOM   1471 H HB3  . ALA   A 1 60  ? 30.059 9.605   11.878  1.00 15.31 ?  60  ALA   A HB3  1 
ATOM   1472 N N    . MET   A 1 61  ? 29.995 8.631   8.992   1.00 11.71 ?  61  MET   A N    1 
ATOM   1473 C CA   . MET   A 1 61  ? 30.133 7.498   8.080   1.00 11.49 ?  61  MET   A CA   1 
ATOM   1474 C C    . MET   A 1 61  ? 30.767 7.927   6.758   1.00 11.46 ?  61  MET   A C    1 
ATOM   1475 O O    . MET   A 1 61  ? 31.653 7.242   6.240   1.00 11.87 ?  61  MET   A O    1 
ATOM   1476 C CB   . MET   A 1 61  ? 28.768 6.835   7.867   1.00 11.37 ?  61  MET   A CB   1 
ATOM   1477 C CG   . MET   A 1 61  ? 28.776 5.670   6.877   1.00 11.85 ?  61  MET   A CG   1 
ATOM   1478 S SD   . MET   A 1 61  ? 27.151 4.931   6.657   1.00 13.02 ?  61  MET   A SD   1 
ATOM   1479 C CE   . MET   A 1 61  ? 26.984 4.087   8.228   1.00 14.86 ?  61  MET   A CE   1 
ATOM   1480 H H    . MET   A 1 61  ? 29.191 8.790   9.243   1.00 14.20 ?  61  MET   A H    1 
ATOM   1481 H HA   . MET   A 1 61  ? 30.711 6.837   8.492   1.00 13.93 ?  61  MET   A HA   1 
ATOM   1482 H HB2  . MET   A 1 61  ? 28.452 6.492   8.715   1.00 13.79 ?  61  MET   A HB2  1 
ATOM   1483 H HB3  . MET   A 1 61  ? 28.147 7.498   7.529   1.00 13.79 ?  61  MET   A HB3  1 
ATOM   1484 H HG2  . MET   A 1 61  ? 29.067 5.983   6.007   1.00 14.37 ?  61  MET   A HG2  1 
ATOM   1485 H HG3  . MET   A 1 61  ? 29.369 4.976   7.198   1.00 14.37 ?  61  MET   A HG3  1 
ATOM   1486 H HE1  . MET   A 1 61  ? 26.151 3.590   8.231   1.00 17.97 ?  61  MET   A HE1  1 
ATOM   1487 H HE2  . MET   A 1 61  ? 27.733 3.484   8.342   1.00 17.97 ?  61  MET   A HE2  1 
ATOM   1488 H HE3  . MET   A 1 61  ? 26.977 4.747   8.941   1.00 17.97 ?  61  MET   A HE3  1 
ATOM   1489 N N    . GLN   A 1 62  ? 30.324 9.062   6.200   1.00 11.63 ?  62  GLN   A N    1 
ATOM   1490 C CA   . GLN   A 1 62  ? 30.880 9.541   4.937   1.00 11.80 ?  62  GLN   A CA   1 
ATOM   1491 C C    . GLN   A 1 62  ? 32.352 9.920   5.077   1.00 11.72 ?  62  GLN   A C    1 
ATOM   1492 O O    . GLN   A 1 62  ? 33.162 9.608   4.195   1.00 12.21 ?  62  GLN   A O    1 
ATOM   1493 C CB   . GLN   A 1 62  ? 30.073 10.726  4.405   1.00 11.71 ?  62  GLN   A CB   1 
ATOM   1494 C CG   . GLN   A 1 62  ? 30.453 11.096  2.980   1.00 11.63 ?  62  GLN   A CG   1 
ATOM   1495 C CD   . GLN   A 1 62  ? 30.116 9.972   2.026   1.00 12.14 ?  62  GLN   A CD   1 
ATOM   1496 O OE1  . GLN   A 1 62  ? 28.937 9.661   1.821   1.00 12.72 ?  62  GLN   A OE1  1 
ATOM   1497 N NE2  . GLN   A 1 62  ? 31.131 9.297   1.498   1.00 12.78 ?  62  GLN   A NE2  1 
ATOM   1498 H H    . GLN   A 1 62  ? 29.706 9.559   6.533   1.00 14.10 ?  62  GLN   A H    1 
ATOM   1499 H HA   . GLN   A 1 62  ? 30.823 8.824   4.286   1.00 14.31 ?  62  GLN   A HA   1 
ATOM   1500 H HB2  . GLN   A 1 62  ? 29.131 10.500  4.415   1.00 14.19 ?  62  GLN   A HB2  1 
ATOM   1501 H HB3  . GLN   A 1 62  ? 30.237 11.498  4.970   1.00 14.19 ?  62  GLN   A HB3  1 
ATOM   1502 H HG2  . GLN   A 1 62  ? 29.958 11.883  2.712   1.00 14.10 ?  62  GLN   A HG2  1 
ATOM   1503 H HG3  . GLN   A 1 62  ? 31.408 11.263  2.932   1.00 14.10 ?  62  GLN   A HG3  1 
ATOM   1504 H HE21 . GLN   A 1 62  ? 31.941 9.530   1.678   1.00 15.48 ?  62  GLN   A HE21 1 
ATOM   1505 H HE22 . GLN   A 1 62  ? 30.983 8.643   0.961   1.00 15.48 ?  62  GLN   A HE22 1 
ATOM   1506 N N    . VAL   A 1 63  ? 32.718 10.591  6.175   1.00 12.11 ?  63  VAL   A N    1 
ATOM   1507 C CA   . VAL   A 1 63  ? 34.112 10.983  6.389   1.00 12.96 ?  63  VAL   A CA   1 
ATOM   1508 C C    . VAL   A 1 63  ? 35.008 9.747   6.448   1.00 12.29 ?  63  VAL   A C    1 
ATOM   1509 O O    . VAL   A 1 63  ? 36.054 9.677   5.786   1.00 12.84 ?  63  VAL   A O    1 
ATOM   1510 C CB   . VAL   A 1 63  ? 34.227 11.852  7.654   1.00 14.87 ?  63  VAL   A CB   1 
ATOM   1511 C CG1  . VAL   A 1 63  ? 35.680 12.108  8.009   1.00 16.41 ?  63  VAL   A CG1  1 
ATOM   1512 C CG2  . VAL   A 1 63  ? 33.482 13.180  7.452   1.00 15.21 ?  63  VAL   A CG2  1 
ATOM   1513 H H    . VAL   A 1 63  ? 32.175 10.823  6.808   1.00 14.68 ?  63  VAL   A H    1 
ATOM   1514 H HA   . VAL   A 1 63  ? 34.394 11.520  5.636   1.00 15.71 ?  63  VAL   A HA   1 
ATOM   1515 H HB   . VAL   A 1 63  ? 33.813 11.389  8.400   1.00 17.99 ?  63  VAL   A HB   1 
ATOM   1516 H HG11 . VAL   A 1 63  ? 35.723 12.834  8.649   1.00 19.84 ?  63  VAL   A HG11 1 
ATOM   1517 H HG12 . VAL   A 1 63  ? 36.058 11.303  8.393   1.00 19.84 ?  63  VAL   A HG12 1 
ATOM   1518 H HG13 . VAL   A 1 63  ? 36.160 12.350  7.201   1.00 19.84 ?  63  VAL   A HG13 1 
ATOM   1519 H HG21 . VAL   A 1 63  ? 33.577 13.721  8.253   1.00 18.40 ?  63  VAL   A HG21 1 
ATOM   1520 H HG22 . VAL   A 1 63  ? 33.865 13.645  6.692   1.00 18.40 ?  63  VAL   A HG22 1 
ATOM   1521 H HG23 . VAL   A 1 63  ? 32.543 12.995  7.289   1.00 18.40 ?  63  VAL   A HG23 1 
ATOM   1522 N N    . GLU   A 1 64  ? 34.589 8.734   7.216   1.00 12.50 ?  64  GLU   A N    1 
ATOM   1523 C CA   . GLU   A 1 64  ? 35.357 7.499   7.308   1.00 12.25 ?  64  GLU   A CA   1 
ATOM   1524 C C    . GLU   A 1 64  ? 35.442 6.815   5.948   1.00 11.73 ?  64  GLU   A C    1 
ATOM   1525 O O    . GLU   A 1 64  ? 36.492 6.266   5.570   1.00 12.47 ?  64  GLU   A O    1 
ATOM   1526 C CB   . GLU   A 1 64  ? 34.675 6.592   8.331   1.00 13.20 ?  64  GLU   A CB   1 
ATOM   1527 C CG   . GLU   A 1 64  ? 35.326 5.243   8.482   1.00 13.86 ?  64  GLU   A CG   1 
ATOM   1528 C CD   . GLU   A 1 64  ? 34.456 4.242   9.213   1.00 14.80 ?  64  GLU   A CD   1 
ATOM   1529 O OE1  . GLU   A 1 64  ? 33.211 4.329   9.095   1.00 15.65 ?  64  GLU   A OE1  1 
ATOM   1530 O OE2  . GLU   A 1 64  ? 35.020 3.346   9.888   1.00 14.99 -1 64  GLU   A OE2  1 
ATOM   1531 H H    . GLU   A 1 64  ? 33.861 8.738   7.682   1.00 15.14 ?  64  GLU   A H    1 
ATOM   1532 H HA   . GLU   A 1 64  ? 36.255 7.704   7.617   1.00 14.85 ?  64  GLU   A HA   1 
ATOM   1533 H HB2  . GLU   A 1 64  ? 34.702 7.035   9.200   1.00 15.98 ?  64  GLU   A HB2  1 
ATOM   1534 H HB3  . GLU   A 1 64  ? 33.756 6.463   8.062   1.00 15.98 ?  64  GLU   A HB3  1 
ATOM   1535 H HG2  . GLU   A 1 64  ? 35.526 4.877   7.603   1.00 16.77 ?  64  GLU   A HG2  1 
ATOM   1536 H HG3  . GLU   A 1 64  ? 36.148 5.343   8.985   1.00 16.77 ?  64  GLU   A HG3  1 
ATOM   1537 N N    . SER   A 1 65  ? 34.320 6.807   5.218   1.00 11.81 ?  65  SER   A N    1 
ATOM   1538 C CA   . SER   A 1 65  ? 34.261 6.159   3.912   1.00 11.47 ?  65  SER   A CA   1 
ATOM   1539 C C    . SER   A 1 65  ? 35.182 6.829   2.901   1.00 11.97 ?  65  SER   A C    1 
ATOM   1540 O O    . SER   A 1 65  ? 35.825 6.150   2.090   1.00 12.75 ?  65  SER   A O    1 
ATOM   1541 C CB   . SER   A 1 65  ? 32.819 6.164   3.387   1.00 11.88 ?  65  SER   A CB   1 
ATOM   1542 O OG   . SER   A 1 65  ? 31.979 5.333   4.170   1.00 12.24 ?  65  SER   A OG   1 
ATOM   1543 H H    . SER   A 1 65  ? 33.581 7.175   5.462   1.00 14.32 ?  65  SER   A H    1 
ATOM   1544 H HA   . SER   A 1 65  ? 34.545 5.238   4.007   1.00 13.91 ?  65  SER   A HA   1 
ATOM   1545 H HB2  . SER   A 1 65  ? 32.478 7.067   3.410   1.00 14.40 ?  65  SER   A HB2  1 
ATOM   1546 H HB3  . SER   A 1 65  ? 32.823 5.832   2.475   1.00 14.40 ?  65  SER   A HB3  1 
ATOM   1547 H HG   . SER   A 1 65  ? 31.969 5.605   4.971   1.00 14.84 ?  65  SER   A HG   1 
ATOM   1548 N N    . ASP   A 1 66  ? 35.255 8.163   2.921   1.00 12.18 ?  66  ASP   A N    1 
ATOM   1549 C CA   . ASP   A 1 66  ? 36.116 8.858   1.969   1.00 12.95 ?  66  ASP   A CA   1 
ATOM   1550 C C    . ASP   A 1 66  ? 37.583 8.509   2.201   1.00 12.71 ?  66  ASP   A C    1 
ATOM   1551 O O    . ASP   A 1 66  ? 38.353 8.341   1.246   1.00 13.77 ?  66  ASP   A O    1 
ATOM   1552 C CB   . ASP   A 1 66  ? 35.901 10.369  2.070   1.00 14.46 ?  66  ASP   A CB   1 
ATOM   1553 C CG   . ASP   A 1 66  ? 34.564 10.833  1.473   1.00 16.36 ?  66  ASP   A CG   1 
ATOM   1554 O OD1  . ASP   A 1 66  ? 33.860 10.029  0.818   1.00 16.55 ?  66  ASP   A OD1  1 
ATOM   1555 O OD2  . ASP   A 1 66  ? 34.239 12.026  1.648   1.00 19.58 -1 66  ASP   A OD2  1 
ATOM   1556 H H    . ASP   A 1 66  ? 34.815 8.679   3.457   1.00 14.76 ?  66  ASP   A H    1 
ATOM   1557 H HA   . ASP   A 1 66  ? 35.877 8.580   1.071   1.00 15.68 ?  66  ASP   A HA   1 
ATOM   1558 H HB2  . ASP   A 1 66  ? 35.916 10.626  3.005   1.00 17.50 ?  66  ASP   A HB2  1 
ATOM   1559 H HB3  . ASP   A 1 66  ? 36.617 10.817  1.592   1.00 17.50 ?  66  ASP   A HB3  1 
ATOM   1560 N N    . ASP   A 1 67  ? 37.987 8.376   3.464   1.00 12.81 ?  67  ASP   A N    1 
ATOM   1561 C CA   . ASP   A 1 67  ? 39.345 7.930   3.759   1.00 13.78 ?  67  ASP   A CA   1 
ATOM   1562 C C    . ASP   A 1 67  ? 39.571 6.496   3.284   1.00 13.73 ?  67  ASP   A C    1 
ATOM   1563 O O    . ASP   A 1 67  ? 40.637 6.175   2.745   1.00 14.55 ?  67  ASP   A O    1 
ATOM   1564 C CB   . ASP   A 1 67  ? 39.617 8.062   5.256   1.00 15.36 ?  67  ASP   A CB   1 
ATOM   1565 C CG   . ASP   A 1 67  ? 40.917 7.395   5.676   1.00 16.78 ?  67  ASP   A CG   1 
ATOM   1566 O OD1  . ASP   A 1 67  ? 41.986 8.037   5.541   1.00 19.67 ?  67  ASP   A OD1  1 
ATOM   1567 O OD2  . ASP   A 1 67  ? 40.863 6.230   6.137   1.00 16.35 -1 67  ASP   A OD2  1 
ATOM   1568 H H    . ASP   A 1 67  ? 37.505 8.544   4.152   1.00 15.52 ?  67  ASP   A H    1 
ATOM   1569 H HA   . ASP   A 1 67  ? 39.972 8.503   3.289   1.00 16.68 ?  67  ASP   A HA   1 
ATOM   1570 H HB2  . ASP   A 1 67  ? 39.674 9.000   5.481   1.00 18.58 ?  67  ASP   A HB2  1 
ATOM   1571 H HB3  . ASP   A 1 67  ? 38.886 7.645   5.743   1.00 18.58 ?  67  ASP   A HB3  1 
ATOM   1572 N N    . TYR   A 1 68  ? 38.575 5.615   3.466   1.00 13.13 ?  68  TYR   A N    1 
ATOM   1573 C CA   . TYR   A 1 68  ? 38.699 4.231   2.997   1.00 13.16 ?  68  TYR   A CA   1 
ATOM   1574 C C    . TYR   A 1 68  ? 38.929 4.183   1.488   1.00 12.87 ?  68  TYR   A C    1 
ATOM   1575 O O    . TYR   A 1 68  ? 39.812 3.458   1.006   1.00 13.62 ?  68  TYR   A O    1 
ATOM   1576 C CB   . TYR   A 1 68  ? 37.452 3.410   3.384   1.00 13.74 ?  68  TYR   A CB   1 
ATOM   1577 C CG   . TYR   A 1 68  ? 37.481 2.019   2.751   1.00 15.21 ?  68  TYR   A CG   1 
ATOM   1578 C CD1  . TYR   A 1 68  ? 37.015 1.822   1.454   1.00 16.83 ?  68  TYR   A CD1  1 
ATOM   1579 C CD2  . TYR   A 1 68  ? 38.033 0.933   3.414   1.00 17.62 ?  68  TYR   A CD2  1 
ATOM   1580 C CE1  . TYR   A 1 68  ? 37.080 0.601   0.842   1.00 18.19 ?  68  TYR   A CE1  1 
ATOM   1581 C CE2  . TYR   A 1 68  ? 38.094 -0.326  2.800   1.00 18.20 ?  68  TYR   A CE2  1 
ATOM   1582 C CZ   . TYR   A 1 68  ? 37.624 -0.461  1.516   1.00 18.80 ?  68  TYR   A CZ   1 
ATOM   1583 O OH   . TYR   A 1 68  ? 37.705 -1.670  0.887   1.00 20.71 ?  68  TYR   A OH   1 
ATOM   1584 H H    . TYR   A 1 68  ? 37.827 5.793   3.858   1.00 15.91 ?  68  TYR   A H    1 
ATOM   1585 H HA   . TYR   A 1 68  ? 39.463 3.825   3.425   1.00 15.95 ?  68  TYR   A HA   1 
ATOM   1586 H HB2  . TYR   A 1 68  ? 37.426 3.299   4.350   1.00 16.64 ?  68  TYR   A HB2  1 
ATOM   1587 H HB3  . TYR   A 1 68  ? 36.652 3.866   3.079   1.00 16.64 ?  68  TYR   A HB3  1 
ATOM   1588 H HD1  . TYR   A 1 68  ? 36.657 2.546   0.988   1.00 20.34 ?  68  TYR   A HD1  1 
ATOM   1589 H HD2  . TYR   A 1 68  ? 38.368 1.035   4.271   1.00 21.29 ?  68  TYR   A HD2  1 
ATOM   1590 H HE1  . TYR   A 1 68  ? 36.761 0.498   -0.027  1.00 21.97 ?  68  TYR   A HE1  1 
ATOM   1591 H HE2  . TYR   A 1 68  ? 38.472 -1.055  3.235   1.00 21.99 ?  68  TYR   A HE2  1 
ATOM   1592 H HH   . TYR   A 1 68  ? 38.049 -2.240  1.398   1.00 25.00 ?  68  TYR   A HH   1 
ATOM   1593 N N    . ILE   A 1 69  ? 38.147 4.952   0.722   1.00 12.73 ?  69  ILE   A N    1 
ATOM   1594 C CA   . ILE   A 1 69  ? 38.284 4.934   -0.734  1.00 13.11 ?  69  ILE   A CA   1 
ATOM   1595 C C    . ILE   A 1 69  ? 39.611 5.550   -1.169  1.00 12.78 ?  69  ILE   A C    1 
ATOM   1596 O O    . ILE   A 1 69  ? 40.255 5.067   -2.108  1.00 13.18 ?  69  ILE   A O    1 
ATOM   1597 C CB   . ILE   A 1 69  ? 37.080 5.631   -1.402  1.00 13.76 ?  69  ILE   A CB   1 
ATOM   1598 C CG1  . ILE   A 1 69  ? 35.762 4.896   -1.123  1.00 14.60 ?  69  ILE   A CG1  1 
ATOM   1599 C CG2  . ILE   A 1 69  ? 37.324 5.816   -2.908  1.00 15.17 ?  69  ILE   A CG2  1 
ATOM   1600 C CD1  . ILE   A 1 69  ? 35.606 3.599   -1.881  1.00 15.32 ?  69  ILE   A CD1  1 
ATOM   1601 H H    . ILE   A 1 69  ? 37.542 5.491   1.017   1.00 15.42 ?  69  ILE   A H    1 
ATOM   1602 H HA   . ILE   A 1 69  ? 38.286 4.011   -1.026  1.00 15.88 ?  69  ILE   A HA   1 
ATOM   1603 H HB   . ILE   A 1 69  ? 37.004 6.513   -1.017  1.00 16.67 ?  69  ILE   A HB   1 
ATOM   1604 H HG12 . ILE   A 1 69  ? 35.719 4.691   -0.175  1.00 17.67 ?  69  ILE   A HG12 1 
ATOM   1605 H HG13 . ILE   A 1 69  ? 35.025 5.475   -1.367  1.00 17.67 ?  69  ILE   A HG13 1 
ATOM   1606 H HG21 . ILE   A 1 69  ? 36.476 6.013   -3.344  1.00 18.35 ?  69  ILE   A HG21 1 
ATOM   1607 H HG22 . ILE   A 1 69  ? 37.935 6.562   -3.043  1.00 18.35 ?  69  ILE   A HG22 1 
ATOM   1608 H HG23 . ILE   A 1 69  ? 37.702 5.006   -3.276  1.00 18.35 ?  69  ILE   A HG23 1 
ATOM   1609 H HD11 . ILE   A 1 69  ? 34.807 3.150   -1.567  1.00 18.53 ?  69  ILE   A HD11 1 
ATOM   1610 H HD12 . ILE   A 1 69  ? 35.521 3.797   -2.828  1.00 18.53 ?  69  ILE   A HD12 1 
ATOM   1611 H HD13 . ILE   A 1 69  ? 36.383 3.044   -1.726  1.00 18.53 ?  69  ILE   A HD13 1 
ATOM   1612 N N    . ALA   A 1 70  ? 40.028 6.634   -0.514  1.00 13.01 ?  70  ALA   A N    1 
ATOM   1613 C CA   . ALA   A 1 70  ? 41.306 7.248   -0.857  1.00 14.16 ?  70  ALA   A CA   1 
ATOM   1614 C C    . ALA   A 1 70  ? 42.457 6.265   -0.687  1.00 14.44 ?  70  ALA   A C    1 
ATOM   1615 O O    . ALA   A 1 70  ? 43.421 6.297   -1.455  1.00 16.57 ?  70  ALA   A O    1 
ATOM   1616 C CB   . ALA   A 1 70  ? 41.537 8.495   -0.002  1.00 14.84 ?  70  ALA   A CB   1 
ATOM   1617 H H    . ALA   A 1 70  ? 39.587 7.031   0.109   1.00 15.76 ?  70  ALA   A H    1 
ATOM   1618 H HA   . ALA   A 1 70  ? 41.278 7.531   -1.788  1.00 17.14 ?  70  ALA   A HA   1 
ATOM   1619 H HB1  . ALA   A 1 70  ? 42.395 8.882   -0.243  1.00 17.96 ?  70  ALA   A HB1  1 
ATOM   1620 H HB2  . ALA   A 1 70  ? 40.828 9.130   -0.162  1.00 17.96 ?  70  ALA   A HB2  1 
ATOM   1621 H HB3  . ALA   A 1 70  ? 41.548 8.233   0.934   1.00 17.96 ?  70  ALA   A HB3  1 
ATOM   1622 N N    . THR   A 1 71  ? 42.360 5.366   0.290   1.00 13.89 ?  71  THR   A N    1 
ATOM   1623 C CA   . THR   A 1 71  ? 43.415 4.383   0.532   1.00 15.45 ?  71  THR   A CA   1 
ATOM   1624 C C    . THR   A 1 71  ? 43.298 3.162   -0.374  1.00 15.72 ?  71  THR   A C    1 
ATOM   1625 O O    . THR   A 1 71  ? 44.313 2.647   -0.867  1.00 17.66 ?  71  THR   A O    1 
ATOM   1626 C CB   . THR   A 1 71  ? 43.348 3.927   1.987   1.00 17.74 ?  71  THR   A CB   1 
ATOM   1627 O OG1  . THR   A 1 71  ? 43.601 5.049   2.839   1.00 19.37 ?  71  THR   A OG1  1 
ATOM   1628 C CG2  . THR   A 1 71  ? 44.355 2.810   2.268   1.00 19.27 ?  71  THR   A CG2  1 
ATOM   1629 H H    . THR   A 1 71  ? 41.692 5.297   0.821   1.00 16.82 ?  71  THR   A H    1 
ATOM   1630 H HA   . THR   A 1 71  ? 44.278 4.790   0.374   1.00 18.69 ?  71  THR   A HA   1 
ATOM   1631 H HB   . THR   A 1 71  ? 42.457 3.576   2.164   1.00 21.44 ?  71  THR   A HB   1 
ATOM   1632 H HG1  . THR   A 1 71  ? 43.016 5.637   2.708   1.00 23.39 ?  71  THR   A HG1  1 
ATOM   1633 H HG21 . THR   A 1 71  ? 44.488 2.721   3.225   1.00 23.27 ?  71  THR   A HG21 1 
ATOM   1634 H HG22 . THR   A 1 71  ? 44.032 1.963   1.918   1.00 23.27 ?  71  THR   A HG22 1 
ATOM   1635 H HG23 . THR   A 1 71  ? 45.207 3.018   1.853   1.00 23.27 ?  71  THR   A HG23 1 
ATOM   1636 N N    . ASN   A 1 72  ? 42.076 2.657   -0.570  1.00 14.64 ?  72  ASN   A N    1 
ATOM   1637 C CA   . ASN   A 1 72  ? 41.862 1.328   -1.133  1.00 14.78 ?  72  ASN   A CA   1 
ATOM   1638 C C    . ASN   A 1 72  ? 41.233 1.320   -2.514  1.00 15.18 ?  72  ASN   A C    1 
ATOM   1639 O O    . ASN   A 1 72  ? 41.249 0.269   -3.170  1.00 16.69 ?  72  ASN   A O    1 
ATOM   1640 C CB   . ASN   A 1 72  ? 40.974 0.510   -0.189  1.00 15.59 ?  72  ASN   A CB   1 
ATOM   1641 C CG   . ASN   A 1 72  ? 41.593 0.351   1.179   1.00 16.43 ?  72  ASN   A CG   1 
ATOM   1642 O OD1  . ASN   A 1 72  ? 41.135 0.944   2.157   1.00 18.33 ?  72  ASN   A OD1  1 
ATOM   1643 N ND2  . ASN   A 1 72  ? 42.650 -0.424  1.253   1.00 17.39 ?  72  ASN   A ND2  1 
ATOM   1644 H H    . ASN   A 1 72  ? 41.345 3.073   -0.387  1.00 17.71 ?  72  ASN   A H    1 
ATOM   1645 H HA   . ASN   A 1 72  ? 42.717 0.878   -1.206  1.00 17.89 ?  72  ASN   A HA   1 
ATOM   1646 H HB2  . ASN   A 1 72  ? 40.121 0.960   -0.092  1.00 18.86 ?  72  ASN   A HB2  1 
ATOM   1647 H HB3  . ASN   A 1 72  ? 40.845 -0.374  -0.566  1.00 18.86 ?  72  ASN   A HB3  1 
ATOM   1648 H HD21 . ASN   A 1 72  ? 43.043 -0.532  2.009   1.00 21.02 ?  72  ASN   A HD21 1 
ATOM   1649 H HD22 . ASN   A 1 72  ? 42.950 -0.808  0.548   1.00 21.02 ?  72  ASN   A HD22 1 
ATOM   1650 N N    . GLY   A 1 73  ? 40.679 2.438   -2.972  1.00 14.52 ?  73  GLY   A N    1 
ATOM   1651 C CA   . GLY   A 1 73  ? 39.942 2.463   -4.210  1.00 14.24 ?  73  GLY   A CA   1 
ATOM   1652 C C    . GLY   A 1 73  ? 38.550 1.877   -4.041  1.00 13.48 ?  73  GLY   A C    1 
ATOM   1653 O O    . GLY   A 1 73  ? 38.169 1.404   -2.963  1.00 14.38 ?  73  GLY   A O    1 
ATOM   1654 H H    . GLY   A 1 73  ? 40.718 3.208   -2.579  1.00 17.57 ?  73  GLY   A H    1 
ATOM   1655 H HA2  . GLY   A 1 73  ? 39.859 3.380   -4.523  1.00 17.24 ?  73  GLY   A HA2  1 
ATOM   1656 H HA3  . GLY   A 1 73  ? 40.414 1.950   -4.883  1.00 17.24 ?  73  GLY   A HA3  1 
ATOM   1657 N N    . PRO   A 1 74  ? 37.772 1.887   -5.122  1.00 14.20 ?  74  PRO   A N    1 
ATOM   1658 C CA   . PRO   A 1 74  ? 36.370 1.456   -5.040  1.00 14.10 ?  74  PRO   A CA   1 
ATOM   1659 C C    . PRO   A 1 74  ? 36.219 -0.028  -4.724  1.00 13.23 ?  74  PRO   A C    1 
ATOM   1660 O O    . PRO   A 1 74  ? 37.087 -0.861  -5.004  1.00 14.35 ?  74  PRO   A O    1 
ATOM   1661 C CB   . PRO   A 1 74  ? 35.823 1.762   -6.439  1.00 16.14 ?  74  PRO   A CB   1 
ATOM   1662 C CG   . PRO   A 1 74  ? 36.763 2.766   -7.027  1.00 19.06 ?  74  PRO   A CG   1 
ATOM   1663 C CD   . PRO   A 1 74  ? 38.108 2.435   -6.447  1.00 16.26 ?  74  PRO   A CD   1 
ATOM   1664 H HA   . PRO   A 1 74  ? 35.890 1.984   -4.382  1.00 17.07 ?  74  PRO   A HA   1 
ATOM   1665 H HB2  . PRO   A 1 74  ? 35.812 0.950   -6.970  1.00 19.52 ?  74  PRO   A HB2  1 
ATOM   1666 H HB3  . PRO   A 1 74  ? 34.928 2.134   -6.367  1.00 19.52 ?  74  PRO   A HB3  1 
ATOM   1667 H HG2  . PRO   A 1 74  ? 36.781 2.680   -7.994  1.00 23.02 ?  74  PRO   A HG2  1 
ATOM   1668 H HG3  . PRO   A 1 74  ? 36.495 3.662   -6.769  1.00 23.02 ?  74  PRO   A HG3  1 
ATOM   1669 H HD2  . PRO   A 1 74  ? 38.561 1.769   -6.990  1.00 19.66 ?  74  PRO   A HD2  1 
ATOM   1670 H HD3  . PRO   A 1 74  ? 38.645 3.244   -6.366  1.00 19.66 ?  74  PRO   A HD3  1 
ATOM   1671 N N    . LEU   A 1 75  ? 35.069 -0.351  -4.138  1.00 12.93 ?  75  LEU   A N    1 
ATOM   1672 C CA   . LEU   A 1 75  ? 34.673 -1.742  -3.986  1.00 12.36 ?  75  LEU   A CA   1 
ATOM   1673 C C    . LEU   A 1 75  ? 34.289 -2.325  -5.344  1.00 13.04 ?  75  LEU   A C    1 
ATOM   1674 O O    . LEU   A 1 75  ? 34.168 -1.615  -6.346  1.00 14.48 ?  75  LEU   A O    1 
ATOM   1675 C CB   . LEU   A 1 75  ? 33.485 -1.868  -3.031  1.00 12.56 ?  75  LEU   A CB   1 
ATOM   1676 C CG   . LEU   A 1 75  ? 33.703 -1.462  -1.577  1.00 14.43 ?  75  LEU   A CG   1 
ATOM   1677 C CD1  . LEU   A 1 75  ? 32.421 -1.657  -0.771  1.00 16.18 ?  75  LEU   A CD1  1 
ATOM   1678 C CD2  . LEU   A 1 75  ? 34.855 -2.193  -0.936  1.00 18.11 ?  75  LEU   A CD2  1 
ATOM   1679 H H    . LEU   A 1 75  ? 34.502 0.219   -3.827  1.00 15.66 ?  75  LEU   A H    1 
ATOM   1680 H HA   . LEU   A 1 75  ? 35.418 -2.248  -3.638  1.00 14.98 ?  75  LEU   A HA   1 
ATOM   1681 H HB2  . LEU   A 1 75  ? 32.765 -1.323  -3.375  1.00 15.23 ?  75  LEU   A HB2  1 
ATOM   1682 H HB3  . LEU   A 1 75  ? 33.209 -2.799  -3.028  1.00 15.23 ?  75  LEU   A HB3  1 
ATOM   1683 H HG   . LEU   A 1 75  ? 33.924 -0.515  -1.558  1.00 17.46 ?  75  LEU   A HG   1 
ATOM   1684 H HD11 . LEU   A 1 75  ? 32.582 -1.389  0.147   1.00 19.57 ?  75  LEU   A HD11 1 
ATOM   1685 H HD12 . LEU   A 1 75  ? 31.722 -1.106  -1.158  1.00 19.57 ?  75  LEU   A HD12 1 
ATOM   1686 H HD13 . LEU   A 1 75  ? 32.166 -2.590  -0.806  1.00 19.57 ?  75  LEU   A HD13 1 
ATOM   1687 H HD21 . LEU   A 1 75  ? 34.907 -1.945  -0.001  1.00 21.88 ?  75  LEU   A HD21 1 
ATOM   1688 H HD22 . LEU   A 1 75  ? 34.709 -3.148  -1.019  1.00 21.88 ?  75  LEU   A HD22 1 
ATOM   1689 H HD23 . LEU   A 1 75  ? 35.682 -1.947  -1.387  1.00 21.88 ?  75  LEU   A HD23 1 
ATOM   1690 N N    . LYS   A 1 76  ? 34.108 -3.648  -5.363  1.00 13.50 ?  76  LYS   A N    1 
ATOM   1691 C CA   . LYS   A 1 76  ? 33.502 -4.370  -6.478  1.00 13.88 ?  76  LYS   A CA   1 
ATOM   1692 C C    . LYS   A 1 76  ? 31.990 -4.456  -6.279  1.00 12.88 ?  76  LYS   A C    1 
ATOM   1693 O O    . LYS   A 1 76  ? 31.509 -4.576  -5.153  1.00 12.76 ?  76  LYS   A O    1 
ATOM   1694 C CB   . LYS   A 1 76  ? 34.039 -5.812  -6.539  1.00 15.67 ?  76  LYS   A CB   1 
ATOM   1695 C CG   . LYS   A 1 76  ? 35.554 -5.926  -6.735  1.00 17.30 ?  76  LYS   A CG   1 
ATOM   1696 C CD   . LYS   A 1 76  ? 36.061 -7.339  -6.534  1.00 18.73 ?  76  LYS   A CD   1 
ATOM   1697 C CE   . LYS   A 1 76  ? 37.564 -7.407  -6.738  1.00 21.13 ?  76  LYS   A CE   1 
ATOM   1698 N NZ   . LYS   A 1 76  ? 38.097 -8.768  -6.538  1.00 22.10 ?  76  LYS   A NZ   1 
ATOM   1699 H H    . LYS   A 1 76  ? 34.335 -4.167  -4.713  1.00 16.35 ?  76  LYS   A H    1 
ATOM   1700 H HA   . LYS   A 1 76  ? 33.695 -3.921  -7.317  1.00 16.81 ?  76  LYS   A HA   1 
ATOM   1701 H HB2  . LYS   A 1 76  ? 33.817 -6.258  -5.706  1.00 18.95 ?  76  LYS   A HB2  1 
ATOM   1702 H HB3  . LYS   A 1 76  ? 33.612 -6.270  -7.278  1.00 18.95 ?  76  LYS   A HB3  1 
ATOM   1703 H HG2  . LYS   A 1 76  ? 35.774 -5.650  -7.638  1.00 20.91 ?  76  LYS   A HG2  1 
ATOM   1704 H HG3  . LYS   A 1 76  ? 35.998 -5.350  -6.093  1.00 20.91 ?  76  LYS   A HG3  1 
ATOM   1705 H HD2  . LYS   A 1 76  ? 35.860 -7.630  -5.630  1.00 22.62 ?  76  LYS   A HD2  1 
ATOM   1706 H HD3  . LYS   A 1 76  ? 35.637 -7.930  -7.179  1.00 22.62 ?  76  LYS   A HD3  1 
ATOM   1707 H HE2  . LYS   A 1 76  ? 37.775 -7.130  -7.642  1.00 25.50 ?  76  LYS   A HE2  1 
ATOM   1708 H HE3  . LYS   A 1 76  ? 37.997 -6.820  -6.098  1.00 25.50 ?  76  LYS   A HE3  1 
ATOM   1709 H HZ1  . LYS   A 1 76  ? 38.977 -8.778  -6.665  1.00 26.67 ?  76  LYS   A HZ1  1 
ATOM   1710 H HZ2  . LYS   A 1 76  ? 37.921 -9.052  -5.712  1.00 26.67 ?  76  LYS   A HZ2  1 
ATOM   1711 H HZ3  . LYS   A 1 76  ? 37.718 -9.334  -7.118  1.00 26.67 ?  76  LYS   A HZ3  1 
ATOM   1712 N N    . VAL   A 1 77  ? 31.237 -4.423  -7.385  1.00 12.96 ?  77  VAL   A N    1 
ATOM   1713 C CA   . VAL   A 1 77  ? 29.826 -4.802  -7.300  1.00 12.80 ?  77  VAL   A CA   1 
ATOM   1714 C C    . VAL   A 1 77  ? 29.758 -6.256  -6.861  1.00 12.65 ?  77  VAL   A C    1 
ATOM   1715 O O    . VAL   A 1 77  ? 30.414 -7.123  -7.450  1.00 13.25 ?  77  VAL   A O    1 
ATOM   1716 C CB   . VAL   A 1 77  ? 29.114 -4.588  -8.643  1.00 14.45 ?  77  VAL   A CB   1 
ATOM   1717 C CG1  . VAL   A 1 77  ? 27.655 -5.026  -8.545  1.00 15.42 ?  77  VAL   A CG1  1 
ATOM   1718 C CG2  . VAL   A 1 77  ? 29.202 -3.135  -9.071  1.00 15.97 ?  77  VAL   A CG2  1 
ATOM   1719 H H    . VAL   A 1 77  ? 31.512 -4.186  -8.166  1.00 15.70 ?  77  VAL   A H    1 
ATOM   1720 H HA   . VAL   A 1 77  ? 29.388 -4.257  -6.630  1.00 15.50 ?  77  VAL   A HA   1 
ATOM   1721 H HB   . VAL   A 1 77  ? 29.549 -5.130  -9.322  1.00 17.48 ?  77  VAL   A HB   1 
ATOM   1722 H HG11 . VAL   A 1 77  ? 27.189 -4.729  -9.339  1.00 18.65 ?  77  VAL   A HG11 1 
ATOM   1723 H HG12 . VAL   A 1 77  ? 27.618 -5.992  -8.478  1.00 18.65 ?  77  VAL   A HG12 1 
ATOM   1724 H HG13 . VAL   A 1 77  ? 27.262 -4.621  -7.757  1.00 18.65 ?  77  VAL   A HG13 1 
ATOM   1725 H HG21 . VAL   A 1 77  ? 28.700 -3.021  -9.893  1.00 19.31 ?  77  VAL   A HG21 1 
ATOM   1726 H HG22 . VAL   A 1 77  ? 28.825 -2.580  -8.372  1.00 19.31 ?  77  VAL   A HG22 1 
ATOM   1727 H HG23 . VAL   A 1 77  ? 30.132 -2.903  -9.215  1.00 19.31 ?  77  VAL   A HG23 1 
ATOM   1728 N N    . GLY   A 1 78  ? 28.973 -6.530  -5.814  1.00 12.27 ?  78  GLY   A N    1 
ATOM   1729 C CA   . GLY   A 1 78  ? 28.959 -7.823  -5.165  1.00 12.46 ?  78  GLY   A CA   1 
ATOM   1730 C C    . GLY   A 1 78  ? 29.884 -7.918  -3.974  1.00 11.86 ?  78  GLY   A C    1 
ATOM   1731 O O    . GLY   A 1 78  ? 29.829 -8.924  -3.249  1.00 12.93 ?  78  GLY   A O    1 
ATOM   1732 H H    . GLY   A 1 78  ? 28.422 -5.960  -5.469  1.00 14.87 ?  78  GLY   A H    1 
ATOM   1733 H HA2  . GLY   A 1 78  ? 28.059 -8.017  -4.866  1.00 15.10 ?  78  GLY   A HA2  1 
ATOM   1734 H HA3  . GLY   A 1 78  ? 29.218 -8.501  -5.809  1.00 15.10 ?  78  GLY   A HA3  1 
ATOM   1735 N N    . GLY   A 1 79  ? 30.734 -6.910  -3.748  1.00 11.91 ?  79  GLY   A N    1 
ATOM   1736 C CA   . GLY   A 1 79  ? 31.696 -6.930  -2.670  1.00 12.52 ?  79  GLY   A CA   1 
ATOM   1737 C C    . GLY   A 1 79  ? 31.253 -6.133  -1.454  1.00 11.30 ?  79  GLY   A C    1 
ATOM   1738 O O    . GLY   A 1 79  ? 30.131 -5.629  -1.367  1.00 12.17 ?  79  GLY   A O    1 
ATOM   1739 H H    . GLY   A 1 79  ? 30.770 -6.192  -4.224  1.00 14.43 ?  79  GLY   A H    1 
ATOM   1740 H HA2  . GLY   A 1 79  ? 31.849 -7.855  -2.399  1.00 15.17 ?  79  GLY   A HA2  1 
ATOM   1741 H HA3  . GLY   A 1 79  ? 32.540 -6.570  -2.986  1.00 15.17 ?  79  GLY   A HA3  1 
ATOM   1742 N N    . SER   A 1 80  ? 32.161 -6.040  -0.484  1.00 12.12 ?  80  SER   A N    1 
ATOM   1743 C CA   . SER   A 1 80  ? 31.841 -5.420  0.793   1.00 11.65 ?  80  SER   A CA   1 
ATOM   1744 C C    . SER   A 1 80  ? 33.118 -4.961  1.485   1.00 11.62 ?  80  SER   A C    1 
ATOM   1745 O O    . SER   A 1 80  ? 34.232 -5.387  1.148   1.00 13.19 ?  80  SER   A O    1 
ATOM   1746 C CB   . SER   A 1 80  ? 31.086 -6.386  1.715   1.00 12.87 ?  80  SER   A CB   1 
ATOM   1747 O OG   . SER   A 1 80  ? 31.918 -7.436  2.182   1.00 14.85 ?  80  SER   A OG   1 
ATOM   1748 H H    . SER   A 1 80  ? 32.974 -6.319  -0.545  1.00 14.69 ?  80  SER   A H    1 
ATOM   1749 H HA   . SER   A 1 80  ? 31.281 -4.645  0.626   1.00 14.13 ?  80  SER   A HA   1 
ATOM   1750 H HB2  . SER   A 1 80  ? 30.750 -5.891  2.476   1.00 15.59 ?  80  SER   A HB2  1 
ATOM   1751 H HB3  . SER   A 1 80  ? 30.345 -6.772  1.219   1.00 15.59 ?  80  SER   A HB3  1 
ATOM   1752 H HG   . SER   A 1 80  ? 32.218 -7.871  1.525   1.00 17.97 ?  80  SER   A HG   1 
ATOM   1753 N N    . CYS   A 1 81  ? 32.927 -4.128  2.506   1.00 11.40 ?  81  CYS   A N    1 
ATOM   1754 C CA   . CYS   A 1 81  ? 33.981 -3.838  3.468   1.00 11.48 ?  81  CYS   A CA   1 
ATOM   1755 C C    . CYS   A 1 81  ? 33.343 -3.600  4.829   1.00 11.41 ?  81  CYS   A C    1 
ATOM   1756 O O    . CYS   A 1 81  ? 32.176 -3.200  4.920   1.00 12.90 ?  81  CYS   A O    1 
ATOM   1757 C CB   . CYS   A 1 81  ? 34.847 -2.649  3.038   1.00 12.77 ?  81  CYS   A CB   1 
ATOM   1758 S SG   . CYS   A 1 81  ? 33.967 -1.059  3.073   1.00 12.69 ?  81  CYS   A SG   1 
ATOM   1759 H H    . CYS   A 1 81  ? 32.186 -3.708  2.669   1.00 13.83 ?  81  CYS   A H    1 
ATOM   1760 H HA   . CYS   A 1 81  ? 34.561 -4.609  3.540   1.00 13.93 ?  81  CYS   A HA   1 
ATOM   1761 H HB2  . CYS   A 1 81  ? 35.612 -2.582  3.633   1.00 15.47 ?  81  CYS   A HB2  1 
ATOM   1762 H HB3  . CYS   A 1 81  ? 35.157 -2.798  2.127   1.00 15.47 ?  81  CYS   A HB3  1 
ATOM   1763 H HG   . CYS   A 1 81  ? 34.720 -0.186  2.721   1.00 15.37 ?  81  CYS   A HG   1 
ATOM   1764 N N    . VAL   A 1 82  ? 34.114 -3.864  5.884   1.00 11.88 ?  82  VAL   A N    1 
ATOM   1765 C CA   . VAL   A 1 82  ? 33.695 -3.616  7.257   1.00 12.20 ?  82  VAL   A CA   1 
ATOM   1766 C C    . VAL   A 1 82  ? 34.296 -2.303  7.727   1.00 12.53 ?  82  VAL   A C    1 
ATOM   1767 O O    . VAL   A 1 82  ? 35.521 -2.134  7.711   1.00 13.51 ?  82  VAL   A O    1 
ATOM   1768 C CB   . VAL   A 1 82  ? 34.115 -4.759  8.195   1.00 13.88 ?  82  VAL   A CB   1 
ATOM   1769 C CG1  . VAL   A 1 82  ? 33.649 -4.467  9.612   1.00 15.11 ?  82  VAL   A CG1  1 
ATOM   1770 C CG2  . VAL   A 1 82  ? 33.571 -6.094  7.706   1.00 15.16 ?  82  VAL   A CG2  1 
ATOM   1771 H H    . VAL   A 1 82  ? 34.901 -4.216  5.826   1.00 14.40 ?  82  VAL   A H    1 
ATOM   1772 H HA   . VAL   A 1 82  ? 32.725 -3.538  7.285   1.00 14.79 ?  82  VAL   A HA   1 
ATOM   1773 H HB   . VAL   A 1 82  ? 35.080 -4.812  8.206   1.00 16.81 ?  82  VAL   A HB   1 
ATOM   1774 H HG11 . VAL   A 1 82  ? 33.738 -5.271  10.146  1.00 18.28 ?  82  VAL   A HG11 1 
ATOM   1775 H HG12 . VAL   A 1 82  ? 34.195 -3.759  9.991   1.00 18.28 ?  82  VAL   A HG12 1 
ATOM   1776 H HG13 . VAL   A 1 82  ? 32.717 -4.189  9.591   1.00 18.28 ?  82  VAL   A HG13 1 
ATOM   1777 H HG21 . VAL   A 1 82  ? 33.808 -6.784  8.346   1.00 18.34 ?  82  VAL   A HG21 1 
ATOM   1778 H HG22 . VAL   A 1 82  ? 32.606 -6.035  7.627   1.00 18.34 ?  82  VAL   A HG22 1 
ATOM   1779 H HG23 . VAL   A 1 82  ? 33.962 -6.297  6.842   1.00 18.34 ?  82  VAL   A HG23 1 
ATOM   1780 N N    . LEU   A 1 83  ? 33.445 -1.384  8.165   1.00 12.47 ?  83  LEU   A N    1 
ATOM   1781 C CA   . LEU   A 1 83  ? 33.866 -0.118  8.745   1.00 12.40 ?  83  LEU   A CA   1 
ATOM   1782 C C    . LEU   A 1 83  ? 33.152 0.056   10.081  1.00 12.64 ?  83  LEU   A C    1 
ATOM   1783 O O    . LEU   A 1 83  ? 32.430 -0.833  10.545  1.00 13.19 ?  83  LEU   A O    1 
ATOM   1784 C CB   . LEU   A 1 83  ? 33.610 1.049   7.776   1.00 12.71 ?  83  LEU   A CB   1 
ATOM   1785 C CG   . LEU   A 1 83  ? 34.506 1.053   6.530   1.00 13.77 ?  83  LEU   A CG   1 
ATOM   1786 C CD1  . LEU   A 1 83  ? 34.078 2.079   5.503   1.00 14.01 ?  83  LEU   A CD1  1 
ATOM   1787 C CD2  . LEU   A 1 83  ? 35.983 1.263   6.907   1.00 14.63 ?  83  LEU   A CD2  1 
ATOM   1788 H H    . LEU   A 1 83  ? 32.590 -1.474  8.135   1.00 15.11 ?  83  LEU   A H    1 
ATOM   1789 H HA   . LEU   A 1 83  ? 34.819 -0.146  8.919   1.00 15.03 ?  83  LEU   A HA   1 
ATOM   1790 H HB2  . LEU   A 1 83  ? 32.686 1.007   7.470   1.00 15.39 ?  83  LEU   A HB2  1 
ATOM   1791 H HB3  . LEU   A 1 83  ? 33.752 1.888   8.245   1.00 15.39 ?  83  LEU   A HB3  1 
ATOM   1792 H HG   . LEU   A 1 83  ? 34.444 0.181   6.115   1.00 16.68 ?  83  LEU   A HG   1 
ATOM   1793 H HD11 . LEU   A 1 83  ? 34.678 2.023   4.737   1.00 16.96 ?  83  LEU   A HD11 1 
ATOM   1794 H HD12 . LEU   A 1 83  ? 33.172 1.882   5.223   1.00 16.96 ?  83  LEU   A HD12 1 
ATOM   1795 H HD13 . LEU   A 1 83  ? 34.125 2.961   5.894   1.00 16.96 ?  83  LEU   A HD13 1 
ATOM   1796 H HD21 . LEU   A 1 83  ? 36.499 1.416   6.098   1.00 17.71 ?  83  LEU   A HD21 1 
ATOM   1797 H HD22 . LEU   A 1 83  ? 36.058 2.032   7.494   1.00 17.71 ?  83  LEU   A HD22 1 
ATOM   1798 H HD23 . LEU   A 1 83  ? 36.315 0.471   7.361   1.00 17.71 ?  83  LEU   A HD23 1 
ATOM   1799 N N    . SER   A 1 84  ? 33.368 1.206   10.715  1.00 13.32 ?  84  SER   A N    1 
ATOM   1800 C CA   . SER   A 1 84  ? 32.721 1.467   11.992  1.00 13.42 ?  84  SER   A CA   1 
ATOM   1801 C C    . SER   A 1 84  ? 31.205 1.558   11.843  1.00 12.86 ?  84  SER   A C    1 
ATOM   1802 O O    . SER   A 1 84  ? 30.685 2.029   10.833  1.00 13.38 ?  84  SER   A O    1 
ATOM   1803 C CB   . SER   A 1 84  ? 33.226 2.788   12.567  1.00 14.57 ?  84  SER   A CB   1 
ATOM   1804 O OG   . SER   A 1 84  ? 32.586 3.085   13.794  1.00 15.40 ?  84  SER   A OG   1 
ATOM   1805 H H    . SER   A 1 84  ? 33.878 1.841   10.429  1.00 16.13 ?  84  SER   A H    1 
ATOM   1806 H HA   . SER   A 1 84  ? 32.933 0.755   12.611  1.00 16.26 ?  84  SER   A HA   1 
ATOM   1807 H HB2  . SER   A 1 84  ? 34.183 2.724   12.708  1.00 17.64 ?  84  SER   A HB2  1 
ATOM   1808 H HB3  . SER   A 1 84  ? 33.034 3.500   11.934  1.00 17.64 ?  84  SER   A HB3  1 
ATOM   1809 H HG   . SER   A 1 84  ? 32.882 3.812   14.101  1.00 18.63 ?  84  SER   A HG   1 
ATOM   1810 N N    . GLY   A 1 85  ? 30.495 1.137   12.889  1.00 13.80 ?  85  GLY   A N    1 
ATOM   1811 C CA   . GLY   A 1 85  ? 29.070 1.374   12.972  1.00 14.79 ?  85  GLY   A CA   1 
ATOM   1812 C C    . GLY   A 1 85  ? 28.698 2.678   13.638  1.00 14.34 ?  85  GLY   A C    1 
ATOM   1813 O O    . GLY   A 1 85  ? 27.508 2.981   13.761  1.00 15.15 ?  85  GLY   A O    1 
ATOM   1814 H H    . GLY   A 1 85  ? 30.824 0.713   13.558  1.00 16.71 ?  85  GLY   A H    1 
ATOM   1815 H HA2  . GLY   A 1 85  ? 28.696 1.369   12.074  1.00 17.90 ?  85  GLY   A HA2  1 
ATOM   1816 H HA3  . GLY   A 1 85  ? 28.660 0.657   13.472  1.00 17.90 ?  85  GLY   A HA3  1 
ATOM   1817 N N    . HIS   A 1 86  ? 29.680 3.452   14.088  1.00 14.07 ?  86  HIS   A N    1 
ATOM   1818 C CA   . HIS   A 1 86  ? 29.449 4.790   14.649  1.00 14.91 ?  86  HIS   A CA   1 
ATOM   1819 C C    . HIS   A 1 86  ? 28.461 4.662   15.803  1.00 15.46 ?  86  HIS   A C    1 
ATOM   1820 O O    . HIS   A 1 86  ? 28.654 3.789   16.665  1.00 16.61 ?  86  HIS   A O    1 
ATOM   1821 C CB   . HIS   A 1 86  ? 29.071 5.764   13.540  1.00 14.66 ?  86  HIS   A CB   1 
ATOM   1822 C CG   . HIS   A 1 86  ? 30.128 5.874   12.501  1.00 14.69 ?  86  HIS   A CG   1 
ATOM   1823 N ND1  . HIS   A 1 86  ? 31.211 6.719   12.632  1.00 15.91 ?  86  HIS   A ND1  1 
ATOM   1824 C CD2  . HIS   A 1 86  ? 30.311 5.196   11.347  1.00 14.47 ?  86  HIS   A CD2  1 
ATOM   1825 C CE1  . HIS   A 1 86  ? 32.006 6.564   11.589  1.00 15.79 ?  86  HIS   A CE1  1 
ATOM   1826 N NE2  . HIS   A 1 86  ? 31.488 5.640   10.801  1.00 15.20 ?  86  HIS   A NE2  1 
ATOM   1827 H H    . HIS   A 1 86  ? 30.503 3.224   14.087  1.00 17.03 ?  86  HIS   A H    1 
ATOM   1828 H HA   . HIS   A 1 86  ? 30.284 5.107   15.019  1.00 18.04 ?  86  HIS   A HA   1 
ATOM   1829 H HB2  . HIS   A 1 86  ? 28.255 5.471   13.105  1.00 17.74 ?  86  HIS   A HB2  1 
ATOM   1830 H HB3  . HIS   A 1 86  ? 28.938 6.654   13.919  1.00 17.74 ?  86  HIS   A HB3  1 
ATOM   1831 H HD2  . HIS   A 1 86  ? 29.755 4.537   10.995  1.00 17.51 ?  86  HIS   A HD2  1 
ATOM   1832 H HE1  . HIS   A 1 86  ? 32.798 7.029   11.423  1.00 19.10 ?  86  HIS   A HE1  1 
ATOM   1833 H HE2  . HIS   A 1 86  ? 31.827 5.371   10.048  1.00 18.38 ?  86  HIS   A HE2  1 
ATOM   1834 N N    . ASN   A 1 87  ? 27.442 5.509   15.874  1.00 16.52 ?  87  ASN   A N    1 
ATOM   1835 C CA   . ASN   A 1 87  ? 26.451 5.482   16.936  1.00 17.58 ?  87  ASN   A CA   1 
ATOM   1836 C C    . ASN   A 1 87  ? 25.339 4.473   16.687  1.00 18.85 ?  87  ASN   A C    1 
ATOM   1837 O O    . ASN   A 1 87  ? 24.409 4.393   17.496  1.00 21.12 ?  87  ASN   A O    1 
ATOM   1838 C CB   . ASN   A 1 87  ? 25.840 6.882   17.105  1.00 18.60 ?  87  ASN   A CB   1 
ATOM   1839 C CG   . ASN   A 1 87  ? 25.338 7.468   15.790  1.00 19.19 ?  87  ASN   A CG   1 
ATOM   1840 O OD1  . ASN   A 1 87  ? 25.985 7.356   14.751  1.00 19.71 ?  87  ASN   A OD1  1 
ATOM   1841 N ND2  . ASN   A 1 87  ? 24.182 8.106   15.838  1.00 20.23 ?  87  ASN   A ND2  1 
ATOM   1842 H H    . ASN   A 1 87  ? 27.308 6.140   15.301  1.00 19.98 ?  87  ASN   A H    1 
ATOM   1843 H HA   . ASN   A 1 87  ? 26.886 5.243   17.771  1.00 21.25 ?  87  ASN   A HA   1 
ATOM   1844 H HB2  . ASN   A 1 87  ? 25.088 6.822   17.722  1.00 22.47 ?  87  ASN   A HB2  1 
ATOM   1845 H HB3  . ASN   A 1 87  ? 26.513 7.479   17.468  1.00 22.47 ?  87  ASN   A HB3  1 
ATOM   1846 H HD21 . ASN   A 1 87  ? 23.858 8.452   15.124  1.00 24.42 ?  87  ASN   A HD21 1 
ATOM   1847 H HD22 . ASN   A 1 87  ? 23.756 8.174   16.584  1.00 24.42 ?  87  ASN   A HD22 1 
ATOM   1848 N N    . LEU   A 1 88  ? 25.412 3.694   15.610  1.00 17.59 ?  88  LEU   A N    1 
ATOM   1849 C CA   . LEU   A 1 88  ? 24.308 2.825   15.216  1.00 17.39 ?  88  LEU   A CA   1 
ATOM   1850 C C    . LEU   A 1 88  ? 24.533 1.349   15.518  1.00 17.17 ?  88  LEU   A C    1 
ATOM   1851 O O    . LEU   A 1 88  ? 23.559 0.611   15.691  1.00 18.47 ?  88  LEU   A O    1 
ATOM   1852 C CB   . LEU   A 1 88  ? 24.045 2.980   13.718  1.00 18.06 ?  88  LEU   A CB   1 
ATOM   1853 C CG   . LEU   A 1 88  ? 23.756 4.402   13.234  1.00 19.84 ?  88  LEU   A CG   1 
ATOM   1854 C CD1  . LEU   A 1 88  ? 23.591 4.417   11.727  1.00 19.83 ?  88  LEU   A CD1  1 
ATOM   1855 C CD2  . LEU   A 1 88  ? 22.521 4.983   13.921  1.00 22.04 ?  88  LEU   A CD2  1 
ATOM   1856 H H    . LEU   A 1 88  ? 26.100 3.650   15.094  1.00 21.25 ?  88  LEU   A H    1 
ATOM   1857 H HA   . LEU   A 1 88  ? 23.513 3.108   15.688  1.00 21.02 ?  88  LEU   A HA   1 
ATOM   1858 H HB2  . LEU   A 1 88  ? 24.819 2.666   13.232  1.00 21.82 ?  88  LEU   A HB2  1 
ATOM   1859 H HB3  . LEU   A 1 88  ? 23.273 2.441   13.488  1.00 21.82 ?  88  LEU   A HB3  1 
ATOM   1860 H HG   . LEU   A 1 88  ? 24.511 4.971   13.450  1.00 23.95 ?  88  LEU   A HG   1 
ATOM   1861 H HD11 . LEU   A 1 88  ? 23.557 5.337   11.419  1.00 23.94 ?  88  LEU   A HD11 1 
ATOM   1862 H HD12 . LEU   A 1 88  ? 24.346 3.960   11.322  1.00 23.94 ?  88  LEU   A HD12 1 
ATOM   1863 H HD13 . LEU   A 1 88  ? 22.766 3.961   11.498  1.00 23.94 ?  88  LEU   A HD13 1 
ATOM   1864 H HD21 . LEU   A 1 88  ? 22.310 5.840   13.518  1.00 26.60 ?  88  LEU   A HD21 1 
ATOM   1865 H HD22 . LEU   A 1 88  ? 21.780 4.371   13.806  1.00 26.60 ?  88  LEU   A HD22 1 
ATOM   1866 H HD23 . LEU   A 1 88  ? 22.714 5.100   14.864  1.00 26.60 ?  88  LEU   A HD23 1 
ATOM   1867 N N    . ALA   A 1 89  ? 25.784 0.908   15.578  1.00 16.24 ?  89  ALA   A N    1 
ATOM   1868 C CA   . ALA   A 1 89  ? 26.133 -0.504  15.674  1.00 15.89 ?  89  ALA   A CA   1 
ATOM   1869 C C    . ALA   A 1 89  ? 27.619 -0.559  15.993  1.00 16.17 ?  89  ALA   A C    1 
ATOM   1870 O O    . ALA   A 1 89  ? 28.324 0.445   15.890  1.00 17.21 ?  89  ALA   A O    1 
ATOM   1871 C CB   . ALA   A 1 89  ? 25.859 -1.218  14.352  1.00 15.24 ?  89  ALA   A CB   1 
ATOM   1872 H H    . ALA   A 1 89  ? 26.468 1.426   15.561  1.00 19.64 ?  89  ALA   A H    1 
ATOM   1873 H HA   . ALA   A 1 89  ? 25.626 -0.928  16.388  1.00 19.22 ?  89  ALA   A HA   1 
ATOM   1874 H HB1  . ALA   A 1 89  ? 26.120 -2.150  14.438  1.00 18.43 ?  89  ALA   A HB1  1 
ATOM   1875 H HB2  . ALA   A 1 89  ? 24.911 -1.160  14.148  1.00 18.43 ?  89  ALA   A HB2  1 
ATOM   1876 H HB3  . ALA   A 1 89  ? 26.375 -0.794  13.651  1.00 18.43 ?  89  ALA   A HB3  1 
ATOM   1877 N N    . LYS   A 1 90  ? 28.105 -1.741  16.366  1.00 16.75 ?  90  LYS   A N    1 
ATOM   1878 C CA   . LYS   A 1 90  ? 29.549 -1.889  16.512  1.00 17.46 ?  90  LYS   A CA   1 
ATOM   1879 C C    . LYS   A 1 90  ? 30.246 -1.698  15.168  1.00 16.23 ?  90  LYS   A C    1 
ATOM   1880 O O    . LYS   A 1 90  ? 31.185 -0.894  15.044  1.00 17.91 ?  90  LYS   A O    1 
ATOM   1881 C CB   . LYS   A 1 90  ? 29.889 -3.246  17.129  1.00 20.41 ?  90  LYS   A CB   1 
ATOM   1882 C CG   . LYS   A 1 90  ? 31.374 -3.407  17.426  1.00 24.84 ?  90  LYS   A CG   1 
ATOM   1883 C CD   . LYS   A 1 90  ? 31.636 -4.615  18.309  1.00 29.75 ?  90  LYS   A CD   1 
ATOM   1884 C CE   . LYS   A 1 90  ? 33.061 -4.626  18.842  1.00 33.45 ?  90  LYS   A CE   1 
ATOM   1885 N NZ   . LYS   A 1 90  ? 34.056 -5.052  17.821  1.00 35.56 ?  90  LYS   A NZ   1 
ATOM   1886 H H    . LYS   A 1 90  ? 27.640 -2.443  16.528  1.00 20.25 ?  90  LYS   A H    1 
ATOM   1887 H HA   . LYS   A 1 90  ? 29.873 -1.200  17.110  1.00 21.10 ?  90  LYS   A HA   1 
ATOM   1888 H HB2  . LYS   A 1 90  ? 29.401 -3.339  17.967  1.00 24.64 ?  90  LYS   A HB2  1 
ATOM   1889 H HB3  . LYS   A 1 90  ? 29.624 -3.948  16.516  1.00 24.64 ?  90  LYS   A HB3  1 
ATOM   1890 H HG2  . LYS   A 1 90  ? 31.854 -3.527  16.593  1.00 29.96 ?  90  LYS   A HG2  1 
ATOM   1891 H HG3  . LYS   A 1 90  ? 31.693 -2.616  17.888  1.00 29.96 ?  90  LYS   A HG3  1 
ATOM   1892 H HD2  . LYS   A 1 90  ? 31.028 -4.597  19.066  1.00 35.85 ?  90  LYS   A HD2  1 
ATOM   1893 H HD3  . LYS   A 1 90  ? 31.498 -5.425  17.791  1.00 35.85 ?  90  LYS   A HD3  1 
ATOM   1894 H HE2  . LYS   A 1 90  ? 33.295 -3.731  19.134  1.00 40.29 ?  90  LYS   A HE2  1 
ATOM   1895 H HE3  . LYS   A 1 90  ? 33.113 -5.243  19.589  1.00 40.29 ?  90  LYS   A HE3  1 
ATOM   1896 H HZ1  . LYS   A 1 90  ? 34.869 -5.083  18.185  1.00 42.82 ?  90  LYS   A HZ1  1 
ATOM   1897 H HZ2  . LYS   A 1 90  ? 33.848 -5.861  17.512  1.00 42.82 ?  90  LYS   A HZ2  1 
ATOM   1898 H HZ3  . LYS   A 1 90  ? 34.064 -4.476  17.144  1.00 42.82 ?  90  LYS   A HZ3  1 
ATOM   1899 N N    . HIS   A 1 91  ? 29.771 -2.404  14.144  1.00 14.07 ?  91  HIS   A N    1 
ATOM   1900 C CA   . HIS   A 1 91  ? 30.339 -2.374  12.811  1.00 13.48 ?  91  HIS   A CA   1 
ATOM   1901 C C    . HIS   A 1 91  ? 29.251 -2.095  11.789  1.00 12.02 ?  91  HIS   A C    1 
ATOM   1902 O O    . HIS   A 1 91  ? 28.086 -2.469  11.976  1.00 13.30 ?  91  HIS   A O    1 
ATOM   1903 C CB   . HIS   A 1 91  ? 30.939 -3.743  12.439  1.00 16.33 ?  91  HIS   A CB   1 
ATOM   1904 C CG   . HIS   A 1 91  ? 31.929 -4.267  13.432  1.00 20.77 ?  91  HIS   A CG   1 
ATOM   1905 N ND1  . HIS   A 1 91  ? 33.210 -3.771  13.538  1.00 22.77 ?  91  HIS   A ND1  1 
ATOM   1906 C CD2  . HIS   A 1 91  ? 31.829 -5.253  14.354  1.00 22.57 ?  91  HIS   A CD2  1 
ATOM   1907 C CE1  . HIS   A 1 91  ? 33.857 -4.427  14.487  1.00 23.59 ?  91  HIS   A CE1  1 
ATOM   1908 N NE2  . HIS   A 1 91  ? 33.041 -5.332  14.998  1.00 23.98 ?  91  HIS   A NE2  1 
ATOM   1909 H H    . HIS   A 1 91  ? 29.096 -2.948  14.210  1.00 17.03 ?  91  HIS   A H    1 
ATOM   1910 H HA   . HIS   A 1 91  ? 31.031 -1.704  12.752  1.00 16.33 ?  91  HIS   A HA   1 
ATOM   1911 H HB2  . HIS   A 1 91  ? 30.222 -4.395  12.370  1.00 19.74 ?  91  HIS   A HB2  1 
ATOM   1912 H HB3  . HIS   A 1 91  ? 31.392 -3.667  11.584  1.00 19.74 ?  91  HIS   A HB3  1 
ATOM   1913 H HD1  . HIS   A 1 91  ? 33.538 -3.136  13.058  1.00 27.48 ?  91  HIS   A HD1  1 
ATOM   1914 H HD2  . HIS   A 1 91  ? 31.085 -5.780  14.523  1.00 27.23 ?  91  HIS   A HD2  1 
ATOM   1915 H HE1  . HIS   A 1 91  ? 34.739 -4.272  14.748  1.00 28.45 ?  91  HIS   A HE1  1 
ATOM   1916 N N    . CYS   A 1 92  ? 29.656 -1.496  10.673  1.00 11.97 ?  92  CYS   A N    1 
ATOM   1917 C CA   . CYS   A 1 92  ? 28.817 -1.417  9.486   1.00 12.14 ?  92  CYS   A CA   1 
ATOM   1918 C C    . CYS   A 1 92  ? 29.455 -2.235  8.376   1.00 11.72 ?  92  CYS   A C    1 
ATOM   1919 O O    . CYS   A 1 92  ? 30.608 -1.986  8.006   1.00 12.60 ?  92  CYS   A O    1 
ATOM   1920 C CB   . CYS   A 1 92  ? 28.604 0.029   9.030   1.00 12.92 ?  92  CYS   A CB   1 
ATOM   1921 S SG   . CYS   A 1 92  ? 27.576 0.140   7.530   1.00 12.35 ?  92  CYS   A SG   1 
ATOM   1922 H H    . CYS   A 1 92  ? 30.424 -1.108  10.587  1.00 14.52 ?  92  CYS   A H    1 
ATOM   1923 H HA   . CYS   A 1 92  ? 27.952 -1.799  9.685   1.00 14.71 ?  92  CYS   A HA   1 
ATOM   1924 H HB2  . CYS   A 1 92  ? 28.159 0.525   9.734   1.00 15.65 ?  92  CYS   A HB2  1 
ATOM   1925 H HB3  . CYS   A 1 92  ? 29.463 0.433   8.830   1.00 15.65 ?  92  CYS   A HB3  1 
ATOM   1926 H HG   . CYS   A 1 92  ? 27.436 1.297   7.236   1.00 14.97 ?  92  CYS   A HG   1 
ATOM   1927 N N    . LEU   A 1 93  ? 28.719 -3.219  7.873   1.00 11.37 ?  93  LEU   A N    1 
ATOM   1928 C CA   . LEU   A 1 93  ? 29.113 -3.978  6.691   1.00 10.80 ?  93  LEU   A CA   1 
ATOM   1929 C C    . LEU   A 1 93  ? 28.514 -3.283  5.471   1.00 10.72 ?  93  LEU   A C    1 
ATOM   1930 O O    . LEU   A 1 93  ? 27.293 -3.339  5.254   1.00 11.14 ?  93  LEU   A O    1 
ATOM   1931 C CB   . LEU   A 1 93  ? 28.628 -5.426  6.793   1.00 11.64 ?  93  LEU   A CB   1 
ATOM   1932 C CG   . LEU   A 1 93  ? 29.013 -6.319  5.613   1.00 11.98 ?  93  LEU   A CG   1 
ATOM   1933 C CD1  . LEU   A 1 93  ? 30.527 -6.579  5.609   1.00 13.09 ?  93  LEU   A CD1  1 
ATOM   1934 C CD2  . LEU   A 1 93  ? 28.241 -7.645  5.629   1.00 13.01 ?  93  LEU   A CD2  1 
ATOM   1935 H H    . LEU   A 1 93  ? 27.962 -3.465  8.207   1.00 13.80 ?  93  LEU   A H    1 
ATOM   1936 H HA   . LEU   A 1 93  ? 30.075 -3.975  6.616   1.00 13.11 ?  93  LEU   A HA   1 
ATOM   1937 H HB2  . LEU   A 1 93  ? 29.005 -5.821  7.599   1.00 14.11 ?  93  LEU   A HB2  1 
ATOM   1938 H HB3  . LEU   A 1 93  ? 27.661 -5.428  6.858   1.00 14.11 ?  93  LEU   A HB3  1 
ATOM   1939 H HG   . LEU   A 1 93  ? 28.799 -5.862  4.792   1.00 14.53 ?  93  LEU   A HG   1 
ATOM   1940 H HD11 . LEU   A 1 93  ? 30.748 -7.190  4.891   1.00 15.85 ?  93  LEU   A HD11 1 
ATOM   1941 H HD12 . LEU   A 1 93  ? 30.999 -5.739  5.484   1.00 15.85 ?  93  LEU   A HD12 1 
ATOM   1942 H HD13 . LEU   A 1 93  ? 30.788 -6.972  6.464   1.00 15.85 ?  93  LEU   A HD13 1 
ATOM   1943 H HD21 . LEU   A 1 93  ? 28.519 -8.180  4.865   1.00 15.76 ?  93  LEU   A HD21 1 
ATOM   1944 H HD22 . LEU   A 1 93  ? 28.437 -8.120  6.451   1.00 15.76 ?  93  LEU   A HD22 1 
ATOM   1945 H HD23 . LEU   A 1 93  ? 27.292 -7.457  5.571   1.00 15.76 ?  93  LEU   A HD23 1 
ATOM   1946 N N    . HIS   A 1 94  ? 29.360 -2.580  4.709   1.00 10.68 ?  94  HIS   A N    1 
ATOM   1947 C CA   . HIS   A 1 94  ? 28.938 -1.907  3.485   1.00 10.59 ?  94  HIS   A CA   1 
ATOM   1948 C C    . HIS   A 1 94  ? 28.943 -2.939  2.369   1.00 10.64 ?  94  HIS   A C    1 
ATOM   1949 O O    . HIS   A 1 94  ? 30.004 -3.467  2.024   1.00 12.24 ?  94  HIS   A O    1 
ATOM   1950 C CB   . HIS   A 1 94  ? 29.895 -0.764  3.158   1.00 10.64 ?  94  HIS   A CB   1 
ATOM   1951 C CG   . HIS   A 1 94  ? 29.887 0.328   4.175   1.00 10.77 ?  94  HIS   A CG   1 
ATOM   1952 N ND1  . HIS   A 1 94  ? 29.012 1.391   4.117   1.00 10.81 ?  94  HIS   A ND1  1 
ATOM   1953 C CD2  . HIS   A 1 94  ? 30.627 0.503   5.293   1.00 11.80 ?  94  HIS   A CD2  1 
ATOM   1954 C CE1  . HIS   A 1 94  ? 29.220 2.176   5.158   1.00 11.36 ?  94  HIS   A CE1  1 
ATOM   1955 N NE2  . HIS   A 1 94  ? 30.195 1.662   5.885   1.00 11.72 ?  94  HIS   A NE2  1 
ATOM   1956 H H    . HIS   A 1 94  ? 30.202 -2.482  4.884   1.00 12.97 ?  94  HIS   A H    1 
ATOM   1957 H HA   . HIS   A 1 94  ? 28.037 -1.555  3.595   1.00 12.85 ?  94  HIS   A HA   1 
ATOM   1958 H HB2  . HIS   A 1 94  ? 30.792 -1.111  3.104   1.00 12.91 ?  94  HIS   A HB2  1 
ATOM   1959 H HB3  . HIS   A 1 94  ? 29.634 -0.375  2.305   1.00 12.91 ?  94  HIS   A HB3  1 
ATOM   1960 H HD2  . HIS   A 1 94  ? 31.299 -0.053  5.600   1.00 14.31 ?  94  HIS   A HD2  1 
ATOM   1961 H HE1  . HIS   A 1 94  ? 28.751 2.962   5.343   1.00 13.78 ?  94  HIS   A HE1  1 
ATOM   1962 H HE2  . HIS   A 1 94  ? 30.506 2.004   6.608   1.00 14.22 ?  94  HIS   A HE2  1 
ATOM   1963 N N    . VAL   A 1 95  ? 27.766 -3.263  1.827   1.00 10.28 ?  95  VAL   A N    1 
ATOM   1964 C CA   . VAL   A 1 95  ? 27.619 -4.293  0.800   1.00 10.36 ?  95  VAL   A CA   1 
ATOM   1965 C C    . VAL   A 1 95  ? 27.072 -3.653  -0.466  1.00 9.78  ?  95  VAL   A C    1 
ATOM   1966 O O    . VAL   A 1 95  ? 26.069 -2.936  -0.414  1.00 11.00 ?  95  VAL   A O    1 
ATOM   1967 C CB   . VAL   A 1 95  ? 26.696 -5.440  1.254   1.00 11.19 ?  95  VAL   A CB   1 
ATOM   1968 C CG1  . VAL   A 1 95  ? 26.581 -6.477  0.149   1.00 12.12 ?  95  VAL   A CG1  1 
ATOM   1969 C CG2  . VAL   A 1 95  ? 27.206 -6.065  2.529   1.00 11.25 ?  95  VAL   A CG2  1 
ATOM   1970 H H    . VAL   A 1 95  ? 27.019 -2.894  2.048   1.00 12.48 ?  95  VAL   A H    1 
ATOM   1971 H HA   . VAL   A 1 95  ? 28.488 -4.668  0.597   1.00 12.58 ?  95  VAL   A HA   1 
ATOM   1972 H HB   . VAL   A 1 95  ? 25.811 -5.088  1.426   1.00 13.57 ?  95  VAL   A HB   1 
ATOM   1973 H HG11 . VAL   A 1 95  ? 26.194 -7.290  0.513   1.00 14.69 ?  95  VAL   A HG11 1 
ATOM   1974 H HG12 . VAL   A 1 95  ? 26.013 -6.134  -0.559  1.00 14.69 ?  95  VAL   A HG12 1 
ATOM   1975 H HG13 . VAL   A 1 95  ? 27.467 -6.670  -0.204  1.00 14.69 ?  95  VAL   A HG13 1 
ATOM   1976 H HG21 . VAL   A 1 95  ? 26.643 -6.824  2.754   1.00 13.65 ?  95  VAL   A HG21 1 
ATOM   1977 H HG22 . VAL   A 1 95  ? 28.119 -6.357  2.396   1.00 13.65 ?  95  VAL   A HG22 1 
ATOM   1978 H HG23 . VAL   A 1 95  ? 27.167 -5.405  3.239   1.00 13.65 ?  95  VAL   A HG23 1 
ATOM   1979 N N    . VAL   A 1 96  ? 27.703 -3.943  -1.604  1.00 10.18 ?  96  VAL   A N    1 
ATOM   1980 C CA   . VAL   A 1 96  ? 27.293 -3.389  -2.888  1.00 10.79 ?  96  VAL   A CA   1 
ATOM   1981 C C    . VAL   A 1 96  ? 26.486 -4.428  -3.658  1.00 11.63 ?  96  VAL   A C    1 
ATOM   1982 O O    . VAL   A 1 96  ? 27.049 -5.365  -4.228  1.00 12.29 ?  96  VAL   A O    1 
ATOM   1983 C CB   . VAL   A 1 96  ? 28.492 -2.915  -3.712  1.00 11.38 ?  96  VAL   A CB   1 
ATOM   1984 C CG1  . VAL   A 1 96  ? 27.987 -2.269  -4.985  1.00 11.54 ?  96  VAL   A CG1  1 
ATOM   1985 C CG2  . VAL   A 1 96  ? 29.358 -1.956  -2.908  1.00 12.25 ?  96  VAL   A CG2  1 
ATOM   1986 H H    . VAL   A 1 96  ? 28.390 -4.468  -1.652  1.00 12.36 ?  96  VAL   A H    1 
ATOM   1987 H HA   . VAL   A 1 96  ? 26.721 -2.627  -2.728  1.00 13.09 ?  96  VAL   A HA   1 
ATOM   1988 H HB   . VAL   A 1 96  ? 29.035 -3.676  -3.958  1.00 13.80 ?  96  VAL   A HB   1 
ATOM   1989 H HG11 . VAL   A 1 96  ? 28.721 -1.784  -5.401  1.00 14.00 ?  96  VAL   A HG11 1 
ATOM   1990 H HG12 . VAL   A 1 96  ? 27.663 -2.953  -5.585  1.00 14.00 ?  96  VAL   A HG12 1 
ATOM   1991 H HG13 . VAL   A 1 96  ? 27.273 -1.649  -4.764  1.00 14.00 ?  96  VAL   A HG13 1 
ATOM   1992 H HG21 . VAL   A 1 96  ? 30.055 -1.605  -3.479  1.00 14.85 ?  96  VAL   A HG21 1 
ATOM   1993 H HG22 . VAL   A 1 96  ? 28.802 -1.234  -2.575  1.00 14.85 ?  96  VAL   A HG22 1 
ATOM   1994 H HG23 . VAL   A 1 96  ? 29.750 -2.440  -2.162  1.00 14.85 ?  96  VAL   A HG23 1 
ATOM   1995 N N    A GLY   A 1 97  ? 25.167 -4.283  -3.665  0.86 11.55 ?  97  GLY   A N    1 
ATOM   1996 N N    B GLY   A 1 97  ? 25.172 -4.234  -3.729  0.14 11.88 ?  97  GLY   A N    1 
ATOM   1997 C CA   A GLY   A 1 97  ? 24.345 -5.035  -4.577  0.86 12.31 ?  97  GLY   A CA   1 
ATOM   1998 C CA   B GLY   A 1 97  ? 24.347 -5.008  -4.625  0.14 12.15 ?  97  GLY   A CA   1 
ATOM   1999 C C    A GLY   A 1 97  ? 24.335 -4.367  -5.938  0.86 12.07 ?  97  GLY   A C    1 
ATOM   2000 C C    B GLY   A 1 97  ? 24.425 -4.474  -6.043  0.14 12.33 ?  97  GLY   A C    1 
ATOM   2001 O O    A GLY   A 1 97  ? 24.622 -3.172  -6.061  0.86 13.08 ?  97  GLY   A O    1 
ATOM   2002 O O    B GLY   A 1 97  ? 24.798 -3.319  -6.271  0.14 12.34 ?  97  GLY   A O    1 
ATOM   2003 H H    A GLY   A 1 97  ? 24.726 -3.752  -3.142  0.86 14.01 ?  97  GLY   A H    1 
ATOM   2004 H H    B GLY   A 1 97  ? 24.737 -3.656  -3.260  0.14 14.40 ?  97  GLY   A H    1 
ATOM   2005 H HA2  A GLY   A 1 97  ? 24.699 -5.933  -4.660  0.86 14.93 ?  97  GLY   A HA2  1 
ATOM   2006 H HA2  B GLY   A 1 97  ? 24.645 -5.931  -4.614  0.14 14.73 ?  97  GLY   A HA2  1 
ATOM   2007 H HA3  A GLY   A 1 97  ? 23.437 -5.083  -4.242  0.86 14.93 ?  97  GLY   A HA3  1 
ATOM   2008 H HA3  B GLY   A 1 97  ? 23.423 -4.976  -4.331  0.14 14.73 ?  97  GLY   A HA3  1 
ATOM   2009 N N    A PRO   A 1 98  ? 24.007 -5.114  -6.989  0.86 12.13 ?  98  PRO   A N    1 
ATOM   2010 N N    B PRO   A 1 98  ? 24.082 -5.302  -7.028  0.14 12.65 ?  98  PRO   A N    1 
ATOM   2011 C CA   A PRO   A 1 98  ? 23.886 -4.497  -8.314  0.86 12.91 ?  98  PRO   A CA   1 
ATOM   2012 C CA   B PRO   A 1 98  ? 24.108 -4.835  -8.421  0.14 13.02 ?  98  PRO   A CA   1 
ATOM   2013 C C    A PRO   A 1 98  ? 22.771 -3.460  -8.347  0.86 13.49 ?  98  PRO   A C    1 
ATOM   2014 C C    B PRO   A 1 98  ? 23.046 -3.779  -8.689  0.14 13.30 ?  98  PRO   A C    1 
ATOM   2015 O O    A PRO   A 1 98  ? 21.699 -3.646  -7.763  0.86 13.47 ?  98  PRO   A O    1 
ATOM   2016 O O    B PRO   A 1 98  ? 21.910 -3.877  -8.217  0.14 13.64 ?  98  PRO   A O    1 
ATOM   2017 C CB   A PRO   A 1 98  ? 23.576 -5.690  -9.230  0.86 13.44 ?  98  PRO   A CB   1 
ATOM   2018 C CB   B PRO   A 1 98  ? 23.837 -6.109  -9.229  0.14 12.73 ?  98  PRO   A CB   1 
ATOM   2019 C CG   A PRO   A 1 98  ? 22.935 -6.701  -8.325  0.86 13.57 ?  98  PRO   A CG   1 
ATOM   2020 C CG   B PRO   A 1 98  ? 23.152 -7.031  -8.272  0.14 12.82 ?  98  PRO   A CG   1 
ATOM   2021 C CD   A PRO   A 1 98  ? 23.679 -6.550  -7.014  0.86 12.65 ?  98  PRO   A CD   1 
ATOM   2022 C CD   B PRO   A 1 98  ? 23.772 -6.739  -6.938  0.14 12.66 ?  98  PRO   A CD   1 
ATOM   2023 H HA   A PRO   A 1 98  ? 24.730 -4.093  -8.576  0.86 15.64 ?  98  PRO   A HA   1 
ATOM   2024 H HA   B PRO   A 1 98  ? 24.983 -4.482  -8.648  0.14 15.77 ?  98  PRO   A HA   1 
ATOM   2025 H HB2  A PRO   A 1 98  ? 22.963 -5.411  -9.926  0.86 16.28 ?  98  PRO   A HB2  1 
ATOM   2026 H HB2  B PRO   A 1 98  ? 23.260 -5.900  -9.981  0.14 15.43 ?  98  PRO   A HB2  1 
ATOM   2027 H HB3  A PRO   A 1 98  ? 24.397 -6.038  -9.608  0.86 16.28 ?  98  PRO   A HB3  1 
ATOM   2028 H HB3  B PRO   A 1 98  ? 24.676 -6.487  -9.533  0.14 15.43 ?  98  PRO   A HB3  1 
ATOM   2029 H HG2  A PRO   A 1 98  ? 21.993 -6.491  -8.213  0.86 16.43 ?  98  PRO   A HG2  1 
ATOM   2030 H HG2  B PRO   A 1 98  ? 22.200 -6.837  -8.258  0.14 15.54 ?  98  PRO   A HG2  1 
ATOM   2031 H HG3  A PRO   A 1 98  ? 23.051 -7.590  -8.689  0.86 16.43 ?  98  PRO   A HG3  1 
ATOM   2032 H HG3  B PRO   A 1 98  ? 23.312 -7.949  -8.534  0.14 15.54 ?  98  PRO   A HG3  1 
ATOM   2033 H HD2  A PRO   A 1 98  ? 23.101 -6.782  -6.266  0.86 15.33 ?  98  PRO   A HD2  1 
ATOM   2034 H HD2  B PRO   A 1 98  ? 23.139 -6.908  -6.223  0.14 15.33 ?  98  PRO   A HD2  1 
ATOM   2035 H HD3  A PRO   A 1 98  ? 24.487 -7.087  -7.015  0.86 15.33 ?  98  PRO   A HD3  1 
ATOM   2036 H HD3  B PRO   A 1 98  ? 24.586 -7.255  -6.822  0.14 15.33 ?  98  PRO   A HD3  1 
ATOM   2037 N N    A ASN   A 1 99  ? 23.043 -2.352  -9.040  0.86 14.15 ?  99  ASN   A N    1 
ATOM   2038 N N    B ASN   A 1 99  ? 23.427 -2.765  -9.465  0.14 13.23 ?  99  ASN   A N    1 
ATOM   2039 C CA   A ASN   A 1 99  ? 22.066 -1.291  -9.263  0.86 14.98 ?  99  ASN   A CA   1 
ATOM   2040 C CA   B ASN   A 1 99  ? 22.520 -1.689  -9.853  0.14 13.63 ?  99  ASN   A CA   1 
ATOM   2041 C C    A ASN   A 1 99  ? 21.495 -1.465  -10.668 0.86 16.60 ?  99  ASN   A C    1 
ATOM   2042 C C    B ASN   A 1 99  ? 21.894 -2.037  -11.199 0.14 14.05 ?  99  ASN   A C    1 
ATOM   2043 O O    A ASN   A 1 99  ? 22.189 -1.234  -11.664 0.86 18.39 ?  99  ASN   A O    1 
ATOM   2044 O O    B ASN   A 1 99  ? 22.560 -1.973  -12.237 0.14 13.54 ?  99  ASN   A O    1 
ATOM   2045 C CB   A ASN   A 1 99  ? 22.716 0.082   -9.089  0.86 15.54 ?  99  ASN   A CB   1 
ATOM   2046 C CB   B ASN   A 1 99  ? 23.267 -0.362  -9.948  0.14 13.39 ?  99  ASN   A CB   1 
ATOM   2047 C CG   A ASN   A 1 99  ? 21.697 1.228   -9.087  0.86 16.61 ?  99  ASN   A CG   1 
ATOM   2048 C CG   B ASN   A 1 99  ? 22.334 0.817   -10.163 0.14 13.69 ?  99  ASN   A CG   1 
ATOM   2049 O OD1  A ASN   A 1 99  ? 20.684 1.182   -9.789  0.86 17.50 ?  99  ASN   A OD1  1 
ATOM   2050 O OD1  B ASN   A 1 99  ? 21.214 0.656   -10.644 0.14 13.35 ?  99  ASN   A OD1  1 
ATOM   2051 N ND2  A ASN   A 1 99  ? 21.977 2.266   -8.300  0.86 17.34 ?  99  ASN   A ND2  1 
ATOM   2052 N ND2  B ASN   A 1 99  ? 22.795 2.010   -9.809  0.14 14.32 ?  99  ASN   A ND2  1 
ATOM   2053 H H    A ASN   A 1 99  ? 23.817 -2.186  -9.378  0.86 17.12 ?  99  ASN   A H    1 
ATOM   2054 H H    B ASN   A 1 99  ? 24.223 -2.674  -9.775  0.14 16.03 ?  99  ASN   A H    1 
ATOM   2055 H HA   A ASN   A 1 99  ? 21.346 -1.378  -8.613  0.86 18.12 ?  99  ASN   A HA   1 
ATOM   2056 H HA   B ASN   A 1 99  ? 21.811 -1.604  -9.197  0.14 16.51 ?  99  ASN   A HA   1 
ATOM   2057 H HB2  A ASN   A 1 99  ? 23.198 0.104   -8.246  0.86 18.80 ?  99  ASN   A HB2  1 
ATOM   2058 H HB2  B ASN   A 1 99  ? 23.756 -0.216  -9.128  0.14 16.22 ?  99  ASN   A HB2  1 
ATOM   2059 H HB3  A ASN   A 1 99  ? 23.331 0.232   -9.824  0.86 18.80 ?  99  ASN   A HB3  1 
ATOM   2060 H HB3  B ASN   A 1 99  ? 23.881 -0.401  -10.701 0.14 16.22 ?  99  ASN   A HB3  1 
ATOM   2061 H HD21 A ASN   A 1 99  ? 21.439 2.934   -8.259  0.86 20.96 ?  99  ASN   A HD21 1 
ATOM   2062 H HD21 B ASN   A 1 99  ? 22.314 2.711   -9.916  0.14 17.33 ?  99  ASN   A HD21 1 
ATOM   2063 H HD22 A ASN   A 1 99  ? 22.696 2.264   -7.825  0.86 20.96 ?  99  ASN   A HD22 1 
ATOM   2064 H HD22 B ASN   A 1 99  ? 23.583 2.085   -9.487  0.14 17.33 ?  99  ASN   A HD22 1 
ATOM   2065 N N    A VAL   A 1 100 ? 20.228 -1.884  -10.740 0.86 17.23 ?  100 VAL   A N    1 
ATOM   2066 N N    B VAL   A 1 100 ? 20.605 -2.379  -11.181 0.14 15.40 ?  100 VAL   A N    1 
ATOM   2067 C CA   A VAL   A 1 100 ? 19.584 -2.118  -12.028 0.86 19.42 ?  100 VAL   A CA   1 
ATOM   2068 C CA   B VAL   A 1 100 ? 19.920 -2.760  -12.412 0.14 16.98 ?  100 VAL   A CA   1 
ATOM   2069 C C    A VAL   A 1 100 ? 19.485 -0.823  -12.821 0.86 20.55 ?  100 VAL   A C    1 
ATOM   2070 C C    B VAL   A 1 100 ? 19.852 -1.589  -13.380 0.14 17.69 ?  100 VAL   A C    1 
ATOM   2071 O O    A VAL   A 1 100 ? 19.549 -0.832  -14.056 0.86 21.67 ?  100 VAL   A O    1 
ATOM   2072 O O    B VAL   A 1 100 ? 19.824 -1.784  -14.602 0.14 17.54 ?  100 VAL   A O    1 
ATOM   2073 C CB   A VAL   A 1 100 ? 18.211 -2.794  -11.819 0.86 21.18 ?  100 VAL   A CB   1 
ATOM   2074 C CB   B VAL   A 1 100 ? 18.523 -3.320  -12.088 0.14 17.72 ?  100 VAL   A CB   1 
ATOM   2075 C CG1  A VAL   A 1 100 ? 17.475 -2.970  -13.143 0.86 21.91 ?  100 VAL   A CG1  1 
ATOM   2076 C CG1  B VAL   A 1 100 ? 17.887 -3.915  -13.333 0.14 17.85 ?  100 VAL   A CG1  1 
ATOM   2077 C CG2  A VAL   A 1 100 ? 18.391 -4.138  -11.129 0.86 22.06 ?  100 VAL   A CG2  1 
ATOM   2078 C CG2  B VAL   A 1 100 ? 18.618 -4.355  -10.979 0.14 18.08 ?  100 VAL   A CG2  1 
ATOM   2079 H H    A VAL   A 1 100 ? 19.722 -2.038  -10.055 0.86 20.83 ?  100 VAL   A H    1 
ATOM   2080 H H    B VAL   A 1 100 ? 20.111 -2.392  -10.477 0.14 18.62 ?  100 VAL   A H    1 
ATOM   2081 H HA   A VAL   A 1 100 ? 20.130 -2.729  -12.541 0.86 23.45 ?  100 VAL   A HA   1 
ATOM   2082 H HA   B VAL   A 1 100 ? 20.424 -3.466  -12.844 0.14 20.53 ?  100 VAL   A HA   1 
ATOM   2083 H HB   A VAL   A 1 100 ? 17.665 -2.236  -11.245 0.86 25.57 ?  100 VAL   A HB   1 
ATOM   2084 H HB   B VAL   A 1 100 ? 17.956 -2.596  -11.778 0.14 21.41 ?  100 VAL   A HB   1 
ATOM   2085 H HG11 A VAL   A 1 100 ? 16.711 -3.555  -13.005 0.86 26.43 ?  100 VAL   A HG11 1 
ATOM   2086 H HG11 B VAL   A 1 100 ? 17.042 -4.324  -13.090 0.14 21.57 ?  100 VAL   A HG11 1 
ATOM   2087 H HG12 A VAL   A 1 100 ? 17.171 -2.104  -13.457 0.86 26.43 ?  100 VAL   A HG12 1 
ATOM   2088 H HG12 B VAL   A 1 100 ? 17.738 -3.210  -13.982 0.14 21.57 ?  100 VAL   A HG12 1 
ATOM   2089 H HG13 A VAL   A 1 100 ? 18.078 -3.366  -13.791 0.86 26.43 ?  100 VAL   A HG13 1 
ATOM   2090 H HG13 B VAL   A 1 100 ? 18.484 -4.585  -13.702 0.14 21.57 ?  100 VAL   A HG13 1 
ATOM   2091 H HG21 A VAL   A 1 100 ? 17.530 -4.577  -11.062 0.86 26.61 ?  100 VAL   A HG21 1 
ATOM   2092 H HG21 B VAL   A 1 100 ? 17.799 -4.871  -10.960 0.14 21.85 ?  100 VAL   A HG21 1 
ATOM   2093 H HG22 A VAL   A 1 100 ? 19.001 -4.682  -11.653 0.86 26.61 ?  100 VAL   A HG22 1 
ATOM   2094 H HG22 B VAL   A 1 100 ? 19.374 -4.935  -11.157 0.14 21.85 ?  100 VAL   A HG22 1 
ATOM   2095 H HG23 A VAL   A 1 100 ? 18.759 -3.992  -10.243 0.86 26.61 ?  100 VAL   A HG23 1 
ATOM   2096 H HG23 B VAL   A 1 100 ? 18.743 -3.900  -10.132 0.14 21.85 ?  100 VAL   A HG23 1 
ATOM   2097 N N    A ASN   A 1 101 ? 19.332 0.307   -12.136 0.86 21.45 ?  101 ASN   A N    1 
ATOM   2098 N N    B ASN   A 1 101 ? 19.814 -0.359  -12.860 0.14 18.48 ?  101 ASN   A N    1 
ATOM   2099 C CA   A ASN   A 1 101 ? 19.278 1.591   -12.826 0.86 23.08 ?  101 ASN   A CA   1 
ATOM   2100 C CA   B ASN   A 1 101 ? 19.769 0.812   -13.732 0.14 19.35 ?  101 ASN   A CA   1 
ATOM   2101 C C    A ASN   A 1 101 ? 20.636 2.024   -13.383 0.86 25.26 ?  101 ASN   A C    1 
ATOM   2102 C C    B ASN   A 1 101 ? 21.105 1.061   -14.423 0.14 20.66 ?  101 ASN   A C    1 
ATOM   2103 O O    A ASN   A 1 101 ? 20.705 3.063   -14.052 0.86 27.40 ?  101 ASN   A O    1 
ATOM   2104 O O    B ASN   A 1 101 ? 21.136 1.670   -15.498 0.14 20.63 ?  101 ASN   A O    1 
ATOM   2105 C CB   A ASN   A 1 101 ? 18.656 2.637   -11.898 0.86 23.00 ?  101 ASN   A CB   1 
ATOM   2106 C CB   B ASN   A 1 101 ? 19.324 2.041   -12.938 0.14 19.08 ?  101 ASN   A CB   1 
ATOM   2107 C CG   A ASN   A 1 101 ? 17.284 2.209   -11.389 0.86 22.73 ?  101 ASN   A CG   1 
ATOM   2108 C CG   B ASN   A 1 101 ? 18.029 1.807   -12.187 0.14 19.07 ?  101 ASN   A CG   1 
ATOM   2109 O OD1  A ASN   A 1 101 ? 16.460 1.697   -12.152 0.86 23.03 ?  101 ASN   A OD1  1 
ATOM   2110 O OD1  B ASN   A 1 101 ? 17.195 1.000   -12.599 0.14 19.42 ?  101 ASN   A OD1  1 
ATOM   2111 N ND2  A ASN   A 1 101 ? 17.043 2.391   -10.093 0.86 22.49 ?  101 ASN   A ND2  1 
ATOM   2112 N ND2  B ASN   A 1 101 ? 17.857 2.507   -11.072 0.14 18.88 ?  101 ASN   A ND2  1 
ATOM   2113 H H    A ASN   A 1 101 ? 19.250 0.357   -11.281 0.86 25.89 ?  101 ASN   A H    1 
ATOM   2114 H H    B ASN   A 1 101 ? 19.796 -0.178  -12.020 0.14 22.33 ?  101 ASN   A H    1 
ATOM   2115 H HA   A ASN   A 1 101 ? 18.685 1.500   -13.583 0.86 27.84 ?  101 ASN   A HA   1 
ATOM   2116 H HA   B ASN   A 1 101 ? 19.112 0.659   -14.424 0.14 23.37 ?  101 ASN   A HA   1 
ATOM   2117 H HB2  A ASN   A 1 101 ? 19.233 2.774   -11.131 0.86 27.74 ?  101 ASN   A HB2  1 
ATOM   2118 H HB2  B ASN   A 1 101 ? 20.008 2.271   -12.291 0.14 23.04 ?  101 ASN   A HB2  1 
ATOM   2119 H HB3  A ASN   A 1 101 ? 18.548 3.472   -12.385 0.86 27.74 ?  101 ASN   A HB3  1 
ATOM   2120 H HB3  B ASN   A 1 101 ? 19.184 2.781   -13.552 0.14 23.04 ?  101 ASN   A HB3  1 
ATOM   2121 H HD21 A ASN   A 1 101 ? 16.282 2.166   -9.760  0.86 27.14 ?  101 ASN   A HD21 1 
ATOM   2122 H HD21 B ASN   A 1 101 ? 17.138 2.412   -10.610 0.14 22.81 ?  101 ASN   A HD21 1 
ATOM   2123 H HD22 A ASN   A 1 101 ? 17.641 2.750   -9.589  0.86 27.14 ?  101 ASN   A HD22 1 
ATOM   2124 H HD22 B ASN   A 1 101 ? 18.462 3.062   -10.815 0.14 22.81 ?  101 ASN   A HD22 1 
ATOM   2125 N N    A LYS   A 1 102 ? 21.696 1.242   -13.149 0.86 26.76 ?  102 LYS   A N    1 
ATOM   2126 N N    B LYS   A 1 102 ? 22.210 0.608   -13.833 0.14 21.98 ?  102 LYS   A N    1 
ATOM   2127 C CA   A LYS   A 1 102 ? 22.984 1.418   -13.809 0.86 27.82 ?  102 LYS   A CA   1 
ATOM   2128 C CA   B LYS   A 1 102 ? 23.517 0.681   -14.473 0.14 23.07 ?  102 LYS   A CA   1 
ATOM   2129 C C    A LYS   A 1 102 ? 23.294 0.298   -14.793 0.86 28.46 ?  102 LYS   A C    1 
ATOM   2130 C C    B LYS   A 1 102 ? 23.786 -0.511  -15.384 0.14 23.25 ?  102 LYS   A C    1 
ATOM   2131 O O    A LYS   A 1 102 ? 24.377 0.297   -15.386 0.86 29.57 ?  102 LYS   A O    1 
ATOM   2132 O O    B LYS   A 1 102 ? 24.916 -0.676  -15.852 0.14 23.11 ?  102 LYS   A O    1 
ATOM   2133 C CB   A LYS   A 1 102 ? 24.119 1.486   -12.778 0.86 28.97 ?  102 LYS   A CB   1 
ATOM   2134 C CB   B LYS   A 1 102 ? 24.634 0.769   -13.427 0.14 23.84 ?  102 LYS   A CB   1 
ATOM   2135 C CG   A LYS   A 1 102 ? 24.001 2.606   -11.765 0.86 29.88 ?  102 LYS   A CG   1 
ATOM   2136 C CG   B LYS   A 1 102 ? 24.645 2.030   -12.578 0.14 24.66 ?  102 LYS   A CG   1 
ATOM   2137 C CD   A LYS   A 1 102 ? 25.187 2.585   -10.805 0.86 31.13 ?  102 LYS   A CD   1 
ATOM   2138 C CD   B LYS   A 1 102 ? 26.026 2.237   -11.962 0.14 25.44 ?  102 LYS   A CD   1 
ATOM   2139 C CE   A LYS   A 1 102 ? 25.094 3.686   -9.758  0.86 32.37 ?  102 LYS   A CE   1 
ATOM   2140 C CE   B LYS   A 1 102 ? 25.971 3.025   -10.662 0.14 26.10 ?  102 LYS   A CE   1 
ATOM   2141 N NZ   A LYS   A 1 102 ? 26.211 3.603   -8.770  0.86 32.85 ?  102 LYS   A NZ   1 
ATOM   2142 N NZ   B LYS   A 1 102 ? 25.717 2.143   -9.489  0.14 26.44 ?  102 LYS   A NZ   1 
ATOM   2143 H H    A LYS   A 1 102 ? 21.688 0.574   -12.605 0.86 32.26 ?  102 LYS   A H    1 
ATOM   2144 H H    B LYS   A 1 102 ? 22.227 0.245   -13.054 0.14 26.52 ?  102 LYS   A H    1 
ATOM   2145 H HA   A LYS   A 1 102 ? 22.977 2.256   -14.294 0.86 33.53 ?  102 LYS   A HA   1 
ATOM   2146 H HA   B LYS   A 1 102 ? 23.557 1.488   -15.011 0.14 27.84 ?  102 LYS   A HA   1 
ATOM   2147 H HB2  A LYS   A 1 102 ? 24.141 0.648   -12.289 0.86 34.91 ?  102 LYS   A HB2  1 
ATOM   2148 H HB2  B LYS   A 1 102 ? 24.552 0.014   -12.826 0.14 28.75 ?  102 LYS   A HB2  1 
ATOM   2149 H HB3  A LYS   A 1 102 ? 24.958 1.607   -13.251 0.86 34.91 ?  102 LYS   A HB3  1 
ATOM   2150 H HB3  B LYS   A 1 102 ? 25.488 0.727   -13.885 0.14 28.75 ?  102 LYS   A HB3  1 
ATOM   2151 H HG2  A LYS   A 1 102 ? 23.990 3.458   -12.227 0.86 36.01 ?  102 LYS   A HG2  1 
ATOM   2152 H HG2  B LYS   A 1 102 ? 24.437 2.799   -13.130 0.14 29.73 ?  102 LYS   A HG2  1 
ATOM   2153 H HG3  A LYS   A 1 102 ? 23.186 2.488   -11.251 0.86 36.01 ?  102 LYS   A HG3  1 
ATOM   2154 H HG3  B LYS   A 1 102 ? 23.998 1.945   -11.865 0.14 29.73 ?  102 LYS   A HG3  1 
ATOM   2155 H HD2  A LYS   A 1 102 ? 25.211 1.731   -10.346 0.86 37.50 ?  102 LYS   A HD2  1 
ATOM   2156 H HD2  B LYS   A 1 102 ? 26.421 1.372   -11.772 0.14 30.67 ?  102 LYS   A HD2  1 
ATOM   2157 H HD3  A LYS   A 1 102 ? 26.006 2.716   -11.310 0.86 37.50 ?  102 LYS   A HD3  1 
ATOM   2158 H HD3  B LYS   A 1 102 ? 26.581 2.727   -12.587 0.14 30.67 ?  102 LYS   A HD3  1 
ATOM   2159 H HE2  A LYS   A 1 102 ? 25.141 4.550   -10.198 0.86 39.00 ?  102 LYS   A HE2  1 
ATOM   2160 H HE2  B LYS   A 1 102 ? 26.822 3.470   -10.522 0.14 31.47 ?  102 LYS   A HE2  1 
ATOM   2161 H HE3  A LYS   A 1 102 ? 24.255 3.600   -9.278  0.86 39.00 ?  102 LYS   A HE3  1 
ATOM   2162 H HE3  B LYS   A 1 102 ? 25.257 3.678   -10.713 0.14 31.47 ?  102 LYS   A HE3  1 
ATOM   2163 H HZ1  A LYS   A 1 102 ? 26.134 4.254   -8.169  0.86 39.56 ?  102 LYS   A HZ1  1 
ATOM   2164 H HZ1  B LYS   A 1 102 ? 25.256 2.587   -8.866  0.14 31.88 ?  102 LYS   A HZ1  1 
ATOM   2165 H HZ2  A LYS   A 1 102 ? 26.186 2.818   -8.350  0.86 39.56 ?  102 LYS   A HZ2  1 
ATOM   2166 H HZ2  B LYS   A 1 102 ? 25.247 1.428   -9.742  0.14 31.88 ?  102 LYS   A HZ2  1 
ATOM   2167 H HZ3  A LYS   A 1 102 ? 26.992 3.683   -9.187  0.86 39.56 ?  102 LYS   A HZ3  1 
ATOM   2168 H HZ3  B LYS   A 1 102 ? 26.484 1.870   -9.140  0.14 31.88 ?  102 LYS   A HZ3  1 
ATOM   2169 N N    A GLY   A 1 103 ? 22.396 -0.671  -14.957 0.86 28.96 ?  103 GLY   A N    1 
ATOM   2170 N N    B GLY   A 1 103 ? 22.780 -1.346  -15.638 0.14 23.61 ?  103 GLY   A N    1 
ATOM   2171 C CA   A GLY   A 1 103 ? 22.613 -1.761  -15.890 0.86 28.99 ?  103 GLY   A CA   1 
ATOM   2172 C CA   B GLY   A 1 103 ? 22.991 -2.538  -16.434 0.14 24.07 ?  103 GLY   A CA   1 
ATOM   2173 C C    A GLY   A 1 103 ? 23.441 -2.912  -15.367 0.86 29.27 ?  103 GLY   A C    1 
ATOM   2174 C C    B GLY   A 1 103 ? 23.839 -3.597  -15.775 0.14 24.36 ?  103 GLY   A C    1 
ATOM   2175 O O    A GLY   A 1 103 ? 23.968 -3.689  -16.167 0.86 30.57 ?  103 GLY   A O    1 
ATOM   2176 O O    B GLY   A 1 103 ? 24.421 -4.434  -16.471 0.14 24.50 ?  103 GLY   A O    1 
ATOM   2177 H H    A GLY   A 1 103 ? 21.656 -0.720  -14.533 0.86 34.90 ?  103 GLY   A H    1 
ATOM   2178 H H    B GLY   A 1 103 ? 21.971 -1.233  -15.370 0.14 28.47 ?  103 GLY   A H    1 
ATOM   2179 H HA2  A GLY   A 1 103 ? 21.752 -2.115  -16.164 0.86 34.93 ?  103 GLY   A HA2  1 
ATOM   2180 H HA2  B GLY   A 1 103 ? 22.137 -2.932  -16.667 0.14 29.03 ?  103 GLY   A HA2  1 
ATOM   2181 H HA3  A GLY   A 1 103 ? 23.058 -1.418  -16.682 0.86 34.93 ?  103 GLY   A HA3  1 
ATOM   2182 H HA3  B GLY   A 1 103 ? 23.444 -2.285  -17.246 0.14 29.03 ?  103 GLY   A HA3  1 
ATOM   2183 N N    A GLU   A 1 104 ? 23.565 -3.061  -14.051 0.86 27.21 ?  104 GLU   A N    1 
ATOM   2184 N N    B GLU   A 1 104 ? 23.924 -3.592  -14.451 0.14 24.27 ?  104 GLU   A N    1 
ATOM   2185 C CA   A GLU   A 1 104 ? 24.453 -4.062  -13.475 0.86 25.57 ?  104 GLU   A CA   1 
ATOM   2186 C CA   B GLU   A 1 104 ? 24.812 -4.496  -13.738 0.14 24.22 ?  104 GLU   A CA   1 
ATOM   2187 C C    A GLU   A 1 104 ? 23.770 -5.426  -13.372 0.86 25.53 ?  104 GLU   A C    1 
ATOM   2188 C C    B GLU   A 1 104 ? 24.118 -5.826  -13.466 0.14 24.71 ?  104 GLU   A C    1 
ATOM   2189 O O    A GLU   A 1 104 ? 22.549 -5.528  -13.225 0.86 25.89 ?  104 GLU   A O    1 
ATOM   2190 O O    B GLU   A 1 104 ? 22.930 -5.872  -13.134 0.14 24.53 ?  104 GLU   A O    1 
ATOM   2191 C CB   A GLU   A 1 104 ? 24.979 -3.581  -12.118 0.86 23.80 ?  104 GLU   A CB   1 
ATOM   2192 C CB   B GLU   A 1 104 ? 25.299 -3.848  -12.441 0.14 23.87 ?  104 GLU   A CB   1 
ATOM   2193 C CG   A GLU   A 1 104 ? 25.863 -2.338  -12.280 0.86 23.47 ?  104 GLU   A CG   1 
ATOM   2194 C CG   B GLU   A 1 104 ? 26.174 -2.623  -12.689 0.14 23.65 ?  104 GLU   A CG   1 
ATOM   2195 C CD   A GLU   A 1 104 ? 26.213 -1.601  -10.992 0.86 22.52 ?  104 GLU   A CD   1 
ATOM   2196 C CD   B GLU   A 1 104 ? 26.575 -1.913  -11.410 0.14 23.43 ?  104 GLU   A CD   1 
ATOM   2197 O OE1  A GLU   A 1 104 ? 25.643 -1.896  -9.922  0.86 21.02 ?  104 GLU   A OE1  1 
ATOM   2198 O OE1  B GLU   A 1 104 ? 26.017 -2.241  -10.343 0.14 23.40 ?  104 GLU   A OE1  1 
ATOM   2199 O OE2  A GLU   A 1 104 ? 27.070 -0.689  -11.074 0.86 23.39 -1 104 GLU   A OE2  1 
ATOM   2200 O OE2  B GLU   A 1 104 ? 27.455 -1.028  -11.474 0.14 23.32 -1 104 GLU   A OE2  1 
ATOM   2201 H H    A GLU   A 1 104 ? 23.144 -2.586  -13.468 0.86 32.80 ?  104 GLU   A H    1 
ATOM   2202 H H    B GLU   A 1 104 ? 23.468 -3.068  -13.945 0.14 29.27 ?  104 GLU   A H    1 
ATOM   2203 H HA   A GLU   A 1 104 ? 25.214 -4.164  -14.064 0.86 30.83 ?  104 GLU   A HA   1 
ATOM   2204 H HA   B GLU   A 1 104 ? 25.590 -4.670  -14.289 0.14 29.22 ?  104 GLU   A HA   1 
ATOM   2205 H HB2  A GLU   A 1 104 ? 24.229 -3.357  -11.547 0.86 28.71 ?  104 GLU   A HB2  1 
ATOM   2206 H HB2  B GLU   A 1 104 ? 24.535 -3.566  -11.916 0.14 28.79 ?  104 GLU   A HB2  1 
ATOM   2207 H HB3  A GLU   A 1 104 ? 25.510 -4.288  -11.718 0.86 28.71 ?  104 GLU   A HB3  1 
ATOM   2208 H HB3  B GLU   A 1 104 ? 25.827 -4.492  -11.943 0.14 28.79 ?  104 GLU   A HB3  1 
ATOM   2209 H HG2  A GLU   A 1 104 ? 26.695 -2.608  -12.695 0.86 28.31 ?  104 GLU   A HG2  1 
ATOM   2210 H HG2  B GLU   A 1 104 ? 26.988 -2.900  -13.141 0.14 28.53 ?  104 GLU   A HG2  1 
ATOM   2211 H HG3  A GLU   A 1 104 ? 25.401 -1.707  -12.851 0.86 28.31 ?  104 GLU   A HG3  1 
ATOM   2212 H HG3  B GLU   A 1 104 ? 25.688 -1.994  -13.249 0.14 28.53 ?  104 GLU   A HG3  1 
ATOM   2213 N N    A ASP   A 1 105 ? 24.587 -6.476  -13.446 0.86 26.32 ?  105 ASP   A N    1 
ATOM   2214 N N    B ASP   A 1 105 ? 24.880 -6.906  -13.621 0.14 25.60 ?  105 ASP   A N    1 
ATOM   2215 C CA   A ASP   A 1 105 ? 24.101 -7.845  -13.596 0.86 27.59 ?  105 ASP   A CA   1 
ATOM   2216 C CA   B ASP   A 1 105 ? 24.357 -8.266  -13.586 0.14 26.52 ?  105 ASP   A CA   1 
ATOM   2217 C C    A ASP   A 1 105 ? 23.426 -8.323  -12.314 0.86 25.33 ?  105 ASP   A C    1 
ATOM   2218 C C    B ASP   A 1 105 ? 23.577 -8.535  -12.306 0.14 26.26 ?  105 ASP   A C    1 
ATOM   2219 O O    A ASP   A 1 105 ? 24.063 -8.400  -11.260 0.86 23.34 ?  105 ASP   A O    1 
ATOM   2220 O O    B ASP   A 1 105 ? 24.135 -8.493  -11.206 0.14 26.01 ?  105 ASP   A O    1 
ATOM   2221 C CB   A ASP   A 1 105 ? 25.285 -8.748  -13.938 0.86 30.94 ?  105 ASP   A CB   1 
ATOM   2222 C CB   B ASP   A 1 105 ? 25.532 -9.243  -13.709 0.14 27.68 ?  105 ASP   A CB   1 
ATOM   2223 C CG   A ASP   A 1 105 ? 24.885 -10.189 -14.143 0.86 33.84 ?  105 ASP   A CG   1 
ATOM   2224 C CG   B ASP   A 1 105 ? 25.092 -10.641 -14.081 0.14 28.73 ?  105 ASP   A CG   1 
ATOM   2225 O OD1  A ASP   A 1 105 ? 23.671 -10.467 -14.207 0.86 34.19 ?  105 ASP   A OD1  1 
ATOM   2226 O OD1  B ASP   A 1 105 ? 23.882 -10.841 -14.309 0.14 29.02 ?  105 ASP   A OD1  1 
ATOM   2227 O OD2  A ASP   A 1 105 ? 25.795 -11.043 -14.243 0.86 35.77 -1 105 ASP   A OD2  1 
ATOM   2228 O OD2  B ASP   A 1 105 ? 25.958 -11.540 -14.151 0.14 29.15 -1 105 ASP   A OD2  1 
ATOM   2229 H H    A ASP   A 1 105 ? 25.444 -6.419  -13.408 0.86 31.73 ?  105 ASP   A H    1 
ATOM   2230 H H    B ASP   A 1 105 ? 25.721 -6.867  -13.761 0.14 30.87 ?  105 ASP   A H    1 
ATOM   2231 H HA   A ASP   A 1 105 ? 23.458 -7.890  -14.318 0.86 33.26 ?  105 ASP   A HA   1 
ATOM   2232 H HA   B ASP   A 1 105 ? 23.772 -8.405  -14.339 0.14 31.97 ?  105 ASP   A HA   1 
ATOM   2233 H HB2  A ASP   A 1 105 ? 25.698 -8.433  -14.757 0.86 37.28 ?  105 ASP   A HB2  1 
ATOM   2234 H HB2  B ASP   A 1 105 ? 26.139 -8.926  -14.399 0.14 33.36 ?  105 ASP   A HB2  1 
ATOM   2235 H HB3  A ASP   A 1 105 ? 25.926 -8.722  -13.212 0.86 37.28 ?  105 ASP   A HB3  1 
ATOM   2236 H HB3  B ASP   A 1 105 ? 25.998 -9.296  -12.860 0.14 33.36 ?  105 ASP   A HB3  1 
ATOM   2237 N N    A ILE   A 1 106 ? 22.145 -8.686  -12.414 0.86 25.39 ?  106 ILE   A N    1 
ATOM   2238 N N    B ILE   A 1 106 ? 22.278 -8.821  -12.451 0.14 26.28 ?  106 ILE   A N    1 
ATOM   2239 C CA   A ILE   A 1 106 ? 21.388 -9.084  -11.235 0.86 24.52 ?  106 ILE   A CA   1 
ATOM   2240 C CA   B ILE   A 1 106 ? 21.463 -9.180  -11.295 0.14 26.25 ?  106 ILE   A CA   1 
ATOM   2241 C C    A ILE   A 1 106 ? 21.926 -10.366 -10.618 0.86 23.18 ?  106 ILE   A C    1 
ATOM   2242 C C    B ILE   A 1 106 ? 21.953 -10.467 -10.650 0.14 25.96 ?  106 ILE   A C    1 
ATOM   2243 O O    A ILE   A 1 106 ? 21.719 -10.597 -9.422  0.86 22.33 ?  106 ILE   A O    1 
ATOM   2244 O O    B ILE   A 1 106 ? 21.693 -10.702 -9.465  0.14 25.84 ?  106 ILE   A O    1 
ATOM   2245 C CB   A ILE   A 1 106 ? 19.881 -9.173  -11.558 0.86 26.26 ?  106 ILE   A CB   1 
ATOM   2246 C CB   B ILE   A 1 106 ? 19.962 -9.248  -11.662 0.14 26.69 ?  106 ILE   A CB   1 
ATOM   2247 C CG1  A ILE   A 1 106 ? 19.048 -9.238  -10.273 0.86 26.92 ?  106 ILE   A CG1  1 
ATOM   2248 C CG1  B ILE   A 1 106 ? 19.092 -9.244  -10.400 0.14 26.86 ?  106 ILE   A CG1  1 
ATOM   2249 C CG2  A ILE   A 1 106 ? 19.589 -10.374 -12.443 0.86 27.11 ?  106 ILE   A CG2  1 
ATOM   2250 C CG2  B ILE   A 1 106 ? 19.661 -10.491 -12.477 0.14 26.87 ?  106 ILE   A CG2  1 
ATOM   2251 C CD1  A ILE   A 1 106 ? 19.148 -7.992  -9.415  0.86 27.39 ?  106 ILE   A CD1  1 
ATOM   2252 C CD1  B ILE   A 1 106 ? 19.287 -8.026  -9.523  0.14 26.90 ?  106 ILE   A CD1  1 
ATOM   2253 H H    A ILE   A 1 106 ? 21.703 -8.713  -13.147 0.86 30.62 ?  106 ILE   A H    1 
ATOM   2254 H H    B ILE   A 1 106 ? 21.845 -8.803  -13.194 0.14 31.68 ?  106 ILE   A H    1 
ATOM   2255 H HA   A ILE   A 1 106 ? 21.500 -8.401  -10.568 0.86 29.57 ?  106 ILE   A HA   1 
ATOM   2256 H HA   B ILE   A 1 106 ? 21.570 -8.485  -10.636 0.14 31.65 ?  106 ILE   A HA   1 
ATOM   2257 H HB   A ILE   A 1 106 ? 19.630 -8.373  -12.042 0.86 31.66 ?  106 ILE   A HB   1 
ATOM   2258 H HB   B ILE   A 1 106 ? 19.735 -8.469  -12.192 0.14 32.18 ?  106 ILE   A HB   1 
ATOM   2259 H HG12 A ILE   A 1 106 ? 18.116 -9.356  -10.510 0.86 32.45 ?  106 ILE   A HG12 1 
ATOM   2260 H HG12 B ILE   A 1 106 ? 18.157 -9.269  -10.663 0.14 32.38 ?  106 ILE   A HG12 1 
ATOM   2261 H HG13 A ILE   A 1 106 ? 19.349 -9.989  -9.739  0.86 32.45 ?  106 ILE   A HG13 1 
ATOM   2262 H HG13 B ILE   A 1 106 ? 19.302 -10.027 -9.869  0.14 32.38 ?  106 ILE   A HG13 1 
ATOM   2263 H HG21 A ILE   A 1 106 ? 18.683 -10.301 -12.782 0.86 32.69 ?  106 ILE   A HG21 1 
ATOM   2264 H HG21 B ILE   A 1 106 ? 18.785 -10.396 -12.884 0.14 32.39 ?  106 ILE   A HG21 1 
ATOM   2265 H HG22 A ILE   A 1 106 ? 20.219 -10.381 -13.179 0.86 32.69 ?  106 ILE   A HG22 1 
ATOM   2266 H HG22 B ILE   A 1 106 ? 20.338 -10.585 -13.162 0.14 32.39 ?  106 ILE   A HG22 1 
ATOM   2267 H HG23 A ILE   A 1 106 ? 19.682 -11.184 -11.919 0.86 32.69 ?  106 ILE   A HG23 1 
ATOM   2268 H HG23 B ILE   A 1 106 ? 19.671 -11.264 -11.891 0.14 32.39 ?  106 ILE   A HG23 1 
ATOM   2269 H HD11 A ILE   A 1 106 ? 18.434 -8.002  -8.761  0.86 33.01 ?  106 ILE   A HD11 1 
ATOM   2270 H HD11 B ILE   A 1 106 ? 18.524 -7.939  -8.933  0.14 32.43 ?  106 ILE   A HD11 1 
ATOM   2271 H HD12 A ILE   A 1 106 ? 20.008 -7.985  -8.963  0.86 33.01 ?  106 ILE   A HD12 1 
ATOM   2272 H HD12 B ILE   A 1 106 ? 20.098 -8.139  -9.002  0.14 32.43 ?  106 ILE   A HD12 1 
ATOM   2273 H HD13 A ILE   A 1 106 ? 19.066 -7.210  -9.983  0.86 33.01 ?  106 ILE   A HD13 1 
ATOM   2274 H HD13 B ILE   A 1 106 ? 19.361 -7.241  -10.088 0.14 32.43 ?  106 ILE   A HD13 1 
ATOM   2275 N N    A GLN   A 1 107 ? 22.628 -11.198 -11.400 0.86 23.80 ?  107 GLN   A N    1 
ATOM   2276 N N    B GLN   A 1 107 ? 22.665 -11.312 -11.401 0.14 25.83 ?  107 GLN   A N    1 
ATOM   2277 C CA   A GLN   A 1 107 ? 23.251 -12.401 -10.853 0.86 26.48 ?  107 GLN   A CA   1 
ATOM   2278 C CA   B GLN   A 1 107 ? 23.285 -12.487 -10.802 0.14 25.91 ?  107 GLN   A CA   1 
ATOM   2279 C C    A GLN   A 1 107 ? 24.232 -12.064 -9.738  0.86 23.89 ?  107 GLN   A C    1 
ATOM   2280 C C    B GLN   A 1 107 ? 24.315 -12.102 -9.747  0.14 22.99 ?  107 GLN   A C    1 
ATOM   2281 O O    A GLN   A 1 107 ? 24.470 -12.886 -8.847  0.86 25.35 ?  107 GLN   A O    1 
ATOM   2282 O O    B GLN   A 1 107 ? 24.682 -12.944 -8.921  0.14 23.35 ?  107 GLN   A O    1 
ATOM   2283 C CB   A GLN   A 1 107 ? 23.962 -13.173 -11.971 0.86 31.34 ?  107 GLN   A CB   1 
ATOM   2284 C CB   B GLN   A 1 107 ? 23.941 -13.359 -11.878 0.14 28.80 ?  107 GLN   A CB   1 
ATOM   2285 C CG   A GLN   A 1 107 ? 23.104 -13.405 -13.211 0.86 36.63 ?  107 GLN   A CG   1 
ATOM   2286 C CG   B GLN   A 1 107 ? 23.069 -13.621 -13.101 0.14 31.48 ?  107 GLN   A CG   1 
ATOM   2287 C CD   A GLN   A 1 107 ? 21.848 -14.197 -12.913 0.86 40.81 ?  107 GLN   A CD   1 
ATOM   2288 C CD   B GLN   A 1 107 ? 21.708 -14.186 -12.750 0.14 33.69 ?  107 GLN   A CD   1 
ATOM   2289 O OE1  A GLN   A 1 107 ? 21.899 -15.246 -12.268 0.86 42.42 ?  107 GLN   A OE1  1 
ATOM   2290 O OE1  B GLN   A 1 107 ? 21.591 -15.100 -11.934 0.14 34.49 ?  107 GLN   A OE1  1 
ATOM   2291 N NE2  A GLN   A 1 107 ? 20.708 -13.696 -13.378 0.86 42.15 ?  107 GLN   A NE2  1 
ATOM   2292 N NE2  B GLN   A 1 107 ? 20.667 -13.638 -13.368 0.14 34.43 ?  107 GLN   A NE2  1 
ATOM   2293 H H    A GLN   A 1 107 ? 22.752 -11.090 -12.242 0.86 28.71 ?  107 GLN   A H    1 
ATOM   2294 H H    B GLN   A 1 107 ? 22.797 -11.227 -12.244 0.14 31.15 ?  107 GLN   A H    1 
ATOM   2295 H HA   A GLN   A 1 107 ? 22.571 -12.984 -10.485 0.86 31.93 ?  107 GLN   A HA   1 
ATOM   2296 H HA   B GLN   A 1 107 ? 22.601 -13.020 -10.369 0.14 31.25 ?  107 GLN   A HA   1 
ATOM   2297 H HB2  A GLN   A 1 107 ? 24.750 -12.677 -12.247 0.86 37.76 ?  107 GLN   A HB2  1 
ATOM   2298 H HB2  B GLN   A 1 107 ? 24.751 -12.922 -12.184 0.14 34.71 ?  107 GLN   A HB2  1 
ATOM   2299 H HB3  A GLN   A 1 107 ? 24.229 -14.046 -11.636 0.86 37.76 ?  107 GLN   A HB3  1 
ATOM   2300 H HB3  B GLN   A 1 107 ? 24.163 -14.221 -11.490 0.14 34.71 ?  107 GLN   A HB3  1 
ATOM   2301 H HG2  A GLN   A 1 107 ? 22.839 -12.549 -13.585 0.86 44.11 ?  107 GLN   A HG2  1 
ATOM   2302 H HG2  B GLN   A 1 107 ? 22.928 -12.791 -13.578 0.14 37.93 ?  107 GLN   A HG2  1 
ATOM   2303 H HG3  A GLN   A 1 107 ? 23.623 -13.899 -13.863 0.86 44.11 ?  107 GLN   A HG3  1 
ATOM   2304 H HG3  B GLN   A 1 107 ? 23.519 -14.259 -13.677 0.14 37.93 ?  107 GLN   A HG3  1 
ATOM   2305 H HE21 A GLN   A 1 107 ? 20.710 -12.961 -13.824 0.86 50.73 ?  107 GLN   A HE21 1 
ATOM   2306 H HE21 B GLN   A 1 107 ? 20.788 -12.998 -13.931 0.14 41.47 ?  107 GLN   A HE21 1 
ATOM   2307 H HE22 A GLN   A 1 107 ? 19.968 -14.110 -13.235 0.86 50.73 ?  107 GLN   A HE22 1 
ATOM   2308 H HE22 B GLN   A 1 107 ? 19.872 -13.923 -13.206 0.14 41.47 ?  107 GLN   A HE22 1 
ATOM   2309 N N    . LEU   A 1 108 ? 24.788 -10.851 -9.750  1.00 19.91 ?  108 LEU   A N    1 
ATOM   2310 C CA   . LEU   A 1 108 ? 25.705 -10.421 -8.704  1.00 16.61 ?  108 LEU   A CA   1 
ATOM   2311 C C    . LEU   A 1 108 ? 25.006 -10.260 -7.363  1.00 14.66 ?  108 LEU   A C    1 
ATOM   2312 O O    . LEU   A 1 108 ? 25.683 -10.101 -6.348  1.00 15.10 ?  108 LEU   A O    1 
ATOM   2313 C CB   . LEU   A 1 108 ? 26.419 -9.123  -9.104  1.00 16.30 ?  108 LEU   A CB   1 
ATOM   2314 C CG   . LEU   A 1 108 ? 27.437 -9.317  -10.229 1.00 18.36 ?  108 LEU   A CG   1 
ATOM   2315 C CD1  . LEU   A 1 108 ? 27.916 -7.990  -10.786 1.00 19.36 ?  108 LEU   A CD1  1 
ATOM   2316 C CD2  . LEU   A 1 108 ? 28.627 -10.128 -9.738  1.00 20.44 ?  108 LEU   A CD2  1 
ATOM   2317 H H    A LEU   A 1 108 ? 24.643 -10.262 -10.352 0.86 24.04 ?  108 LEU   A H    1 
ATOM   2318 H H    B LEU   A 1 108 ? 24.601 -10.257 -10.336 0.14 24.04 ?  108 LEU   A H    1 
ATOM   2319 H HA   . LEU   A 1 108 ? 26.381 -11.104 -8.587  1.00 20.08 ?  108 LEU   A HA   1 
ATOM   2320 H HB2  . LEU   A 1 108 ? 25.760 -8.481  -9.409  1.00 19.71 ?  108 LEU   A HB2  1 
ATOM   2321 H HB3  . LEU   A 1 108 ? 26.891 -8.773  -8.334  1.00 19.71 ?  108 LEU   A HB3  1 
ATOM   2322 H HG   . LEU   A 1 108 ? 27.020 -9.816  -10.951 1.00 22.18 ?  108 LEU   A HG   1 
ATOM   2323 H HD11 . LEU   A 1 108 ? 28.529 -8.159  -11.521 1.00 23.39 ?  108 LEU   A HD11 1 
ATOM   2324 H HD12 . LEU   A 1 108 ? 27.151 -7.487  -11.103 1.00 23.39 ?  108 LEU   A HD12 1 
ATOM   2325 H HD13 . LEU   A 1 108 ? 28.370 -7.499  -10.084 1.00 23.39 ?  108 LEU   A HD13 1 
ATOM   2326 H HD21 . LEU   A 1 108 ? 29.337 -10.074 -10.392 1.00 24.68 ?  108 LEU   A HD21 1 
ATOM   2327 H HD22 . LEU   A 1 108 ? 28.925 -9.762  -8.890  1.00 24.68 ?  108 LEU   A HD22 1 
ATOM   2328 H HD23 . LEU   A 1 108 ? 28.353 -11.052 -9.619  1.00 24.68 ?  108 LEU   A HD23 1 
ATOM   2329 N N    . LEU   A 1 109 ? 23.672 -10.319 -7.327  1.00 14.29 ?  109 LEU   A N    1 
ATOM   2330 C CA   . LEU   A 1 109 ? 22.968 -10.191 -6.055  1.00 13.58 ?  109 LEU   A CA   1 
ATOM   2331 C C    . LEU   A 1 109 ? 23.316 -11.342 -5.113  1.00 12.88 ?  109 LEU   A C    1 
ATOM   2332 O O    . LEU   A 1 109 ? 23.461 -11.143 -3.902  1.00 13.23 ?  109 LEU   A O    1 
ATOM   2333 C CB   . LEU   A 1 109 ? 21.462 -10.108 -6.304  1.00 14.25 ?  109 LEU   A CB   1 
ATOM   2334 C CG   . LEU   A 1 109 ? 20.583 -9.810  -5.090  1.00 14.57 ?  109 LEU   A CG   1 
ATOM   2335 C CD1  . LEU   A 1 109 ? 21.037 -8.534  -4.389  1.00 14.47 ?  109 LEU   A CD1  1 
ATOM   2336 C CD2  . LEU   A 1 109 ? 19.113 -9.711  -5.504  1.00 15.56 ?  109 LEU   A CD2  1 
ATOM   2337 H H    . LEU   A 1 109 ? 23.160 -10.431 -8.010  1.00 17.29 ?  109 LEU   A H    1 
ATOM   2338 H HA   . LEU   A 1 109 ? 23.250 -9.370  -5.629  1.00 16.45 ?  109 LEU   A HA   1 
ATOM   2339 H HB2  . LEU   A 1 109 ? 21.303 -9.399  -6.949  1.00 17.25 ?  109 LEU   A HB2  1 
ATOM   2340 H HB3  . LEU   A 1 109 ? 21.164 -10.949 -6.670  1.00 17.25 ?  109 LEU   A HB3  1 
ATOM   2341 H HG   . LEU   A 1 109 ? 20.663 -10.537 -4.459  1.00 17.64 ?  109 LEU   A HG   1 
ATOM   2342 H HD11 . LEU   A 1 109 ? 20.333 -8.217  -3.806  1.00 17.51 ?  109 LEU   A HD11 1 
ATOM   2343 H HD12 . LEU   A 1 109 ? 21.837 -8.726  -3.871  1.00 17.51 ?  109 LEU   A HD12 1 
ATOM   2344 H HD13 . LEU   A 1 109 ? 21.238 -7.860  -5.060  1.00 17.51 ?  109 LEU   A HD13 1 
ATOM   2345 H HD21 . LEU   A 1 109 ? 18.589 -9.406  -4.745  1.00 18.82 ?  109 LEU   A HD21 1 
ATOM   2346 H HD22 . LEU   A 1 109 ? 19.028 -9.082  -6.236  1.00 18.82 ?  109 LEU   A HD22 1 
ATOM   2347 H HD23 . LEU   A 1 109 ? 18.804 -10.588 -5.784  1.00 18.82 ?  109 LEU   A HD23 1 
ATOM   2348 N N    . LYS   A 1 110 ? 23.460 -12.559 -5.648  1.00 12.90 ?  110 LYS   A N    1 
ATOM   2349 C CA   . LYS   A 1 110 ? 23.844 -13.677 -4.787  1.00 13.02 ?  110 LYS   A CA   1 
ATOM   2350 C C    . LYS   A 1 110 ? 25.233 -13.455 -4.187  1.00 12.31 ?  110 LYS   A C    1 
ATOM   2351 O O    . LYS   A 1 110 ? 25.439 -13.658 -2.987  1.00 12.31 ?  110 LYS   A O    1 
ATOM   2352 C CB   . LYS   A 1 110 ? 23.760 -15.008 -5.546  1.00 14.00 ?  110 LYS   A CB   1 
ATOM   2353 C CG   . LYS   A 1 110 ? 23.974 -16.232 -4.643  1.00 13.87 ?  110 LYS   A CG   1 
ATOM   2354 C CD   . LYS   A 1 110 ? 23.754 -17.550 -5.363  1.00 14.79 ?  110 LYS   A CD   1 
ATOM   2355 C CE   . LYS   A 1 110 ? 23.853 -18.732 -4.414  1.00 15.93 ?  110 LYS   A CE   1 
ATOM   2356 N NZ   . LYS   A 1 110 ? 22.669 -18.869 -3.525  1.00 15.98 ?  110 LYS   A NZ   1 
ATOM   2357 H H    . LYS   A 1 110 ? 23.340 -12.763 -6.473  1.00 15.63 ?  110 LYS   A H    1 
ATOM   2358 H HA   . LYS   A 1 110 ? 23.210 -13.728 -4.049  1.00 15.77 ?  110 LYS   A HA   1 
ATOM   2359 H HB2  . LYS   A 1 110 ? 22.880 -15.084 -5.951  1.00 16.95 ?  110 LYS   A HB2  1 
ATOM   2360 H HB3  . LYS   A 1 110 ? 24.443 -15.020 -6.232  1.00 16.95 ?  110 LYS   A HB3  1 
ATOM   2361 H HG2  . LYS   A 1 110 ? 24.881 -16.216 -4.306  1.00 16.79 ?  110 LYS   A HG2  1 
ATOM   2362 H HG3  . LYS   A 1 110 ? 23.345 -16.184 -3.903  1.00 16.79 ?  110 LYS   A HG3  1 
ATOM   2363 H HD2  . LYS   A 1 110 ? 22.870 -17.552 -5.758  1.00 17.89 ?  110 LYS   A HD2  1 
ATOM   2364 H HD3  . LYS   A 1 110 ? 24.432 -17.649 -6.048  1.00 17.89 ?  110 LYS   A HD3  1 
ATOM   2365 H HE2  . LYS   A 1 110 ? 23.939 -19.544 -4.933  1.00 19.27 ?  110 LYS   A HE2  1 
ATOM   2366 H HE3  . LYS   A 1 110 ? 24.638 -18.615 -3.849  1.00 19.27 ?  110 LYS   A HE3  1 
ATOM   2367 H HZ1  . LYS   A 1 110 ? 22.768 -19.570 -2.990  1.00 19.32 ?  110 LYS   A HZ1  1 
ATOM   2368 H HZ2  . LYS   A 1 110 ? 22.571 -18.135 -3.030  1.00 19.32 ?  110 LYS   A HZ2  1 
ATOM   2369 H HZ3  . LYS   A 1 110 ? 21.934 -18.981 -4.018  1.00 19.32 ?  110 LYS   A HZ3  1 
ATOM   2370 N N    . SER   A 1 111 ? 26.189 -13.010 -5.006  1.00 12.71 ?  111 SER   A N    1 
ATOM   2371 C CA   . SER   A 1 111 ? 27.521 -12.694 -4.494  1.00 12.74 ?  111 SER   A CA   1 
ATOM   2372 C C    . SER   A 1 111 ? 27.457 -11.653 -3.379  1.00 11.83 ?  111 SER   A C    1 
ATOM   2373 O O    . SER   A 1 111 ? 28.160 -11.768 -2.369  1.00 12.72 ?  111 SER   A O    1 
ATOM   2374 C CB   . SER   A 1 111 ? 28.407 -12.198 -5.636  1.00 13.94 ?  111 SER   A CB   1 
ATOM   2375 O OG   . SER   A 1 111 ? 28.529 -13.192 -6.645  1.00 16.28 ?  111 SER   A OG   1 
ATOM   2376 H H    . SER   A 1 111 ? 26.086 -12.885 -5.850  1.00 15.39 ?  111 SER   A H    1 
ATOM   2377 H HA   . SER   A 1 111 ? 27.918 -13.500 -4.133  1.00 15.43 ?  111 SER   A HA   1 
ATOM   2378 H HB2  . SER   A 1 111 ? 28.005 -11.408 -6.030  1.00 16.88 ?  111 SER   A HB2  1 
ATOM   2379 H HB3  . SER   A 1 111 ? 29.284 -11.981 -5.282  1.00 16.88 ?  111 SER   A HB3  1 
ATOM   2380 H HG   . SER   A 1 111 ? 29.041 -12.907 -7.261  1.00 19.68 ?  111 SER   A HG   1 
ATOM   2381 N N    . ALA   A 1 112 ? 26.617 -10.628 -3.554  1.00 12.16 ?  112 ALA   A N    1 
ATOM   2382 C CA   . ALA   A 1 112 ? 26.465 -9.594  -2.530  1.00 11.47 ?  112 ALA   A CA   1 
ATOM   2383 C C    . ALA   A 1 112 ? 25.996 -10.198 -1.208  1.00 11.63 ?  112 ALA   A C    1 
ATOM   2384 O O    . ALA   A 1 112 ? 26.544 -9.897  -0.137  1.00 12.21 ?  112 ALA   A O    1 
ATOM   2385 C CB   . ALA   A 1 112 ? 25.508 -8.502  -3.025  1.00 12.35 ?  112 ALA   A CB   1 
ATOM   2386 H H    . ALA   A 1 112 ? 26.131 -10.504 -4.253  1.00 14.75 ?  112 ALA   A H    1 
ATOM   2387 H HA   . ALA   A 1 112 ? 27.323 -9.174  -2.373  1.00 13.91 ?  112 ALA   A HA   1 
ATOM   2388 H HB1  . ALA   A 1 112 ? 25.425 -7.816  -2.338  1.00 14.97 ?  112 ALA   A HB1  1 
ATOM   2389 H HB2  . ALA   A 1 112 ? 25.857 -8.112  -3.838  1.00 14.97 ?  112 ALA   A HB2  1 
ATOM   2390 H HB3  . ALA   A 1 112 ? 24.634 -8.896  -3.194  1.00 14.97 ?  112 ALA   A HB3  1 
ATOM   2391 N N    . TYR   A 1 113 ? 24.966 -11.050 -1.260  1.00 12.31 ?  113 TYR   A N    1 
ATOM   2392 C CA   . TYR   A 1 113 ? 24.452 -11.658 -0.035  1.00 11.56 ?  113 TYR   A CA   1 
ATOM   2393 C C    . TYR   A 1 113 ? 25.454 -12.612 0.610   1.00 11.23 ?  113 TYR   A C    1 
ATOM   2394 O O    . TYR   A 1 113 ? 25.414 -12.804 1.831   1.00 12.03 ?  113 TYR   A O    1 
ATOM   2395 C CB   . TYR   A 1 113 ? 23.134 -12.385 -0.311  1.00 12.29 ?  113 TYR   A CB   1 
ATOM   2396 C CG   . TYR   A 1 113 ? 21.910 -11.502 -0.214  1.00 11.98 ?  113 TYR   A CG   1 
ATOM   2397 C CD1  . TYR   A 1 113 ? 21.543 -10.912 0.994   1.00 12.27 ?  113 TYR   A CD1  1 
ATOM   2398 C CD2  . TYR   A 1 113 ? 21.102 -11.264 -1.320  1.00 12.42 ?  113 TYR   A CD2  1 
ATOM   2399 C CE1  . TYR   A 1 113 ? 20.415 -10.129 1.097   1.00 12.50 ?  113 TYR   A CE1  1 
ATOM   2400 C CE2  . TYR   A 1 113 ? 19.955 -10.470 -1.222  1.00 12.36 ?  113 TYR   A CE2  1 
ATOM   2401 C CZ   . TYR   A 1 113 ? 19.622 -9.909  -0.012  1.00 12.18 ?  113 TYR   A CZ   1 
ATOM   2402 O OH   . TYR   A 1 113 ? 18.497 -9.119  0.109   1.00 13.48 ?  113 TYR   A OH   1 
ATOM   2403 H H    . TYR   A 1 113 ? 24.558 -11.287 -1.980  1.00 14.93 ?  113 TYR   A H    1 
ATOM   2404 H HA   . TYR   A 1 113 ? 24.272 -10.954 0.605   1.00 14.01 ?  113 TYR   A HA   1 
ATOM   2405 H HB2  . TYR   A 1 113 ? 23.154 -12.746 -1.208  1.00 14.90 ?  113 TYR   A HB2  1 
ATOM   2406 H HB3  . TYR   A 1 113 ? 23.029 -13.101 0.333   1.00 14.90 ?  113 TYR   A HB3  1 
ATOM   2407 H HD1  . TYR   A 1 113 ? 22.071 -11.062 1.752   1.00 14.88 ?  113 TYR   A HD1  1 
ATOM   2408 H HD2  . TYR   A 1 113 ? 21.318 -11.654 -2.130  1.00 15.05 ?  113 TYR   A HD2  1 
ATOM   2409 H HE1  . TYR   A 1 113 ? 20.194 -9.743  1.916   1.00 15.14 ?  113 TYR   A HE1  1 
ATOM   2410 H HE2  . TYR   A 1 113 ? 19.419 -10.321 -1.967  1.00 14.98 ?  113 TYR   A HE2  1 
ATOM   2411 H HH   . TYR   A 1 113 ? 18.107 -9.063  -0.638  1.00 16.32 ?  113 TYR   A HH   1 
ATOM   2412 N N    . GLU   A 1 114 ? 26.347 -13.226 -0.176  1.00 11.77 ?  114 GLU   A N    1 
ATOM   2413 C CA   . GLU   A 1 114 ? 27.347 -14.113 0.420   1.00 11.77 ?  114 GLU   A CA   1 
ATOM   2414 C C    . GLU   A 1 114 ? 28.193 -13.406 1.473   1.00 11.55 ?  114 GLU   A C    1 
ATOM   2415 O O    . GLU   A 1 114 ? 28.681 -14.043 2.417   1.00 12.23 ?  114 GLU   A O    1 
ATOM   2416 C CB   . GLU   A 1 114 ? 28.215 -14.759 -0.667  1.00 12.08 ?  114 GLU   A CB   1 
ATOM   2417 C CG   . GLU   A 1 114 ? 27.459 -15.806 -1.451  1.00 12.67 ?  114 GLU   A CG   1 
ATOM   2418 C CD   . GLU   A 1 114 ? 28.167 -16.338 -2.692  1.00 13.28 ?  114 GLU   A CD   1 
ATOM   2419 O OE1  . GLU   A 1 114 ? 29.116 -15.712 -3.187  1.00 13.55 ?  114 GLU   A OE1  1 
ATOM   2420 O OE2  . GLU   A 1 114 ? 27.727 -17.406 -3.189  1.00 14.32 -1 114 GLU   A OE2  1 
ATOM   2421 H H    . GLU   A 1 114 ? 26.393 -13.144 -1.039  1.00 14.27 ?  114 GLU   A H    1 
ATOM   2422 H HA   . GLU   A 1 114 ? 26.880 -14.830 0.861   1.00 14.28 ?  114 GLU   A HA   1 
ATOM   2423 H HB2  . GLU   A 1 114 ? 28.516 -14.080 -1.295  1.00 14.65 ?  114 GLU   A HB2  1 
ATOM   2424 H HB3  . GLU   A 1 114 ? 28.981 -15.191 -0.256  1.00 14.65 ?  114 GLU   A HB3  1 
ATOM   2425 H HG2  . GLU   A 1 114 ? 27.293 -16.568 -0.871  1.00 15.36 ?  114 GLU   A HG2  1 
ATOM   2426 H HG3  . GLU   A 1 114 ? 26.611 -15.430 -1.737  1.00 15.36 ?  114 GLU   A HG3  1 
ATOM   2427 N N    . ASN   A 1 115 ? 28.380 -12.090 1.342   1.00 11.51 ?  115 ASN   A N    1 
ATOM   2428 C CA   . ASN   A 1 115 ? 29.144 -11.358 2.346   1.00 11.83 ?  115 ASN   A CA   1 
ATOM   2429 C C    . ASN   A 1 115 ? 28.528 -11.493 3.735   1.00 11.62 ?  115 ASN   A C    1 
ATOM   2430 O O    . ASN   A 1 115 ? 29.238 -11.420 4.744   1.00 12.26 ?  115 ASN   A O    1 
ATOM   2431 C CB   . ASN   A 1 115 ? 29.246 -9.882  1.965   1.00 11.92 ?  115 ASN   A CB   1 
ATOM   2432 C CG   . ASN   A 1 115 ? 30.045 -9.664  0.706   1.00 13.00 ?  115 ASN   A CG   1 
ATOM   2433 O OD1  . ASN   A 1 115 ? 31.264 -9.801  0.716   1.00 16.34 ?  115 ASN   A OD1  1 
ATOM   2434 N ND2  . ASN   A 1 115 ? 29.378 -9.341  -0.379  1.00 12.62 ?  115 ASN   A ND2  1 
ATOM   2435 H H    . ASN   A 1 115 ? 28.070 -11.602 0.701   1.00 13.97 ?  115 ASN   A H    1 
ATOM   2436 H HA   . ASN   A 1 115 ? 30.042 -11.723 2.383   1.00 14.35 ?  115 ASN   A HA   1 
ATOM   2437 H HB2  . ASN   A 1 115 ? 28.352 -9.532  1.831   1.00 14.46 ?  115 ASN   A HB2  1 
ATOM   2438 H HB3  . ASN   A 1 115 ? 29.684 -9.404  2.689   1.00 14.46 ?  115 ASN   A HB3  1 
ATOM   2439 H HD21 . ASN   A 1 115 ? 29.798 -9.204  -1.115  1.00 15.29 ?  115 ASN   A HD21 1 
ATOM   2440 H HD22 . ASN   A 1 115 ? 28.520 -9.265  -0.353  1.00 15.29 ?  115 ASN   A HD22 1 
ATOM   2441 N N    . PHE   A 1 116 ? 27.201 -11.660 3.816   1.00 11.99 ?  116 PHE   A N    1 
ATOM   2442 C CA   . PHE   A 1 116 ? 26.554 -11.768 5.123   1.00 11.83 ?  116 PHE   A CA   1 
ATOM   2443 C C    . PHE   A 1 116 ? 27.031 -13.004 5.890   1.00 12.10 ?  116 PHE   A C    1 
ATOM   2444 O O    . PHE   A 1 116 ? 26.956 -13.028 7.120   1.00 12.51 ?  116 PHE   A O    1 
ATOM   2445 C CB   . PHE   A 1 116 ? 25.023 -11.895 4.993   1.00 12.10 ?  116 PHE   A CB   1 
ATOM   2446 C CG   . PHE   A 1 116 ? 24.270 -10.645 4.529   1.00 11.85 ?  116 PHE   A CG   1 
ATOM   2447 C CD1  . PHE   A 1 116 ? 24.841 -9.622  3.784   1.00 12.03 ?  116 PHE   A CD1  1 
ATOM   2448 C CD2  . PHE   A 1 116 ? 22.910 -10.552 4.844   1.00 12.52 ?  116 PHE   A CD2  1 
ATOM   2449 C CE1  . PHE   A 1 116 ? 24.063 -8.548  3.369   1.00 12.33 ?  116 PHE   A CE1  1 
ATOM   2450 C CE2  . PHE   A 1 116 ? 22.136 -9.481  4.439   1.00 12.50 ?  116 PHE   A CE2  1 
ATOM   2451 C CZ   . PHE   A 1 116 ? 22.707 -8.474  3.702   1.00 12.14 ?  116 PHE   A CZ   1 
ATOM   2452 H H    . PHE   A 1 116 ? 26.668 -11.702 3.144   1.00 14.53 ?  116 PHE   A H    1 
ATOM   2453 H HA   . PHE   A 1 116 ? 26.749 -10.978 5.653   1.00 14.35 ?  116 PHE   A HA   1 
ATOM   2454 H HB2  . PHE   A 1 116 ? 24.832 -12.599 4.354   1.00 14.67 ?  116 PHE   A HB2  1 
ATOM   2455 H HB3  . PHE   A 1 116 ? 24.665 -12.143 5.860   1.00 14.67 ?  116 PHE   A HB3  1 
ATOM   2456 H HD1  . PHE   A 1 116 ? 25.738 -9.675  3.553   1.00 14.59 ?  116 PHE   A HD1  1 
ATOM   2457 H HD2  . PHE   A 1 116 ? 22.514 -11.242 5.339   1.00 15.17 ?  116 PHE   A HD2  1 
ATOM   2458 H HE1  . PHE   A 1 116 ? 24.457 -7.868  2.877   1.00 14.94 ?  116 PHE   A HE1  1 
ATOM   2459 H HE2  . PHE   A 1 116 ? 21.231 -9.451  4.673   1.00 15.15 ?  116 PHE   A HE2  1 
ATOM   2460 H HZ   . PHE   A 1 116 ? 22.195 -7.746  3.435   1.00 14.72 ?  116 PHE   A HZ   1 
ATOM   2461 N N    . ASN   A 1 117 ? 27.481 -14.049 5.184   1.00 12.17 ?  117 ASN   A N    1 
ATOM   2462 C CA   . ASN   A 1 117 ? 27.851 -15.299 5.845   1.00 12.53 ?  117 ASN   A CA   1 
ATOM   2463 C C    . ASN   A 1 117 ? 29.116 -15.181 6.676   1.00 12.90 ?  117 ASN   A C    1 
ATOM   2464 O O    . ASN   A 1 117 ? 29.419 -16.098 7.445   1.00 14.11 ?  117 ASN   A O    1 
ATOM   2465 C CB   . ASN   A 1 117 ? 27.964 -16.421 4.814   1.00 12.82 ?  117 ASN   A CB   1 
ATOM   2466 C CG   . ASN   A 1 117 ? 26.606 -16.815 4.282   1.00 12.71 ?  117 ASN   A CG   1 
ATOM   2467 O OD1  . ASN   A 1 117 ? 25.632 -16.852 5.038   1.00 13.59 ?  117 ASN   A OD1  1 
ATOM   2468 N ND2  . ASN   A 1 117 ? 26.521 -17.071 2.991   1.00 12.65 ?  117 ASN   A ND2  1 
ATOM   2469 H H    . ASN   A 1 117 ? 27.559 -14.055 4.322   1.00 14.75 ?  117 ASN   A H    1 
ATOM   2470 H HA   . ASN   A 1 117 ? 27.127 -15.534 6.446   1.00 15.18 ?  117 ASN   A HA   1 
ATOM   2471 H HB2  . ASN   A 1 117 ? 28.511 -16.119 4.069   1.00 15.54 ?  117 ASN   A HB2  1 
ATOM   2472 H HB3  . ASN   A 1 117 ? 28.360 -17.195 5.233   1.00 15.54 ?  117 ASN   A HB3  1 
ATOM   2473 H HD21 . ASN   A 1 117 ? 25.768 -17.289 2.646   1.00 15.32 ?  117 ASN   A HD21 1 
ATOM   2474 H HD22 . ASN   A 1 117 ? 27.225 -17.019 2.493   1.00 15.32 ?  117 ASN   A HD22 1 
ATOM   2475 N N    . GLN   A 1 118 ? 29.840 -14.072 6.559   1.00 13.01 ?  118 GLN   A N    1 
ATOM   2476 C CA   . GLN   A 1 118 ? 31.020 -13.834 7.378   1.00 13.32 ?  118 GLN   A CA   1 
ATOM   2477 C C    . GLN   A 1 118 ? 30.680 -13.273 8.751   1.00 13.20 ?  118 GLN   A C    1 
ATOM   2478 O O    . GLN   A 1 118 ? 31.596 -12.986 9.531   1.00 15.16 ?  118 GLN   A O    1 
ATOM   2479 C CB   . GLN   A 1 118 ? 32.006 -12.925 6.640   1.00 13.38 ?  118 GLN   A CB   1 
ATOM   2480 C CG   . GLN   A 1 118 ? 32.487 -13.501 5.323   1.00 13.73 ?  118 GLN   A CG   1 
ATOM   2481 C CD   . GLN   A 1 118 ? 33.322 -14.756 5.502   1.00 14.16 ?  118 GLN   A CD   1 
ATOM   2482 O OE1  . GLN   A 1 118 ? 34.177 -14.830 6.396   1.00 14.88 ?  118 GLN   A OE1  1 
ATOM   2483 N NE2  . GLN   A 1 118 ? 33.075 -15.758 4.655   1.00 14.14 ?  118 GLN   A NE2  1 
ATOM   2484 H H    . GLN   A 1 118 ? 29.660 -13.426 6.008   1.00 15.76 ?  118 GLN   A H    1 
ATOM   2485 H HA   . GLN   A 1 118 ? 31.457 -14.688 7.514   1.00 16.13 ?  118 GLN   A HA   1 
ATOM   2486 H HB2  . GLN   A 1 118 ? 31.575 -12.077 6.460   1.00 16.20 ?  118 GLN   A HB2  1 
ATOM   2487 H HB3  . GLN   A 1 118 ? 32.782 -12.790 7.207   1.00 16.20 ?  118 GLN   A HB3  1 
ATOM   2488 H HG2  . GLN   A 1 118 ? 31.714 -13.724 4.775   1.00 16.62 ?  118 GLN   A HG2  1 
ATOM   2489 H HG3  . GLN   A 1 118 ? 33.032 -12.842 4.871   1.00 16.62 ?  118 GLN   A HG3  1 
ATOM   2490 H HE21 . GLN   A 1 118 ? 32.464 -15.669 4.047   1.00 17.12 ?  118 GLN   A HE21 1 
ATOM   2491 H HE22 . GLN   A 1 118 ? 33.509 -16.495 4.715   1.00 17.12 ?  118 GLN   A HE22 1 
ATOM   2492 N N    . HIS   A 1 119 ? 29.391 -13.118 9.065   1.00 13.10 ?  119 HIS   A N    1 
ATOM   2493 C CA   . HIS   A 1 119 ? 28.931 -12.517 10.314  1.00 13.56 ?  119 HIS   A CA   1 
ATOM   2494 C C    . HIS   A 1 119 ? 27.790 -13.337 10.890  1.00 13.97 ?  119 HIS   A C    1 
ATOM   2495 O O    . HIS   A 1 119 ? 26.839 -13.665 10.175  1.00 14.72 ?  119 HIS   A O    1 
ATOM   2496 C CB   . HIS   A 1 119 ? 28.477 -11.075 10.055  1.00 14.10 ?  119 HIS   A CB   1 
ATOM   2497 C CG   . HIS   A 1 119 ? 29.559 -10.255 9.448   1.00 15.42 ?  119 HIS   A CG   1 
ATOM   2498 N ND1  . HIS   A 1 119 ? 30.537 -9.658  10.209  1.00 17.72 ?  119 HIS   A ND1  1 
ATOM   2499 C CD2  . HIS   A 1 119 ? 29.900 -10.047 8.157   1.00 16.64 ?  119 HIS   A CD2  1 
ATOM   2500 C CE1  . HIS   A 1 119 ? 31.403 -9.060  9.411   1.00 18.22 ?  119 HIS   A CE1  1 
ATOM   2501 N NE2  . HIS   A 1 119 ? 31.049 -9.292  8.159   1.00 18.12 ?  119 HIS   A NE2  1 
ATOM   2502 H H    . HIS   A 1 119 ? 28.739 -13.370 8.556   1.00 15.86 ?  119 HIS   A H    1 
ATOM   2503 H HA   . HIS   A 1 119 ? 29.663 -12.508 10.954  1.00 16.42 ?  119 HIS   A HA   1 
ATOM   2504 H HB2  . HIS   A 1 119 ? 27.722 -11.094 9.447   1.00 17.07 ?  119 HIS   A HB2  1 
ATOM   2505 H HB3  . HIS   A 1 119 ? 28.219 -10.677 10.900  1.00 17.07 ?  119 HIS   A HB3  1 
ATOM   2506 H HD1  . HIS   A 1 119 ? 30.563 -9.657  11.072  1.00 21.41 ?  119 HIS   A HD1  1 
ATOM   2507 H HD2  . HIS   A 1 119 ? 29.437 -10.351 7.409   1.00 20.11 ?  119 HIS   A HD2  1 
ATOM   2508 H HE1  . HIS   A 1 119 ? 32.137 -8.565  9.687   1.00 22.01 ?  119 HIS   A HE1  1 
ATOM   2509 N N    . GLU   A 1 120 ? 27.886 -13.651 12.184  1.00 14.93 ?  120 GLU   A N    1 
ATOM   2510 C CA   . GLU   A 1 120 ? 26.941 -14.585 12.792  1.00 16.85 ?  120 GLU   A CA   1 
ATOM   2511 C C    . GLU   A 1 120 ? 25.521 -14.021 12.849  1.00 15.46 ?  120 GLU   A C    1 
ATOM   2512 O O    . GLU   A 1 120 ? 24.545 -14.780 12.738  1.00 15.39 ?  120 GLU   A O    1 
ATOM   2513 C CB   . GLU   A 1 120 ? 27.421 -14.980 14.191  1.00 21.66 ?  120 GLU   A CB   1 
ATOM   2514 C CG   . GLU   A 1 120 ? 28.578 -15.962 14.196  1.00 29.28 ?  120 GLU   A CG   1 
ATOM   2515 C CD   . GLU   A 1 120 ? 28.699 -16.709 15.508  1.00 36.18 ?  120 GLU   A CD   1 
ATOM   2516 O OE1  . GLU   A 1 120 ? 28.341 -16.134 16.559  1.00 38.00 ?  120 GLU   A OE1  1 
ATOM   2517 O OE2  . GLU   A 1 120 ? 29.147 -17.875 15.489  1.00 40.06 -1 120 GLU   A OE2  1 
ATOM   2518 H H    . GLU   A 1 120 ? 28.485 -13.344 12.728  1.00 18.07 ?  120 GLU   A H    1 
ATOM   2519 H HA   . GLU   A 1 120 ? 26.913 -15.389 12.259  1.00 20.37 ?  120 GLU   A HA   1 
ATOM   2520 H HB2  . GLU   A 1 120 ? 27.712 -14.185 14.666  1.00 26.15 ?  120 GLU   A HB2  1 
ATOM   2521 H HB3  . GLU   A 1 120 ? 26.684 -15.394 14.673  1.00 26.15 ?  120 GLU   A HB3  1 
ATOM   2522 H HG2  . GLU   A 1 120 ? 28.452 -16.607 13.481  1.00 35.28 ?  120 GLU   A HG2  1 
ATOM   2523 H HG3  . GLU   A 1 120 ? 29.408 -15.480 14.070  1.00 35.28 ?  120 GLU   A HG3  1 
ATOM   2524 N N    . VAL   A 1 121 ? 25.388 -12.710 13.071  1.00 14.85 ?  121 VAL   A N    1 
ATOM   2525 C CA   . VAL   A 1 121 ? 24.097 -12.038 13.201  1.00 14.89 ?  121 VAL   A CA   1 
ATOM   2526 C C    . VAL   A 1 121 ? 24.207 -10.655 12.570  1.00 13.70 ?  121 VAL   A C    1 
ATOM   2527 O O    . VAL   A 1 121 ? 25.180 -9.933  12.813  1.00 14.57 ?  121 VAL   A O    1 
ATOM   2528 C CB   . VAL   A 1 121 ? 23.669 -11.898 14.681  1.00 17.99 ?  121 VAL   A CB   1 
ATOM   2529 C CG1  . VAL   A 1 121 ? 22.285 -11.258 14.786  1.00 18.66 ?  121 VAL   A CG1  1 
ATOM   2530 C CG2  . VAL   A 1 121 ? 23.676 -13.233 15.400  1.00 20.26 ?  121 VAL   A CG2  1 
ATOM   2531 H H    . VAL   A 1 121 ? 26.055 -12.171 13.161  1.00 17.97 ?  121 VAL   A H    1 
ATOM   2532 H HA   . VAL   A 1 121 ? 23.418 -12.549 12.736  1.00 18.02 ?  121 VAL   A HA   1 
ATOM   2533 H HB   . VAL   A 1 121 ? 24.293 -11.317 15.139  1.00 21.74 ?  121 VAL   A HB   1 
ATOM   2534 H HG11 . VAL   A 1 121 ? 21.972 -11.321 15.703  1.00 22.54 ?  121 VAL   A HG11 1 
ATOM   2535 H HG12 . VAL   A 1 121 ? 22.345 -10.325 14.524  1.00 22.54 ?  121 VAL   A HG12 1 
ATOM   2536 H HG13 . VAL   A 1 121 ? 21.673 -11.728 14.197  1.00 22.54 ?  121 VAL   A HG13 1 
ATOM   2537 H HG21 . VAL   A 1 121 ? 23.328 -13.112 16.304  1.00 24.46 ?  121 VAL   A HG21 1 
ATOM   2538 H HG22 . VAL   A 1 121 ? 23.109 -13.858 14.919  1.00 24.46 ?  121 VAL   A HG22 1 
ATOM   2539 H HG23 . VAL   A 1 121 ? 24.581 -13.569 15.441  1.00 24.46 ?  121 VAL   A HG23 1 
ATOM   2540 N N    . LEU   A 1 122 ? 23.190 -10.267 11.793  1.00 13.54 ?  122 LEU   A N    1 
ATOM   2541 C CA   . LEU   A 1 122 ? 23.192 -8.966  11.129  1.00 13.34 ?  122 LEU   A CA   1 
ATOM   2542 C C    . LEU   A 1 122 ? 21.795 -8.374  11.096  1.00 13.07 ?  122 LEU   A C    1 
ATOM   2543 O O    . LEU   A 1 122 ? 20.807 -9.098  10.960  1.00 14.22 ?  122 LEU   A O    1 
ATOM   2544 C CB   . LEU   A 1 122 ? 23.610 -9.059  9.656   1.00 14.77 ?  122 LEU   A CB   1 
ATOM   2545 C CG   . LEU   A 1 122 ? 24.807 -9.908  9.272   1.00 14.82 ?  122 LEU   A CG   1 
ATOM   2546 C CD1  . LEU   A 1 122 ? 24.388 -11.359 9.057   1.00 15.93 ?  122 LEU   A CD1  1 
ATOM   2547 C CD2  . LEU   A 1 122 ? 25.468 -9.332  8.026   1.00 14.08 ?  122 LEU   A CD2  1 
ATOM   2548 H H    . LEU   A 1 122 ? 22.489 -10.741 11.630  1.00 16.39 ?  122 LEU   A H    1 
ATOM   2549 H HA   . LEU   A 1 122 ? 23.791 -8.354  11.591  1.00 16.15 ?  122 LEU   A HA   1 
ATOM   2550 H HB2  . LEU   A 1 122 ? 22.862 -9.411  9.156   1.00 17.87 ?  122 LEU   A HB2  1 
ATOM   2551 H HB3  . LEU   A 1 122 ? 23.806 -8.163  9.344   1.00 17.87 ?  122 LEU   A HB3  1 
ATOM   2552 H HG   . LEU   A 1 122 ? 25.469 -9.889  9.984   1.00 17.93 ?  122 LEU   A HG   1 
ATOM   2553 H HD11 . LEU   A 1 122 ? 25.153 -11.876 8.762   1.00 19.26 ?  122 LEU   A HD11 1 
ATOM   2554 H HD12 . LEU   A 1 122 ? 24.052 -11.716 9.894   1.00 19.26 ?  122 LEU   A HD12 1 
ATOM   2555 H HD13 . LEU   A 1 122 ? 23.691 -11.389 8.382   1.00 19.26 ?  122 LEU   A HD13 1 
ATOM   2556 H HD21 . LEU   A 1 122 ? 26.206 -9.907  7.755   1.00 17.05 ?  122 LEU   A HD21 1 
ATOM   2557 H HD22 . LEU   A 1 122 ? 24.813 -9.286  7.311   1.00 17.05 ?  122 LEU   A HD22 1 
ATOM   2558 H HD23 . LEU   A 1 122 ? 25.804 -8.443  8.223   1.00 17.05 ?  122 LEU   A HD23 1 
ATOM   2559 N N    A LEU   A 1 123 ? 21.723 -7.043  11.181  0.86 12.65 ?  123 LEU   A N    1 
ATOM   2560 N N    B LEU   A 1 123 ? 21.744 -7.048  11.242  0.14 12.76 ?  123 LEU   A N    1 
ATOM   2561 C CA   A LEU   A 1 123 ? 20.545 -6.255  10.818  0.86 12.61 ?  123 LEU   A CA   1 
ATOM   2562 C CA   B LEU   A 1 123 ? 20.558 -6.244  10.980  0.14 12.73 ?  123 LEU   A CA   1 
ATOM   2563 C C    A LEU   A 1 123 ? 20.776 -5.715  9.413   0.86 12.25 ?  123 LEU   A C    1 
ATOM   2564 C C    B LEU   A 1 123 ? 20.762 -5.616  9.608   0.14 12.42 ?  123 LEU   A C    1 
ATOM   2565 O O    A LEU   A 1 123 ? 21.839 -5.152  9.152   0.86 12.42 ?  123 LEU   A O    1 
ATOM   2566 O O    B LEU   A 1 123 ? 21.562 -4.686  9.461   0.14 12.32 ?  123 LEU   A O    1 
ATOM   2567 C CB   A LEU   A 1 123 ? 20.411 -5.082  11.792  0.86 13.10 ?  123 LEU   A CB   1 
ATOM   2568 C CB   B LEU   A 1 123 ? 20.412 -5.162  12.048  0.14 13.02 ?  123 LEU   A CB   1 
ATOM   2569 C CG   A LEU   A 1 123 ? 19.372 -4.014  11.452  0.86 13.78 ?  123 LEU   A CG   1 
ATOM   2570 C CG   B LEU   A 1 123 ? 19.391 -4.057  11.761  0.14 13.36 ?  123 LEU   A CG   1 
ATOM   2571 C CD1  A LEU   A 1 123 ? 17.969 -4.606  11.447  0.86 14.62 ?  123 LEU   A CD1  1 
ATOM   2572 C CD1  B LEU   A 1 123 ? 17.975 -4.609  11.795  0.14 13.66 ?  123 LEU   A CD1  1 
ATOM   2573 C CD2  A LEU   A 1 123 ? 19.462 -2.850  12.439  0.86 14.86 ?  123 LEU   A CD2  1 
ATOM   2574 C CD2  B LEU   A 1 123 ? 19.549 -2.900  12.739  0.14 13.67 ?  123 LEU   A CD2  1 
ATOM   2575 H H    A LEU   A 1 123 ? 22.378 -6.548  11.455  0.86 15.33 ?  123 LEU   A H    1 
ATOM   2576 H H    B LEU   A 1 123 ? 22.421 -6.571  11.494  0.14 15.47 ?  123 LEU   A H    1 
ATOM   2577 H HA   A LEU   A 1 123 ? 19.742 -6.798  10.840  0.86 15.29 ?  123 LEU   A HA   1 
ATOM   2578 H HA   B LEU   A 1 123 ? 19.767 -6.801  10.968  0.14 15.42 ?  123 LEU   A HA   1 
ATOM   2579 H HB2  A LEU   A 1 123 ? 20.174 -5.436  12.665  0.86 15.87 ?  123 LEU   A HB2  1 
ATOM   2580 H HB2  B LEU   A 1 123 ? 20.150 -5.591  12.877  0.14 15.77 ?  123 LEU   A HB2  1 
ATOM   2581 H HB3  A LEU   A 1 123 ? 21.268 -4.633  11.852  0.86 15.87 ?  123 LEU   A HB3  1 
ATOM   2582 H HB3  B LEU   A 1 123 ? 21.275 -4.734  12.166  0.14 15.77 ?  123 LEU   A HB3  1 
ATOM   2583 H HG   A LEU   A 1 123 ? 19.550 -3.661  10.565  0.86 16.68 ?  123 LEU   A HG   1 
ATOM   2584 H HG   B LEU   A 1 123 ? 19.545 -3.703  10.873  0.14 16.18 ?  123 LEU   A HG   1 
ATOM   2585 H HD11 A LEU   A 1 123 ? 17.325 -3.903  11.269  0.86 17.69 ?  123 LEU   A HD11 1 
ATOM   2586 H HD11 B LEU   A 1 123 ? 17.351 -3.888  11.620  0.14 16.54 ?  123 LEU   A HD11 1 
ATOM   2587 H HD12 A LEU   A 1 123 ? 17.912 -5.288  10.757  0.86 17.69 ?  123 LEU   A HD12 1 
ATOM   2588 H HD12 B LEU   A 1 123 ? 17.888 -5.295  11.114  0.14 16.54 ?  123 LEU   A HD12 1 
ATOM   2589 H HD13 A LEU   A 1 123 ? 17.789 -5.004  12.316  0.86 17.69 ?  123 LEU   A HD13 1 
ATOM   2590 H HD13 B LEU   A 1 123 ? 17.805 -4.990  12.671  0.14 16.54 ?  123 LEU   A HD13 1 
ATOM   2591 H HD21 A LEU   A 1 123 ? 18.796 -2.188  12.207  0.86 17.99 ?  123 LEU   A HD21 1 
ATOM   2592 H HD21 B LEU   A 1 123 ? 18.887 -2.222  12.532  0.14 16.55 ?  123 LEU   A HD21 1 
ATOM   2593 H HD22 A LEU   A 1 123 ? 19.294 -3.189  13.335  0.86 17.99 ?  123 LEU   A HD22 1 
ATOM   2594 H HD22 B LEU   A 1 123 ? 19.417 -3.229  13.641  0.14 16.55 ?  123 LEU   A HD22 1 
ATOM   2595 H HD23 A LEU   A 1 123 ? 20.349 -2.466  12.392  0.86 17.99 ?  123 LEU   A HD23 1 
ATOM   2596 H HD23 B LEU   A 1 123 ? 20.441 -2.530  12.647  0.14 16.55 ?  123 LEU   A HD23 1 
ATOM   2597 N N    A ALA   A 1 124 ? 19.803 -5.870  8.511   0.86 11.47 ?  124 ALA   A N    1 
ATOM   2598 N N    B ALA   A 1 124 ? 20.052 -6.120  8.608   0.14 12.22 ?  124 ALA   A N    1 
ATOM   2599 C CA   A ALA   A 1 124 ? 20.079 -5.578  7.110   0.86 11.52 ?  124 ALA   A CA   1 
ATOM   2600 C CA   B ALA   A 1 124 ? 20.303 -5.773  7.221   0.14 12.32 ?  124 ALA   A CA   1 
ATOM   2601 C C    A ALA   A 1 124 ? 18.830 -5.114  6.373   0.86 11.74 ?  124 ALA   A C    1 
ATOM   2602 C C    B ALA   A 1 124 ? 19.046 -5.245  6.544   0.14 12.19 ?  124 ALA   A C    1 
ATOM   2603 O O    A ALA   A 1 124 ? 17.702 -5.495  6.725   0.86 12.63 ?  124 ALA   A O    1 
ATOM   2604 O O    B ALA   A 1 124 ? 17.922 -5.548  6.965   0.14 12.13 ?  124 ALA   A O    1 
ATOM   2605 C CB   A ALA   A 1 124 ? 20.650 -6.803  6.391   0.86 12.27 ?  124 ALA   A CB   1 
ATOM   2606 C CB   B ALA   A 1 124 ? 20.801 -7.001  6.446   0.14 12.47 ?  124 ALA   A CB   1 
ATOM   2607 H H    A ALA   A 1 124 ? 19.002 -6.136  8.680   0.86 13.92 ?  124 ALA   A H    1 
ATOM   2608 H H    B ALA   A 1 124 ? 19.406 -6.676  8.711   0.14 14.81 ?  124 ALA   A H    1 
ATOM   2609 H HA   A ALA   A 1 124 ? 20.740 -4.870  7.070   0.86 13.97 ?  124 ALA   A HA   1 
ATOM   2610 H HA   B ALA   A 1 124 ? 20.988 -5.087  7.186   0.14 14.94 ?  124 ALA   A HA   1 
ATOM   2611 H HB1  A ALA   A 1 124 ? 20.825 -6.571  5.462   0.86 14.87 ?  124 ALA   A HB1  1 
ATOM   2612 H HB1  B ALA   A 1 124 ? 20.964 -6.749  5.523   0.14 15.11 ?  124 ALA   A HB1  1 
ATOM   2613 H HB2  A ALA   A 1 124 ? 21.482 -7.062  6.823   0.86 14.87 ?  124 ALA   A HB2  1 
ATOM   2614 H HB2  B ALA   A 1 124 ? 21.622 -7.319  6.852   0.14 15.11 ?  124 ALA   A HB2  1 
ATOM   2615 H HB3  A ALA   A 1 124 ? 20.012 -7.526  6.438   0.86 14.87 ?  124 ALA   A HB3  1 
ATOM   2616 H HB3  B ALA   A 1 124 ? 20.122 -7.693  6.484   0.14 15.11 ?  124 ALA   A HB3  1 
ATOM   2617 N N    A PRO   A 1 125 ? 19.010 -4.357  5.294   0.86 11.68 ?  125 PRO   A N    1 
ATOM   2618 N N    B PRO   A 1 125 ? 19.204 -4.447  5.487   0.14 11.93 ?  125 PRO   A N    1 
ATOM   2619 C CA   A PRO   A 1 125 ? 17.947 -4.123  4.320   0.86 12.24 ?  125 PRO   A CA   1 
ATOM   2620 C CA   B PRO   A 1 125 ? 18.057 -4.084  4.651   0.14 12.02 ?  125 PRO   A CA   1 
ATOM   2621 C C    A PRO   A 1 125 ? 18.011 -5.198  3.240   0.86 12.23 ?  125 PRO   A C    1 
ATOM   2622 C C    B PRO   A 1 125 ? 17.975 -5.018  3.457   0.14 12.33 ?  125 PRO   A C    1 
ATOM   2623 O O    A PRO   A 1 125 ? 18.976 -5.957  3.139   0.86 12.85 ?  125 PRO   A O    1 
ATOM   2624 O O    B PRO   A 1 125 ? 18.843 -5.880  3.291   0.14 12.37 ?  125 PRO   A O    1 
ATOM   2625 C CB   A PRO   A 1 125 ? 18.369 -2.775  3.721   0.86 12.51 ?  125 PRO   A CB   1 
ATOM   2626 C CB   B PRO   A 1 125 ? 18.407 -2.661  4.210   0.14 12.06 ?  125 PRO   A CB   1 
ATOM   2627 C CG   A PRO   A 1 125 ? 19.881 -2.934  3.606   0.86 12.25 ?  125 PRO   A CG   1 
ATOM   2628 C CG   B PRO   A 1 125 ? 19.912 -2.713  4.057   0.14 12.18 ?  125 PRO   A CG   1 
ATOM   2629 C CD   A PRO   A 1 125 ? 20.273 -3.711  4.870   0.86 12.21 ?  125 PRO   A CD   1 
ATOM   2630 C CD   B PRO   A 1 125 ? 20.426 -3.742  5.057   0.14 12.15 ?  125 PRO   A CD   1 
ATOM   2631 H HA   A PRO   A 1 125 ? 17.068 -4.078  4.732   0.86 14.84 ?  125 PRO   A HA   1 
ATOM   2632 H HA   B PRO   A 1 125 ? 17.227 -4.091  5.156   0.14 14.57 ?  125 PRO   A HA   1 
ATOM   2633 H HB2  A PRO   A 1 125 ? 17.950 -2.654  2.850   0.86 15.16 ?  125 PRO   A HB2  1 
ATOM   2634 H HB2  B PRO   A 1 125 ? 17.976 -2.460  3.363   0.14 14.62 ?  125 PRO   A HB2  1 
ATOM   2635 H HB3  A PRO   A 1 125 ? 18.127 -2.051  4.325   0.86 15.16 ?  125 PRO   A HB3  1 
ATOM   2636 H HB3  B PRO   A 1 125 ? 18.146 -2.024  4.894   0.14 14.62 ?  125 PRO   A HB3  1 
ATOM   2637 H HG2  A PRO   A 1 125 ? 20.098 -3.439  2.806   0.86 14.85 ?  125 PRO   A HG2  1 
ATOM   2638 H HG2  B PRO   A 1 125 ? 20.133 -2.981  3.152   0.14 14.77 ?  125 PRO   A HG2  1 
ATOM   2639 H HG3  A PRO   A 1 125 ? 20.300 -2.059  3.585   0.86 14.85 ?  125 PRO   A HG3  1 
ATOM   2640 H HG3  B PRO   A 1 125 ? 20.285 -1.841  4.250   0.14 14.77 ?  125 PRO   A HG3  1 
ATOM   2641 H HD2  A PRO   A 1 125 ? 20.946 -4.375  4.659   0.86 14.80 ?  125 PRO   A HD2  1 
ATOM   2642 H HD2  B PRO   A 1 125 ? 21.040 -4.358  4.622   0.14 14.73 ?  125 PRO   A HD2  1 
ATOM   2643 H HD3  A PRO   A 1 125 ? 20.592 -3.092  5.553   0.86 14.80 ?  125 PRO   A HD3  1 
ATOM   2644 H HD3  B PRO   A 1 125 ? 20.846 -3.298  5.811   0.14 14.73 ?  125 PRO   A HD3  1 
ATOM   2645 N N    A LEU   A 1 126 ? 16.972 -5.234  2.411   0.86 12.43 ?  126 LEU   A N    1 
ATOM   2646 N N    B LEU   A 1 126 ? 16.954 -4.865  2.621   0.14 12.89 ?  126 LEU   A N    1 
ATOM   2647 C CA   A LEU   A 1 126 ? 17.005 -6.063  1.214   0.86 12.65 ?  126 LEU   A CA   1 
ATOM   2648 C CA   B LEU   A 1 126 ? 16.907 -5.617  1.375   0.14 13.41 ?  126 LEU   A CA   1 
ATOM   2649 C C    A LEU   A 1 126 ? 17.937 -5.451  0.177   0.86 12.59 ?  126 LEU   A C    1 
ATOM   2650 C C    B LEU   A 1 126 ? 17.923 -5.040  0.395   0.14 13.32 ?  126 LEU   A C    1 
ATOM   2651 O O    A LEU   A 1 126 ? 17.707 -4.333  -0.303  0.86 12.83 ?  126 LEU   A O    1 
ATOM   2652 O O    B LEU   A 1 126 ? 18.069 -3.821  0.280   0.14 13.66 ?  126 LEU   A O    1 
ATOM   2653 C CB   A LEU   A 1 126 ? 15.605 -6.220  0.635   0.86 13.18 ?  126 LEU   A CB   1 
ATOM   2654 C CB   B LEU   A 1 126 ? 15.503 -5.528  0.775   0.14 14.64 ?  126 LEU   A CB   1 
ATOM   2655 C CG   A LEU   A 1 126 ? 14.679 -7.159  1.406   0.86 14.52 ?  126 LEU   A CG   1 
ATOM   2656 C CG   B LEU   A 1 126 ? 14.908 -6.791  0.150   0.14 15.49 ?  126 LEU   A CG   1 
ATOM   2657 C CD1  A LEU   A 1 126 ? 13.256 -7.031  0.895   0.86 15.80 ?  126 LEU   A CD1  1 
ATOM   2658 C CD1  B LEU   A 1 126 ? 15.163 -7.999  1.032   0.14 15.80 ?  126 LEU   A CD1  1 
ATOM   2659 C CD2  A LEU   A 1 126 ? 15.165 -8.612  1.288   0.86 14.97 ?  126 LEU   A CD2  1 
ATOM   2660 C CD2  B LEU   A 1 126 ? 13.413 -6.607  -0.071  0.14 15.60 ?  126 LEU   A CD2  1 
ATOM   2661 H H    A LEU   A 1 126 ? 16.247 -4.786  2.515   0.86 15.07 ?  126 LEU   A H    1 
ATOM   2662 H H    B LEU   A 1 126 ? 16.281 -4.345  2.756   0.14 15.62 ?  126 LEU   A H    1 
ATOM   2663 H HA   A LEU   A 1 126 ? 17.347 -6.938  1.438   0.86 15.32 ?  126 LEU   A HA   1 
ATOM   2664 H HA   B LEU   A 1 126 ? 17.138 -6.543  1.555   0.14 16.24 ?  126 LEU   A HA   1 
ATOM   2665 H HB2  A LEU   A 1 126 ? 15.180 -5.348  0.617   0.86 15.97 ?  126 LEU   A HB2  1 
ATOM   2666 H HB2  B LEU   A 1 126 ? 14.894 -5.245  1.473   0.14 17.72 ?  126 LEU   A HB2  1 
ATOM   2667 H HB3  A LEU   A 1 126 ? 15.681 -6.563  -0.268  0.86 15.97 ?  126 LEU   A HB3  1 
ATOM   2668 H HB3  B LEU   A 1 126 ? 15.524 -4.851  0.079   0.14 17.72 ?  126 LEU   A HB3  1 
ATOM   2669 H HG   A LEU   A 1 126 ? 14.690 -6.918  2.347   0.86 17.57 ?  126 LEU   A HG   1 
ATOM   2670 H HG   B LEU   A 1 126 ? 15.323 -6.947  -0.713  0.14 18.73 ?  126 LEU   A HG   1 
ATOM   2671 H HD11 A LEU   A 1 126 ? 12.689 -7.639  1.391   0.86 19.11 ?  126 LEU   A HD11 1 
ATOM   2672 H HD11 B LEU   A 1 126 ? 14.500 -8.675  0.838   0.14 19.10 ?  126 LEU   A HD11 1 
ATOM   2673 H HD12 A LEU   A 1 126 ? 12.963 -6.119  1.019   0.86 19.11 ?  126 LEU   A HD12 1 
ATOM   2674 H HD12 B LEU   A 1 126 ? 16.052 -8.342  0.846   0.14 19.10 ?  126 LEU   A HD12 1 
ATOM   2675 H HD13 A LEU   A 1 126 ? 13.244 -7.261  -0.049  0.86 19.11 ?  126 LEU   A HD13 1 
ATOM   2676 H HD13 B LEU   A 1 126 ? 15.099 -7.727  1.962   0.14 19.10 ?  126 LEU   A HD13 1 
ATOM   2677 H HD21 A LEU   A 1 126 ? 14.496 -9.200  1.665   0.86 18.11 ?  126 LEU   A HD21 1 
ATOM   2678 H HD21 B LEU   A 1 126 ? 13.054 -7.405  -0.491  0.14 18.87 ?  126 LEU   A HD21 1 
ATOM   2679 H HD22 A LEU   A 1 126 ? 15.304 -8.821  0.351   0.86 18.11 ?  126 LEU   A HD22 1 
ATOM   2680 H HD22 B LEU   A 1 126 ? 12.982 -6.466  0.788   0.14 18.87 ?  126 LEU   A HD22 1 
ATOM   2681 H HD23 A LEU   A 1 126 ? 16.002 -8.707  1.773   0.86 18.11 ?  126 LEU   A HD23 1 
ATOM   2682 H HD23 B LEU   A 1 126 ? 13.267 -5.838  -0.643  0.14 18.87 ?  126 LEU   A HD23 1 
ATOM   2683 N N    A LEU   A 1 127 ? 18.984 -6.190  -0.182  0.86 12.42 ?  127 LEU   A N    1 
ATOM   2684 N N    B LEU   A 1 127 ? 18.639 -5.917  -0.306  0.14 12.92 ?  127 LEU   A N    1 
ATOM   2685 C CA   A LEU   A 1 127 ? 19.966 -5.684  -1.128  0.86 12.41 ?  127 LEU   A CA   1 
ATOM   2686 C CA   B LEU   A 1 127 ? 19.688 -5.481  -1.218  0.14 12.49 ?  127 LEU   A CA   1 
ATOM   2687 C C    A LEU   A 1 127 ? 19.339 -5.475  -2.496  0.86 11.90 ?  127 LEU   A C    1 
ATOM   2688 C C    B LEU   A 1 127 ? 19.176 -5.399  -2.656  0.14 12.38 ?  127 LEU   A C    1 
ATOM   2689 O O    A LEU   A 1 127 ? 18.519 -6.271  -2.961  0.86 12.48 ?  127 LEU   A O    1 
ATOM   2690 O O    B LEU   A 1 127 ? 18.273 -6.134  -3.066  0.14 12.31 ?  127 LEU   A O    1 
ATOM   2691 C CB   A LEU   A 1 127 ? 21.147 -6.651  -1.250  0.86 13.59 ?  127 LEU   A CB   1 
ATOM   2692 C CB   B LEU   A 1 127 ? 20.915 -6.400  -1.141  0.14 12.36 ?  127 LEU   A CB   1 
ATOM   2693 C CG   A LEU   A 1 127 ? 21.932 -6.935  0.023   0.86 13.47 ?  127 LEU   A CG   1 
ATOM   2694 C CG   B LEU   A 1 127 ? 21.792 -6.320  0.119   0.14 11.65 ?  127 LEU   A CG   1 
ATOM   2695 C CD1  A LEU   A 1 127 ? 23.029 -7.928  -0.269  0.86 14.17 ?  127 LEU   A CD1  1 
ATOM   2696 C CD1  B LEU   A 1 127 ? 23.019 -7.226  -0.005  0.14 11.76 ?  127 LEU   A CD1  1 
ATOM   2697 C CD2  A LEU   A 1 127 ? 22.536 -5.661  0.564   0.86 14.10 ?  127 LEU   A CD2  1 
ATOM   2698 C CD2  B LEU   A 1 127 ? 22.211 -4.885  0.418   0.14 11.35 ?  127 LEU   A CD2  1 
ATOM   2699 H H    A LEU   A 1 127 ? 19.148 -6.973  0.116   0.86 15.05 ?  127 LEU   A H    1 
ATOM   2700 H H    B LEU   A 1 127 ? 18.538 -6.773  -0.263  0.14 15.65 ?  127 LEU   A H    1 
ATOM   2701 H HA   A LEU   A 1 127 ? 20.299 -4.827  -0.819  0.86 15.04 ?  127 LEU   A HA   1 
ATOM   2702 H HA   B LEU   A 1 127 ? 19.976 -4.590  -0.947  0.14 15.13 ?  127 LEU   A HA   1 
ATOM   2703 H HB2  A LEU   A 1 127 ? 20.803 -7.493  -1.579  0.86 16.46 ?  127 LEU   A HB2  1 
ATOM   2704 H HB2  B LEU   A 1 127 ? 20.612 -7.317  -1.212  0.14 14.98 ?  127 LEU   A HB2  1 
ATOM   2705 H HB3  A LEU   A 1 127 ? 21.765 -6.278  -1.895  0.86 16.46 ?  127 LEU   A HB3  1 
ATOM   2706 H HB3  B LEU   A 1 127 ? 21.490 -6.194  -1.894  0.14 14.98 ?  127 LEU   A HB3  1 
ATOM   2707 H HG   A LEU   A 1 127 ? 21.340 -7.313  0.694   0.86 16.31 ?  127 LEU   A HG   1 
ATOM   2708 H HG   B LEU   A 1 127 ? 21.278 -6.638  0.877   0.14 14.13 ?  127 LEU   A HG   1 
ATOM   2709 H HD11 A LEU   A 1 127 ? 23.505 -8.123  0.553   0.86 17.15 ?  127 LEU   A HD11 1 
ATOM   2710 H HD11 B LEU   A 1 127 ? 23.549 -7.159  0.806   0.14 14.26 ?  127 LEU   A HD11 1 
ATOM   2711 H HD12 A LEU   A 1 127 ? 22.634 -8.744  -0.621  0.86 17.15 ?  127 LEU   A HD12 1 
ATOM   2712 H HD12 B LEU   A 1 127 ? 22.725 -8.142  -0.131  0.14 14.26 ?  127 LEU   A HD12 1 
ATOM   2713 H HD13 A LEU   A 1 127 ? 23.634 -7.547  -0.922  0.86 17.15 ?  127 LEU   A HD13 1 
ATOM   2714 H HD13 B LEU   A 1 127 ? 23.547 -6.941  -0.768  0.14 14.26 ?  127 LEU   A HD13 1 
ATOM   2715 H HD21 A LEU   A 1 127 ? 23.126 -5.886  1.305   0.86 17.07 ?  127 LEU   A HD21 1 
ATOM   2716 H HD21 B LEU   A 1 127 ? 22.914 -4.892  1.084   0.14 13.76 ?  127 LEU   A HD21 1 
ATOM   2717 H HD22 A LEU   A 1 127 ? 23.051 -5.235  -0.142  0.86 17.07 ?  127 LEU   A HD22 1 
ATOM   2718 H HD22 B LEU   A 1 127 ? 22.533 -4.476  -0.401  0.14 13.76 ?  127 LEU   A HD22 1 
ATOM   2719 H HD23 A LEU   A 1 127 ? 21.833 -5.075  0.865   0.86 17.07 ?  127 LEU   A HD23 1 
ATOM   2720 H HD23 B LEU   A 1 127 ? 21.441 -4.398  0.751   0.14 13.76 ?  127 LEU   A HD23 1 
ATOM   2721 N N    A SER   A 1 128 ? 19.775 -4.412  -3.156  0.86 11.92 ?  128 SER   A N    1 
ATOM   2722 N N    B SER   A 1 128 ? 19.773 -4.478  -3.413  0.14 12.47 ?  128 SER   A N    1 
ATOM   2723 C CA   A SER   A 1 128 ? 19.351 -4.010  -4.489  0.86 11.80 ?  128 SER   A CA   1 
ATOM   2724 C CA   B SER   A 1 128 ? 19.453 -4.181  -4.811  0.14 12.46 ?  128 SER   A CA   1 
ATOM   2725 C C    A SER   A 1 128 ? 17.895 -3.564  -4.564  0.86 12.14 ?  128 SER   A C    1 
ATOM   2726 C C    B SER   A 1 128 ? 18.054 -3.614  -5.042  0.14 12.64 ?  128 SER   A C    1 
ATOM   2727 O O    A SER   A 1 128 ? 17.430 -3.237  -5.654  0.86 13.38 ?  128 SER   A O    1 
ATOM   2728 O O    B SER   A 1 128 ? 17.691 -3.329  -6.188  0.14 12.61 ?  128 SER   A O    1 
ATOM   2729 C CB   A SER   A 1 128 ? 19.696 -5.036  -5.579  0.86 12.18 ?  128 SER   A CB   1 
ATOM   2730 C CB   B SER   A 1 128 ? 19.704 -5.373  -5.745  0.14 12.46 ?  128 SER   A CB   1 
ATOM   2731 O OG   A SER   A 1 128 ? 21.111 -5.236  -5.654  0.86 12.48 ?  128 SER   A OG   1 
ATOM   2732 O OG   B SER   A 1 128 ? 21.091 -5.655  -5.841  0.14 12.51 ?  128 SER   A OG   1 
ATOM   2733 H H    A SER   A 1 128 ? 20.371 -3.881  -2.832  0.86 14.45 ?  128 SER   A H    1 
ATOM   2734 H H    B SER   A 1 128 ? 20.410 -3.989  -3.112  0.14 15.12 ?  128 SER   A H    1 
ATOM   2735 H HA   A SER   A 1 128 ? 19.863 -3.225  -4.706  0.86 14.31 ?  128 SER   A HA   1 
ATOM   2736 H HA   B SER   A 1 128 ? 20.078 -3.499  -5.082  0.14 15.10 ?  128 SER   A HA   1 
ATOM   2737 H HB2  A SER   A 1 128 ? 19.260 -5.877  -5.376  0.86 14.77 ?  128 SER   A HB2  1 
ATOM   2738 H HB2  B SER   A 1 128 ? 19.242 -6.153  -5.415  0.14 15.10 ?  128 SER   A HB2  1 
ATOM   2739 H HB3  A SER   A 1 128 ? 19.377 -4.699  -6.437  0.86 14.77 ?  128 SER   A HB3  1 
ATOM   2740 H HB3  B SER   A 1 128 ? 19.368 -5.143  -6.636  0.14 15.10 ?  128 SER   A HB3  1 
ATOM   2741 H HG   A SER   A 1 128 ? 21.492 -4.510  -5.828  0.86 15.12 ?  128 SER   A HG   1 
ATOM   2742 H HG   B SER   A 1 128 ? 21.500 -4.985  -6.140  0.14 15.15 ?  128 SER   A HG   1 
ATOM   2743 N N    A ALA   A 1 129 ? 17.187 -3.478  -3.434  0.86 12.95 ?  129 ALA   A N    1 
ATOM   2744 N N    B ALA   A 1 129 ? 17.269 -3.426  -3.983  0.14 13.08 ?  129 ALA   A N    1 
ATOM   2745 C CA   A ALA   A 1 129 ? 15.825 -2.962  -3.423  0.86 13.22 ?  129 ALA   A CA   1 
ATOM   2746 C CA   B ALA   A 1 129 ? 15.964 -2.796  -4.109  0.14 13.61 ?  129 ALA   A CA   1 
ATOM   2747 C C    A ALA   A 1 129 ? 15.834 -1.429  -3.423  0.86 12.92 ?  129 ALA   A C    1 
ATOM   2748 C C    B ALA   A 1 129 ? 16.138 -1.277  -4.032  0.14 13.92 ?  129 ALA   A C    1 
ATOM   2749 O O    A ALA   A 1 129 ? 16.880 -0.779  -3.530  0.86 12.87 ?  129 ALA   A O    1 
ATOM   2750 O O    B ALA   A 1 129 ? 17.248 -0.751  -4.152  0.14 13.62 ?  129 ALA   A O    1 
ATOM   2751 C CB   A ALA   A 1 129 ? 15.047 -3.542  -2.239  0.86 14.73 ?  129 ALA   A CB   1 
ATOM   2752 C CB   B ALA   A 1 129 ? 15.008 -3.350  -3.053  0.14 14.03 ?  129 ALA   A CB   1 
ATOM   2753 H H    A ALA   A 1 129 ? 17.481 -3.701  -2.650  0.86 15.69 ?  129 ALA   A H    1 
ATOM   2754 H H    B ALA   A 1 129 ? 17.464 -3.646  -3.175  0.14 15.85 ?  129 ALA   A H    1 
ATOM   2755 H HA   A ALA   A 1 129 ? 15.383 -3.251  -4.230  0.86 16.01 ?  129 ALA   A HA   1 
ATOM   2756 H HA   B ALA   A 1 129 ? 15.596 -3.014  -4.983  0.14 16.48 ?  129 ALA   A HA   1 
ATOM   2757 H HB1  A ALA   A 1 129 ? 14.137 -3.195  -2.258  0.86 17.83 ?  129 ALA   A HB1  1 
ATOM   2758 H HB1  B ALA   A 1 129 ? 14.137 -2.936  -3.162  0.14 16.99 ?  129 ALA   A HB1  1 
ATOM   2759 H HB2  A ALA   A 1 129 ? 15.030 -4.508  -2.315  0.86 17.83 ?  129 ALA   A HB2  1 
ATOM   2760 H HB2  B ALA   A 1 129 ? 14.932 -4.311  -3.171  0.14 16.99 ?  129 ALA   A HB2  1 
ATOM   2761 H HB3  A ALA   A 1 129 ? 15.479 -3.281  -1.411  0.86 17.83 ?  129 ALA   A HB3  1 
ATOM   2762 H HB3  B ALA   A 1 129 ? 15.362 -3.152  -2.172  0.14 16.99 ?  129 ALA   A HB3  1 
ATOM   2763 N N    A GLY   A 1 130 ? 14.642 -0.843  -3.338  0.86 14.25 ?  130 GLY   A N    1 
ATOM   2764 N N    B GLY   A 1 130 ? 15.042 -0.548  -3.833  0.14 14.50 ?  130 GLY   A N    1 
ATOM   2765 C CA   A GLY   A 1 130 ? 14.543 0.607   -3.307  0.86 14.96 ?  130 GLY   A CA   1 
ATOM   2766 C CA   B GLY   A 1 130 ? 15.143 0.900   -3.757  0.14 15.14 ?  130 GLY   A CA   1 
ATOM   2767 C C    A GLY   A 1 130 ? 15.151 1.224   -4.550  0.86 14.15 ?  130 GLY   A C    1 
ATOM   2768 C C    B GLY   A 1 130 ? 15.581 1.482   -5.088  0.14 15.76 ?  130 GLY   A C    1 
ATOM   2769 O O    A GLY   A 1 130 ? 14.903 0.770   -5.671  0.86 14.16 ?  130 GLY   A O    1 
ATOM   2770 O O    B GLY   A 1 130 ? 15.139 1.051   -6.159  0.14 16.23 ?  130 GLY   A O    1 
ATOM   2771 H H    A GLY   A 1 130 ? 13.887 -1.259  -3.301  0.86 17.24 ?  130 GLY   A H    1 
ATOM   2772 H H    B GLY   A 1 130 ? 14.247 -0.855  -3.748  0.14 17.54 ?  130 GLY   A H    1 
ATOM   2773 H HA2  A GLY   A 1 130 ? 13.604 0.867   -3.251  0.86 18.10 ?  130 GLY   A HA2  1 
ATOM   2774 H HA2  B GLY   A 1 130 ? 14.283 1.280   -3.514  0.14 18.31 ?  130 GLY   A HA2  1 
ATOM   2775 H HA3  A GLY   A 1 130 ? 15.005 0.950   -2.533  0.86 18.10 ?  130 GLY   A HA3  1 
ATOM   2776 H HA3  B GLY   A 1 130 ? 15.794 1.150   -3.083  0.14 18.31 ?  130 GLY   A HA3  1 
ATOM   2777 N N    A ILE   A 1 131 ? 15.959 2.273   -4.352  0.86 13.79 ?  131 ILE   A N    1 
ATOM   2778 N N    B ILE   A 1 131 ? 16.480 2.468   -5.026  0.14 16.02 ?  131 ILE   A N    1 
ATOM   2779 C CA   A ILE   A 1 131 ? 16.525 3.023   -5.470  0.86 13.50 ?  131 ILE   A CA   1 
ATOM   2780 C CA   B ILE   A 1 131 ? 16.958 3.114   -6.244  0.14 16.19 ?  131 ILE   A CA   1 
ATOM   2781 C C    A ILE   A 1 131 ? 17.541 2.236   -6.281  0.86 12.83 ?  131 ILE   A C    1 
ATOM   2782 C C    B ILE   A 1 131 ? 17.838 2.201   -7.084  0.14 15.83 ?  131 ILE   A C    1 
ATOM   2783 O O    A ILE   A 1 131 ? 17.980 2.730   -7.327  0.86 13.86 ?  131 ILE   A O    1 
ATOM   2784 O O    B ILE   A 1 131 ? 18.221 2.580   -8.197  0.14 15.65 ?  131 ILE   A O    1 
ATOM   2785 C CB   A ILE   A 1 131 ? 17.115 4.389   -5.051  0.86 14.80 ?  131 ILE   A CB   1 
ATOM   2786 C CB   B ILE   A 1 131 ? 17.665 4.451   -5.926  0.14 16.92 ?  131 ILE   A CB   1 
ATOM   2787 C CG1  A ILE   A 1 131 ? 18.393 4.224   -4.214  0.86 16.47 ?  131 ILE   A CG1  1 
ATOM   2788 C CG1  B ILE   A 1 131 ? 19.118 4.217   -5.505  0.14 17.61 ?  131 ILE   A CG1  1 
ATOM   2789 C CG2  A ILE   A 1 131 ? 16.072 5.213   -4.307  0.86 15.58 ?  131 ILE   A CG2  1 
ATOM   2790 C CG2  B ILE   A 1 131 ? 16.915 5.201   -4.827  0.14 17.07 ?  131 ILE   A CG2  1 
ATOM   2791 C CD1  A ILE   A 1 131 ? 19.051 5.560   -3.841  0.86 18.00 ?  131 ILE   A CD1  1 
ATOM   2792 C CD1  B ILE   A 1 131 ? 19.903 5.488   -5.303  0.14 17.96 ?  131 ILE   A CD1  1 
ATOM   2793 H H    A ILE   A 1 131 ? 16.172 2.569   -3.576  0.86 16.70 ?  131 ILE   A H    1 
ATOM   2794 H H    B ILE   A 1 131 ? 16.827 2.771   -4.297  0.14 19.37 ?  131 ILE   A H    1 
ATOM   2795 H HA   A ILE   A 1 131 ? 15.800 3.223   -6.073  0.86 16.35 ?  131 ILE   A HA   1 
ATOM   2796 H HA   B ILE   A 1 131 ? 16.191 3.331   -6.789  0.14 19.58 ?  131 ILE   A HA   1 
ATOM   2797 H HB   A ILE   A 1 131 ? 17.349 4.870   -5.860  0.86 17.90 ?  131 ILE   A HB   1 
ATOM   2798 H HB   B ILE   A 1 131 ? 17.659 5.004   -6.723  0.14 20.45 ?  131 ILE   A HB   1 
ATOM   2799 H HG12 A ILE   A 1 131 ? 18.176 3.761   -3.393  0.86 19.92 ?  131 ILE   A HG12 1 
ATOM   2800 H HG12 B ILE   A 1 131 ? 19.125 3.721   -4.672  0.14 21.28 ?  131 ILE   A HG12 1 
ATOM   2801 H HG13 A ILE   A 1 131 ? 19.044 3.714   -4.721  0.86 19.92 ?  131 ILE   A HG13 1 
ATOM   2802 H HG13 B ILE   A 1 131 ? 19.583 3.719   -6.192  0.14 21.28 ?  131 ILE   A HG13 1 
ATOM   2803 H HG21 A ILE   A 1 131 ? 16.395 6.121   -4.212  0.86 18.85 ?  131 ILE   A HG21 1 
ATOM   2804 H HG21 B ILE   A 1 131 ? 17.190 6.132   -4.832  0.14 20.63 ?  131 ILE   A HG21 1 
ATOM   2805 H HG22 A ILE   A 1 131 ? 15.248 5.204   -4.815  0.86 18.85 ?  131 ILE   A HG22 1 
ATOM   2806 H HG22 B ILE   A 1 131 ? 15.962 5.138   -4.994  0.14 20.63 ?  131 ILE   A HG22 1 
ATOM   2807 H HG23 A ILE   A 1 131 ? 15.927 4.817   -3.433  0.86 18.85 ?  131 ILE   A HG23 1 
ATOM   2808 H HG23 B ILE   A 1 131 ? 17.126 4.801   -3.968  0.14 20.63 ?  131 ILE   A HG23 1 
ATOM   2809 H HD11 A ILE   A 1 131 ? 19.912 5.387   -3.427  0.86 21.74 ?  131 ILE   A HD11 1 
ATOM   2810 H HD11 B ILE   A 1 131 ? 20.830 5.259   -5.136  0.14 21.70 ?  131 ILE   A HD11 1 
ATOM   2811 H HD12 A ILE   A 1 131 ? 19.173 6.091   -4.645  0.86 21.74 ?  131 ILE   A HD12 1 
ATOM   2812 H HD12 B ILE   A 1 131 ? 19.837 6.029   -6.107  0.14 21.70 ?  131 ILE   A HD12 1 
ATOM   2813 H HD13 A ILE   A 1 131 ? 18.477 6.035   -3.218  0.86 21.74 ?  131 ILE   A HD13 1 
ATOM   2814 H HD13 B ILE   A 1 131 ? 19.538 5.970   -4.547  0.14 21.70 ?  131 ILE   A HD13 1 
ATOM   2815 N N    A PHE   A 1 132 ? 17.947 1.039   -5.832  0.86 12.55 ?  132 PHE   A N    1 
ATOM   2816 N N    B PHE   A 1 132 ? 18.173 1.011   -6.583  0.14 15.49 ?  132 PHE   A N    1 
ATOM   2817 C CA   A PHE   A 1 132 ? 18.797 0.182   -6.650  0.86 13.00 ?  132 PHE   A CA   1 
ATOM   2818 C CA   B PHE   A 1 132 ? 19.043 0.105   -7.324  0.14 15.35 ?  132 PHE   A CA   1 
ATOM   2819 C C    A PHE   A 1 132 ? 18.013 -0.575  -7.724  0.86 13.66 ?  132 PHE   A C    1 
ATOM   2820 C C    B PHE   A 1 132 ? 18.305 -0.654  -8.422  0.14 15.38 ?  132 PHE   A C    1 
ATOM   2821 O O    A PHE   A 1 132 ? 18.627 -1.216  -8.583  0.86 14.85 ?  132 PHE   A O    1 
ATOM   2822 O O    B PHE   A 1 132 ? 18.954 -1.182  -9.333  0.14 15.37 ?  132 PHE   A O    1 
ATOM   2823 C CB   A PHE   A 1 132 ? 19.603 -0.794  -5.776  0.86 12.90 ?  132 PHE   A CB   1 
ATOM   2824 C CB   B PHE   A 1 132 ? 19.746 -0.861  -6.367  0.14 15.11 ?  132 PHE   A CB   1 
ATOM   2825 C CG   A PHE   A 1 132 ? 20.836 -0.188  -5.117  0.86 12.74 ?  132 PHE   A CG   1 
ATOM   2826 C CG   B PHE   A 1 132 ? 20.845 -0.222  -5.559  0.14 15.30 ?  132 PHE   A CG   1 
ATOM   2827 C CD1  A PHE   A 1 132 ? 20.727 0.848   -4.209  0.86 13.88 ?  132 PHE   A CD1  1 
ATOM   2828 C CD1  B PHE   A 1 132 ? 20.561 0.776   -4.639  0.14 15.46 ?  132 PHE   A CD1  1 
ATOM   2829 C CD2  A PHE   A 1 132 ? 22.094 -0.712  -5.370  0.86 13.18 ?  132 PHE   A CD2  1 
ATOM   2830 C CD2  B PHE   A 1 132 ? 22.160 -0.624  -5.715  0.14 15.60 ?  132 PHE   A CD2  1 
ATOM   2831 C CE1  A PHE   A 1 132 ? 21.859 1.380   -3.597  0.86 14.28 ?  132 PHE   A CE1  1 
ATOM   2832 C CE1  B PHE   A 1 132 ? 21.569 1.364   -3.897  0.14 15.62 ?  132 PHE   A CE1  1 
ATOM   2833 C CE2  A PHE   A 1 132 ? 23.224 -0.194  -4.755  0.86 14.18 ?  132 PHE   A CE2  1 
ATOM   2834 C CE2  B PHE   A 1 132 ? 23.172 -0.041  -4.975  0.14 15.88 ?  132 PHE   A CE2  1 
ATOM   2835 C CZ   A PHE   A 1 132 ? 23.104 0.856   -3.868  0.86 14.18 ?  132 PHE   A CZ   1 
ATOM   2836 C CZ   B PHE   A 1 132 ? 22.875 0.954   -4.064  0.14 15.78 ?  132 PHE   A CZ   1 
ATOM   2837 H H    A PHE   A 1 132 ? 17.739 0.703   -5.061  0.86 15.20 ?  132 PHE   A H    1 
ATOM   2838 H H    B PHE   A 1 132 ? 17.908 0.711   -5.822  0.14 18.73 ?  132 PHE   A H    1 
ATOM   2839 H HA   A PHE   A 1 132 ? 19.437 0.746   -7.105  0.86 15.74 ?  132 PHE   A HA   1 
ATOM   2840 H HA   B PHE   A 1 132 ? 19.732 0.638   -7.747  0.14 18.57 ?  132 PHE   A HA   1 
ATOM   2841 H HB2  A PHE   A 1 132 ? 19.025 -1.126  -5.069  0.86 15.63 ?  132 PHE   A HB2  1 
ATOM   2842 H HB2  B PHE   A 1 132 ? 19.094 -1.217  -5.747  0.14 18.28 ?  132 PHE   A HB2  1 
ATOM   2843 H HB3  A PHE   A 1 132 ? 19.896 -1.538  -6.330  0.86 15.63 ?  132 PHE   A HB3  1 
ATOM   2844 H HB3  B PHE   A 1 132 ? 20.139 -1.580  -6.885  0.14 18.28 ?  132 PHE   A HB3  1 
ATOM   2845 H HD1  A PHE   A 1 132 ? 19.892 1.209   -4.021  0.86 16.80 ?  132 PHE   A HD1  1 
ATOM   2846 H HD1  B PHE   A 1 132 ? 19.683 1.059   -4.522  0.14 18.70 ?  132 PHE   A HD1  1 
ATOM   2847 H HD2  A PHE   A 1 132 ? 22.183 -1.427  -5.969  0.86 15.96 ?  132 PHE   A HD2  1 
ATOM   2848 H HD2  B PHE   A 1 132 ? 22.366 -1.294  -6.327  0.14 18.87 ?  132 PHE   A HD2  1 
ATOM   2849 H HE1  A PHE   A 1 132 ? 21.777 2.089   -2.998  0.86 17.28 ?  132 PHE   A HE1  1 
ATOM   2850 H HE1  B PHE   A 1 132 ? 21.366 2.035   -3.284  0.14 18.89 ?  132 PHE   A HE1  1 
ATOM   2851 H HE2  A PHE   A 1 132 ? 24.061 -0.552  -4.950  0.86 17.16 ?  132 PHE   A HE2  1 
ATOM   2852 H HE2  B PHE   A 1 132 ? 24.052 -0.320  -5.090  0.14 19.20 ?  132 PHE   A HE2  1 
ATOM   2853 H HZ   A PHE   A 1 132 ? 23.861 1.212   -3.462  0.86 17.16 ?  132 PHE   A HZ   1 
ATOM   2854 H HZ   B PHE   A 1 132 ? 23.555 1.348   -3.565  0.14 19.08 ?  132 PHE   A HZ   1 
ATOM   2855 N N    A GLY   A 1 133 ? 16.681 -0.538  -7.695  0.86 13.51 ?  133 GLY   A N    1 
ATOM   2856 N N    B GLY   A 1 133 ? 16.972 -0.738  -8.351  0.14 15.36 ?  133 GLY   A N    1 
ATOM   2857 C CA   A GLY   A 1 133 ? 15.886 -0.901  -8.852  0.86 14.55 ?  133 GLY   A CA   1 
ATOM   2858 C CA   B GLY   A 1 133 ? 16.138 -1.135  -9.468  0.14 15.60 ?  133 GLY   A CA   1 
ATOM   2859 C C    A GLY   A 1 133 ? 15.549 -2.367  -9.045  0.86 14.94 ?  133 GLY   A C    1 
ATOM   2860 C C    B GLY   A 1 133 ? 15.522 -2.518  -9.344  0.14 15.88 ?  133 GLY   A C    1 
ATOM   2861 O O    A GLY   A 1 133 ? 14.904 -2.692  -10.051 0.86 16.66 ?  133 GLY   A O    1 
ATOM   2862 O O    B GLY   A 1 133 ? 14.428 -2.746  -9.877  0.14 15.89 ?  133 GLY   A O    1 
ATOM   2863 H H    A GLY   A 1 133 ? 16.212 -0.300  -7.012  0.86 16.36 ?  133 GLY   A H    1 
ATOM   2864 H H    B GLY   A 1 133 ? 16.525 -0.570  -7.635  0.14 18.59 ?  133 GLY   A H    1 
ATOM   2865 H HA2  A GLY   A 1 133 ? 15.044 -0.426  -8.813  0.86 17.61 ?  133 GLY   A HA2  1 
ATOM   2866 H HA2  B GLY   A 1 133 ? 15.418 -0.493  -9.566  0.14 18.87 ?  133 GLY   A HA2  1 
ATOM   2867 H HA3  A GLY   A 1 133 ? 16.353 -0.606  -9.652  0.86 17.61 ?  133 GLY   A HA3  1 
ATOM   2868 H HA3  B GLY   A 1 133 ? 16.669 -1.114  -10.279 0.14 18.87 ?  133 GLY   A HA3  1 
ATOM   2869 N N    A ALA   A 1 134 ? 15.963 -3.262  -8.147  0.86 14.09 ?  134 ALA   A N    1 
ATOM   2870 N N    B ALA   A 1 134 ? 16.192 -3.441  -8.659  0.14 15.98 ?  134 ALA   A N    1 
ATOM   2871 C CA   A ALA   A 1 134 ? 15.621 -4.669  -8.299  0.86 14.86 ?  134 ALA   A CA   1 
ATOM   2872 C CA   B ALA   A 1 134 ? 15.766 -4.832  -8.677  0.14 16.23 ?  134 ALA   A CA   1 
ATOM   2873 C C    A ALA   A 1 134 ? 14.260 -4.964  -7.668  0.86 15.61 ?  134 ALA   A C    1 
ATOM   2874 C C    B ALA   A 1 134 ? 14.427 -5.009  -7.970  0.14 16.69 ?  134 ALA   A C    1 
ATOM   2875 O O    A ALA   A 1 134 ? 13.726 -4.180  -6.878  0.86 16.64 ?  134 ALA   A O    1 
ATOM   2876 O O    B ALA   A 1 134 ? 14.010 -4.191  -7.145  0.14 16.98 ?  134 ALA   A O    1 
ATOM   2877 C CB   A ALA   A 1 134 ? 16.693 -5.566  -7.678  0.86 15.91 ?  134 ALA   A CB   1 
ATOM   2878 C CB   B ALA   A 1 134 ? 16.817 -5.725  -8.021  0.14 16.25 ?  134 ALA   A CB   1 
ATOM   2879 H H    A ALA   A 1 134 ? 16.451 -3.077  -7.453  0.86 17.06 ?  134 ALA   A H    1 
ATOM   2880 H H    B ALA   A 1 134 ? 16.883 -3.285  -8.174  0.14 19.32 ?  134 ALA   A H    1 
ATOM   2881 H HA   A ALA   A 1 134 ? 15.574 -4.875  -9.246  0.86 17.98 ?  134 ALA   A HA   1 
ATOM   2882 H HA   B ALA   A 1 134 ? 15.654 -5.117  -9.593  0.14 19.63 ?  134 ALA   A HA   1 
ATOM   2883 H HB1  A ALA   A 1 134 ? 16.443 -6.492  -7.815  0.86 19.24 ?  134 ALA   A HB1  1 
ATOM   2884 H HB1  B ALA   A 1 134 ? 16.516 -6.647  -8.063  0.14 19.64 ?  134 ALA   A HB1  1 
ATOM   2885 H HB2  A ALA   A 1 134 ? 17.547 -5.387  -8.108  0.86 19.24 ?  134 ALA   A HB2  1 
ATOM   2886 H HB2  B ALA   A 1 134 ? 17.651 -5.626  -8.503  0.14 19.64 ?  134 ALA   A HB2  1 
ATOM   2887 H HB3  A ALA   A 1 134 ? 16.756 -5.374  -6.730  0.86 19.24 ?  134 ALA   A HB3  1 
ATOM   2888 H HB3  B ALA   A 1 134 ? 16.931 -5.455  -7.098  0.14 19.64 ?  134 ALA   A HB3  1 
ATOM   2889 N N    A ASP   A 1 135 ? 13.706 -6.115  -8.035  0.86 16.44 ?  135 ASP   A N    1 
ATOM   2890 N N    B ASP   A 1 135 ? 13.752 -6.107  -8.306  0.14 17.07 ?  135 ASP   A N    1 
ATOM   2891 C CA   A ASP   A 1 135 ? 12.449 -6.594  -7.462  0.86 17.66 ?  135 ASP   A CA   1 
ATOM   2892 C CA   B ASP   A 1 135 ? 12.465 -6.418  -7.700  0.14 17.52 ?  135 ASP   A CA   1 
ATOM   2893 C C    A ASP   A 1 135 ? 12.698 -7.054  -6.030  0.86 17.01 ?  135 ASP   A C    1 
ATOM   2894 C C    B ASP   A 1 135 ? 12.675 -6.949  -6.286  0.14 17.23 ?  135 ASP   A C    1 
ATOM   2895 O O    A ASP   A 1 135 ? 13.466 -8.004  -5.824  0.86 16.47 ?  135 ASP   A O    1 
ATOM   2896 O O    B ASP   A 1 135 ? 13.442 -7.899  -6.095  0.14 17.04 ?  135 ASP   A O    1 
ATOM   2897 C CB   A ASP   A 1 135 ? 11.956 -7.764  -8.310  0.86 20.50 ?  135 ASP   A CB   1 
ATOM   2898 C CB   B ASP   A 1 135 ? 11.729 -7.458  -8.536  0.14 18.47 ?  135 ASP   A CB   1 
ATOM   2899 C CG   A ASP   A 1 135 ? 10.656 -8.379  -7.794  0.86 23.54 ?  135 ASP   A CG   1 
ATOM   2900 C CG   B ASP   A 1 135 ? 10.567 -8.078  -7.797  0.14 19.29 ?  135 ASP   A CG   1 
ATOM   2901 O OD1  A ASP   A 1 135 ? 10.123 -7.910  -6.766  0.86 23.41 ?  135 ASP   A OD1  1 
ATOM   2902 O OD1  B ASP   A 1 135 ? 9.620  -7.342  -7.448  0.14 19.73 ?  135 ASP   A OD1  1 
ATOM   2903 O OD2  A ASP   A 1 135 ? 10.162 -9.332  -8.439  0.86 26.69 -1 135 ASP   A OD2  1 
ATOM   2904 O OD2  B ASP   A 1 135 ? 10.609 -9.303  -7.563  0.14 19.51 -1 135 ASP   A OD2  1 
ATOM   2905 H H    A ASP   A 1 135 ? 14.045 -6.646  -8.620  0.86 19.87 ?  135 ASP   A H    1 
ATOM   2906 H H    B ASP   A 1 135 ? 14.015 -6.690  -8.883  0.14 20.63 ?  135 ASP   A H    1 
ATOM   2907 H HA   A ASP   A 1 135 ? 11.786 -5.886  -7.482  0.86 21.34 ?  135 ASP   A HA   1 
ATOM   2908 H HA   B ASP   A 1 135 ? 11.926 -5.615  -7.671  0.14 21.17 ?  135 ASP   A HA   1 
ATOM   2909 H HB2  A ASP   A 1 135 ? 11.796 -7.449  -9.212  0.86 24.75 ?  135 ASP   A HB2  1 
ATOM   2910 H HB2  B ASP   A 1 135 ? 11.392 -7.037  -9.343  0.14 22.31 ?  135 ASP   A HB2  1 
ATOM   2911 H HB3  A ASP   A 1 135 ? 12.640 -8.452  -8.315  0.86 24.75 ?  135 ASP   A HB3  1 
ATOM   2912 H HB3  B ASP   A 1 135 ? 12.338 -8.176  -8.765  0.14 22.31 ?  135 ASP   A HB3  1 
ATOM   2913 N N    A PRO   A 1 136 ? 12.097 -6.415  -5.019  0.86 17.38 ?  136 PRO   A N    1 
ATOM   2914 N N    B PRO   A 1 136 ? 12.017 -6.370  -5.277  0.14 17.26 ?  136 PRO   A N    1 
ATOM   2915 C CA   A PRO   A 1 136 ? 12.362 -6.832  -3.629  0.86 17.34 ?  136 PRO   A CA   1 
ATOM   2916 C CA   B PRO   A 1 136 ? 12.243 -6.831  -3.896  0.14 17.16 ?  136 PRO   A CA   1 
ATOM   2917 C C    A PRO   A 1 136 ? 11.918 -8.251  -3.311  0.86 15.79 ?  136 PRO   A C    1 
ATOM   2918 C C    B PRO   A 1 136 ? 11.870 -8.285  -3.663  0.14 16.84 ?  136 PRO   A C    1 
ATOM   2919 O O    A PRO   A 1 136 ? 12.512 -8.886  -2.433  0.86 15.13 ?  136 PRO   A O    1 
ATOM   2920 O O    B PRO   A 1 136 ? 12.494 -8.945  -2.823  0.14 16.73 ?  136 PRO   A O    1 
ATOM   2921 C CB   A PRO   A 1 136 ? 11.606 -5.785  -2.797  0.86 18.89 ?  136 PRO   A CB   1 
ATOM   2922 C CB   B PRO   A 1 136 ? 11.388 -5.865  -3.059  0.14 17.40 ?  136 PRO   A CB   1 
ATOM   2923 C CG   A PRO   A 1 136 ? 10.566 -5.246  -3.724  0.86 20.44 ?  136 PRO   A CG   1 
ATOM   2924 C CG   B PRO   A 1 136 ? 10.367 -5.332  -4.017  0.14 17.70 ?  136 PRO   A CG   1 
ATOM   2925 C CD   A PRO   A 1 136 ? 11.186 -5.260  -5.084  0.86 18.89 ?  136 PRO   A CD   1 
ATOM   2926 C CD   B PRO   A 1 136 ? 11.050 -5.263  -5.341  0.14 17.56 ?  136 PRO   A CD   1 
ATOM   2927 H HA   A PRO   A 1 136 ? 13.314 -6.750  -3.432  0.86 20.95 ?  136 PRO   A HA   1 
ATOM   2928 H HA   B PRO   A 1 136 ? 13.173 -6.711  -3.653  0.14 20.74 ?  136 PRO   A HA   1 
ATOM   2929 H HB2  A PRO   A 1 136 ? 11.197 -6.209  -2.028  0.86 22.81 ?  136 PRO   A HB2  1 
ATOM   2930 H HB2  B PRO   A 1 136 ? 10.960 -6.343  -2.332  0.14 21.03 ?  136 PRO   A HB2  1 
ATOM   2931 H HB3  A PRO   A 1 136 ? 12.216 -5.080  -2.517  0.86 22.81 ?  136 PRO   A HB3  1 
ATOM   2932 H HB3  B PRO   A 1 136 ? 11.945 -5.146  -2.717  0.14 21.03 ?  136 PRO   A HB3  1 
ATOM   2933 H HG2  A PRO   A 1 136 ? 9.785  -5.820  -3.702  0.86 24.67 ?  136 PRO   A HG2  1 
ATOM   2934 H HG2  B PRO   A 1 136 ? 9.611  -5.937  -4.056  0.14 21.39 ?  136 PRO   A HG2  1 
ATOM   2935 H HG3  A PRO   A 1 136 ? 10.335 -4.342  -3.466  0.86 24.67 ?  136 PRO   A HG3  1 
ATOM   2936 H HG3  B PRO   A 1 136 ? 10.085 -4.448  -3.737  0.14 21.39 ?  136 PRO   A HG3  1 
ATOM   2937 H HD2  A PRO   A 1 136 ? 10.506 -5.411  -5.763  0.86 22.81 ?  136 PRO   A HD2  1 
ATOM   2938 H HD2  B PRO   A 1 136 ? 10.413 -5.409  -6.059  0.14 21.22 ?  136 PRO   A HD2  1 
ATOM   2939 H HD3  A PRO   A 1 136 ? 11.675 -4.439  -5.248  0.86 22.81 ?  136 PRO   A HD3  1 
ATOM   2940 H HD3  B PRO   A 1 136 ? 11.517 -4.420  -5.444  0.14 21.22 ?  136 PRO   A HD3  1 
ATOM   2941 N N    A ILE   A 1 137 ? 10.892 -8.769  -3.989  0.86 16.38 ?  137 ILE   A N    1 
ATOM   2942 N N    B ILE   A 1 137 ? 10.875 -8.808  -4.382  0.14 16.69 ?  137 ILE   A N    1 
ATOM   2943 C CA   A ILE   A 1 137 ? 10.506 -10.165 -3.785  0.86 16.56 ?  137 ILE   A CA   1 
ATOM   2944 C CA   B ILE   A 1 137 ? 10.500 -10.211 -4.223  0.14 16.64 ?  137 ILE   A CA   1 
ATOM   2945 C C    A ILE   A 1 137 ? 11.644 -11.090 -4.201  0.86 15.98 ?  137 ILE   A C    1 
ATOM   2946 C C    B ILE   A 1 137 ? 11.670 -11.115 -4.583  0.14 16.40 ?  137 ILE   A C    1 
ATOM   2947 O O    A ILE   A 1 137 ? 11.958 -12.073 -3.516  0.86 16.23 ?  137 ILE   A O    1 
ATOM   2948 O O    B ILE   A 1 137 ? 11.886 -12.159 -3.956  0.14 16.46 ?  137 ILE   A O    1 
ATOM   2949 C CB   A ILE   A 1 137 ? 9.198  -10.477 -4.542  0.86 18.30 ?  137 ILE   A CB   1 
ATOM   2950 C CB   B ILE   A 1 137 ? 9.250  -10.524 -5.067  0.14 16.95 ?  137 ILE   A CB   1 
ATOM   2951 C CG1  A ILE   A 1 137 ? 8.034  -9.621  -4.018  0.86 20.65 ?  137 ILE   A CG1  1 
ATOM   2952 C CG1  B ILE   A 1 137 ? 8.078  -9.651  -4.612  0.14 17.22 ?  137 ILE   A CG1  1 
ATOM   2953 C CG2  A ILE   A 1 137 ? 8.865  -11.962 -4.435  0.86 19.00 ?  137 ILE   A CG2  1 
ATOM   2954 C CG2  B ILE   A 1 137 ? 8.893  -12.002 -4.973  0.14 16.88 ?  137 ILE   A CG2  1 
ATOM   2955 C CD1  A ILE   A 1 137 ? 6.741  -9.797  -4.793  0.86 22.20 ?  137 ILE   A CD1  1 
ATOM   2956 C CD1  B ILE   A 1 137 ? 7.050  -9.407  -5.688  0.14 17.36 ?  137 ILE   A CD1  1 
ATOM   2957 H H    A ILE   A 1 137 ? 10.419 -8.336  -4.560  0.86 19.81 ?  137 ILE   A H    1 
ATOM   2958 H H    B ILE   A 1 137 ? 10.408 -8.377  -4.959  0.14 20.18 ?  137 ILE   A H    1 
ATOM   2959 H HA   A ILE   A 1 137 ? 10.346 -10.302 -2.842  0.86 20.02 ?  137 ILE   A HA   1 
ATOM   2960 H HA   B ILE   A 1 137 ? 10.277 -10.376 -3.294  0.14 20.11 ?  137 ILE   A HA   1 
ATOM   2961 H HB   A ILE   A 1 137 ? 9.333  -10.262 -5.476  0.86 22.11 ?  137 ILE   A HB   1 
ATOM   2962 H HB   B ILE   A 1 137 ? 9.447  -10.320 -5.992  0.14 20.48 ?  137 ILE   A HB   1 
ATOM   2963 H HG12 A ILE   A 1 137 ? 7.869  -9.856  -3.092  0.86 24.93 ?  137 ILE   A HG12 1 
ATOM   2964 H HG12 B ILE   A 1 137 ? 7.635  -10.093 -3.871  0.14 20.81 ?  137 ILE   A HG12 1 
ATOM   2965 H HG13 A ILE   A 1 137 ? 8.291  -8.683  -4.073  0.86 24.93 ?  137 ILE   A HG13 1 
ATOM   2966 H HG13 B ILE   A 1 137 ? 8.416  -8.789  -4.323  0.14 20.81 ?  137 ILE   A HG13 1 
ATOM   2967 H HG21 A ILE   A 1 137 ? 7.973  -12.120 -4.775  0.86 22.94 ?  137 ILE   A HG21 1 
ATOM   2968 H HG21 B ILE   A 1 137 ? 8.003  -12.133 -5.337  0.14 20.41 ?  137 ILE   A HG21 1 
ATOM   2969 H HG22 A ILE   A 1 137 ? 9.507  -12.464 -4.956  0.86 22.94 ?  137 ILE   A HG22 1 
ATOM   2970 H HG22 B ILE   A 1 137 ? 9.537  -12.519 -5.483  0.14 20.41 ?  137 ILE   A HG22 1 
ATOM   2971 H HG23 A ILE   A 1 137 ? 8.913  -12.223 -3.504  0.86 22.94 ?  137 ILE   A HG23 1 
ATOM   2972 H HG23 B ILE   A 1 137 ? 8.911  -12.273 -4.042  0.14 20.41 ?  137 ILE   A HG23 1 
ATOM   2973 H HD11 A ILE   A 1 137 ? 6.055  -10.119 -4.190  0.86 26.79 ?  137 ILE   A HD11 1 
ATOM   2974 H HD11 B ILE   A 1 137 ? 6.660  -8.529  -5.555  0.14 20.98 ?  137 ILE   A HD11 1 
ATOM   2975 H HD12 A ILE   A 1 137 ? 6.493  -8.941  -5.164  0.86 26.79 ?  137 ILE   A HD12 1 
ATOM   2976 H HD12 B ILE   A 1 137 ? 7.482  -9.445  -6.555  0.14 20.98 ?  137 ILE   A HD12 1 
ATOM   2977 H HD13 A ILE   A 1 137 ? 6.883  -10.434 -5.511  0.86 26.79 ?  137 ILE   A HD13 1 
ATOM   2978 H HD13 B ILE   A 1 137 ? 6.365  -10.090 -5.629  0.14 20.98 ?  137 ILE   A HD13 1 
ATOM   2979 N N    A HIS   A 1 138 ? 12.279 -10.784 -5.333  0.86 16.34 ?  138 HIS   A N    1 
ATOM   2980 N N    B HIS   A 1 138 ? 12.441 -10.733 -5.602  0.14 16.23 ?  138 HIS   A N    1 
ATOM   2981 C CA   A HIS   A 1 138 ? 13.438 -11.556 -5.769  0.86 16.21 ?  138 HIS   A CA   1 
ATOM   2982 C CA   B HIS   A 1 138 ? 13.614 -11.516 -5.967  0.14 15.84 ?  138 HIS   A CA   1 
ATOM   2983 C C    A HIS   A 1 138 ? 14.597 -11.422 -4.787  0.86 15.09 ?  138 HIS   A C    1 
ATOM   2984 C C    B HIS   A 1 138 ? 14.714 -11.389 -4.920  0.14 15.03 ?  138 HIS   A C    1 
ATOM   2985 O O    A HIS   A 1 138 ? 15.259 -12.413 -4.453  0.86 15.48 ?  138 HIS   A O    1 
ATOM   2986 O O    B HIS   A 1 138 ? 15.427 -12.360 -4.642  0.14 14.90 ?  138 HIS   A O    1 
ATOM   2987 C CB   A HIS   A 1 138 ? 13.845 -11.115 -7.173  0.86 16.90 ?  138 HIS   A CB   1 
ATOM   2988 C CB   B HIS   A 1 138 ? 14.123 -11.085 -7.342  0.14 16.49 ?  138 HIS   A CB   1 
ATOM   2989 C CG   A HIS   A 1 138 ? 15.119 -11.737 -7.646  0.86 17.72 ?  138 HIS   A CG   1 
ATOM   2990 C CG   B HIS   A 1 138 ? 15.339 -11.832 -7.793  0.14 17.08 ?  138 HIS   A CG   1 
ATOM   2991 N ND1  A HIS   A 1 138 ? 15.247 -13.091 -7.880  0.86 18.93 ?  138 HIS   A ND1  1 
ATOM   2992 N ND1  B HIS   A 1 138 ? 15.306 -13.164 -8.147  0.14 17.52 ?  138 HIS   A ND1  1 
ATOM   2993 C CD2  A HIS   A 1 138 ? 16.329 -11.192 -7.913  0.86 17.96 ?  138 HIS   A CD2  1 
ATOM   2994 C CD2  B HIS   A 1 138 ? 16.624 -11.434 -7.943  0.14 17.36 ?  138 HIS   A CD2  1 
ATOM   2995 C CE1  A HIS   A 1 138 ? 16.479 -13.350 -8.279  0.86 19.36 ?  138 HIS   A CE1  1 
ATOM   2996 C CE1  B HIS   A 1 138 ? 16.519 -13.553 -8.498  0.14 17.78 ?  138 HIS   A CE1  1 
ATOM   2997 N NE2  A HIS   A 1 138 ? 17.156 -12.215 -8.308  0.86 18.76 ?  138 HIS   A NE2  1 
ATOM   2998 N NE2  B HIS   A 1 138 ? 17.337 -12.522 -8.383  0.14 17.61 ?  138 HIS   A NE2  1 
ATOM   2999 H H    A HIS   A 1 138 ? 12.066 -10.133 -5.860  0.86 19.75 ?  138 HIS   A H    1 
ATOM   3000 H H    B HIS   A 1 138 ? 12.302 -10.040 -6.093  0.14 19.63 ?  138 HIS   A H    1 
ATOM   3001 H HA   A HIS   A 1 138 ? 13.190 -12.488 -5.813  0.86 19.61 ?  138 HIS   A HA   1 
ATOM   3002 H HA   B HIS   A 1 138 ? 13.363 -12.449 -6.021  0.14 19.15 ?  138 HIS   A HA   1 
ATOM   3003 H HB2  A HIS   A 1 138 ? 13.141 -11.365 -7.798  0.86 20.43 ?  138 HIS   A HB2  1 
ATOM   3004 H HB2  B HIS   A 1 138 ? 13.422 -11.238 -7.995  0.14 19.93 ?  138 HIS   A HB2  1 
ATOM   3005 H HB3  A HIS   A 1 138 ? 13.962 -10.152 -7.184  0.86 20.43 ?  138 HIS   A HB3  1 
ATOM   3006 H HB3  B HIS   A 1 138 ? 14.348 -10.143 -7.313  0.14 19.93 ?  138 HIS   A HB3  1 
ATOM   3007 H HD1  A HIS   A 1 138 ? 14.619 -13.674 -7.786  0.86 22.86 ?  138 HIS   A HD1  1 
ATOM   3008 H HD2  A HIS   A 1 138 ? 16.555 -10.295 -7.846  0.86 21.70 ?  138 HIS   A HD2  1 
ATOM   3009 H HD2  B HIS   A 1 138 ? 16.960 -10.582 -7.779  0.14 20.98 ?  138 HIS   A HD2  1 
ATOM   3010 H HE1  A HIS   A 1 138 ? 16.812 -14.191 -8.500  0.86 23.38 ?  138 HIS   A HE1  1 
ATOM   3011 H HE1  B HIS   A 1 138 ? 16.755 -14.407 -8.778  0.14 21.48 ?  138 HIS   A HE1  1 
ATOM   3012 H HE2  B HIS   A 1 138 ? 18.178 -12.531 -8.556  0.14 21.28 ?  138 HIS   A HE2  1 
ATOM   3013 N N    . SER   A 1 139 ? 14.867 -10.204 -4.324  1.00 14.49 ?  139 SER   A N    1 
ATOM   3014 C CA   . SER   A 1 139 ? 15.942 -10.014 -3.358  1.00 14.27 ?  139 SER   A CA   1 
ATOM   3015 C C    . SER   A 1 139 ? 15.727 -10.857 -2.106  1.00 13.99 ?  139 SER   A C    1 
ATOM   3016 O O    . SER   A 1 139 ? 16.675 -11.454 -1.579  1.00 14.11 ?  139 SER   A O    1 
ATOM   3017 C CB   . SER   A 1 139 ? 16.075 -8.533  -3.006  1.00 14.30 ?  139 SER   A CB   1 
ATOM   3018 O OG   . SER   A 1 139 ? 17.162 -8.362  -2.111  1.00 14.60 ?  139 SER   A OG   1 
ATOM   3019 H H    A SER   A 1 139 ? 14.451 -9.485  -4.542  0.86 17.53 ?  139 SER   A H    1 
ATOM   3020 H H    B SER   A 1 139 ? 14.379 -9.511  -4.461  0.14 17.53 ?  139 SER   A H    1 
ATOM   3021 H HA   . SER   A 1 139 ? 16.782 -10.291 -3.756  1.00 17.27 ?  139 SER   A HA   1 
ATOM   3022 H HB2  . SER   A 1 139 ? 16.245 -8.019  -3.814  1.00 17.31 ?  139 SER   A HB2  1 
ATOM   3023 H HB3  . SER   A 1 139 ? 15.261 -8.224  -2.578  1.00 17.31 ?  139 SER   A HB3  1 
ATOM   3024 H HG   . SER   A 1 139 ? 17.252 -7.551  -1.911  1.00 17.67 ?  139 SER   A HG   1 
ATOM   3025 N N    . LEU   A 1 140 ? 14.486 -10.918 -1.617  1.00 14.10 ?  140 LEU   A N    1 
ATOM   3026 C CA   . LEU   A 1 140 ? 14.201 -11.739 -0.442  1.00 13.89 ?  140 LEU   A CA   1 
ATOM   3027 C C    . LEU   A 1 140 ? 14.462 -13.218 -0.724  1.00 13.91 ?  140 LEU   A C    1 
ATOM   3028 O O    . LEU   A 1 140 ? 15.023 -13.936 0.117   1.00 14.67 ?  140 LEU   A O    1 
ATOM   3029 C CB   . LEU   A 1 140 ? 12.761 -11.512 0.020   1.00 14.69 ?  140 LEU   A CB   1 
ATOM   3030 C CG   . LEU   A 1 140 ? 12.305 -12.357 1.212   1.00 15.05 ?  140 LEU   A CG   1 
ATOM   3031 C CD1  . LEU   A 1 140 ? 13.219 -12.186 2.422   1.00 15.71 ?  140 LEU   A CD1  1 
ATOM   3032 C CD2  . LEU   A 1 140 ? 10.848 -12.040 1.583   1.00 16.14 ?  140 LEU   A CD2  1 
ATOM   3033 H H    . LEU   A 1 140 ? 13.805 -10.498 -1.934  1.00 17.06 ?  140 LEU   A H    1 
ATOM   3034 H HA   . LEU   A 1 140 ? 14.789 -11.468 0.279   1.00 16.82 ?  140 LEU   A HA   1 
ATOM   3035 H HB2  . LEU   A 1 140 ? 12.666 -10.585 0.272   1.00 17.78 ?  140 LEU   A HB2  1 
ATOM   3036 H HB3  . LEU   A 1 140 ? 12.171 -11.715 -0.720  1.00 17.78 ?  140 LEU   A HB3  1 
ATOM   3037 H HG   . LEU   A 1 140 ? 12.330 -13.293 0.955   1.00 18.20 ?  140 LEU   A HG   1 
ATOM   3038 H HD11 . LEU   A 1 140 ? 12.835 -12.667 3.176   1.00 18.99 ?  140 LEU   A HD11 1 
ATOM   3039 H HD12 . LEU   A 1 140 ? 14.091 -12.556 2.209   1.00 18.99 ?  140 LEU   A HD12 1 
ATOM   3040 H HD13 . LEU   A 1 140 ? 13.295 -11.247 2.632   1.00 18.99 ?  140 LEU   A HD13 1 
ATOM   3041 H HD21 . LEU   A 1 140 ? 10.586 -12.593 2.339   1.00 19.51 ?  140 LEU   A HD21 1 
ATOM   3042 H HD22 . LEU   A 1 140 ? 10.777 -11.104 1.820   1.00 19.51 ?  140 LEU   A HD22 1 
ATOM   3043 H HD23 . LEU   A 1 140 ? 10.276 -12.235 0.823   1.00 19.51 ?  140 LEU   A HD23 1 
ATOM   3044 N N    . ARG   A 1 141 ? 14.074 -13.689 -1.911  1.00 14.59 ?  141 ARG   A N    1 
ATOM   3045 C CA   . ARG   A 1 141 ? 14.319 -15.081 -2.279  1.00 15.51 ?  141 ARG   A CA   1 
ATOM   3046 C C    . ARG   A 1 141 ? 15.817 -15.382 -2.293  1.00 14.58 ?  141 ARG   A C    1 
ATOM   3047 O O    . ARG   A 1 141 ? 16.267 -16.395 -1.743  1.00 14.70 ?  141 ARG   A O    1 
ATOM   3048 C CB   . ARG   A 1 141 ? 13.701 -15.331 -3.656  1.00 17.56 ?  141 ARG   A CB   1 
ATOM   3049 C CG   . ARG   A 1 141 ? 13.715 -16.764 -4.129  1.00 20.86 ?  141 ARG   A CG   1 
ATOM   3050 C CD   . ARG   A 1 141 ? 12.683 -17.557 -3.402  1.00 23.51 ?  141 ARG   A CD   1 
ATOM   3051 N NE   . ARG   A 1 141 ? 13.289 -18.343 -2.342  1.00 23.79 ?  141 ARG   A NE   1 
ATOM   3052 C CZ   . ARG   A 1 141 ? 12.602 -18.898 -1.354  1.00 24.18 ?  141 ARG   A CZ   1 
ATOM   3053 N NH1  . ARG   A 1 141 ? 11.312 -18.656 -1.189  1.00 23.94 ?  141 ARG   A NH1  1 
ATOM   3054 N NH2  . ARG   A 1 141 ? 13.225 -19.710 -0.506  1.00 24.87 ?  141 ARG   A NH2  1 
ATOM   3055 H H    . ARG   A 1 141 ? 13.671 -13.227 -2.516  1.00 17.65 ?  141 ARG   A H    1 
ATOM   3056 H HA   . ARG   A 1 141 ? 13.894 -15.667 -1.638  1.00 18.76 ?  141 ARG   A HA   1 
ATOM   3057 H HB2  . ARG   A 1 141 ? 12.778 -15.031 -3.640  1.00 21.23 ?  141 ARG   A HB2  1 
ATOM   3058 H HB3  . ARG   A 1 141 ? 14.193 -14.805 -4.309  1.00 21.23 ?  141 ARG   A HB3  1 
ATOM   3059 H HG2  . ARG   A 1 141 ? 13.520 -16.795 -5.079  1.00 25.18 ?  141 ARG   A HG2  1 
ATOM   3060 H HG3  . ARG   A 1 141 ? 14.589 -17.156 -3.954  1.00 25.18 ?  141 ARG   A HG3  1 
ATOM   3061 H HD2  . ARG   A 1 141 ? 12.036 -16.956 -2.998  1.00 28.35 ?  141 ARG   A HD2  1 
ATOM   3062 H HD3  . ARG   A 1 141 ? 12.241 -18.157 -4.023  1.00 28.35 ?  141 ARG   A HD3  1 
ATOM   3063 H HE   . ARG   A 1 141 ? 14.112 -18.576 -2.435  1.00 28.69 ?  141 ARG   A HE   1 
ATOM   3064 H HH11 . ARG   A 1 141 ? 10.892 -18.142 -1.736  1.00 28.87 ?  141 ARG   A HH11 1 
ATOM   3065 H HH12 . ARG   A 1 141 ? 10.888 -19.024 -0.538  1.00 28.87 ?  141 ARG   A HH12 1 
ATOM   3066 H HH21 . ARG   A 1 141 ? 14.066 -19.870 -0.602  1.00 29.99 ?  141 ARG   A HH21 1 
ATOM   3067 H HH22 . ARG   A 1 141 ? 12.795 -20.066 0.148   1.00 29.99 ?  141 ARG   A HH22 1 
ATOM   3068 N N    . VAL   A 1 142 ? 16.607 -14.510 -2.923  1.00 13.96 ?  142 VAL   A N    1 
ATOM   3069 C CA   . VAL   A 1 142 ? 18.053 -14.716 -2.953  1.00 14.11 ?  142 VAL   A CA   1 
ATOM   3070 C C    . VAL   A 1 142 ? 18.622 -14.700 -1.541  1.00 13.06 ?  142 VAL   A C    1 
ATOM   3071 O O    . VAL   A 1 142 ? 19.481 -15.519 -1.195  1.00 13.86 ?  142 VAL   A O    1 
ATOM   3072 C CB   . VAL   A 1 142 ? 18.746 -13.689 -3.868  1.00 14.12 ?  142 VAL   A CB   1 
ATOM   3073 C CG1  . VAL   A 1 142 ? 20.260 -13.894 -3.826  1.00 14.31 ?  142 VAL   A CG1  1 
ATOM   3074 C CG2  . VAL   A 1 142 ? 18.255 -13.820 -5.295  1.00 15.94 ?  142 VAL   A CG2  1 
ATOM   3075 H H    . VAL   A 1 142 ? 16.336 -13.797 -3.335  1.00 16.90 ?  142 VAL   A H    1 
ATOM   3076 H HA   . VAL   A 1 142 ? 18.229 -15.585 -3.326  1.00 17.07 ?  142 VAL   A HA   1 
ATOM   3077 H HB   . VAL   A 1 142 ? 18.559 -12.784 -3.558  1.00 17.09 ?  142 VAL   A HB   1 
ATOM   3078 H HG11 . VAL   A 1 142 ? 20.669 -13.398 -4.555  1.00 17.32 ?  142 VAL   A HG11 1 
ATOM   3079 H HG12 . VAL   A 1 142 ? 20.607 -13.564 -2.978  1.00 17.32 ?  142 VAL   A HG12 1 
ATOM   3080 H HG13 . VAL   A 1 142 ? 20.455 -14.836 -3.918  1.00 17.32 ?  142 VAL   A HG13 1 
ATOM   3081 H HG21 . VAL   A 1 142 ? 18.676 -13.135 -5.839  1.00 19.27 ?  142 VAL   A HG21 1 
ATOM   3082 H HG22 . VAL   A 1 142 ? 18.498 -14.699 -5.626  1.00 19.27 ?  142 VAL   A HG22 1 
ATOM   3083 H HG23 . VAL   A 1 142 ? 17.296 -13.713 -5.307  1.00 19.27 ?  142 VAL   A HG23 1 
ATOM   3084 N N    . CYS   A 1 143 ? 18.154 -13.775 -0.702  1.00 13.16 ?  143 CYS   A N    1 
ATOM   3085 C CA   . CYS   A 1 143 ? 18.618 -13.731 0.681   1.00 13.74 ?  143 CYS   A CA   1 
ATOM   3086 C C    . CYS   A 1 143 ? 18.395 -15.074 1.368   1.00 12.99 ?  143 CYS   A C    1 
ATOM   3087 O O    . CYS   A 1 143 ? 19.313 -15.653 1.954   1.00 13.26 ?  143 CYS   A O    1 
ATOM   3088 C CB   . CYS   A 1 143 ? 17.877 -12.629 1.434   1.00 13.90 ?  143 CYS   A CB   1 
ATOM   3089 S SG   . CYS   A 1 143 ? 18.367 -12.446 3.161   1.00 14.15 ?  143 CYS   A SG   1 
ATOM   3090 H H    . CYS   A 1 143 ? 17.576 -13.171 -0.907  1.00 15.94 ?  143 CYS   A H    1 
ATOM   3091 H HA   . CYS   A 1 143 ? 19.566 -13.534 0.697   1.00 16.64 ?  143 CYS   A HA   1 
ATOM   3092 H HB2  . CYS   A 1 143 ? 18.039 -11.783 0.988   1.00 16.83 ?  143 CYS   A HB2  1 
ATOM   3093 H HB3  . CYS   A 1 143 ? 16.931 -12.826 1.420   1.00 16.83 ?  143 CYS   A HB3  1 
ATOM   3094 H HG   . CYS   A 1 143 ? 17.762 -11.526 3.636   1.00 17.13 ?  143 CYS   A HG   1 
ATOM   3095 N N    . VAL   A 1 144 ? 17.163 -15.578 1.308   1.00 13.88 ?  144 VAL   A N    1 
ATOM   3096 C CA   . VAL   A 1 144 ? 16.822 -16.813 2.007   1.00 15.47 ?  144 VAL   A CA   1 
ATOM   3097 C C    . VAL   A 1 144 ? 17.635 -17.988 1.477   1.00 14.94 ?  144 VAL   A C    1 
ATOM   3098 O O    . VAL   A 1 144 ? 18.010 -18.893 2.234   1.00 15.71 ?  144 VAL   A O    1 
ATOM   3099 C CB   . VAL   A 1 144 ? 15.302 -17.054 1.906   1.00 18.22 ?  144 VAL   A CB   1 
ATOM   3100 C CG1  . VAL   A 1 144 ? 14.955 -18.489 2.238   1.00 20.19 ?  144 VAL   A CG1  1 
ATOM   3101 C CG2  . VAL   A 1 144 ? 14.561 -16.057 2.802   1.00 18.31 ?  144 VAL   A CG2  1 
ATOM   3102 H H    . VAL   A 1 144 ? 16.508 -15.216 0.873   1.00 16.81 ?  144 VAL   A H    1 
ATOM   3103 H HA   . VAL   A 1 144 ? 17.034 -16.700 2.944   1.00 18.72 ?  144 VAL   A HA   1 
ATOM   3104 H HB   . VAL   A 1 144 ? 15.018 -16.882 0.992   1.00 22.01 ?  144 VAL   A HB   1 
ATOM   3105 H HG11 . VAL   A 1 144 ? 14.004 -18.544 2.434   1.00 24.38 ?  144 VAL   A HG11 1 
ATOM   3106 H HG12 . VAL   A 1 144 ? 15.165 -19.050 1.477   1.00 24.38 ?  144 VAL   A HG12 1 
ATOM   3107 H HG13 . VAL   A 1 144 ? 15.465 -18.765 3.013   1.00 24.38 ?  144 VAL   A HG13 1 
ATOM   3108 H HG21 . VAL   A 1 144 ? 13.603 -16.184 2.700   1.00 22.12 ?  144 VAL   A HG21 1 
ATOM   3109 H HG22 . VAL   A 1 144 ? 14.816 -16.205 3.725   1.00 22.12 ?  144 VAL   A HG22 1 
ATOM   3110 H HG23 . VAL   A 1 144 ? 14.797 -15.149 2.538   1.00 22.12 ?  144 VAL   A HG23 1 
ATOM   3111 N N    . ASP   A 1 145 ? 17.905 -18.009 0.175   1.00 15.55 ?  145 ASP   A N    1 
ATOM   3112 C CA   . ASP   A 1 145 ? 18.624 -19.115 -0.451  1.00 15.88 ?  145 ASP   A CA   1 
ATOM   3113 C C    . ASP   A 1 145 ? 20.146 -18.962 -0.411  1.00 15.37 ?  145 ASP   A C    1 
ATOM   3114 O O    . ASP   A 1 145 ? 20.851 -19.852 -0.901  1.00 17.58 ?  145 ASP   A O    1 
ATOM   3115 C CB   . ASP   A 1 145 ? 18.180 -19.261 -1.908  1.00 17.39 ?  145 ASP   A CB   1 
ATOM   3116 C CG   . ASP   A 1 145 ? 16.728 -19.688 -2.042  1.00 19.54 ?  145 ASP   A CG   1 
ATOM   3117 O OD1  . ASP   A 1 145 ? 16.155 -20.225 -1.071  1.00 20.47 ?  145 ASP   A OD1  1 
ATOM   3118 O OD2  . ASP   A 1 145 ? 16.163 -19.486 -3.134  1.00 20.99 -1 145 ASP   A OD2  1 
ATOM   3119 H H    . ASP   A 1 145 ? 17.655 -17.394 -0.377  1.00 18.81 ?  145 ASP   A H    1 
ATOM   3120 H HA   . ASP   A 1 145 ? 18.393 -19.933 0.011   1.00 19.20 ?  145 ASP   A HA   1 
ATOM   3121 H HB2  . ASP   A 1 145 ? 18.292 -18.410 -2.362  1.00 21.01 ?  145 ASP   A HB2  1 
ATOM   3122 H HB3  . ASP   A 1 145 ? 18.725 -19.939 -2.335  1.00 21.01 ?  145 ASP   A HB3  1 
ATOM   3123 N N    . THR   A 1 146 ? 20.668 -17.873 0.146   1.00 13.68 ?  146 THR   A N    1 
ATOM   3124 C CA   . THR   A 1 146 ? 22.105 -17.614 0.155   1.00 13.28 ?  146 THR   A CA   1 
ATOM   3125 C C    . THR   A 1 146 ? 22.674 -17.428 1.549   1.00 13.01 ?  146 THR   A C    1 
ATOM   3126 O O    . THR   A 1 146 ? 23.747 -17.964 1.852   1.00 14.10 ?  146 THR   A O    1 
ATOM   3127 C CB   . THR   A 1 146 ? 22.426 -16.362 -0.683  1.00 13.50 ?  146 THR   A CB   1 
ATOM   3128 O OG1  . THR   A 1 146 ? 21.895 -16.528 -1.999  1.00 14.17 ?  146 THR   A OG1  1 
ATOM   3129 C CG2  . THR   A 1 146 ? 23.936 -16.131 -0.773  1.00 14.15 ?  146 THR   A CG2  1 
ATOM   3130 H H    . THR   A 1 146 ? 20.203 -17.249 0.524   1.00 16.56 ?  146 THR   A H    1 
ATOM   3131 H HA   . THR   A 1 146 ? 22.563 -18.361 -0.248  1.00 16.08 ?  146 THR   A HA   1 
ATOM   3132 H HB   . THR   A 1 146 ? 22.027 -15.579 -0.271  1.00 16.35 ?  146 THR   A HB   1 
ATOM   3133 H HG1  . THR   A 1 146 ? 21.063 -16.606 -1.963  1.00 17.16 ?  146 THR   A HG1  1 
ATOM   3134 H HG21 . THR   A 1 146 ? 24.129 -15.469 -1.453  1.00 17.13 ?  146 THR   A HG21 1 
ATOM   3135 H HG22 . THR   A 1 146 ? 24.276 -15.816 0.079   1.00 17.13 ?  146 THR   A HG22 1 
ATOM   3136 H HG23 . THR   A 1 146 ? 24.382 -16.961 -1.004  1.00 17.13 ?  146 THR   A HG23 1 
ATOM   3137 N N    . VAL   A 1 147 ? 21.992 -16.663 2.394   1.00 12.70 ?  147 VAL   A N    1 
ATOM   3138 C CA   . VAL   A 1 147 ? 22.479 -16.368 3.733   1.00 12.93 ?  147 VAL   A CA   1 
ATOM   3139 C C    . VAL   A 1 147 ? 22.158 -17.538 4.651   1.00 13.27 ?  147 VAL   A C    1 
ATOM   3140 O O    . VAL   A 1 147 ? 21.017 -18.016 4.699   1.00 13.83 ?  147 VAL   A O    1 
ATOM   3141 C CB   . VAL   A 1 147 ? 21.860 -15.058 4.253   1.00 13.19 ?  147 VAL   A CB   1 
ATOM   3142 C CG1  . VAL   A 1 147 ? 22.413 -14.743 5.618   1.00 14.41 ?  147 VAL   A CG1  1 
ATOM   3143 C CG2  . VAL   A 1 147 ? 22.115 -13.909 3.278   1.00 14.02 ?  147 VAL   A CG2  1 
ATOM   3144 H H    . VAL   A 1 147 ? 21.225 -16.307 2.221   1.00 15.39 ?  147 VAL   A H    1 
ATOM   3145 H HA   . VAL   A 1 147 ? 23.441 -16.260 3.704   1.00 15.66 ?  147 VAL   A HA   1 
ATOM   3146 H HB   . VAL   A 1 147 ? 20.904 -15.177 4.342   1.00 15.98 ?  147 VAL   A HB   1 
ATOM   3147 H HG11 . VAL   A 1 147 ? 22.169 -13.840 5.854   1.00 17.44 ?  147 VAL   A HG11 1 
ATOM   3148 H HG12 . VAL   A 1 147 ? 22.040 -15.368 6.263   1.00 17.44 ?  147 VAL   A HG12 1 
ATOM   3149 H HG13 . VAL   A 1 147 ? 23.380 -14.834 5.595   1.00 17.44 ?  147 VAL   A HG13 1 
ATOM   3150 H HG21 . VAL   A 1 147 ? 21.781 -13.085 3.672   1.00 16.98 ?  147 VAL   A HG21 1 
ATOM   3151 H HG22 . VAL   A 1 147 ? 23.066 -13.835 3.116   1.00 16.98 ?  147 VAL   A HG22 1 
ATOM   3152 H HG23 . VAL   A 1 147 ? 21.647 -14.090 2.449   1.00 16.98 ?  147 VAL   A HG23 1 
ATOM   3153 N N    . ARG   A 1 148 ? 23.177 -18.007 5.370   1.00 13.71 ?  148 ARG   A N    1 
ATOM   3154 C CA   . ARG   A 1 148 ? 23.050 -19.088 6.335   1.00 13.81 ?  148 ARG   A CA   1 
ATOM   3155 C C    . ARG   A 1 148 ? 23.186 -18.613 7.771   1.00 13.94 ?  148 ARG   A C    1 
ATOM   3156 O O    . ARG   A 1 148 ? 22.782 -19.333 8.691   1.00 15.66 ?  148 ARG   A O    1 
ATOM   3157 C CB   . ARG   A 1 148 ? 24.094 -20.180 6.055   1.00 14.19 ?  148 ARG   A CB   1 
ATOM   3158 C CG   . ARG   A 1 148 ? 23.930 -20.815 4.685   1.00 15.74 ?  148 ARG   A CG   1 
ATOM   3159 C CD   . ARG   A 1 148 ? 25.017 -21.843 4.380   1.00 16.98 ?  148 ARG   A CD   1 
ATOM   3160 N NE   . ARG   A 1 148 ? 26.355 -21.264 4.406   1.00 16.83 ?  148 ARG   A NE   1 
ATOM   3161 C CZ   . ARG   A 1 148 ? 26.866 -20.530 3.427   1.00 16.03 ?  148 ARG   A CZ   1 
ATOM   3162 N NH1  . ARG   A 1 148 ? 26.185 -20.294 2.316   1.00 16.72 ?  148 ARG   A NH1  1 
ATOM   3163 N NH2  . ARG   A 1 148 ? 28.082 -20.003 3.572   1.00 16.63 ?  148 ARG   A NH2  1 
ATOM   3164 H H    . ARG   A 1 148 ? 23.980 -17.700 5.305   1.00 16.60 ?  148 ARG   A H    1 
ATOM   3165 H HA   . ARG   A 1 148 ? 22.178 -19.489 6.241   1.00 16.72 ?  148 ARG   A HA   1 
ATOM   3166 H HB2  . ARG   A 1 148 ? 24.983 -19.804 6.100   1.00 17.18 ?  148 ARG   A HB2  1 
ATOM   3167 H HB3  . ARG   A 1 148 ? 23.999 -20.891 6.714   1.00 17.18 ?  148 ARG   A HB3  1 
ATOM   3168 H HG2  . ARG   A 1 148 ? 23.067 -21.255 4.644   1.00 19.04 ?  148 ARG   A HG2  1 
ATOM   3169 H HG3  . ARG   A 1 148 ? 23.977 -20.114 4.013   1.00 19.04 ?  148 ARG   A HG3  1 
ATOM   3170 H HD2  . ARG   A 1 148 ? 24.979 -22.547 5.046   1.00 20.52 ?  148 ARG   A HD2  1 
ATOM   3171 H HD3  . ARG   A 1 148 ? 24.859 -22.215 3.496   1.00 20.52 ?  148 ARG   A HD3  1 
ATOM   3172 H HE   . ARG   A 1 148 ? 26.841 -21.406 5.096   1.00 20.34 ?  148 ARG   A HE   1 
ATOM   3173 H HH11 . ARG   A 1 148 ? 25.397 -20.616 2.212   1.00 20.22 ?  148 ARG   A HH11 1 
ATOM   3174 H HH12 . ARG   A 1 148 ? 26.532 -19.805 1.696   1.00 20.22 ?  148 ARG   A HH12 1 
ATOM   3175 H HH21 . ARG   A 1 148 ? 28.528 -20.146 4.293   1.00 20.10 ?  148 ARG   A HH21 1 
ATOM   3176 H HH22 . ARG   A 1 148 ? 28.422 -19.519 2.947   1.00 20.10 ?  148 ARG   A HH22 1 
ATOM   3177 N N    . THR   A 1 149 ? 23.736 -17.423 7.977   1.00 13.92 ?  149 THR   A N    1 
ATOM   3178 C CA   . THR   A 1 149 ? 23.814 -16.813 9.292   1.00 14.23 ?  149 THR   A CA   1 
ATOM   3179 C C    . THR   A 1 149 ? 22.484 -16.126 9.605   1.00 13.78 ?  149 THR   A C    1 
ATOM   3180 O O    . THR   A 1 149 ? 21.547 -16.126 8.796   1.00 14.60 ?  149 THR   A O    1 
ATOM   3181 C CB   . THR   A 1 149 ? 25.014 -15.872 9.345   1.00 14.94 ?  149 THR   A CB   1 
ATOM   3182 O OG1  . THR   A 1 149 ? 24.881 -14.929 8.280   1.00 14.91 ?  149 THR   A OG1  1 
ATOM   3183 C CG2  . THR   A 1 149 ? 26.331 -16.658 9.207   1.00 15.46 ?  149 THR   A CG2  1 
ATOM   3184 H H    . THR   A 1 149 ? 24.086 -16.935 7.354   1.00 16.85 ?  149 THR   A H    1 
ATOM   3185 H HA   . THR   A 1 149 ? 23.949 -17.513 9.950   1.00 17.22 ?  149 THR   A HA   1 
ATOM   3186 H HB   . THR   A 1 149 ? 25.019 -15.409 10.192  1.00 18.07 ?  149 THR   A HB   1 
ATOM   3187 H HG1  . THR   A 1 149 ? 25.536 -14.396 8.282   1.00 18.04 ?  149 THR   A HG1  1 
ATOM   3188 H HG21 . THR   A 1 149 ? 27.087 -16.054 9.258   1.00 18.71 ?  149 THR   A HG21 1 
ATOM   3189 H HG22 . THR   A 1 149 ? 26.405 -17.316 9.918   1.00 18.71 ?  149 THR   A HG22 1 
ATOM   3190 H HG23 . THR   A 1 149 ? 26.358 -17.122 8.351   1.00 18.71 ?  149 THR   A HG23 1 
ATOM   3191 N N    . ASN   A 1 150 ? 22.366 -15.581 10.809  1.00 13.63 ?  150 ASN   A N    1 
ATOM   3192 C CA   . ASN   A 1 150 ? 21.084 -15.070 11.299  1.00 14.91 ?  150 ASN   A CA   1 
ATOM   3193 C C    . ASN   A 1 150 ? 20.896 -13.626 10.848  1.00 13.97 ?  150 ASN   A C    1 
ATOM   3194 O O    . ASN   A 1 150 ? 21.637 -12.730 11.274  1.00 15.58 ?  150 ASN   A O    1 
ATOM   3195 C CB   . ASN   A 1 150 ? 21.032 -15.189 12.816  1.00 17.70 ?  150 ASN   A CB   1 
ATOM   3196 C CG   . ASN   A 1 150 ? 20.899 -16.623 13.270  1.00 22.00 ?  150 ASN   A CG   1 
ATOM   3197 O OD1  . ASN   A 1 150 ? 20.275 -17.437 12.591  1.00 23.25 ?  150 ASN   A OD1  1 
ATOM   3198 N ND2  . ASN   A 1 150 ? 21.498 -16.948 14.409  1.00 24.49 ?  150 ASN   A ND2  1 
ATOM   3199 H H    . ASN   A 1 150 ? 23.018 -15.487 11.364  1.00 16.50 ?  150 ASN   A H    1 
ATOM   3200 H HA   . ASN   A 1 150 ? 20.365 -15.607 10.927  1.00 18.04 ?  150 ASN   A HA   1 
ATOM   3201 H HB2  . ASN   A 1 150 ? 21.849 -14.830 13.194  1.00 21.39 ?  150 ASN   A HB2  1 
ATOM   3202 H HB3  . ASN   A 1 150 ? 20.265 -14.699 13.149  1.00 21.39 ?  150 ASN   A HB3  1 
ATOM   3203 H HD21 . ASN   A 1 150 ? 21.452 -17.756 14.708  1.00 29.54 ?  150 ASN   A HD21 1 
ATOM   3204 H HD22 . ASN   A 1 150 ? 21.927 -16.352 14.858  1.00 29.54 ?  150 ASN   A HD22 1 
ATOM   3205 N N    . VAL   A 1 151 ? 19.905 -13.394 9.995   1.00 13.96 ?  151 VAL   A N    1 
ATOM   3206 C CA   . VAL   A 1 151 ? 19.693 -12.081 9.407   1.00 13.94 ?  151 VAL   A CA   1 
ATOM   3207 C C    . VAL   A 1 151 ? 18.307 -11.568 9.777   1.00 13.69 ?  151 VAL   A C    1 
ATOM   3208 O O    . VAL   A 1 151 ? 17.303 -12.284 9.637   1.00 15.02 ?  151 VAL   A O    1 
ATOM   3209 C CB   . VAL   A 1 151 ? 19.975 -12.064 7.889   1.00 15.38 ?  151 VAL   A CB   1 
ATOM   3210 C CG1  . VAL   A 1 151 ? 19.151 -13.081 7.133   1.00 16.34 ?  151 VAL   A CG1  1 
ATOM   3211 C CG2  . VAL   A 1 151 ? 19.787 -10.648 7.327   1.00 15.50 ?  151 VAL   A CG2  1 
ATOM   3212 H H    . VAL   A 1 151 ? 19.340 -13.987 9.741   1.00 16.90 ?  151 VAL   A H    1 
ATOM   3213 H HA   . VAL   A 1 151 ? 20.334 -11.469 9.807   1.00 16.88 ?  151 VAL   A HA   1 
ATOM   3214 H HB   . VAL   A 1 151 ? 20.909 -12.297 7.753   1.00 18.61 ?  151 VAL   A HB   1 
ATOM   3215 H HG11 . VAL   A 1 151 ? 19.352 -13.019 6.185   1.00 19.76 ?  151 VAL   A HG11 1 
ATOM   3216 H HG12 . VAL   A 1 151 ? 19.374 -13.974 7.454   1.00 19.76 ?  151 VAL   A HG12 1 
ATOM   3217 H HG13 . VAL   A 1 151 ? 18.209 -12.907 7.282   1.00 19.76 ?  151 VAL   A HG13 1 
ATOM   3218 H HG21 . VAL   A 1 151 ? 20.103 -10.628 6.407   1.00 18.75 ?  151 VAL   A HG21 1 
ATOM   3219 H HG22 . VAL   A 1 151 ? 18.848 -10.415 7.356   1.00 18.75 ?  151 VAL   A HG22 1 
ATOM   3220 H HG23 . VAL   A 1 151 ? 20.302 -10.022 7.862   1.00 18.75 ?  151 VAL   A HG23 1 
ATOM   3221 N N    . TYR   A 1 152 ? 18.288 -10.323 10.272  1.00 13.41 ?  152 TYR   A N    1 
ATOM   3222 C CA   . TYR   A 1 152 ? 17.095 -9.584  10.662  1.00 12.98 ?  152 TYR   A CA   1 
ATOM   3223 C C    . TYR   A 1 152 ? 16.902 -8.478  9.634   1.00 12.84 ?  152 TYR   A C    1 
ATOM   3224 O O    . TYR   A 1 152 ? 17.674 -7.515  9.591   1.00 13.28 ?  152 TYR   A O    1 
ATOM   3225 C CB   . TYR   A 1 152 ? 17.279 -9.045  12.079  1.00 13.94 ?  152 TYR   A CB   1 
ATOM   3226 C CG   . TYR   A 1 152 ? 17.242 -10.179 13.073  1.00 14.70 ?  152 TYR   A CG   1 
ATOM   3227 C CD1  . TYR   A 1 152 ? 18.376 -10.932 13.350  1.00 16.49 ?  152 TYR   A CD1  1 
ATOM   3228 C CD2  . TYR   A 1 152 ? 16.058 -10.541 13.698  1.00 15.16 ?  152 TYR   A CD2  1 
ATOM   3229 C CE1  . TYR   A 1 152 ? 18.336 -12.002 14.230  1.00 17.54 ?  152 TYR   A CE1  1 
ATOM   3230 C CE2  . TYR   A 1 152 ? 16.007 -11.615 14.582  1.00 16.41 ?  152 TYR   A CE2  1 
ATOM   3231 C CZ   . TYR   A 1 152 ? 17.151 -12.339 14.843  1.00 17.12 ?  152 TYR   A CZ   1 
ATOM   3232 O OH   . TYR   A 1 152 ? 17.109 -13.411 15.718  1.00 19.44 ?  152 TYR   A OH   1 
ATOM   3233 H H    . TYR   A 1 152 ? 19.008 -9.858  10.383  1.00 16.24 ?  152 TYR   A H    1 
ATOM   3234 H HA   . TYR   A 1 152 ? 16.326 -10.175 10.648  1.00 15.72 ?  152 TYR   A HA   1 
ATOM   3235 H HB2  . TYR   A 1 152 ? 18.142 -8.609  12.150  1.00 16.88 ?  152 TYR   A HB2  1 
ATOM   3236 H HB3  . TYR   A 1 152 ? 16.568 -8.426  12.291  1.00 16.88 ?  152 TYR   A HB3  1 
ATOM   3237 H HD1  . TYR   A 1 152 ? 19.177 -10.713 12.933  1.00 19.93 ?  152 TYR   A HD1  1 
ATOM   3238 H HD2  . TYR   A 1 152 ? 15.279 -10.059 13.521  1.00 18.34 ?  152 TYR   A HD2  1 
ATOM   3239 H HE1  . TYR   A 1 152 ? 19.105 -12.491 14.412  1.00 21.19 ?  152 TYR   A HE1  1 
ATOM   3240 H HE2  . TYR   A 1 152 ? 15.202 -11.837 15.002  1.00 19.84 ?  152 TYR   A HE2  1 
ATOM   3241 H HH   . TYR   A 1 152 ? 16.328 -13.492 16.030  1.00 23.47 ?  152 TYR   A HH   1 
ATOM   3242 N N    . LEU   A 1 153 ? 15.894 -8.647  8.781   1.00 13.12 ?  153 LEU   A N    1 
ATOM   3243 C CA   . LEU   A 1 153 ? 15.629 -7.730  7.680   1.00 13.45 ?  153 LEU   A CA   1 
ATOM   3244 C C    . LEU   A 1 153 ? 14.632 -6.663  8.107   1.00 14.05 ?  153 LEU   A C    1 
ATOM   3245 O O    . LEU   A 1 153 ? 13.539 -6.981  8.586   1.00 15.22 ?  153 LEU   A O    1 
ATOM   3246 C CB   . LEU   A 1 153 ? 15.056 -8.485  6.482   1.00 13.23 ?  153 LEU   A CB   1 
ATOM   3247 C CG   . LEU   A 1 153 ? 15.982 -9.509  5.823   1.00 13.85 ?  153 LEU   A CG   1 
ATOM   3248 C CD1  . LEU   A 1 153 ? 15.182 -10.391 4.890   1.00 13.94 ?  153 LEU   A CD1  1 
ATOM   3249 C CD2  . LEU   A 1 153 ? 17.096 -8.815  5.064   1.00 14.20 ?  153 LEU   A CD2  1 
ATOM   3250 H H    . LEU   A 1 153 ? 15.330 -9.300  8.825   1.00 15.89 ?  153 LEU   A H    1 
ATOM   3251 H HA   . LEU   A 1 153 ? 16.455 -7.305  7.420   1.00 16.29 ?  153 LEU   A HA   1 
ATOM   3252 H HB2  . LEU   A 1 153 ? 14.259 -8.950  6.773   1.00 16.02 ?  153 LEU   A HB2  1 
ATOM   3253 H HB3  . LEU   A 1 153 ? 14.818 -7.828  5.805   1.00 16.02 ?  153 LEU   A HB3  1 
ATOM   3254 H HG   . LEU   A 1 153 ? 16.383 -10.065 6.513   1.00 16.77 ?  153 LEU   A HG   1 
ATOM   3255 H HD11 . LEU   A 1 153 ? 15.761 -11.083 4.538   1.00 16.88 ?  153 LEU   A HD11 1 
ATOM   3256 H HD12 . LEU   A 1 153 ? 14.452 -10.794 5.387   1.00 16.88 ?  153 LEU   A HD12 1 
ATOM   3257 H HD13 . LEU   A 1 153 ? 14.831 -9.849  4.168   1.00 16.88 ?  153 LEU   A HD13 1 
ATOM   3258 H HD21 . LEU   A 1 153 ? 17.660 -9.488  4.659   1.00 17.19 ?  153 LEU   A HD21 1 
ATOM   3259 H HD22 . LEU   A 1 153 ? 16.699 -8.254  4.380   1.00 17.19 ?  153 LEU   A HD22 1 
ATOM   3260 H HD23 . LEU   A 1 153 ? 17.608 -8.274  5.682   1.00 17.19 ?  153 LEU   A HD23 1 
ATOM   3261 N N    A ALA   A 1 154 ? 14.995 -5.405  7.871   0.86 14.06 ?  154 ALA   A N    1 
ATOM   3262 N N    B ALA   A 1 154 ? 15.022 -5.398  7.965   0.14 13.87 ?  154 ALA   A N    1 
ATOM   3263 C CA   A ALA   A 1 154 ? 14.126 -4.258  8.091   0.86 15.24 ?  154 ALA   A CA   1 
ATOM   3264 C CA   B ALA   A 1 154 ? 14.191 -4.258  8.338   0.14 14.04 ?  154 ALA   A CA   1 
ATOM   3265 C C    A ALA   A 1 154 ? 13.627 -3.752  6.743   0.86 15.25 ?  154 ALA   A C    1 
ATOM   3266 C C    B ALA   A 1 154 ? 13.735 -3.583  7.052   0.14 13.99 ?  154 ALA   A C    1 
ATOM   3267 O O    A ALA   A 1 154 ? 14.427 -3.412  5.864   0.86 15.56 ?  154 ALA   A O    1 
ATOM   3268 O O    B ALA   A 1 154 ? 14.556 -3.034  6.309   0.14 13.60 ?  154 ALA   A O    1 
ATOM   3269 C CB   A ALA   A 1 154 ? 14.884 -3.141  8.805   0.86 15.59 ?  154 ALA   A CB   1 
ATOM   3270 C CB   B ALA   A 1 154 ? 14.973 -3.287  9.220   0.14 14.05 ?  154 ALA   A CB   1 
ATOM   3271 H H    A ALA   A 1 154 ? 15.776 -5.183  7.573   0.86 17.02 ?  154 ALA   A H    1 
ATOM   3272 H H    B ALA   A 1 154 ? 15.786 -5.165  7.642   0.14 16.80 ?  154 ALA   A H    1 
ATOM   3273 H HA   A ALA   A 1 154 ? 13.368 -4.516  8.638   0.86 18.44 ?  154 ALA   A HA   1 
ATOM   3274 H HA   B ALA   A 1 154 ? 13.411 -4.560  8.829   0.14 16.99 ?  154 ALA   A HA   1 
ATOM   3275 H HB1  A ALA   A 1 154 ? 14.287 -2.385  8.938   0.86 18.86 ?  154 ALA   A HB1  1 
ATOM   3276 H HB1  B ALA   A 1 154 ? 14.401 -2.538  9.454   0.14 17.00 ?  154 ALA   A HB1  1 
ATOM   3277 H HB2  A ALA   A 1 154 ? 15.205 -3.463  9.660   0.86 18.86 ?  154 ALA   A HB2  1 
ATOM   3278 H HB2  B ALA   A 1 154 ? 15.259 -3.748  10.025  0.14 17.00 ?  154 ALA   A HB2  1 
ATOM   3279 H HB3  A ALA   A 1 154 ? 15.638 -2.866  8.253   0.86 18.86 ?  154 ALA   A HB3  1 
ATOM   3280 H HB3  B ALA   A 1 154 ? 15.748 -2.968  8.730   0.14 17.00 ?  154 ALA   A HB3  1 
ATOM   3281 N N    A VAL   A 1 155 ? 12.308 -3.688  6.593   0.86 15.92 ?  155 VAL   A N    1 
ATOM   3282 N N    B VAL   A 1 155 ? 12.433 -3.623  6.790   0.14 14.59 ?  155 VAL   A N    1 
ATOM   3283 C CA   A VAL   A 1 155 ? 11.656 -3.214  5.378   0.86 17.02 ?  155 VAL   A CA   1 
ATOM   3284 C CA   B VAL   A 1 155 ? 11.856 -3.103  5.555   0.14 15.47 ?  155 VAL   A CA   1 
ATOM   3285 C C    A VAL   A 1 155 ? 10.897 -1.940  5.730   0.86 18.27 ?  155 VAL   A C    1 
ATOM   3286 C C    B VAL   A 1 155 ? 11.020 -1.883  5.914   0.14 16.49 ?  155 VAL   A C    1 
ATOM   3287 O O    A VAL   A 1 155 ? 9.947  -1.981  6.521   0.86 18.88 ?  155 VAL   A O    1 
ATOM   3288 O O    B VAL   A 1 155 ? 9.978  -2.001  6.570   0.14 16.60 ?  155 VAL   A O    1 
ATOM   3289 C CB   A VAL   A 1 155 ? 10.719 -4.278  4.783   0.86 17.23 ?  155 VAL   A CB   1 
ATOM   3290 C CB   B VAL   A 1 155 ? 11.026 -4.167  4.824   0.14 15.45 ?  155 VAL   A CB   1 
ATOM   3291 C CG1  A VAL   A 1 155 ? 9.985  -3.724  3.575   0.86 18.26 ?  155 VAL   A CG1  1 
ATOM   3292 C CG1  B VAL   A 1 155 ? 10.452 -3.604  3.531   0.14 15.28 ?  155 VAL   A CG1  1 
ATOM   3293 C CG2  A VAL   A 1 155 ? 11.516 -5.521  4.401   0.86 17.77 ?  155 VAL   A CG2  1 
ATOM   3294 C CG2  B VAL   A 1 155 ? 11.884 -5.390  4.540   0.14 15.62 ?  155 VAL   A CG2  1 
ATOM   3295 H H    A VAL   A 1 155 ? 11.751 -3.933  7.205   0.86 19.25 ?  155 VAL   A H    1 
ATOM   3296 H H    B VAL   A 1 155 ? 11.846 -3.951  7.329   0.14 17.66 ?  155 VAL   A H    1 
ATOM   3297 H HA   A VAL   A 1 155 ? 12.327 -2.998  4.717   0.86 20.57 ?  155 VAL   A HA   1 
ATOM   3298 H HA   B VAL   A 1 155 ? 12.567 -2.816  4.965   0.14 18.71 ?  155 VAL   A HA   1 
ATOM   3299 H HB   A VAL   A 1 155 ? 10.061 -4.537  5.453   0.86 20.83 ?  155 VAL   A HB   1 
ATOM   3300 H HB   B VAL   A 1 155 ? 10.288 -4.441  5.390   0.14 18.69 ?  155 VAL   A HB   1 
ATOM   3301 H HG11 A VAL   A 1 155 ? 9.561  -4.457  3.102   0.86 22.06 ?  155 VAL   A HG11 1 
ATOM   3302 H HG11 B VAL   A 1 155 ? 10.058 -4.330  3.021   0.14 18.48 ?  155 VAL   A HG11 1 
ATOM   3303 H HG12 A VAL   A 1 155 ? 9.311  -3.092  3.874   0.86 22.06 ?  155 VAL   A HG12 1 
ATOM   3304 H HG12 B VAL   A 1 155 ? 9.774  -2.945  3.744   0.14 18.48 ?  155 VAL   A HG12 1 
ATOM   3305 H HG13 A VAL   A 1 155 ? 10.623 -3.281  2.996   0.86 22.06 ?  155 VAL   A HG13 1 
ATOM   3306 H HG13 B VAL   A 1 155 ? 11.167 -3.194  3.021   0.14 18.48 ?  155 VAL   A HG13 1 
ATOM   3307 H HG21 A VAL   A 1 155 ? 10.921 -6.170  3.998   0.86 21.47 ?  155 VAL   A HG21 1 
ATOM   3308 H HG21 B VAL   A 1 155 ? 11.367 -6.024  4.019   0.14 18.90 ?  155 VAL   A HG21 1 
ATOM   3309 H HG22 A VAL   A 1 155 ? 12.208 -5.268  3.769   0.86 21.47 ?  155 VAL   A HG22 1 
ATOM   3310 H HG22 B VAL   A 1 155 ? 12.670 -5.115  4.041   0.14 18.90 ?  155 VAL   A HG22 1 
ATOM   3311 H HG23 A VAL   A 1 155 ? 11.924 -5.898  5.199   0.86 21.47 ?  155 VAL   A HG23 1 
ATOM   3312 H HG23 B VAL   A 1 155 ? 12.152 -5.793  5.381   0.14 18.90 ?  155 VAL   A HG23 1 
ATOM   3313 N N    A PHE   A 1 156 ? 11.318 -0.814  5.142   0.86 19.95 ?  156 PHE   A N    1 
ATOM   3314 N N    B PHE   A 1 156 ? 11.480 -0.708  5.487   0.14 17.39 ?  156 PHE   A N    1 
ATOM   3315 C CA   A PHE   A 1 156 ? 10.774 0.493   5.519   0.86 21.94 ?  156 PHE   A CA   1 
ATOM   3316 C CA   B PHE   A 1 156 ? 10.821 0.557   5.812   0.14 18.60 ?  156 PHE   A CA   1 
ATOM   3317 C C    A PHE   A 1 156 ? 9.305  0.635   5.135   0.86 22.19 ?  156 PHE   A C    1 
ATOM   3318 C C    B PHE   A 1 156 ? 9.807  0.937   4.727   0.14 19.26 ?  156 PHE   A C    1 
ATOM   3319 O O    A PHE   A 1 156 ? 8.499  1.158   5.916   0.86 23.32 ?  156 PHE   A O    1 
ATOM   3320 O O    B PHE   A 1 156 ? 9.877  1.990   4.093   0.14 19.46 ?  156 PHE   A O    1 
ATOM   3321 C CB   A PHE   A 1 156 ? 11.602 1.592   4.852   0.86 22.95 ?  156 PHE   A CB   1 
ATOM   3322 C CB   B PHE   A 1 156 ? 11.870 1.643   6.040   0.14 18.96 ?  156 PHE   A CB   1 
ATOM   3323 C CG   A PHE   A 1 156 ? 11.128 2.986   5.161   0.86 24.50 ?  156 PHE   A CG   1 
ATOM   3324 C CG   B PHE   A 1 156 ? 11.304 2.959   6.490   0.14 19.46 ?  156 PHE   A CG   1 
ATOM   3325 C CD1  A PHE   A 1 156 ? 11.076 3.430   6.472   0.86 25.66 ?  156 PHE   A CD1  1 
ATOM   3326 C CD1  B PHE   A 1 156 ? 10.249 3.011   7.385   0.14 19.62 ?  156 PHE   A CD1  1 
ATOM   3327 C CD2  A PHE   A 1 156 ? 10.753 3.854   4.145   0.86 25.22 ?  156 PHE   A CD2  1 
ATOM   3328 C CD2  B PHE   A 1 156 ? 11.844 4.148   6.027   0.14 19.63 ?  156 PHE   A CD2  1 
ATOM   3329 C CE1  A PHE   A 1 156 ? 10.649 4.707   6.770   0.86 26.76 ?  156 PHE   A CE1  1 
ATOM   3330 C CE1  B PHE   A 1 156 ? 9.733  4.224   7.797   0.14 19.64 ?  156 PHE   A CE1  1 
ATOM   3331 C CE2  A PHE   A 1 156 ? 10.323 5.140   4.435   0.86 26.35 ?  156 PHE   A CE2  1 
ATOM   3332 C CE2  B PHE   A 1 156 ? 11.333 5.364   6.437   0.14 19.79 ?  156 PHE   A CE2  1 
ATOM   3333 C CZ   A PHE   A 1 156 ? 10.276 5.569   5.750   0.86 26.93 ?  156 PHE   A CZ   1 
ATOM   3334 C CZ   B PHE   A 1 156 ? 10.276 5.401   7.324   0.14 19.72 ?  156 PHE   A CZ   1 
ATOM   3335 H H    A PHE   A 1 156 ? 11.923 -0.786  4.531   0.86 24.08 ?  156 PHE   A H    1 
ATOM   3336 H H    B PHE   A 1 156 ? 12.192 -0.612  5.010   0.14 21.01 ?  156 PHE   A H    1 
ATOM   3337 H HA   A PHE   A 1 156 ? 10.852 0.603   6.478   0.86 26.48 ?  156 PHE   A HA   1 
ATOM   3338 H HA   B PHE   A 1 156 ? 10.332 0.439   6.638   0.14 22.47 ?  156 PHE   A HA   1 
ATOM   3339 H HB2  A PHE   A 1 156 ? 12.523 1.518   5.152   0.86 27.68 ?  156 PHE   A HB2  1 
ATOM   3340 H HB2  B PHE   A 1 156 ? 12.492 1.335   6.718   0.14 22.91 ?  156 PHE   A HB2  1 
ATOM   3341 H HB3  A PHE   A 1 156 ? 11.564 1.472   3.889   0.86 27.68 ?  156 PHE   A HB3  1 
ATOM   3342 H HB3  B PHE   A 1 156 ? 12.348 1.800   5.213   0.14 22.91 ?  156 PHE   A HB3  1 
ATOM   3343 H HD1  A PHE   A 1 156 ? 11.331 2.853   7.160   0.86 30.94 ?  156 PHE   A HD1  1 
ATOM   3344 H HD1  B PHE   A 1 156 ? 9.879  2.220   7.706   0.14 23.69 ?  156 PHE   A HD1  1 
ATOM   3345 H HD2  A PHE   A 1 156 ? 10.784 3.565   3.260   0.86 30.41 ?  156 PHE   A HD2  1 
ATOM   3346 H HD2  B PHE   A 1 156 ? 12.557 4.127   5.431   0.14 23.71 ?  156 PHE   A HD2  1 
ATOM   3347 H HE1  A PHE   A 1 156 ? 10.618 4.993   7.654   0.86 32.26 ?  156 PHE   A HE1  1 
ATOM   3348 H HE1  B PHE   A 1 156 ? 9.021  4.247   8.394   0.14 23.72 ?  156 PHE   A HE1  1 
ATOM   3349 H HE2  A PHE   A 1 156 ? 10.069 5.710   3.748   0.86 31.76 ?  156 PHE   A HE2  1 
ATOM   3350 H HE2  B PHE   A 1 156 ? 11.701 6.157   6.117   0.14 23.89 ?  156 PHE   A HE2  1 
ATOM   3351 H HZ   A PHE   A 1 156 ? 9.985  6.427   5.949   0.86 32.46 ?  156 PHE   A HZ   1 
ATOM   3352 H HZ   B PHE   A 1 156 ? 9.929  6.217   7.601   0.14 23.81 ?  156 PHE   A HZ   1 
ATOM   3353 N N    A ASP   A 1 157 ? 8.950  0.211   3.930   0.86 22.26 ?  157 ASP   A N    1 
ATOM   3354 N N    B ASP   A 1 157 ? 8.839  0.039   4.533   0.14 19.64 ?  157 ASP   A N    1 
ATOM   3355 C CA   A ASP   A 1 157 ? 7.622  0.449   3.383   0.86 23.47 ?  157 ASP   A CA   1 
ATOM   3356 C CA   B ASP   A 1 157 ? 7.750  0.247   3.578   0.14 20.36 ?  157 ASP   A CA   1 
ATOM   3357 C C    A ASP   A 1 157 ? 6.651  -0.618  3.884   0.86 23.51 ?  157 ASP   A C    1 
ATOM   3358 C C    B ASP   A 1 157 ? 6.637  -0.733  3.934   0.14 20.81 ?  157 ASP   A C    1 
ATOM   3359 O O    A ASP   A 1 157 ? 6.848  -1.814  3.629   0.86 22.82 ?  157 ASP   A O    1 
ATOM   3360 O O    B ASP   A 1 157 ? 6.774  -1.935  3.684   0.14 20.78 ?  157 ASP   A O    1 
ATOM   3361 C CB   A ASP   A 1 157 ? 7.709  0.415   1.861   0.86 25.41 ?  157 ASP   A CB   1 
ATOM   3362 C CB   B ASP   A 1 157 ? 8.233  0.031   2.147   0.14 20.69 ?  157 ASP   A CB   1 
ATOM   3363 C CG   A ASP   A 1 157 ? 6.445  0.901   1.201   0.86 27.78 ?  157 ASP   A CG   1 
ATOM   3364 C CG   B ASP   A 1 157 ? 7.218  0.497   1.117   0.14 21.11 ?  157 ASP   A CG   1 
ATOM   3365 O OD1  A ASP   A 1 157 ? 6.215  2.124   1.198   0.86 29.95 ?  157 ASP   A OD1  1 
ATOM   3366 O OD1  B ASP   A 1 157 ? 6.040  0.090   1.214   0.14 21.02 ?  157 ASP   A OD1  1 
ATOM   3367 O OD2  A ASP   A 1 157 ? 5.667  0.063   0.699   0.86 27.88 -1 157 ASP   A OD2  1 
ATOM   3368 O OD2  B ASP   A 1 157 ? 7.588  1.284   0.222   0.14 21.58 -1 157 ASP   A OD2  1 
ATOM   3369 H H    A ASP   A 1 157 ? 9.474  -0.217  3.398   0.86 26.86 ?  157 ASP   A H    1 
ATOM   3370 H H    B ASP   A 1 157 ? 8.789  -0.706  4.948   0.14 23.72 ?  157 ASP   A H    1 
ATOM   3371 H HA   A ASP   A 1 157 ? 7.303  1.326   3.661   0.86 28.31 ?  157 ASP   A HA   1 
ATOM   3372 H HA   B ASP   A 1 157 ? 7.409  1.148   3.654   0.14 24.58 ?  157 ASP   A HA   1 
ATOM   3373 H HB2  A ASP   A 1 157 ? 8.464  0.961   1.576   0.86 30.64 ?  157 ASP   A HB2  1 
ATOM   3374 H HB2  B ASP   A 1 157 ? 9.055  0.529   2.011   0.14 24.98 ?  157 ASP   A HB2  1 
ATOM   3375 H HB3  A ASP   A 1 157 ? 7.843  -0.499  1.575   0.86 30.64 ?  157 ASP   A HB3  1 
ATOM   3376 H HB3  B ASP   A 1 157 ? 8.397  -0.917  1.999   0.14 24.98 ?  157 ASP   A HB3  1 
ATOM   3377 N N    A LYS   A 1 158 ? 5.601  -0.187  4.594   0.86 24.79 ?  158 LYS   A N    1 
ATOM   3378 N N    B LYS   A 1 158 ? 5.542  -0.224  4.510   0.14 21.18 ?  158 LYS   A N    1 
ATOM   3379 C CA   A LYS   A 1 158 ? 4.654  -1.142  5.165   0.86 25.44 ?  158 LYS   A CA   1 
ATOM   3380 C CA   B LYS   A 1 158 ? 4.472  -1.108  4.969   0.14 21.53 ?  158 LYS   A CA   1 
ATOM   3381 C C    A LYS   A 1 158 ? 3.932  -1.914  4.068   0.86 24.61 ?  158 LYS   A C    1 
ATOM   3382 C C    B LYS   A 1 158 ? 3.807  -1.836  3.804   0.14 21.58 ?  158 LYS   A C    1 
ATOM   3383 O O    A LYS   A 1 158 ? 3.740  -3.134  4.170   0.86 24.40 ?  158 LYS   A O    1 
ATOM   3384 O O    B LYS   A 1 158 ? 3.479  -3.023  3.912   0.14 21.56 ?  158 LYS   A O    1 
ATOM   3385 C CB   A LYS   A 1 158 ? 3.658  -0.406  6.068   0.86 26.91 ?  158 LYS   A CB   1 
ATOM   3386 C CB   B LYS   A 1 158 ? 3.465  -0.315  5.814   0.14 21.78 ?  158 LYS   A CB   1 
ATOM   3387 C CG   A LYS   A 1 158 ? 2.439  -1.229  6.497   0.86 28.12 ?  158 LYS   A CG   1 
ATOM   3388 C CG   B LYS   A 1 158 ? 2.017  -0.327  5.335   0.14 21.95 ?  158 LYS   A CG   1 
ATOM   3389 C CD   A LYS   A 1 158 ? 2.820  -2.477  7.292   0.86 29.38 ?  158 LYS   A CD   1 
ATOM   3390 C CD   B LYS   A 1 158 ? 1.217  -1.436  5.989   0.14 22.04 ?  158 LYS   A CD   1 
ATOM   3391 C CE   A LYS   A 1 158 ? 1.568  -3.205  7.784   0.86 30.30 ?  158 LYS   A CE   1 
ATOM   3392 C CE   B LYS   A 1 158 ? -0.206 -1.445  5.468   0.14 21.92 ?  158 LYS   A CE   1 
ATOM   3393 N NZ   A LYS   A 1 158 ? 1.866  -4.527  8.406   0.86 30.84 ?  158 LYS   A NZ   1 
ATOM   3394 N NZ   B LYS   A 1 158 ? -0.241 -1.737  4.009   0.14 21.86 ?  158 LYS   A NZ   1 
ATOM   3395 H H    A LYS   A 1 158 ? 5.431  0.636   4.761   0.86 29.90 ?  158 LYS   A H    1 
ATOM   3396 H H    B LYS   A 1 158 ? 5.396  0.615   4.654   0.14 25.57 ?  158 LYS   A H    1 
ATOM   3397 H HA   A LYS   A 1 158 ? 5.139  -1.776  5.722   0.86 30.68 ?  158 LYS   A HA   1 
ATOM   3398 H HA   B LYS   A 1 158 ? 4.854  -1.783  5.539   0.14 25.98 ?  158 LYS   A HA   1 
ATOM   3399 H HB2  A LYS   A 1 158 ? 4.118  -0.122  6.879   0.86 32.44 ?  158 LYS   A HB2  1 
ATOM   3400 H HB2  B LYS   A 1 158 ? 3.469  -0.682  6.717   0.14 26.29 ?  158 LYS   A HB2  1 
ATOM   3401 H HB3  A LYS   A 1 158 ? 3.333  0.379   5.597   0.86 32.44 ?  158 LYS   A HB3  1 
ATOM   3402 H HB3  B LYS   A 1 158 ? 3.746  0.613   5.850   0.14 26.29 ?  158 LYS   A HB3  1 
ATOM   3403 H HG2  A LYS   A 1 158 ? 1.874  -0.678  7.062   0.86 33.90 ?  158 LYS   A HG2  1 
ATOM   3404 H HG2  B LYS   A 1 158 ? 1.615  0.503   5.608   0.14 26.49 ?  158 LYS   A HG2  1 
ATOM   3405 H HG3  A LYS   A 1 158 ? 1.942  -1.505  5.712   0.86 33.90 ?  158 LYS   A HG3  1 
ATOM   3406 H HG3  B LYS   A 1 158 ? 1.946  -0.402  4.371   0.14 26.49 ?  158 LYS   A HG3  1 
ATOM   3407 H HD2  A LYS   A 1 158 ? 3.323  -3.079  6.724   0.86 35.40 ?  158 LYS   A HD2  1 
ATOM   3408 H HD2  B LYS   A 1 158 ? 1.622  -2.294  5.792   0.14 26.60 ?  158 LYS   A HD2  1 
ATOM   3409 H HD3  A LYS   A 1 158 ? 3.348  -2.217  8.064   0.86 35.40 ?  158 LYS   A HD3  1 
ATOM   3410 H HD3  B LYS   A 1 158 ? 1.191  -1.287  6.949   0.14 26.60 ?  158 LYS   A HD3  1 
ATOM   3411 H HE2  A LYS   A 1 158 ? 1.125  -2.655  8.449   0.86 36.51 ?  158 LYS   A HE2  1 
ATOM   3412 H HE2  B LYS   A 1 158 ? -0.714 -2.129  5.930   0.14 26.46 ?  158 LYS   A HE2  1 
ATOM   3413 H HE3  A LYS   A 1 158 ? 0.975  -3.354  7.032   0.86 36.51 ?  158 LYS   A HE3  1 
ATOM   3414 H HE3  B LYS   A 1 158 ? -0.607 -0.572  5.615   0.14 26.46 ?  158 LYS   A HE3  1 
ATOM   3415 H HZ1  A LYS   A 1 158 ? 1.112  -4.914  8.676   0.86 37.16 ?  158 LYS   A HZ1  1 
ATOM   3416 H HZ1  B LYS   A 1 158 ? -1.082 -1.832  3.739   0.14 26.39 ?  158 LYS   A HZ1  1 
ATOM   3417 H HZ2  A LYS   A 1 158 ? 2.267  -5.058  7.814   0.86 37.16 ?  158 LYS   A HZ2  1 
ATOM   3418 H HZ2  B LYS   A 1 158 ? 0.135  -1.069  3.555   0.14 26.39 ?  158 LYS   A HZ2  1 
ATOM   3419 H HZ3  A LYS   A 1 158 ? 2.404  -4.420  9.107   0.86 37.16 ?  158 LYS   A HZ3  1 
ATOM   3420 H HZ3  B LYS   A 1 158 ? 0.205  -2.488  3.839   0.14 26.39 ?  158 LYS   A HZ3  1 
ATOM   3421 N N    A ASN   A 1 159 ? 3.524  -1.221  3.007   0.86 25.30 ?  159 ASN   A N    1 
ATOM   3422 N N    B ASN   A 1 159 ? 3.603  -1.142  2.682   0.14 21.83 ?  159 ASN   A N    1 
ATOM   3423 C CA   A ASN   A 1 159 ? 2.868  -1.909  1.904   0.86 25.43 ?  159 ASN   A CA   1 
ATOM   3424 C CA   B ASN   A 1 159 ? 2.950  -1.768  1.535   0.14 21.98 ?  159 ASN   A CA   1 
ATOM   3425 C C    A ASN   A 1 159 ? 3.771  -2.988  1.311   0.86 24.24 ?  159 ASN   A C    1 
ATOM   3426 C C    B ASN   A 1 159 ? 3.811  -2.879  0.951   0.14 21.45 ?  159 ASN   A C    1 
ATOM   3427 O O    A ASN   A 1 159 ? 3.322  -4.116  1.061   0.86 23.22 ?  159 ASN   A O    1 
ATOM   3428 O O    B ASN   A 1 159 ? 3.278  -3.866  0.431   0.14 21.39 ?  159 ASN   A O    1 
ATOM   3429 C CB   A ASN   A 1 159 ? 2.409  -0.890  0.857   0.86 27.41 ?  159 ASN   A CB   1 
ATOM   3430 C CB   B ASN   A 1 159 ? 2.632  -0.732  0.449   0.14 22.69 ?  159 ASN   A CB   1 
ATOM   3431 C CG   A ASN   A 1 159 ? 1.194  -0.097  1.314   0.86 30.07 ?  159 ASN   A CG   1 
ATOM   3432 C CG   B ASN   A 1 159 ? 2.829  0.700   0.916   0.14 23.46 ?  159 ASN   A CG   1 
ATOM   3433 O OD1  A ASN   A 1 159 ? 0.329  -0.628  2.007   0.86 31.37 ?  159 ASN   A OD1  1 
ATOM   3434 O OD1  B ASN   A 1 159 ? 3.723  1.402   0.442   0.14 23.75 ?  159 ASN   A OD1  1 
ATOM   3435 N ND2  A ASN   A 1 159 ? 1.124  1.176   0.931   0.86 31.43 ?  159 ASN   A ND2  1 
ATOM   3436 N ND2  B ASN   A 1 159 ? 2.008  1.133   1.865   0.14 23.76 ?  159 ASN   A ND2  1 
ATOM   3437 H H    A ASN   A 1 159 ? 3.623  -0.372  2.911   0.86 30.51 ?  159 ASN   A H    1 
ATOM   3438 H H    B ASN   A 1 159 ? 3.850  -0.333  2.577   0.14 26.34 ?  159 ASN   A H    1 
ATOM   3439 H HA   A ASN   A 1 159 ? 2.081  -2.348  2.251   0.86 30.66 ?  159 ASN   A HA   1 
ATOM   3440 H HA   B ASN   A 1 159 ? 2.109  -2.171  1.817   0.14 26.52 ?  159 ASN   A HA   1 
ATOM   3441 H HB2  A ASN   A 1 159 ? 3.127  -0.261  0.685   0.86 33.03 ?  159 ASN   A HB2  1 
ATOM   3442 H HB2  B ASN   A 1 159 ? 3.215  -0.888  -0.310  0.14 27.38 ?  159 ASN   A HB2  1 
ATOM   3443 H HB3  A ASN   A 1 159 ? 2.172  -1.359  0.046   0.86 33.03 ?  159 ASN   A HB3  1 
ATOM   3444 H HB3  B ASN   A 1 159 ? 1.705  -0.833  0.184   0.14 27.38 ?  159 ASN   A HB3  1 
ATOM   3445 H HD21 A ASN   A 1 159 ? 0.455  1.662   1.169   0.86 37.86 ?  159 ASN   A HD21 1 
ATOM   3446 H HD21 B ASN   A 1 159 ? 2.088  1.933   2.168   0.14 28.66 ?  159 ASN   A HD21 1 
ATOM   3447 H HD22 A ASN   A 1 159 ? 1.751  1.513   0.451   0.86 37.86 ?  159 ASN   A HD22 1 
ATOM   3448 H HD22 B ASN   A 1 159 ? 1.394  0.615   2.174   0.14 28.66 ?  159 ASN   A HD22 1 
ATOM   3449 N N    A LEU   A 1 160 ? 5.055  -2.675  1.119   0.86 22.99 ?  160 LEU   A N    1 
ATOM   3450 N N    B LEU   A 1 160 ? 5.136  -2.737  1.024   0.14 20.78 ?  160 LEU   A N    1 
ATOM   3451 C CA   A LEU   A 1 160 ? 5.984  -3.672  0.595   0.86 21.80 ?  160 LEU   A CA   1 
ATOM   3452 C CA   B LEU   A 1 160 ? 6.028  -3.780  0.532   0.14 20.10 ?  160 LEU   A CA   1 
ATOM   3453 C C    A LEU   A 1 160 ? 6.176  -4.819  1.577   0.86 20.60 ?  160 LEU   A C    1 
ATOM   3454 C C    B LEU   A 1 160 ? 6.141  -4.931  1.525   0.14 19.55 ?  160 LEU   A C    1 
ATOM   3455 O O    A LEU   A 1 160 ? 6.204  -5.989  1.176   0.86 21.49 ?  160 LEU   A O    1 
ATOM   3456 O O    B LEU   A 1 160 ? 6.135  -6.102  1.127   0.14 19.66 ?  160 LEU   A O    1 
ATOM   3457 C CB   A LEU   A 1 160 ? 7.326  -3.025  0.256   0.86 21.65 ?  160 LEU   A CB   1 
ATOM   3458 C CB   B LEU   A 1 160 ? 7.409  -3.192  0.240   0.14 19.99 ?  160 LEU   A CB   1 
ATOM   3459 C CG   A LEU   A 1 160 ? 8.397  -4.021  -0.191  0.86 22.25 ?  160 LEU   A CG   1 
ATOM   3460 C CG   B LEU   A 1 160 ? 8.443  -4.209  -0.243  0.14 19.96 ?  160 LEU   A CG   1 
ATOM   3461 C CD1  A LEU   A 1 160 ? 7.932  -4.777  -1.416  0.86 23.00 ?  160 LEU   A CD1  1 
ATOM   3462 C CD1  B LEU   A 1 160 ? 7.953  -4.871  -1.518  0.14 20.00 ?  160 LEU   A CD1  1 
ATOM   3463 C CD2  A LEU   A 1 160 ? 9.709  -3.321  -0.469  0.86 22.20 ?  160 LEU   A CD2  1 
ATOM   3464 C CD2  B LEU   A 1 160 ? 9.799  -3.555  -0.454  0.14 19.89 ?  160 LEU   A CD2  1 
ATOM   3465 H H    A LEU   A 1 160 ? 5.413  -1.904  1.292   0.86 27.73 ?  160 LEU   A H    1 
ATOM   3466 H H    B LEU   A 1 160 ? 5.537  -2.048  1.346   0.14 25.09 ?  160 LEU   A H    1 
ATOM   3467 H HA   A LEU   A 1 160 ? 5.613  -4.035  -0.218  0.86 26.30 ?  160 LEU   A HA   1 
ATOM   3468 H HA   B LEU   A 1 160 ? 5.672  -4.131  -0.296  0.14 24.27 ?  160 LEU   A HA   1 
ATOM   3469 H HB2  A LEU   A 1 160 ? 7.194  -2.382  -0.463  0.86 26.13 ?  160 LEU   A HB2  1 
ATOM   3470 H HB2  B LEU   A 1 160 ? 7.322  -2.512  -0.450  0.14 24.13 ?  160 LEU   A HB2  1 
ATOM   3471 H HB3  A LEU   A 1 160 ? 7.661  -2.570  1.044   0.86 26.13 ?  160 LEU   A HB3  1 
ATOM   3472 H HB3  B LEU   A 1 160 ? 7.755  -2.789  1.051   0.14 24.13 ?  160 LEU   A HB3  1 
ATOM   3473 H HG   A LEU   A 1 160 ? 8.552  -4.663  0.518   0.86 26.85 ?  160 LEU   A HG   1 
ATOM   3474 H HG   B LEU   A 1 160 ? 8.551  -4.899  0.430   0.14 24.10 ?  160 LEU   A HG   1 
ATOM   3475 H HD11 A LEU   A 1 160 ? 8.666  -5.309  -1.751  0.86 27.75 ?  160 LEU   A HD11 1 
ATOM   3476 H HD11 B LEU   A 1 160 ? 8.670  -5.402  -1.890  0.14 24.15 ?  160 LEU   A HD11 1 
ATOM   3477 H HD12 A LEU   A 1 160 ? 7.191  -5.354  -1.170  0.86 27.75 ?  160 LEU   A HD12 1 
ATOM   3478 H HD12 B LEU   A 1 160 ? 7.195  -5.441  -1.307  0.14 24.15 ?  160 LEU   A HD12 1 
ATOM   3479 H HD13 A LEU   A 1 160 ? 7.646  -4.140  -2.089  0.86 27.75 ?  160 LEU   A HD13 1 
ATOM   3480 H HD13 B LEU   A 1 160 ? 7.685  -4.183  -2.147  0.14 24.15 ?  160 LEU   A HD13 1 
ATOM   3481 H HD21 A LEU   A 1 160 ? 10.366 -3.981  -0.746  0.86 26.79 ?  160 LEU   A HD21 1 
ATOM   3482 H HD21 B LEU   A 1 160 ? 10.430 -4.227  -0.756  0.14 24.02 ?  160 LEU   A HD21 1 
ATOM   3483 H HD22 A LEU   A 1 160 ? 9.578  -2.671  -1.177  0.86 26.79 ?  160 LEU   A HD22 1 
ATOM   3484 H HD22 B LEU   A 1 160 ? 9.712  -2.857  -1.121  0.14 24.02 ?  160 LEU   A HD22 1 
ATOM   3485 H HD23 A LEU   A 1 160 ? 10.009 -2.875  0.338   0.86 26.79 ?  160 LEU   A HD23 1 
ATOM   3486 H HD23 B LEU   A 1 160 ? 10.099 -3.175  0.387   0.14 24.02 ?  160 LEU   A HD23 1 
ATOM   3487 N N    A TYR   A 1 161 ? 6.314  -4.504  2.866   0.86 19.86 ?  161 TYR   A N    1 
ATOM   3488 N N    B TYR   A 1 161 ? 6.253  -4.616  2.817   0.14 19.12 ?  161 TYR   A N    1 
ATOM   3489 C CA   A TYR   A 1 161 ? 6.450  -5.552  3.871   0.86 19.46 ?  161 TYR   A CA   1 
ATOM   3490 C CA   B TYR   A 1 161 ? 6.348  -5.659  3.833   0.14 18.78 ?  161 TYR   A CA   1 
ATOM   3491 C C    A TYR   A 1 161 ? 5.309  -6.563  3.775   0.86 19.97 ?  161 TYR   A C    1 
ATOM   3492 C C    B TYR   A 1 161 ? 5.146  -6.596  3.778   0.14 18.93 ?  161 TYR   A C    1 
ATOM   3493 O O    A TYR   A 1 161 ? 5.538  -7.779  3.745   0.86 19.82 ?  161 TYR   A O    1 
ATOM   3494 O O    B TYR   A 1 161 ? 5.293  -7.815  3.927   0.14 18.77 ?  161 TYR   A O    1 
ATOM   3495 C CB   A TYR   A 1 161 ? 6.527  -4.934  5.269   0.86 19.98 ?  161 TYR   A CB   1 
ATOM   3496 C CB   B TYR   A 1 161 ? 6.473  -5.019  5.216   0.14 18.51 ?  161 TYR   A CB   1 
ATOM   3497 C CG   A TYR   A 1 161 ? 6.431  -5.968  6.354   0.86 19.42 ?  161 TYR   A CG   1 
ATOM   3498 C CG   B TYR   A 1 161 ? 6.336  -5.989  6.368   0.14 18.12 ?  161 TYR   A CG   1 
ATOM   3499 C CD1  A TYR   A 1 161 ? 7.559  -6.648  6.787   0.86 19.04 ?  161 TYR   A CD1  1 
ATOM   3500 C CD1  B TYR   A 1 161 ? 7.427  -6.721  6.820   0.14 18.00 ?  161 TYR   A CD1  1 
ATOM   3501 C CD2  A TYR   A 1 161 ? 5.207  -6.280  6.937   0.86 19.73 ?  161 TYR   A CD2  1 
ATOM   3502 C CD2  B TYR   A 1 161 ? 5.119  -6.159  7.018   0.14 17.99 ?  161 TYR   A CD2  1 
ATOM   3503 C CE1  A TYR   A 1 161 ? 7.476  -7.612  7.766   0.86 18.88 ?  161 TYR   A CE1  1 
ATOM   3504 C CE1  B TYR   A 1 161 ? 7.306  -7.605  7.877   0.14 17.95 ?  161 TYR   A CE1  1 
ATOM   3505 C CE2  A TYR   A 1 161 ? 5.114  -7.244  7.919   0.86 19.33 ?  161 TYR   A CE2  1 
ATOM   3506 C CE2  B TYR   A 1 161 ? 4.989  -7.040  8.075   0.14 17.98 ?  161 TYR   A CE2  1 
ATOM   3507 C CZ   A TYR   A 1 161 ? 6.252  -7.906  8.329   0.86 19.36 ?  161 TYR   A CZ   1 
ATOM   3508 C CZ   B TYR   A 1 161 ? 6.085  -7.760  8.501   0.14 18.10 ?  161 TYR   A CZ   1 
ATOM   3509 O OH   A TYR   A 1 161 ? 6.174  -8.867  9.308   0.86 20.17 ?  161 TYR   A OH   1 
ATOM   3510 O OH   B TYR   A 1 161 ? 5.958  -8.637  9.554   0.14 18.50 ?  161 TYR   A OH   1 
ATOM   3511 H H    A TYR   A 1 161 ? 6.321  -3.703  3.181   0.86 23.98 ?  161 TYR   A H    1 
ATOM   3512 H H    B TYR   A 1 161 ? 6.277  -3.816  3.123   0.14 23.09 ?  161 TYR   A H    1 
ATOM   3513 H HA   A TYR   A 1 161 ? 7.276  -6.028  3.718   0.86 23.49 ?  161 TYR   A HA   1 
ATOM   3514 H HA   B TYR   A 1 161 ? 7.147  -6.185  3.674   0.14 22.69 ?  161 TYR   A HA   1 
ATOM   3515 H HB2  A TYR   A 1 161 ? 7.379  -4.475  5.370   0.86 24.12 ?  161 TYR   A HB2  1 
ATOM   3516 H HB2  B TYR   A 1 161 ? 7.346  -4.599  5.287   0.14 22.36 ?  161 TYR   A HB2  1 
ATOM   3517 H HB3  A TYR   A 1 161 ? 5.798  -4.306  5.387   0.86 24.12 ?  161 TYR   A HB3  1 
ATOM   3518 H HB3  B TYR   A 1 161 ? 5.780  -4.347  5.313   0.14 22.36 ?  161 TYR   A HB3  1 
ATOM   3519 H HD1  A TYR   A 1 161 ? 8.384  -6.453  6.409   0.86 23.00 ?  161 TYR   A HD1  1 
ATOM   3520 H HD1  B TYR   A 1 161 ? 8.251  -6.619  6.402   0.14 21.75 ?  161 TYR   A HD1  1 
ATOM   3521 H HD2  A TYR   A 1 161 ? 4.435  -5.841  6.662   0.86 23.83 ?  161 TYR   A HD2  1 
ATOM   3522 H HD2  B TYR   A 1 161 ? 4.377  -5.675  6.734   0.14 21.74 ?  161 TYR   A HD2  1 
ATOM   3523 H HE1  A TYR   A 1 161 ? 8.242  -8.062  8.052   0.86 22.81 ?  161 TYR   A HE1  1 
ATOM   3524 H HE1  B TYR   A 1 161 ? 8.045  -8.092  8.167   0.14 21.68 ?  161 TYR   A HE1  1 
ATOM   3525 H HE2  A TYR   A 1 161 ? 4.284  -7.449  8.306   0.86 23.35 ?  161 TYR   A HE2  1 
ATOM   3526 H HE2  B TYR   A 1 161 ? 4.167  -7.146  8.498   0.14 21.73 ?  161 TYR   A HE2  1 
ATOM   3527 H HH   A TYR   A 1 161 ? 6.924  -9.200  9.470   0.86 24.35 ?  161 TYR   A HH   1 
ATOM   3528 H HH   B TYR   A 1 161 ? 5.171  -8.623  9.849   0.14 22.35 ?  161 TYR   A HH   1 
ATOM   3529 N N    A ASP   A 1 162 ? 4.066  -6.074  3.722   0.86 21.04 ?  162 ASP   A N    1 
ATOM   3530 N N    B ASP   A 1 162 ? 3.949  -6.045  3.564   0.14 19.33 ?  162 ASP   A N    1 
ATOM   3531 C CA   A ASP   A 1 162 ? 2.918  -6.982  3.658   0.86 21.59 ?  162 ASP   A CA   1 
ATOM   3532 C CA   B ASP   A 1 162 ? 2.751  -6.877  3.488   0.14 19.64 ?  162 ASP   A CA   1 
ATOM   3533 C C    A ASP   A 1 162 ? 2.962  -7.828  2.391   0.86 21.61 ?  162 ASP   A C    1 
ATOM   3534 C C    B ASP   A 1 162 ? 2.826  -7.836  2.306   0.14 20.13 ?  162 ASP   A C    1 
ATOM   3535 O O    A ASP   A 1 162 ? 2.603  -9.013  2.411   0.86 22.41 ?  162 ASP   A O    1 
ATOM   3536 O O    B ASP   A 1 162 ? 2.548  -9.033  2.443   0.14 20.23 ?  162 ASP   A O    1 
ATOM   3537 C CB   A ASP   A 1 162 ? 1.599  -6.201  3.733   0.86 22.25 ?  162 ASP   A CB   1 
ATOM   3538 C CB   B ASP   A 1 162 ? 1.505  -5.995  3.378   0.14 19.63 ?  162 ASP   A CB   1 
ATOM   3539 C CG   A ASP   A 1 162 ? 1.314  -5.632  5.107   0.86 23.75 ?  162 ASP   A CG   1 
ATOM   3540 C CG   B ASP   A 1 162 ? 1.303  -5.109  4.593   0.14 19.65 ?  162 ASP   A CG   1 
ATOM   3541 O OD1  A ASP   A 1 162 ? 1.971  -6.049  6.082   0.86 25.01 ?  162 ASP   A OD1  1 
ATOM   3542 O OD1  B ASP   A 1 162 ? 1.806  -5.460  5.681   0.14 19.71 ?  162 ASP   A OD1  1 
ATOM   3543 O OD2  A ASP   A 1 162 ? 0.408  -4.768  5.205   0.86 25.06 -1 162 ASP   A OD2  1 
ATOM   3544 O OD2  B ASP   A 1 162 ? 0.632  -4.064  4.462   0.14 19.67 -1 162 ASP   A OD2  1 
ATOM   3545 H H    A ASP   A 1 162 ? 3.860  -5.239  3.724   0.86 25.40 ?  162 ASP   A H    1 
ATOM   3546 H H    B ASP   A 1 162 ? 3.807  -5.204  3.466   0.14 23.35 ?  162 ASP   A H    1 
ATOM   3547 H HA   A ASP   A 1 162 ? 2.951  -7.589  4.412   0.86 26.06 ?  162 ASP   A HA   1 
ATOM   3548 H HA   B ASP   A 1 162 ? 2.677  -7.402  4.299   0.14 23.71 ?  162 ASP   A HA   1 
ATOM   3549 H HB2  A ASP   A 1 162 ? 1.632  -5.461  3.119   0.86 26.85 ?  162 ASP   A HB2  1 
ATOM   3550 H HB2  B ASP   A 1 162 ? 1.591  -5.423  2.600   0.14 23.70 ?  162 ASP   A HB2  1 
ATOM   3551 H HB3  A ASP   A 1 162 ? 0.867  -6.796  3.516   0.86 26.85 ?  162 ASP   A HB3  1 
ATOM   3552 H HB3  B ASP   A 1 162 ? 0.725  -6.565  3.284   0.14 23.70 ?  162 ASP   A HB3  1 
ATOM   3553 N N    A LYS   A 1 163 ? 3.409  -7.239  1.278   0.86 22.90 ?  163 LYS   A N    1 
ATOM   3554 N N    B LYS   A 1 163 ? 3.190  -7.323  1.129   0.14 20.74 ?  163 LYS   A N    1 
ATOM   3555 C CA   A LYS   A 1 163 ? 3.495  -7.996  0.033   0.86 23.39 ?  163 LYS   A CA   1 
ATOM   3556 C CA   B LYS   A 1 163 ? 3.301  -8.186  -0.042  0.14 21.13 ?  163 LYS   A CA   1 
ATOM   3557 C C    A LYS   A 1 163 ? 4.577  -9.067  0.107   0.86 22.47 ?  163 LYS   A C    1 
ATOM   3558 C C    B LYS   A 1 163 ? 4.403  -9.221  0.146   0.14 20.65 ?  163 LYS   A C    1 
ATOM   3559 O O    A LYS   A 1 163 ? 4.403  -10.169 -0.422  0.86 22.97 ?  163 LYS   A O    1 
ATOM   3560 O O    B LYS   A 1 163 ? 4.238  -10.390 -0.222  0.14 20.82 ?  163 LYS   A O    1 
ATOM   3561 C CB   A LYS   A 1 163 ? 3.750  -7.053  -1.144  0.86 26.42 ?  163 LYS   A CB   1 
ATOM   3562 C CB   B LYS   A 1 163 ? 3.550  -7.340  -1.292  0.14 22.07 ?  163 LYS   A CB   1 
ATOM   3563 C CG   A LYS   A 1 163 ? 3.793  -7.761  -2.488  0.86 29.35 ?  163 LYS   A CG   1 
ATOM   3564 C CG   B LYS   A 1 163 ? 3.735  -8.151  -2.567  0.14 22.93 ?  163 LYS   A CG   1 
ATOM   3565 C CD   A LYS   A 1 163 ? 4.165  -6.812  -3.611  0.86 32.65 ?  163 LYS   A CD   1 
ATOM   3566 C CD   B LYS   A 1 163 ? 4.847  -7.581  -3.429  0.14 23.68 ?  163 LYS   A CD   1 
ATOM   3567 C CE   A LYS   A 1 163 ? 4.043  -7.492  -4.966  0.86 34.94 ?  163 LYS   A CE   1 
ATOM   3568 C CE   B LYS   A 1 163 ? 4.515  -6.185  -3.928  0.14 24.27 ?  163 LYS   A CE   1 
ATOM   3569 N NZ   A LYS   A 1 163 ? 4.673  -6.693  -6.054  0.86 36.07 ?  163 LYS   A NZ   1 
ATOM   3570 N NZ   B LYS   A 1 163 ? 5.637  -5.601  -4.712  0.14 24.61 ?  163 LYS   A NZ   1 
ATOM   3571 H H    A LYS   A 1 163 ? 3.661  -6.412  1.221   0.86 27.63 ?  163 LYS   A H    1 
ATOM   3572 H H    B LYS   A 1 163 ? 3.379  -6.497  0.986   0.14 25.03 ?  163 LYS   A H    1 
ATOM   3573 H HA   A LYS   A 1 163 ? 2.645  -8.433  -0.119  0.86 28.21 ?  163 LYS   A HA   1 
ATOM   3574 H HA   B LYS   A 1 163 ? 2.464  -8.657  -0.169  0.14 25.51 ?  163 LYS   A HA   1 
ATOM   3575 H HB2  A LYS   A 1 163 ? 3.037  -6.393  -1.182  0.86 31.85 ?  163 LYS   A HB2  1 
ATOM   3576 H HB2  B LYS   A 1 163 ? 2.786  -6.750  -1.430  0.14 26.64 ?  163 LYS   A HB2  1 
ATOM   3577 H HB3  A LYS   A 1 163 ? 4.601  -6.609  -1.015  0.86 31.85 ?  163 LYS   A HB3  1 
ATOM   3578 H HB3  B LYS   A 1 163 ? 4.349  -6.807  -1.160  0.14 26.64 ?  163 LYS   A HB3  1 
ATOM   3579 H HG2  A LYS   A 1 163 ? 4.459  -8.467  -2.459  0.86 35.37 ?  163 LYS   A HG2  1 
ATOM   3580 H HG2  B LYS   A 1 163 ? 3.957  -9.071  -2.353  0.14 27.67 ?  163 LYS   A HG2  1 
ATOM   3581 H HG3  A LYS   A 1 163 ? 2.918  -8.135  -2.680  0.86 35.37 ?  163 LYS   A HG3  1 
ATOM   3582 H HG3  B LYS   A 1 163 ? 2.914  -8.122  -3.079  0.14 27.67 ?  163 LYS   A HG3  1 
ATOM   3583 H HD2  A LYS   A 1 163 ? 3.565  -6.049  -3.599  0.86 39.32 ?  163 LYS   A HD2  1 
ATOM   3584 H HD2  B LYS   A 1 163 ? 5.665  -7.533  -2.908  0.14 28.56 ?  163 LYS   A HD2  1 
ATOM   3585 H HD3  A LYS   A 1 163 ? 5.083  -6.520  -3.496  0.86 39.32 ?  163 LYS   A HD3  1 
ATOM   3586 H HD3  B LYS   A 1 163 ? 4.972  -8.156  -4.198  0.14 28.56 ?  163 LYS   A HD3  1 
ATOM   3587 H HE2  A LYS   A 1 163 ? 4.471  -8.361  -4.930  0.86 42.08 ?  163 LYS   A HE2  1 
ATOM   3588 H HE2  B LYS   A 1 163 ? 3.733  -6.230  -4.501  0.14 29.27 ?  163 LYS   A HE2  1 
ATOM   3589 H HE3  A LYS   A 1 163 ? 3.105  -7.598  -5.180  0.86 42.08 ?  163 LYS   A HE3  1 
ATOM   3590 H HE3  B LYS   A 1 163 ? 4.342  -5.603  -3.171  0.14 29.27 ?  163 LYS   A HE3  1 
ATOM   3591 H HZ1  A LYS   A 1 163 ? 4.587  -7.117  -6.832  0.86 43.43 ?  163 LYS   A HZ1  1 
ATOM   3592 H HZ1  B LYS   A 1 163 ? 5.419  -4.786  -4.994  0.14 29.68 ?  163 LYS   A HZ1  1 
ATOM   3593 H HZ2  A LYS   A 1 163 ? 4.278  -5.897  -6.113  0.86 43.43 ?  163 LYS   A HZ2  1 
ATOM   3594 H HZ2  B LYS   A 1 163 ? 6.366  -5.548  -4.205  0.14 29.68 ?  163 LYS   A HZ2  1 
ATOM   3595 H HZ3  A LYS   A 1 163 ? 5.538  -6.575  -5.884  0.86 43.43 ?  163 LYS   A HZ3  1 
ATOM   3596 H HZ3  B LYS   A 1 163 ? 5.813  -6.114  -5.418  0.14 29.68 ?  163 LYS   A HZ3  1 
ATOM   3597 N N    A LEU   A 1 164 ? 5.710  -8.755  0.743   0.86 20.59 ?  164 LEU   A N    1 
ATOM   3598 N N    B LEU   A 1 164 ? 5.536  -8.811  0.721   0.14 19.93 ?  164 LEU   A N    1 
ATOM   3599 C CA   A LEU   A 1 164 ? 6.791  -9.732  0.869   0.86 19.47 ?  164 LEU   A CA   1 
ATOM   3600 C CA   B LEU   A 1 164 ? 6.624  -9.751  0.971   0.14 19.35 ?  164 LEU   A CA   1 
ATOM   3601 C C    A LEU   A 1 164 ? 6.364  -10.921 1.717   0.86 19.47 ?  164 LEU   A C    1 
ATOM   3602 C C    B LEU   A 1 164 ? 6.171  -10.879 1.888   0.14 19.21 ?  164 LEU   A C    1 
ATOM   3603 O O    A LEU   A 1 164 ? 6.679  -12.071 1.392   0.86 19.87 ?  164 LEU   A O    1 
ATOM   3604 O O    B LEU   A 1 164 ? 6.448  -12.055 1.630   0.14 19.27 ?  164 LEU   A O    1 
ATOM   3605 C CB   A LEU   A 1 164 ? 8.013  -9.065  1.496   0.86 18.73 ?  164 LEU   A CB   1 
ATOM   3606 C CB   B LEU   A 1 164 ? 7.815  -9.016  1.588   0.14 18.93 ?  164 LEU   A CB   1 
ATOM   3607 C CG   A LEU   A 1 164 ? 8.770  -8.061  0.623   0.86 19.03 ?  164 LEU   A CG   1 
ATOM   3608 C CG   B LEU   A 1 164 ? 8.622  -8.086  0.680   0.14 18.78 ?  164 LEU   A CG   1 
ATOM   3609 C CD1  A LEU   A 1 164 ? 9.689  -7.188  1.466   0.86 18.97 ?  164 LEU   A CD1  1 
ATOM   3610 C CD1  B LEU   A 1 164 ? 9.669  -7.340  1.491   0.14 18.79 ?  164 LEU   A CD1  1 
ATOM   3611 C CD2  A LEU   A 1 164 ? 9.559  -8.776  -0.457  0.86 19.20 ?  164 LEU   A CD2  1 
ATOM   3612 C CD2  B LEU   A 1 164 ? 9.274  -8.864  -0.451  0.14 18.62 ?  164 LEU   A CD2  1 
ATOM   3613 H H    A LEU   A 1 164 ? 5.880  -7.990  1.103   0.86 24.85 ?  164 LEU   A H    1 
ATOM   3614 H H    B LEU   A 1 164 ? 5.693  -8.005  0.972   0.14 24.07 ?  164 LEU   A H    1 
ATOM   3615 H HA   A LEU   A 1 164 ? 7.037  -10.057 -0.007  0.86 23.51 ?  164 LEU   A HA   1 
ATOM   3616 H HA   B LEU   A 1 164 ? 6.907  -10.142 0.131   0.14 23.37 ?  164 LEU   A HA   1 
ATOM   3617 H HB2  A LEU   A 1 164 ? 7.728  -8.592  2.292   0.86 22.62 ?  164 LEU   A HB2  1 
ATOM   3618 H HB2  B LEU   A 1 164 ? 7.485  -8.478  2.324   0.14 22.87 ?  164 LEU   A HB2  1 
ATOM   3619 H HB3  A LEU   A 1 164 ? 8.644  -9.759  1.744   0.86 22.62 ?  164 LEU   A HB3  1 
ATOM   3620 H HB3  B LEU   A 1 164 ? 8.430  -9.682  1.931   0.14 22.87 ?  164 LEU   A HB3  1 
ATOM   3621 H HG   A LEU   A 1 164 ? 8.131  -7.478  0.189   0.86 22.98 ?  164 LEU   A HG   1 
ATOM   3622 H HG   B LEU   A 1 164 ? 8.026  -7.431  0.287   0.14 22.69 ?  164 LEU   A HG   1 
ATOM   3623 H HD11 A LEU   A 1 164 ? 10.159 -6.567  0.888   0.86 22.92 ?  164 LEU   A HD11 1 
ATOM   3624 H HD11 B LEU   A 1 164 ? 10.169 -6.756  0.900   0.14 22.70 ?  164 LEU   A HD11 1 
ATOM   3625 H HD12 A LEU   A 1 164 ? 9.158  -6.698  2.114   0.86 22.92 ?  164 LEU   A HD12 1 
ATOM   3626 H HD12 B LEU   A 1 164 ? 9.223  -6.816  2.175   0.14 22.70 ?  164 LEU   A HD12 1 
ATOM   3627 H HD13 A LEU   A 1 164 ? 10.330 -7.754  1.929   0.86 22.92 ?  164 LEU   A HD13 1 
ATOM   3628 H HD13 B LEU   A 1 164 ? 10.266 -7.984  1.905   0.14 22.70 ?  164 LEU   A HD13 1 
ATOM   3629 H HD21 A LEU   A 1 164 ? 10.052 -8.117  -0.975  0.86 23.19 ?  164 LEU   A HD21 1 
ATOM   3630 H HD21 B LEU   A 1 164 ? 9.878  -8.276  -0.931  0.14 22.49 ?  164 LEU   A HD21 1 
ATOM   3631 H HD22 A LEU   A 1 164 ? 10.176 -9.397  -0.041  0.86 23.19 ?  164 LEU   A HD22 1 
ATOM   3632 H HD22 B LEU   A 1 164 ? 9.767  -9.611  -0.077  0.14 22.49 ?  164 LEU   A HD22 1 
ATOM   3633 H HD23 A LEU   A 1 164 ? 8.943  -9.253  -1.033  0.86 23.19 ?  164 LEU   A HD23 1 
ATOM   3634 H HD23 B LEU   A 1 164 ? 8.584  -9.189  -1.050  0.14 22.49 ?  164 LEU   A HD23 1 
ATOM   3635 N N    A VAL   A 1 165 ? 5.681  -10.657 2.831   0.86 19.00 ?  165 VAL   A N    1 
ATOM   3636 N N    B VAL   A 1 165 ? 5.473  -10.536 2.974   0.14 19.10 ?  165 VAL   A N    1 
ATOM   3637 C CA   A VAL   A 1 165 ? 5.205  -11.732 3.696   0.86 18.86 ?  165 VAL   A CA   1 
ATOM   3638 C CA   B VAL   A 1 165 ? 5.041  -11.551 3.928   0.14 18.96 ?  165 VAL   A CA   1 
ATOM   3639 C C    A VAL   A 1 165 ? 4.159  -12.573 2.974   0.86 19.14 ?  165 VAL   A C    1 
ATOM   3640 C C    B VAL   A 1 165 ? 3.842  -12.346 3.423   0.14 18.88 ?  165 VAL   A C    1 
ATOM   3641 O O    A VAL   A 1 165 ? 4.256  -13.804 2.925   0.86 18.65 ?  165 VAL   A O    1 
ATOM   3642 O O    B VAL   A 1 165 ? 3.600  -13.456 3.912   0.14 19.39 ?  165 VAL   A O    1 
ATOM   3643 C CB   A VAL   A 1 165 ? 4.649  -11.145 5.007   0.86 18.88 ?  165 VAL   A CB   1 
ATOM   3644 C CB   B VAL   A 1 165 ? 4.764  -10.926 5.308   0.14 18.92 ?  165 VAL   A CB   1 
ATOM   3645 C CG1  A VAL   A 1 165 ? 3.890  -12.207 5.807   0.86 19.29 ?  165 VAL   A CG1  1 
ATOM   3646 C CG1  B VAL   A 1 165 ? 3.470  -10.127 5.293   0.14 18.96 ?  165 VAL   A CG1  1 
ATOM   3647 C CG2  A VAL   A 1 165 ? 5.770  -10.517 5.836   0.86 19.19 ?  165 VAL   A CG2  1 
ATOM   3648 C CG2  B VAL   A 1 165 ? 4.721  -11.997 6.388   0.14 18.99 ?  165 VAL   A CG2  1 
ATOM   3649 H H    A VAL   A 1 165 ? 5.480  -9.871  3.108   0.86 22.95 ?  165 VAL   A H    1 
ATOM   3650 H H    B VAL   A 1 165 ? 5.244  -9.733  3.179   0.14 23.07 ?  165 VAL   A H    1 
ATOM   3651 H HA   A VAL   A 1 165 ? 5.947  -12.312 3.928   0.86 22.78 ?  165 VAL   A HA   1 
ATOM   3652 H HA   B VAL   A 1 165 ? 5.766  -12.180 4.043   0.14 22.89 ?  165 VAL   A HA   1 
ATOM   3653 H HB   A VAL   A 1 165 ? 4.016  -10.442 4.790   0.86 22.81 ?  165 VAL   A HB   1 
ATOM   3654 H HB   B VAL   A 1 165 ? 5.486  -10.315 5.526   0.14 22.85 ?  165 VAL   A HB   1 
ATOM   3655 H HG11 A VAL   A 1 165 ? 3.795  -11.902 6.724   0.86 23.30 ?  165 VAL   A HG11 1 
ATOM   3656 H HG11 B VAL   A 1 165 ? 3.389  -9.644  6.130   0.14 22.90 ?  165 VAL   A HG11 1 
ATOM   3657 H HG12 A VAL   A 1 165 ? 3.011  -12.333 5.413   0.86 23.30 ?  165 VAL   A HG12 1 
ATOM   3658 H HG12 B VAL   A 1 165 ? 3.498  -9.503  4.554   0.14 22.90 ?  165 VAL   A HG12 1 
ATOM   3659 H HG13 A VAL   A 1 165 ? 4.389  -13.035 5.784   0.86 23.30 ?  165 VAL   A HG13 1 
ATOM   3660 H HG13 B VAL   A 1 165 ? 2.719  -10.733 5.190   0.14 22.90 ?  165 VAL   A HG13 1 
ATOM   3661 H HG21 A VAL   A 1 165 ? 5.397  -10.156 6.657   0.86 23.17 ?  165 VAL   A HG21 1 
ATOM   3662 H HG21 B VAL   A 1 165 ? 4.634  -11.568 7.255   0.14 22.94 ?  165 VAL   A HG21 1 
ATOM   3663 H HG22 A VAL   A 1 165 ? 6.431  -11.194 6.041   0.86 23.17 ?  165 VAL   A HG22 1 
ATOM   3664 H HG22 B VAL   A 1 165 ? 3.960  -12.575 6.229   0.14 22.94 ?  165 VAL   A HG22 1 
ATOM   3665 H HG23 A VAL   A 1 165 ? 6.177  -9.801  5.320   0.86 23.17 ?  165 VAL   A HG23 1 
ATOM   3666 H HG23 B VAL   A 1 165 ? 5.542  -12.511 6.355   0.14 22.94 ?  165 VAL   A HG23 1 
ATOM   3667 N N    A SER   A 1 166 ? 3.144  -11.919 2.405   0.86 20.33 ?  166 SER   A N    1 
ATOM   3668 N N    B SER   A 1 166 ? 3.090  -11.819 2.453   0.14 18.31 ?  166 SER   A N    1 
ATOM   3669 C CA   A SER   A 1 166 ? 2.017  -12.644 1.828   0.86 21.41 ?  166 SER   A CA   1 
ATOM   3670 C CA   B SER   A 1 166 ? 1.881  -12.509 2.011   0.14 17.73 ?  166 SER   A CA   1 
ATOM   3671 C C    A SER   A 1 166 ? 2.417  -13.459 0.611   0.86 21.76 ?  166 SER   A C    1 
ATOM   3672 C C    B SER   A 1 166 ? 2.182  -13.574 0.959   0.14 18.50 ?  166 SER   A C    1 
ATOM   3673 O O    A SER   A 1 166 ? 1.732  -14.435 0.281   0.86 23.54 ?  166 SER   A O    1 
ATOM   3674 O O    B SER   A 1 166 ? 1.790  -14.735 1.117   0.14 18.33 ?  166 SER   A O    1 
ATOM   3675 C CB   A SER   A 1 166 ? 0.899  -11.674 1.436   0.86 23.44 ?  166 SER   A CB   1 
ATOM   3676 C CB   B SER   A 1 166 ? 0.837  -11.505 1.510   0.14 16.62 ?  166 SER   A CB   1 
ATOM   3677 O OG   A SER   A 1 166 ? 0.306  -11.073 2.574   0.86 25.15 ?  166 SER   A OG   1 
ATOM   3678 O OG   B SER   A 1 166 ? 1.207  -10.957 0.260   0.14 15.44 ?  166 SER   A OG   1 
ATOM   3679 H H    A SER   A 1 166 ? 3.087  -11.068 2.344   0.86 24.54 ?  166 SER   A H    1 
ATOM   3680 H H    B SER   A 1 166 ? 3.250  -11.075 2.052   0.14 22.12 ?  166 SER   A H    1 
ATOM   3681 H HA   A SER   A 1 166 ? 1.655  -13.255 2.492   0.86 25.84 ?  166 SER   A HA   1 
ATOM   3682 H HA   B SER   A 1 166 ? 1.495  -12.959 2.769   0.14 21.43 ?  166 SER   A HA   1 
ATOM   3683 H HB2  A SER   A 1 166 ? 1.266  -10.989 0.855   0.86 28.27 ?  166 SER   A HB2  1 
ATOM   3684 H HB2  B SER   A 1 166 ? -0.017 -11.959 1.410   0.14 20.09 ?  166 SER   A HB2  1 
ATOM   3685 H HB3  A SER   A 1 166 ? 0.201  -12.160 0.974   0.86 28.27 ?  166 SER   A HB3  1 
ATOM   3686 H HB3  B SER   A 1 166 ? 0.747  -10.788 2.162   0.14 20.09 ?  166 SER   A HB3  1 
ATOM   3687 H HG   A SER   A 1 166 ? -0.276 -10.513 2.336   0.86 30.33 ?  166 SER   A HG   1 
ATOM   3688 H HG   B SER   A 1 166 ? 1.977  -10.628 0.306   0.14 18.67 ?  166 SER   A HG   1 
ATOM   3689 N N    A SER   A 1 167 ? 3.500  -13.083 -0.065  0.86 20.89 ?  167 SER   A N    1 
ATOM   3690 N N    B SER   A 1 167 ? 2.887  -13.208 -0.112  0.14 19.58 ?  167 SER   A N    1 
ATOM   3691 C CA   A SER   A 1 167 ? 3.950  -13.801 -1.246  0.86 21.08 ?  167 SER   A CA   1 
ATOM   3692 C CA   B SER   A 1 167 ? 3.121  -14.110 -1.241  0.14 20.58 ?  167 SER   A CA   1 
ATOM   3693 C C    A SER   A 1 167 ? 5.109  -14.747 -0.959  0.86 20.83 ?  167 SER   A C    1 
ATOM   3694 C C    B SER   A 1 167 ? 4.537  -14.672 -1.251  0.14 21.27 ?  167 SER   A C    1 
ATOM   3695 O O    A SER   A 1 167 ? 5.614  -15.381 -1.891  0.86 22.10 ?  167 SER   A O    1 
ATOM   3696 O O    B SER   A 1 167 ? 5.162  -14.786 -2.309  0.14 21.36 ?  167 SER   A O    1 
ATOM   3697 C CB   A SER   A 1 167 ? 4.343  -12.819 -2.358  0.86 21.95 ?  167 SER   A CB   1 
ATOM   3698 C CB   B SER   A 1 167 ? 2.792  -13.424 -2.565  0.14 20.94 ?  167 SER   A CB   1 
ATOM   3699 O OG   A SER   A 1 167 ? 5.401  -11.965 -1.947  0.86 22.29 ?  167 SER   A OG   1 
ATOM   3700 O OG   B SER   A 1 167 ? 1.405  -13.145 -2.663  0.14 21.22 ?  167 SER   A OG   1 
ATOM   3701 H H    A SER   A 1 167 ? 3.988  -12.400 0.144   0.86 25.22 ?  167 SER   A H    1 
ATOM   3702 H H    B SER   A 1 167 ? 3.260  -12.441 -0.202  0.14 23.65 ?  167 SER   A H    1 
ATOM   3703 H HA   A SER   A 1 167 ? 3.213  -14.330 -1.578  0.86 25.45 ?  167 SER   A HA   1 
ATOM   3704 H HA   B SER   A 1 167 ? 2.517  -14.860 -1.158  0.14 24.85 ?  167 SER   A HA   1 
ATOM   3705 H HB2  A SER   A 1 167 ? 4.635  -13.326 -3.131  0.86 26.49 ?  167 SER   A HB2  1 
ATOM   3706 H HB2  B SER   A 1 167 ? 3.285  -12.593 -2.626  0.14 25.28 ?  167 SER   A HB2  1 
ATOM   3707 H HB3  A SER   A 1 167 ? 3.566  -12.284 -2.593  0.86 26.49 ?  167 SER   A HB3  1 
ATOM   3708 H HB3  B SER   A 1 167 ? 3.042  -14.013 -3.296  0.14 25.28 ?  167 SER   A HB3  1 
ATOM   3709 H HG   A SER   A 1 167 ? 5.150  -11.503 -1.286  0.86 26.90 ?  167 SER   A HG   1 
ATOM   3710 H HG   B SER   A 1 167 ? 1.238  -12.769 -3.396  0.14 25.61 ?  167 SER   A HG   1 
ATOM   3711 N N    A PHE   A 1 168 ? 5.542  -14.864 0.297   0.86 20.28 ?  168 PHE   A N    1 
ATOM   3712 N N    B PHE   A 1 168 ? 5.061  -15.041 -0.086  0.14 22.00 ?  168 PHE   A N    1 
ATOM   3713 C CA   A PHE   A 1 168 ? 6.724  -15.664 0.597   0.86 20.66 ?  168 PHE   A CA   1 
ATOM   3714 C CA   B PHE   A 1 168 ? 6.372  -15.669 -0.006  0.14 22.69 ?  168 PHE   A CA   1 
ATOM   3715 C C    A PHE   A 1 168 ? 6.412  -17.149 0.497   0.86 22.38 ?  168 PHE   A C    1 
ATOM   3716 C C    B PHE   A 1 168 ? 6.252  -17.165 -0.260  0.14 24.07 ?  168 PHE   A C    1 
ATOM   3717 O O    A PHE   A 1 168 ? 5.458  -17.642 1.107   0.86 23.99 ?  168 PHE   A O    1 
ATOM   3718 O O    B PHE   A 1 168 ? 5.334  -17.823 0.238   0.14 24.08 ?  168 PHE   A O    1 
ATOM   3719 C CB   A PHE   A 1 168 ? 7.255  -15.365 1.996   0.86 19.07 ?  168 PHE   A CB   1 
ATOM   3720 C CB   B PHE   A 1 168 ? 6.988  -15.429 1.373   0.14 22.02 ?  168 PHE   A CB   1 
ATOM   3721 C CG   A PHE   A 1 168 ? 8.523  -16.110 2.314   0.86 17.94 ?  168 PHE   A CG   1 
ATOM   3722 C CG   B PHE   A 1 168 ? 8.275  -16.174 1.603   0.14 21.40 ?  168 PHE   A CG   1 
ATOM   3723 C CD1  A PHE   A 1 168 ? 9.714  -15.734 1.720   0.86 18.22 ?  168 PHE   A CD1  1 
ATOM   3724 C CD1  B PHE   A 1 168 ? 9.423  -15.837 0.904   0.14 21.12 ?  168 PHE   A CD1  1 
ATOM   3725 C CD2  A PHE   A 1 168 ? 8.529  -17.203 3.170   0.86 17.27 ?  168 PHE   A CD2  1 
ATOM   3726 C CD2  B PHE   A 1 168 ? 8.339  -17.205 2.526   0.14 21.12 ?  168 PHE   A CD2  1 
ATOM   3727 C CE1  A PHE   A 1 168 ? 10.887 -16.409 1.987   0.86 17.58 ?  168 PHE   A CE1  1 
ATOM   3728 C CE1  B PHE   A 1 168 ? 10.607 -16.519 1.117   0.14 20.93 ?  168 PHE   A CE1  1 
ATOM   3729 C CE2  A PHE   A 1 168 ? 9.713  -17.882 3.442   0.86 17.31 ?  168 PHE   A CE2  1 
ATOM   3730 C CE2  B PHE   A 1 168 ? 9.521  -17.890 2.743   0.14 20.90 ?  168 PHE   A CE2  1 
ATOM   3731 C CZ   A PHE   A 1 168 ? 10.887 -17.482 2.846   0.86 17.49 ?  168 PHE   A CZ   1 
ATOM   3732 C CZ   B PHE   A 1 168 ? 10.656 -17.545 2.038   0.14 20.88 ?  168 PHE   A CZ   1 
ATOM   3733 H H    A PHE   A 1 168 ? 5.179  -14.489 0.982   0.86 24.49 ?  168 PHE   A H    1 
ATOM   3734 H H    B PHE   A 1 168 ? 4.673  -14.932 0.673   0.14 26.54 ?  168 PHE   A H    1 
ATOM   3735 H HA   A PHE   A 1 168 ? 7.422  -15.454 -0.045  0.86 24.94 ?  168 PHE   A HA   1 
ATOM   3736 H HA   B PHE   A 1 168 ? 6.956  -15.286 -0.677  0.14 27.38 ?  168 PHE   A HA   1 
ATOM   3737 H HB2  A PHE   A 1 168 ? 7.444  -14.415 2.065   0.86 23.04 ?  168 PHE   A HB2  1 
ATOM   3738 H HB2  B PHE   A 1 168 ? 7.173  -14.482 1.472   0.14 26.58 ?  168 PHE   A HB2  1 
ATOM   3739 H HB3  A PHE   A 1 168 ? 6.588  -15.619 2.649   0.86 23.04 ?  168 PHE   A HB3  1 
ATOM   3740 H HB3  B PHE   A 1 168 ? 6.356  -15.713 2.052   0.14 26.58 ?  168 PHE   A HB3  1 
ATOM   3741 H HD1  A PHE   A 1 168 ? 9.734  -15.007 1.142   0.86 22.02 ?  168 PHE   A HD1  1 
ATOM   3742 H HD1  B PHE   A 1 168 ? 9.396  -15.147 0.281   0.14 25.49 ?  168 PHE   A HD1  1 
ATOM   3743 H HD2  A PHE   A 1 168 ? 7.740  -17.475 3.575   0.86 20.87 ?  168 PHE   A HD2  1 
ATOM   3744 H HD2  B PHE   A 1 168 ? 7.577  -17.441 3.005   0.14 25.49 ?  168 PHE   A HD2  1 
ATOM   3745 H HE1  A PHE   A 1 168 ? 11.690 -16.141 1.589   0.86 21.24 ?  168 PHE   A HE1  1 
ATOM   3746 H HE1  B PHE   A 1 168 ? 11.371 -16.285 0.640   0.14 25.27 ?  168 PHE   A HE1  1 
ATOM   3747 H HE2  A PHE   A 1 168 ? 9.709  -18.612 4.021   0.86 20.92 ?  168 PHE   A HE2  1 
ATOM   3748 H HE2  B PHE   A 1 168 ? 9.551  -18.581 3.365   0.14 25.23 ?  168 PHE   A HE2  1 
ATOM   3749 H HZ   A PHE   A 1 168 ? 11.682 -17.939 3.027   0.86 21.14 ?  168 PHE   A HZ   1 
ATOM   3750 H HZ   B PHE   A 1 168 ? 11.452 -18.004 2.182   0.14 25.20 ?  168 PHE   A HZ   1 
ATOM   3751 N N    A LEU   A 1 169 ? 7.249  -17.867 -0.245  0.86 25.03 ?  169 LEU   A N    1 
ATOM   3752 N N    B LEU   A 1 169 ? 7.185  -17.699 -1.043  0.14 25.36 ?  169 LEU   A N    1 
ATOM   3753 C CA   A LEU   A 1 169 ? 7.068  -19.296 -0.408  0.86 29.82 ?  169 LEU   A CA   1 
ATOM   3754 C CA   B LEU   A 1 169 ? 7.185  -19.122 -1.367  0.14 26.60 ?  169 LEU   A CA   1 
ATOM   3755 C C    A LEU   A 1 169 ? 7.943  -20.036 0.589   0.86 31.29 ?  169 LEU   A C    1 
ATOM   3756 C C    B LEU   A 1 169 ? 8.544  -19.743 -1.070  0.14 26.86 ?  169 LEU   A C    1 
ATOM   3757 O O    A LEU   A 1 169 ? 7.455  -20.474 1.631   0.86 31.80 ?  169 LEU   A O    1 
ATOM   3758 O O    B LEU   A 1 169 ? 9.089  -19.595 0.024   0.14 26.86 ?  169 LEU   A O    1 
ATOM   3759 C CB   A LEU   A 1 169 ? 7.394  -19.719 -1.844  0.86 32.29 ?  169 LEU   A CB   1 
ATOM   3760 C CB   B LEU   A 1 169 ? 6.826  -19.342 -2.838  0.14 27.45 ?  169 LEU   A CB   1 
ATOM   3761 C CG   A LEU   A 1 169 ? 7.060  -21.168 -2.209  0.86 34.18 ?  169 LEU   A CG   1 
ATOM   3762 C CG   B LEU   A 1 169 ? 6.539  -20.795 -3.228  0.14 28.14 ?  169 LEU   A CG   1 
ATOM   3763 C CD1  A LEU   A 1 169 ? 5.645  -21.522 -1.778  0.86 34.88 ?  169 LEU   A CD1  1 
ATOM   3764 C CD1  B LEU   A 1 169 ? 5.180  -21.236 -2.697  0.14 28.40 ?  169 LEU   A CD1  1 
ATOM   3765 C CD2  A LEU   A 1 169 ? 7.234  -21.394 -3.704  0.86 34.75 ?  169 LEU   A CD2  1 
ATOM   3766 C CD2  B LEU   A 1 169 ? 6.625  -20.993 -4.735  0.14 28.35 ?  169 LEU   A CD2  1 
ATOM   3767 O OXT  A LEU   A 1 169 ? 9.147  -20.195 0.386   0.86 31.14 -1 169 LEU   A OXT  1 
ATOM   3768 O OXT  B LEU   A 1 169 ? 9.131  -20.411 -1.921  0.14 26.97 -1 169 LEU   A OXT  1 
ATOM   3769 H H    A LEU   A 1 169 ? 7.932  -17.547 -0.660  0.86 30.19 ?  169 LEU   A H    1 
ATOM   3770 H H    B LEU   A 1 169 ? 7.832  -17.256 -1.398  0.14 30.59 ?  169 LEU   A H    1 
ATOM   3771 H HA   A LEU   A 1 169 ? 6.148  -19.520 -0.218  0.86 35.93 ?  169 LEU   A HA   1 
ATOM   3772 H HA   B LEU   A 1 169 ? 6.523  -19.573 -0.823  0.14 32.06 ?  169 LEU   A HA   1 
ATOM   3773 H HB2  A LEU   A 1 169 ? 6.896  -19.148 -2.448  0.86 38.89 ?  169 LEU   A HB2  1 
ATOM   3774 H HB2  B LEU   A 1 169 ? 6.033  -18.824 -3.043  0.14 33.09 ?  169 LEU   A HB2  1 
ATOM   3775 H HB3  A LEU   A 1 169 ? 8.344  -19.597 -1.993  0.86 38.89 ?  169 LEU   A HB3  1 
ATOM   3776 H HB3  B LEU   A 1 169 ? 7.566  -19.036 -3.385  0.14 33.09 ?  169 LEU   A HB3  1 
ATOM   3777 H HG   A LEU   A 1 169 ? 7.672  -21.761 -1.745  0.86 41.16 ?  169 LEU   A HG   1 
ATOM   3778 H HG   B LEU   A 1 169 ? 7.208  -21.365 -2.822  0.14 33.92 ?  169 LEU   A HG   1 
ATOM   3779 H HD11 A LEU   A 1 169 ? 5.378  -22.343 -2.216  0.86 42.00 ?  169 LEU   A HD11 1 
ATOM   3780 H HD11 B LEU   A 1 169 ? 5.008  -22.145 -2.988  0.14 34.23 ?  169 LEU   A HD11 1 
ATOM   3781 H HD12 A LEU   A 1 169 ? 5.628  -21.641 -0.815  0.86 42.00 ?  169 LEU   A HD12 1 
ATOM   3782 H HD12 B LEU   A 1 169 ? 5.191  -21.195 -1.728  0.14 34.23 ?  169 LEU   A HD12 1 
ATOM   3783 H HD13 A LEU   A 1 169 ? 5.048  -20.801 -2.034  0.86 42.00 ?  169 LEU   A HD13 1 
ATOM   3784 H HD13 B LEU   A 1 169 ? 4.497  -20.643 -3.046  0.14 34.23 ?  169 LEU   A HD13 1 
ATOM   3785 H HD21 A LEU   A 1 169 ? 7.024  -22.319 -3.911  0.86 41.85 ?  169 LEU   A HD21 1 
ATOM   3786 H HD21 B LEU   A 1 169 ? 6.594  -21.943 -4.929  0.14 34.17 ?  169 LEU   A HD21 1 
ATOM   3787 H HD22 A LEU   A 1 169 ? 6.631  -20.804 -4.184  0.86 41.85 ?  169 LEU   A HD22 1 
ATOM   3788 H HD22 B LEU   A 1 169 ? 5.878  -20.545 -5.159  0.14 34.17 ?  169 LEU   A HD22 1 
ATOM   3789 H HD23 A LEU   A 1 169 ? 8.152  -21.200 -3.949  0.86 41.85 ?  169 LEU   A HD23 1 
ATOM   3790 H HD23 B LEU   A 1 169 ? 7.462  -20.620 -5.054  0.14 34.17 ?  169 LEU   A HD23 1 
ATOM   3791 N N    A SER   B 1 1   ? 50.819 -9.228  -23.797 0.86 29.98 ?  1   SER   B N    1 
ATOM   3792 N N    B SER   B 1 1   ? 50.842 -9.266  -23.809 0.14 29.06 ?  1   SER   B N    1 
ATOM   3793 C CA   A SER   B 1 1   ? 51.304 -10.279 -22.880 0.86 29.18 ?  1   SER   B CA   1 
ATOM   3794 C CA   B SER   B 1 1   ? 51.327 -10.256 -22.824 0.14 28.98 ?  1   SER   B CA   1 
ATOM   3795 C C    A SER   B 1 1   ? 50.231 -11.332 -22.631 0.86 27.65 ?  1   SER   B C    1 
ATOM   3796 C C    B SER   B 1 1   ? 50.278 -11.337 -22.612 0.14 28.69 ?  1   SER   B C    1 
ATOM   3797 O O    A SER   B 1 1   ? 49.035 -11.143 -22.917 0.86 26.93 ?  1   SER   B O    1 
ATOM   3798 O O    B SER   B 1 1   ? 49.129 -11.195 -23.032 0.14 28.57 ?  1   SER   B O    1 
ATOM   3799 C CB   A SER   B 1 1   ? 51.750 -9.681  -21.549 0.86 29.94 ?  1   SER   B CB   1 
ATOM   3800 C CB   B SER   B 1 1   ? 51.654 -9.577  -21.498 0.14 29.01 ?  1   SER   B CB   1 
ATOM   3801 O OG   A SER   B 1 1   ? 50.638 -9.446  -20.706 0.86 32.18 ?  1   SER   B OG   1 
ATOM   3802 O OG   B SER   B 1 1   ? 50.547 -9.629  -20.618 0.14 29.32 ?  1   SER   B OG   1 
ATOM   3803 H H1   A SER   B 1 1   ? 50.719 -9.574  -24.608 0.86 36.12 ?  1   SER   B H1   1 
ATOM   3804 H H1   B SER   B 1 1   ? 51.541 -8.860  -24.175 0.14 35.02 ?  1   SER   B H1   1 
ATOM   3805 H H2   A SER   B 1 1   ? 50.043 -8.921  -23.500 0.86 36.12 ?  1   SER   B H2   1 
ATOM   3806 H H2   B SER   B 1 1   ? 50.374 -9.686  -24.436 0.14 35.02 ?  1   SER   B H2   1 
ATOM   3807 H H3   A SER   B 1 1   ? 51.417 -8.572  -23.820 0.86 36.12 ?  1   SER   B H3   1 
ATOM   3808 H H3   B SER   B 1 1   ? 50.330 -8.673  -23.394 0.14 35.02 ?  1   SER   B H3   1 
ATOM   3809 H HA   A SER   B 1 1   ? 52.066 -10.709 -23.292 0.86 35.17 ?  1   SER   B HA   1 
ATOM   3810 H HA   B SER   B 1 1   ? 52.129 -10.666 -23.171 0.14 34.92 ?  1   SER   B HA   1 
ATOM   3811 H HB2  A SER   B 1 1   ? 52.344 -10.308 -21.112 0.86 36.07 ?  1   SER   B HB2  1 
ATOM   3812 H HB2  B SER   B 1 1   ? 52.410 -10.032 -21.098 0.14 34.95 ?  1   SER   B HB2  1 
ATOM   3813 H HB3  A SER   B 1 1   ? 52.210 -8.844  -21.716 0.86 36.07 ?  1   SER   B HB3  1 
ATOM   3814 H HB3  B SER   B 1 1   ? 51.876 -8.647  -21.665 0.14 34.95 ?  1   SER   B HB3  1 
ATOM   3815 H HG   A SER   B 1 1   ? 50.880 -8.990  -20.040 0.86 38.76 ?  1   SER   B HG   1 
ATOM   3816 H HG   B SER   B 1 1   ? 50.706 -9.166  -19.937 0.14 35.33 ?  1   SER   B HG   1 
ATOM   3817 N N    A MET   B 1 2   ? 50.688 -12.448 -22.081 0.86 27.19 ?  2   MET   B N    1 
ATOM   3818 N N    B MET   B 1 2   ? 50.684 -12.415 -21.949 0.14 28.46 ?  2   MET   B N    1 
ATOM   3819 C CA   A MET   B 1 2   ? 49.883 -13.648 -21.912 0.86 27.47 ?  2   MET   B CA   1 
ATOM   3820 C CA   B MET   B 1 2   ? 49.864 -13.612 -21.801 0.14 28.16 ?  2   MET   B CA   1 
ATOM   3821 C C    A MET   B 1 2   ? 49.646 -13.854 -20.421 0.86 25.63 ?  2   MET   B C    1 
ATOM   3822 C C    B MET   B 1 2   ? 49.599 -13.847 -20.321 0.14 26.35 ?  2   MET   B C    1 
ATOM   3823 O O    A MET   B 1 2   ? 50.585 -14.145 -19.672 0.86 26.05 ?  2   MET   B O    1 
ATOM   3824 O O    B MET   B 1 2   ? 50.492 -14.286 -19.587 0.14 26.58 ?  2   MET   B O    1 
ATOM   3825 C CB   A MET   B 1 2   ? 50.632 -14.829 -22.517 0.86 31.29 ?  2   MET   B CB   1 
ATOM   3826 C CB   B MET   B 1 2   ? 50.587 -14.801 -22.421 0.14 29.73 ?  2   MET   B CB   1 
ATOM   3827 C CG   A MET   B 1 2   ? 49.807 -16.091 -22.703 0.86 34.93 ?  2   MET   B CG   1 
ATOM   3828 C CG   B MET   B 1 2   ? 49.695 -15.981 -22.767 0.14 31.16 ?  2   MET   B CG   1 
ATOM   3829 S SD   A MET   B 1 2   ? 50.665 -17.282 -23.751 0.86 38.77 ?  2   MET   B SD   1 
ATOM   3830 S SD   B MET   B 1 2   ? 50.546 -17.143 -23.844 0.14 32.42 ?  2   MET   B SD   1 
ATOM   3831 C CE   A MET   B 1 2   ? 51.185 -16.206 -25.074 0.86 38.62 ?  2   MET   B CE   1 
ATOM   3832 C CE   B MET   B 1 2   ? 51.319 -16.002 -24.984 0.14 32.67 ?  2   MET   B CE   1 
ATOM   3833 H H    A MET   B 1 2   ? 51.492 -12.545 -21.788 0.86 32.78 ?  2   MET   B H    1 
ATOM   3834 H H    B MET   B 1 2   ? 51.455 -12.480 -21.574 0.14 34.29 ?  2   MET   B H    1 
ATOM   3835 H HA   A MET   B 1 2   ? 49.036 -13.556 -22.375 0.86 33.11 ?  2   MET   B HA   1 
ATOM   3836 H HA   B MET   B 1 2   ? 49.027 -13.498 -22.274 0.14 33.94 ?  2   MET   B HA   1 
ATOM   3837 H HB2  A MET   B 1 2   ? 50.959 -14.535 -23.376 0.86 37.70 ?  2   MET   B HB2  1 
ATOM   3838 H HB2  B MET   B 1 2   ? 51.014 -14.465 -23.220 0.14 35.83 ?  2   MET   B HB2  1 
ATOM   3839 H HB3  A MET   B 1 2   ? 51.378 -15.066 -21.950 0.86 37.70 ?  2   MET   B HB3  1 
ATOM   3840 H HB3  B MET   B 1 2   ? 51.259 -15.129 -21.810 0.14 35.83 ?  2   MET   B HB3  1 
ATOM   3841 H HG2  A MET   B 1 2   ? 49.645 -16.498 -21.832 0.86 42.06 ?  2   MET   B HG2  1 
ATOM   3842 H HG2  B MET   B 1 2   ? 49.448 -16.445 -21.950 0.14 37.54 ?  2   MET   B HG2  1 
ATOM   3843 H HG3  A MET   B 1 2   ? 48.968 -15.874 -23.135 0.86 42.06 ?  2   MET   B HG3  1 
ATOM   3844 H HG3  B MET   B 1 2   ? 48.903 -15.671 -23.228 0.14 37.54 ?  2   MET   B HG3  1 
ATOM   3845 H HE1  A MET   B 1 2   ? 51.333 -16.741 -25.855 0.86 46.49 ?  2   MET   B HE1  1 
ATOM   3846 H HE1  B MET   B 1 2   ? 51.513 -16.472 -25.794 0.14 39.36 ?  2   MET   B HE1  1 
ATOM   3847 H HE2  A MET   B 1 2   ? 50.474 -15.562 -25.235 0.86 46.49 ?  2   MET   B HE2  1 
ATOM   3848 H HE2  B MET   B 1 2   ? 50.705 -15.268 -25.163 0.14 39.36 ?  2   MET   B HE2  1 
ATOM   3849 H HE3  A MET   B 1 2   ? 52.001 -15.739 -24.822 0.86 46.49 ?  2   MET   B HE3  1 
ATOM   3850 H HE3  B MET   B 1 2   ? 52.140 -15.657 -24.586 0.14 39.36 ?  2   MET   B HE3  1 
ATOM   3851 N N    A VAL   B 1 3   ? 48.400 -13.672 -19.991 0.86 22.95 ?  3   VAL   B N    1 
ATOM   3852 N N    B VAL   B 1 3   ? 48.378 -13.551 -19.887 0.14 24.18 ?  3   VAL   B N    1 
ATOM   3853 C CA   A VAL   B 1 3   ? 47.988 -13.920 -18.616 0.86 21.95 ?  3   VAL   B CA   1 
ATOM   3854 C CA   B VAL   B 1 3   ? 47.943 -13.822 -18.523 0.14 22.17 ?  3   VAL   B CA   1 
ATOM   3855 C C    A VAL   B 1 3   ? 46.748 -14.805 -18.637 0.86 20.02 ?  3   VAL   B C    1 
ATOM   3856 C C    B VAL   B 1 3   ? 46.695 -14.691 -18.568 0.14 20.04 ?  3   VAL   B C    1 
ATOM   3857 O O    A VAL   B 1 3   ? 46.011 -14.863 -19.623 0.86 20.72 ?  3   VAL   B O    1 
ATOM   3858 O O    B VAL   B 1 3   ? 45.897 -14.623 -19.508 0.14 19.94 ?  3   VAL   B O    1 
ATOM   3859 C CB   A VAL   B 1 3   ? 47.717 -12.612 -17.833 0.86 23.84 ?  3   VAL   B CB   1 
ATOM   3860 C CB   B VAL   B 1 3   ? 47.681 -12.530 -17.717 0.14 22.43 ?  3   VAL   B CB   1 
ATOM   3861 C CG1  A VAL   B 1 3   ? 48.991 -11.763 -17.738 0.86 24.47 ?  3   VAL   B CG1  1 
ATOM   3862 C CG1  B VAL   B 1 3   ? 48.950 -11.695 -17.615 0.14 22.53 ?  3   VAL   B CG1  1 
ATOM   3863 C CG2  A VAL   B 1 3   ? 46.581 -11.825 -18.471 0.86 24.46 ?  3   VAL   B CG2  1 
ATOM   3864 C CG2  B VAL   B 1 3   ? 46.551 -11.730 -18.343 0.14 22.51 ?  3   VAL   B CG2  1 
ATOM   3865 H H    A VAL   B 1 3   ? 47.757 -13.406 -20.495 0.86 27.69 ?  3   VAL   B H    1 
ATOM   3866 H H    B VAL   B 1 3   ? 47.776 -13.181 -20.379 0.14 29.16 ?  3   VAL   B H    1 
ATOM   3867 H HA   A VAL   B 1 3   ? 48.688 -14.402 -18.151 0.86 26.49 ?  3   VAL   B HA   1 
ATOM   3868 H HA   B VAL   B 1 3   ? 48.638 -14.319 -18.067 0.14 26.75 ?  3   VAL   B HA   1 
ATOM   3869 H HB   A VAL   B 1 3   ? 47.453 -12.838 -16.928 0.86 28.76 ?  3   VAL   B HB   1 
ATOM   3870 H HB   B VAL   B 1 3   ? 47.412 -12.774 -16.818 0.14 27.06 ?  3   VAL   B HB   1 
ATOM   3871 H HG11 A VAL   B 1 3   ? 48.797 -10.956 -17.235 0.86 29.51 ?  3   VAL   B HG11 1 
ATOM   3872 H HG11 B VAL   B 1 3   ? 48.764 -10.903 -17.086 0.14 27.19 ?  3   VAL   B HG11 1 
ATOM   3873 H HG12 A VAL   B 1 3   ? 49.680 -12.276 -17.285 0.86 29.51 ?  3   VAL   B HG12 1 
ATOM   3874 H HG12 B VAL   B 1 3   ? 49.642 -12.224 -17.186 0.14 27.19 ?  3   VAL   B HG12 1 
ATOM   3875 H HG13 A VAL   B 1 3   ? 49.285 -11.533 -18.633 0.86 29.51 ?  3   VAL   B HG13 1 
ATOM   3876 H HG13 B VAL   B 1 3   ? 49.233 -11.439 -18.506 0.14 27.19 ?  3   VAL   B HG13 1 
ATOM   3877 H HG21 A VAL   B 1 3   ? 46.542 -10.944 -18.070 0.86 29.50 ?  3   VAL   B HG21 1 
ATOM   3878 H HG21 B VAL   B 1 3   ? 46.506 -10.863 -17.914 0.14 27.16 ?  3   VAL   B HG21 1 
ATOM   3879 H HG22 A VAL   B 1 3   ? 46.745 -11.750 -19.423 0.86 29.50 ?  3   VAL   B HG22 1 
ATOM   3880 H HG22 B VAL   B 1 3   ? 46.729 -11.623 -19.290 0.14 27.16 ?  3   VAL   B HG22 1 
ATOM   3881 H HG23 A VAL   B 1 3   ? 45.747 -12.296 -18.314 0.86 29.50 ?  3   VAL   B HG23 1 
ATOM   3882 H HG23 B VAL   B 1 3   ? 45.717 -12.208 -18.215 0.14 27.16 ?  3   VAL   B HG23 1 
ATOM   3883 N N    . ASN   B 1 4   ? 46.529 -15.510 -17.530 1.00 18.15 ?  4   ASN   B N    1 
ATOM   3884 C CA   . ASN   B 1 4   ? 45.390 -16.417 -17.417 1.00 16.79 ?  4   ASN   B CA   1 
ATOM   3885 C C    . ASN   B 1 4   ? 45.330 -17.379 -18.601 1.00 17.23 ?  4   ASN   B C    1 
ATOM   3886 O O    . ASN   B 1 4   ? 44.265 -17.638 -19.157 1.00 18.13 ?  4   ASN   B O    1 
ATOM   3887 C CB   . ASN   B 1 4   ? 44.074 -15.650 -17.254 1.00 16.35 ?  4   ASN   B CB   1 
ATOM   3888 C CG   . ASN   B 1 4   ? 44.032 -14.840 -15.970 1.00 15.36 ?  4   ASN   B CG   1 
ATOM   3889 O OD1  . ASN   B 1 4   ? 44.321 -15.357 -14.893 1.00 15.15 ?  4   ASN   B OD1  1 
ATOM   3890 N ND2  . ASN   B 1 4   ? 43.688 -13.557 -16.082 1.00 16.60 ?  4   ASN   B ND2  1 
ATOM   3891 H H    A ASN   B 1 4   ? 47.034 -15.490 -16.836 0.86 21.93 ?  4   ASN   B H    1 
ATOM   3892 H H    B ASN   B 1 4   ? 47.071 -15.551 -16.865 0.14 21.93 ?  4   ASN   B H    1 
ATOM   3893 H HA   . ASN   B 1 4   ? 45.513 -16.956 -16.619 1.00 20.29 ?  4   ASN   B HA   1 
ATOM   3894 H HB2  . ASN   B 1 4   ? 43.966 -15.042 -17.999 1.00 19.77 ?  4   ASN   B HB2  1 
ATOM   3895 H HB3  . ASN   B 1 4   ? 43.339 -16.287 -17.235 1.00 19.77 ?  4   ASN   B HB3  1 
ATOM   3896 H HD21 . ASN   B 1 4   ? 43.647 -13.055 -15.382 1.00 20.07 ?  4   ASN   B HD21 1 
ATOM   3897 H HD22 . ASN   B 1 4   ? 43.497 -13.224 -16.854 1.00 20.07 ?  4   ASN   B HD22 1 
ATOM   3898 N N    . SER   B 1 5   ? 46.487 -17.913 -18.989 1.00 18.42 ?  5   SER   B N    1 
ATOM   3899 C CA   . SER   B 1 5   ? 46.575 -18.828 -20.127 1.00 20.91 ?  5   SER   B CA   1 
ATOM   3900 C C    . SER   B 1 5   ? 46.573 -20.265 -19.615 1.00 22.44 ?  5   SER   B C    1 
ATOM   3901 O O    . SER   B 1 5   ? 47.582 -20.964 -19.609 1.00 24.95 ?  5   SER   B O    1 
ATOM   3902 C CB   . SER   B 1 5   ? 47.819 -18.526 -20.959 1.00 22.68 ?  5   SER   B CB   1 
ATOM   3903 O OG   . SER   B 1 5   ? 49.009 -18.761 -20.221 1.00 25.53 ?  5   SER   B OG   1 
ATOM   3904 H H    . SER   B 1 5   ? 47.244 -17.763 -18.607 1.00 22.25 ?  5   SER   B H    1 
ATOM   3905 H HA   . SER   B 1 5   ? 45.800 -18.712 -20.696 1.00 25.25 ?  5   SER   B HA   1 
ATOM   3906 H HB2  . SER   B 1 5   ? 47.816 -19.090 -21.750 1.00 27.36 ?  5   SER   B HB2  1 
ATOM   3907 H HB3  . SER   B 1 5   ? 47.788 -17.593 -21.223 1.00 27.36 ?  5   SER   B HB3  1 
ATOM   3908 H HG   . SER   B 1 5   ? 49.065 -19.575 -20.023 1.00 30.78 ?  5   SER   B HG   1 
ATOM   3909 N N    . PHE   B 1 6   ? 45.396 -20.684 -19.165 1.00 22.63 ?  6   PHE   B N    1 
ATOM   3910 C CA   . PHE   B 1 6   ? 45.203 -22.029 -18.648 1.00 21.98 ?  6   PHE   B CA   1 
ATOM   3911 C C    . PHE   B 1 6   ? 45.124 -23.008 -19.809 1.00 25.50 ?  6   PHE   B C    1 
ATOM   3912 O O    . PHE   B 1 6   ? 44.463 -22.739 -20.815 1.00 27.70 ?  6   PHE   B O    1 
ATOM   3913 C CB   . PHE   B 1 6   ? 43.908 -22.079 -17.833 1.00 19.62 ?  6   PHE   B CB   1 
ATOM   3914 C CG   . PHE   B 1 6   ? 43.933 -21.221 -16.592 1.00 17.92 ?  6   PHE   B CG   1 
ATOM   3915 C CD1  . PHE   B 1 6   ? 44.446 -21.719 -15.410 1.00 16.92 ?  6   PHE   B CD1  1 
ATOM   3916 C CD2  . PHE   B 1 6   ? 43.448 -19.915 -16.613 1.00 17.15 ?  6   PHE   B CD2  1 
ATOM   3917 C CE1  . PHE   B 1 6   ? 44.470 -20.940 -14.260 1.00 16.26 ?  6   PHE   B CE1  1 
ATOM   3918 C CE2  . PHE   B 1 6   ? 43.472 -19.128 -15.470 1.00 17.65 ?  6   PHE   B CE2  1 
ATOM   3919 C CZ   . PHE   B 1 6   ? 43.988 -19.633 -14.296 1.00 16.62 ?  6   PHE   B CZ   1 
ATOM   3920 H H    . PHE   B 1 6   ? 44.683 -20.209 -19.161 1.00 27.30 ?  6   PHE   B H    1 
ATOM   3921 H HA   . PHE   B 1 6   ? 45.943 -22.279 -18.075 1.00 26.53 ?  6   PHE   B HA   1 
ATOM   3922 H HB2  . PHE   B 1 6   ? 43.176 -21.770 -18.391 1.00 23.69 ?  6   PHE   B HB2  1 
ATOM   3923 H HB3  . PHE   B 1 6   ? 43.744 -22.993 -17.554 1.00 23.69 ?  6   PHE   B HB3  1 
ATOM   3924 H HD1  . PHE   B 1 6   ? 44.780 -22.586 -15.385 1.00 20.45 ?  6   PHE   B HD1  1 
ATOM   3925 H HD2  . PHE   B 1 6   ? 43.096 -19.571 -17.403 1.00 20.73 ?  6   PHE   B HD2  1 
ATOM   3926 H HE1  . PHE   B 1 6   ? 44.829 -21.282 -13.470 1.00 19.66 ?  6   PHE   B HE1  1 
ATOM   3927 H HE2  . PHE   B 1 6   ? 43.139 -18.256 -15.495 1.00 21.33 ?  6   PHE   B HE2  1 
ATOM   3928 H HZ   . PHE   B 1 6   ? 44.006 -19.112 -13.525 1.00 20.09 ?  6   PHE   B HZ   1 
ATOM   3929 N N    . SER   B 1 7   ? 45.824 -24.138 -19.677 1.00 26.06 ?  7   SER   B N    1 
ATOM   3930 C CA   . SER   B 1 7   ? 45.911 -25.121 -20.748 1.00 28.99 ?  7   SER   B CA   1 
ATOM   3931 C C    . SER   B 1 7   ? 45.857 -26.528 -20.171 1.00 28.07 ?  7   SER   B C    1 
ATOM   3932 O O    . SER   B 1 7   ? 46.457 -26.809 -19.130 1.00 29.11 ?  7   SER   B O    1 
ATOM   3933 C CB   . SER   B 1 7   ? 47.205 -24.942 -21.558 1.00 32.26 ?  7   SER   B CB   1 
ATOM   3934 O OG   . SER   B 1 7   ? 47.193 -25.744 -22.726 1.00 34.62 ?  7   SER   B OG   1 
ATOM   3935 H H    . SER   B 1 7   ? 46.267 -24.356 -18.969 1.00 31.41 ?  7   SER   B H    1 
ATOM   3936 H HA   . SER   B 1 7   ? 45.162 -25.014 -21.348 1.00 34.94 ?  7   SER   B HA   1 
ATOM   3937 H HB2  . SER   B 1 7   ? 47.289 -24.008 -21.815 1.00 38.87 ?  7   SER   B HB2  1 
ATOM   3938 H HB3  . SER   B 1 7   ? 47.963 -25.199 -21.010 1.00 38.87 ?  7   SER   B HB3  1 
ATOM   3939 H HG   . SER   B 1 7   ? 47.905 -25.629 -23.162 1.00 41.70 ?  7   SER   B HG   1 
ATOM   3940 N N    . GLY   B 1 8   ? 45.131 -27.409 -20.858 1.00 27.89 ?  8   GLY   B N    1 
ATOM   3941 C CA   . GLY   B 1 8   ? 45.094 -28.806 -20.485 1.00 27.14 ?  8   GLY   B CA   1 
ATOM   3942 C C    . GLY   B 1 8   ? 44.153 -29.143 -19.357 1.00 25.65 ?  8   GLY   B C    1 
ATOM   3943 O O    . GLY   B 1 8   ? 44.297 -30.211 -18.747 1.00 27.30 ?  8   GLY   B O    1 
ATOM   3944 H H    . GLY   B 1 8   ? 44.652 -27.211 -21.540 1.00 33.61 ?  8   GLY   B H    1 
ATOM   3945 H HA2  . GLY   B 1 8   ? 44.826 -29.329 -21.255 1.00 32.71 ?  8   GLY   B HA2  1 
ATOM   3946 H HA3  . GLY   B 1 8   ? 45.980 -29.088 -20.220 1.00 32.71 ?  8   GLY   B HA3  1 
ATOM   3947 N N    . TYR   B 1 9   ? 43.170 -28.290 -19.075 1.00 23.30 ?  9   TYR   B N    1 
ATOM   3948 C CA   . TYR   B 1 9   ? 42.218 -28.565 -18.010 1.00 21.14 ?  9   TYR   B CA   1 
ATOM   3949 C C    . TYR   B 1 9   ? 41.031 -29.358 -18.525 1.00 20.75 ?  9   TYR   B C    1 
ATOM   3950 O O    . TYR   B 1 9   ? 40.607 -29.217 -19.677 1.00 22.96 ?  9   TYR   B O    1 
ATOM   3951 C CB   . TYR   B 1 9   ? 41.715 -27.278 -17.360 1.00 20.65 ?  9   TYR   B CB   1 
ATOM   3952 C CG   . TYR   B 1 9   ? 42.743 -26.657 -16.446 1.00 19.73 ?  9   TYR   B CG   1 
ATOM   3953 C CD1  . TYR   B 1 9   ? 43.841 -25.993 -16.967 1.00 20.38 ?  9   TYR   B CD1  1 
ATOM   3954 C CD2  . TYR   B 1 9   ? 42.630 -26.750 -15.067 1.00 19.15 ?  9   TYR   B CD2  1 
ATOM   3955 C CE1  . TYR   B 1 9   ? 44.801 -25.436 -16.143 1.00 20.56 ?  9   TYR   B CE1  1 
ATOM   3956 C CE2  . TYR   B 1 9   ? 43.582 -26.197 -14.233 1.00 19.55 ?  9   TYR   B CE2  1 
ATOM   3957 C CZ   . TYR   B 1 9   ? 44.668 -25.533 -14.778 1.00 20.58 ?  9   TYR   B CZ   1 
ATOM   3958 O OH   . TYR   B 1 9   ? 45.622 -24.985 -13.956 1.00 21.39 ?  9   TYR   B OH   1 
ATOM   3959 H H    . TYR   B 1 9   ? 43.013 -27.560 -19.503 1.00 28.11 ?  9   TYR   B H    1 
ATOM   3960 H HA   . TYR   B 1 9   ? 42.649 -29.092 -17.325 1.00 25.52 ?  9   TYR   B HA   1 
ATOM   3961 H HB2  . TYR   B 1 9   ? 41.487 -26.629 -18.047 1.00 24.93 ?  9   TYR   B HB2  1 
ATOM   3962 H HB3  . TYR   B 1 9   ? 40.935 -27.487 -16.827 1.00 24.93 ?  9   TYR   B HB3  1 
ATOM   3963 H HD1  . TYR   B 1 9   ? 43.936 -25.925 -17.890 1.00 24.60 ?  9   TYR   B HD1  1 
ATOM   3964 H HD2  . TYR   B 1 9   ? 41.898 -27.198 -14.697 1.00 23.13 ?  9   TYR   B HD2  1 
ATOM   3965 H HE1  . TYR   B 1 9   ? 45.527 -24.995 -16.510 1.00 24.82 ?  9   TYR   B HE1  1 
ATOM   3966 H HE2  . TYR   B 1 9   ? 43.484 -26.272 -13.309 1.00 23.60 ?  9   TYR   B HE2  1 
ATOM   3967 H HH   . TYR   B 1 9   ? 46.219 -24.621 -14.423 1.00 25.81 ?  9   TYR   B HH   1 
ATOM   3968 N N    . LEU   B 1 10  ? 40.506 -30.210 -17.651 1.00 18.62 ?  10  LEU   B N    1 
ATOM   3969 C CA   . LEU   B 1 10  ? 39.295 -30.965 -17.917 1.00 18.45 ?  10  LEU   B CA   1 
ATOM   3970 C C    . LEU   B 1 10  ? 38.110 -30.197 -17.353 1.00 18.17 ?  10  LEU   B C    1 
ATOM   3971 O O    . LEU   B 1 10  ? 38.126 -29.781 -16.191 1.00 18.09 ?  10  LEU   B O    1 
ATOM   3972 C CB   . LEU   B 1 10  ? 39.392 -32.333 -17.244 1.00 19.62 ?  10  LEU   B CB   1 
ATOM   3973 C CG   . LEU   B 1 10  ? 38.244 -33.284 -17.564 1.00 21.40 ?  10  LEU   B CG   1 
ATOM   3974 C CD1  . LEU   B 1 10  ? 38.374 -33.816 -18.985 1.00 22.77 ?  10  LEU   B CD1  1 
ATOM   3975 C CD2  . LEU   B 1 10  ? 38.182 -34.419 -16.557 1.00 22.76 ?  10  LEU   B CD2  1 
ATOM   3976 H H    . LEU   B 1 10  ? 40.841 -30.369 -16.869 1.00 22.49 ?  10  LEU   B H    1 
ATOM   3977 H HA   . LEU   B 1 10  ? 39.174 -31.089 -18.866 1.00 22.29 ?  10  LEU   B HA   1 
ATOM   3978 H HB2  . LEU   B 1 10  ? 40.215 -32.764 -17.525 1.00 23.69 ?  10  LEU   B HB2  1 
ATOM   3979 H HB3  . LEU   B 1 10  ? 39.407 -32.211 -16.279 1.00 23.69 ?  10  LEU   B HB3  1 
ATOM   3980 H HG   . LEU   B 1 10  ? 37.407 -32.800 -17.507 1.00 25.83 ?  10  LEU   B HG   1 
ATOM   3981 H HD11 . LEU   B 1 10  ? 37.663 -34.453 -19.150 1.00 27.47 ?  10  LEU   B HD11 1 
ATOM   3982 H HD12 . LEU   B 1 10  ? 38.304 -33.073 -19.605 1.00 27.47 ?  10  LEU   B HD12 1 
ATOM   3983 H HD13 . LEU   B 1 10  ? 39.236 -34.248 -19.081 1.00 27.47 ?  10  LEU   B HD13 1 
ATOM   3984 H HD21 . LEU   B 1 10  ? 37.445 -35.007 -16.792 1.00 27.46 ?  10  LEU   B HD21 1 
ATOM   3985 H HD22 . LEU   B 1 10  ? 39.017 -34.906 -16.579 1.00 27.46 ?  10  LEU   B HD22 1 
ATOM   3986 H HD23 . LEU   B 1 10  ? 38.035 -34.045 -15.674 1.00 27.46 ?  10  LEU   B HD23 1 
ATOM   3987 N N    . LYS   B 1 11  ? 37.089 -30.007 -18.177 1.00 19.43 ?  11  LYS   B N    1 
ATOM   3988 C CA   . LYS   B 1 11  ? 35.897 -29.287 -17.757 1.00 21.42 ?  11  LYS   B CA   1 
ATOM   3989 C C    . LYS   B 1 11  ? 35.013 -30.214 -16.930 1.00 20.55 ?  11  LYS   B C    1 
ATOM   3990 O O    . LYS   B 1 11  ? 34.631 -31.298 -17.394 1.00 22.54 ?  11  LYS   B O    1 
ATOM   3991 C CB   . LYS   B 1 11  ? 35.151 -28.795 -18.995 1.00 25.36 ?  11  LYS   B CB   1 
ATOM   3992 C CG   . LYS   B 1 11  ? 33.942 -27.923 -18.719 1.00 29.02 ?  11  LYS   B CG   1 
ATOM   3993 C CD   . LYS   B 1 11  ? 33.165 -27.666 -20.005 1.00 32.16 ?  11  LYS   B CD   1 
ATOM   3994 C CE   . LYS   B 1 11  ? 32.137 -26.564 -19.830 1.00 34.42 ?  11  LYS   B CE   1 
ATOM   3995 N NZ   . LYS   B 1 11  ? 32.785 -25.236 -19.664 1.00 35.60 ?  11  LYS   B NZ   1 
ATOM   3996 H H    . LYS   B 1 11  ? 37.062 -30.291 -18.988 1.00 23.47 ?  11  LYS   B H    1 
ATOM   3997 H HA   . LYS   B 1 11  ? 36.154 -28.522 -17.214 1.00 25.85 ?  11  LYS   B HA   1 
ATOM   3998 H HB2  . LYS   B 1 11  ? 35.766 -28.276 -19.537 1.00 30.58 ?  11  LYS   B HB2  1 
ATOM   3999 H HB3  . LYS   B 1 11  ? 34.847 -29.566 -19.495 1.00 30.58 ?  11  LYS   B HB3  1 
ATOM   4000 H HG2  . LYS   B 1 11  ? 33.355 -28.372 -18.092 1.00 34.98 ?  11  LYS   B HG2  1 
ATOM   4001 H HG3  . LYS   B 1 11  ? 34.234 -27.071 -18.361 1.00 34.98 ?  11  LYS   B HG3  1 
ATOM   4002 H HD2  . LYS   B 1 11  ? 33.783 -27.397 -20.703 1.00 38.74 ?  11  LYS   B HD2  1 
ATOM   4003 H HD3  . LYS   B 1 11  ? 32.701 -28.478 -20.264 1.00 38.74 ?  11  LYS   B HD3  1 
ATOM   4004 H HE2  . LYS   B 1 11  ? 31.568 -26.530 -20.615 1.00 41.45 ?  11  LYS   B HE2  1 
ATOM   4005 H HE3  . LYS   B 1 11  ? 31.606 -26.747 -19.039 1.00 41.45 ?  11  LYS   B HE3  1 
ATOM   4006 H HZ1  . LYS   B 1 11  ? 32.164 -24.601 -19.600 1.00 42.87 ?  11  LYS   B HZ1  1 
ATOM   4007 H HZ2  . LYS   B 1 11  ? 33.282 -25.229 -18.926 1.00 42.87 ?  11  LYS   B HZ2  1 
ATOM   4008 H HZ3  . LYS   B 1 11  ? 33.305 -25.061 -20.365 1.00 42.87 ?  11  LYS   B HZ3  1 
ATOM   4009 N N    . LEU   B 1 12  ? 34.678 -29.786 -15.712 1.00 18.83 ?  12  LEU   B N    1 
ATOM   4010 C CA   . LEU   B 1 12  ? 33.722 -30.493 -14.866 1.00 18.51 ?  12  LEU   B CA   1 
ATOM   4011 C C    . LEU   B 1 12  ? 32.331 -29.887 -14.949 1.00 18.31 ?  12  LEU   B C    1 
ATOM   4012 O O    . LEU   B 1 12  ? 31.347 -30.607 -15.120 1.00 18.91 ?  12  LEU   B O    1 
ATOM   4013 C CB   . LEU   B 1 12  ? 34.191 -30.507 -13.406 1.00 17.89 ?  12  LEU   B CB   1 
ATOM   4014 C CG   . LEU   B 1 12  ? 35.521 -31.202 -13.131 1.00 17.90 ?  12  LEU   B CG   1 
ATOM   4015 C CD1  . LEU   B 1 12  ? 35.852 -31.153 -11.649 1.00 18.00 ?  12  LEU   B CD1  1 
ATOM   4016 C CD2  . LEU   B 1 12  ? 35.514 -32.642 -13.632 1.00 18.74 ?  12  LEU   B CD2  1 
ATOM   4017 H H    . LEU   B 1 12  ? 34.987 -29.063 -15.350 1.00 22.75 ?  12  LEU   B H    1 
ATOM   4018 H HA   . LEU   B 1 12  ? 33.653 -31.406 -15.169 1.00 22.36 ?  12  LEU   B HA   1 
ATOM   4019 H HB2  . LEU   B 1 12  ? 34.272 -29.592 -13.102 1.00 21.62 ?  12  LEU   B HB2  1 
ATOM   4020 H HB3  . LEU   B 1 12  ? 33.515 -30.962 -12.877 1.00 21.62 ?  12  LEU   B HB3  1 
ATOM   4021 H HG   . LEU   B 1 12  ? 36.223 -30.725 -13.603 1.00 21.63 ?  12  LEU   B HG   1 
ATOM   4022 H HD11 . LEU   B 1 12  ? 36.703 -31.596 -11.500 1.00 21.75 ?  12  LEU   B HD11 1 
ATOM   4023 H HD12 . LEU   B 1 12  ? 35.909 -30.226 -11.366 1.00 21.75 ?  12  LEU   B HD12 1 
ATOM   4024 H HD13 . LEU   B 1 12  ? 35.153 -31.608 -11.153 1.00 21.75 ?  12  LEU   B HD13 1 
ATOM   4025 H HD21 . LEU   B 1 12  ? 36.319 -33.086 -13.323 1.00 22.64 ?  12  LEU   B HD21 1 
ATOM   4026 H HD22 . LEU   B 1 12  ? 34.731 -33.092 -13.285 1.00 22.64 ?  12  LEU   B HD22 1 
ATOM   4027 H HD23 . LEU   B 1 12  ? 35.491 -32.636 -14.603 1.00 22.64 ?  12  LEU   B HD23 1 
ATOM   4028 N N    . THR   B 1 13  ? 32.238 -28.567 -14.833 1.00 18.04 ?  13  THR   B N    1 
ATOM   4029 C CA   . THR   B 1 13  ? 31.008 -27.816 -15.030 1.00 18.17 ?  13  THR   B CA   1 
ATOM   4030 C C    . THR   B 1 13  ? 31.338 -26.615 -15.909 1.00 20.41 ?  13  THR   B C    1 
ATOM   4031 O O    . THR   B 1 13  ? 32.480 -26.427 -16.344 1.00 21.23 ?  13  THR   B O    1 
ATOM   4032 C CB   . THR   B 1 13  ? 30.412 -27.342 -13.700 1.00 17.99 ?  13  THR   B CB   1 
ATOM   4033 O OG1  . THR   B 1 13  ? 31.255 -26.322 -13.154 1.00 17.69 ?  13  THR   B OG1  1 
ATOM   4034 C CG2  . THR   B 1 13  ? 30.294 -28.493 -12.706 1.00 18.68 ?  13  THR   B CG2  1 
ATOM   4035 H H    . THR   B 1 13  ? 32.907 -28.061 -14.633 1.00 21.80 ?  13  THR   B H    1 
ATOM   4036 H HA   . THR   B 1 13  ? 30.355 -28.373 -15.477 1.00 21.95 ?  13  THR   B HA   1 
ATOM   4037 H HB   . THR   B 1 13  ? 29.521 -26.981 -13.852 1.00 21.74 ?  13  THR   B HB   1 
ATOM   4038 H HG1  . THR   B 1 13  ? 30.946 -25.560 -13.345 1.00 21.37 ?  13  THR   B HG1  1 
ATOM   4039 H HG21 . THR   B 1 13  ? 29.778 -28.215 -11.933 1.00 22.57 ?  13  THR   B HG21 1 
ATOM   4040 H HG22 . THR   B 1 13  ? 29.853 -29.248 -13.125 1.00 22.57 ?  13  THR   B HG22 1 
ATOM   4041 H HG23 . THR   B 1 13  ? 31.178 -28.768 -12.413 1.00 22.57 ?  13  THR   B HG23 1 
ATOM   4042 N N    A ASP   B 1 14  ? 30.325 -25.788 -16.164 0.86 21.65 ?  14  ASP   B N    1 
ATOM   4043 N N    B ASP   B 1 14  ? 30.328 -25.777 -16.152 0.14 21.06 ?  14  ASP   B N    1 
ATOM   4044 C CA   A ASP   B 1 14  ? 30.531 -24.626 -17.019 0.86 23.41 ?  14  ASP   B CA   1 
ATOM   4045 C CA   B ASP   B 1 14  ? 30.518 -24.619 -17.019 0.14 21.81 ?  14  ASP   B CA   1 
ATOM   4046 C C    A ASP   B 1 14  ? 31.631 -23.715 -16.489 0.86 21.57 ?  14  ASP   B C    1 
ATOM   4047 C C    B ASP   B 1 14  ? 31.536 -23.632 -16.466 0.14 20.34 ?  14  ASP   B C    1 
ATOM   4048 O O    A ASP   B 1 14  ? 32.277 -23.010 -17.274 0.86 23.19 ?  14  ASP   B O    1 
ATOM   4049 O O    B ASP   B 1 14  ? 32.021 -22.779 -17.219 0.14 20.54 ?  14  ASP   B O    1 
ATOM   4050 C CB   A ASP   B 1 14  ? 29.224 -23.848 -17.170 0.86 27.37 ?  14  ASP   B CB   1 
ATOM   4051 C CB   B ASP   B 1 14  ? 29.188 -23.899 -17.249 0.14 24.00 ?  14  ASP   B CB   1 
ATOM   4052 C CG   A ASP   B 1 14  ? 28.252 -24.517 -18.118 0.86 31.52 ?  14  ASP   B CG   1 
ATOM   4053 C CG   B ASP   B 1 14  ? 28.288 -24.635 -18.224 0.14 25.94 ?  14  ASP   B CG   1 
ATOM   4054 O OD1  A ASP   B 1 14  ? 28.681 -25.368 -18.927 0.86 32.92 ?  14  ASP   B OD1  1 
ATOM   4055 O OD1  B ASP   B 1 14  ? 28.816 -25.324 -19.121 0.14 26.62 ?  14  ASP   B OD1  1 
ATOM   4056 O OD2  A ASP   B 1 14  ? 27.052 -24.186 -18.052 0.86 33.25 -1 14  ASP   B OD2  1 
ATOM   4057 O OD2  B ASP   B 1 14  ? 27.050 -24.527 -18.092 0.14 26.58 -1 14  ASP   B OD2  1 
ATOM   4058 H H    A ASP   B 1 14  ? 29.526 -25.876 -15.855 0.86 26.13 ?  14  ASP   B H    1 
ATOM   4059 H H    B ASP   B 1 14  ? 29.534 -25.857 -15.829 0.14 25.42 ?  14  ASP   B H    1 
ATOM   4060 H HA   A ASP   B 1 14  ? 30.800 -24.927 -17.897 0.86 28.24 ?  14  ASP   B HA   1 
ATOM   4061 H HA   B ASP   B 1 14  ? 30.841 -24.926 -17.879 0.14 26.32 ?  14  ASP   B HA   1 
ATOM   4062 H HB2  A ASP   B 1 14  ? 28.782 -23.793 -16.309 0.86 33.00 ?  14  ASP   B HB2  1 
ATOM   4063 H HB2  B ASP   B 1 14  ? 28.716 -23.830 -16.405 0.14 28.95 ?  14  ASP   B HB2  1 
ATOM   4064 H HB3  A ASP   B 1 14  ? 29.419 -22.959 -17.503 0.86 33.00 ?  14  ASP   B HB3  1 
ATOM   4065 H HB3  B ASP   B 1 14  ? 29.370 -23.010 -17.599 0.14 28.95 ?  14  ASP   B HB3  1 
ATOM   4066 N N    . ASN   B 1 15  ? 31.860 -23.709 -15.173 1.00 18.78 ?  15  ASN   B N    1 
ATOM   4067 C CA   . ASN   B 1 15  ? 32.826 -22.789 -14.572 1.00 16.31 ?  15  ASN   B CA   1 
ATOM   4068 C C    . ASN   B 1 15  ? 33.922 -23.442 -13.738 1.00 14.81 ?  15  ASN   B C    1 
ATOM   4069 O O    . ASN   B 1 15  ? 34.767 -22.716 -13.206 1.00 15.44 ?  15  ASN   B O    1 
ATOM   4070 C CB   . ASN   B 1 15  ? 32.116 -21.734 -13.708 1.00 16.81 ?  15  ASN   B CB   1 
ATOM   4071 C CG   . ASN   B 1 15  ? 31.489 -22.333 -12.469 1.00 15.93 ?  15  ASN   B CG   1 
ATOM   4072 O OD1  . ASN   B 1 15  ? 30.547 -23.134 -12.557 1.00 18.00 ?  15  ASN   B OD1  1 
ATOM   4073 N ND2  . ASN   B 1 15  ? 32.013 -21.981 -11.310 1.00 15.41 ?  15  ASN   B ND2  1 
ATOM   4074 H H    A ASN   B 1 15  ? 31.462 -24.223 -14.607 0.86 22.69 ?  15  ASN   B H    1 
ATOM   4075 H H    B ASN   B 1 15  ? 31.514 -24.270 -14.618 0.14 22.69 ?  15  ASN   B H    1 
ATOM   4076 H HA   . ASN   B 1 15  ? 33.271 -22.311 -15.283 1.00 19.72 ?  15  ASN   B HA   1 
ATOM   4077 H HB2  . ASN   B 1 15  ? 32.770 -21.063 -13.432 1.00 20.31 ?  15  ASN   B HB2  1 
ATOM   4078 H HB3  . ASN   B 1 15  ? 31.417 -21.308 -14.230 1.00 20.31 ?  15  ASN   B HB3  1 
ATOM   4079 H HD21 . ASN   B 1 15  ? 31.686 -22.293 -10.577 1.00 18.64 ?  15  ASN   B HD21 1 
ATOM   4080 H HD22 . ASN   B 1 15  ? 32.677 -21.427 -11.277 1.00 18.64 ?  15  ASN   B HD22 1 
ATOM   4081 N N    . VAL   B 1 16  ? 33.936 -24.768 -13.591 1.00 14.89 ?  16  VAL   B N    1 
ATOM   4082 C CA   . VAL   B 1 16  ? 34.939 -25.464 -12.790 1.00 14.55 ?  16  VAL   B CA   1 
ATOM   4083 C C    . VAL   B 1 16  ? 35.727 -26.403 -13.689 1.00 14.95 ?  16  VAL   B C    1 
ATOM   4084 O O    . VAL   B 1 16  ? 35.146 -27.274 -14.353 1.00 16.21 ?  16  VAL   B O    1 
ATOM   4085 C CB   . VAL   B 1 16  ? 34.315 -26.230 -11.609 1.00 14.64 ?  16  VAL   B CB   1 
ATOM   4086 C CG1  . VAL   B 1 16  ? 35.399 -26.965 -10.818 1.00 14.59 ?  16  VAL   B CG1  1 
ATOM   4087 C CG2  . VAL   B 1 16  ? 33.521 -25.288 -10.712 1.00 15.70 ?  16  VAL   B CG2  1 
ATOM   4088 H H    . VAL   B 1 16  ? 33.356 -25.300 -13.950 1.00 18.01 ?  16  VAL   B H    1 
ATOM   4089 H HA   . VAL   B 1 16  ? 35.558 -24.811 -12.425 1.00 17.61 ?  16  VAL   B HA   1 
ATOM   4090 H HB   . VAL   B 1 16  ? 33.705 -26.897 -11.960 1.00 17.72 ?  16  VAL   B HB   1 
ATOM   4091 H HG11 . VAL   B 1 16  ? 35.019 -27.271 -9.980  1.00 17.65 ?  16  VAL   B HG11 1 
ATOM   4092 H HG12 . VAL   B 1 16  ? 35.714 -27.724 -11.334 1.00 17.65 ?  16  VAL   B HG12 1 
ATOM   4093 H HG13 . VAL   B 1 16  ? 36.132 -26.354 -10.644 1.00 17.65 ?  16  VAL   B HG13 1 
ATOM   4094 H HG21 . VAL   B 1 16  ? 33.186 -25.786 -9.952  1.00 18.99 ?  16  VAL   B HG21 1 
ATOM   4095 H HG22 . VAL   B 1 16  ? 34.104 -24.574 -10.411 1.00 18.99 ?  16  VAL   B HG22 1 
ATOM   4096 H HG23 . VAL   B 1 16  ? 32.782 -24.919 -11.220 1.00 18.99 ?  16  VAL   B HG23 1 
ATOM   4097 N N    . TYR   B 1 17  ? 37.053 -26.243 -13.666 1.00 15.05 ?  17  TYR   B N    1 
ATOM   4098 C CA   . TYR   B 1 17  ? 37.997 -27.003 -14.473 1.00 15.26 ?  17  TYR   B CA   1 
ATOM   4099 C C    . TYR   B 1 17  ? 39.047 -27.617 -13.554 1.00 14.43 ?  17  TYR   B C    1 
ATOM   4100 O O    . TYR   B 1 17  ? 39.334 -27.080 -12.478 1.00 15.03 ?  17  TYR   B O    1 
ATOM   4101 C CB   . TYR   B 1 17  ? 38.706 -26.082 -15.477 1.00 18.06 ?  17  TYR   B CB   1 
ATOM   4102 C CG   . TYR   B 1 17  ? 37.780 -25.312 -16.385 1.00 21.24 ?  17  TYR   B CG   1 
ATOM   4103 C CD1  . TYR   B 1 17  ? 37.199 -24.118 -15.974 1.00 22.97 ?  17  TYR   B CD1  1 
ATOM   4104 C CD2  . TYR   B 1 17  ? 37.488 -25.776 -17.659 1.00 23.06 ?  17  TYR   B CD2  1 
ATOM   4105 C CE1  . TYR   B 1 17  ? 36.350 -23.411 -16.806 1.00 24.57 ?  17  TYR   B CE1  1 
ATOM   4106 C CE2  . TYR   B 1 17  ? 36.644 -25.077 -18.500 1.00 24.79 ?  17  TYR   B CE2  1 
ATOM   4107 C CZ   . TYR   B 1 17  ? 36.077 -23.898 -18.067 1.00 25.42 ?  17  TYR   B CZ   1 
ATOM   4108 O OH   . TYR   B 1 17  ? 35.238 -23.200 -18.904 1.00 26.70 ?  17  TYR   B OH   1 
ATOM   4109 H H    . TYR   B 1 17  ? 37.455 -25.668 -13.159 1.00 18.20 ?  17  TYR   B H    1 
ATOM   4110 H HA   . TYR   B 1 17  ? 37.537 -27.711 -14.955 1.00 18.46 ?  17  TYR   B HA   1 
ATOM   4111 H HB2  . TYR   B 1 17  ? 39.247 -25.442 -14.992 1.00 21.82 ?  17  TYR   B HB2  1 
ATOM   4112 H HB3  . TYR   B 1 17  ? 39.269 -26.626 -16.045 1.00 21.82 ?  17  TYR   B HB3  1 
ATOM   4113 H HD1  . TYR   B 1 17  ? 37.383 -23.791 -15.125 1.00 27.71 ?  17  TYR   B HD1  1 
ATOM   4114 H HD2  . TYR   B 1 17  ? 37.863 -26.573 -17.956 1.00 27.82 ?  17  TYR   B HD2  1 
ATOM   4115 H HE1  . TYR   B 1 17  ? 35.966 -22.612 -16.518 1.00 29.63 ?  17  TYR   B HE1  1 
ATOM   4116 H HE2  . TYR   B 1 17  ? 36.450 -25.402 -19.352 1.00 29.89 ?  17  TYR   B HE2  1 
ATOM   4117 H HH   . TYR   B 1 17  ? 35.149 -23.603 -19.637 1.00 32.18 ?  17  TYR   B HH   1 
ATOM   4118 N N    . ILE   B 1 18  ? 39.663 -28.719 -13.990 1.00 14.59 ?  18  ILE   B N    1 
ATOM   4119 C CA   . ILE   B 1 18  ? 40.598 -29.442 -13.132 1.00 14.48 ?  18  ILE   B CA   1 
ATOM   4120 C C    . ILE   B 1 18  ? 41.759 -29.996 -13.954 1.00 14.89 ?  18  ILE   B C    1 
ATOM   4121 O O    . ILE   B 1 18  ? 41.596 -30.390 -15.114 1.00 16.01 ?  18  ILE   B O    1 
ATOM   4122 C CB   . ILE   B 1 18  ? 39.849 -30.542 -12.333 1.00 15.09 ?  18  ILE   B CB   1 
ATOM   4123 C CG1  . ILE   B 1 18  ? 40.707 -31.093 -11.187 1.00 15.89 ?  18  ILE   B CG1  1 
ATOM   4124 C CG2  . ILE   B 1 18  ? 39.343 -31.654 -13.260 1.00 15.54 ?  18  ILE   B CG2  1 
ATOM   4125 C CD1  . ILE   B 1 18  ? 39.892 -31.913 -10.180 1.00 17.35 ?  18  ILE   B CD1  1 
ATOM   4126 H H    . ILE   B 1 18  ? 39.564 -29.065 -14.771 1.00 17.66 ?  18  ILE   B H    1 
ATOM   4127 H HA   . ILE   B 1 18  ? 40.967 -28.821 -12.482 1.00 17.53 ?  18  ILE   B HA   1 
ATOM   4128 H HB   . ILE   B 1 18  ? 39.070 -30.133 -11.928 1.00 18.26 ?  18  ILE   B HB   1 
ATOM   4129 H HG12 . ILE   B 1 18  ? 41.395 -31.669 -11.551 1.00 19.21 ?  18  ILE   B HG12 1 
ATOM   4130 H HG13 . ILE   B 1 18  ? 41.109 -30.352 -10.708 1.00 19.21 ?  18  ILE   B HG13 1 
ATOM   4131 H HG21 . ILE   B 1 18  ? 38.756 -32.242 -12.757 1.00 18.80 ?  18  ILE   B HG21 1 
ATOM   4132 H HG22 . ILE   B 1 18  ? 38.855 -31.250 -13.993 1.00 18.80 ?  18  ILE   B HG22 1 
ATOM   4133 H HG23 . ILE   B 1 18  ? 40.100 -32.154 -13.599 1.00 18.80 ?  18  ILE   B HG23 1 
ATOM   4134 H HD11 . ILE   B 1 18  ? 40.470 -32.191 -9.452  1.00 20.96 ?  18  ILE   B HD11 1 
ATOM   4135 H HD12 . ILE   B 1 18  ? 39.168 -31.364 -9.834  1.00 20.96 ?  18  ILE   B HD12 1 
ATOM   4136 H HD13 . ILE   B 1 18  ? 39.525 -32.693 -10.627 1.00 20.96 ?  18  ILE   B HD13 1 
ATOM   4137 N N    . LYS   B 1 19  ? 42.940 -30.031 -13.332 1.00 15.43 ?  19  LYS   B N    1 
ATOM   4138 C CA   . LYS   B 1 19  ? 44.152 -30.511 -13.983 1.00 16.27 ?  19  LYS   B CA   1 
ATOM   4139 C C    . LYS   B 1 19  ? 45.041 -31.195 -12.954 1.00 16.12 ?  19  LYS   B C    1 
ATOM   4140 O O    . LYS   B 1 19  ? 45.123 -30.762 -11.804 1.00 15.87 ?  19  LYS   B O    1 
ATOM   4141 C CB   . LYS   B 1 19  ? 44.928 -29.349 -14.620 1.00 17.86 ?  19  LYS   B CB   1 
ATOM   4142 C CG   . LYS   B 1 19  ? 46.128 -29.757 -15.458 1.00 19.85 ?  19  LYS   B CG   1 
ATOM   4143 C CD   . LYS   B 1 19  ? 46.854 -28.519 -15.972 1.00 22.02 ?  19  LYS   B CD   1 
ATOM   4144 C CE   . LYS   B 1 19  ? 48.010 -28.876 -16.887 1.00 24.20 ?  19  LYS   B CE   1 
ATOM   4145 N NZ   . LYS   B 1 19  ? 48.768 -27.673 -17.325 1.00 25.53 ?  19  LYS   B NZ   1 
ATOM   4146 H H    . LYS   B 1 19  ? 43.056 -29.777 -12.517 1.00 18.67 ?  19  LYS   B H    1 
ATOM   4147 H HA   . LYS   B 1 19  ? 43.914 -31.151 -14.674 1.00 19.67 ?  19  LYS   B HA   1 
ATOM   4148 H HB2  . LYS   B 1 19  ? 44.322 -28.858 -15.199 1.00 21.58 ?  19  LYS   B HB2  1 
ATOM   4149 H HB3  . LYS   B 1 19  ? 45.243 -28.765 -13.912 1.00 21.58 ?  19  LYS   B HB3  1 
ATOM   4150 H HG2  . LYS   B 1 19  ? 46.739 -30.276 -14.914 1.00 23.97 ?  19  LYS   B HG2  1 
ATOM   4151 H HG3  . LYS   B 1 19  ? 45.824 -30.279 -16.219 1.00 23.97 ?  19  LYS   B HG3  1 
ATOM   4152 H HD2  . LYS   B 1 19  ? 46.229 -27.967 -16.470 1.00 26.57 ?  19  LYS   B HD2  1 
ATOM   4153 H HD3  . LYS   B 1 19  ? 47.206 -28.022 -15.216 1.00 26.57 ?  19  LYS   B HD3  1 
ATOM   4154 H HE2  . LYS   B 1 19  ? 48.617 -29.465 -16.413 1.00 29.18 ?  19  LYS   B HE2  1 
ATOM   4155 H HE3  . LYS   B 1 19  ? 47.661 -29.322 -17.676 1.00 29.18 ?  19  LYS   B HE3  1 
ATOM   4156 H HZ1  . LYS   B 1 19  ? 49.359 -27.898 -17.951 1.00 30.79 ?  19  LYS   B HZ1  1 
ATOM   4157 H HZ2  . LYS   B 1 19  ? 48.210 -27.066 -17.659 1.00 30.79 ?  19  LYS   B HZ2  1 
ATOM   4158 H HZ3  . LYS   B 1 19  ? 49.201 -27.318 -16.634 1.00 30.79 ?  19  LYS   B HZ3  1 
ATOM   4159 N N    . ASN   B 1 20  ? 45.728 -32.250 -13.384 1.00 17.61 ?  20  ASN   B N    1 
ATOM   4160 C CA   . ASN   B 1 20  ? 46.757 -32.880 -12.564 1.00 18.55 ?  20  ASN   B CA   1 
ATOM   4161 C C    . ASN   B 1 20  ? 48.036 -32.068 -12.744 1.00 19.25 ?  20  ASN   B C    1 
ATOM   4162 O O    . ASN   B 1 20  ? 48.687 -32.159 -13.792 1.00 21.35 ?  20  ASN   B O    1 
ATOM   4163 C CB   . ASN   B 1 20  ? 46.933 -34.330 -13.015 1.00 20.38 ?  20  ASN   B CB   1 
ATOM   4164 C CG   . ASN   B 1 20  ? 48.094 -35.042 -12.331 1.00 21.81 ?  20  ASN   B CG   1 
ATOM   4165 O OD1  . ASN   B 1 20  ? 48.761 -35.884 -12.943 1.00 24.31 ?  20  ASN   B OD1  1 
ATOM   4166 N ND2  . ASN   B 1 20  ? 48.324 -34.735 -11.064 1.00 21.37 ?  20  ASN   B ND2  1 
ATOM   4167 H H    . ASN   B 1 20  ? 45.618 -32.615 -14.153 1.00 21.28 ?  20  ASN   B H    1 
ATOM   4168 H HA   . ASN   B 1 20  ? 46.480 -32.864 -11.630 1.00 22.41 ?  20  ASN   B HA   1 
ATOM   4169 H HB2  . ASN   B 1 20  ? 46.117 -34.821 -12.812 1.00 24.60 ?  20  ASN   B HB2  1 
ATOM   4170 H HB3  . ASN   B 1 20  ? 47.089 -34.337 -13.970 1.00 24.60 ?  20  ASN   B HB3  1 
ATOM   4171 H HD21 . ASN   B 1 20  ? 48.970 -35.110 -10.643 1.00 25.79 ?  20  ASN   B HD21 1 
ATOM   4172 H HD22 . ASN   B 1 20  ? 47.832 -34.152 -10.659 1.00 25.79 ?  20  ASN   B HD22 1 
ATOM   4173 N N    . ALA   B 1 21  ? 48.396 -31.267 -11.739 1.00 18.59 ?  21  ALA   B N    1 
ATOM   4174 C CA   . ALA   B 1 21  ? 49.494 -30.329 -11.898 1.00 19.41 ?  21  ALA   B CA   1 
ATOM   4175 C C    . ALA   B 1 21  ? 49.954 -29.828 -10.537 1.00 18.44 ?  21  ALA   B C    1 
ATOM   4176 O O    . ALA   B 1 21  ? 49.212 -29.859 -9.551  1.00 18.27 ?  21  ALA   B O    1 
ATOM   4177 C CB   . ALA   B 1 21  ? 49.077 -29.156 -12.785 1.00 20.59 ?  21  ALA   B CB   1 
ATOM   4178 H H    . ALA   B 1 21  ? 48.019 -31.256 -10.959 1.00 22.45 ?  21  ALA   B H    1 
ATOM   4179 H HA   . ALA   B 1 21  ? 50.235 -30.788 -12.319 1.00 23.44 ?  21  ALA   B HA   1 
ATOM   4180 H HB1  . ALA   B 1 21  ? 49.854 -28.617 -12.958 1.00 24.86 ?  21  ALA   B HB1  1 
ATOM   4181 H HB2  . ALA   B 1 21  ? 48.723 -29.514 -13.616 1.00 24.86 ?  21  ALA   B HB2  1 
ATOM   4182 H HB3  . ALA   B 1 21  ? 48.393 -28.646 -12.327 1.00 24.86 ?  21  ALA   B HB3  1 
ATOM   4183 N N    . ASP   B 1 22  ? 51.209 -29.377 -10.514 1.00 17.89 ?  22  ASP   B N    1 
ATOM   4184 C CA   . ASP   B 1 22  ? 51.823 -28.693 -9.380  1.00 17.09 ?  22  ASP   B CA   1 
ATOM   4185 C C    . ASP   B 1 22  ? 51.423 -27.222 -9.457  1.00 15.52 ?  22  ASP   B C    1 
ATOM   4186 O O    . ASP   B 1 22  ? 51.742 -26.547 -10.439 1.00 15.97 ?  22  ASP   B O    1 
ATOM   4187 C CB   . ASP   B 1 22  ? 53.340 -28.874 -9.532  1.00 18.83 ?  22  ASP   B CB   1 
ATOM   4188 C CG   . ASP   B 1 22  ? 54.173 -28.117 -8.500  1.00 20.60 ?  22  ASP   B CG   1 
ATOM   4189 O OD1  . ASP   B 1 22  ? 53.807 -27.006 -8.083  1.00 20.91 ?  22  ASP   B OD1  1 
ATOM   4190 O OD2  . ASP   B 1 22  ? 55.257 -28.633 -8.136  1.00 22.61 -1 22  ASP   B OD2  1 
ATOM   4191 H H    . ASP   B 1 22  ? 51.752 -29.464 -11.181 1.00 21.61 ?  22  ASP   B H    1 
ATOM   4192 H HA   . ASP   B 1 22  ? 51.527 -29.083 -8.539  1.00 20.66 ?  22  ASP   B HA   1 
ATOM   4193 H HB2  . ASP   B 1 22  ? 53.561 -29.808 -9.447  1.00 22.74 ?  22  ASP   B HB2  1 
ATOM   4194 H HB3  . ASP   B 1 22  ? 53.607 -28.542 -10.403 1.00 22.74 ?  22  ASP   B HB3  1 
ATOM   4195 N N    . ILE   B 1 23  ? 50.714 -26.730 -8.435  1.00 14.93 ?  23  ILE   B N    1 
ATOM   4196 C CA   . ILE   B 1 23  ? 50.125 -25.387 -8.503  1.00 14.08 ?  23  ILE   B CA   1 
ATOM   4197 C C    . ILE   B 1 23  ? 51.183 -24.299 -8.647  1.00 13.66 ?  23  ILE   B C    1 
ATOM   4198 O O    . ILE   B 1 23  ? 50.918 -23.257 -9.258  1.00 13.50 ?  23  ILE   B O    1 
ATOM   4199 C CB   . ILE   B 1 23  ? 49.198 -25.137 -7.298  1.00 14.43 ?  23  ILE   B CB   1 
ATOM   4200 C CG1  . ILE   B 1 23  ? 48.371 -23.867 -7.508  1.00 15.17 ?  23  ILE   B CG1  1 
ATOM   4201 C CG2  . ILE   B 1 23  ? 49.976 -25.095 -6.002  1.00 15.62 ?  23  ILE   B CG2  1 
ATOM   4202 C CD1  . ILE   B 1 23  ? 47.242 -23.707 -6.506  1.00 15.75 ?  23  ILE   B CD1  1 
ATOM   4203 H H    . ILE   B 1 23  ? 50.566 -27.148 -7.699  1.00 18.06 ?  23  ILE   B H    1 
ATOM   4204 H HA   . ILE   B 1 23  ? 49.572 -25.345 -9.295  1.00 17.05 ?  23  ILE   B HA   1 
ATOM   4205 H HB   . ILE   B 1 23  ? 48.582 -25.882 -7.244  1.00 17.46 ?  23  ILE   B HB   1 
ATOM   4206 H HG12 . ILE   B 1 23  ? 48.958 -23.096 -7.425  1.00 18.36 ?  23  ILE   B HG12 1 
ATOM   4207 H HG13 . ILE   B 1 23  ? 47.987 -23.889 -8.399  1.00 18.36 ?  23  ILE   B HG13 1 
ATOM   4208 H HG21 . ILE   B 1 23  ? 49.355 -25.085 -5.258  1.00 18.89 ?  23  ILE   B HG21 1 
ATOM   4209 H HG22 . ILE   B 1 23  ? 50.545 -25.880 -5.947  1.00 18.89 ?  23  ILE   B HG22 1 
ATOM   4210 H HG23 . ILE   B 1 23  ? 50.524 -24.292 -5.985  1.00 18.89 ?  23  ILE   B HG23 1 
ATOM   4211 H HD11 . ILE   B 1 23  ? 46.724 -22.925 -6.740  1.00 19.05 ?  23  ILE   B HD11 1 
ATOM   4212 H HD12 . ILE   B 1 23  ? 46.681 -24.501 -6.544  1.00 19.05 ?  23  ILE   B HD12 1 
ATOM   4213 H HD13 . ILE   B 1 23  ? 47.618 -23.611 -5.620  1.00 19.05 ?  23  ILE   B HD13 1 
ATOM   4214 N N    . VAL   B 1 24  ? 52.378 -24.505 -8.086  1.00 14.08 ?  24  VAL   B N    1 
ATOM   4215 C CA   . VAL   B 1 24  ? 53.453 -23.522 -8.244  1.00 14.71 ?  24  VAL   B CA   1 
ATOM   4216 C C    . VAL   B 1 24  ? 53.911 -23.469 -9.694  1.00 15.08 ?  24  VAL   B C    1 
ATOM   4217 O O    . VAL   B 1 24  ? 54.057 -22.390 -10.284 1.00 15.56 ?  24  VAL   B O    1 
ATOM   4218 C CB   . VAL   B 1 24  ? 54.632 -23.842 -7.302  1.00 15.56 ?  24  VAL   B CB   1 
ATOM   4219 C CG1  . VAL   B 1 24  ? 55.847 -22.960 -7.633  1.00 16.45 ?  24  VAL   B CG1  1 
ATOM   4220 C CG2  . VAL   B 1 24  ? 54.224 -23.656 -5.865  1.00 16.53 ?  24  VAL   B CG2  1 
ATOM   4221 H H    . VAL   B 1 24  ? 52.590 -25.191 -7.616  1.00 17.05 ?  24  VAL   B H    1 
ATOM   4222 H HA   . VAL   B 1 24  ? 53.115 -22.645 -8.004  1.00 17.79 ?  24  VAL   B HA   1 
ATOM   4223 H HB   . VAL   B 1 24  ? 54.891 -24.768 -7.417  1.00 18.83 ?  24  VAL   B HB   1 
ATOM   4224 H HG11 . VAL   B 1 24  ? 56.451 -22.955 -6.872  1.00 19.88 ?  24  VAL   B HG11 1 
ATOM   4225 H HG12 . VAL   B 1 24  ? 56.300 -23.324 -8.409  1.00 19.88 ?  24  VAL   B HG12 1 
ATOM   4226 H HG13 . VAL   B 1 24  ? 55.543 -22.057 -7.816  1.00 19.88 ?  24  VAL   B HG13 1 
ATOM   4227 H HG21 . VAL   B 1 24  ? 54.943 -23.956 -5.290  1.00 19.99 ?  24  VAL   B HG21 1 
ATOM   4228 H HG22 . VAL   B 1 24  ? 54.045 -22.715 -5.709  1.00 19.99 ?  24  VAL   B HG22 1 
ATOM   4229 H HG23 . VAL   B 1 24  ? 53.423 -24.177 -5.694  1.00 19.99 ?  24  VAL   B HG23 1 
ATOM   4230 N N    . GLU   B 1 25  ? 54.166 -24.639 -10.287 1.00 16.22 ?  25  GLU   B N    1 
ATOM   4231 C CA   . GLU   B 1 25  ? 54.565 -24.674 -11.688 1.00 17.98 ?  25  GLU   B CA   1 
ATOM   4232 C C    . GLU   B 1 25  ? 53.460 -24.130 -12.580 1.00 16.32 ?  25  GLU   B C    1 
ATOM   4233 O O    . GLU   B 1 25  ? 53.728 -23.421 -13.559 1.00 17.44 ?  25  GLU   B O    1 
ATOM   4234 C CB   . GLU   B 1 25  ? 54.965 -26.098 -12.079 1.00 22.07 ?  25  GLU   B CB   1 
ATOM   4235 C CG   . GLU   B 1 25  ? 56.256 -26.552 -11.409 1.00 27.98 ?  25  GLU   B CG   1 
ATOM   4236 C CD   . GLU   B 1 25  ? 57.379 -25.528 -11.512 1.00 33.59 ?  25  GLU   B CD   1 
ATOM   4237 O OE1  . GLU   B 1 25  ? 57.758 -25.165 -12.647 1.00 35.65 ?  25  GLU   B OE1  1 
ATOM   4238 O OE2  . GLU   B 1 25  ? 57.871 -25.070 -10.455 1.00 35.51 -1 25  GLU   B OE2  1 
ATOM   4239 H H    . GLU   B 1 25  ? 54.111 -25.407 -9.904  1.00 19.61 ?  25  GLU   B H    1 
ATOM   4240 H HA   . GLU   B 1 25  ? 55.326 -24.093 -11.807 1.00 21.72 ?  25  GLU   B HA   1 
ATOM   4241 H HB2  . GLU   B 1 25  ? 54.259 -26.712 -11.809 1.00 26.63 ?  25  GLU   B HB2  1 
ATOM   4242 H HB3  . GLU   B 1 25  ? 55.089 -26.141 -13.039 1.00 26.63 ?  25  GLU   B HB3  1 
ATOM   4243 H HG2  . GLU   B 1 25  ? 56.094 -26.690 -10.468 1.00 33.72 ?  25  GLU   B HG2  1 
ATOM   4244 H HG3  . GLU   B 1 25  ? 56.556 -27.373 -11.828 1.00 33.72 ?  25  GLU   B HG3  1 
ATOM   4245 N N    A GLU   B 1 26  ? 52.206 -24.442 -12.250 0.86 15.70 ?  26  GLU   B N    1 
ATOM   4246 N N    B GLU   B 1 26  ? 52.204 -24.441 -12.250 0.14 15.89 ?  26  GLU   B N    1 
ATOM   4247 C CA   A GLU   B 1 26  ? 51.083 -23.910 -13.017 0.86 16.01 ?  26  GLU   B CA   1 
ATOM   4248 C CA   B GLU   B 1 26  ? 51.084 -23.906 -13.018 0.14 15.65 ?  26  GLU   B CA   1 
ATOM   4249 C C    A GLU   B 1 26  ? 51.029 -22.392 -12.935 0.86 15.01 ?  26  GLU   B C    1 
ATOM   4250 C C    B GLU   B 1 26  ? 51.041 -22.388 -12.937 0.14 14.98 ?  26  GLU   B C    1 
ATOM   4251 O O    A GLU   B 1 26  ? 50.812 -21.718 -13.946 0.86 16.32 ?  26  GLU   B O    1 
ATOM   4252 O O    B GLU   B 1 26  ? 50.871 -21.705 -13.953 0.14 15.28 ?  26  GLU   B O    1 
ATOM   4253 C CB   A GLU   B 1 26  ? 49.764 -24.497 -12.511 0.86 18.58 ?  26  GLU   B CB   1 
ATOM   4254 C CB   B GLU   B 1 26  ? 49.770 -24.500 -12.513 0.14 16.27 ?  26  GLU   B CB   1 
ATOM   4255 C CG   A GLU   B 1 26  ? 49.321 -25.765 -13.213 0.86 22.27 ?  26  GLU   B CG   1 
ATOM   4256 C CG   B GLU   B 1 26  ? 49.413 -25.829 -13.141 0.14 17.05 ?  26  GLU   B CG   1 
ATOM   4257 C CD   A GLU   B 1 26  ? 49.034 -25.559 -14.703 0.86 23.70 ?  26  GLU   B CD   1 
ATOM   4258 C CD   B GLU   B 1 26  ? 49.194 -25.758 -14.637 0.14 17.22 ?  26  GLU   B CD   1 
ATOM   4259 O OE1  A GLU   B 1 26  ? 47.998 -24.959 -15.073 0.86 23.92 ?  26  GLU   B OE1  1 
ATOM   4260 O OE1  B GLU   B 1 26  ? 48.431 -24.883 -15.094 0.14 17.03 ?  26  GLU   B OE1  1 
ATOM   4261 O OE2  A GLU   B 1 26  ? 49.855 -26.012 -15.511 0.86 25.72 -1 26  GLU   B OE2  1 
ATOM   4262 O OE2  B GLU   B 1 26  ? 49.782 -26.593 -15.355 0.14 17.40 -1 26  GLU   B OE2  1 
ATOM   4263 H H    A GLU   B 1 26  ? 51.977 -24.958 -11.596 0.86 18.99 ?  26  GLU   B H    1 
ATOM   4264 H H    B GLU   B 1 26  ? 51.977 -24.952 -11.595 0.14 19.22 ?  26  GLU   B H    1 
ATOM   4265 H HA   A GLU   B 1 26  ? 51.190 -24.158 -13.947 0.86 19.36 ?  26  GLU   B HA   1 
ATOM   4266 H HA   B GLU   B 1 26  ? 51.191 -24.153 -13.947 0.14 18.93 ?  26  GLU   B HA   1 
ATOM   4267 H HB2  A GLU   B 1 26  ? 49.854 -24.699 -11.567 0.86 22.45 ?  26  GLU   B HB2  1 
ATOM   4268 H HB2  B GLU   B 1 26  ? 49.839 -24.641 -11.552 0.14 19.68 ?  26  GLU   B HB2  1 
ATOM   4269 H HB3  A GLU   B 1 26  ? 49.063 -23.836 -12.636 0.86 22.45 ?  26  GLU   B HB3  1 
ATOM   4270 H HB3  B GLU   B 1 26  ? 49.051 -23.877 -12.698 0.14 19.68 ?  26  GLU   B HB3  1 
ATOM   4271 H HG2  A GLU   B 1 26  ? 50.024 -26.427 -13.122 0.86 26.87 ?  26  GLU   B HG2  1 
ATOM   4272 H HG2  B GLU   B 1 26  ? 50.141 -26.441 -12.996 0.14 20.60 ?  26  GLU   B HG2  1 
ATOM   4273 H HG3  A GLU   B 1 26  ? 48.506 -26.087 -12.797 0.86 26.87 ?  26  GLU   B HG3  1 
ATOM   4274 H HG3  B GLU   B 1 26  ? 48.598 -26.156 -12.736 0.14 20.60 ?  26  GLU   B HG3  1 
ATOM   4275 N N    . ALA   B 1 27  ? 51.187 -21.839 -11.729 1.00 14.33 ?  27  ALA   B N    1 
ATOM   4276 C CA   . ALA   B 1 27  ? 51.147 -20.389 -11.578 1.00 14.82 ?  27  ALA   B CA   1 
ATOM   4277 C C    . ALA   B 1 27  ? 52.223 -19.723 -12.425 1.00 15.65 ?  27  ALA   B C    1 
ATOM   4278 O O    . ALA   B 1 27  ? 51.963 -18.720 -13.105 1.00 16.34 ?  27  ALA   B O    1 
ATOM   4279 C CB   . ALA   B 1 27  ? 51.283 -20.009 -10.105 1.00 15.21 ?  27  ALA   B CB   1 
ATOM   4280 H H    A ALA   B 1 27  ? 51.310 -22.276 -10.997 0.86 17.34 ?  27  ALA   B H    1 
ATOM   4281 H H    B ALA   B 1 27  ? 51.310 -22.277 -10.998 0.14 17.34 ?  27  ALA   B H    1 
ATOM   4282 H HA   . ALA   B 1 27  ? 50.291 -20.065 -11.886 1.00 17.94 ?  27  ALA   B HA   1 
ATOM   4283 H HB1  . ALA   B 1 27  ? 51.249 -19.043 -10.023 1.00 18.40 ?  27  ALA   B HB1  1 
ATOM   4284 H HB2  . ALA   B 1 27  ? 50.546 -20.406 -9.609  1.00 18.40 ?  27  ALA   B HB2  1 
ATOM   4285 H HB3  . ALA   B 1 27  ? 52.126 -20.343 -9.765  1.00 18.40 ?  27  ALA   B HB3  1 
ATOM   4286 N N    . LYS   B 1 28  ? 53.435 -20.282 -12.424 1.00 17.19 ?  28  LYS   B N    1 
ATOM   4287 C CA   . LYS   B 1 28  ? 54.510 -19.664 -13.192 1.00 19.25 ?  28  LYS   B CA   1 
ATOM   4288 C C    . LYS   B 1 28  ? 54.248 -19.736 -14.693 1.00 20.49 ?  28  LYS   B C    1 
ATOM   4289 O O    . LYS   B 1 28  ? 54.666 -18.840 -15.435 1.00 21.55 ?  28  LYS   B O    1 
ATOM   4290 C CB   . LYS   B 1 28  ? 55.867 -20.268 -12.810 1.00 22.13 ?  28  LYS   B CB   1 
ATOM   4291 C CG   . LYS   B 1 28  ? 56.275 -19.937 -11.376 1.00 25.00 ?  28  LYS   B CG   1 
ATOM   4292 C CD   . LYS   B 1 28  ? 57.711 -20.327 -11.051 1.00 29.20 ?  28  LYS   B CD   1 
ATOM   4293 C CE   . LYS   B 1 28  ? 57.829 -21.795 -10.717 1.00 32.19 ?  28  LYS   B CE   1 
ATOM   4294 N NZ   . LYS   B 1 28  ? 59.183 -22.126 -10.188 1.00 33.16 ?  28  LYS   B NZ   1 
ATOM   4295 H H    . LYS   B 1 28  ? 53.655 -20.998 -12.002 1.00 20.78 ?  28  LYS   B H    1 
ATOM   4296 H HA   . LYS   B 1 28  ? 54.545 -18.725 -12.962 1.00 23.24 ?  28  LYS   B HA   1 
ATOM   4297 H HB2  . LYS   B 1 28  ? 55.822 -21.230 -12.891 1.00 26.70 ?  28  LYS   B HB2  1 
ATOM   4298 H HB3  . LYS   B 1 28  ? 56.550 -19.913 -13.402 1.00 26.70 ?  28  LYS   B HB3  1 
ATOM   4299 H HG2  . LYS   B 1 28  ? 56.184 -18.979 -11.242 1.00 30.15 ?  28  LYS   B HG2  1 
ATOM   4300 H HG3  . LYS   B 1 28  ? 55.687 -20.411 -10.770 1.00 30.15 ?  28  LYS   B HG3  1 
ATOM   4301 H HD2  . LYS   B 1 28  ? 58.271 -20.141 -11.820 1.00 35.18 ?  28  LYS   B HD2  1 
ATOM   4302 H HD3  . LYS   B 1 28  ? 58.009 -19.812 -10.285 1.00 35.18 ?  28  LYS   B HD3  1 
ATOM   4303 H HE2  . LYS   B 1 28  ? 57.173 -22.024 -10.038 1.00 38.78 ?  28  LYS   B HE2  1 
ATOM   4304 H HE3  . LYS   B 1 28  ? 57.678 -22.321 -11.518 1.00 38.78 ?  28  LYS   B HE3  1 
ATOM   4305 H HZ1  . LYS   B 1 28  ? 59.233 -22.994 -9.997  1.00 39.94 ?  28  LYS   B HZ1  1 
ATOM   4306 H HZ2  . LYS   B 1 28  ? 59.804 -21.928 -10.794 1.00 39.94 ?  28  LYS   B HZ2  1 
ATOM   4307 H HZ3  . LYS   B 1 28  ? 59.344 -21.658 -9.447  1.00 39.94 ?  28  LYS   B HZ3  1 
ATOM   4308 N N    A LYS   B 1 29  ? 53.559 -20.779 -15.154 0.86 21.46 ?  29  LYS   B N    1 
ATOM   4309 N N    B LYS   B 1 29  ? 53.540 -20.768 -15.155 0.14 21.90 ?  29  LYS   B N    1 
ATOM   4310 C CA   A LYS   B 1 29  ? 53.270 -20.919 -16.578 0.86 24.06 ?  29  LYS   B CA   1 
ATOM   4311 C CA   B LYS   B 1 29  ? 53.271 -20.908 -16.582 0.14 23.59 ?  29  LYS   B CA   1 
ATOM   4312 C C    A LYS   B 1 29  ? 52.019 -20.156 -17.000 0.86 23.20 ?  29  LYS   B C    1 
ATOM   4313 C C    B LYS   B 1 29  ? 52.004 -20.178 -17.017 0.14 22.69 ?  29  LYS   B C    1 
ATOM   4314 O O    A LYS   B 1 29  ? 52.015 -19.519 -18.058 0.86 24.37 ?  29  LYS   B O    1 
ATOM   4315 O O    B LYS   B 1 29  ? 51.980 -19.571 -18.093 0.14 22.91 ?  29  LYS   B O    1 
ATOM   4316 C CB   A LYS   B 1 29  ? 53.140 -22.398 -16.941 0.86 28.15 ?  29  LYS   B CB   1 
ATOM   4317 C CB   B LYS   B 1 29  ? 53.172 -22.389 -16.958 0.14 26.31 ?  29  LYS   B CB   1 
ATOM   4318 C CG   A LYS   B 1 29  ? 52.983 -22.662 -18.426 0.86 32.10 ?  29  LYS   B CG   1 
ATOM   4319 C CG   B LYS   B 1 29  ? 53.008 -22.637 -18.452 0.14 28.81 ?  29  LYS   B CG   1 
ATOM   4320 C CD   A LYS   B 1 29  ? 53.195 -24.130 -18.751 0.86 35.07 ?  29  LYS   B CD   1 
ATOM   4321 C CD   B LYS   B 1 29  ? 53.228 -24.101 -18.803 0.14 30.80 ?  29  LYS   B CD   1 
ATOM   4322 C CE   A LYS   B 1 29  ? 52.090 -25.002 -18.175 0.86 37.06 ?  29  LYS   B CE   1 
ATOM   4323 C CE   B LYS   B 1 29  ? 52.196 -25.001 -18.139 0.14 32.16 ?  29  LYS   B CE   1 
ATOM   4324 N NZ   A LYS   B 1 29  ? 52.300 -26.442 -18.496 0.86 38.22 ?  29  LYS   B NZ   1 
ATOM   4325 N NZ   B LYS   B 1 29  ? 52.413 -26.433 -18.478 0.14 32.93 ?  29  LYS   B NZ   1 
ATOM   4326 H H    A LYS   B 1 29  ? 53.261 -21.416 -14.663 0.86 25.90 ?  29  LYS   B H    1 
ATOM   4327 H H    B LYS   B 1 29  ? 53.208 -21.398 -14.663 0.14 26.43 ?  29  LYS   B H    1 
ATOM   4328 H HA   A LYS   B 1 29  ? 54.009 -20.556 -17.079 0.86 29.03 ?  29  LYS   B HA   1 
ATOM   4329 H HA   B LYS   B 1 29  ? 54.014 -20.531 -17.073 0.14 28.46 ?  29  LYS   B HA   1 
ATOM   4330 H HB2  A LYS   B 1 29  ? 53.940 -22.858 -16.645 0.86 33.93 ?  29  LYS   B HB2  1 
ATOM   4331 H HB2  B LYS   B 1 29  ? 53.981 -22.841 -16.671 0.14 31.72 ?  29  LYS   B HB2  1 
ATOM   4332 H HB3  A LYS   B 1 29  ? 52.364 -22.763 -16.495 0.86 33.93 ?  29  LYS   B HB3  1 
ATOM   4333 H HB3  B LYS   B 1 29  ? 52.403 -22.773 -16.508 0.14 31.72 ?  29  LYS   B HB3  1 
ATOM   4334 H HG2  A LYS   B 1 29  ? 52.088 -22.416 -18.703 0.86 38.67 ?  29  LYS   B HG2  1 
ATOM   4335 H HG2  B LYS   B 1 29  ? 52.108 -22.393 -18.721 0.14 34.73 ?  29  LYS   B HG2  1 
ATOM   4336 H HG3  A LYS   B 1 29  ? 53.641 -22.144 -18.916 0.86 38.67 ?  29  LYS   B HG3  1 
ATOM   4337 H HG3  B LYS   B 1 29  ? 53.659 -22.107 -18.939 0.14 34.73 ?  29  LYS   B HG3  1 
ATOM   4338 H HD2  A LYS   B 1 29  ? 53.202 -24.245 -19.714 0.86 42.24 ?  29  LYS   B HD2  1 
ATOM   4339 H HD2  B LYS   B 1 29  ? 53.156 -24.214 -19.764 0.14 37.10 ?  29  LYS   B HD2  1 
ATOM   4340 H HD3  A LYS   B 1 29  ? 54.040 -24.421 -18.373 0.86 42.24 ?  29  LYS   B HD3  1 
ATOM   4341 H HD3  B LYS   B 1 29  ? 54.109 -24.373 -18.499 0.14 37.10 ?  29  LYS   B HD3  1 
ATOM   4342 H HE2  A LYS   B 1 29  ? 52.075 -24.907 -17.209 0.86 44.62 ?  29  LYS   B HE2  1 
ATOM   4343 H HE2  B LYS   B 1 29  ? 52.260 -24.909 -17.175 0.14 38.74 ?  29  LYS   B HE2  1 
ATOM   4344 H HE3  A LYS   B 1 29  ? 51.238 -24.727 -18.550 0.86 44.62 ?  29  LYS   B HE3  1 
ATOM   4345 H HE3  B LYS   B 1 29  ? 51.310 -24.746 -18.441 0.14 38.74 ?  29  LYS   B HE3  1 
ATOM   4346 H HZ1  A LYS   B 1 29  ? 51.642 -26.931 -18.149 0.86 46.02 ?  29  LYS   B HZ1  1 
ATOM   4347 H HZ1  B LYS   B 1 29  ? 51.798 -26.937 -18.078 0.14 39.67 ?  29  LYS   B HZ1  1 
ATOM   4348 H HZ2  A LYS   B 1 29  ? 52.312 -26.559 -19.378 0.86 46.02 ?  29  LYS   B HZ2  1 
ATOM   4349 H HZ2  B LYS   B 1 29  ? 52.354 -26.549 -19.358 0.14 39.67 ?  29  LYS   B HZ2  1 
ATOM   4350 H HZ3  A LYS   B 1 29  ? 53.075 -26.720 -18.157 0.86 46.02 ?  29  LYS   B HZ3  1 
ATOM   4351 H HZ3  B LYS   B 1 29  ? 53.220 -26.691 -18.206 0.14 39.67 ?  29  LYS   B HZ3  1 
ATOM   4352 N N    . VAL   B 1 30  ? 50.948 -20.227 -16.202 1.00 21.73 ?  30  VAL   B N    1 
ATOM   4353 C CA   . VAL   B 1 30  ? 49.665 -19.626 -16.584 1.00 21.22 ?  30  VAL   B CA   1 
ATOM   4354 C C    . VAL   B 1 30  ? 49.659 -18.110 -16.431 1.00 19.96 ?  30  VAL   B C    1 
ATOM   4355 O O    . VAL   B 1 30  ? 48.913 -17.410 -17.133 1.00 20.76 ?  30  VAL   B O    1 
ATOM   4356 C CB   . VAL   B 1 30  ? 48.553 -20.255 -15.721 1.00 22.61 ?  30  VAL   B CB   1 
ATOM   4357 C CG1  . VAL   B 1 30  ? 47.263 -19.449 -15.805 1.00 23.18 ?  30  VAL   B CG1  1 
ATOM   4358 C CG2  . VAL   B 1 30  ? 48.326 -21.705 -16.117 1.00 23.58 ?  30  VAL   B CG2  1 
ATOM   4359 H H    A VAL   B 1 30  ? 50.931 -20.635 -15.441 0.86 26.22 ?  30  VAL   B H    1 
ATOM   4360 H H    B VAL   B 1 30  ? 50.940 -20.614 -15.429 0.14 26.22 ?  30  VAL   B H    1 
ATOM   4361 H HA   . VAL   B 1 30  ? 49.477 -19.853 -17.510 1.00 25.61 ?  30  VAL   B HA   1 
ATOM   4362 H HB   . VAL   B 1 30  ? 48.837 -20.257 -14.795 1.00 27.28 ?  30  VAL   B HB   1 
ATOM   4363 H HG11 . VAL   B 1 30  ? 46.520 -20.031 -15.572 1.00 27.97 ?  30  VAL   B HG11 1 
ATOM   4364 H HG12 . VAL   B 1 30  ? 47.306 -18.712 -15.180 1.00 27.97 ?  30  VAL   B HG12 1 
ATOM   4365 H HG13 . VAL   B 1 30  ? 47.145 -19.128 -16.708 1.00 27.97 ?  30  VAL   B HG13 1 
ATOM   4366 H HG21 . VAL   B 1 30  ? 47.627 -22.083 -15.556 1.00 28.44 ?  30  VAL   B HG21 1 
ATOM   4367 H HG22 . VAL   B 1 30  ? 48.052 -21.740 -17.048 1.00 28.44 ?  30  VAL   B HG22 1 
ATOM   4368 H HG23 . VAL   B 1 30  ? 49.149 -22.200 -15.995 1.00 28.44 ?  30  VAL   B HG23 1 
ATOM   4369 N N    . LYS   B 1 31  ? 50.436 -17.593 -15.494 1.00 19.42 ?  31  LYS   B N    1 
ATOM   4370 C CA   . LYS   B 1 31  ? 50.458 -16.179 -15.147 1.00 19.88 ?  31  LYS   B CA   1 
ATOM   4371 C C    . LYS   B 1 31  ? 49.063 -15.704 -14.744 1.00 17.68 ?  31  LYS   B C    1 
ATOM   4372 O O    . LYS   B 1 31  ? 48.518 -14.782 -15.360 1.00 18.78 ?  31  LYS   B O    1 
ATOM   4373 C CB   . LYS   B 1 31  ? 51.075 -15.370 -16.294 1.00 23.22 ?  31  LYS   B CB   1 
ATOM   4374 C CG   . LYS   B 1 31  ? 52.520 -15.782 -16.596 1.00 26.59 ?  31  LYS   B CG   1 
ATOM   4375 C CD   . LYS   B 1 31  ? 53.097 -15.027 -17.775 1.00 30.03 ?  31  LYS   B CD   1 
ATOM   4376 C CE   . LYS   B 1 31  ? 54.582 -15.300 -17.920 1.00 32.78 ?  31  LYS   B CE   1 
ATOM   4377 N NZ   . LYS   B 1 31  ? 55.326 -14.904 -16.691 1.00 33.82 ?  31  LYS   B NZ   1 
ATOM   4378 H H    . LYS   B 1 31  ? 50.974 -18.071 -15.033 1.00 23.46 ?  31  LYS   B H    1 
ATOM   4379 H HA   . LYS   B 1 31  ? 51.025 -16.082 -14.381 1.00 24.00 ?  31  LYS   B HA   1 
ATOM   4380 H HB2  . LYS   B 1 31  ? 50.553 -15.503 -17.101 1.00 28.01 ?  31  LYS   B HB2  1 
ATOM   4381 H HB3  . LYS   B 1 31  ? 51.076 -14.435 -16.047 1.00 28.01 ?  31  LYS   B HB3  1 
ATOM   4382 H HG2  . LYS   B 1 31  ? 53.068 -15.600 -15.817 1.00 32.06 ?  31  LYS   B HG2  1 
ATOM   4383 H HG3  . LYS   B 1 31  ? 52.547 -16.731 -16.805 1.00 32.06 ?  31  LYS   B HG3  1 
ATOM   4384 H HD2  . LYS   B 1 31  ? 52.653 -15.316 -18.587 1.00 36.18 ?  31  LYS   B HD2  1 
ATOM   4385 H HD3  . LYS   B 1 31  ? 52.972 -14.078 -17.638 1.00 36.18 ?  31  LYS   B HD3  1 
ATOM   4386 H HE2  . LYS   B 1 31  ? 54.724 -16.250 -18.068 1.00 39.48 ?  31  LYS   B HE2  1 
ATOM   4387 H HE3  . LYS   B 1 31  ? 54.933 -14.789 -18.666 1.00 39.48 ?  31  LYS   B HE3  1 
ATOM   4388 H HZ1  . LYS   B 1 31  ? 56.203 -14.931 -16.842 1.00 40.73 ?  31  LYS   B HZ1  1 
ATOM   4389 H HZ2  . LYS   B 1 31  ? 55.099 -14.077 -16.453 1.00 40.73 ?  31  LYS   B HZ2  1 
ATOM   4390 H HZ3  . LYS   B 1 31  ? 55.131 -15.459 -16.023 1.00 40.73 ?  31  LYS   B HZ3  1 
ATOM   4391 N N    . PRO   B 1 32  ? 48.460 -16.298 -13.708 1.00 15.29 ?  32  PRO   B N    1 
ATOM   4392 C CA   . PRO   B 1 32  ? 47.080 -15.943 -13.347 1.00 14.65 ?  32  PRO   B CA   1 
ATOM   4393 C C    . PRO   B 1 32  ? 46.993 -14.604 -12.634 1.00 14.51 ?  32  PRO   B C    1 
ATOM   4394 O O    . PRO   B 1 32  ? 47.916 -14.179 -11.936 1.00 15.76 ?  32  PRO   B O    1 
ATOM   4395 C CB   . PRO   B 1 32  ? 46.688 -17.063 -12.376 1.00 14.94 ?  32  PRO   B CB   1 
ATOM   4396 C CG   . PRO   B 1 32  ? 47.995 -17.403 -11.704 1.00 15.27 ?  32  PRO   B CG   1 
ATOM   4397 C CD   . PRO   B 1 32  ? 49.042 -17.277 -12.769 1.00 15.53 ?  32  PRO   B CD   1 
ATOM   4398 H HA   . PRO   B 1 32  ? 46.493 -15.955 -14.125 1.00 17.72 ?  32  PRO   B HA   1 
ATOM   4399 H HB2  . PRO   B 1 32  ? 46.039 -16.734 -11.732 1.00 18.07 ?  32  PRO   B HB2  1 
ATOM   4400 H HB3  . PRO   B 1 32  ? 46.340 -17.824 -12.865 1.00 18.07 ?  32  PRO   B HB3  1 
ATOM   4401 H HG2  . PRO   B 1 32  ? 48.168 -16.769 -10.985 1.00 18.47 ?  32  PRO   B HG2  1 
ATOM   4402 H HG3  . PRO   B 1 32  ? 47.967 -18.307 -11.362 1.00 18.47 ?  32  PRO   B HG3  1 
ATOM   4403 H HD2  . PRO   B 1 32  ? 49.865 -16.929 -12.396 1.00 18.78 ?  32  PRO   B HD2  1 
ATOM   4404 H HD3  . PRO   B 1 32  ? 49.176 -18.126 -13.209 1.00 18.78 ?  32  PRO   B HD3  1 
ATOM   4405 N N    . THR   B 1 33  ? 45.840 -13.948 -12.802 1.00 14.19 ?  33  THR   B N    1 
ATOM   4406 C CA   . THR   B 1 33  ? 45.549 -12.770 -11.994 1.00 14.48 ?  33  THR   B CA   1 
ATOM   4407 C C    . THR   B 1 33  ? 45.501 -13.121 -10.513 1.00 14.09 ?  33  THR   B C    1 
ATOM   4408 O O    . THR   B 1 33  ? 45.973 -12.345 -9.670  1.00 14.95 ?  33  THR   B O    1 
ATOM   4409 C CB   . THR   B 1 33  ? 44.230 -12.134 -12.441 1.00 15.15 ?  33  THR   B CB   1 
ATOM   4410 O OG1  . THR   B 1 33  ? 44.272 -11.869 -13.845 1.00 15.15 ?  33  THR   B OG1  1 
ATOM   4411 C CG2  . THR   B 1 33  ? 43.989 -10.831 -11.693 1.00 16.36 ?  33  THR   B CG2  1 
ATOM   4412 H H    . THR   B 1 33  ? 45.218 -14.170 -13.362 1.00 17.18 ?  33  THR   B H    1 
ATOM   4413 H HA   . THR   B 1 33  ? 46.250 -12.120 -12.129 1.00 17.52 ?  33  THR   B HA   1 
ATOM   4414 H HB   . THR   B 1 33  ? 43.494 -12.740 -12.248 1.00 18.33 ?  33  THR   B HB   1 
ATOM   4415 H HG1  . THR   B 1 33  ? 43.544 -11.509 -14.096 1.00 18.33 ?  33  THR   B HG1  1 
ATOM   4416 H HG21 . THR   B 1 33  ? 43.240 -10.358 -12.082 1.00 19.78 ?  33  THR   B HG21 1 
ATOM   4417 H HG22 . THR   B 1 33  ? 43.799 -11.014 -10.760 1.00 19.78 ?  33  THR   B HG22 1 
ATOM   4418 H HG23 . THR   B 1 33  ? 44.781 -10.270 -11.750 1.00 19.78 ?  33  THR   B HG23 1 
ATOM   4419 N N    . VAL   B 1 34  ? 44.945 -14.289 -10.174 1.00 13.36 ?  34  VAL   B N    1 
ATOM   4420 C CA   . VAL   B 1 34  ? 44.759 -14.687 -8.782  1.00 12.71 ?  34  VAL   B CA   1 
ATOM   4421 C C    . VAL   B 1 34  ? 45.185 -16.139 -8.616  1.00 11.67 ?  34  VAL   B C    1 
ATOM   4422 O O    . VAL   B 1 34  ? 44.664 -17.028 -9.300  1.00 12.66 ?  34  VAL   B O    1 
ATOM   4423 C CB   . VAL   B 1 34  ? 43.287 -14.533 -8.339  1.00 13.79 ?  34  VAL   B CB   1 
ATOM   4424 C CG1  . VAL   B 1 34  ? 43.117 -14.986 -6.894  1.00 14.59 ?  34  VAL   B CG1  1 
ATOM   4425 C CG2  . VAL   B 1 34  ? 42.799 -13.101 -8.531  1.00 14.75 ?  34  VAL   B CG2  1 
ATOM   4426 H H    . VAL   B 1 34  ? 44.670 -14.879 -10.740 1.00 16.18 ?  34  VAL   B H    1 
ATOM   4427 H HA   . VAL   B 1 34  ? 45.312 -14.136 -8.208  1.00 15.40 ?  34  VAL   B HA   1 
ATOM   4428 H HB   . VAL   B 1 34  ? 42.735 -15.108 -8.893  1.00 16.69 ?  34  VAL   B HB   1 
ATOM   4429 H HG11 . VAL   B 1 34  ? 42.261 -14.666 -6.562  1.00 17.66 ?  34  VAL   B HG11 1 
ATOM   4430 H HG12 . VAL   B 1 34  ? 43.138 -15.956 -6.858  1.00 17.66 ?  34  VAL   B HG12 1 
ATOM   4431 H HG13 . VAL   B 1 34  ? 43.835 -14.617 -6.359  1.00 17.66 ?  34  VAL   B HG13 1 
ATOM   4432 H HG21 . VAL   B 1 34  ? 41.882 -13.037 -8.215  1.00 17.84 ?  34  VAL   B HG21 1 
ATOM   4433 H HG22 . VAL   B 1 34  ? 43.367 -12.503 -8.028  1.00 17.84 ?  34  VAL   B HG22 1 
ATOM   4434 H HG23 . VAL   B 1 34  ? 42.834 -12.881 -9.476  1.00 17.84 ?  34  VAL   B HG23 1 
ATOM   4435 N N    . VAL   B 1 35  ? 46.087 -16.387 -7.670  1.00 11.25 ?  35  VAL   B N    1 
ATOM   4436 C CA   . VAL   B 1 35  ? 46.323 -17.733 -7.155  1.00 11.31 ?  35  VAL   B CA   1 
ATOM   4437 C C    . VAL   B 1 35  ? 45.783 -17.793 -5.735  1.00 10.91 ?  35  VAL   B C    1 
ATOM   4438 O O    . VAL   B 1 35  ? 46.001 -16.873 -4.940  1.00 11.30 ?  35  VAL   B O    1 
ATOM   4439 C CB   . VAL   B 1 35  ? 47.807 -18.161 -7.232  1.00 12.03 ?  35  VAL   B CB   1 
ATOM   4440 C CG1  . VAL   B 1 35  ? 48.711 -17.328 -6.310  1.00 12.85 ?  35  VAL   B CG1  1 
ATOM   4441 C CG2  . VAL   B 1 35  ? 47.939 -19.655 -6.918  1.00 12.79 ?  35  VAL   B CG2  1 
ATOM   4442 H H    . VAL   B 1 35  ? 46.588 -15.783 -7.310  1.00 13.65 ?  35  VAL   B H    1 
ATOM   4443 H HA   . VAL   B 1 35  ? 45.808 -18.361 -7.683  1.00 13.72 ?  35  VAL   B HA   1 
ATOM   4444 H HB   . VAL   B 1 35  ? 48.111 -18.031 -8.145  1.00 14.58 ?  35  VAL   B HB   1 
ATOM   4445 H HG11 . VAL   B 1 35  ? 49.633 -17.560 -6.486  1.00 15.57 ?  35  VAL   B HG11 1 
ATOM   4446 H HG12 . VAL   B 1 35  ? 48.559 -16.390 -6.487  1.00 15.57 ?  35  VAL   B HG12 1 
ATOM   4447 H HG13 . VAL   B 1 35  ? 48.487 -17.533 -5.386  1.00 15.57 ?  35  VAL   B HG13 1 
ATOM   4448 H HG21 . VAL   B 1 35  ? 48.860 -19.924 -7.030  1.00 15.50 ?  35  VAL   B HG21 1 
ATOM   4449 H HG22 . VAL   B 1 35  ? 47.655 -19.815 -6.002  1.00 15.50 ?  35  VAL   B HG22 1 
ATOM   4450 H HG23 . VAL   B 1 35  ? 47.371 -20.163 -7.526  1.00 15.50 ?  35  VAL   B HG23 1 
ATOM   4451 N N    . VAL   B 1 36  ? 45.066 -18.872 -5.419  1.00 10.74 ?  36  VAL   B N    1 
ATOM   4452 C CA   . VAL   B 1 36  ? 44.519 -19.082 -4.086  1.00 10.66 ?  36  VAL   B CA   1 
ATOM   4453 C C    . VAL   B 1 36  ? 45.521 -19.846 -3.227  1.00 10.40 ?  36  VAL   B C    1 
ATOM   4454 O O    . VAL   B 1 36  ? 46.068 -20.874 -3.651  1.00 11.67 ?  36  VAL   B O    1 
ATOM   4455 C CB   . VAL   B 1 36  ? 43.184 -19.842 -4.168  1.00 11.33 ?  36  VAL   B CB   1 
ATOM   4456 C CG1  . VAL   B 1 36  ? 42.673 -20.209 -2.784  1.00 11.78 ?  36  VAL   B CG1  1 
ATOM   4457 C CG2  . VAL   B 1 36  ? 42.158 -19.020 -4.927  1.00 12.02 ?  36  VAL   B CG2  1 
ATOM   4458 H H    . VAL   B 1 36  ? 44.894 -19.511 -5.970  1.00 13.03 ?  36  VAL   B H    1 
ATOM   4459 H HA   . VAL   B 1 36  ? 44.353 -18.222 -3.671  1.00 12.94 ?  36  VAL   B HA   1 
ATOM   4460 H HB   . VAL   B 1 36  ? 43.321 -20.667 -4.662  1.00 13.74 ?  36  VAL   B HB   1 
ATOM   4461 H HG11 . VAL   B 1 36  ? 41.733 -20.446 -2.847  1.00 14.28 ?  36  VAL   B HG11 1 
ATOM   4462 H HG12 . VAL   B 1 36  ? 43.181 -20.958 -2.444  1.00 14.28 ?  36  VAL   B HG12 1 
ATOM   4463 H HG13 . VAL   B 1 36  ? 42.776 -19.440 -2.199  1.00 14.28 ?  36  VAL   B HG13 1 
ATOM   4464 H HG21 . VAL   B 1 36  ? 41.317 -19.502 -4.949  1.00 14.57 ?  36  VAL   B HG21 1 
ATOM   4465 H HG22 . VAL   B 1 36  ? 42.043 -18.168 -4.482  1.00 14.57 ?  36  VAL   B HG22 1 
ATOM   4466 H HG23 . VAL   B 1 36  ? 42.478 -18.876 -5.836  1.00 14.57 ?  36  VAL   B HG23 1 
ATOM   4467 N N    . ASN   B 1 37  ? 45.747 -19.353 -2.010  1.00 11.00 ?  37  ASN   B N    1 
ATOM   4468 C CA   . ASN   B 1 37  ? 46.498 -20.077 -0.998  1.00 11.21 ?  37  ASN   B CA   1 
ATOM   4469 C C    . ASN   B 1 37  ? 45.546 -20.748 -0.011  1.00 11.28 ?  37  ASN   B C    1 
ATOM   4470 O O    . ASN   B 1 37  ? 44.540 -20.164 0.402   1.00 11.60 ?  37  ASN   B O    1 
ATOM   4471 C CB   . ASN   B 1 37  ? 47.433 -19.129 -0.243  1.00 11.20 ?  37  ASN   B CB   1 
ATOM   4472 C CG   . ASN   B 1 37  ? 48.283 -19.841 0.773   1.00 11.52 ?  37  ASN   B CG   1 
ATOM   4473 O OD1  . ASN   B 1 37  ? 48.632 -21.016 0.589   1.00 12.46 ?  37  ASN   B OD1  1 
ATOM   4474 N ND2  . ASN   B 1 37  ? 48.626 -19.156 1.852   1.00 11.71 ?  37  ASN   B ND2  1 
ATOM   4475 H H    . ASN   B 1 37  ? 45.465 -18.585 -1.742  1.00 13.35 ?  37  ASN   B H    1 
ATOM   4476 H HA   . ASN   B 1 37  ? 47.030 -20.771 -1.417  1.00 13.60 ?  37  ASN   B HA   1 
ATOM   4477 H HB2  . ASN   B 1 37  ? 48.026 -18.705 -0.883  1.00 13.59 ?  37  ASN   B HB2  1 
ATOM   4478 H HB3  . ASN   B 1 37  ? 46.907 -18.463 0.220   1.00 13.59 ?  37  ASN   B HB3  1 
ATOM   4479 H HD21 . ASN   B 1 37  ? 49.111 -19.528 2.462   1.00 14.20 ?  37  ASN   B HD21 1 
ATOM   4480 H HD22 . ASN   B 1 37  ? 48.364 -18.350 1.954   1.00 14.20 ?  37  ASN   B HD22 1 
ATOM   4481 N N    . ALA   B 1 38  ? 45.889 -21.983 0.368   1.00 11.60 ?  38  ALA   B N    1 
ATOM   4482 C CA   . ALA   B 1 38  ? 45.239 -22.720 1.454   1.00 11.85 ?  38  ALA   B CA   1 
ATOM   4483 C C    . ALA   B 1 38  ? 45.838 -22.243 2.775   1.00 12.00 ?  38  ALA   B C    1 
ATOM   4484 O O    . ALA   B 1 38  ? 46.743 -22.853 3.352   1.00 12.82 ?  38  ALA   B O    1 
ATOM   4485 C CB   . ALA   B 1 38  ? 45.453 -24.219 1.263   1.00 13.36 ?  38  ALA   B CB   1 
ATOM   4486 H H    . ALA   B 1 38  ? 46.533 -22.424 0.009   1.00 14.07 ?  38  ALA   B H    1 
ATOM   4487 H HA   . ALA   B 1 38  ? 44.285 -22.533 1.459   1.00 14.37 ?  38  ALA   B HA   1 
ATOM   4488 H HB1  . ALA   B 1 38  ? 45.009 -24.696 1.990   1.00 16.18 ?  38  ALA   B HB1  1 
ATOM   4489 H HB2  . ALA   B 1 38  ? 45.064 -24.487 0.416   1.00 16.18 ?  38  ALA   B HB2  1 
ATOM   4490 H HB3  . ALA   B 1 38  ? 46.398 -24.410 1.275   1.00 16.18 ?  38  ALA   B HB3  1 
ATOM   4491 N N    . ALA   B 1 39  ? 45.316 -21.109 3.248   1.00 11.51 ?  39  ALA   B N    1 
ATOM   4492 C CA   . ALA   B 1 39  ? 45.864 -20.376 4.378   1.00 11.69 ?  39  ALA   B CA   1 
ATOM   4493 C C    . ALA   B 1 39  ? 45.239 -20.824 5.700   1.00 11.64 ?  39  ALA   B C    1 
ATOM   4494 O O    . ALA   B 1 39  ? 44.210 -21.508 5.743   1.00 12.88 ?  39  ALA   B O    1 
ATOM   4495 C CB   . ALA   B 1 39  ? 45.637 -18.870 4.181   1.00 12.36 ?  39  ALA   B CB   1 
ATOM   4496 H H    . ALA   B 1 39  ? 44.618 -20.735 2.915   1.00 13.96 ?  39  ALA   B H    1 
ATOM   4497 H HA   . ALA   B 1 39  ? 46.817 -20.530 4.430   1.00 14.18 ?  39  ALA   B HA   1 
ATOM   4498 H HB1  . ALA   B 1 39  ? 46.008 -18.390 4.940   1.00 14.98 ?  39  ALA   B HB1  1 
ATOM   4499 H HB2  . ALA   B 1 39  ? 46.085 -18.587 3.365   1.00 14.98 ?  39  ALA   B HB2  1 
ATOM   4500 H HB3  . ALA   B 1 39  ? 44.687 -18.696 4.112   1.00 14.98 ?  39  ALA   B HB3  1 
ATOM   4501 N N    . ASN   B 1 40  ? 45.877 -20.406 6.791   1.00 12.85 ?  40  ASN   B N    1 
ATOM   4502 C CA   . ASN   B 1 40  ? 45.316 -20.451 8.132   1.00 13.35 ?  40  ASN   B CA   1 
ATOM   4503 C C    . ASN   B 1 40  ? 45.134 -19.021 8.652   1.00 13.08 ?  40  ASN   B C    1 
ATOM   4504 O O    . ASN   B 1 40  ? 45.555 -18.044 8.025   1.00 13.17 ?  40  ASN   B O    1 
ATOM   4505 C CB   . ASN   B 1 40  ? 46.169 -21.320 9.075   1.00 14.40 ?  40  ASN   B CB   1 
ATOM   4506 C CG   . ASN   B 1 40  ? 47.631 -20.920 9.094   1.00 15.13 ?  40  ASN   B CG   1 
ATOM   4507 O OD1  . ASN   B 1 40  ? 47.957 -19.737 9.154   1.00 17.15 ?  40  ASN   B OD1  1 
ATOM   4508 N ND2  . ASN   B 1 40  ? 48.520 -21.902 9.049   1.00 15.40 ?  40  ASN   B ND2  1 
ATOM   4509 H H    . ASN   B 1 40  ? 46.673 -20.083 6.771   1.00 15.57 ?  40  ASN   B H    1 
ATOM   4510 H HA   . ASN   B 1 40  ? 44.434 -20.850 8.087   1.00 16.17 ?  40  ASN   B HA   1 
ATOM   4511 H HB2  . ASN   B 1 40  ? 45.825 -21.234 9.978   1.00 17.43 ?  40  ASN   B HB2  1 
ATOM   4512 H HB3  . ASN   B 1 40  ? 46.114 -22.242 8.785   1.00 17.43 ?  40  ASN   B HB3  1 
ATOM   4513 H HD21 . ASN   B 1 40  ? 49.360 -21.723 9.056   1.00 18.62 ?  40  ASN   B HD21 1 
ATOM   4514 H HD22 . ASN   B 1 40  ? 48.254 -22.719 9.007   1.00 18.62 ?  40  ASN   B HD22 1 
ATOM   4515 N N    . VAL   B 1 41  ? 44.484 -18.894 9.810   1.00 13.54 ?  41  VAL   B N    1 
ATOM   4516 C CA   . VAL   B 1 41  ? 44.030 -17.571 10.253  1.00 14.64 ?  41  VAL   B CA   1 
ATOM   4517 C C    . VAL   B 1 41  ? 45.186 -16.624 10.554  1.00 14.25 ?  41  VAL   B C    1 
ATOM   4518 O O    . VAL   B 1 41  ? 45.016 -15.399 10.476  1.00 14.55 ?  41  VAL   B O    1 
ATOM   4519 C CB   . VAL   B 1 41  ? 43.054 -17.646 11.445  1.00 16.25 ?  41  VAL   B CB   1 
ATOM   4520 C CG1  . VAL   B 1 41  ? 41.756 -18.332 11.042  1.00 16.89 ?  41  VAL   B CG1  1 
ATOM   4521 C CG2  . VAL   B 1 41  ? 43.700 -18.325 12.641  1.00 17.21 ?  41  VAL   B CG2  1 
ATOM   4522 H H    . VAL   B 1 41  ? 44.296 -19.538 10.341  1.00 16.40 ?  41  VAL   B H    1 
ATOM   4523 H HA   . VAL   B 1 41  ? 43.533 -17.172 9.524   1.00 17.71 ?  41  VAL   B HA   1 
ATOM   4524 H HB   . VAL   B 1 41  ? 42.826 -16.742 11.716  1.00 19.65 ?  41  VAL   B HB   1 
ATOM   4525 H HG11 . VAL   B 1 41  ? 41.153 -18.343 11.804  1.00 20.41 ?  41  VAL   B HG11 1 
ATOM   4526 H HG12 . VAL   B 1 41  ? 41.353 -17.840 10.310  1.00 20.41 ?  41  VAL   B HG12 1 
ATOM   4527 H HG13 . VAL   B 1 41  ? 41.953 -19.240 10.764  1.00 20.41 ?  41  VAL   B HG13 1 
ATOM   4528 H HG21 . VAL   B 1 41  ? 43.056 -18.369 13.365  1.00 20.80 ?  41  VAL   B HG21 1 
ATOM   4529 H HG22 . VAL   B 1 41  ? 43.970 -19.222 12.386  1.00 20.80 ?  41  VAL   B HG22 1 
ATOM   4530 H HG23 . VAL   B 1 41  ? 44.473 -17.811 12.915  1.00 20.80 ?  41  VAL   B HG23 1 
ATOM   4531 N N    . TYR   B 1 42  ? 46.352 -17.145 10.932  1.00 14.44 ?  42  TYR   B N    1 
ATOM   4532 C CA   . TYR   B 1 42  ? 47.508 -16.299 11.205  1.00 15.05 ?  42  TYR   B CA   1 
ATOM   4533 C C    . TYR   B 1 42  ? 48.472 -16.220 10.027  1.00 14.21 ?  42  TYR   B C    1 
ATOM   4534 O O    . TYR   B 1 42  ? 49.562 -15.650 10.165  1.00 15.45 ?  42  TYR   B O    1 
ATOM   4535 C CB   . TYR   B 1 42  ? 48.204 -16.705 12.510  1.00 16.94 ?  42  TYR   B CB   1 
ATOM   4536 C CG   . TYR   B 1 42  ? 47.606 -16.016 13.732  1.00 17.72 ?  42  TYR   B CG   1 
ATOM   4537 C CD1  . TYR   B 1 42  ? 47.828 -14.661 13.965  1.00 17.23 ?  42  TYR   B CD1  1 
ATOM   4538 C CD2  . TYR   B 1 42  ? 46.817 -16.710 14.639  1.00 19.45 ?  42  TYR   B CD2  1 
ATOM   4539 C CE1  . TYR   B 1 42  ? 47.287 -14.021 15.063  1.00 18.46 ?  42  TYR   B CE1  1 
ATOM   4540 C CE2  . TYR   B 1 42  ? 46.272 -16.076 15.746  1.00 19.67 ?  42  TYR   B CE2  1 
ATOM   4541 C CZ   . TYR   B 1 42  ? 46.510 -14.727 15.951  1.00 20.18 ?  42  TYR   B CZ   1 
ATOM   4542 O OH   . TYR   B 1 42  ? 45.979 -14.074 17.046  1.00 23.07 ?  42  TYR   B OH   1 
ATOM   4543 H H    . TYR   B 1 42  ? 46.499 -17.993 11.025  1.00 17.48 ?  42  TYR   B H    1 
ATOM   4544 H HA   . TYR   B 1 42  ? 47.177 -15.402 11.343  1.00 18.21 ?  42  TYR   B HA   1 
ATOM   4545 H HB2  . TYR   B 1 42  ? 48.118 -17.662 12.633  1.00 20.48 ?  42  TYR   B HB2  1 
ATOM   4546 H HB3  . TYR   B 1 42  ? 49.141 -16.459 12.455  1.00 20.48 ?  42  TYR   B HB3  1 
ATOM   4547 H HD1  . TYR   B 1 42  ? 48.355 -14.175 13.364  1.00 20.82 ?  42  TYR   B HD1  1 
ATOM   4548 H HD2  . TYR   B 1 42  ? 46.652 -17.616 14.500  1.00 23.48 ?  42  TYR   B HD2  1 
ATOM   4549 H HE1  . TYR   B 1 42  ? 47.450 -13.116 15.198  1.00 22.30 ?  42  TYR   B HE1  1 
ATOM   4550 H HE2  . TYR   B 1 42  ? 45.742 -16.556 16.343  1.00 23.76 ?  42  TYR   B HE2  1 
ATOM   4551 H HH   . TYR   B 1 42  ? 46.207 -13.269 17.030  1.00 27.84 ?  42  TYR   B HH   1 
ATOM   4552 N N    . LEU   B 1 43  ? 48.077 -16.736 8.866   1.00 12.96 ?  43  LEU   B N    1 
ATOM   4553 C CA   . LEU   B 1 43  ? 48.895 -16.664 7.658   1.00 12.71 ?  43  LEU   B CA   1 
ATOM   4554 C C    . LEU   B 1 43  ? 50.311 -17.167 7.916   1.00 13.31 ?  43  LEU   B C    1 
ATOM   4555 O O    . LEU   B 1 43  ? 51.289 -16.563 7.473   1.00 13.90 ?  43  LEU   B O    1 
ATOM   4556 C CB   . LEU   B 1 43  ? 48.906 -15.256 7.057   1.00 13.09 ?  43  LEU   B CB   1 
ATOM   4557 C CG   . LEU   B 1 43  ? 47.550 -14.647 6.675   1.00 13.43 ?  43  LEU   B CG   1 
ATOM   4558 C CD1  . LEU   B 1 43  ? 47.768 -13.241 6.102   1.00 14.98 ?  43  LEU   B CD1  1 
ATOM   4559 C CD2  . LEU   B 1 43  ? 46.784 -15.528 5.699   1.00 13.61 ?  43  LEU   B CD2  1 
ATOM   4560 H H    . LEU   B 1 43  ? 47.337 -17.162 8.753   1.00 15.70 ?  43  LEU   B H    1 
ATOM   4561 H HA   . LEU   B 1 43  ? 48.501 -17.251 6.992   1.00 15.40 ?  43  LEU   B HA   1 
ATOM   4562 H HB2  . LEU   B 1 43  ? 49.317 -14.657 7.699   1.00 15.85 ?  43  LEU   B HB2  1 
ATOM   4563 H HB3  . LEU   B 1 43  ? 49.443 -15.279 6.251   1.00 15.85 ?  43  LEU   B HB3  1 
ATOM   4564 H HG   . LEU   B 1 43  ? 47.012 -14.557 7.475   1.00 16.26 ?  43  LEU   B HG   1 
ATOM   4565 H HD11 . LEU   B 1 43  ? 46.907 -12.861 5.864   1.00 18.13 ?  43  LEU   B HD11 1 
ATOM   4566 H HD12 . LEU   B 1 43  ? 48.195 -12.689 6.778   1.00 18.13 ?  43  LEU   B HD12 1 
ATOM   4567 H HD13 . LEU   B 1 43  ? 48.333 -13.302 5.318   1.00 18.13 ?  43  LEU   B HD13 1 
ATOM   4568 H HD21 . LEU   B 1 43  ? 45.976 -15.070 5.418   1.00 16.48 ?  43  LEU   B HD21 1 
ATOM   4569 H HD22 . LEU   B 1 43  ? 47.343 -15.712 4.926   1.00 16.48 ?  43  LEU   B HD22 1 
ATOM   4570 H HD23 . LEU   B 1 43  ? 46.551 -16.364 6.138   1.00 16.48 ?  43  LEU   B HD23 1 
ATOM   4571 N N    . LYS   B 1 44  ? 50.414 -18.289 8.629   1.00 13.55 ?  44  LYS   B N    1 
ATOM   4572 C CA   . LYS   B 1 44  ? 51.680 -18.976 8.860   1.00 13.94 ?  44  LYS   B CA   1 
ATOM   4573 C C    . LYS   B 1 44  ? 51.793 -20.090 7.826   1.00 13.39 ?  44  LYS   B C    1 
ATOM   4574 O O    . LYS   B 1 44  ? 51.094 -21.106 7.912   1.00 14.92 ?  44  LYS   B O    1 
ATOM   4575 C CB   . LYS   B 1 44  ? 51.745 -19.499 10.294  1.00 15.93 ?  44  LYS   B CB   1 
ATOM   4576 C CG   . LYS   B 1 44  ? 51.927 -18.398 11.329  1.00 18.92 ?  44  LYS   B CG   1 
ATOM   4577 C CD   . LYS   B 1 44  ? 53.124 -17.526 10.957  1.00 21.89 ?  44  LYS   B CD   1 
ATOM   4578 C CE   . LYS   B 1 44  ? 53.572 -16.621 12.076  1.00 24.70 ?  44  LYS   B CE   1 
ATOM   4579 N NZ   . LYS   B 1 44  ? 54.763 -15.818 11.696  1.00 26.06 ?  44  LYS   B NZ   1 
ATOM   4580 H H    . LYS   B 1 44  ? 49.744 -18.672 9.008   1.00 16.41 ?  44  LYS   B H    1 
ATOM   4581 H HA   . LYS   B 1 44  ? 52.414 -18.363 8.701   1.00 16.87 ?  44  LYS   B HA   1 
ATOM   4582 H HB2  . LYS   B 1 44  ? 50.912 -19.962 10.496  1.00 19.27 ?  44  LYS   B HB2  1 
ATOM   4583 H HB3  . LYS   B 1 44  ? 52.489 -20.111 10.374  1.00 19.27 ?  44  LYS   B HB3  1 
ATOM   4584 H HG2  . LYS   B 1 44  ? 51.133 -17.844 11.357  1.00 22.86 ?  44  LYS   B HG2  1 
ATOM   4585 H HG3  . LYS   B 1 44  ? 52.094 -18.799 12.199  1.00 22.86 ?  44  LYS   B HG3  1 
ATOM   4586 H HD2  . LYS   B 1 44  ? 53.865 -18.106 10.703  1.00 26.41 ?  44  LYS   B HD2  1 
ATOM   4587 H HD3  . LYS   B 1 44  ? 52.877 -16.963 10.206  1.00 26.41 ?  44  LYS   B HD3  1 
ATOM   4588 H HE2  . LYS   B 1 44  ? 52.857 -16.006 12.277  1.00 29.79 ?  44  LYS   B HE2  1 
ATOM   4589 H HE3  . LYS   B 1 44  ? 53.796 -17.159 12.850  1.00 29.79 ?  44  LYS   B HE3  1 
ATOM   4590 H HZ1  . LYS   B 1 44  ? 55.002 -15.293 12.373  1.00 31.42 ?  44  LYS   B HZ1  1 
ATOM   4591 H HZ2  . LYS   B 1 44  ? 55.443 -16.352 11.488  1.00 31.42 ?  44  LYS   B HZ2  1 
ATOM   4592 H HZ3  . LYS   B 1 44  ? 54.573 -15.306 10.989  1.00 31.42 ?  44  LYS   B HZ3  1 
ATOM   4593 N N    . HIS   B 1 45  ? 52.646 -19.873 6.826   1.00 12.92 ?  45  HIS   B N    1 
ATOM   4594 C CA   . HIS   B 1 45  ? 52.670 -20.706 5.624   1.00 13.48 ?  45  HIS   B CA   1 
ATOM   4595 C C    . HIS   B 1 45  ? 53.689 -21.829 5.790   1.00 15.76 ?  45  HIS   B C    1 
ATOM   4596 O O    . HIS   B 1 45  ? 54.759 -21.839 5.189   1.00 18.12 ?  45  HIS   B O    1 
ATOM   4597 C CB   . HIS   B 1 45  ? 52.977 -19.861 4.400   1.00 13.06 ?  45  HIS   B CB   1 
ATOM   4598 C CG   . HIS   B 1 45  ? 52.113 -18.651 4.288   1.00 13.30 ?  45  HIS   B CG   1 
ATOM   4599 N ND1  . HIS   B 1 45  ? 50.732 -18.716 4.264   1.00 13.79 ?  45  HIS   B ND1  1 
ATOM   4600 C CD2  . HIS   B 1 45  ? 52.438 -17.340 4.212   1.00 14.02 ?  45  HIS   B CD2  1 
ATOM   4601 C CE1  . HIS   B 1 45  ? 50.253 -17.489 4.162   1.00 13.06 ?  45  HIS   B CE1  1 
ATOM   4602 N NE2  . HIS   B 1 45  ? 51.264 -16.639 4.130   1.00 13.74 ?  45  HIS   B NE2  1 
ATOM   4603 H H    . HIS   B 1 45  ? 53.219 -19.231 6.814   1.00 15.65 ?  45  HIS   B H    1 
ATOM   4604 H HA   . HIS   B 1 45  ? 51.793 -21.106 5.499   1.00 16.32 ?  45  HIS   B HA   1 
ATOM   4605 H HB2  . HIS   B 1 45  ? 53.900 -19.571 4.440   1.00 15.81 ?  45  HIS   B HB2  1 
ATOM   4606 H HB3  . HIS   B 1 45  ? 52.838 -20.404 3.602   1.00 15.81 ?  45  HIS   B HB3  1 
ATOM   4607 H HD2  . HIS   B 1 45  ? 53.297 -16.982 4.210   1.00 16.97 ?  45  HIS   B HD2  1 
ATOM   4608 H HE1  . HIS   B 1 45  ? 49.353 -17.267 4.116   1.00 15.82 ?  45  HIS   B HE1  1 
ATOM   4609 H HE2  . HIS   B 1 45  ? 51.192 -15.786 4.069   1.00 16.64 ?  45  HIS   B HE2  1 
ATOM   4610 N N    A GLY   B 1 46  ? 53.320 -22.799 6.621   0.86 16.49 ?  46  GLY   B N    1 
ATOM   4611 N N    B GLY   B 1 46  ? 53.328 -22.791 6.632   0.14 16.65 ?  46  GLY   B N    1 
ATOM   4612 C CA   A GLY   B 1 46  ? 54.234 -23.866 6.984   0.86 18.37 ?  46  GLY   B CA   1 
ATOM   4613 C CA   B GLY   B 1 46  ? 54.244 -23.862 6.966   0.14 17.72 ?  46  GLY   B CA   1 
ATOM   4614 C C    A GLY   B 1 46  ? 54.283 -25.067 6.057   0.86 20.45 ?  46  GLY   B C    1 
ATOM   4615 C C    B GLY   B 1 46  ? 54.267 -25.009 5.977   0.14 18.83 ?  46  GLY   B C    1 
ATOM   4616 O O    A GLY   B 1 46  ? 55.354 -25.454 5.579   0.86 23.75 ?  46  GLY   B O    1 
ATOM   4617 O O    B GLY   B 1 46  ? 55.300 -25.278 5.356   0.14 19.19 ?  46  GLY   B O    1 
ATOM   4618 H H    A GLY   B 1 46  ? 52.549 -22.840 7.010   0.86 19.93 ?  46  GLY   B H    1 
ATOM   4619 H H    B GLY   B 1 46  ? 52.563 -22.839 7.026   0.14 20.12 ?  46  GLY   B H    1 
ATOM   4620 H HA2  A GLY   B 1 46  ? 55.128 -23.499 7.049   0.86 22.19 ?  46  GLY   B HA2  1 
ATOM   4621 H HA2  B GLY   B 1 46  ? 55.141 -23.499 7.024   0.14 21.42 ?  46  GLY   B HA2  1 
ATOM   4622 H HA3  A GLY   B 1 46  ? 53.987 -24.197 7.864   0.86 22.19 ?  46  GLY   B HA3  1 
ATOM   4623 H HA3  B GLY   B 1 46  ? 54.007 -24.216 7.836   0.14 21.42 ?  46  GLY   B HA3  1 
ATOM   4624 N N    . GLY   B 1 47  ? 53.134 -25.690 5.812   1.00 19.53 ?  47  GLY   B N    1 
ATOM   4625 C CA   . GLY   B 1 47  ? 53.080 -26.944 5.089   1.00 17.00 ?  47  GLY   B CA   1 
ATOM   4626 C C    . GLY   B 1 47  ? 52.165 -26.908 3.880   1.00 14.85 ?  47  GLY   B C    1 
ATOM   4627 O O    . GLY   B 1 47  ? 51.515 -25.903 3.592   1.00 15.09 ?  47  GLY   B O    1 
ATOM   4628 H H    A GLY   B 1 47  ? 52.366 -25.412 6.080   0.86 23.59 ?  47  GLY   B H    1 
ATOM   4629 H H    B GLY   B 1 47  ? 52.372 -25.433 6.117   0.14 23.59 ?  47  GLY   B H    1 
ATOM   4630 H HA2  . GLY   B 1 47  ? 53.968 -27.182 4.785   1.00 20.54 ?  47  GLY   B HA2  1 
ATOM   4631 H HA3  . GLY   B 1 47  ? 52.767 -27.638 5.687   1.00 20.54 ?  47  GLY   B HA3  1 
ATOM   4632 N N    . GLY   B 1 48  ? 52.112 -28.048 3.190   1.00 14.06 ?  48  GLY   B N    1 
ATOM   4633 C CA   . GLY   B 1 48  ? 51.185 -28.198 2.087   1.00 14.01 ?  48  GLY   B CA   1 
ATOM   4634 C C    . GLY   B 1 48  ? 51.332 -27.092 1.066   1.00 13.42 ?  48  GLY   B C    1 
ATOM   4635 O O    . GLY   B 1 48  ? 52.441 -26.634 0.755   1.00 13.77 ?  48  GLY   B O    1 
ATOM   4636 H H    . GLY   B 1 48  ? 52.612 -28.728 3.334   1.00 17.02 ?  48  GLY   B H    1 
ATOM   4637 H HA2  . GLY   B 1 48  ? 51.337 -29.049 1.648   1.00 16.96 ?  48  GLY   B HA2  1 
ATOM   4638 H HA3  . GLY   B 1 48  ? 50.275 -28.182 2.424   1.00 16.96 ?  48  GLY   B HA3  1 
ATOM   4639 N N    . VAL   B 1 49  ? 50.187 -26.655 0.533   1.00 13.27 ?  49  VAL   B N    1 
ATOM   4640 C CA   . VAL   B 1 49  ? 50.170 -25.628 -0.506  1.00 12.88 ?  49  VAL   B CA   1 
ATOM   4641 C C    . VAL   B 1 49  ? 50.827 -24.341 -0.015  1.00 12.20 ?  49  VAL   B C    1 
ATOM   4642 O O    . VAL   B 1 49  ? 51.606 -23.712 -0.741  1.00 13.26 ?  49  VAL   B O    1 
ATOM   4643 C CB   . VAL   B 1 49  ? 48.725 -25.374 -0.984  1.00 14.43 ?  49  VAL   B CB   1 
ATOM   4644 C CG1  . VAL   B 1 49  ? 48.637 -24.097 -1.824  1.00 14.50 ?  49  VAL   B CG1  1 
ATOM   4645 C CG2  . VAL   B 1 49  ? 48.198 -26.571 -1.764  1.00 16.72 ?  49  VAL   B CG2  1 
ATOM   4646 H H    . VAL   B 1 49  ? 49.404 -26.940 0.753   1.00 16.07 ?  49  VAL   B H    1 
ATOM   4647 H HA   . VAL   B 1 49  ? 50.678 -25.943 -1.270  1.00 15.61 ?  49  VAL   B HA   1 
ATOM   4648 H HB   . VAL   B 1 49  ? 48.158 -25.253 -0.208  1.00 17.46 ?  49  VAL   B HB   1 
ATOM   4649 H HG11 . VAL   B 1 49  ? 47.803 -24.106 -2.323  1.00 17.54 ?  49  VAL   B HG11 1 
ATOM   4650 H HG12 . VAL   B 1 49  ? 48.655 -23.324 -1.235  1.00 17.54 ?  49  VAL   B HG12 1 
ATOM   4651 H HG13 . VAL   B 1 49  ? 49.386 -24.066 -2.437  1.00 17.54 ?  49  VAL   B HG13 1 
ATOM   4652 H HG21 . VAL   B 1 49  ? 47.289 -26.384 -2.047  1.00 20.21 ?  49  VAL   B HG21 1 
ATOM   4653 H HG22 . VAL   B 1 49  ? 48.763 -26.710 -2.542  1.00 20.21 ?  49  VAL   B HG22 1 
ATOM   4654 H HG23 . VAL   B 1 49  ? 48.218 -27.350 -1.194  1.00 20.21 ?  49  VAL   B HG23 1 
ATOM   4655 N N    . ALA   B 1 50  ? 50.479 -23.898 1.195   1.00 12.27 ?  50  ALA   B N    1 
ATOM   4656 C CA   . ALA   B 1 50  ? 50.998 -22.618 1.671   1.00 12.22 ?  50  ALA   B CA   1 
ATOM   4657 C C    . ALA   B 1 50  ? 52.520 -22.646 1.780   1.00 12.20 ?  50  ALA   B C    1 
ATOM   4658 O O    . ALA   B 1 50  ? 53.201 -21.680 1.411   1.00 12.48 ?  50  ALA   B O    1 
ATOM   4659 C CB   . ALA   B 1 50  ? 50.375 -22.256 3.017   1.00 12.49 ?  50  ALA   B CB   1 
ATOM   4660 H H    . ALA   B 1 50  ? 49.964 -24.309 1.748   1.00 14.87 ?  50  ALA   B H    1 
ATOM   4661 H HA   . ALA   B 1 50  ? 50.765 -21.925 1.038   1.00 14.81 ?  50  ALA   B HA   1 
ATOM   4662 H HB1  . ALA   B 1 50  ? 50.729 -21.401 3.312   1.00 15.14 ?  50  ALA   B HB1  1 
ATOM   4663 H HB2  . ALA   B 1 50  ? 49.412 -22.195 2.911   1.00 15.14 ?  50  ALA   B HB2  1 
ATOM   4664 H HB3  . ALA   B 1 50  ? 50.593 -22.945 3.664   1.00 15.14 ?  50  ALA   B HB3  1 
ATOM   4665 N N    . GLY   B 1 51  ? 53.072 -23.740 2.299   1.00 13.06 ?  51  GLY   B N    1 
ATOM   4666 C CA   . GLY   B 1 51  ? 54.519 -23.849 2.364   1.00 13.67 ?  51  GLY   B CA   1 
ATOM   4667 C C    . GLY   B 1 51  ? 55.169 -23.792 0.997   1.00 13.44 ?  51  GLY   B C    1 
ATOM   4668 O O    . GLY   B 1 51  ? 56.214 -23.156 0.820   1.00 14.29 ?  51  GLY   B O    1 
ATOM   4669 H H    . GLY   B 1 51  ? 52.645 -24.418 2.609   1.00 15.82 ?  51  GLY   B H    1 
ATOM   4670 H HA2  . GLY   B 1 51  ? 54.878 -23.124 2.901   1.00 16.55 ?  51  GLY   B HA2  1 
ATOM   4671 H HA3  . GLY   B 1 51  ? 54.766 -24.690 2.783   1.00 16.55 ?  51  GLY   B HA3  1 
ATOM   4672 N N    . ALA   B 1 52  ? 54.567 -24.456 0.012   1.00 13.01 ?  52  ALA   B N    1 
ATOM   4673 C CA   . ALA   B 1 52  ? 55.127 -24.459 -1.333  1.00 13.43 ?  52  ALA   B CA   1 
ATOM   4674 C C    . ALA   B 1 52  ? 55.050 -23.080 -1.978  1.00 12.85 ?  52  ALA   B C    1 
ATOM   4675 O O    . ALA   B 1 52  ? 56.018 -22.636 -2.615  1.00 13.86 ?  52  ALA   B O    1 
ATOM   4676 C CB   . ALA   B 1 52  ? 54.413 -25.490 -2.200  1.00 14.16 ?  52  ALA   B CB   1 
ATOM   4677 H H    . ALA   B 1 52  ? 53.834 -24.900 0.096   1.00 15.76 ?  52  ALA   B H    1 
ATOM   4678 H HA   . ALA   B 1 52  ? 56.062 -24.707 -1.279  1.00 16.26 ?  52  ALA   B HA   1 
ATOM   4679 H HB1  . ALA   B 1 52  ? 54.805 -25.476 -3.088  1.00 17.14 ?  52  ALA   B HB1  1 
ATOM   4680 H HB2  . ALA   B 1 52  ? 54.529 -26.366 -1.801  1.00 17.14 ?  52  ALA   B HB2  1 
ATOM   4681 H HB3  . ALA   B 1 52  ? 53.473 -25.266 -2.247  1.00 17.14 ?  52  ALA   B HB3  1 
ATOM   4682 N N    . LEU   B 1 53  ? 53.906 -22.402 -1.859  1.00 12.39 ?  53  LEU   B N    1 
ATOM   4683 C CA   . LEU   B 1 53  ? 53.794 -21.066 -2.435  1.00 12.60 ?  53  LEU   B CA   1 
ATOM   4684 C C    . LEU   B 1 53  ? 54.798 -20.124 -1.789  1.00 12.55 ?  53  LEU   B C    1 
ATOM   4685 O O    . LEU   B 1 53  ? 55.502 -19.377 -2.479  1.00 13.26 ?  53  LEU   B O    1 
ATOM   4686 C CB   . LEU   B 1 53  ? 52.365 -20.534 -2.271  1.00 13.32 ?  53  LEU   B CB   1 
ATOM   4687 C CG   . LEU   B 1 53  ? 51.231 -21.257 -3.012  1.00 13.97 ?  53  LEU   B CG   1 
ATOM   4688 C CD1  . LEU   B 1 53  ? 49.887 -20.630 -2.687  1.00 15.27 ?  53  LEU   B CD1  1 
ATOM   4689 C CD2  . LEU   B 1 53  ? 51.457 -21.272 -4.518  1.00 15.60 ?  53  LEU   B CD2  1 
ATOM   4690 H H    . LEU   B 1 53  ? 53.200 -22.688 -1.457  1.00 15.01 ?  53  LEU   B H    1 
ATOM   4691 H HA   . LEU   B 1 53  ? 53.992 -21.118 -3.386  1.00 15.27 ?  53  LEU   B HA   1 
ATOM   4692 H HB2  . LEU   B 1 53  ? 52.146 -20.557 -1.330  1.00 16.13 ?  53  LEU   B HB2  1 
ATOM   4693 H HB3  . LEU   B 1 53  ? 52.356 -19.615 -2.580  1.00 16.13 ?  53  LEU   B HB3  1 
ATOM   4694 H HG   . LEU   B 1 53  ? 51.198 -22.179 -2.708  1.00 16.92 ?  53  LEU   B HG   1 
ATOM   4695 H HD11 . LEU   B 1 53  ? 49.189 -21.110 -3.163  1.00 18.47 ?  53  LEU   B HD11 1 
ATOM   4696 H HD12 . LEU   B 1 53  ? 49.732 -20.693 -1.729  1.00 18.47 ?  53  LEU   B HD12 1 
ATOM   4697 H HD13 . LEU   B 1 53  ? 49.897 -19.702 -2.960  1.00 18.47 ?  53  LEU   B HD13 1 
ATOM   4698 H HD21 . LEU   B 1 53  ? 50.716 -21.732 -4.946  1.00 18.87 ?  53  LEU   B HD21 1 
ATOM   4699 H HD22 . LEU   B 1 53  ? 51.508 -20.361 -4.839  1.00 18.87 ?  53  LEU   B HD22 1 
ATOM   4700 H HD23 . LEU   B 1 53  ? 52.286 -21.740 -4.708  1.00 18.87 ?  53  LEU   B HD23 1 
ATOM   4701 N N    . ASN   B 1 54  ? 54.893 -20.156 -0.462  1.00 12.27 ?  54  ASN   B N    1 
ATOM   4702 C CA   . ASN   B 1 54  ? 55.808 -19.243 0.210   1.00 13.14 ?  54  ASN   B CA   1 
ATOM   4703 C C    . ASN   B 1 54  ? 57.252 -19.521 -0.184  1.00 13.62 ?  54  ASN   B C    1 
ATOM   4704 O O    . ASN   B 1 54  ? 58.022 -18.586 -0.428  1.00 14.09 ?  54  ASN   B O    1 
ATOM   4705 C CB   . ASN   B 1 54  ? 55.635 -19.308 1.721   1.00 13.96 ?  54  ASN   B CB   1 
ATOM   4706 C CG   . ASN   B 1 54  ? 56.617 -18.404 2.434   1.00 13.60 ?  54  ASN   B CG   1 
ATOM   4707 O OD1  . ASN   B 1 54  ? 56.638 -17.192 2.192   1.00 14.04 ?  54  ASN   B OD1  1 
ATOM   4708 N ND2  . ASN   B 1 54  ? 57.464 -18.982 3.283   1.00 15.22 ?  54  ASN   B ND2  1 
ATOM   4709 H H    . ASN   B 1 54  ? 54.454 -20.688 0.057   1.00 14.87 ?  54  ASN   B H    1 
ATOM   4710 H HA   . ASN   B 1 54  ? 55.594 -18.342 -0.073  1.00 15.91 ?  54  ASN   B HA   1 
ATOM   4711 H HB2  . ASN   B 1 54  ? 54.735 -19.017 1.953   1.00 16.90 ?  54  ASN   B HB2  1 
ATOM   4712 H HB3  . ASN   B 1 54  ? 55.782 -20.214 2.024   1.00 16.90 ?  54  ASN   B HB3  1 
ATOM   4713 H HD21 . ASN   B 1 54  ? 58.046 -18.504 3.700   1.00 18.42 ?  54  ASN   B HD21 1 
ATOM   4714 H HD22 . ASN   B 1 54  ? 57.432 -19.830 3.410   1.00 18.42 ?  54  ASN   B HD22 1 
ATOM   4715 N N    . LYS   B 1 55  ? 57.637 -20.800 -0.250  1.00 14.22 ?  55  LYS   B N    1 
ATOM   4716 C CA   . LYS   B 1 55  ? 58.992 -21.142 -0.673  1.00 15.39 ?  55  LYS   B CA   1 
ATOM   4717 C C    . LYS   B 1 55  ? 59.288 -20.600 -2.066  1.00 15.07 ?  55  LYS   B C    1 
ATOM   4718 O O    . LYS   B 1 55  ? 60.383 -20.081 -2.320  1.00 15.56 ?  55  LYS   B O    1 
ATOM   4719 C CB   . LYS   B 1 55  ? 59.185 -22.657 -0.630  1.00 16.68 ?  55  LYS   B CB   1 
ATOM   4720 C CG   . LYS   B 1 55  ? 60.587 -23.103 -1.011  1.00 20.90 ?  55  LYS   B CG   1 
ATOM   4721 C CD   . LYS   B 1 55  ? 60.762 -24.606 -0.871  1.00 24.25 ?  55  LYS   B CD   1 
ATOM   4722 C CE   . LYS   B 1 55  ? 60.651 -25.065 0.580   1.00 26.90 ?  55  LYS   B CE   1 
ATOM   4723 N NZ   . LYS   B 1 55  ? 61.070 -26.477 0.751   1.00 28.59 ?  55  LYS   B NZ   1 
ATOM   4724 H H    . LYS   B 1 55  ? 57.135 -21.475 -0.060  1.00 17.21 ?  55  LYS   B H    1 
ATOM   4725 H HA   . LYS   B 1 55  ? 59.623 -20.745 -0.055  1.00 18.62 ?  55  LYS   B HA   1 
ATOM   4726 H HB2  . LYS   B 1 55  ? 59.004 -22.965 0.271   1.00 20.16 ?  55  LYS   B HB2  1 
ATOM   4727 H HB3  . LYS   B 1 55  ? 58.563 -23.071 -1.250  1.00 20.16 ?  55  LYS   B HB3  1 
ATOM   4728 H HG2  . LYS   B 1 55  ? 60.757 -22.863 -1.936  1.00 25.22 ?  55  LYS   B HG2  1 
ATOM   4729 H HG3  . LYS   B 1 55  ? 61.227 -22.664 -0.428  1.00 25.22 ?  55  LYS   B HG3  1 
ATOM   4730 H HD2  . LYS   B 1 55  ? 60.073 -25.059 -1.383  1.00 29.25 ?  55  LYS   B HD2  1 
ATOM   4731 H HD3  . LYS   B 1 55  ? 61.640 -24.858 -1.198  1.00 29.25 ?  55  LYS   B HD3  1 
ATOM   4732 H HE2  . LYS   B 1 55  ? 61.220 -24.502 1.132   1.00 32.43 ?  55  LYS   B HE2  1 
ATOM   4733 H HE3  . LYS   B 1 55  ? 59.725 -24.981 0.867   1.00 32.43 ?  55  LYS   B HE3  1 
ATOM   4734 H HZ1  . LYS   B 1 55  ? 60.974 -26.718 1.602   1.00 34.46 ?  55  LYS   B HZ1  1 
ATOM   4735 H HZ2  . LYS   B 1 55  ? 60.564 -27.003 0.242   1.00 34.46 ?  55  LYS   B HZ2  1 
ATOM   4736 H HZ3  . LYS   B 1 55  ? 61.920 -26.570 0.514   1.00 34.46 ?  55  LYS   B HZ3  1 
ATOM   4737 N N    . ALA   B 1 56  ? 58.317 -20.690 -2.981  1.00 14.61 ?  56  ALA   B N    1 
ATOM   4738 C CA   . ALA   B 1 56  ? 58.537 -20.177 -4.328  1.00 15.61 ?  56  ALA   B CA   1 
ATOM   4739 C C    . ALA   B 1 56  ? 58.804 -18.676 -4.324  1.00 14.95 ?  56  ALA   B C    1 
ATOM   4740 O O    . ALA   B 1 56  ? 59.530 -18.177 -5.193  1.00 15.92 ?  56  ALA   B O    1 
ATOM   4741 C CB   . ALA   B 1 56  ? 57.354 -20.524 -5.231  1.00 16.65 ?  56  ALA   B CB   1 
ATOM   4742 H H    . ALA   B 1 56  ? 57.532 -21.015 -2.844  1.00 17.68 ?  56  ALA   B H    1 
ATOM   4743 H HA   . ALA   B 1 56  ? 59.323 -20.601 -4.692  1.00 18.88 ?  56  ALA   B HA   1 
ATOM   4744 H HB1  . ALA   B 1 56  ? 57.528 -20.180 -6.124  1.00 20.13 ?  56  ALA   B HB1  1 
ATOM   4745 H HB2  . ALA   B 1 56  ? 57.261 -21.489 -5.264  1.00 20.13 ?  56  ALA   B HB2  1 
ATOM   4746 H HB3  . ALA   B 1 56  ? 56.549 -20.123 -4.874  1.00 20.13 ?  56  ALA   B HB3  1 
ATOM   4747 N N    . THR   B 1 57  ? 58.239 -17.944 -3.361  1.00 14.78 ?  57  THR   B N    1 
ATOM   4748 C CA   . THR   B 1 57  ? 58.485 -16.506 -3.234  1.00 14.92 ?  57  THR   B CA   1 
ATOM   4749 C C    . THR   B 1 57  ? 59.740 -16.180 -2.427  1.00 15.49 ?  57  THR   B C    1 
ATOM   4750 O O    . THR   B 1 57  ? 59.980 -15.003 -2.120  1.00 16.08 ?  57  THR   B O    1 
ATOM   4751 C CB   . THR   B 1 57  ? 57.284 -15.777 -2.596  1.00 14.12 ?  57  THR   B CB   1 
ATOM   4752 O OG1  . THR   B 1 57  ? 57.263 -15.990 -1.177  1.00 14.47 ?  57  THR   B OG1  1 
ATOM   4753 C CG2  . THR   B 1 57  ? 55.958 -16.199 -3.228  1.00 14.13 ?  57  THR   B CG2  1 
ATOM   4754 H H    . THR   B 1 57  ? 57.692 -18.249 -2.772  1.00 17.88 ?  57  THR   B H    1 
ATOM   4755 H HA   . THR   B 1 57  ? 58.605 -16.132 -4.124  1.00 18.05 ?  57  THR   B HA   1 
ATOM   4756 H HB   . THR   B 1 57  ? 57.386 -14.823 -2.761  1.00 17.09 ?  57  THR   B HB   1 
ATOM   4757 H HG1  . THR   B 1 57  ? 57.199 -16.808 -1.011  1.00 17.51 ?  57  THR   B HG1  1 
ATOM   4758 H HG21 . THR   B 1 57  ? 55.236 -15.652 -2.884  1.00 17.10 ?  57  THR   B HG21 1 
ATOM   4759 H HG22 . THR   B 1 57  ? 56.001 -16.097 -4.191  1.00 17.10 ?  57  THR   B HG22 1 
ATOM   4760 H HG23 . THR   B 1 57  ? 55.774 -17.128 -3.020  1.00 17.10 ?  57  THR   B HG23 1 
ATOM   4761 N N    . ASN   B 1 58  ? 60.530 -17.186 -2.064  1.00 16.25 ?  58  ASN   B N    1 
ATOM   4762 C CA   . ASN   B 1 58  ? 61.729 -16.967 -1.256  1.00 19.41 ?  58  ASN   B CA   1 
ATOM   4763 C C    . ASN   B 1 58  ? 61.390 -16.255 0.054   1.00 16.81 ?  58  ASN   B C    1 
ATOM   4764 O O    . ASN   B 1 58  ? 62.118 -15.373 0.516   1.00 17.54 ?  58  ASN   B O    1 
ATOM   4765 C CB   . ASN   B 1 58  ? 62.809 -16.209 -2.032  1.00 28.52 ?  58  ASN   B CB   1 
ATOM   4766 C CG   . ASN   B 1 58  ? 64.184 -16.358 -1.409  1.00 38.80 ?  58  ASN   B CG   1 
ATOM   4767 O OD1  . ASN   B 1 58  ? 64.476 -17.361 -0.756  1.00 41.72 ?  58  ASN   B OD1  1 
ATOM   4768 N ND2  . ASN   B 1 58  ? 65.036 -15.358 -1.606  1.00 45.48 ?  58  ASN   B ND2  1 
ATOM   4769 H H    . ASN   B 1 58  ? 60.392 -18.013 -2.269  1.00 19.65 ?  58  ASN   B H    1 
ATOM   4770 H HA   . ASN   B 1 58  ? 62.100 -17.837 -1.032  1.00 23.44 ?  58  ASN   B HA   1 
ATOM   4771 H HB2  . ASN   B 1 58  ? 62.852 -16.553 -2.939  1.00 34.37 ?  58  ASN   B HB2  1 
ATOM   4772 H HB3  . ASN   B 1 58  ? 62.589 -15.266 -2.044  1.00 34.37 ?  58  ASN   B HB3  1 
ATOM   4773 H HD21 . ASN   B 1 58  ? 65.829 -15.396 -1.274  1.00 54.73 ?  58  ASN   B HD21 1 
ATOM   4774 H HD22 . ASN   B 1 58  ? 64.796 -14.673 -2.067  1.00 54.73 ?  58  ASN   B HD22 1 
ATOM   4775 N N    . ASN   B 1 59  ? 60.267 -16.644 0.658   1.00 15.77 ?  59  ASN   B N    1 
ATOM   4776 C CA   . ASN   B 1 59  ? 59.787 -16.175 1.960   1.00 15.61 ?  59  ASN   B CA   1 
ATOM   4777 C C    . ASN   B 1 59  ? 59.193 -14.767 1.907   1.00 15.17 ?  59  ASN   B C    1 
ATOM   4778 O O    . ASN   B 1 59  ? 58.762 -14.264 2.949   1.00 15.17 ?  59  ASN   B O    1 
ATOM   4779 C CB   . ASN   B 1 59  ? 60.855 -16.239 3.067   1.00 16.70 ?  59  ASN   B CB   1 
ATOM   4780 C CG   . ASN   B 1 59  ? 60.261 -16.417 4.449   1.00 18.07 ?  59  ASN   B CG   1 
ATOM   4781 O OD1  . ASN   B 1 59  ? 59.438 -17.308 4.676   1.00 17.95 ?  59  ASN   B OD1  1 
ATOM   4782 N ND2  . ASN   B 1 59  ? 60.675 -15.567 5.383   1.00 19.06 ?  59  ASN   B ND2  1 
ATOM   4783 H H    . ASN   B 1 59  ? 59.725 -17.219 0.307   1.00 19.08 ?  59  ASN   B H    1 
ATOM   4784 H HA   . ASN   B 1 59  ? 59.075 -16.773 2.238   1.00 18.88 ?  59  ASN   B HA   1 
ATOM   4785 H HB2  . ASN   B 1 59  ? 61.444 -16.991 2.904   1.00 20.19 ?  59  ASN   B HB2  1 
ATOM   4786 H HB3  . ASN   B 1 59  ? 61.361 -15.413 3.070   1.00 20.19 ?  59  ASN   B HB3  1 
ATOM   4787 H HD21 . ASN   B 1 59  ? 60.364 -15.623 6.185   1.00 23.02 ?  59  ASN   B HD21 1 
ATOM   4788 H HD22 . ASN   B 1 59  ? 61.247 -14.958 5.187   1.00 23.02 ?  59  ASN   B HD22 1 
ATOM   4789 N N    . ALA   B 1 60  ? 59.120 -14.125 0.738   1.00 14.96 ?  60  ALA   B N    1 
ATOM   4790 C CA   . ALA   B 1 60  ? 58.521 -12.792 0.671   1.00 14.82 ?  60  ALA   B CA   1 
ATOM   4791 C C    . ALA   B 1 60  ? 57.050 -12.818 1.070   1.00 13.99 ?  60  ALA   B C    1 
ATOM   4792 O O    . ALA   B 1 60  ? 56.550 -11.872 1.689   1.00 14.79 ?  60  ALA   B O    1 
ATOM   4793 C CB   . ALA   B 1 60  ? 58.693 -12.207 -0.730  1.00 16.07 ?  60  ALA   B CB   1 
ATOM   4794 H H    . ALA   B 1 60  ? 59.411 -14.435 -0.009  1.00 18.10 ?  60  ALA   B H    1 
ATOM   4795 H HA   . ALA   B 1 60  ? 58.985 -12.214 1.296   1.00 17.93 ?  60  ALA   B HA   1 
ATOM   4796 H HB1  . ALA   B 1 60  ? 58.293 -11.326 -0.752  1.00 19.44 ?  60  ALA   B HB1  1 
ATOM   4797 H HB2  . ALA   B 1 60  ? 59.643 -12.145 -0.931  1.00 19.44 ?  60  ALA   B HB2  1 
ATOM   4798 H HB3  . ALA   B 1 60  ? 58.258 -12.789 -1.371  1.00 19.44 ?  60  ALA   B HB3  1 
ATOM   4799 N N    . MET   B 1 61  ? 56.342 -13.892 0.720   1.00 13.32 ?  61  MET   B N    1 
ATOM   4800 C CA   . MET   B 1 61  ? 54.948 -14.019 1.118   1.00 13.23 ?  61  MET   B CA   1 
ATOM   4801 C C    . MET   B 1 61  ? 54.818 -14.024 2.639   1.00 13.16 ?  61  MET   B C    1 
ATOM   4802 O O    . MET   B 1 61  ? 53.923 -13.371 3.193   1.00 13.24 ?  61  MET   B O    1 
ATOM   4803 C CB   . MET   B 1 61  ? 54.369 -15.286 0.487   1.00 13.15 ?  61  MET   B CB   1 
ATOM   4804 C CG   . MET   B 1 61  ? 52.920 -15.577 0.895   1.00 12.79 ?  61  MET   B CG   1 
ATOM   4805 S SD   . MET   B 1 61  ? 52.292 -17.088 0.137   1.00 13.55 ?  61  MET   B SD   1 
ATOM   4806 C CE   . MET   B 1 61  ? 52.047 -16.494 -1.537  1.00 14.89 ?  61  MET   B CE   1 
ATOM   4807 H H    . MET   B 1 61  ? 56.645 -14.553 0.253   1.00 16.14 ?  61  MET   B H    1 
ATOM   4808 H HA   . MET   B 1 61  ? 54.453 -13.264 0.761   1.00 16.03 ?  61  MET   B HA   1 
ATOM   4809 H HB2  . MET   B 1 61  ? 54.391 -15.198 -0.480  1.00 15.92 ?  61  MET   B HB2  1 
ATOM   4810 H HB3  . MET   B 1 61  ? 54.908 -16.046 0.757   1.00 15.92 ?  61  MET   B HB3  1 
ATOM   4811 H HG2  . MET   B 1 61  ? 52.870 -15.681 1.858   1.00 15.50 ?  61  MET   B HG2  1 
ATOM   4812 H HG3  . MET   B 1 61  ? 52.355 -14.837 0.611   1.00 15.50 ?  61  MET   B HG3  1 
ATOM   4813 H HE1  . MET   B 1 61  ? 51.662 -17.206 -2.071  1.00 18.02 ?  61  MET   B HE1  1 
ATOM   4814 H HE2  . MET   B 1 61  ? 51.446 -15.732 -1.519  1.00 18.02 ?  61  MET   B HE2  1 
ATOM   4815 H HE3  . MET   B 1 61  ? 52.904 -16.229 -1.908  1.00 18.02 ?  61  MET   B HE3  1 
ATOM   4816 N N    . GLN   B 1 62  ? 55.703 -14.741 3.338   1.00 12.92 ?  62  GLN   B N    1 
ATOM   4817 C CA   . GLN   B 1 62  ? 55.599 -14.798 4.794   1.00 13.55 ?  62  GLN   B CA   1 
ATOM   4818 C C    . GLN   B 1 62  ? 55.883 -13.441 5.426   1.00 13.98 ?  62  GLN   B C    1 
ATOM   4819 O O    . GLN   B 1 62  ? 55.201 -13.040 6.376   1.00 14.52 ?  62  GLN   B O    1 
ATOM   4820 C CB   . GLN   B 1 62  ? 56.560 -15.843 5.358   1.00 13.80 ?  62  GLN   B CB   1 
ATOM   4821 C CG   . GLN   B 1 62  ? 56.337 -16.127 6.835   1.00 14.38 ?  62  GLN   B CG   1 
ATOM   4822 C CD   . GLN   B 1 62  ? 54.958 -16.717 7.083   1.00 13.96 ?  62  GLN   B CD   1 
ATOM   4823 O OE1  . GLN   B 1 62  ? 54.697 -17.868 6.740   1.00 14.49 ?  62  GLN   B OE1  1 
ATOM   4824 N NE2  . GLN   B 1 62  ? 54.058 -15.919 7.641   1.00 14.63 ?  62  GLN   B NE2  1 
ATOM   4825 H H    . GLN   B 1 62  ? 56.352 -15.195 2.996   1.00 15.66 ?  62  GLN   B H    1 
ATOM   4826 H HA   . GLN   B 1 62  ? 54.696 -15.056 5.028   1.00 16.40 ?  62  GLN   B HA   1 
ATOM   4827 H HB2  . GLN   B 1 62  ? 56.445 -16.674 4.872   1.00 16.71 ?  62  GLN   B HB2  1 
ATOM   4828 H HB3  . GLN   B 1 62  ? 57.471 -15.522 5.249   1.00 16.71 ?  62  GLN   B HB3  1 
ATOM   4829 H HG2  . GLN   B 1 62  ? 57.003 -16.769 7.136   1.00 17.41 ?  62  GLN   B HG2  1 
ATOM   4830 H HG3  . GLN   B 1 62  ? 56.417 -15.303 7.337   1.00 17.41 ?  62  GLN   B HG3  1 
ATOM   4831 H HE21 . GLN   B 1 62  ? 54.272 -15.115 7.856   1.00 17.70 ?  62  GLN   B HE21 1 
ATOM   4832 H HE22 . GLN   B 1 62  ? 53.266 -16.212 7.793   1.00 17.70 ?  62  GLN   B HE22 1 
ATOM   4833 N N    . VAL   B 1 63  ? 56.895 -12.728 4.933   1.00 14.42 ?  63  VAL   B N    1 
ATOM   4834 C CA   . VAL   B 1 63  ? 57.195 -11.408 5.489   1.00 15.34 ?  63  VAL   B CA   1 
ATOM   4835 C C    . VAL   B 1 63  ? 56.001 -10.476 5.306   1.00 14.63 ?  63  VAL   B C    1 
ATOM   4836 O O    . VAL   B 1 63  ? 55.593 -9.765  6.236   1.00 15.30 ?  63  VAL   B O    1 
ATOM   4837 C CB   . VAL   B 1 63  ? 58.490 -10.842 4.876   1.00 16.95 ?  63  VAL   B CB   1 
ATOM   4838 C CG1  . VAL   B 1 63  ? 58.710 -9.396  5.324   1.00 17.62 ?  63  VAL   B CG1  1 
ATOM   4839 C CG2  . VAL   B 1 63  ? 59.681 -11.712 5.271   1.00 17.76 ?  63  VAL   B CG2  1 
ATOM   4840 H H    . VAL   B 1 63  ? 57.412 -12.979 4.288   1.00 17.45 ?  63  VAL   B H    1 
ATOM   4841 H HA   . VAL   B 1 63  ? 57.346 -11.508 6.438   1.00 18.56 ?  63  VAL   B HA   1 
ATOM   4842 H HB   . VAL   B 1 63  ? 58.424 -10.854 3.910   1.00 20.49 ?  63  VAL   B HB   1 
ATOM   4843 H HG11 . VAL   B 1 63  ? 59.626 -9.141  5.133   1.00 21.29 ?  63  VAL   B HG11 1 
ATOM   4844 H HG12 . VAL   B 1 63  ? 58.099 -8.818  4.845   1.00 21.29 ?  63  VAL   B HG12 1 
ATOM   4845 H HG13 . VAL   B 1 63  ? 58.547 -9.334  6.281   1.00 21.29 ?  63  VAL   B HG13 1 
ATOM   4846 H HG21 . VAL   B 1 63  ? 60.490 -11.329 4.894   1.00 21.46 ?  63  VAL   B HG21 1 
ATOM   4847 H HG22 . VAL   B 1 63  ? 59.748 -11.732 6.240   1.00 21.46 ?  63  VAL   B HG22 1 
ATOM   4848 H HG23 . VAL   B 1 63  ? 59.547 -12.607 4.929   1.00 21.46 ?  63  VAL   B HG23 1 
ATOM   4849 N N    . GLU   B 1 64  ? 55.427 -10.466 4.102   1.00 14.52 ?  64  GLU   B N    1 
ATOM   4850 C CA   . GLU   B 1 64  ? 54.261 -9.626  3.835   1.00 13.96 ?  64  GLU   B CA   1 
ATOM   4851 C C    . GLU   B 1 64  ? 53.082 -10.029 4.716   1.00 13.54 ?  64  GLU   B C    1 
ATOM   4852 O O    . GLU   B 1 64  ? 52.334 -9.171  5.216   1.00 14.26 ?  64  GLU   B O    1 
ATOM   4853 C CB   . GLU   B 1 64  ? 53.902 -9.769  2.354   1.00 14.39 ?  64  GLU   B CB   1 
ATOM   4854 C CG   . GLU   B 1 64  ? 52.647 -9.025  1.922   1.00 14.63 ?  64  GLU   B CG   1 
ATOM   4855 C CD   . GLU   B 1 64  ? 52.105 -9.513  0.583   1.00 15.71 ?  64  GLU   B CD   1 
ATOM   4856 O OE1  . GLU   B 1 64  ? 52.285 -10.717 0.250   1.00 16.65 ?  64  GLU   B OE1  1 
ATOM   4857 O OE2  . GLU   B 1 64  ? 51.480 -8.695  -0.137  1.00 16.31 -1 64  GLU   B OE2  1 
ATOM   4858 H H    . GLU   B 1 64  ? 55.700 -10.929 3.424   1.00 17.57 ?  64  GLU   B H    1 
ATOM   4859 H HA   . GLU   B 1 64  ? 54.484 -8.699  4.010   1.00 16.90 ?  64  GLU   B HA   1 
ATOM   4860 H HB2  . GLU   B 1 64  ? 54.638 -9.421  1.818   1.00 17.41 ?  64  GLU   B HB2  1 
ATOM   4861 H HB3  . GLU   B 1 64  ? 53.773 -10.706 2.155   1.00 17.41 ?  64  GLU   B HB3  1 
ATOM   4862 H HG2  . GLU   B 1 64  ? 51.945 -9.152  2.584   1.00 17.70 ?  64  GLU   B HG2  1 
ATOM   4863 H HG3  . GLU   B 1 64  ? 52.847 -8.081  1.835   1.00 17.70 ?  64  GLU   B HG3  1 
ATOM   4864 N N    . SER   B 1 65  ? 52.900 -11.336 4.907   1.00 13.31 ?  65  SER   B N    1 
ATOM   4865 C CA   . SER   B 1 65  ? 51.792 -11.843 5.705   1.00 13.33 ?  65  SER   B CA   1 
ATOM   4866 C C    . SER   B 1 65  ? 51.923 -11.441 7.169   1.00 13.52 ?  65  SER   B C    1 
ATOM   4867 O O    . SER   B 1 65  ? 50.926 -11.059 7.801   1.00 14.15 ?  65  SER   B O    1 
ATOM   4868 C CB   . SER   B 1 65  ? 51.704 -13.368 5.569   1.00 13.62 ?  65  SER   B CB   1 
ATOM   4869 O OG   . SER   B 1 65  ? 51.364 -13.764 4.251   1.00 13.98 ?  65  SER   B OG   1 
ATOM   4870 H H    . SER   B 1 65  ? 53.409 -11.956 4.587   1.00 16.11 ?  65  SER   B H    1 
ATOM   4871 H HA   . SER   B 1 65  ? 50.962 -11.469 5.368   1.00 16.15 ?  65  SER   B HA   1 
ATOM   4872 H HB2  . SER   B 1 65  ? 52.563 -13.754 5.792   1.00 16.49 ?  65  SER   B HB2  1 
ATOM   4873 H HB3  . SER   B 1 65  ? 51.024 -13.698 6.180   1.00 16.49 ?  65  SER   B HB3  1 
ATOM   4874 H HG   . SER   B 1 65  ? 51.935 -13.466 3.705   1.00 16.93 ?  65  SER   B HG   1 
ATOM   4875 N N    . ASP   B 1 66  ? 53.133 -11.547 7.737   1.00 13.85 ?  66  ASP   B N    1 
ATOM   4876 C CA   . ASP   B 1 66  ? 53.326 -11.153 9.131   1.00 14.31 ?  66  ASP   B CA   1 
ATOM   4877 C C    . ASP   B 1 66  ? 53.009 -9.673  9.334   1.00 14.76 ?  66  ASP   B C    1 
ATOM   4878 O O    . ASP   B 1 66  ? 52.442 -9.284  10.361  1.00 14.98 ?  66  ASP   B O    1 
ATOM   4879 C CB   . ASP   B 1 66  ? 54.760 -11.458 9.569   1.00 15.84 ?  66  ASP   B CB   1 
ATOM   4880 C CG   . ASP   B 1 66  ? 55.031 -12.953 9.729   1.00 17.53 ?  66  ASP   B CG   1 
ATOM   4881 O OD1  . ASP   B 1 66  ? 54.082 -13.769 9.646   1.00 18.22 ?  66  ASP   B OD1  1 
ATOM   4882 O OD2  . ASP   B 1 66  ? 56.210 -13.315 9.948   1.00 20.54 -1 66  ASP   B OD2  1 
ATOM   4883 H H    . ASP   B 1 66  ? 53.837 -11.846 7.342   1.00 16.77 ?  66  ASP   B H    1 
ATOM   4884 H HA   . ASP   B 1 66  ? 52.727 -11.664 9.693   1.00 17.32 ?  66  ASP   B HA   1 
ATOM   4885 H HB2  . ASP   B 1 66  ? 55.375 -11.110 8.902   1.00 19.16 ?  66  ASP   B HB2  1 
ATOM   4886 H HB3  . ASP   B 1 66  ? 54.925 -11.029 10.425  1.00 19.16 ?  66  ASP   B HB3  1 
ATOM   4887 N N    . ASP   B 1 67  ? 53.385 -8.828  8.373   1.00 14.22 ?  67  ASP   B N    1 
ATOM   4888 C CA   . ASP   B 1 67  ? 53.035 -7.415  8.463   1.00 15.00 ?  67  ASP   B CA   1 
ATOM   4889 C C    . ASP   B 1 67  ? 51.520 -7.207  8.372   1.00 15.10 ?  67  ASP   B C    1 
ATOM   4890 O O    . ASP   B 1 67  ? 50.952 -6.396  9.114   1.00 15.46 ?  67  ASP   B O    1 
ATOM   4891 C CB   . ASP   B 1 67  ? 53.758 -6.645  7.367   1.00 16.14 ?  67  ASP   B CB   1 
ATOM   4892 C CG   . ASP   B 1 67  ? 53.340 -5.200  7.327   1.00 17.68 ?  67  ASP   B CG   1 
ATOM   4893 O OD1  . ASP   B 1 67  ? 53.823 -4.400  8.163   1.00 18.87 ?  67  ASP   B OD1  1 
ATOM   4894 O OD2  . ASP   B 1 67  ? 52.491 -4.883  6.482   1.00 18.93 -1 67  ASP   B OD2  1 
ATOM   4895 H H    . ASP   B 1 67  ? 53.840 -9.046  7.673   1.00 17.21 ?  67  ASP   B H    1 
ATOM   4896 H HA   . ASP   B 1 67  ? 53.338 -7.072  9.317   1.00 18.15 ?  67  ASP   B HA   1 
ATOM   4897 H HB2  . ASP   B 1 67  ? 54.717 -6.681  7.530   1.00 19.52 ?  67  ASP   B HB2  1 
ATOM   4898 H HB3  . ASP   B 1 67  ? 53.558 -7.049  6.506   1.00 19.52 ?  67  ASP   B HB3  1 
ATOM   4899 N N    . TYR   B 1 68  ? 50.844 -7.934  7.475   1.00 14.52 ?  68  TYR   B N    1 
ATOM   4900 C CA   . TYR   B 1 68  ? 49.384 -7.860  7.410   1.00 15.24 ?  68  TYR   B CA   1 
ATOM   4901 C C    . TYR   B 1 68  ? 48.755 -8.213  8.755   1.00 14.84 ?  68  TYR   B C    1 
ATOM   4902 O O    . TYR   B 1 68  ? 47.825 -7.535  9.213   1.00 15.48 ?  68  TYR   B O    1 
ATOM   4903 C CB   . TYR   B 1 68  ? 48.848 -8.785  6.310   1.00 16.29 ?  68  TYR   B CB   1 
ATOM   4904 C CG   . TYR   B 1 68  ? 47.337 -8.938  6.366   1.00 17.29 ?  68  TYR   B CG   1 
ATOM   4905 C CD1  . TYR   B 1 68  ? 46.747 -9.894  7.186   1.00 18.28 ?  68  TYR   B CD1  1 
ATOM   4906 C CD2  . TYR   B 1 68  ? 46.506 -8.097  5.646   1.00 18.41 ?  68  TYR   B CD2  1 
ATOM   4907 C CE1  . TYR   B 1 68  ? 45.379 -10.018 7.274   1.00 19.46 ?  68  TYR   B CE1  1 
ATOM   4908 C CE2  . TYR   B 1 68  ? 45.125 -8.221  5.723   1.00 18.95 ?  68  TYR   B CE2  1 
ATOM   4909 C CZ   . TYR   B 1 68  ? 44.583 -9.182  6.539   1.00 19.45 ?  68  TYR   B CZ   1 
ATOM   4910 O OH   . TYR   B 1 68  ? 43.215 -9.306  6.635   1.00 20.58 ?  68  TYR   B OH   1 
ATOM   4911 H H    . TYR   B 1 68  ? 51.203 -8.476  6.908   1.00 17.57 ?  68  TYR   B H    1 
ATOM   4912 H HA   . TYR   B 1 68  ? 49.129 -6.953  7.191   1.00 18.44 ?  68  TYR   B HA   1 
ATOM   4913 H HB2  . TYR   B 1 68  ? 49.076 -8.414  5.446   1.00 19.70 ?  68  TYR   B HB2  1 
ATOM   4914 H HB3  . TYR   B 1 68  ? 49.242 -9.664  6.413   1.00 19.70 ?  68  TYR   B HB3  1 
ATOM   4915 H HD1  . TYR   B 1 68  ? 47.288 -10.466 7.685   1.00 22.09 ?  68  TYR   B HD1  1 
ATOM   4916 H HD2  . TYR   B 1 68  ? 46.879 -7.443  5.107   1.00 22.24 ?  68  TYR   B HD2  1 
ATOM   4917 H HE1  . TYR   B 1 68  ? 45.001 -10.678 7.817   1.00 23.50 ?  68  TYR   B HE1  1 
ATOM   4918 H HE2  . TYR   B 1 68  ? 44.571 -7.654  5.237   1.00 22.89 ?  68  TYR   B HE2  1 
ATOM   4919 H HH   . TYR   B 1 68  ? 42.824 -8.750  6.134   1.00 24.84 ?  68  TYR   B HH   1 
ATOM   4920 N N    . ILE   B 1 69  ? 49.245 -9.278  9.399   1.00 14.39 ?  69  ILE   B N    1 
ATOM   4921 C CA   . ILE   B 1 69  ? 48.688 -9.706  10.681  1.00 15.34 ?  69  ILE   B CA   1 
ATOM   4922 C C    . ILE   B 1 69  ? 48.945 -8.660  11.760  1.00 14.85 ?  69  ILE   B C    1 
ATOM   4923 O O    . ILE   B 1 69  ? 48.075 -8.378  12.593  1.00 15.06 ?  69  ILE   B O    1 
ATOM   4924 C CB   . ILE   B 1 69  ? 49.263 -11.085 11.069  1.00 16.33 ?  69  ILE   B CB   1 
ATOM   4925 C CG1  . ILE   B 1 69  ? 48.740 -12.198 10.146  1.00 16.76 ?  69  ILE   B CG1  1 
ATOM   4926 C CG2  . ILE   B 1 69  ? 48.982 -11.402 12.531  1.00 17.66 ?  69  ILE   B CG2  1 
ATOM   4927 C CD1  . ILE   B 1 69  ? 47.263 -12.518 10.302  1.00 16.83 ?  69  ILE   B CD1  1 
ATOM   4928 H H    . ILE   B 1 69  ? 49.894 -9.766  9.117   1.00 17.41 ?  69  ILE   B H    1 
ATOM   4929 H HA   . ILE   B 1 69  ? 47.729 -9.804  10.586  1.00 18.56 ?  69  ILE   B HA   1 
ATOM   4930 H HB   . ILE   B 1 69  ? 50.228 -11.042 10.959  1.00 19.74 ?  69  ILE   B HB   1 
ATOM   4931 H HG12 . ILE   B 1 69  ? 48.889 -11.928 9.225   1.00 20.26 ?  69  ILE   B HG12 1 
ATOM   4932 H HG13 . ILE   B 1 69  ? 49.242 -13.010 10.328  1.00 20.26 ?  69  ILE   B HG13 1 
ATOM   4933 H HG21 . ILE   B 1 69  ? 49.116 -12.353 12.675  1.00 21.34 ?  69  ILE   B HG21 1 
ATOM   4934 H HG22 . ILE   B 1 69  ? 49.595 -10.898 13.091  1.00 21.34 ?  69  ILE   B HG22 1 
ATOM   4935 H HG23 . ILE   B 1 69  ? 48.067 -11.163 12.736  1.00 21.34 ?  69  ILE   B HG23 1 
ATOM   4936 H HD11 . ILE   B 1 69  ? 47.030 -13.228 9.682   1.00 20.35 ?  69  ILE   B HD11 1 
ATOM   4937 H HD12 . ILE   B 1 69  ? 47.097 -12.812 11.213  1.00 20.35 ?  69  ILE   B HD12 1 
ATOM   4938 H HD13 . ILE   B 1 69  ? 46.743 -11.726 10.108  1.00 20.35 ?  69  ILE   B HD13 1 
ATOM   4939 N N    . ALA   B 1 70  ? 50.139 -8.073  11.779  1.00 14.81 ?  70  ALA   B N    1 
ATOM   4940 C CA   . ALA   B 1 70  ? 50.418 -7.036  12.767  1.00 14.60 ?  70  ALA   B CA   1 
ATOM   4941 C C    . ALA   B 1 70  ? 49.412 -5.896  12.664  1.00 15.26 ?  70  ALA   B C    1 
ATOM   4942 O O    . ALA   B 1 70  ? 48.966 -5.351  13.681  1.00 15.56 ?  70  ALA   B O    1 
ATOM   4943 C CB   . ALA   B 1 70  ? 51.847 -6.518  12.595  1.00 15.33 ?  70  ALA   B CB   1 
ATOM   4944 H H    . ALA   B 1 70  ? 50.785 -8.255  11.248  1.00 17.92 ?  70  ALA   B H    1 
ATOM   4945 H HA   . ALA   B 1 70  ? 50.352 -7.418  13.658  1.00 17.67 ?  70  ALA   B HA   1 
ATOM   4946 H HB1  . ALA   B 1 70  ? 52.036 -5.863  13.287  1.00 18.55 ?  70  ALA   B HB1  1 
ATOM   4947 H HB2  . ALA   B 1 70  ? 52.469 -7.262  12.672  1.00 18.55 ?  70  ALA   B HB2  1 
ATOM   4948 H HB3  . ALA   B 1 70  ? 51.935 -6.108  11.719  1.00 18.55 ?  70  ALA   B HB3  1 
ATOM   4949 N N    . THR   B 1 71  ? 49.042 -5.520  11.442  1.00 15.58 ?  71  THR   B N    1 
ATOM   4950 C CA   . THR   B 1 71  ? 48.143 -4.389  11.238  1.00 16.45 ?  71  THR   B CA   1 
ATOM   4951 C C    . THR   B 1 71  ? 46.680 -4.764  11.447  1.00 17.21 ?  71  THR   B C    1 
ATOM   4952 O O    . THR   B 1 71  ? 45.901 -3.956  11.966  1.00 18.64 ?  71  THR   B O    1 
ATOM   4953 C CB   . THR   B 1 71  ? 48.361 -3.823  9.834   1.00 18.23 ?  71  THR   B CB   1 
ATOM   4954 O OG1  . THR   B 1 71  ? 49.696 -3.314  9.729   1.00 20.31 ?  71  THR   B OG1  1 
ATOM   4955 C CG2  . THR   B 1 71  ? 47.359 -2.723  9.517   1.00 19.67 ?  71  THR   B CG2  1 
ATOM   4956 H H    . THR   B 1 71  ? 49.299 -5.905  10.719  1.00 18.85 ?  71  THR   B H    1 
ATOM   4957 H HA   . THR   B 1 71  ? 48.367 -3.692  11.874  1.00 19.89 ?  71  THR   B HA   1 
ATOM   4958 H HB   . THR   B 1 71  ? 48.253 -4.529  9.180   1.00 22.03 ?  71  THR   B HB   1 
ATOM   4959 H HG1  . THR   B 1 71  ? 49.827 -2.983  8.965   1.00 24.52 ?  71  THR   B HG1  1 
ATOM   4960 H HG21 . THR   B 1 71  ? 47.661 -2.211  8.749   1.00 23.75 ?  71  THR   B HG21 1 
ATOM   4961 H HG22 . THR   B 1 71  ? 46.494 -3.107  9.317   1.00 23.75 ?  71  THR   B HG22 1 
ATOM   4962 H HG23 . THR   B 1 71  ? 47.275 -2.123  10.276  1.00 23.75 ?  71  THR   B HG23 1 
ATOM   4963 N N    . ASN   B 1 72  ? 46.288 -5.977  11.053  1.00 16.96 ?  72  ASN   B N    1 
ATOM   4964 C CA   . ASN   B 1 72  ? 44.882 -6.328  10.921  1.00 16.99 ?  72  ASN   B CA   1 
ATOM   4965 C C    . ASN   B 1 72  ? 44.403 -7.422  11.861  1.00 17.95 ?  72  ASN   B C    1 
ATOM   4966 O O    . ASN   B 1 72  ? 43.186 -7.577  12.022  1.00 18.73 ?  72  ASN   B O    1 
ATOM   4967 C CB   . ASN   B 1 72  ? 44.580 -6.749  9.475   1.00 17.82 ?  72  ASN   B CB   1 
ATOM   4968 C CG   . ASN   B 1 72  ? 44.852 -5.642  8.488   1.00 19.00 ?  72  ASN   B CG   1 
ATOM   4969 O OD1  . ASN   B 1 72  ? 45.868 -5.641  7.787   1.00 20.47 ?  72  ASN   B OD1  1 
ATOM   4970 N ND2  . ASN   B 1 72  ? 43.965 -4.668  8.453   1.00 20.79 ?  72  ASN   B ND2  1 
ATOM   4971 H H    . ASN   B 1 72  ? 46.829 -6.623  10.856  1.00 20.51 ?  72  ASN   B H    1 
ATOM   4972 H HA   . ASN   B 1 72  ? 44.356 -5.536  11.102  1.00 20.54 ?  72  ASN   B HA   1 
ATOM   4973 H HB2  . ASN   B 1 72  ? 45.144 -7.506  9.239   1.00 21.53 ?  72  ASN   B HB2  1 
ATOM   4974 H HB3  . ASN   B 1 72  ? 43.647 -6.995  9.403   1.00 21.53 ?  72  ASN   B HB3  1 
ATOM   4975 H HD21 . ASN   B 1 72  ? 44.066 -4.011  7.907   1.00 25.09 ?  72  ASN   B HD21 1 
ATOM   4976 H HD22 . ASN   B 1 72  ? 43.269 -4.701  8.960   1.00 25.09 ?  72  ASN   B HD22 1 
ATOM   4977 N N    . GLY   B 1 73  ? 45.300 -8.175  12.487  1.00 17.19 ?  73  GLY   B N    1 
ATOM   4978 C CA   . GLY   B 1 73  ? 44.895 -9.315  13.273  1.00 16.60 ?  73  GLY   B CA   1 
ATOM   4979 C C    . GLY   B 1 73  ? 44.545 -10.505 12.403  1.00 15.54 ?  73  GLY   B C    1 
ATOM   4980 O O    . GLY   B 1 73  ? 44.538 -10.422 11.173  1.00 15.39 ?  73  GLY   B O    1 
ATOM   4981 H H    . GLY   B 1 73  ? 46.150 -8.039  12.468  1.00 20.78 ?  73  GLY   B H    1 
ATOM   4982 H HA2  . GLY   B 1 73  ? 45.617 -9.565  13.871  1.00 20.07 ?  73  GLY   B HA2  1 
ATOM   4983 H HA3  . GLY   B 1 73  ? 44.120 -9.079  13.810  1.00 20.07 ?  73  GLY   B HA3  1 
ATOM   4984 N N    . PRO   B 1 74  ? 44.237 -11.633 13.037  1.00 15.24 ?  74  PRO   B N    1 
ATOM   4985 C CA   . PRO   B 1 74  ? 43.994 -12.867 12.288  1.00 14.96 ?  74  PRO   B CA   1 
ATOM   4986 C C    . PRO   B 1 74  ? 42.692 -12.817 11.499  1.00 14.31 ?  74  PRO   B C    1 
ATOM   4987 O O    . PRO   B 1 74  ? 41.754 -12.075 11.813  1.00 15.81 ?  74  PRO   B O    1 
ATOM   4988 C CB   . PRO   B 1 74  ? 43.927 -13.931 13.388  1.00 16.47 ?  74  PRO   B CB   1 
ATOM   4989 C CG   . PRO   B 1 74  ? 43.464 -13.188 14.593  1.00 17.98 ?  74  PRO   B CG   1 
ATOM   4990 C CD   . PRO   B 1 74  ? 44.115 -11.837 14.490  1.00 17.08 ?  74  PRO   B CD   1 
ATOM   4991 H HA   . PRO   B 1 74  ? 44.740 -13.051 11.689  1.00 18.10 ?  74  PRO   B HA   1 
ATOM   4992 H HB2  . PRO   B 1 74  ? 43.289 -14.616 13.134  1.00 19.91 ?  74  PRO   B HB2  1 
ATOM   4993 H HB3  . PRO   B 1 74  ? 44.807 -14.310 13.529  1.00 19.91 ?  74  PRO   B HB3  1 
ATOM   4994 H HG2  . PRO   B 1 74  ? 42.498 -13.107 14.573  1.00 21.72 ?  74  PRO   B HG2  1 
ATOM   4995 H HG3  . PRO   B 1 74  ? 43.757 -13.651 15.391  1.00 21.72 ?  74  PRO   B HG3  1 
ATOM   4996 H HD2  . PRO   B 1 74  ? 43.546 -11.156 14.887  1.00 20.64 ?  74  PRO   B HD2  1 
ATOM   4997 H HD3  . PRO   B 1 74  ? 44.993 -11.850 14.901  1.00 20.64 ?  74  PRO   B HD3  1 
ATOM   4998 N N    . LEU   B 1 75  ? 42.661 -13.628 10.446  1.00 13.59 ?  75  LEU   B N    1 
ATOM   4999 C CA   . LEU   B 1 75  ? 41.449 -13.849 9.676   1.00 13.62 ?  75  LEU   B CA   1 
ATOM   5000 C C    . LEU   B 1 75  ? 40.471 -14.705 10.480  1.00 13.91 ?  75  LEU   B C    1 
ATOM   5001 O O    . LEU   B 1 75  ? 40.808 -15.260 11.527  1.00 14.96 ?  75  LEU   B O    1 
ATOM   5002 C CB   . LEU   B 1 75  ? 41.779 -14.570 8.369   1.00 13.71 ?  75  LEU   B CB   1 
ATOM   5003 C CG   . LEU   B 1 75  ? 42.599 -13.812 7.320   1.00 15.76 ?  75  LEU   B CG   1 
ATOM   5004 C CD1  . LEU   B 1 75  ? 42.747 -14.635 6.045   1.00 16.85 ?  75  LEU   B CD1  1 
ATOM   5005 C CD2  . LEU   B 1 75  ? 42.013 -12.460 7.002   1.00 19.37 ?  75  LEU   B CD2  1 
ATOM   5006 H H    . LEU   B 1 75  ? 43.340 -14.071 10.151  1.00 16.45 ?  75  LEU   B H    1 
ATOM   5007 H HA   . LEU   B 1 75  ? 41.025 -13.003 9.469   1.00 16.50 ?  75  LEU   B HA   1 
ATOM   5008 H HB2  . LEU   B 1 75  ? 42.278 -15.376 8.583   1.00 16.61 ?  75  LEU   B HB2  1 
ATOM   5009 H HB3  . LEU   B 1 75  ? 40.945 -14.823 7.940   1.00 16.61 ?  75  LEU   B HB3  1 
ATOM   5010 H HG   . LEU   B 1 75  ? 43.491 -13.671 7.670   1.00 19.06 ?  75  LEU   B HG   1 
ATOM   5011 H HD11 . LEU   B 1 75  ? 43.277 -14.134 5.400   1.00 20.37 ?  75  LEU   B HD11 1 
ATOM   5012 H HD12 . LEU   B 1 75  ? 43.195 -15.472 6.253   1.00 20.37 ?  75  LEU   B HD12 1 
ATOM   5013 H HD13 . LEU   B 1 75  ? 41.868 -14.816 5.675   1.00 20.37 ?  75  LEU   B HD13 1 
ATOM   5014 H HD21 . LEU   B 1 75  ? 42.498 -12.072 6.260   1.00 23.39 ?  75  LEU   B HD21 1 
ATOM   5015 H HD22 . LEU   B 1 75  ? 41.079 -12.571 6.770   1.00 23.39 ?  75  LEU   B HD22 1 
ATOM   5016 H HD23 . LEU   B 1 75  ? 42.096 -11.895 7.786   1.00 23.39 ?  75  LEU   B HD23 1 
ATOM   5017 N N    . LYS   B 1 76  ? 39.237 -14.801 9.970   1.00 15.38 ?  76  LYS   B N    1 
ATOM   5018 C CA   . LYS   B 1 76  ? 38.241 -15.761 10.438  1.00 16.76 ?  76  LYS   B CA   1 
ATOM   5019 C C    . LYS   B 1 76  ? 38.334 -17.033 9.598   1.00 15.18 ?  76  LYS   B C    1 
ATOM   5020 O O    . LYS   B 1 76  ? 38.612 -16.977 8.401   1.00 14.96 ?  76  LYS   B O    1 
ATOM   5021 C CB   . LYS   B 1 76  ? 36.819 -15.197 10.261  1.00 18.89 ?  76  LYS   B CB   1 
ATOM   5022 C CG   . LYS   B 1 76  ? 36.555 -13.789 10.822  1.00 21.41 ?  76  LYS   B CG   1 
ATOM   5023 C CD   . LYS   B 1 76  ? 35.133 -13.288 10.507  1.00 23.16 ?  76  LYS   B CD   1 
ATOM   5024 C CE   . LYS   B 1 76  ? 34.881 -11.911 11.106  1.00 25.48 ?  76  LYS   B CE   1 
ATOM   5025 N NZ   . LYS   B 1 76  ? 33.568 -11.331 10.708  1.00 26.25 ?  76  LYS   B NZ   1 
ATOM   5026 H H    . LYS   B 1 76  ? 38.950 -14.304 9.333   1.00 18.60 ?  76  LYS   B H    1 
ATOM   5027 H HA   . LYS   B 1 76  ? 38.390 -15.983 11.371  1.00 20.26 ?  76  LYS   B HA   1 
ATOM   5028 H HB2  . LYS   B 1 76  ? 36.621 -15.169 9.311   1.00 22.81 ?  76  LYS   B HB2  1 
ATOM   5029 H HB3  . LYS   B 1 76  ? 36.196 -15.800 10.698  1.00 22.81 ?  76  LYS   B HB3  1 
ATOM   5030 H HG2  . LYS   B 1 76  ? 36.664 -13.806 11.785  1.00 25.84 ?  76  LYS   B HG2  1 
ATOM   5031 H HG3  . LYS   B 1 76  ? 37.188 -13.168 10.426  1.00 25.84 ?  76  LYS   B HG3  1 
ATOM   5032 H HD2  . LYS   B 1 76  ? 35.019 -13.228 9.545   1.00 27.94 ?  76  LYS   B HD2  1 
ATOM   5033 H HD3  . LYS   B 1 76  ? 34.485 -13.906 10.882  1.00 27.94 ?  76  LYS   B HD3  1 
ATOM   5034 H HE2  . LYS   B 1 76  ? 34.899 -11.980 12.073  1.00 30.73 ?  76  LYS   B HE2  1 
ATOM   5035 H HE3  . LYS   B 1 76  ? 35.579 -11.305 10.806  1.00 30.73 ?  76  LYS   B HE3  1 
ATOM   5036 H HZ1  . LYS   B 1 76  ? 33.527 -11.246 9.823   1.00 31.65 ?  76  LYS   B HZ1  1 
ATOM   5037 H HZ2  . LYS   B 1 76  ? 32.906 -11.861 10.979  1.00 31.65 ?  76  LYS   B HZ2  1 
ATOM   5038 H HZ3  . LYS   B 1 76  ? 33.464 -10.528 11.079  1.00 31.65 ?  76  LYS   B HZ3  1 
ATOM   5039 N N    . VAL   B 1 77  ? 38.084 -18.189 10.226  1.00 15.56 ?  77  VAL   B N    1 
ATOM   5040 C CA   . VAL   B 1 77  ? 37.873 -19.401 9.439   1.00 15.66 ?  77  VAL   B CA   1 
ATOM   5041 C C    . VAL   B 1 77  ? 36.681 -19.166 8.521   1.00 14.33 ?  77  VAL   B C    1 
ATOM   5042 O O    . VAL   B 1 77  ? 35.613 -18.726 8.966   1.00 14.59 ?  77  VAL   B O    1 
ATOM   5043 C CB   . VAL   B 1 77  ? 37.674 -20.628 10.342  1.00 17.30 ?  77  VAL   B CB   1 
ATOM   5044 C CG1  . VAL   B 1 77  ? 37.407 -21.867 9.489   1.00 18.13 ?  77  VAL   B CG1  1 
ATOM   5045 C CG2  . VAL   B 1 77  ? 38.900 -20.857 11.232  1.00 19.10 ?  77  VAL   B CG2  1 
ATOM   5046 H H    . VAL   B 1 77  ? 38.047 -18.295 11.074  1.00 18.82 ?  77  VAL   B H    1 
ATOM   5047 H HA   . VAL   B 1 77  ? 38.648 -19.560 8.880   1.00 18.94 ?  77  VAL   B HA   1 
ATOM   5048 H HB   . VAL   B 1 77  ? 36.901 -20.482 10.913  1.00 20.91 ?  77  VAL   B HB   1 
ATOM   5049 H HG11 . VAL   B 1 77  ? 37.448 -22.653 10.056  1.00 21.90 ?  77  VAL   B HG11 1 
ATOM   5050 H HG12 . VAL   B 1 77  ? 36.523 -21.797 9.090   1.00 21.90 ?  77  VAL   B HG12 1 
ATOM   5051 H HG13 . VAL   B 1 77  ? 38.079 -21.924 8.795   1.00 21.90 ?  77  VAL   B HG13 1 
ATOM   5052 H HG21 . VAL   B 1 77  ? 38.756 -21.657 11.758  1.00 23.07 ?  77  VAL   B HG21 1 
ATOM   5053 H HG22 . VAL   B 1 77  ? 39.678 -20.962 10.667  1.00 23.07 ?  77  VAL   B HG22 1 
ATOM   5054 H HG23 . VAL   B 1 77  ? 39.009 -20.090 11.814  1.00 23.07 ?  77  VAL   B HG23 1 
ATOM   5055 N N    . GLY   B 1 78  ? 36.866 -19.444 7.232   1.00 13.97 ?  78  GLY   B N    1 
ATOM   5056 C CA   . GLY   B 1 78  ? 35.899 -19.124 6.210   1.00 13.61 ?  78  GLY   B CA   1 
ATOM   5057 C C    . GLY   B 1 78  ? 36.146 -17.804 5.513   1.00 13.23 ?  78  GLY   B C    1 
ATOM   5058 O O    . GLY   B 1 78  ? 35.465 -17.504 4.525   1.00 13.81 ?  78  GLY   B O    1 
ATOM   5059 H H    . GLY   B 1 78  ? 37.566 -19.833 6.928   1.00 16.91 ?  78  GLY   B H    1 
ATOM   5060 H HA2  . GLY   B 1 78  ? 35.903 -19.819 5.538   1.00 16.48 ?  78  GLY   B HA2  1 
ATOM   5061 H HA3  . GLY   B 1 78  ? 35.014 -19.086 6.605   1.00 16.48 ?  78  GLY   B HA3  1 
ATOM   5062 N N    . GLY   B 1 79  ? 37.090 -16.999 6.005   1.00 13.46 ?  79  GLY   B N    1 
ATOM   5063 C CA   . GLY   B 1 79  ? 37.392 -15.703 5.434   1.00 13.19 ?  79  GLY   B CA   1 
ATOM   5064 C C    . GLY   B 1 79  ? 38.626 -15.720 4.543   1.00 12.61 ?  79  GLY   B C    1 
ATOM   5065 O O    . GLY   B 1 79  ? 39.244 -16.757 4.293   1.00 13.23 ?  79  GLY   B O    1 
ATOM   5066 H H    . GLY   B 1 79  ? 37.581 -17.195 6.680   1.00 16.31 ?  79  GLY   B H    1 
ATOM   5067 H HA2  . GLY   B 1 79  ? 36.638 -15.396 4.906   1.00 15.98 ?  79  GLY   B HA2  1 
ATOM   5068 H HA3  . GLY   B 1 79  ? 37.541 -15.064 6.150   1.00 15.98 ?  79  GLY   B HA3  1 
ATOM   5069 N N    . SER   B 1 80  ? 38.994 -14.522 4.079   1.00 12.78 ?  80  SER   B N    1 
ATOM   5070 C CA   . SER   B 1 80  ? 40.096 -14.386 3.135   1.00 12.73 ?  80  SER   B CA   1 
ATOM   5071 C C    . SER   B 1 80  ? 40.673 -12.978 3.191   1.00 12.62 ?  80  SER   B C    1 
ATOM   5072 O O    . SER   B 1 80  ? 40.058 -12.049 3.717   1.00 13.93 ?  80  SER   B O    1 
ATOM   5073 C CB   . SER   B 1 80  ? 39.646 -14.681 1.700   1.00 13.17 ?  80  SER   B CB   1 
ATOM   5074 O OG   . SER   B 1 80  ? 38.820 -13.654 1.188   1.00 14.30 ?  80  SER   B OG   1 
ATOM   5075 H H    . SER   B 1 80  ? 38.621 -13.777 4.292   1.00 15.49 ?  80  SER   B H    1 
ATOM   5076 H HA   . SER   B 1 80  ? 40.791 -15.013 3.375   1.00 15.43 ?  80  SER   B HA   1 
ATOM   5077 H HB2  . SER   B 1 80  ? 40.428 -14.755 1.132   1.00 15.95 ?  80  SER   B HB2  1 
ATOM   5078 H HB3  . SER   B 1 80  ? 39.150 -15.513 1.691   1.00 15.95 ?  80  SER   B HB3  1 
ATOM   5079 H HG   . SER   B 1 80  ? 38.128 -13.576 1.666   1.00 17.31 ?  80  SER   B HG   1 
ATOM   5080 N N    . CYS   B 1 81  ? 41.863 -12.831 2.609   1.00 12.52 ?  81  CYS   B N    1 
ATOM   5081 C CA   . CYS   B 1 81  ? 42.414 -11.520 2.294   1.00 12.42 ?  81  CYS   B CA   1 
ATOM   5082 C C    . CYS   B 1 81  ? 43.187 -11.606 0.985   1.00 11.81 ?  81  CYS   B C    1 
ATOM   5083 O O    . CYS   B 1 81  ? 43.701 -12.669 0.614   1.00 12.99 ?  81  CYS   B O    1 
ATOM   5084 C CB   . CYS   B 1 81  ? 43.301 -10.975 3.421   1.00 13.77 ?  81  CYS   B CB   1 
ATOM   5085 S SG   . CYS   B 1 81  ? 44.832 -11.901 3.676   1.00 13.62 ?  81  CYS   B SG   1 
ATOM   5086 H H    . CYS   B 1 81  ? 42.379 -13.484 2.379   1.00 15.17 ?  81  CYS   B H    1 
ATOM   5087 H HA   . CYS   B 1 81  ? 41.681 -10.894 2.169   1.00 15.06 ?  81  CYS   B HA   1 
ATOM   5088 H HB2  . CYS   B 1 81  ? 43.544 -10.058 3.216   1.00 16.67 ?  81  CYS   B HB2  1 
ATOM   5089 H HB3  . CYS   B 1 81  ? 42.797 -10.996 4.254   1.00 16.67 ?  81  CYS   B HB3  1 
ATOM   5090 H HG   . CYS   B 1 81  ? 45.448 -11.402 4.581   1.00 16.49 ?  81  CYS   B HG   1 
ATOM   5091 N N    . VAL   B 1 82  ? 43.296 -10.462 0.309   1.00 12.06 ?  82  VAL   B N    1 
ATOM   5092 C CA   . VAL   B 1 82  ? 44.062 -10.333 -0.927  1.00 12.26 ?  82  VAL   B CA   1 
ATOM   5093 C C    . VAL   B 1 82  ? 45.402 -9.690  -0.608  1.00 12.63 ?  82  VAL   B C    1 
ATOM   5094 O O    . VAL   B 1 82  ? 45.449 -8.571  -0.078  1.00 13.77 ?  82  VAL   B O    1 
ATOM   5095 C CB   . VAL   B 1 82  ? 43.315 -9.498  -1.978  1.00 13.29 ?  82  VAL   B CB   1 
ATOM   5096 C CG1  . VAL   B 1 82  ? 44.164 -9.355  -3.243  1.00 14.88 ?  82  VAL   B CG1  1 
ATOM   5097 C CG2  . VAL   B 1 82  ? 41.958 -10.105 -2.292  1.00 14.42 ?  82  VAL   B CG2  1 
ATOM   5098 H H    . VAL   B 1 82  ? 42.915 -9.722  0.550   1.00 14.62 ?  82  VAL   B H    1 
ATOM   5099 H HA   . VAL   B 1 82  ? 44.225 -11.210 -1.297  1.00 14.86 ?  82  VAL   B HA   1 
ATOM   5100 H HB   . VAL   B 1 82  ? 43.165 -8.609  -1.627  1.00 16.09 ?  82  VAL   B HB   1 
ATOM   5101 H HG11 . VAL   B 1 82  ? 43.605 -9.040  -3.969  1.00 18.01 ?  82  VAL   B HG11 1 
ATOM   5102 H HG12 . VAL   B 1 82  ? 44.878 -8.715  -3.078  1.00 18.01 ?  82  VAL   B HG12 1 
ATOM   5103 H HG13 . VAL   B 1 82  ? 44.544 -10.219 -3.470  1.00 18.01 ?  82  VAL   B HG13 1 
ATOM   5104 H HG21 . VAL   B 1 82  ? 41.527 -9.583  -2.990  1.00 17.45 ?  82  VAL   B HG21 1 
ATOM   5105 H HG22 . VAL   B 1 82  ? 42.080 -11.020 -2.598  1.00 17.45 ?  82  VAL   B HG22 1 
ATOM   5106 H HG23 . VAL   B 1 82  ? 41.412 -10.097 -1.491  1.00 17.45 ?  82  VAL   B HG23 1 
ATOM   5107 N N    . LEU   B 1 83  ? 46.484 -10.366 -0.978  1.00 12.40 ?  83  LEU   B N    1 
ATOM   5108 C CA   . LEU   B 1 83  ? 47.840 -9.851  -0.856  1.00 12.19 ?  83  LEU   B CA   1 
ATOM   5109 C C    . LEU   B 1 83  ? 48.539 -9.994  -2.209  1.00 12.07 ?  83  LEU   B C    1 
ATOM   5110 O O    . LEU   B 1 83  ? 47.938 -10.418 -3.201  1.00 12.25 ?  83  LEU   B O    1 
ATOM   5111 C CB   . LEU   B 1 83  ? 48.586 -10.537 0.295   1.00 12.97 ?  83  LEU   B CB   1 
ATOM   5112 C CG   . LEU   B 1 83  ? 48.079 -10.178 1.695   1.00 14.47 ?  83  LEU   B CG   1 
ATOM   5113 C CD1  . LEU   B 1 83  ? 48.699 -11.048 2.772   1.00 15.15 ?  83  LEU   B CD1  1 
ATOM   5114 C CD2  . LEU   B 1 83  ? 48.299 -8.702  2.017   1.00 15.56 ?  83  LEU   B CD2  1 
ATOM   5115 H H    . LEU   B 1 83  ? 46.451 -11.157 -1.321  1.00 15.03 ?  83  LEU   B H    1 
ATOM   5116 H HA   . LEU   B 1 83  ? 47.792 -8.907  -0.658  1.00 14.77 ?  83  LEU   B HA   1 
ATOM   5117 H HB2  . LEU   B 1 83  ? 48.503 -11.496 0.193   1.00 15.71 ?  83  LEU   B HB2  1 
ATOM   5118 H HB3  . LEU   B 1 83  ? 49.521 -10.283 0.250   1.00 15.71 ?  83  LEU   B HB3  1 
ATOM   5119 H HG   . LEU   B 1 83  ? 47.123 -10.332 1.717   1.00 17.51 ?  83  LEU   B HG   1 
ATOM   5120 H HD11 . LEU   B 1 83  ? 48.336 -10.791 3.635   1.00 18.33 ?  83  LEU   B HD11 1 
ATOM   5121 H HD12 . LEU   B 1 83  ? 48.478 -11.978 2.589   1.00 18.33 ?  83  LEU   B HD12 1 
ATOM   5122 H HD13 . LEU   B 1 83  ? 49.658 -10.930 2.766   1.00 18.33 ?  83  LEU   B HD13 1 
ATOM   5123 H HD21 . LEU   B 1 83  ? 48.100 -8.550  2.955   1.00 18.82 ?  83  LEU   B HD21 1 
ATOM   5124 H HD22 . LEU   B 1 83  ? 49.224 -8.473  1.835   1.00 18.82 ?  83  LEU   B HD22 1 
ATOM   5125 H HD23 . LEU   B 1 83  ? 47.710 -8.165  1.465   1.00 18.82 ?  83  LEU   B HD23 1 
ATOM   5126 N N    . SER   B 1 84  ? 49.816 -9.620  -2.261  1.00 13.16 ?  84  SER   B N    1 
ATOM   5127 C CA   . SER   B 1 84  ? 50.556 -9.738  -3.508  1.00 13.55 ?  84  SER   B CA   1 
ATOM   5128 C C    . SER   B 1 84  ? 50.719 -11.201 -3.913  1.00 12.75 ?  84  SER   B C    1 
ATOM   5129 O O    . SER   B 1 84  ? 50.833 -12.094 -3.073  1.00 12.62 ?  84  SER   B O    1 
ATOM   5130 C CB   . SER   B 1 84  ? 51.945 -9.120  -3.365  1.00 15.53 ?  84  SER   B CB   1 
ATOM   5131 O OG   . SER   B 1 84  ? 52.689 -9.332  -4.548  1.00 17.48 ?  84  SER   B OG   1 
ATOM   5132 H H    . SER   B 1 84  ? 50.260 -9.285  -1.603  1.00 15.93 ?  84  SER   B H    1 
ATOM   5133 H HA   . SER   B 1 84  ? 50.083 -9.275  -4.214  1.00 16.41 ?  84  SER   B HA   1 
ATOM   5134 H HB2  . SER   B 1 84  ? 51.855 -8.163  -3.212  1.00 18.78 ?  84  SER   B HB2  1 
ATOM   5135 H HB3  . SER   B 1 84  ? 52.408 -9.532  -2.622  1.00 18.78 ?  84  SER   B HB3  1 
ATOM   5136 H HG   . SER   B 1 84  ? 53.457 -8.985  -4.477  1.00 21.12 ?  84  SER   B HG   1 
ATOM   5137 N N    . GLY   B 1 85  ? 50.781 -11.427 -5.219  1.00 13.79 ?  85  GLY   B N    1 
ATOM   5138 C CA   . GLY   B 1 85  ? 51.128 -12.717 -5.764  1.00 14.41 ?  85  GLY   B CA   1 
ATOM   5139 C C    . GLY   B 1 85  ? 52.600 -12.902 -6.066  1.00 13.47 ?  85  GLY   B C    1 
ATOM   5140 O O    . GLY   B 1 85  ? 52.987 -13.980 -6.523  1.00 14.09 ?  85  GLY   B O    1 
ATOM   5141 H H    . GLY   B 1 85  ? 50.639 -10.835 -5.817  1.00 16.70 ?  85  GLY   B H    1 
ATOM   5142 H HA2  . GLY   B 1 85  ? 50.864 -13.412 -5.138  1.00 17.44 ?  85  GLY   B HA2  1 
ATOM   5143 H HA3  . GLY   B 1 85  ? 50.640 -12.857 -6.588  1.00 17.44 ?  85  GLY   B HA3  1 
ATOM   5144 N N    . HIS   B 1 86  ? 53.447 -11.899 -5.841  1.00 13.57 ?  86  HIS   B N    1 
ATOM   5145 C CA   . HIS   B 1 86  ? 54.915 -12.064 -5.927  1.00 13.34 ?  86  HIS   B CA   1 
ATOM   5146 C C    . HIS   B 1 86  ? 55.287 -12.578 -7.317  1.00 13.54 ?  86  HIS   B C    1 
ATOM   5147 O O    . HIS   B 1 86  ? 54.908 -11.963 -8.324  1.00 14.50 ?  86  HIS   B O    1 
ATOM   5148 C CB   . HIS   B 1 86  ? 55.407 -12.907 -4.753  1.00 13.84 ?  86  HIS   B CB   1 
ATOM   5149 C CG   . HIS   B 1 86  ? 55.081 -12.306 -3.426  1.00 14.09 ?  86  HIS   B CG   1 
ATOM   5150 N ND1  . HIS   B 1 86  ? 55.899 -11.390 -2.804  1.00 16.12 ?  86  HIS   B ND1  1 
ATOM   5151 C CD2  . HIS   B 1 86  ? 54.004 -12.462 -2.620  1.00 14.80 ?  86  HIS   B CD2  1 
ATOM   5152 C CE1  . HIS   B 1 86  ? 55.337 -11.005 -1.672  1.00 15.64 ?  86  HIS   B CE1  1 
ATOM   5153 N NE2  . HIS   B 1 86  ? 54.186 -11.639 -1.537  1.00 15.15 ?  86  HIS   B NE2  1 
ATOM   5154 H H    . HIS   B 1 86  ? 53.199 -11.103 -5.643  1.00 16.44 ?  86  HIS   B H    1 
ATOM   5155 H HA   . HIS   B 1 86  ? 55.320 -11.191 -5.832  1.00 16.16 ?  86  HIS   B HA   1 
ATOM   5156 H HB2  . HIS   B 1 86  ? 54.999 -13.786 -4.797  1.00 16.75 ?  86  HIS   B HB2  1 
ATOM   5157 H HB3  . HIS   B 1 86  ? 56.376 -12.993 -4.810  1.00 16.75 ?  86  HIS   B HB3  1 
ATOM   5158 H HD2  . HIS   B 1 86  ? 53.267 -13.014 -2.781  1.00 17.90 ?  86  HIS   B HD2  1 
ATOM   5159 H HE1  . HIS   B 1 86  ? 55.697 -10.407 -1.061  1.00 18.92 ?  86  HIS   B HE1  1 
ATOM   5160 H HE2  . HIS   B 1 86  ? 53.643 -11.565 -0.873  1.00 18.32 ?  86  HIS   B HE2  1 
ATOM   5161 N N    . ASN   B 1 87  ? 56.039 -13.670 -7.425  1.00 13.89 ?  87  ASN   B N    1 
ATOM   5162 C CA   . ASN   B 1 87  ? 56.440 -14.242 -8.702  1.00 14.97 ?  87  ASN   B CA   1 
ATOM   5163 C C    . ASN   B 1 87  ? 55.462 -15.285 -9.210  1.00 14.64 ?  87  ASN   B C    1 
ATOM   5164 O O    . ASN   B 1 87  ? 55.781 -15.993 -10.172 1.00 16.51 ?  87  ASN   B O    1 
ATOM   5165 C CB   . ASN   B 1 87  ? 57.838 -14.864 -8.586  1.00 17.09 ?  87  ASN   B CB   1 
ATOM   5166 C CG   . ASN   B 1 87  ? 57.894 -15.988 -7.557  1.00 18.02 ?  87  ASN   B CG   1 
ATOM   5167 O OD1  . ASN   B 1 87  ? 57.257 -15.918 -6.504  1.00 16.75 ?  87  ASN   B OD1  1 
ATOM   5168 N ND2  . ASN   B 1 87  ? 58.650 -17.042 -7.870  1.00 20.16 ?  87  ASN   B ND2  1 
ATOM   5169 H H    . ASN   B 1 87  ? 56.332 -14.113 -6.749  1.00 16.82 ?  87  ASN   B H    1 
ATOM   5170 H HA   . ASN   B 1 87  ? 56.485 -13.534 -9.360  1.00 18.12 ?  87  ASN   B HA   1 
ATOM   5171 H HB2  . ASN   B 1 87  ? 58.092 -15.231 -9.449  1.00 20.65 ?  87  ASN   B HB2  1 
ATOM   5172 H HB3  . ASN   B 1 87  ? 58.468 -14.178 -8.320  1.00 20.65 ?  87  ASN   B HB3  1 
ATOM   5173 H HD21 . ASN   B 1 87  ? 58.718 -17.699 -7.323  1.00 24.35 ?  87  ASN   B HD21 1 
ATOM   5174 H HD22 . ASN   B 1 87  ? 59.078 -17.059 -8.619  1.00 24.35 ?  87  ASN   B HD22 1 
ATOM   5175 N N    . LEU   B 1 88  ? 54.284 -15.392 -8.590  1.00 13.75 ?  88  LEU   B N    1 
ATOM   5176 C CA   . LEU   B 1 88  ? 53.301 -16.417 -8.924  1.00 14.15 ?  88  LEU   B CA   1 
ATOM   5177 C C    . LEU   B 1 88  ? 52.068 -15.895 -9.644  1.00 13.97 ?  88  LEU   B C    1 
ATOM   5178 O O    . LEU   B 1 88  ? 51.459 -16.642 -10.422 1.00 15.56 ?  88  LEU   B O    1 
ATOM   5179 C CB   . LEU   B 1 88  ? 52.825 -17.107 -7.644  1.00 14.85 ?  88  LEU   B CB   1 
ATOM   5180 C CG   . LEU   B 1 88  ? 53.949 -17.752 -6.847  1.00 17.27 ?  88  LEU   B CG   1 
ATOM   5181 C CD1  . LEU   B 1 88  ? 53.453 -18.095 -5.454  1.00 19.11 ?  88  LEU   B CD1  1 
ATOM   5182 C CD2  . LEU   B 1 88  ? 54.426 -18.988 -7.575  1.00 20.55 ?  88  LEU   B CD2  1 
ATOM   5183 H H    . LEU   B 1 88  ? 54.030 -14.876 -7.946  1.00 16.65 ?  88  LEU   B H    1 
ATOM   5184 H HA   . LEU   B 1 88  ? 53.710 -17.081 -9.488  1.00 17.13 ?  88  LEU   B HA   1 
ATOM   5185 H HB2  . LEU   B 1 88  ? 52.388 -16.459 -7.069  1.00 17.96 ?  88  LEU   B HB2  1 
ATOM   5186 H HB3  . LEU   B 1 88  ? 52.191 -17.810 -7.880  1.00 17.96 ?  88  LEU   B HB3  1 
ATOM   5187 H HG   . LEU   B 1 88  ? 54.689 -17.130 -6.770  1.00 20.87 ?  88  LEU   B HG   1 
ATOM   5188 H HD11 . LEU   B 1 88  ? 54.116 -18.646 -5.012  1.00 23.08 ?  88  LEU   B HD11 1 
ATOM   5189 H HD12 . LEU   B 1 88  ? 53.319 -17.272 -4.957  1.00 23.08 ?  88  LEU   B HD12 1 
ATOM   5190 H HD13 . LEU   B 1 88  ? 52.616 -18.575 -5.530  1.00 23.08 ?  88  LEU   B HD13 1 
ATOM   5191 H HD21 . LEU   B 1 88  ? 55.081 -19.441 -7.025  1.00 24.81 ?  88  LEU   B HD21 1 
ATOM   5192 H HD22 . LEU   B 1 88  ? 53.667 -19.568 -7.738  1.00 24.81 ?  88  LEU   B HD22 1 
ATOM   5193 H HD23 . LEU   B 1 88  ? 54.827 -18.722 -8.418  1.00 24.81 ?  88  LEU   B HD23 1 
ATOM   5194 N N    . ALA   B 1 89  ? 51.663 -14.659 -9.373  1.00 13.48 ?  89  ALA   B N    1 
ATOM   5195 C CA   . ALA   B 1 89  ? 50.376 -14.162 -9.836  1.00 12.41 ?  89  ALA   B CA   1 
ATOM   5196 C C    . ALA   B 1 89  ? 50.344 -12.675 -9.540  1.00 12.71 ?  89  ALA   B C    1 
ATOM   5197 O O    . ALA   B 1 89  ? 51.172 -12.161 -8.789  1.00 13.89 ?  89  ALA   B O    1 
ATOM   5198 C CB   . ALA   B 1 89  ? 49.225 -14.833 -9.096  1.00 12.80 ?  89  ALA   B CB   1 
ATOM   5199 H H    . ALA   B 1 89  ? 52.105 -14.079 -8.908  1.00 16.32 ?  89  ALA   B H    1 
ATOM   5200 H HA   . ALA   B 1 89  ? 50.277 -14.303 -10.796 1.00 15.04 ?  89  ALA   B HA   1 
ATOM   5201 H HB1  . ALA   B 1 89  ? 48.382 -14.498 -9.451  1.00 15.51 ?  89  ALA   B HB1  1 
ATOM   5202 H HB2  . ALA   B 1 89  ? 49.281 -15.792 -9.238  1.00 15.51 ?  89  ALA   B HB2  1 
ATOM   5203 H HB3  . ALA   B 1 89  ? 49.294 -14.629 -8.156  1.00 15.51 ?  89  ALA   B HB3  1 
ATOM   5204 N N    . LYS   B 1 90  ? 49.359 -11.983 -10.107 1.00 13.69 ?  90  LYS   B N    1 
ATOM   5205 C CA   . LYS   B 1 90  ? 49.167 -10.596 -9.704  1.00 13.93 ?  90  LYS   B CA   1 
ATOM   5206 C C    . LYS   B 1 90  ? 48.845 -10.519 -8.216  1.00 13.83 ?  90  LYS   B C    1 
ATOM   5207 O O    . LYS   B 1 90  ? 49.487 -9.772  -7.466  1.00 14.94 ?  90  LYS   B O    1 
ATOM   5208 C CB   . LYS   B 1 90  ? 48.090 -9.931  -10.558 1.00 15.90 ?  90  LYS   B CB   1 
ATOM   5209 C CG   . LYS   B 1 90  ? 47.785 -8.485  -10.170 1.00 16.24 ?  90  LYS   B CG   1 
ATOM   5210 C CD   . LYS   B 1 90  ? 48.989 -7.582  -10.255 1.00 19.41 ?  90  LYS   B CD   1 
ATOM   5211 C CE   . LYS   B 1 90  ? 48.544 -6.164  -9.979  1.00 21.54 ?  90  LYS   B CE   1 
ATOM   5212 N NZ   . LYS   B 1 90  ? 49.680 -5.217  -9.913  1.00 21.32 ?  90  LYS   B NZ   1 
ATOM   5213 H H    . LYS   B 1 90  ? 48.805 -12.283 -10.696 1.00 16.58 ?  90  LYS   B H    1 
ATOM   5214 H HA   . LYS   B 1 90  ? 49.995 -10.118 -9.853  1.00 16.86 ?  90  LYS   B HA   1 
ATOM   5215 H HB2  . LYS   B 1 90  ? 48.384 -9.930  -11.486 1.00 19.23 ?  90  LYS   B HB2  1 
ATOM   5216 H HB3  . LYS   B 1 90  ? 47.268 -10.443 -10.483 1.00 19.23 ?  90  LYS   B HB3  1 
ATOM   5217 H HG2  . LYS   B 1 90  ? 47.101 -8.138  -10.768 1.00 19.63 ?  90  LYS   B HG2  1 
ATOM   5218 H HG3  . LYS   B 1 90  ? 47.451 -8.467  -9.255  1.00 19.63 ?  90  LYS   B HG3  1 
ATOM   5219 H HD2  . LYS   B 1 90  ? 49.643 -7.840  -9.587  1.00 23.44 ?  90  LYS   B HD2  1 
ATOM   5220 H HD3  . LYS   B 1 90  ? 49.369 -7.624  -11.146 1.00 23.44 ?  90  LYS   B HD3  1 
ATOM   5221 H HE2  . LYS   B 1 90  ? 47.952 -5.869  -10.690 1.00 26.00 ?  90  LYS   B HE2  1 
ATOM   5222 H HE3  . LYS   B 1 90  ? 48.082 -6.131  -9.127  1.00 26.00 ?  90  LYS   B HE3  1 
ATOM   5223 H HZ1  . LYS   B 1 90  ? 49.384 -4.390  -9.751  1.00 25.73 ?  90  LYS   B HZ1  1 
ATOM   5224 H HZ2  . LYS   B 1 90  ? 50.240 -5.453  -9.263  1.00 25.73 ?  90  LYS   B HZ2  1 
ATOM   5225 H HZ3  . LYS   B 1 90  ? 50.122 -5.213  -10.688 1.00 25.73 ?  90  LYS   B HZ3  1 
ATOM   5226 N N    . HIS   B 1 91  ? 47.876 -11.319 -7.768  1.00 12.15 ?  91  HIS   B N    1 
ATOM   5227 C CA   . HIS   B 1 91  ? 47.422 -11.353 -6.389  1.00 12.45 ?  91  HIS   B CA   1 
ATOM   5228 C C    . HIS   B 1 91  ? 47.419 -12.787 -5.876  1.00 11.51 ?  91  HIS   B C    1 
ATOM   5229 O O    . HIS   B 1 91  ? 47.178 -13.740 -6.630  1.00 12.35 ?  91  HIS   B O    1 
ATOM   5230 C CB   . HIS   B 1 91  ? 45.970 -10.877 -6.267  1.00 13.82 ?  91  HIS   B CB   1 
ATOM   5231 C CG   . HIS   B 1 91  ? 45.750 -9.472  -6.721  1.00 17.24 ?  91  HIS   B CG   1 
ATOM   5232 N ND1  . HIS   B 1 91  ? 46.334 -8.385  -6.107  1.00 19.99 ?  91  HIS   B ND1  1 
ATOM   5233 C CD2  . HIS   B 1 91  ? 44.979 -8.974  -7.713  1.00 19.57 ?  91  HIS   B CD2  1 
ATOM   5234 C CE1  . HIS   B 1 91  ? 45.943 -7.275  -6.712  1.00 20.88 ?  91  HIS   B CE1  1 
ATOM   5235 N NE2  . HIS   B 1 91  ? 45.118 -7.606  -7.689  1.00 21.26 ?  91  HIS   B NE2  1 
ATOM   5236 H H    . HIS   B 1 91  ? 47.444 -11.867 -8.270  1.00 14.73 ?  91  HIS   B H    1 
ATOM   5237 H HA   . HIS   B 1 91  ? 47.991 -10.798 -5.822  1.00 15.09 ?  91  HIS   B HA   1 
ATOM   5238 H HB2  . HIS   B 1 91  ? 45.408 -11.455 -6.804  1.00 16.73 ?  91  HIS   B HB2  1 
ATOM   5239 H HB3  . HIS   B 1 91  ? 45.699 -10.935 -5.333  1.00 16.73 ?  91  HIS   B HB3  1 
ATOM   5240 H HD1  . HIS   B 1 91  ? 46.870 -8.423  -5.432  1.00 24.14 ?  91  HIS   B HD1  1 
ATOM   5241 H HD2  . HIS   B 1 91  ? 44.457 -9.462  -8.306  1.00 23.63 ?  91  HIS   B HD2  1 
ATOM   5242 H HE1  . HIS   B 1 91  ? 46.204 -6.412  -6.484  1.00 25.21 ?  91  HIS   B HE1  1 
ATOM   5243 N N    . CYS   B 1 92  ? 47.618 -12.925 -4.574  1.00 11.73 ?  92  CYS   B N    1 
ATOM   5244 C CA   . CYS   B 1 92  ? 47.307 -14.160 -3.865  1.00 11.57 ?  92  CYS   B CA   1 
ATOM   5245 C C    . CYS   B 1 92  ? 46.085 -13.922 -2.986  1.00 10.97 ?  92  CYS   B C    1 
ATOM   5246 O O    . CYS   B 1 92  ? 46.087 -13.024 -2.135  1.00 11.99 ?  92  CYS   B O    1 
ATOM   5247 C CB   . CYS   B 1 92  ? 48.485 -14.613 -3.009  1.00 11.81 ?  92  CYS   B CB   1 
ATOM   5248 S SG   . CYS   B 1 92  ? 48.134 -16.159 -2.104  1.00 12.14 ?  92  CYS   B SG   1 
ATOM   5249 H H    . CYS   B 1 92  ? 47.956 -12.312 -4.067  1.00 14.22 ?  92  CYS   B H    1 
ATOM   5250 H HA   . CYS   B 1 92  ? 47.105 -14.858 -4.507  1.00 14.03 ?  92  CYS   B HA   1 
ATOM   5251 H HB2  . CYS   B 1 92  ? 49.251 -14.761 -3.578  1.00 14.32 ?  92  CYS   B HB2  1 
ATOM   5252 H HB3  . CYS   B 1 92  ? 48.678 -13.924 -2.355  1.00 14.32 ?  92  CYS   B HB3  1 
ATOM   5253 H HG   . CYS   B 1 92  ? 49.115 -16.465 -1.483  1.00 14.71 ?  92  CYS   B HG   1 
ATOM   5254 N N    . LEU   B 1 93  ? 45.050 -14.732 -3.192  1.00 11.02 ?  93  LEU   B N    1 
ATOM   5255 C CA   . LEU   B 1 93  ? 43.878 -14.751 -2.323  1.00 11.03 ?  93  LEU   B CA   1 
ATOM   5256 C C    . LEU   B 1 93  ? 44.100 -15.815 -1.256  1.00 10.61 ?  93  LEU   B C    1 
ATOM   5257 O O    . LEU   B 1 93  ? 44.039 -17.018 -1.544  1.00 11.46 ?  93  LEU   B O    1 
ATOM   5258 C CB   . LEU   B 1 93  ? 42.608 -15.034 -3.126  1.00 11.87 ?  93  LEU   B CB   1 
ATOM   5259 C CG   . LEU   B 1 93  ? 41.296 -15.064 -2.330  1.00 12.43 ?  93  LEU   B CG   1 
ATOM   5260 C CD1  . LEU   B 1 93  ? 40.946 -13.675 -1.825  1.00 13.02 ?  93  LEU   B CD1  1 
ATOM   5261 C CD2  . LEU   B 1 93  ? 40.168 -15.650 -3.166  1.00 12.33 ?  93  LEU   B CD2  1 
ATOM   5262 H H    . LEU   B 1 93  ? 45.004 -15.304 -3.845  1.00 13.37 ?  93  LEU   B H    1 
ATOM   5263 H HA   . LEU   B 1 93  ? 43.786 -13.891 -1.893  1.00 13.38 ?  93  LEU   B HA   1 
ATOM   5264 H HB2  . LEU   B 1 93  ? 42.513 -14.340 -3.801  1.00 14.39 ?  93  LEU   B HB2  1 
ATOM   5265 H HB3  . LEU   B 1 93  ? 42.698 -15.893 -3.558  1.00 14.39 ?  93  LEU   B HB3  1 
ATOM   5266 H HG   . LEU   B 1 93  ? 41.414 -15.633 -1.554  1.00 15.07 ?  93  LEU   B HG   1 
ATOM   5267 H HD11 . LEU   B 1 93  ? 40.096 -13.712 -1.362  1.00 15.77 ?  93  LEU   B HD11 1 
ATOM   5268 H HD12 . LEU   B 1 93  ? 41.642 -13.376 -1.217  1.00 15.77 ?  93  LEU   B HD12 1 
ATOM   5269 H HD13 . LEU   B 1 93  ? 40.887 -13.071 -2.582  1.00 15.77 ?  93  LEU   B HD13 1 
ATOM   5270 H HD21 . LEU   B 1 93  ? 39.349 -15.652 -2.643  1.00 14.94 ?  93  LEU   B HD21 1 
ATOM   5271 H HD22 . LEU   B 1 93  ? 40.047 -15.108 -3.963  1.00 14.94 ?  93  LEU   B HD22 1 
ATOM   5272 H HD23 . LEU   B 1 93  ? 40.398 -16.558 -3.419  1.00 14.94 ?  93  LEU   B HD23 1 
ATOM   5273 N N    . HIS   B 1 94  ? 44.380 -15.385 -0.033  1.00 10.70 ?  94  HIS   B N    1 
ATOM   5274 C CA   . HIS   B 1 94  ? 44.590 -16.293 1.089   1.00 10.83 ?  94  HIS   B CA   1 
ATOM   5275 C C    . HIS   B 1 94  ? 43.224 -16.645 1.665   1.00 11.24 ?  94  HIS   B C    1 
ATOM   5276 O O    . HIS   B 1 94  ? 42.552 -15.777 2.225   1.00 12.72 ?  94  HIS   B O    1 
ATOM   5277 C CB   . HIS   B 1 94  ? 45.465 -15.622 2.146   1.00 11.40 ?  94  HIS   B CB   1 
ATOM   5278 C CG   . HIS   B 1 94  ? 46.847 -15.312 1.671   1.00 11.44 ?  94  HIS   B CG   1 
ATOM   5279 N ND1  . HIS   B 1 94  ? 47.879 -16.221 1.752   1.00 11.83 ?  94  HIS   B ND1  1 
ATOM   5280 C CD2  . HIS   B 1 94  ? 47.350 -14.201 1.083   1.00 11.71 ?  94  HIS   B CD2  1 
ATOM   5281 C CE1  . HIS   B 1 94  ? 48.967 -15.671 1.242   1.00 12.08 ?  94  HIS   B CE1  1 
ATOM   5282 N NE2  . HIS   B 1 94  ? 48.677 -14.446 0.832   1.00 12.08 ?  94  HIS   B NE2  1 
ATOM   5283 H H    . HIS   B 1 94  ? 44.465 -14.550 0.173   1.00 12.98 ?  94  HIS   B H    1 
ATOM   5284 H HA   . HIS   B 1 94  ? 45.026 -17.104 0.781   1.00 13.15 ?  94  HIS   B HA   1 
ATOM   5285 H HB2  . HIS   B 1 94  ? 45.049 -14.787 2.409   1.00 13.83 ?  94  HIS   B HB2  1 
ATOM   5286 H HB3  . HIS   B 1 94  ? 45.539 -16.212 2.908   1.00 13.83 ?  94  HIS   B HB3  1 
ATOM   5287 H HD2  . HIS   B 1 94  ? 46.893 -13.418 0.888   1.00 14.20 ?  94  HIS   B HD2  1 
ATOM   5288 H HE1  . HIS   B 1 94  ? 49.802 -16.085 1.177   1.00 14.64 ?  94  HIS   B HE1  1 
ATOM   5289 H HE2  . HIS   B 1 94  ? 49.233 -13.902 0.460   1.00 14.65 ?  94  HIS   B HE2  1 
ATOM   5290 N N    . VAL   B 1 95  ? 42.795 -17.899 1.516   1.00 11.25 ?  95  VAL   B N    1 
ATOM   5291 C CA   . VAL   B 1 95  ? 41.467 -18.350 1.943   1.00 11.49 ?  95  VAL   B CA   1 
ATOM   5292 C C    . VAL   B 1 95  ? 41.634 -19.391 3.038   1.00 11.46 ?  95  VAL   B C    1 
ATOM   5293 O O    . VAL   B 1 95  ? 42.416 -20.333 2.882   1.00 12.18 ?  95  VAL   B O    1 
ATOM   5294 C CB   . VAL   B 1 95  ? 40.657 -18.948 0.777   1.00 11.62 ?  95  VAL   B CB   1 
ATOM   5295 C CG1  . VAL   B 1 95  ? 39.269 -19.409 1.256   1.00 12.92 ?  95  VAL   B CG1  1 
ATOM   5296 C CG2  . VAL   B 1 95  ? 40.519 -17.956 -0.356  1.00 11.93 ?  95  VAL   B CG2  1 
ATOM   5297 H H    . VAL   B 1 95  ? 43.266 -18.527 1.161   1.00 13.65 ?  95  VAL   B H    1 
ATOM   5298 H HA   . VAL   B 1 95  ? 40.969 -17.602 2.305   1.00 13.94 ?  95  VAL   B HA   1 
ATOM   5299 H HB   . VAL   B 1 95  ? 41.125 -19.727 0.434   1.00 14.09 ?  95  VAL   B HB   1 
ATOM   5300 H HG11 . VAL   B 1 95  ? 38.718 -19.613 0.479   1.00 15.65 ?  95  VAL   B HG11 1 
ATOM   5301 H HG12 . VAL   B 1 95  ? 39.365 -20.206 1.802   1.00 15.65 ?  95  VAL   B HG12 1 
ATOM   5302 H HG13 . VAL   B 1 95  ? 38.857 -18.700 1.771   1.00 15.65 ?  95  VAL   B HG13 1 
ATOM   5303 H HG21 . VAL   B 1 95  ? 39.949 -18.342 -1.040  1.00 14.47 ?  95  VAL   B HG21 1 
ATOM   5304 H HG22 . VAL   B 1 95  ? 40.119 -17.145 -0.009  1.00 14.47 ?  95  VAL   B HG22 1 
ATOM   5305 H HG23 . VAL   B 1 95  ? 41.396 -17.772 -0.715  1.00 14.47 ?  95  VAL   B HG23 1 
ATOM   5306 N N    . VAL   B 1 96  ? 40.903 -19.223 4.138   1.00 12.14 ?  96  VAL   B N    1 
ATOM   5307 C CA   . VAL   B 1 96  ? 40.989 -20.132 5.281   1.00 12.09 ?  96  VAL   B CA   1 
ATOM   5308 C C    . VAL   B 1 96  ? 39.799 -21.091 5.234   1.00 12.91 ?  96  VAL   B C    1 
ATOM   5309 O O    . VAL   B 1 96  ? 38.682 -20.733 5.614   1.00 13.26 ?  96  VAL   B O    1 
ATOM   5310 C CB   . VAL   B 1 96  ? 41.031 -19.386 6.618   1.00 12.75 ?  96  VAL   B CB   1 
ATOM   5311 C CG1  . VAL   B 1 96  ? 41.214 -20.379 7.764   1.00 13.68 ?  96  VAL   B CG1  1 
ATOM   5312 C CG2  . VAL   B 1 96  ? 42.137 -18.339 6.637   1.00 13.68 ?  96  VAL   B CG2  1 
ATOM   5313 H H    . VAL   B 1 96  ? 40.345 -18.577 4.254   1.00 14.71 ?  96  VAL   B H    1 
ATOM   5314 H HA   . VAL   B 1 96  ? 41.803 -20.658 5.211   1.00 14.66 ?  96  VAL   B HA   1 
ATOM   5315 H HB   . VAL   B 1 96  ? 40.183 -18.933 6.755   1.00 15.45 ?  96  VAL   B HB   1 
ATOM   5316 H HG11 . VAL   B 1 96  ? 41.394 -19.887 8.585   1.00 16.56 ?  96  VAL   B HG11 1 
ATOM   5317 H HG12 . VAL   B 1 96  ? 40.408 -20.906 7.869   1.00 16.56 ?  96  VAL   B HG12 1 
ATOM   5318 H HG13 . VAL   B 1 96  ? 41.967 -20.960 7.564   1.00 16.56 ?  96  VAL   B HG13 1 
ATOM   5319 H HG21 . VAL   B 1 96  ? 42.170 -17.926 7.516   1.00 16.56 ?  96  VAL   B HG21 1 
ATOM   5320 H HG22 . VAL   B 1 96  ? 42.982 -18.763 6.437   1.00 16.56 ?  96  VAL   B HG22 1 
ATOM   5321 H HG23 . VAL   B 1 96  ? 41.939 -17.660 5.967   1.00 16.56 ?  96  VAL   B HG23 1 
ATOM   5322 N N    . GLY   B 1 97  ? 40.033 -22.326 4.799   1.00 12.93 ?  97  GLY   B N    1 
ATOM   5323 C CA   . GLY   B 1 97  ? 39.059 -23.383 4.959   1.00 13.45 ?  97  GLY   B CA   1 
ATOM   5324 C C    . GLY   B 1 97  ? 39.177 -23.992 6.338   1.00 14.71 ?  97  GLY   B C    1 
ATOM   5325 O O    . GLY   B 1 97  ? 40.217 -23.874 6.996   1.00 14.99 ?  97  GLY   B O    1 
ATOM   5326 H H    . GLY   B 1 97  ? 40.764 -22.571 4.403   1.00 15.66 ?  97  GLY   B H    1 
ATOM   5327 H HA2  . GLY   B 1 97  ? 38.167 -23.012 4.835   1.00 16.29 ?  97  GLY   B HA2  1 
ATOM   5328 H HA3  . GLY   B 1 97  ? 39.205 -24.066 4.285   1.00 16.29 ?  97  GLY   B HA3  1 
ATOM   5329 N N    . PRO   B 1 98  ? 38.127 -24.669 6.799   1.00 15.01 ?  98  PRO   B N    1 
ATOM   5330 C CA   . PRO   B 1 98  ? 38.219 -25.369 8.085   1.00 15.80 ?  98  PRO   B CA   1 
ATOM   5331 C C    . PRO   B 1 98  ? 39.242 -26.495 8.040   1.00 15.37 ?  98  PRO   B C    1 
ATOM   5332 O O    . PRO   B 1 98  ? 39.352 -27.223 7.053   1.00 15.47 ?  98  PRO   B O    1 
ATOM   5333 C CB   . PRO   B 1 98  ? 36.799 -25.911 8.290   1.00 15.76 ?  98  PRO   B CB   1 
ATOM   5334 C CG   . PRO   B 1 98  ? 36.250 -26.054 6.916   1.00 15.75 ?  98  PRO   B CG   1 
ATOM   5335 C CD   . PRO   B 1 98  ? 36.816 -24.878 6.155   1.00 15.13 ?  98  PRO   B CD   1 
ATOM   5336 H HA   . PRO   B 1 98  ? 38.446 -24.751 8.791   1.00 19.11 ?  98  PRO   B HA   1 
ATOM   5337 H HB2  . PRO   B 1 98  ? 36.840 -26.774 8.733   1.00 19.06 ?  98  PRO   B HB2  1 
ATOM   5338 H HB3  . PRO   B 1 98  ? 36.280 -25.280 8.804   1.00 19.06 ?  98  PRO   B HB3  1 
ATOM   5339 H HG2  . PRO   B 1 98  ? 36.550 -26.893 6.528   1.00 19.05 ?  98  PRO   B HG2  1 
ATOM   5340 H HG3  . PRO   B 1 98  ? 35.284 -26.013 6.944   1.00 19.05 ?  98  PRO   B HG3  1 
ATOM   5341 H HD2  . PRO   B 1 98  ? 36.925 -25.107 5.213   1.00 18.31 ?  98  PRO   B HD2  1 
ATOM   5342 H HD3  . PRO   B 1 98  ? 36.258 -24.098 6.268   1.00 18.31 ?  98  PRO   B HD3  1 
ATOM   5343 N N    . ASN   B 1 99  ? 39.986 -26.635 9.131   1.00 16.80 ?  99  ASN   B N    1 
ATOM   5344 C CA   . ASN   B 1 99  ? 40.960 -27.711 9.295   1.00 17.20 ?  99  ASN   B CA   1 
ATOM   5345 C C    . ASN   B 1 99  ? 40.328 -28.799 10.163  1.00 19.45 ?  99  ASN   B C    1 
ATOM   5346 O O    . ASN   B 1 99  ? 40.244 -28.663 11.385  1.00 20.16 ?  99  ASN   B O    1 
ATOM   5347 C CB   . ASN   B 1 99  ? 42.229 -27.160 9.932   1.00 17.63 ?  99  ASN   B CB   1 
ATOM   5348 C CG   . ASN   B 1 99  ? 43.369 -28.157 9.927   1.00 18.86 ?  99  ASN   B CG   1 
ATOM   5349 O OD1  . ASN   B 1 99  ? 43.159 -29.354 10.084  1.00 19.65 ?  99  ASN   B OD1  1 
ATOM   5350 N ND2  . ASN   B 1 99  ? 44.585 -27.665 9.737   1.00 18.83 ?  99  ASN   B ND2  1 
ATOM   5351 H H    . ASN   B 1 99  ? 39.942 -26.110 9.808   1.00 20.31 ?  99  ASN   B H    1 
ATOM   5352 H HA   . ASN   B 1 99  ? 41.181 -28.097 8.435   1.00 20.79 ?  99  ASN   B HA   1 
ATOM   5353 H HB2  . ASN   B 1 99  ? 42.509 -26.379 9.442   1.00 21.31 ?  99  ASN   B HB2  1 
ATOM   5354 H HB3  . ASN   B 1 99  ? 42.036 -26.926 10.857  1.00 21.31 ?  99  ASN   B HB3  1 
ATOM   5355 H HD21 . ASN   B 1 99  ? 45.264 -28.187 9.724   1.00 22.74 ?  99  ASN   B HD21 1 
ATOM   5356 H HD22 . ASN   B 1 99  ? 44.685 -26.817 9.628   1.00 22.74 ?  99  ASN   B HD22 1 
ATOM   5357 N N    A VAL   B 1 100 ? 39.873 -29.878 9.519   0.86 21.18 ?  100 VAL   B N    1 
ATOM   5358 N N    B VAL   B 1 100 ? 39.879 -29.881 9.519   0.14 21.49 ?  100 VAL   B N    1 
ATOM   5359 C CA   A VAL   B 1 100 ? 39.253 -30.982 10.249  0.86 24.05 ?  100 VAL   B CA   1 
ATOM   5360 C CA   B VAL   B 1 100 ? 39.262 -30.987 10.247  0.14 23.59 ?  100 VAL   B CA   1 
ATOM   5361 C C    A VAL   B 1 100 ? 40.254 -31.653 11.183  0.86 24.33 ?  100 VAL   B C    1 
ATOM   5362 C C    B VAL   B 1 100 ? 40.261 -31.630 11.197  0.14 24.33 ?  100 VAL   B C    1 
ATOM   5363 O O    A VAL   B 1 100 ? 39.874 -32.182 12.234  0.86 25.16 ?  100 VAL   B O    1 
ATOM   5364 O O    B VAL   B 1 100 ? 39.888 -32.102 12.277  0.14 24.59 ?  100 VAL   B O    1 
ATOM   5365 C CB   A VAL   B 1 100 ? 38.617 -31.983 9.260   0.86 26.76 ?  100 VAL   B CB   1 
ATOM   5366 C CB   B VAL   B 1 100 ? 38.663 -32.008 9.259   0.14 24.81 ?  100 VAL   B CB   1 
ATOM   5367 C CG1  A VAL   B 1 100 ? 38.165 -33.246 9.978   0.86 27.79 ?  100 VAL   B CG1  1 
ATOM   5368 C CG1  B VAL   B 1 100 ? 38.135 -33.232 9.998   0.14 25.26 ?  100 VAL   B CG1  1 
ATOM   5369 C CG2  A VAL   B 1 100 ? 37.444 -31.338 8.532   0.86 27.53 ?  100 VAL   B CG2  1 
ATOM   5370 C CG2  B VAL   B 1 100 ? 37.557 -31.360 8.444   0.14 25.23 ?  100 VAL   B CG2  1 
ATOM   5371 H H    A VAL   B 1 100 ? 39.905 -29.989 8.666   0.86 25.56 ?  100 VAL   B H    1 
ATOM   5372 H H    B VAL   B 1 100 ? 39.922 -29.998 8.670   0.14 25.94 ?  100 VAL   B H    1 
ATOM   5373 H HA   A VAL   B 1 100 ? 38.535 -30.625 10.794  0.86 29.01 ?  100 VAL   B HA   1 
ATOM   5374 H HA   B VAL   B 1 100 ? 38.531 -30.642 10.783  0.14 28.46 ?  100 VAL   B HA   1 
ATOM   5375 H HB   A VAL   B 1 100 ? 39.276 -32.238 8.599   0.86 32.26 ?  100 VAL   B HB   1 
ATOM   5376 H HB   B VAL   B 1 100 ? 39.354 -32.306 8.647   0.14 29.92 ?  100 VAL   B HB   1 
ATOM   5377 H HG11 A VAL   B 1 100 ? 37.571 -33.745 9.392   0.86 33.50 ?  100 VAL   B HG11 1 
ATOM   5378 H HG11 B VAL   B 1 100 ? 37.570 -33.744 9.397   0.14 30.46 ?  100 VAL   B HG11 1 
ATOM   5379 H HG12 A VAL   B 1 100 ? 38.942 -33.786 10.193  0.86 33.50 ?  100 VAL   B HG12 1 
ATOM   5380 H HG12 B VAL   B 1 100 ? 38.884 -33.777 10.288  0.14 30.46 ?  100 VAL   B HG12 1 
ATOM   5381 H HG13 A VAL   B 1 100 ? 37.694 -33.001 10.789  0.86 33.50 ?  100 VAL   B HG13 1 
ATOM   5382 H HG13 B VAL   B 1 100 ? 37.619 -32.939 10.765  0.14 30.46 ?  100 VAL   B HG13 1 
ATOM   5383 H HG21 A VAL   B 1 100 ? 37.069 -31.981 7.907   0.86 33.19 ?  100 VAL   B HG21 1 
ATOM   5384 H HG21 B VAL   B 1 100 ? 37.174 -32.022 7.848   0.14 30.42 ?  100 VAL   B HG21 1 
ATOM   5385 H HG22 A VAL   B 1 100 ? 36.771 -31.080 9.181   0.86 33.19 ?  100 VAL   B HG22 1 
ATOM   5386 H HG22 B VAL   B 1 100 ? 36.877 -31.025 9.049   0.14 30.42 ?  100 VAL   B HG22 1 
ATOM   5387 H HG23 A VAL   B 1 100 ? 37.761 -30.559 8.053   0.86 33.19 ?  100 VAL   B HG23 1 
ATOM   5388 H HG23 B VAL   B 1 100 ? 37.934 -30.630 7.930   0.14 30.42 ?  100 VAL   B HG23 1 
ATOM   5389 N N    . ASN   B 1 101 ? 41.539 -31.665 10.816  1.00 24.77 ?  101 ASN   B N    1 
ATOM   5390 C CA   . ASN   B 1 101 ? 42.563 -32.208 11.708  1.00 27.23 ?  101 ASN   B CA   1 
ATOM   5391 C C    . ASN   B 1 101 ? 42.728 -31.371 12.971  1.00 30.05 ?  101 ASN   B C    1 
ATOM   5392 O O    . ASN   B 1 101 ? 43.345 -31.841 13.936  1.00 31.14 ?  101 ASN   B O    1 
ATOM   5393 C CB   . ASN   B 1 101 ? 43.900 -32.334 10.975  1.00 27.28 ?  101 ASN   B CB   1 
ATOM   5394 C CG   . ASN   B 1 101 ? 43.905 -33.470 9.975   1.00 27.02 ?  101 ASN   B CG   1 
ATOM   5395 O OD1  . ASN   B 1 101 ? 43.255 -34.491 10.183  1.00 27.93 ?  101 ASN   B OD1  1 
ATOM   5396 N ND2  . ASN   B 1 101 ? 44.633 -33.294 8.880   1.00 26.38 ?  101 ASN   B ND2  1 
ATOM   5397 H H    A ASN   B 1 101 ? 41.832 -31.386 10.059  0.86 29.87 ?  101 ASN   B H    1 
ATOM   5398 H H    B ASN   B 1 101 ? 41.830 -31.392 10.056  0.14 29.87 ?  101 ASN   B H    1 
ATOM   5399 H HA   . ASN   B 1 101 ? 42.294 -33.097 11.980  1.00 32.83 ?  101 ASN   B HA   1 
ATOM   5400 H HB2  . ASN   B 1 101 ? 44.083 -31.513 10.493  1.00 32.88 ?  101 ASN   B HB2  1 
ATOM   5401 H HB3  . ASN   B 1 101 ? 44.602 -32.502 11.623  1.00 32.88 ?  101 ASN   B HB3  1 
ATOM   5402 H HD21 . ASN   B 1 101 ? 44.667 -33.913 8.283   1.00 31.80 ?  101 ASN   B HD21 1 
ATOM   5403 H HD22 . ASN   B 1 101 ? 45.072 -32.564 8.768   1.00 31.80 ?  101 ASN   B HD22 1 
ATOM   5404 N N    A LYS   B 1 102 ? 42.199 -30.147 12.983  0.86 31.29 ?  102 LYS   B N    1 
ATOM   5405 N N    B LYS   B 1 102 ? 42.204 -30.146 12.981  0.14 31.77 ?  102 LYS   B N    1 
ATOM   5406 C CA   A LYS   B 1 102 ? 42.176 -29.297 14.166  0.86 33.14 ?  102 LYS   B CA   1 
ATOM   5407 C CA   B LYS   B 1 102 ? 42.182 -29.303 14.168  0.14 33.40 ?  102 LYS   B CA   1 
ATOM   5408 C C    A LYS   B 1 102 ? 40.802 -29.250 14.820  0.86 32.62 ?  102 LYS   B C    1 
ATOM   5409 C C    B LYS   B 1 102 ? 40.821 -29.289 14.852  0.14 33.03 ?  102 LYS   B C    1 
ATOM   5410 O O    A LYS   B 1 102 ? 40.586 -28.442 15.729  0.86 33.10 ?  102 LYS   B O    1 
ATOM   5411 O O    B LYS   B 1 102 ? 40.642 -28.556 15.830  0.14 33.37 ?  102 LYS   B O    1 
ATOM   5412 C CB   A LYS   B 1 102 ? 42.599 -27.872 13.808  0.86 35.88 ?  102 LYS   B CB   1 
ATOM   5413 C CB   B LYS   B 1 102 ? 42.587 -27.869 13.812  0.14 35.27 ?  102 LYS   B CB   1 
ATOM   5414 C CG   A LYS   B 1 102 ? 44.066 -27.698 13.459  0.86 38.51 ?  102 LYS   B CG   1 
ATOM   5415 C CG   B LYS   B 1 102 ? 44.056 -27.692 13.457  0.14 36.85 ?  102 LYS   B CG   1 
ATOM   5416 C CD   A LYS   B 1 102 ? 44.338 -26.256 13.051  0.86 41.08 ?  102 LYS   B CD   1 
ATOM   5417 C CD   B LYS   B 1 102 ? 44.342 -26.252 13.053  0.14 38.23 ?  102 LYS   B CD   1 
ATOM   5418 C CE   A LYS   B 1 102 ? 45.816 -25.992 12.815  0.86 43.05 ?  102 LYS   B CE   1 
ATOM   5419 C CE   B LYS   B 1 102 ? 45.827 -26.007 12.839  0.14 39.22 ?  102 LYS   B CE   1 
ATOM   5420 N NZ   A LYS   B 1 102 ? 46.060 -24.582 12.385  0.86 44.24 ?  102 LYS   B NZ   1 
ATOM   5421 N NZ   B LYS   B 1 102 ? 46.095 -24.604 12.415  0.14 39.77 ?  102 LYS   B NZ   1 
ATOM   5422 H H    A LYS   B 1 102 ? 41.832 -29.779 12.298  0.86 37.69 ?  102 LYS   B H    1 
ATOM   5423 H H    B LYS   B 1 102 ? 41.845 -29.773 12.293  0.14 38.27 ?  102 LYS   B H    1 
ATOM   5424 H HA   A LYS   B 1 102 ? 42.812 -29.641 14.812  0.86 39.92 ?  102 LYS   B HA   1 
ATOM   5425 H HA   B LYS   B 1 102 ? 42.831 -29.640 14.802  0.14 40.23 ?  102 LYS   B HA   1 
ATOM   5426 H HB2  A LYS   B 1 102 ? 42.079 -27.579 13.044  0.86 43.20 ?  102 LYS   B HB2  1 
ATOM   5427 H HB2  B LYS   B 1 102 ? 42.065 -27.578 13.049  0.14 42.47 ?  102 LYS   B HB2  1 
ATOM   5428 H HB3  A LYS   B 1 102 ? 42.410 -27.295 14.566  0.86 43.20 ?  102 LYS   B HB3  1 
ATOM   5429 H HB3  B LYS   B 1 102 ? 42.401 -27.296 14.572  0.14 42.47 ?  102 LYS   B HB3  1 
ATOM   5430 H HG2  A LYS   B 1 102 ? 44.612 -27.908 14.233  0.86 46.36 ?  102 LYS   B HG2  1 
ATOM   5431 H HG2  B LYS   B 1 102 ? 44.604 -27.908 14.228  0.14 44.37 ?  102 LYS   B HG2  1 
ATOM   5432 H HG3  A LYS   B 1 102 ? 44.293 -28.277 12.715  0.86 46.36 ?  102 LYS   B HG3  1 
ATOM   5433 H HG3  B LYS   B 1 102 ? 44.280 -28.270 12.711  0.14 44.37 ?  102 LYS   B HG3  1 
ATOM   5434 H HD2  A LYS   B 1 102 ? 43.861 -26.064 12.228  0.86 49.45 ?  102 LYS   B HD2  1 
ATOM   5435 H HD2  B LYS   B 1 102 ? 43.880 -26.056 12.223  0.14 46.03 ?  102 LYS   B HD2  1 
ATOM   5436 H HD3  A LYS   B 1 102 ? 44.034 -25.664 13.757  0.86 49.45 ?  102 LYS   B HD3  1 
ATOM   5437 H HD3  B LYS   B 1 102 ? 44.035 -25.657 13.755  0.14 46.03 ?  102 LYS   B HD3  1 
ATOM   5438 H HE2  A LYS   B 1 102 ? 46.304 -26.147 13.639  0.86 51.81 ?  102 LYS   B HE2  1 
ATOM   5439 H HE2  B LYS   B 1 102 ? 46.302 -26.169 13.670  0.14 47.21 ?  102 LYS   B HE2  1 
ATOM   5440 H HE3  A LYS   B 1 102 ? 46.139 -26.583 12.117  0.86 51.81 ?  102 LYS   B HE3  1 
ATOM   5441 H HE3  B LYS   B 1 102 ? 46.154 -26.601 12.145  0.14 47.21 ?  102 LYS   B HE3  1 
ATOM   5442 H HZ1  A LYS   B 1 102 ? 46.930 -24.451 12.253  0.86 53.24 ?  102 LYS   B HZ1  1 
ATOM   5443 H HZ1  B LYS   B 1 102 ? 46.969 -24.484 12.296  0.14 47.87 ?  102 LYS   B HZ1  1 
ATOM   5444 H HZ2  A LYS   B 1 102 ? 45.624 -24.416 11.627  0.86 53.24 ?  102 LYS   B HZ2  1 
ATOM   5445 H HZ2  B LYS   B 1 102 ? 45.672 -24.432 11.651  0.14 47.87 ?  102 LYS   B HZ2  1 
ATOM   5446 H HZ3  A LYS   B 1 102 ? 45.774 -24.019 13.012  0.86 53.24 ?  102 LYS   B HZ3  1 
ATOM   5447 H HZ3  B LYS   B 1 102 ? 45.807 -24.038 13.039  0.14 47.87 ?  102 LYS   B HZ3  1 
ATOM   5448 N N    . GLY   B 1 103 ? 39.862 -30.073 14.364  1.00 32.19 ?  103 GLY   B N    1 
ATOM   5449 C CA   . GLY   B 1 103 ? 38.537 -30.112 14.946  1.00 31.60 ?  103 GLY   B CA   1 
ATOM   5450 C C    . GLY   B 1 103 ? 37.596 -29.025 14.478  1.00 30.33 ?  103 GLY   B C    1 
ATOM   5451 O O    . GLY   B 1 103 ? 36.517 -28.871 15.061  1.00 31.28 ?  103 GLY   B O    1 
ATOM   5452 H H    A GLY   B 1 103 ? 39.970 -30.617 13.709  0.86 38.77 ?  103 GLY   B H    1 
ATOM   5453 H H    B GLY   B 1 103 ? 39.961 -30.597 13.691  0.14 38.77 ?  103 GLY   B H    1 
ATOM   5454 H HA2  . GLY   B 1 103 ? 38.128 -30.966 14.739  1.00 38.06 ?  103 GLY   B HA2  1 
ATOM   5455 H HA3  . GLY   B 1 103 ? 38.613 -30.044 15.912  1.00 38.06 ?  103 GLY   B HA3  1 
ATOM   5456 N N    A GLU   B 1 104 ? 37.962 -28.273 13.443  0.86 28.30 ?  104 GLU   B N    1 
ATOM   5457 N N    B GLU   B 1 104 ? 37.961 -28.269 13.448  0.14 30.05 ?  104 GLU   B N    1 
ATOM   5458 C CA   A GLU   B 1 104 ? 37.133 -27.172 12.980  0.86 26.23 ?  104 GLU   B CA   1 
ATOM   5459 C CA   B GLU   B 1 104 ? 37.119 -27.180 12.983  0.14 29.58 ?  104 GLU   B CA   1 
ATOM   5460 C C    A GLU   B 1 104 ? 35.955 -27.688 12.158  0.86 27.34 ?  104 GLU   B C    1 
ATOM   5461 C C    B GLU   B 1 104 ? 35.962 -27.713 12.143  0.14 29.77 ?  104 GLU   B C    1 
ATOM   5462 O O    A GLU   B 1 104 ? 36.001 -28.777 11.576  0.86 28.19 ?  104 GLU   B O    1 
ATOM   5463 O O    B GLU   B 1 104 ? 36.053 -28.774 11.519  0.14 29.88 ?  104 GLU   B O    1 
ATOM   5464 C CB   A GLU   B 1 104 ? 37.977 -26.175 12.186  0.86 24.25 ?  104 GLU   B CB   1 
ATOM   5465 C CB   B GLU   B 1 104 ? 37.950 -26.172 12.189  0.14 28.95 ?  104 GLU   B CB   1 
ATOM   5466 C CG   A GLU   B 1 104 ? 39.080 -25.569 13.040  0.86 22.71 ?  104 GLU   B CG   1 
ATOM   5467 C CG   B GLU   B 1 104 ? 39.046 -25.527 13.025  0.14 28.46 ?  104 GLU   B CG   1 
ATOM   5468 C CD   A GLU   B 1 104 ? 40.017 -24.652 12.285  0.86 21.57 ?  104 GLU   B CD   1 
ATOM   5469 C CD   B GLU   B 1 104 ? 39.962 -24.634 12.212  0.14 28.09 ?  104 GLU   B CD   1 
ATOM   5470 O OE1  A GLU   B 1 104 ? 40.037 -24.668 11.033  0.86 20.03 ?  104 GLU   B OE1  1 
ATOM   5471 O OE1  B GLU   B 1 104 ? 39.861 -24.644 10.967  0.14 27.84 ?  104 GLU   B OE1  1 
ATOM   5472 O OE2  A GLU   B 1 104 ? 40.746 -23.906 12.969  0.86 22.78 -1 104 GLU   B OE2  1 
ATOM   5473 O OE2  B GLU   B 1 104 ? 40.786 -23.920 12.821  0.14 28.16 -1 104 GLU   B OE2  1 
ATOM   5474 H H    A GLU   B 1 104 ? 38.693 -28.374 13.001  0.86 34.11 ?  104 GLU   B H    1 
ATOM   5475 H H    B GLU   B 1 104 ? 38.693 -28.366 13.007  0.14 36.21 ?  104 GLU   B H    1 
ATOM   5476 H HA   A GLU   B 1 104 ? 36.776 -26.705 13.752  0.86 31.63 ?  104 GLU   B HA   1 
ATOM   5477 H HA   B GLU   B 1 104 ? 36.745 -26.720 13.749  0.14 35.64 ?  104 GLU   B HA   1 
ATOM   5478 H HB2  A GLU   B 1 104 ? 38.390 -26.629 11.437  0.86 29.25 ?  104 GLU   B HB2  1 
ATOM   5479 H HB2  B GLU   B 1 104 ? 38.370 -26.625 11.442  0.14 34.89 ?  104 GLU   B HB2  1 
ATOM   5480 H HB3  A GLU   B 1 104 ? 37.409 -25.454 11.871  0.86 29.25 ?  104 GLU   B HB3  1 
ATOM   5481 H HB3  B GLU   B 1 104 ? 37.367 -25.467 11.865  0.14 34.89 ?  104 GLU   B HB3  1 
ATOM   5482 H HG2  A GLU   B 1 104 ? 38.677 -25.048 13.755  0.86 27.40 ?  104 GLU   B HG2  1 
ATOM   5483 H HG2  B GLU   B 1 104 ? 38.636 -24.985 13.719  0.14 34.29 ?  104 GLU   B HG2  1 
ATOM   5484 H HG3  A GLU   B 1 104 ? 39.616 -26.282 13.421  0.86 27.40 ?  104 GLU   B HG3  1 
ATOM   5485 H HG3  B GLU   B 1 104 ? 39.586 -26.225 13.431  0.14 34.29 ?  104 GLU   B HG3  1 
ATOM   5486 N N    A ASP   B 1 105 ? 34.890 -26.892 12.128  0.86 27.78 ?  105 ASP   B N    1 
ATOM   5487 N N    B ASP   B 1 105 ? 34.866 -26.958 12.137  0.14 29.77 ?  105 ASP   B N    1 
ATOM   5488 C CA   A ASP   B 1 105 ? 33.611 -27.334 11.586  0.86 29.07 ?  105 ASP   B CA   1 
ATOM   5489 C CA   B ASP   B 1 105 ? 33.615 -27.429 11.557  0.14 29.91 ?  105 ASP   B CA   1 
ATOM   5490 C C    A ASP   B 1 105 ? 33.671 -27.380 10.063  0.86 27.35 ?  105 ASP   B C    1 
ATOM   5491 C C    B ASP   B 1 105 ? 33.711 -27.444 10.035  0.14 29.16 ?  105 ASP   B C    1 
ATOM   5492 O O    A ASP   B 1 105 ? 33.822 -26.345 9.407   0.86 26.63 ?  105 ASP   B O    1 
ATOM   5493 O O    B ASP   B 1 105 ? 33.980 -26.413 9.409   0.14 29.02 ?  105 ASP   B O    1 
ATOM   5494 C CB   A ASP   B 1 105 ? 32.504 -26.389 12.051  0.86 32.33 ?  105 ASP   B CB   1 
ATOM   5495 C CB   B ASP   B 1 105 ? 32.468 -26.530 12.013  0.14 30.65 ?  105 ASP   B CB   1 
ATOM   5496 C CG   A ASP   B 1 105 ? 31.126 -26.847 11.615  0.86 35.40 ?  105 ASP   B CG   1 
ATOM   5497 C CG   B ASP   B 1 105 ? 31.106 -27.109 11.679  0.14 31.35 ?  105 ASP   B CG   1 
ATOM   5498 O OD1  A ASP   B 1 105 ? 31.019 -27.935 11.010  0.86 35.45 ?  105 ASP   B OD1  1 
ATOM   5499 O OD1  B ASP   B 1 105 ? 31.053 -28.143 10.980  0.14 31.54 ?  105 ASP   B OD1  1 
ATOM   5500 O OD2  A ASP   B 1 105 ? 30.145 -26.119 11.880  0.86 37.43 -1 105 ASP   B OD2  1 
ATOM   5501 O OD2  B ASP   B 1 105 ? 30.088 -26.537 12.123  0.14 31.56 -1 105 ASP   B OD2  1 
ATOM   5502 H H    A ASP   B 1 105 ? 34.888 -26.083 12.410  0.86 33.48 ?  105 ASP   B H    1 
ATOM   5503 H H    B ASP   B 1 105 ? 34.822 -26.164 12.461  0.14 35.87 ?  105 ASP   B H    1 
ATOM   5504 H HA   A ASP   B 1 105 ? 33.406 -28.223 11.914  0.86 35.03 ?  105 ASP   B HA   1 
ATOM   5505 H HA   B ASP   B 1 105 ? 33.432 -28.332 11.860  0.14 36.04 ?  105 ASP   B HA   1 
ATOM   5506 H HB2  A ASP   B 1 105 ? 32.521 -26.331 13.023  0.86 38.94 ?  105 ASP   B HB2  1 
ATOM   5507 H HB2  B ASP   B 1 105 ? 32.520 -26.415 12.977  0.14 36.92 ?  105 ASP   B HB2  1 
ATOM   5508 H HB3  A ASP   B 1 105 ? 32.654 -25.509 11.670  0.86 38.94 ?  105 ASP   B HB3  1 
ATOM   5509 H HB3  B ASP   B 1 105 ? 32.547 -25.667 11.575  0.14 36.92 ?  105 ASP   B HB3  1 
ATOM   5510 N N    A ILE   B 1 106 ? 33.534 -28.586 9.503   0.86 26.71 ?  106 ILE   B N    1 
ATOM   5511 N N    B ILE   B 1 106 ? 33.486 -28.620 9.442   0.14 28.43 ?  106 ILE   B N    1 
ATOM   5512 C CA   A ILE   B 1 106 ? 33.529 -28.763 8.056   0.86 25.66 ?  106 ILE   B CA   1 
ATOM   5513 C CA   B ILE   B 1 106 ? 33.516 -28.762 7.991   0.14 27.79 ?  106 ILE   B CA   1 
ATOM   5514 C C    A ILE   B 1 106 ? 32.435 -27.936 7.385   0.86 24.16 ?  106 ILE   B C    1 
ATOM   5515 C C    B ILE   B 1 106 ? 32.424 -27.939 7.319   0.14 27.09 ?  106 ILE   B C    1 
ATOM   5516 O O    A ILE   B 1 106 ? 32.547 -27.602 6.201   0.86 23.40 ?  106 ILE   B O    1 
ATOM   5517 O O    B ILE   B 1 106 ? 32.522 -27.641 6.124   0.14 26.96 ?  106 ILE   B O    1 
ATOM   5518 C CB   A ILE   B 1 106 ? 33.431 -30.273 7.727   0.86 26.61 ?  106 ILE   B CB   1 
ATOM   5519 C CB   B ILE   B 1 106 ? 33.429 -30.259 7.611   0.14 27.89 ?  106 ILE   B CB   1 
ATOM   5520 C CG1  A ILE   B 1 106 ? 33.675 -30.525 6.240   0.86 27.51 ?  106 ILE   B CG1  1 
ATOM   5521 C CG1  B ILE   B 1 106 ? 33.715 -30.465 6.121   0.14 27.91 ?  106 ILE   B CG1  1 
ATOM   5522 C CG2  A ILE   B 1 106 ? 32.080 -30.835 8.159   0.86 27.66 ?  106 ILE   B CG2  1 
ATOM   5523 C CG2  B ILE   B 1 106 ? 32.063 -30.827 7.976   0.14 28.05 ?  106 ILE   B CG2  1 
ATOM   5524 C CD1  A ILE   B 1 106 ? 35.036 -30.072 5.775   0.86 27.90 ?  106 ILE   B CD1  1 
ATOM   5525 C CD1  B ILE   B 1 106 ? 35.077 -29.970 5.688   0.14 27.92 ?  106 ILE   B CD1  1 
ATOM   5526 H H    A ILE   B 1 106 ? 33.448 -29.315 9.949   0.86 32.20 ?  106 ILE   B H    1 
ATOM   5527 H H    B ILE   B 1 106 ? 33.327 -29.351 9.862   0.14 34.27 ?  106 ILE   B H    1 
ATOM   5528 H HA   A ILE   B 1 106 ? 34.378 -28.446 7.718   0.86 30.95 ?  106 ILE   B HA   1 
ATOM   5529 H HA   B ILE   B 1 106 ? 34.366 -28.427 7.675   0.14 33.49 ?  106 ILE   B HA   1 
ATOM   5530 H HB   A ILE   B 1 106 ? 34.120 -30.739 8.229   0.86 32.08 ?  106 ILE   B HB   1 
ATOM   5531 H HB   B ILE   B 1 106 ? 34.100 -30.740 8.117   0.14 33.62 ?  106 ILE   B HB   1 
ATOM   5532 H HG12 A ILE   B 1 106 ? 33.607 -31.480 6.069   0.86 33.16 ?  106 ILE   B HG12 1 
ATOM   5533 H HG12 B ILE   B 1 106 ? 33.672 -31.416 5.924   0.14 33.64 ?  106 ILE   B HG12 1 
ATOM   5534 H HG13 A ILE   B 1 106 ? 33.008 -30.051 5.724   0.86 33.16 ?  106 ILE   B HG13 1 
ATOM   5535 H HG13 B ILE   B 1 106 ? 33.048 -29.994 5.601   0.14 33.64 ?  106 ILE   B HG13 1 
ATOM   5536 H HG21 A ILE   B 1 106 ? 32.088 -31.799 8.046   0.86 33.34 ?  106 ILE   B HG21 1 
ATOM   5537 H HG21 B ILE   B 1 106 ? 32.082 -31.790 7.862   0.14 33.81 ?  106 ILE   B HG21 1 
ATOM   5538 H HG22 A ILE   B 1 106 ? 31.930 -30.615 9.092   0.86 33.34 ?  106 ILE   B HG22 1 
ATOM   5539 H HG22 B ILE   B 1 106 ? 31.867 -30.608 8.900   0.14 33.81 ?  106 ILE   B HG22 1 
ATOM   5540 H HG23 A ILE   B 1 106 ? 31.383 -30.444 7.611   0.86 33.34 ?  106 ILE   B HG23 1 
ATOM   5541 H HG23 B ILE   B 1 106 ? 31.391 -30.439 7.394   0.14 33.81 ?  106 ILE   B HG23 1 
ATOM   5542 H HD11 A ILE   B 1 106 ? 35.231 -30.482 4.919   0.86 33.63 ?  106 ILE   B HD11 1 
ATOM   5543 H HD11 B ILE   B 1 106 ? 35.289 -30.353 4.824   0.14 33.65 ?  106 ILE   B HD11 1 
ATOM   5544 H HD12 A ILE   B 1 106 ? 35.036 -29.105 5.685   0.86 33.63 ?  106 ILE   B HD12 1 
ATOM   5545 H HD12 B ILE   B 1 106 ? 35.055 -29.002 5.625   0.14 33.65 ?  106 ILE   B HD12 1 
ATOM   5546 H HD13 A ILE   B 1 106 ? 35.702 -30.343 6.429   0.86 33.63 ?  106 ILE   B HD13 1 
ATOM   5547 H HD13 B ILE   B 1 106 ? 35.736 -30.247 6.344   0.14 33.65 ?  106 ILE   B HD13 1 
ATOM   5548 N N    A GLN   B 1 107 ? 31.380 -27.577 8.120   0.86 24.93 ?  107 GLN   B N    1 
ATOM   5549 N N    B GLN   B 1 107 ? 31.380 -27.562 8.060   0.14 26.68 ?  107 GLN   B N    1 
ATOM   5550 C CA   A GLN   B 1 107 ? 30.309 -26.766 7.548   0.86 25.20 ?  107 GLN   B CA   1 
ATOM   5551 C CA   B GLN   B 1 107 ? 30.307 -26.754 7.490   0.14 26.20 ?  107 GLN   B CA   1 
ATOM   5552 C C    A GLN   B 1 107 ? 30.802 -25.411 7.046   0.86 23.30 ?  107 GLN   B C    1 
ATOM   5553 C C    B GLN   B 1 107 ? 30.796 -25.384 7.036   0.14 23.76 ?  107 GLN   B C    1 
ATOM   5554 O O    A GLN   B 1 107 ? 30.164 -24.823 6.168   0.86 24.54 ?  107 GLN   B O    1 
ATOM   5555 O O    B GLN   B 1 107 ? 30.140 -24.751 6.201   0.14 23.99 ?  107 GLN   B O    1 
ATOM   5556 C CB   A GLN   B 1 107 ? 29.195 -26.583 8.585   0.86 28.91 ?  107 GLN   B CB   1 
ATOM   5557 C CB   B GLN   B 1 107 ? 29.176 -26.604 8.512   0.14 28.29 ?  107 GLN   B CB   1 
ATOM   5558 C CG   A GLN   B 1 107 ? 27.863 -26.109 8.015   0.86 32.86 ?  107 GLN   B CG   1 
ATOM   5559 C CG   B GLN   B 1 107 ? 27.858 -26.097 7.938   0.14 30.16 ?  107 GLN   B CG   1 
ATOM   5560 C CD   A GLN   B 1 107 ? 27.764 -24.597 7.918   0.86 35.69 ?  107 GLN   B CD   1 
ATOM   5561 C CD   B GLN   B 1 107 ? 27.742 -24.585 7.969   0.14 31.62 ?  107 GLN   B CD   1 
ATOM   5562 O OE1  A GLN   B 1 107 ? 28.610 -23.871 8.443   0.86 36.76 ?  107 GLN   B OE1  1 
ATOM   5563 O OE1  B GLN   B 1 107 ? 28.581 -23.895 8.551   0.14 32.12 ?  107 GLN   B OE1  1 
ATOM   5564 N NE2  A GLN   B 1 107 ? 26.720 -24.114 7.246   0.86 36.70 ?  107 GLN   B NE2  1 
ATOM   5565 N NE2  B GLN   B 1 107 ? 26.694 -24.060 7.344   0.14 32.13 ?  107 GLN   B NE2  1 
ATOM   5566 H H    A GLN   B 1 107 ? 31.266 -27.788 8.941   0.86 30.06 ?  107 GLN   B H    1 
ATOM   5567 H H    B GLN   B 1 107 ? 31.268 -27.765 8.886   0.14 32.16 ?  107 GLN   B H    1 
ATOM   5568 H HA   A GLN   B 1 107 ? 29.933 -27.246 6.791   0.86 30.39 ?  107 GLN   B HA   1 
ATOM   5569 H HA   B GLN   B 1 107 ? 29.947 -27.215 6.716   0.14 31.59 ?  107 GLN   B HA   1 
ATOM   5570 H HB2  A GLN   B 1 107 ? 29.041 -27.432 9.022   0.86 34.84 ?  107 GLN   B HB2  1 
ATOM   5571 H HB2  B GLN   B 1 107 ? 29.004 -27.470 8.908   0.14 34.10 ?  107 GLN   B HB2  1 
ATOM   5572 H HB3  A GLN   B 1 107 ? 29.490 -25.929 9.238   0.86 34.84 ?  107 GLN   B HB3  1 
ATOM   5573 H HB3  B GLN   B 1 107 ? 29.458 -25.983 9.201   0.14 34.10 ?  107 GLN   B HB3  1 
ATOM   5574 H HG2  A GLN   B 1 107 ? 27.750 -26.471 7.123   0.86 39.58 ?  107 GLN   B HG2  1 
ATOM   5575 H HG2  B GLN   B 1 107 ? 27.783 -26.383 7.015   0.14 36.34 ?  107 GLN   B HG2  1 
ATOM   5576 H HG3  A GLN   B 1 107 ? 27.145 -26.424 8.591   0.86 39.58 ?  107 GLN   B HG3  1 
ATOM   5577 H HG3  B GLN   B 1 107 ? 27.125 -26.467 8.459   0.14 36.34 ?  107 GLN   B HG3  1 
ATOM   5578 H HE21 A GLN   B 1 107 ? 26.149 -24.652 6.891   0.86 44.18 ?  107 GLN   B HE21 1 
ATOM   5579 H HE21 B GLN   B 1 107 ? 26.128 -24.573 6.947   0.14 38.71 ?  107 GLN   B HE21 1 
ATOM   5580 H HE22 A GLN   B 1 107 ? 26.613 -23.264 7.166   0.86 44.18 ?  107 GLN   B HE22 1 
ATOM   5581 H HE22 B GLN   B 1 107 ? 26.581 -23.208 7.336   0.14 38.71 ?  107 GLN   B HE22 1 
ATOM   5582 N N    . LEU   B 1 108 ? 31.929 -24.911 7.561   1.00 21.28 ?  108 LEU   B N    1 
ATOM   5583 C CA   . LEU   B 1 108 ? 32.483 -23.616 7.155   1.00 19.15 ?  108 LEU   B CA   1 
ATOM   5584 C C    . LEU   B 1 108 ? 33.123 -23.636 5.774   1.00 16.66 ?  108 LEU   B C    1 
ATOM   5585 O O    . LEU   B 1 108 ? 33.554 -22.579 5.287   1.00 16.53 ?  108 LEU   B O    1 
ATOM   5586 C CB   . LEU   B 1 108 ? 33.492 -23.142 8.200   1.00 19.91 ?  108 LEU   B CB   1 
ATOM   5587 C CG   . LEU   B 1 108 ? 32.862 -22.630 9.495   1.00 21.59 ?  108 LEU   B CG   1 
ATOM   5588 C CD1  . LEU   B 1 108 ? 33.881 -22.589 10.618  1.00 21.75 ?  108 LEU   B CD1  1 
ATOM   5589 C CD2  . LEU   B 1 108 ? 32.276 -21.247 9.273   1.00 22.48 ?  108 LEU   B CD2  1 
ATOM   5590 H H    A LEU   B 1 108 ? 32.390 -25.309 8.163   0.86 25.69 ?  108 LEU   B H    1 
ATOM   5591 H H    B LEU   B 1 108 ? 32.388 -25.320 8.158   0.14 25.69 ?  108 LEU   B H    1 
ATOM   5592 H HA   . LEU   B 1 108 ? 31.763 -22.973 7.130   1.00 23.13 ?  108 LEU   B HA   1 
ATOM   5593 H HB2  . LEU   B 1 108 ? 34.072 -23.883 8.432   1.00 24.04 ?  108 LEU   B HB2  1 
ATOM   5594 H HB3  . LEU   B 1 108 ? 34.013 -22.420 7.822   1.00 24.04 ?  108 LEU   B HB3  1 
ATOM   5595 H HG   . LEU   B 1 108 ? 32.140 -23.224 9.762   1.00 26.05 ?  108 LEU   B HG   1 
ATOM   5596 H HD11 . LEU   B 1 108 ? 33.446 -22.280 11.430  1.00 26.25 ?  108 LEU   B HD11 1 
ATOM   5597 H HD12 . LEU   B 1 108 ? 34.236 -23.481 10.754  1.00 26.25 ?  108 LEU   B HD12 1 
ATOM   5598 H HD13 . LEU   B 1 108 ? 34.595 -21.981 10.373  1.00 26.25 ?  108 LEU   B HD13 1 
ATOM   5599 H HD21 . LEU   B 1 108 ? 31.943 -20.905 10.116  1.00 27.12 ?  108 LEU   B HD21 1 
ATOM   5600 H HD22 . LEU   B 1 108 ? 32.971 -20.664 8.929   1.00 27.12 ?  108 LEU   B HD22 1 
ATOM   5601 H HD23 . LEU   B 1 108 ? 31.551 -21.311 8.631   1.00 27.12 ?  108 LEU   B HD23 1 
ATOM   5602 N N    . LEU   B 1 109 ? 33.192 -24.802 5.135   1.00 15.58 ?  109 LEU   B N    1 
ATOM   5603 C CA   . LEU   B 1 109 ? 33.828 -24.905 3.829   1.00 14.81 ?  109 LEU   B CA   1 
ATOM   5604 C C    . LEU   B 1 109 ? 33.062 -24.128 2.767   1.00 14.16 ?  109 LEU   B C    1 
ATOM   5605 O O    . LEU   B 1 109 ? 33.677 -23.529 1.877   1.00 14.06 ?  109 LEU   B O    1 
ATOM   5606 C CB   . LEU   B 1 109 ? 33.963 -26.380 3.449   1.00 15.29 ?  109 LEU   B CB   1 
ATOM   5607 C CG   . LEU   B 1 109 ? 34.732 -26.718 2.177   1.00 14.72 ?  109 LEU   B CG   1 
ATOM   5608 C CD1  . LEU   B 1 109 ? 36.116 -26.067 2.183   1.00 14.85 ?  109 LEU   B CD1  1 
ATOM   5609 C CD2  . LEU   B 1 109 ? 34.851 -28.241 2.042   1.00 15.93 ?  109 LEU   B CD2  1 
ATOM   5610 H H    . LEU   B 1 109 ? 32.891 -25.545 5.436   1.00 18.84 ?  109 LEU   B H    1 
ATOM   5611 H HA   . LEU   B 1 109 ? 34.722 -24.531 3.880   1.00 17.92 ?  109 LEU   B HA   1 
ATOM   5612 H HB2  . LEU   B 1 109 ? 34.415 -26.837 4.175   1.00 18.50 ?  109 LEU   B HB2  1 
ATOM   5613 H HB3  . LEU   B 1 109 ? 33.073 -26.748 3.347   1.00 18.50 ?  109 LEU   B HB3  1 
ATOM   5614 H HG   . LEU   B 1 109 ? 34.240 -26.395 1.404   1.00 17.81 ?  109 LEU   B HG   1 
ATOM   5615 H HD11 . LEU   B 1 109 ? 36.637 -26.422 1.446   1.00 17.97 ?  109 LEU   B HD11 1 
ATOM   5616 H HD12 . LEU   B 1 109 ? 36.012 -25.111 2.087   1.00 17.97 ?  109 LEU   B HD12 1 
ATOM   5617 H HD13 . LEU   B 1 109 ? 36.555 -26.274 3.025   1.00 17.97 ?  109 LEU   B HD13 1 
ATOM   5618 H HD21 . LEU   B 1 109 ? 35.413 -28.450 1.277   1.00 19.26 ?  109 LEU   B HD21 1 
ATOM   5619 H HD22 . LEU   B 1 109 ? 35.249 -28.601 2.850   1.00 19.26 ?  109 LEU   B HD22 1 
ATOM   5620 H HD23 . LEU   B 1 109 ? 33.967 -28.623 1.913   1.00 19.26 ?  109 LEU   B HD23 1 
ATOM   5621 N N    . LYS   B 1 110 ? 31.728 -24.091 2.851   1.00 13.99 ?  110 LYS   B N    1 
ATOM   5622 C CA   . LYS   B 1 110 ? 30.972 -23.329 1.861   1.00 13.69 ?  110 LYS   B CA   1 
ATOM   5623 C C    . LYS   B 1 110 ? 31.306 -21.841 1.949   1.00 13.53 ?  110 LYS   B C    1 
ATOM   5624 O O    . LYS   B 1 110 ? 31.556 -21.191 0.932   1.00 13.64 ?  110 LYS   B O    1 
ATOM   5625 C CB   . LYS   B 1 110 ? 29.468 -23.578 2.006   1.00 14.50 ?  110 LYS   B CB   1 
ATOM   5626 C CG   . LYS   B 1 110 ? 28.667 -22.958 0.864   1.00 14.97 ?  110 LYS   B CG   1 
ATOM   5627 C CD   . LYS   B 1 110 ? 27.203 -23.391 0.893   1.00 15.54 ?  110 LYS   B CD   1 
ATOM   5628 C CE   . LYS   B 1 110 ? 26.433 -22.853 -0.313  1.00 16.52 ?  110 LYS   B CE   1 
ATOM   5629 N NZ   . LYS   B 1 110 ? 26.748 -23.573 -1.576  1.00 16.59 ?  110 LYS   B NZ   1 
ATOM   5630 H H    . LYS   B 1 110 ? 31.258 -24.491 3.447   1.00 16.94 ?  110 LYS   B H    1 
ATOM   5631 H HA   . LYS   B 1 110 ? 31.234 -23.635 0.976   1.00 16.58 ?  110 LYS   B HA   1 
ATOM   5632 H HB2  . LYS   B 1 110 ? 29.304 -24.537 2.003   1.00 17.55 ?  110 LYS   B HB2  1 
ATOM   5633 H HB3  . LYS   B 1 110 ? 29.161 -23.191 2.837   1.00 17.55 ?  110 LYS   B HB3  1 
ATOM   5634 H HG2  . LYS   B 1 110 ? 28.695 -21.993 0.941   1.00 18.12 ?  110 LYS   B HG2  1 
ATOM   5635 H HG3  . LYS   B 1 110 ? 29.045 -23.239 0.016   1.00 18.12 ?  110 LYS   B HG3  1 
ATOM   5636 H HD2  . LYS   B 1 110 ? 27.154 -24.362 0.877   1.00 18.79 ?  110 LYS   B HD2  1 
ATOM   5637 H HD3  . LYS   B 1 110 ? 26.783 -23.050 1.700   1.00 18.79 ?  110 LYS   B HD3  1 
ATOM   5638 H HE2  . LYS   B 1 110 ? 25.485 -22.939 -0.148  1.00 19.98 ?  110 LYS   B HE2  1 
ATOM   5639 H HE3  . LYS   B 1 110 ? 26.667 -21.918 -0.439  1.00 19.98 ?  110 LYS   B HE3  1 
ATOM   5640 H HZ1  . LYS   B 1 110 ? 26.285 -23.227 -2.249  1.00 20.06 ?  110 LYS   B HZ1  1 
ATOM   5641 H HZ2  . LYS   B 1 110 ? 27.619 -23.505 -1.758  1.00 20.06 ?  110 LYS   B HZ2  1 
ATOM   5642 H HZ3  . LYS   B 1 110 ? 26.542 -24.436 -1.492  1.00 20.06 ?  110 LYS   B HZ3  1 
ATOM   5643 N N    . SER   B 1 111 ? 31.331 -21.292 3.166   1.00 14.40 ?  111 SER   B N    1 
ATOM   5644 C CA   . SER   B 1 111 ? 31.717 -19.892 3.339   1.00 14.32 ?  111 SER   B CA   1 
ATOM   5645 C C    . SER   B 1 111 ? 33.103 -19.623 2.756   1.00 13.81 ?  111 SER   B C    1 
ATOM   5646 O O    . SER   B 1 111 ? 33.321 -18.592 2.105   1.00 13.81 ?  111 SER   B O    1 
ATOM   5647 C CB   . SER   B 1 111 ? 31.692 -19.530 4.822   1.00 15.47 ?  111 SER   B CB   1 
ATOM   5648 O OG   . SER   B 1 111 ? 30.380 -19.545 5.339   1.00 16.99 ?  111 SER   B OG   1 
ATOM   5649 H H    . SER   B 1 111 ? 31.134 -21.706 3.895   1.00 17.42 ?  111 SER   B H    1 
ATOM   5650 H HA   . SER   B 1 111 ? 31.080 -19.327 2.875   1.00 17.33 ?  111 SER   B HA   1 
ATOM   5651 H HB2  . SER   B 1 111 ? 32.227 -20.172 5.312   1.00 18.71 ?  111 SER   B HB2  1 
ATOM   5652 H HB3  . SER   B 1 111 ? 32.057 -18.640 4.934   1.00 18.71 ?  111 SER   B HB3  1 
ATOM   5653 H HG   . SER   B 1 111 ? 30.387 -19.344 6.161   1.00 20.54 ?  111 SER   B HG   1 
ATOM   5654 N N    . ALA   B 1 112 ? 34.050 -20.536 2.985   1.00 13.55 ?  112 ALA   B N    1 
ATOM   5655 C CA   . ALA   B 1 112 ? 35.396 -20.373 2.437   1.00 13.07 ?  112 ALA   B CA   1 
ATOM   5656 C C    . ALA   B 1 112 ? 35.358 -20.276 0.914   1.00 12.66 ?  112 ALA   B C    1 
ATOM   5657 O O    . ALA   B 1 112 ? 35.984 -19.392 0.317   1.00 13.07 ?  112 ALA   B O    1 
ATOM   5658 C CB   . ALA   B 1 112 ? 36.294 -21.523 2.904   1.00 13.81 ?  112 ALA   B CB   1 
ATOM   5659 H H    . ALA   B 1 112 ? 33.938 -21.253 3.456   1.00 16.41 ?  112 ALA   B H    1 
ATOM   5660 H HA   . ALA   B 1 112 ? 35.769 -19.549 2.781   1.00 15.83 ?  112 ALA   B HA   1 
ATOM   5661 H HB1  . ALA   B 1 112 ? 37.186 -21.392 2.538   1.00 16.72 ?  112 ALA   B HB1  1 
ATOM   5662 H HB2  . ALA   B 1 112 ? 36.338 -21.518 3.876   1.00 16.72 ?  112 ALA   B HB2  1 
ATOM   5663 H HB3  . ALA   B 1 112 ? 35.929 -22.363 2.594   1.00 16.72 ?  112 ALA   B HB3  1 
ATOM   5664 N N    . TYR   B 1 113 ? 34.616 -21.177 0.262   1.00 12.54 ?  113 TYR   B N    1 
ATOM   5665 C CA   . TYR   B 1 113 ? 34.545 -21.133 -1.194  1.00 12.34 ?  113 TYR   B CA   1 
ATOM   5666 C C    . TYR   B 1 113 ? 33.833 -19.885 -1.713  1.00 11.95 ?  113 TYR   B C    1 
ATOM   5667 O O    . TYR   B 1 113 ? 34.108 -19.448 -2.837  1.00 12.39 ?  113 TYR   B O    1 
ATOM   5668 C CB   . TYR   B 1 113 ? 33.882 -22.394 -1.750  1.00 12.26 ?  113 TYR   B CB   1 
ATOM   5669 C CG   . TYR   B 1 113 ? 34.841 -23.545 -2.014  1.00 13.08 ?  113 TYR   B CG   1 
ATOM   5670 C CD1  . TYR   B 1 113 ? 35.824 -23.443 -2.993  1.00 13.65 ?  113 TYR   B CD1  1 
ATOM   5671 C CD2  . TYR   B 1 113 ? 34.747 -24.741 -1.306  1.00 13.35 ?  113 TYR   B CD2  1 
ATOM   5672 C CE1  . TYR   B 1 113 ? 36.702 -24.478 -3.244  1.00 13.41 ?  113 TYR   B CE1  1 
ATOM   5673 C CE2  . TYR   B 1 113 ? 35.620 -25.789 -1.552  1.00 13.66 ?  113 TYR   B CE2  1 
ATOM   5674 C CZ   . TYR   B 1 113 ? 36.589 -25.659 -2.529  1.00 13.48 ?  113 TYR   B CZ   1 
ATOM   5675 O OH   . TYR   B 1 113 ? 37.470 -26.677 -2.802  1.00 14.39 ?  113 TYR   B OH   1 
ATOM   5676 H H    . TYR   B 1 113 ? 34.153 -21.805 0.637   1.00 15.20 ?  113 TYR   B H    1 
ATOM   5677 H HA   . TYR   B 1 113 ? 35.447 -21.107 -1.530  1.00 14.95 ?  113 TYR   B HA   1 
ATOM   5678 H HB2  . TYR   B 1 113 ? 33.216 -22.706 -1.111  1.00 14.86 ?  113 TYR   B HB2  1 
ATOM   5679 H HB3  . TYR   B 1 113 ? 33.443 -22.169 -2.586  1.00 14.86 ?  113 TYR   B HB3  1 
ATOM   5680 H HD1  . TYR   B 1 113 ? 35.905 -22.650 -3.482  1.00 16.53 ?  113 TYR   B HD1  1 
ATOM   5681 H HD2  . TYR   B 1 113 ? 34.090 -24.829 -0.656  1.00 16.17 ?  113 TYR   B HD2  1 
ATOM   5682 H HE1  . TYR   B 1 113 ? 37.356 -24.390 -3.908  1.00 16.24 ?  113 TYR   B HE1  1 
ATOM   5683 H HE2  . TYR   B 1 113 ? 35.542 -26.582 -1.078  1.00 16.54 ?  113 TYR   B HE2  1 
ATOM   5684 H HH   . TYR   B 1 113 ? 37.294 -27.342 -2.317  1.00 17.42 ?  113 TYR   B HH   1 
ATOM   5685 N N    . GLU   B 1 114 ? 32.914 -19.309 -0.934  1.00 12.37 ?  114 GLU   B N    1 
ATOM   5686 C CA   . GLU   B 1 114 ? 32.234 -18.101 -1.392  1.00 12.22 ?  114 GLU   B CA   1 
ATOM   5687 C C    . GLU   B 1 114 ? 33.213 -16.978 -1.692  1.00 11.97 ?  114 GLU   B C    1 
ATOM   5688 O O    . GLU   B 1 114 ? 32.928 -16.119 -2.532  1.00 12.52 ?  114 GLU   B O    1 
ATOM   5689 C CB   . GLU   B 1 114 ? 31.175 -17.670 -0.376  1.00 12.81 ?  114 GLU   B CB   1 
ATOM   5690 C CG   . GLU   B 1 114 ? 29.944 -18.578 -0.445  1.00 12.97 ?  114 GLU   B CG   1 
ATOM   5691 C CD   . GLU   B 1 114 ? 28.924 -18.401 0.676   1.00 13.30 ?  114 GLU   B CD   1 
ATOM   5692 O OE1  . GLU   B 1 114 ? 29.220 -17.787 1.722   1.00 13.59 ?  114 GLU   B OE1  1 
ATOM   5693 O OE2  . GLU   B 1 114 ? 27.795 -18.940 0.516   1.00 14.21 -1 114 GLU   B OE2  1 
ATOM   5694 H H    . GLU   B 1 114 ? 32.655 -19.601 -0.161  1.00 14.99 ?  114 GLU   B H    1 
ATOM   5695 H HA   . GLU   B 1 114 ? 31.771 -18.300 -2.214  1.00 14.81 ?  114 GLU   B HA   1 
ATOM   5696 H HB2  . GLU   B 1 114 ? 31.541 -17.724 0.522   1.00 15.52 ?  114 GLU   B HB2  1 
ATOM   5697 H HB3  . GLU   B 1 114 ? 30.888 -16.764 -0.568  1.00 15.52 ?  114 GLU   B HB3  1 
ATOM   5698 H HG2  . GLU   B 1 114 ? 29.490 -18.416 -1.281  1.00 15.72 ?  114 GLU   B HG2  1 
ATOM   5699 H HG3  . GLU   B 1 114 ? 30.248 -19.503 -0.413  1.00 15.72 ?  114 GLU   B HG3  1 
ATOM   5700 N N    . ASN   B 1 115 ? 34.383 -16.973 -1.045  1.00 11.79 ?  115 ASN   B N    1 
ATOM   5701 C CA   . ASN   B 1 115 ? 35.366 -15.937 -1.340  1.00 11.98 ?  115 ASN   B CA   1 
ATOM   5702 C C    . ASN   B 1 115 ? 35.779 -15.947 -2.807  1.00 11.93 ?  115 ASN   B C    1 
ATOM   5703 O O    . ASN   B 1 115 ? 36.167 -14.904 -3.355  1.00 12.60 ?  115 ASN   B O    1 
ATOM   5704 C CB   . ASN   B 1 115 ? 36.604 -16.113 -0.454  1.00 12.91 ?  115 ASN   B CB   1 
ATOM   5705 C CG   . ASN   B 1 115 ? 36.331 -15.847 1.009   1.00 13.33 ?  115 ASN   B CG   1 
ATOM   5706 O OD1  . ASN   B 1 115 ? 36.308 -14.694 1.443   1.00 15.52 ?  115 ASN   B OD1  1 
ATOM   5707 N ND2  . ASN   B 1 115 ? 36.181 -16.912 1.794   1.00 13.23 ?  115 ASN   B ND2  1 
ATOM   5708 H H    . ASN   B 1 115 ? 34.624 -17.534 -0.435  1.00 14.30 ?  115 ASN   B H    1 
ATOM   5709 H HA   . ASN   B 1 115 ? 34.987 -15.064 -1.145  1.00 14.52 ?  115 ASN   B HA   1 
ATOM   5710 H HB2  . ASN   B 1 115 ? 36.925 -17.024 -0.540  1.00 15.64 ?  115 ASN   B HB2  1 
ATOM   5711 H HB3  . ASN   B 1 115 ? 37.291 -15.491 -0.739  1.00 15.64 ?  115 ASN   B HB3  1 
ATOM   5712 H HD21 . ASN   B 1 115 ? 36.033 -16.808 2.637   1.00 16.02 ?  115 ASN   B HD21 1 
ATOM   5713 H HD22 . ASN   B 1 115 ? 36.219 -17.704 1.462   1.00 16.02 ?  115 ASN   B HD22 1 
ATOM   5714 N N    . PHE   B 1 116 ? 35.766 -17.127 -3.442  1.00 11.82 ?  116 PHE   B N    1 
ATOM   5715 C CA   . PHE   B 1 116 ? 36.184 -17.221 -4.835  1.00 11.85 ?  116 PHE   B CA   1 
ATOM   5716 C C    . PHE   B 1 116 ? 35.283 -16.392 -5.745  1.00 11.57 ?  116 PHE   B C    1 
ATOM   5717 O O    . PHE   B 1 116 ? 35.716 -15.955 -6.815  1.00 12.30 ?  116 PHE   B O    1 
ATOM   5718 C CB   . PHE   B 1 116 ? 36.149 -18.672 -5.352  1.00 11.38 ?  116 PHE   B CB   1 
ATOM   5719 C CG   . PHE   B 1 116 ? 37.220 -19.624 -4.803  1.00 11.45 ?  116 PHE   B CG   1 
ATOM   5720 C CD1  . PHE   B 1 116 ? 37.876 -19.435 -3.594  1.00 12.06 ?  116 PHE   B CD1  1 
ATOM   5721 C CD2  . PHE   B 1 116 ? 37.532 -20.762 -5.546  1.00 11.84 ?  116 PHE   B CD2  1 
ATOM   5722 C CE1  . PHE   B 1 116 ? 38.807 -20.370 -3.141  1.00 12.66 ?  116 PHE   B CE1  1 
ATOM   5723 C CE2  . PHE   B 1 116 ? 38.458 -21.696 -5.097  1.00 12.16 ?  116 PHE   B CE2  1 
ATOM   5724 C CZ   . PHE   B 1 116 ? 39.099 -21.498 -3.903  1.00 12.13 ?  116 PHE   B CZ   1 
ATOM   5725 H H    . PHE   B 1 116 ? 35.505 -17.872 -3.096  1.00 14.33 ?  116 PHE   B H    1 
ATOM   5726 H HA   . PHE   B 1 116 ? 37.087 -16.893 -4.925  1.00 14.36 ?  116 PHE   B HA   1 
ATOM   5727 H HB2  . PHE   B 1 116 ? 35.277 -19.053 -5.132  1.00 13.80 ?  116 PHE   B HB2  1 
ATOM   5728 H HB3  . PHE   B 1 116 ? 36.243 -18.656 -6.320  1.00 13.80 ?  116 PHE   B HB3  1 
ATOM   5729 H HD1  . PHE   B 1 116 ? 37.674 -18.692 -3.076  1.00 14.62 ?  116 PHE   B HD1  1 
ATOM   5730 H HD2  . PHE   B 1 116 ? 37.088 -20.913 -6.354  1.00 14.36 ?  116 PHE   B HD2  1 
ATOM   5731 H HE1  . PHE   B 1 116 ? 39.249 -20.235 -2.336  1.00 15.34 ?  116 PHE   B HE1  1 
ATOM   5732 H HE2  . PHE   B 1 116 ? 38.654 -22.443 -5.614  1.00 14.73 ?  116 PHE   B HE2  1 
ATOM   5733 H HZ   . PHE   B 1 116 ? 39.734 -22.107 -3.606  1.00 14.71 ?  116 PHE   B HZ   1 
ATOM   5734 N N    . ASN   B 1 117 ? 34.015 -16.186 -5.358  1.00 12.21 ?  117 ASN   B N    1 
ATOM   5735 C CA   . ASN   B 1 117 ? 33.070 -15.481 -6.221  1.00 12.43 ?  117 ASN   B CA   1 
ATOM   5736 C C    . ASN   B 1 117 ? 33.380 -13.999 -6.373  1.00 12.27 ?  117 ASN   B C    1 
ATOM   5737 O O    . ASN   B 1 117 ? 32.794 -13.344 -7.238  1.00 13.47 ?  117 ASN   B O    1 
ATOM   5738 C CB   . ASN   B 1 117 ? 31.640 -15.703 -5.734  1.00 12.88 ?  117 ASN   B CB   1 
ATOM   5739 C CG   . ASN   B 1 117 ? 31.188 -17.117 -5.987  1.00 12.65 ?  117 ASN   B CG   1 
ATOM   5740 O OD1  . ASN   B 1 117 ? 31.547 -17.711 -7.010  1.00 13.99 ?  117 ASN   B OD1  1 
ATOM   5741 N ND2  . ASN   B 1 117 ? 30.452 -17.689 -5.047  1.00 12.87 ?  117 ASN   B ND2  1 
ATOM   5742 H H    . ASN   B 1 117 ? 33.686 -16.440 -4.603  1.00 14.80 ?  117 ASN   B H    1 
ATOM   5743 H HA   . ASN   B 1 117 ? 33.124 -15.876 -7.102  1.00 15.06 ?  117 ASN   B HA   1 
ATOM   5744 H HB2  . ASN   B 1 117 ? 31.592 -15.535 -4.775  1.00 15.61 ?  117 ASN   B HB2  1 
ATOM   5745 H HB3  . ASN   B 1 117 ? 31.040 -15.094 -6.201  1.00 15.61 ?  117 ASN   B HB3  1 
ATOM   5746 H HD21 . ASN   B 1 117 ? 30.173 -18.494 -5.150  1.00 15.59 ?  117 ASN   B HD21 1 
ATOM   5747 H HD22 . ASN   B 1 117 ? 30.230 -17.247 -4.339  1.00 15.59 ?  117 ASN   B HD22 1 
ATOM   5748 N N    . GLN   B 1 118 ? 34.309 -13.473 -5.594  1.00 12.47 ?  118 GLN   B N    1 
ATOM   5749 C CA   . GLN   B 1 118 ? 34.741 -12.088 -5.735  1.00 12.83 ?  118 GLN   B CA   1 
ATOM   5750 C C    . GLN   B 1 118 ? 35.811 -11.896 -6.806  1.00 13.12 ?  118 GLN   B C    1 
ATOM   5751 O O    . GLN   B 1 118 ? 36.284 -10.767 -6.983  1.00 14.54 ?  118 GLN   B O    1 
ATOM   5752 C CB   . GLN   B 1 118 ? 35.224 -11.562 -4.385  1.00 13.59 ?  118 GLN   B CB   1 
ATOM   5753 C CG   . GLN   B 1 118 ? 34.144 -11.589 -3.312  1.00 14.05 ?  118 GLN   B CG   1 
ATOM   5754 C CD   . GLN   B 1 118 ? 32.966 -10.683 -3.641  1.00 13.94 ?  118 GLN   B CD   1 
ATOM   5755 O OE1  . GLN   B 1 118 ? 33.146 -9.538  -4.082  1.00 14.54 ?  118 GLN   B OE1  1 
ATOM   5756 N NE2  . GLN   B 1 118 ? 31.753 -11.181 -3.425  1.00 14.58 ?  118 GLN   B NE2  1 
ATOM   5757 H H    . GLN   B 1 118 ? 34.724 -13.899 -4.971  1.00 15.12 ?  118 GLN   B H    1 
ATOM   5758 H HA   . GLN   B 1 118 ? 33.974 -11.556 -6.002  1.00 15.54 ?  118 GLN   B HA   1 
ATOM   5759 H HB2  . GLN   B 1 118 ? 35.963 -12.107 -4.079  1.00 16.45 ?  118 GLN   B HB2  1 
ATOM   5760 H HB3  . GLN   B 1 118 ? 35.512 -10.640 -4.489  1.00 16.45 ?  118 GLN   B HB3  1 
ATOM   5761 H HG2  . GLN   B 1 118 ? 33.813 -12.499 -3.224  1.00 17.01 ?  118 GLN   B HG2  1 
ATOM   5762 H HG3  . GLN   B 1 118 ? 34.528 -11.294 -2.472  1.00 17.01 ?  118 GLN   B HG3  1 
ATOM   5763 H HE21 . GLN   B 1 118 ? 31.665 -11.979 -3.113  1.00 17.65 ?  118 GLN   B HE21 1 
ATOM   5764 H HE22 . GLN   B 1 118 ? 31.063 -10.706 -3.598  1.00 17.65 ?  118 GLN   B HE22 1 
ATOM   5765 N N    . HIS   B 1 119 ? 36.179 -12.956 -7.537  1.00 12.68 ?  119 HIS   B N    1 
ATOM   5766 C CA   . HIS   B 1 119 ? 37.220 -12.902 -8.559  1.00 12.85 ?  119 HIS   B CA   1 
ATOM   5767 C C    . HIS   B 1 119 ? 36.741 -13.634 -9.798  1.00 12.58 ?  119 HIS   B C    1 
ATOM   5768 O O    . HIS   B 1 119 ? 36.236 -14.752 -9.694  1.00 13.54 ?  119 HIS   B O    1 
ATOM   5769 C CB   . HIS   B 1 119 ? 38.505 -13.530 -8.020  1.00 13.58 ?  119 HIS   B CB   1 
ATOM   5770 C CG   . HIS   B 1 119 ? 38.981 -12.842 -6.788  1.00 14.62 ?  119 HIS   B CG   1 
ATOM   5771 N ND1  . HIS   B 1 119 ? 39.763 -11.707 -6.829  1.00 16.45 ?  119 HIS   B ND1  1 
ATOM   5772 C CD2  . HIS   B 1 119 ? 38.689 -13.055 -5.485  1.00 15.94 ?  119 HIS   B CD2  1 
ATOM   5773 C CE1  . HIS   B 1 119 ? 39.967 -11.278 -5.597  1.00 17.66 ?  119 HIS   B CE1  1 
ATOM   5774 N NE2  . HIS   B 1 119 ? 39.327 -12.077 -4.763  1.00 17.65 ?  119 HIS   B NE2  1 
ATOM   5775 H H    . HIS   B 1 119 ? 35.823 -13.738 -7.461  1.00 15.36 ?  119 HIS   B H    1 
ATOM   5776 H HA   . HIS   B 1 119 ? 37.398 -11.975 -8.795  1.00 15.57 ?  119 HIS   B HA   1 
ATOM   5777 H HB2  . HIS   B 1 119 ? 38.341 -14.459 -7.810  1.00 16.44 ?  119 HIS   B HB2  1 
ATOM   5778 H HB3  . HIS   B 1 119 ? 39.199 -13.457 -8.699  1.00 16.44 ?  119 HIS   B HB3  1 
ATOM   5779 H HD2  . HIS   B 1 119 ? 38.170 -13.746 -5.144  1.00 19.27 ?  119 HIS   B HD2  1 
ATOM   5780 H HE1  . HIS   B 1 119 ? 40.492 -10.549 -5.353  1.00 21.34 ?  119 HIS   B HE1  1 
ATOM   5781 H HE2  . HIS   B 1 119 ? 39.329 -12.011 -3.906  1.00 21.33 ?  119 HIS   B HE2  1 
ATOM   5782 N N    . GLU   B 1 120 ? 36.892 -13.016 -10.970 1.00 13.37 ?  120 GLU   B N    1 
ATOM   5783 C CA   . GLU   B 1 120 ? 36.304 -13.600 -12.171 1.00 14.75 ?  120 GLU   B CA   1 
ATOM   5784 C C    . GLU   B 1 120 ? 36.979 -14.902 -12.586 1.00 13.81 ?  120 GLU   B C    1 
ATOM   5785 O O    . GLU   B 1 120 ? 36.313 -15.769 -13.161 1.00 13.84 ?  120 GLU   B O    1 
ATOM   5786 C CB   . GLU   B 1 120 ? 36.305 -12.594 -13.319 1.00 19.23 ?  120 GLU   B CB   1 
ATOM   5787 C CG   . GLU   B 1 120 ? 35.389 -11.410 -13.066 1.00 25.97 ?  120 GLU   B CG   1 
ATOM   5788 C CD   . GLU   B 1 120 ? 35.236 -10.507 -14.274 1.00 32.32 ?  120 GLU   B CD   1 
ATOM   5789 O OE1  . GLU   B 1 120 ? 36.213 -10.362 -15.040 1.00 34.57 ?  120 GLU   B OE1  1 
ATOM   5790 O OE2  . GLU   B 1 120 ? 34.136 -9.943  -14.452 1.00 35.19 -1 120 GLU   B OE2  1 
ATOM   5791 H H    . GLU   B 1 120 ? 37.320 -12.275 -11.095 1.00 16.20 ?  120 GLU   B H    1 
ATOM   5792 H HA   . GLU   B 1 120 ? 35.385 -13.816 -11.978 1.00 17.85 ?  120 GLU   B HA   1 
ATOM   5793 H HB2  . GLU   B 1 120 ? 37.201 -12.256 -13.451 1.00 23.22 ?  120 GLU   B HB2  1 
ATOM   5794 H HB3  . GLU   B 1 120 ? 35.996 -13.040 -14.127 1.00 23.22 ?  120 GLU   B HB3  1 
ATOM   5795 H HG2  . GLU   B 1 120 ? 34.506 -11.736 -12.824 1.00 31.32 ?  120 GLU   B HG2  1 
ATOM   5796 H HG3  . GLU   B 1 120 ? 35.754 -10.879 -12.341 1.00 31.32 ?  120 GLU   B HG3  1 
ATOM   5797 N N    . VAL   B 1 121 ? 38.281 -15.050 -12.324 1.00 13.33 ?  121 VAL   B N    1 
ATOM   5798 C CA   . VAL   B 1 121 ? 39.031 -16.255 -12.675 1.00 13.23 ?  121 VAL   B CA   1 
ATOM   5799 C C    . VAL   B 1 121 ? 40.144 -16.458 -11.651 1.00 12.82 ?  121 VAL   B C    1 
ATOM   5800 O O    . VAL   B 1 121 ? 40.821 -15.501 -11.258 1.00 13.61 ?  121 VAL   B O    1 
ATOM   5801 C CB   . VAL   B 1 121 ? 39.550 -16.208 -14.133 1.00 15.16 ?  121 VAL   B CB   1 
ATOM   5802 C CG1  . VAL   B 1 121 ? 40.419 -14.978 -14.387 1.00 16.62 ?  121 VAL   B CG1  1 
ATOM   5803 C CG2  . VAL   B 1 121 ? 40.290 -17.490 -14.485 1.00 16.77 ?  121 VAL   B CG2  1 
ATOM   5804 H H    . VAL   B 1 121 ? 38.770 -14.450 -11.939 1.00 16.15 ?  121 VAL   B H    1 
ATOM   5805 H HA   . VAL   B 1 121 ? 38.425 -17.010 -12.614 1.00 16.02 ?  121 VAL   B HA   1 
ATOM   5806 H HB   . VAL   B 1 121 ? 38.785 -16.147 -14.732 1.00 18.34 ?  121 VAL   B HB   1 
ATOM   5807 H HG11 . VAL   B 1 121 ? 40.724 -14.992 -15.308 1.00 20.09 ?  121 VAL   B HG11 1 
ATOM   5808 H HG12 . VAL   B 1 121 ? 39.891 -14.181 -14.226 1.00 20.09 ?  121 VAL   B HG12 1 
ATOM   5809 H HG13 . VAL   B 1 121 ? 41.178 -15.002 -13.786 1.00 20.09 ?  121 VAL   B HG13 1 
ATOM   5810 H HG21 . VAL   B 1 121 ? 40.493 -17.490 -15.435 1.00 20.27 ?  121 VAL   B HG21 1 
ATOM   5811 H HG22 . VAL   B 1 121 ? 41.117 -17.528 -13.976 1.00 20.27 ?  121 VAL   B HG22 1 
ATOM   5812 H HG23 . VAL   B 1 121 ? 39.731 -18.250 -14.267 1.00 20.27 ?  121 VAL   B HG23 1 
ATOM   5813 N N    . LEU   B 1 122 ? 40.331 -17.715 -11.219 1.00 12.39 ?  122 LEU   B N    1 
ATOM   5814 C CA   . LEU   B 1 122 ? 41.308 -18.073 -10.193 1.00 11.58 ?  122 LEU   B CA   1 
ATOM   5815 C C    . LEU   B 1 122 ? 41.958 -19.413 -10.513 1.00 11.55 ?  122 LEU   B C    1 
ATOM   5816 O O    . LEU   B 1 122 ? 41.299 -20.330 -11.019 1.00 12.93 ?  122 LEU   B O    1 
ATOM   5817 C CB   . LEU   B 1 122 ? 40.652 -18.294 -8.818  1.00 13.72 ?  122 LEU   B CB   1 
ATOM   5818 C CG   . LEU   B 1 122 ? 39.629 -17.272 -8.321  1.00 14.17 ?  122 LEU   B CG   1 
ATOM   5819 C CD1  . LEU   B 1 122 ? 38.222 -17.619 -8.795  1.00 15.17 ?  122 LEU   B CD1  1 
ATOM   5820 C CD2  . LEU   B 1 122 ? 39.682 -17.163 -6.808  1.00 13.57 ?  122 LEU   B CD2  1 
ATOM   5821 H H    . LEU   B 1 122 ? 39.892 -18.396 -11.517 1.00 15.02 ?  122 LEU   B H    1 
ATOM   5822 H HA   . LEU   B 1 122 ? 41.991 -17.384 -10.118 1.00 14.05 ?  122 LEU   B HA   1 
ATOM   5823 H HB2  . LEU   B 1 122 ? 40.194 -19.149 -8.845  1.00 16.62 ?  122 LEU   B HB2  1 
ATOM   5824 H HB3  . LEU   B 1 122 ? 41.354 -18.331 -8.155  1.00 16.62 ?  122 LEU   B HB3  1 
ATOM   5825 H HG   . LEU   B 1 122 ? 39.858 -16.400 -8.685  1.00 17.15 ?  122 LEU   B HG   1 
ATOM   5826 H HD11 . LEU   B 1 122 ? 37.602 -16.962 -8.438  1.00 18.35 ?  122 LEU   B HD11 1 
ATOM   5827 H HD12 . LEU   B 1 122 ? 38.203 -17.593 -9.765  1.00 18.35 ?  122 LEU   B HD12 1 
ATOM   5828 H HD13 . LEU   B 1 122 ? 37.992 -18.501 -8.478  1.00 18.35 ?  122 LEU   B HD13 1 
ATOM   5829 H HD21 . LEU   B 1 122 ? 39.010 -16.531 -6.510  1.00 16.43 ?  122 LEU   B HD21 1 
ATOM   5830 H HD22 . LEU   B 1 122 ? 39.514 -18.035 -6.421  1.00 16.43 ?  122 LEU   B HD22 1 
ATOM   5831 H HD23 . LEU   B 1 122 ? 40.566 -16.850 -6.544  1.00 16.43 ?  122 LEU   B HD23 1 
ATOM   5832 N N    . LEU   B 1 123 ? 43.247 -19.524 -10.158 1.00 11.43 ?  123 LEU   B N    1 
ATOM   5833 C CA   . LEU   B 1 123 ? 43.960 -20.794 -10.044 1.00 12.04 ?  123 LEU   B CA   1 
ATOM   5834 C C    . LEU   B 1 123 ? 43.934 -21.182 -8.572  1.00 11.39 ?  123 LEU   B C    1 
ATOM   5835 O O    . LEU   B 1 123 ? 44.282 -20.359 -7.720  1.00 11.88 ?  123 LEU   B O    1 
ATOM   5836 C CB   . LEU   B 1 123 ? 45.410 -20.599 -10.500 1.00 12.41 ?  123 LEU   B CB   1 
ATOM   5837 C CG   . LEU   B 1 123 ? 46.355 -21.780 -10.262 1.00 12.91 ?  123 LEU   B CG   1 
ATOM   5838 C CD1  . LEU   B 1 123 ? 45.918 -23.026 -11.037 1.00 13.40 ?  123 LEU   B CD1  1 
ATOM   5839 C CD2  . LEU   B 1 123 ? 47.789 -21.393 -10.624 1.00 13.67 ?  123 LEU   B CD2  1 
ATOM   5840 H H    . LEU   B 1 123 ? 43.742 -18.845 -9.961  1.00 13.87 ?  123 LEU   B H    1 
ATOM   5841 H HA   . LEU   B 1 123 ? 43.525 -21.480 -10.578 1.00 14.59 ?  123 LEU   B HA   1 
ATOM   5842 H HB2  . LEU   B 1 123 ? 45.405 -20.423 -11.454 1.00 15.04 ?  123 LEU   B HB2  1 
ATOM   5843 H HB3  . LEU   B 1 123 ? 45.776 -19.838 -10.031 1.00 15.04 ?  123 LEU   B HB3  1 
ATOM   5844 H HG   . LEU   B 1 123 ? 46.341 -22.009 -9.318  1.00 15.64 ?  123 LEU   B HG   1 
ATOM   5845 H HD11 . LEU   B 1 123 ? 46.556 -23.739 -10.875 1.00 16.22 ?  123 LEU   B HD11 1 
ATOM   5846 H HD12 . LEU   B 1 123 ? 45.036 -23.299 -10.731 1.00 16.22 ?  123 LEU   B HD12 1 
ATOM   5847 H HD13 . LEU   B 1 123 ? 45.888 -22.816 -11.982 1.00 16.22 ?  123 LEU   B HD13 1 
ATOM   5848 H HD21 . LEU   B 1 123 ? 48.370 -22.151 -10.466 1.00 16.55 ?  123 LEU   B HD21 1 
ATOM   5849 H HD22 . LEU   B 1 123 ? 47.817 -21.138 -11.559 1.00 16.55 ?  123 LEU   B HD22 1 
ATOM   5850 H HD23 . LEU   B 1 123 ? 48.058 -20.644 -10.068 1.00 16.55 ?  123 LEU   B HD23 1 
ATOM   5851 N N    . ALA   B 1 124 ? 43.494 -22.409 -8.263  1.00 11.60 ?  124 ALA   B N    1 
ATOM   5852 C CA   . ALA   B 1 124 ? 43.244 -22.745 -6.868  1.00 11.81 ?  124 ALA   B CA   1 
ATOM   5853 C C    . ALA   B 1 124 ? 43.514 -24.205 -6.536  1.00 11.30 ?  124 ALA   B C    1 
ATOM   5854 O O    . ALA   B 1 124 ? 43.382 -25.082 -7.402  1.00 12.19 ?  124 ALA   B O    1 
ATOM   5855 C CB   . ALA   B 1 124 ? 41.789 -22.427 -6.494  1.00 12.37 ?  124 ALA   B CB   1 
ATOM   5856 H H    . ALA   B 1 124 ? 43.322 -23.043 -8.827  1.00 14.07 ?  124 ALA   B H    1 
ATOM   5857 H HA   . ALA   B 1 124 ? 43.817 -22.193 -6.320  1.00 14.32 ?  124 ALA   B HA   1 
ATOM   5858 H HB1  . ALA   B 1 124 ? 41.640 -22.656 -5.563  1.00 14.99 ?  124 ALA   B HB1  1 
ATOM   5859 H HB2  . ALA   B 1 124 ? 41.627 -21.480 -6.631  1.00 14.99 ?  124 ALA   B HB2  1 
ATOM   5860 H HB3  . ALA   B 1 124 ? 41.194 -22.947 -7.060  1.00 14.99 ?  124 ALA   B HB3  1 
ATOM   5861 N N    . PRO   B 1 125 ? 43.820 -24.493 -5.275  1.00 11.60 ?  125 PRO   B N    1 
ATOM   5862 C CA   . PRO   B 1 125 ? 43.754 -25.860 -4.754  1.00 12.62 ?  125 PRO   B CA   1 
ATOM   5863 C C    . PRO   B 1 125 ? 42.352 -26.133 -4.208  1.00 12.61 ?  125 PRO   B C    1 
ATOM   5864 O O    . PRO   B 1 125 ? 41.551 -25.222 -4.007  1.00 13.24 ?  125 PRO   B O    1 
ATOM   5865 C CB   . PRO   B 1 125 ? 44.743 -25.793 -3.585  1.00 13.65 ?  125 PRO   B CB   1 
ATOM   5866 C CG   . PRO   B 1 125 ? 44.500 -24.396 -3.015  1.00 13.76 ?  125 PRO   B CG   1 
ATOM   5867 C CD   . PRO   B 1 125 ? 44.140 -23.523 -4.212  1.00 12.40 ?  125 PRO   B CD   1 
ATOM   5868 H HA   . PRO   B 1 125 ? 44.029 -26.526 -5.404  1.00 15.29 ?  125 PRO   B HA   1 
ATOM   5869 H HB2  . PRO   B 1 125 ? 44.535 -26.473 -2.925  1.00 16.53 ?  125 PRO   B HB2  1 
ATOM   5870 H HB3  . PRO   B 1 125 ? 45.655 -25.881 -3.904  1.00 16.53 ?  125 PRO   B HB3  1 
ATOM   5871 H HG2  . PRO   B 1 125 ? 43.765 -24.416 -2.380  1.00 16.66 ?  125 PRO   B HG2  1 
ATOM   5872 H HG3  . PRO   B 1 125 ? 45.309 -24.066 -2.581  1.00 16.66 ?  125 PRO   B HG3  1 
ATOM   5873 H HD2  . PRO   B 1 125 ? 43.371 -22.968 -4.016  1.00 15.03 ?  125 PRO   B HD2  1 
ATOM   5874 H HD3  . PRO   B 1 125 ? 44.908 -22.974 -4.473  1.00 15.03 ?  125 PRO   B HD3  1 
ATOM   5875 N N    . LEU   B 1 126 ? 42.079 -27.412 -3.932  1.00 13.30 ?  126 LEU   B N    1 
ATOM   5876 C CA   . LEU   B 1 126 ? 40.860 -27.785 -3.215  1.00 13.70 ?  126 LEU   B CA   1 
ATOM   5877 C C    . LEU   B 1 126 ? 40.972 -27.388 -1.749  1.00 13.69 ?  126 LEU   B C    1 
ATOM   5878 O O    . LEU   B 1 126 ? 41.860 -27.858 -1.030  1.00 15.60 ?  126 LEU   B O    1 
ATOM   5879 C CB   . LEU   B 1 126 ? 40.598 -29.283 -3.330  1.00 15.21 ?  126 LEU   B CB   1 
ATOM   5880 C CG   . LEU   B 1 126 ? 40.071 -29.766 -4.680  1.00 16.12 ?  126 LEU   B CG   1 
ATOM   5881 C CD1  . LEU   B 1 126 ? 40.103 -31.286 -4.769  1.00 18.01 ?  126 LEU   B CD1  1 
ATOM   5882 C CD2  . LEU   B 1 126 ? 38.658 -29.239 -4.941  1.00 16.62 ?  126 LEU   B CD2  1 
ATOM   5883 H H    . LEU   B 1 126 ? 42.585 -28.079 -4.139  1.00 16.10 ?  126 LEU   B H    1 
ATOM   5884 H HA   . LEU   B 1 126 ? 40.109 -27.310 -3.603  1.00 16.59 ?  126 LEU   B HA   1 
ATOM   5885 H HB2  . LEU   B 1 126 ? 41.422 -29.754 -3.157  1.00 18.39 ?  126 LEU   B HB2  1 
ATOM   5886 H HB3  . LEU   B 1 126 ? 39.936 -29.527 -2.659  1.00 18.39 ?  126 LEU   B HB3  1 
ATOM   5887 H HG   . LEU   B 1 126 ? 40.644 -29.411 -5.379  1.00 19.49 ?  126 LEU   B HG   1 
ATOM   5888 H HD11 . LEU   B 1 126 ? 39.761 -31.557 -5.636  1.00 21.76 ?  126 LEU   B HD11 1 
ATOM   5889 H HD12 . LEU   B 1 126 ? 41.014 -31.587 -4.660  1.00 21.76 ?  126 LEU   B HD12 1 
ATOM   5890 H HD13 . LEU   B 1 126 ? 39.542 -31.652 -4.066  1.00 21.76 ?  126 LEU   B HD13 1 
ATOM   5891 H HD21 . LEU   B 1 126 ? 38.307 -29.658 -5.743  1.00 20.09 ?  126 LEU   B HD21 1 
ATOM   5892 H HD22 . LEU   B 1 126 ? 38.094 -29.455 -4.182  1.00 20.09 ?  126 LEU   B HD22 1 
ATOM   5893 H HD23 . LEU   B 1 126 ? 38.691 -28.275 -5.063  1.00 20.09 ?  126 LEU   B HD23 1 
ATOM   5894 N N    . LEU   B 1 127 ? 40.045 -26.556 -1.290  1.00 13.36 ?  127 LEU   B N    1 
ATOM   5895 C CA   . LEU   B 1 127 ? 40.099 -26.063 0.075   1.00 13.54 ?  127 LEU   B CA   1 
ATOM   5896 C C    . LEU   B 1 127 ? 39.817 -27.180 1.071   1.00 13.35 ?  127 LEU   B C    1 
ATOM   5897 O O    . LEU   B 1 127 ? 38.994 -28.070 0.841   1.00 13.74 ?  127 LEU   B O    1 
ATOM   5898 C CB   . LEU   B 1 127 ? 39.088 -24.933 0.279   1.00 14.04 ?  127 LEU   B CB   1 
ATOM   5899 C CG   . LEU   B 1 127 ? 39.261 -23.662 -0.558  1.00 14.73 ?  127 LEU   B CG   1 
ATOM   5900 C CD1  . LEU   B 1 127 ? 38.136 -22.693 -0.235  1.00 15.20 ?  127 LEU   B CD1  1 
ATOM   5901 C CD2  . LEU   B 1 127 ? 40.621 -23.013 -0.333  1.00 15.30 ?  127 LEU   B CD2  1 
ATOM   5902 H H    . LEU   B 1 127 ? 39.373 -26.254 -1.749  1.00 16.18 ?  127 LEU   B H    1 
ATOM   5903 H HA   . LEU   B 1 127 ? 40.989 -25.706 0.248   1.00 16.39 ?  127 LEU   B HA   1 
ATOM   5904 H HB2  . LEU   B 1 127 ? 38.205 -25.283 0.085   1.00 17.00 ?  127 LEU   B HB2  1 
ATOM   5905 H HB3  . LEU   B 1 127 ? 39.123 -24.664 1.212   1.00 17.00 ?  127 LEU   B HB3  1 
ATOM   5906 H HG   . LEU   B 1 127 ? 39.183 -23.887 -1.495  1.00 17.83 ?  127 LEU   B HG   1 
ATOM   5907 H HD11 . LEU   B 1 127 ? 38.250 -21.883 -0.763  1.00 18.38 ?  127 LEU   B HD11 1 
ATOM   5908 H HD12 . LEU   B 1 127 ? 37.284 -23.104 -0.447  1.00 18.38 ?  127 LEU   B HD12 1 
ATOM   5909 H HD13 . LEU   B 1 127 ? 38.167 -22.469 0.712   1.00 18.38 ?  127 LEU   B HD13 1 
ATOM   5910 H HD21 . LEU   B 1 127 ? 40.657 -22.172 -0.818  1.00 18.51 ?  127 LEU   B HD21 1 
ATOM   5911 H HD22 . LEU   B 1 127 ? 40.743 -22.850 0.617   1.00 18.51 ?  127 LEU   B HD22 1 
ATOM   5912 H HD23 . LEU   B 1 127 ? 41.310 -23.611 -0.657  1.00 18.51 ?  127 LEU   B HD23 1 
ATOM   5913 N N    . SER   B 1 128 ? 40.499 -27.097 2.205   1.00 13.68 ?  128 SER   B N    1 
ATOM   5914 C CA   . SER   B 1 128 ? 40.384 -28.015 3.330   1.00 13.95 ?  128 SER   B CA   1 
ATOM   5915 C C    . SER   B 1 128 ? 40.879 -29.426 3.018   1.00 15.01 ?  128 SER   B C    1 
ATOM   5916 O O    . SER   B 1 128 ? 40.782 -30.303 3.880   1.00 16.43 ?  128 SER   B O    1 
ATOM   5917 C CB   . SER   B 1 128 ? 38.983 -28.027 3.962   1.00 14.48 ?  128 SER   B CB   1 
ATOM   5918 O OG   . SER   B 1 128 ? 38.675 -26.747 4.518   1.00 15.05 ?  128 SER   B OG   1 
ATOM   5919 H H    . SER   B 1 128 ? 41.064 -26.467 2.357   1.00 16.57 ?  128 SER   B H    1 
ATOM   5920 H HA   . SER   B 1 128 ? 40.972 -27.678 4.014   1.00 16.88 ?  128 SER   B HA   1 
ATOM   5921 H HB2  . SER   B 1 128 ? 38.323 -28.253 3.287   1.00 17.53 ?  128 SER   B HB2  1 
ATOM   5922 H HB3  . SER   B 1 128 ? 38.965 -28.701 4.673   1.00 17.53 ?  128 SER   B HB3  1 
ATOM   5923 H HG   . SER   B 1 128 ? 39.249 -26.557 5.106   1.00 18.21 ?  128 SER   B HG   1 
ATOM   5924 N N    . ALA   B 1 129 ? 41.452 -29.661 1.835   1.00 16.09 ?  129 ALA   B N    1 
ATOM   5925 C CA   . ALA   B 1 129 ? 41.996 -30.966 1.493   1.00 17.61 ?  129 ALA   B CA   1 
ATOM   5926 C C    . ALA   B 1 129 ? 43.395 -31.135 2.078   1.00 16.45 ?  129 ALA   B C    1 
ATOM   5927 O O    . ALA   B 1 129 ? 43.952 -30.230 2.716   1.00 16.14 ?  129 ALA   B O    1 
ATOM   5928 C CB   . ALA   B 1 129 ? 42.029 -31.148 -0.023  1.00 19.90 ?  129 ALA   B CB   1 
ATOM   5929 H H    . ALA   B 1 129 ? 41.536 -29.073 1.207   1.00 19.46 ?  129 ALA   B H    1 
ATOM   5930 H HA   . ALA   B 1 129 ? 41.426 -31.653 1.866   1.00 21.28 ?  129 ALA   B HA   1 
ATOM   5931 H HB1  . ALA   B 1 129 ? 42.382 -32.031 -0.227  1.00 24.03 ?  129 ALA   B HB1  1 
ATOM   5932 H HB2  . ALA   B 1 129 ? 41.129 -31.065 -0.372  1.00 24.03 ?  129 ALA   B HB2  1 
ATOM   5933 H HB3  . ALA   B 1 129 ? 42.601 -30.468 -0.413  1.00 24.03 ?  129 ALA   B HB3  1 
ATOM   5934 N N    . GLY   B 1 130 ? 43.969 -32.314 1.837   1.00 16.37 ?  130 GLY   B N    1 
ATOM   5935 C CA   . GLY   B 1 130 ? 45.360 -32.544 2.181   1.00 17.00 ?  130 GLY   B CA   1 
ATOM   5936 C C    . GLY   B 1 130 ? 45.571 -32.447 3.673   1.00 16.76 ?  130 GLY   B C    1 
ATOM   5937 O O    . GLY   B 1 130 ? 44.867 -33.083 4.471   1.00 17.35 ?  130 GLY   B O    1 
ATOM   5938 H H    . GLY   B 1 130 ? 43.580 -32.986 1.469   1.00 19.79 ?  130 GLY   B H    1 
ATOM   5939 H HA2  . GLY   B 1 130 ? 45.631 -33.429 1.885   1.00 20.55 ?  130 GLY   B HA2  1 
ATOM   5940 H HA3  . GLY   B 1 130 ? 45.924 -31.887 1.741   1.00 20.55 ?  130 GLY   B HA3  1 
ATOM   5941 N N    . ILE   B 1 131 ? 46.542 -31.614 4.063   1.00 17.10 ?  131 ILE   B N    1 
ATOM   5942 C CA   . ILE   B 1 131 ? 46.900 -31.486 5.469   1.00 18.02 ?  131 ILE   B CA   1 
ATOM   5943 C C    . ILE   B 1 131 ? 45.782 -30.893 6.306   1.00 17.24 ?  131 ILE   B C    1 
ATOM   5944 O O    . ILE   B 1 131 ? 45.858 -30.952 7.538   1.00 18.81 ?  131 ILE   B O    1 
ATOM   5945 C CB   . ILE   B 1 131 ? 48.220 -30.706 5.673   1.00 20.05 ?  131 ILE   B CB   1 
ATOM   5946 C CG1  . ILE   B 1 131 ? 48.051 -29.222 5.309   1.00 20.79 ?  131 ILE   B CG1  1 
ATOM   5947 C CG2  . ILE   B 1 131 ? 49.351 -31.341 4.863   1.00 21.30 ?  131 ILE   B CG2  1 
ATOM   5948 C CD1  . ILE   B 1 131 ? 49.261 -28.361 5.649   1.00 21.67 ?  131 ILE   B CD1  1 
ATOM   5949 H H    . ILE   B 1 131 ? 47.003 -31.116 3.534   1.00 20.66 ?  131 ILE   B H    1 
ATOM   5950 H HA   . ILE   B 1 131 ? 47.049 -32.378 5.812   1.00 21.77 ?  131 ILE   B HA   1 
ATOM   5951 H HB   . ILE   B 1 131 ? 48.452 -30.759 6.613   1.00 24.21 ?  131 ILE   B HB   1 
ATOM   5952 H HG12 . ILE   B 1 131 ? 47.892 -29.152 4.356   1.00 25.09 ?  131 ILE   B HG12 1 
ATOM   5953 H HG13 . ILE   B 1 131 ? 47.292 -28.856 5.794   1.00 25.09 ?  131 ILE   B HG13 1 
ATOM   5954 H HG21 . ILE   B 1 131 ? 50.186 -30.926 5.119   1.00 25.71 ?  131 ILE   B HG21 1 
ATOM   5955 H HG22 . ILE   B 1 131 ? 49.372 -32.288 5.053   1.00 25.71 ?  131 ILE   B HG22 1 
ATOM   5956 H HG23 . ILE   B 1 131 ? 49.177 -31.192 3.921   1.00 25.71 ?  131 ILE   B HG23 1 
ATOM   5957 H HD11 . ILE   B 1 131 ? 49.040 -27.431 5.478   1.00 26.16 ?  131 ILE   B HD11 1 
ATOM   5958 H HD12 . ILE   B 1 131 ? 49.480 -28.482 6.586   1.00 26.16 ?  131 ILE   B HD12 1 
ATOM   5959 H HD13 . ILE   B 1 131 ? 50.006 -28.633 5.094   1.00 26.16 ?  131 ILE   B HD13 1 
ATOM   5960 N N    . PHE   B 1 132 ? 44.751 -30.319 5.676   1.00 16.04 ?  132 PHE   B N    1 
ATOM   5961 C CA   . PHE   B 1 132 ? 43.594 -29.812 6.409   1.00 16.52 ?  132 PHE   B CA   1 
ATOM   5962 C C    . PHE   B 1 132 ? 42.569 -30.899 6.740   1.00 17.99 ?  132 PHE   B C    1 
ATOM   5963 O O    . PHE   B 1 132 ? 41.665 -30.642 7.540   1.00 19.82 ?  132 PHE   B O    1 
ATOM   5964 C CB   . PHE   B 1 132 ? 42.913 -28.675 5.633   1.00 15.59 ?  132 PHE   B CB   1 
ATOM   5965 C CG   . PHE   B 1 132 ? 43.613 -27.330 5.744   1.00 15.92 ?  132 PHE   B CG   1 
ATOM   5966 C CD1  . PHE   B 1 132 ? 44.907 -27.145 5.273   1.00 17.40 ?  132 PHE   B CD1  1 
ATOM   5967 C CD2  . PHE   B 1 132 ? 42.939 -26.236 6.273   1.00 15.06 ?  132 PHE   B CD2  1 
ATOM   5968 C CE1  . PHE   B 1 132 ? 45.526 -25.903 5.367   1.00 17.72 ?  132 PHE   B CE1  1 
ATOM   5969 C CE2  . PHE   B 1 132 ? 43.548 -24.992 6.363   1.00 15.91 ?  132 PHE   B CE2  1 
ATOM   5970 C CZ   . PHE   B 1 132 ? 44.840 -24.828 5.910   1.00 17.00 ?  132 PHE   B CZ   1 
ATOM   5971 H H    . PHE   B 1 132 ? 44.700 -30.207 4.823   1.00 19.39 ?  132 PHE   B H    1 
ATOM   5972 H HA   . PHE   B 1 132 ? 43.907 -29.438 7.247   1.00 19.97 ?  132 PHE   B HA   1 
ATOM   5973 H HB2  . PHE   B 1 132 ? 42.890 -28.912 4.695   1.00 18.86 ?  132 PHE   B HB2  1 
ATOM   5974 H HB3  . PHE   B 1 132 ? 42.010 -28.564 5.969   1.00 18.86 ?  132 PHE   B HB3  1 
ATOM   5975 H HD1  . PHE   B 1 132 ? 45.374 -27.866 4.912   1.00 21.03 ?  132 PHE   B HD1  1 
ATOM   5976 H HD2  . PHE   B 1 132 ? 42.068 -26.344 6.580   1.00 18.23 ?  132 PHE   B HD2  1 
ATOM   5977 H HE1  . PHE   B 1 132 ? 46.398 -25.790 5.062   1.00 21.42 ?  132 PHE   B HE1  1 
ATOM   5978 H HE2  . PHE   B 1 132 ? 43.086 -24.271 6.730   1.00 19.24 ?  132 PHE   B HE2  1 
ATOM   5979 H HZ   . PHE   B 1 132 ? 45.252 -23.990 5.974   1.00 20.55 ?  132 PHE   B HZ   1 
ATOM   5980 N N    . GLY   B 1 133 ? 42.669 -32.095 6.143   1.00 17.48 ?  133 GLY   B N    1 
ATOM   5981 C CA   . GLY   B 1 133 ? 41.956 -33.263 6.637   1.00 18.20 ?  133 GLY   B CA   1 
ATOM   5982 C C    . GLY   B 1 133 ? 40.559 -33.525 6.102   1.00 18.45 ?  133 GLY   B C    1 
ATOM   5983 O O    . GLY   B 1 133 ? 39.967 -34.541 6.479   1.00 20.77 ?  133 GLY   B O    1 
ATOM   5984 H H    . GLY   B 1 133 ? 43.152 -32.244 5.446   1.00 21.13 ?  133 GLY   B H    1 
ATOM   5985 H HA2  . GLY   B 1 133 ? 42.490 -34.045 6.437   1.00 21.99 ?  133 GLY   B HA2  1 
ATOM   5986 H HA3  . GLY   B 1 133 ? 41.895 -33.188 7.602   1.00 21.99 ?  133 GLY   B HA3  1 
ATOM   5987 N N    . ALA   B 1 134 ? 40.006 -32.666 5.252   1.00 17.75 ?  134 ALA   B N    1 
ATOM   5988 C CA   . ALA   B 1 134 ? 38.678 -32.941 4.719   1.00 18.07 ?  134 ALA   B CA   1 
ATOM   5989 C C    . ALA   B 1 134 ? 38.764 -33.926 3.556   1.00 17.82 ?  134 ALA   B C    1 
ATOM   5990 O O    . ALA   B 1 134 ? 39.814 -34.102 2.933   1.00 19.06 ?  134 ALA   B O    1 
ATOM   5991 C CB   . ALA   B 1 134 ? 38.003 -31.648 4.260   1.00 18.52 ?  134 ALA   B CB   1 
ATOM   5992 H H    . ALA   B 1 134 ? 40.367 -31.932 4.978   1.00 21.44 ?  134 ALA   B H    1 
ATOM   5993 H HA   . ALA   B 1 134 ? 38.131 -33.335 5.417   1.00 21.83 ?  134 ALA   B HA   1 
ATOM   5994 H HB1  . ALA   B 1 134 ? 37.116 -31.859 3.929   1.00 22.37 ?  134 ALA   B HB1  1 
ATOM   5995 H HB2  . ALA   B 1 134 ? 37.940 -31.040 5.012   1.00 22.37 ?  134 ALA   B HB2  1 
ATOM   5996 H HB3  . ALA   B 1 134 ? 38.534 -31.249 3.554   1.00 22.37 ?  134 ALA   B HB3  1 
ATOM   5997 N N    . ASP   B 1 135 ? 37.635 -34.562 3.266   1.00 18.06 ?  135 ASP   B N    1 
ATOM   5998 C CA   . ASP   B 1 135 ? 37.537 -35.452 2.116   1.00 18.70 ?  135 ASP   B CA   1 
ATOM   5999 C C    . ASP   B 1 135 ? 37.631 -34.614 0.847   1.00 17.75 ?  135 ASP   B C    1 
ATOM   6000 O O    . ASP   B 1 135 ? 36.774 -33.747 0.626   1.00 17.77 ?  135 ASP   B O    1 
ATOM   6001 C CB   . ASP   B 1 135 ? 36.196 -36.187 2.175   1.00 20.54 ?  135 ASP   B CB   1 
ATOM   6002 C CG   . ASP   B 1 135 ? 36.002 -37.170 1.032   1.00 22.77 ?  135 ASP   B CG   1 
ATOM   6003 O OD1  . ASP   B 1 135 ? 36.861 -37.227 0.128   1.00 22.67 ?  135 ASP   B OD1  1 
ATOM   6004 O OD2  . ASP   B 1 135 ? 34.990 -37.911 1.053   1.00 26.18 -1 135 ASP   B OD2  1 
ATOM   6005 H H    . ASP   B 1 135 ? 36.910 -34.490 3.720   1.00 21.82 ?  135 ASP   B H    1 
ATOM   6006 H HA   . ASP   B 1 135 ? 38.258 -36.102 2.146   1.00 22.59 ?  135 ASP   B HA   1 
ATOM   6007 H HB2  . ASP   B 1 135 ? 36.153 -36.685 3.005   1.00 24.80 ?  135 ASP   B HB2  1 
ATOM   6008 H HB3  . ASP   B 1 135 ? 35.484 -35.533 2.139   1.00 24.80 ?  135 ASP   B HB3  1 
ATOM   6009 N N    . PRO   B 1 136 ? 38.640 -34.818 -0.004  1.00 17.96 ?  136 PRO   B N    1 
ATOM   6010 C CA   . PRO   B 1 136 ? 38.735 -33.995 -1.222  1.00 17.13 ?  136 PRO   B CA   1 
ATOM   6011 C C    . PRO   B 1 136 ? 37.545 -34.143 -2.149  1.00 16.33 ?  136 PRO   B C    1 
ATOM   6012 O O    . PRO   B 1 136 ? 37.214 -33.195 -2.872  1.00 15.42 ?  136 PRO   B O    1 
ATOM   6013 C CB   . PRO   B 1 136 ? 40.043 -34.472 -1.870  1.00 18.08 ?  136 PRO   B CB   1 
ATOM   6014 C CG   . PRO   B 1 136 ? 40.230 -35.871 -1.335  1.00 19.44 ?  136 PRO   B CG   1 
ATOM   6015 C CD   . PRO   B 1 136 ? 39.720 -35.814 0.075   1.00 18.67 ?  136 PRO   B CD   1 
ATOM   6016 H HA   . PRO   B 1 136 ? 38.828 -33.057 -0.986  1.00 20.70 ?  136 PRO   B HA   1 
ATOM   6017 H HB2  . PRO   B 1 136 ? 39.947 -34.483 -2.837  1.00 21.85 ?  136 PRO   B HB2  1 
ATOM   6018 H HB3  . PRO   B 1 136 ? 40.773 -33.897 -1.601  1.00 21.85 ?  136 PRO   B HB3  1 
ATOM   6019 H HG2  . PRO   B 1 136 ? 39.711 -36.503 -1.859  1.00 23.48 ?  136 PRO   B HG2  1 
ATOM   6020 H HG3  . PRO   B 1 136 ? 41.171 -36.109 -1.346  1.00 23.48 ?  136 PRO   B HG3  1 
ATOM   6021 H HD2  . PRO   B 1 136 ? 39.364 -36.675 0.346   1.00 22.55 ?  136 PRO   B HD2  1 
ATOM   6022 H HD3  . PRO   B 1 136 ? 40.415 -35.510 0.683   1.00 22.55 ?  136 PRO   B HD3  1 
ATOM   6023 N N    . ILE   B 1 137 ? 36.886 -35.307 -2.148  1.00 16.59 ?  137 ILE   B N    1 
ATOM   6024 C CA   . ILE   B 1 137 ? 35.670 -35.482 -2.942  1.00 17.02 ?  137 ILE   B CA   1 
ATOM   6025 C C    . ILE   B 1 137 ? 34.588 -34.517 -2.466  1.00 16.44 ?  137 ILE   B C    1 
ATOM   6026 O O    . ILE   B 1 137 ? 33.870 -33.904 -3.270  1.00 16.27 ?  137 ILE   B O    1 
ATOM   6027 C CB   . ILE   B 1 137 ? 35.202 -36.953 -2.884  1.00 19.04 ?  137 ILE   B CB   1 
ATOM   6028 C CG1  . ILE   B 1 137 ? 36.177 -37.854 -3.642  1.00 21.71 ?  137 ILE   B CG1  1 
ATOM   6029 C CG2  . ILE   B 1 137 ? 33.801 -37.098 -3.451  1.00 19.82 ?  137 ILE   B CG2  1 
ATOM   6030 C CD1  . ILE   B 1 137 ? 35.881 -39.341 -3.502  1.00 24.07 ?  137 ILE   B CD1  1 
ATOM   6031 H H    . ILE   B 1 137 ? 37.116 -36.006 -1.700  1.00 20.05 ?  137 ILE   B H    1 
ATOM   6032 H HA   . ILE   B 1 137 ? 35.869 -35.271 -3.869  1.00 20.57 ?  137 ILE   B HA   1 
ATOM   6033 H HB   . ILE   B 1 137 ? 35.184 -37.229 -1.958  1.00 22.99 ?  137 ILE   B HB   1 
ATOM   6034 H HG12 . ILE   B 1 137 ? 36.137 -37.634 -4.587  1.00 26.19 ?  137 ILE   B HG12 1 
ATOM   6035 H HG13 . ILE   B 1 137 ? 37.071 -37.698 -3.305  1.00 26.19 ?  137 ILE   B HG13 1 
ATOM   6036 H HG21 . ILE   B 1 137 ? 33.577 -38.041 -3.523  1.00 23.93 ?  137 ILE   B HG21 1 
ATOM   6037 H HG22 . ILE   B 1 137 ? 33.166 -36.668 -2.857  1.00 23.93 ?  137 ILE   B HG22 1 
ATOM   6038 H HG23 . ILE   B 1 137 ? 33.767 -36.687 -4.328  1.00 23.93 ?  137 ILE   B HG23 1 
ATOM   6039 H HD11 . ILE   B 1 137 ? 36.607 -39.833 -3.907  1.00 29.03 ?  137 ILE   B HD11 1 
ATOM   6040 H HD12 . ILE   B 1 137 ? 35.809 -39.562 -2.560  1.00 29.03 ?  137 ILE   B HD12 1 
ATOM   6041 H HD13 . ILE   B 1 137 ? 35.050 -39.549 -3.957  1.00 29.03 ?  137 ILE   B HD13 1 
ATOM   6042 N N    . HIS   B 1 138 ? 34.463 -34.358 -1.152  1.00 16.79 ?  138 HIS   B N    1 
ATOM   6043 C CA   . HIS   B 1 138 ? 33.510 -33.391 -0.619  1.00 17.22 ?  138 HIS   B CA   1 
ATOM   6044 C C    . HIS   B 1 138 ? 33.925 -31.960 -0.938  1.00 16.28 ?  138 HIS   B C    1 
ATOM   6045 O O    . HIS   B 1 138 ? 33.078 -31.117 -1.250  1.00 17.01 ?  138 HIS   B O    1 
ATOM   6046 C CB   . HIS   B 1 138 ? 33.387 -33.568 0.887   1.00 18.66 ?  138 HIS   B CB   1 
ATOM   6047 C CG   . HIS   B 1 138 ? 32.443 -32.597 1.516   1.00 19.45 ?  138 HIS   B CG   1 
ATOM   6048 N ND1  . HIS   B 1 138 ? 31.104 -32.552 1.194   1.00 21.27 ?  138 HIS   B ND1  1 
ATOM   6049 C CD2  . HIS   B 1 138 ? 32.649 -31.605 2.413   1.00 20.04 ?  138 HIS   B CD2  1 
ATOM   6050 C CE1  . HIS   B 1 138 ? 30.521 -31.588 1.883   1.00 20.99 ?  138 HIS   B CE1  1 
ATOM   6051 N NE2  . HIS   B 1 138 ? 31.436 -31.000 2.633   1.00 20.57 ?  138 HIS   B NE2  1 
ATOM   6052 H H    . HIS   B 1 138 ? 34.913 -34.785 -0.563  1.00 20.30 ?  138 HIS   B H    1 
ATOM   6053 H HA   . HIS   B 1 138 ? 32.639 -33.554 -1.018  1.00 20.81 ?  138 HIS   B HA   1 
ATOM   6054 H HB2  . HIS   B 1 138 ? 33.059 -34.461 1.073   1.00 22.53 ?  138 HIS   B HB2  1 
ATOM   6055 H HB3  . HIS   B 1 138 ? 34.257 -33.441 1.290   1.00 22.53 ?  138 HIS   B HB3  1 
ATOM   6056 H HD1  . HIS   B 1 138 ? 30.709 -33.077 0.634   1.00 25.67 ?  138 HIS   B HD1  1 
ATOM   6057 H HD2  . HIS   B 1 138 ? 33.450 -31.382 2.820   1.00 24.20 ?  138 HIS   B HD2  1 
ATOM   6058 H HE1  . HIS   B 1 138 ? 29.613 -31.370 1.847   1.00 25.34 ?  138 HIS   B HE1  1 
ATOM   6059 N N    . SER   B 1 139 ? 35.220 -31.662 -0.857  1.00 15.48 ?  139 SER   B N    1 
ATOM   6060 C CA   . SER   B 1 139 ? 35.665 -30.316 -1.179  1.00 14.96 ?  139 SER   B CA   1 
ATOM   6061 C C    . SER   B 1 139 ? 35.324 -29.957 -2.617  1.00 14.23 ?  139 SER   B C    1 
ATOM   6062 O O    . SER   B 1 139 ? 34.876 -28.839 -2.892  1.00 14.51 ?  139 SER   B O    1 
ATOM   6063 C CB   . SER   B 1 139 ? 37.163 -30.186 -0.921  1.00 15.65 ?  139 SER   B CB   1 
ATOM   6064 O OG   . SER   B 1 139 ? 37.578 -28.846 -1.157  1.00 15.65 ?  139 SER   B OG   1 
ATOM   6065 H H    . SER   B 1 139 ? 35.837 -32.209 -0.629  1.00 18.73 ?  139 SER   B H    1 
ATOM   6066 H HA   . SER   B 1 139 ? 35.207 -29.688 -0.606  1.00 18.10 ?  139 SER   B HA   1 
ATOM   6067 H HB2  . SER   B 1 139 ? 37.347 -30.422 0.003   1.00 18.92 ?  139 SER   B HB2  1 
ATOM   6068 H HB3  . SER   B 1 139 ? 37.646 -30.782 -1.517  1.00 18.92 ?  139 SER   B HB3  1 
ATOM   6069 H HG   . SER   B 1 139 ? 38.408 -28.776 -1.009  1.00 18.93 ?  139 SER   B HG   1 
ATOM   6070 N N    . LEU   B 1 140 ? 35.519 -30.894 -3.548  1.00 14.12 ?  140 LEU   B N    1 
ATOM   6071 C CA   . LEU   B 1 140 ? 35.149 -30.642 -4.935  1.00 14.36 ?  140 LEU   B CA   1 
ATOM   6072 C C    . LEU   B 1 140 ? 33.642 -30.417 -5.063  1.00 14.35 ?  140 LEU   B C    1 
ATOM   6073 O O    . LEU   B 1 140 ? 33.199 -29.540 -5.809  1.00 14.55 ?  140 LEU   B O    1 
ATOM   6074 C CB   . LEU   B 1 140 ? 35.620 -31.805 -5.815  1.00 14.62 ?  140 LEU   B CB   1 
ATOM   6075 C CG   . LEU   B 1 140 ? 35.260 -31.700 -7.290  1.00 14.81 ?  140 LEU   B CG   1 
ATOM   6076 C CD1  . LEU   B 1 140 ? 35.819 -30.418 -7.892  1.00 15.94 ?  140 LEU   B CD1  1 
ATOM   6077 C CD2  . LEU   B 1 140 ? 35.749 -32.935 -8.037  1.00 15.67 ?  140 LEU   B CD2  1 
ATOM   6078 H H    . LEU   B 1 140 ? 35.852 -31.675 -3.405  1.00 17.09 ?  140 LEU   B H    1 
ATOM   6079 H HA   . LEU   B 1 140 ? 35.603 -29.840 -5.241  1.00 17.38 ?  140 LEU   B HA   1 
ATOM   6080 H HB2  . LEU   B 1 140 ? 36.592 -31.865 -5.763  1.00 17.69 ?  140 LEU   B HB2  1 
ATOM   6081 H HB3  . LEU   B 1 140 ? 35.231 -32.628 -5.484  1.00 17.69 ?  140 LEU   B HB3  1 
ATOM   6082 H HG   . LEU   B 1 140 ? 34.293 -31.663 -7.373  1.00 17.92 ?  140 LEU   B HG   1 
ATOM   6083 H HD11 . LEU   B 1 140 ? 35.694 -30.445 -8.853  1.00 19.27 ?  140 LEU   B HD11 1 
ATOM   6084 H HD12 . LEU   B 1 140 ? 35.342 -29.659 -7.519  1.00 19.27 ?  140 LEU   B HD12 1 
ATOM   6085 H HD13 . LEU   B 1 140 ? 36.761 -30.357 -7.680  1.00 19.27 ?  140 LEU   B HD13 1 
ATOM   6086 H HD21 . LEU   B 1 140 ? 35.506 -32.848 -8.973  1.00 18.96 ?  140 LEU   B HD21 1 
ATOM   6087 H HD22 . LEU   B 1 140 ? 36.708 -32.996 -7.944  1.00 18.96 ?  140 LEU   B HD22 1 
ATOM   6088 H HD23 . LEU   B 1 140 ? 35.322 -33.716 -7.654  1.00 18.96 ?  140 LEU   B HD23 1 
ATOM   6089 N N    . ARG   B 1 141 ? 32.840 -31.210 -4.348  1.00 14.53 ?  141 ARG   B N    1 
ATOM   6090 C CA   . ARG   B 1 141 ? 31.390 -31.037 -4.337  1.00 15.55 ?  141 ARG   B CA   1 
ATOM   6091 C C    . ARG   B 1 141 ? 31.007 -29.629 -3.899  1.00 14.74 ?  141 ARG   B C    1 
ATOM   6092 O O    . ARG   B 1 141 ? 30.201 -28.950 -4.553  1.00 15.19 ?  141 ARG   B O    1 
ATOM   6093 C CB   . ARG   B 1 141 ? 30.810 -32.071 -3.367  1.00 17.53 ?  141 ARG   B CB   1 
ATOM   6094 C CG   . ARG   B 1 141 ? 29.339 -31.953 -3.030  1.00 19.92 ?  141 ARG   B CG   1 
ATOM   6095 C CD   . ARG   B 1 141 ? 28.522 -32.579 -4.092  1.00 21.54 ?  141 ARG   B CD   1 
ATOM   6096 N NE   . ARG   B 1 141 ? 28.266 -31.670 -5.198  1.00 22.29 ?  141 ARG   B NE   1 
ATOM   6097 C CZ   . ARG   B 1 141 ? 28.263 -32.024 -6.475  1.00 21.52 ?  141 ARG   B CZ   1 
ATOM   6098 N NH1  . ARG   B 1 141 ? 28.703 -33.211 -6.867  1.00 21.20 ?  141 ARG   B NH1  1 
ATOM   6099 N NH2  . ARG   B 1 141 ? 27.799 -31.169 -7.382  1.00 22.13 ?  141 ARG   B NH2  1 
ATOM   6100 H H    . ARG   B 1 141 ? 33.123 -31.857 -3.860  1.00 17.58 ?  141 ARG   B H    1 
ATOM   6101 H HA   . ARG   B 1 141 ? 31.035 -31.195 -5.222  1.00 18.81 ?  141 ARG   B HA   1 
ATOM   6102 H HB2  . ARG   B 1 141 ? 30.956 -32.953 -3.747  1.00 21.18 ?  141 ARG   B HB2  1 
ATOM   6103 H HB3  . ARG   B 1 141 ? 31.299 -32.008 -2.533  1.00 21.18 ?  141 ARG   B HB3  1 
ATOM   6104 H HG2  . ARG   B 1 141 ? 29.170 -32.405 -2.193  1.00 24.05 ?  141 ARG   B HG2  1 
ATOM   6105 H HG3  . ARG   B 1 141 ? 29.089 -31.013 -2.957  1.00 24.05 ?  141 ARG   B HG3  1 
ATOM   6106 H HD2  . ARG   B 1 141 ? 28.990 -33.364 -4.426  1.00 25.99 ?  141 ARG   B HD2  1 
ATOM   6107 H HD3  . ARG   B 1 141 ? 27.674 -32.846 -3.714  1.00 25.99 ?  141 ARG   B HD3  1 
ATOM   6108 H HE   . ARG   B 1 141 ? 28.092 -30.850 -5.008  1.00 26.89 ?  141 ARG   B HE   1 
ATOM   6109 H HH11 . ARG   B 1 141 ? 28.993 -33.784 -6.292  1.00 25.59 ?  141 ARG   B HH11 1 
ATOM   6110 H HH12 . ARG   B 1 141 ? 28.698 -33.416 -7.700  1.00 25.59 ?  141 ARG   B HH12 1 
ATOM   6111 H HH21 . ARG   B 1 141 ? 27.519 -30.391 -7.138  1.00 26.71 ?  141 ARG   B HH21 1 
ATOM   6112 H HH22 . ARG   B 1 141 ? 27.811 -31.376 -8.217  1.00 26.71 ?  141 ARG   B HH22 1 
ATOM   6113 N N    . VAL   B 1 142 ? 31.563 -29.181 -2.774  1.00 14.78 ?  142 VAL   B N    1 
ATOM   6114 C CA   . VAL   B 1 142 ? 31.231 -27.847 -2.286  1.00 14.54 ?  142 VAL   B CA   1 
ATOM   6115 C C    . VAL   B 1 142 ? 31.704 -26.788 -3.276  1.00 14.49 ?  142 VAL   B C    1 
ATOM   6116 O O    . VAL   B 1 142 ? 30.998 -25.807 -3.541  1.00 14.81 ?  142 VAL   B O    1 
ATOM   6117 C CB   . VAL   B 1 142 ? 31.785 -27.619 -0.866  1.00 15.30 ?  142 VAL   B CB   1 
ATOM   6118 C CG1  . VAL   B 1 142 ? 31.474 -26.195 -0.386  1.00 15.31 ?  142 VAL   B CG1  1 
ATOM   6119 C CG2  . VAL   B 1 142 ? 31.208 -28.643 0.098   1.00 15.97 ?  142 VAL   B CG2  1 
ATOM   6120 H H    . VAL   B 1 142 ? 32.122 -29.619 -2.285  1.00 17.88 ?  142 VAL   B H    1 
ATOM   6121 H HA   . VAL   B 1 142 ? 30.271 -27.774 -2.230  1.00 17.60 ?  142 VAL   B HA   1 
ATOM   6122 H HB   . VAL   B 1 142 ? 32.750 -27.729 -0.877  1.00 18.51 ?  142 VAL   B HB   1 
ATOM   6123 H HG11 . VAL   B 1 142 ? 31.669 -26.132 0.561   1.00 18.52 ?  142 VAL   B HG11 1 
ATOM   6124 H HG12 . VAL   B 1 142 ? 32.031 -25.567 -0.878  1.00 18.52 ?  142 VAL   B HG12 1 
ATOM   6125 H HG13 . VAL   B 1 142 ? 30.539 -26.005 -0.548  1.00 18.52 ?  142 VAL   B HG13 1 
ATOM   6126 H HG21 . VAL   B 1 142 ? 31.535 -28.456 0.992   1.00 19.32 ?  142 VAL   B HG21 1 
ATOM   6127 H HG22 . VAL   B 1 142 ? 30.241 -28.584 0.079   1.00 19.32 ?  142 VAL   B HG22 1 
ATOM   6128 H HG23 . VAL   B 1 142 ? 31.491 -29.530 -0.177  1.00 19.32 ?  142 VAL   B HG23 1 
ATOM   6129 N N    . CYS   B 1 143 ? 32.889 -26.988 -3.862  1.00 13.92 ?  143 CYS   B N    1 
ATOM   6130 C CA   . CYS   B 1 143 ? 33.385 -26.051 -4.868  1.00 13.75 ?  143 CYS   B CA   1 
ATOM   6131 C C    . CYS   B 1 143 ? 32.384 -25.906 -6.014  1.00 13.87 ?  143 CYS   B C    1 
ATOM   6132 O O    . CYS   B 1 143 ? 31.970 -24.793 -6.366  1.00 14.27 ?  143 CYS   B O    1 
ATOM   6133 C CB   . CYS   B 1 143 ? 34.745 -26.523 -5.389  1.00 14.40 ?  143 CYS   B CB   1 
ATOM   6134 S SG   . CYS   B 1 143 ? 35.487 -25.423 -6.613  1.00 14.46 ?  143 CYS   B SG   1 
ATOM   6135 H H    . CYS   B 1 143 ? 33.417 -27.647 -3.698  1.00 16.85 ?  143 CYS   B H    1 
ATOM   6136 H HA   . CYS   B 1 143 ? 33.507 -25.181 -4.460  1.00 16.64 ?  143 CYS   B HA   1 
ATOM   6137 H HB2  . CYS   B 1 143 ? 35.364 -26.595 -4.645  1.00 17.43 ?  143 CYS   B HB2  1 
ATOM   6138 H HB3  . CYS   B 1 143 ? 34.636 -27.392 -5.800  1.00 17.43 ?  143 CYS   B HB3  1 
ATOM   6139 H HG   . CYS   B 1 143 ? 36.561 -25.859 -6.937  1.00 17.50 ?  143 CYS   B HG   1 
ATOM   6140 N N    . VAL   B 1 144 ? 31.963 -27.027 -6.599  1.00 14.36 ?  144 VAL   B N    1 
ATOM   6141 C CA   . VAL   B 1 144 ? 31.059 -26.950 -7.744  1.00 15.19 ?  144 VAL   B CA   1 
ATOM   6142 C C    . VAL   B 1 144 ? 29.717 -26.341 -7.363  1.00 15.42 ?  144 VAL   B C    1 
ATOM   6143 O O    . VAL   B 1 144 ? 29.091 -25.644 -8.172  1.00 16.41 ?  144 VAL   B O    1 
ATOM   6144 C CB   . VAL   B 1 144 ? 30.902 -28.356 -8.344  1.00 18.11 ?  144 VAL   B CB   1 
ATOM   6145 C CG1  . VAL   B 1 144 ? 29.638 -28.464 -9.198  1.00 21.35 ?  144 VAL   B CG1  1 
ATOM   6146 C CG2  . VAL   B 1 144 ? 32.162 -28.749 -9.114  1.00 18.21 ?  144 VAL   B CG2  1 
ATOM   6147 H H    . VAL   B 1 144 ? 32.184 -27.823 -6.361  1.00 17.38 ?  144 VAL   B H    1 
ATOM   6148 H HA   . VAL   B 1 144 ? 31.459 -26.382 -8.420  1.00 18.38 ?  144 VAL   B HA   1 
ATOM   6149 H HB   . VAL   B 1 144 ? 30.813 -28.991 -7.615  1.00 21.89 ?  144 VAL   B HB   1 
ATOM   6150 H HG11 . VAL   B 1 144 ? 29.723 -29.238 -9.780  1.00 25.77 ?  144 VAL   B HG11 1 
ATOM   6151 H HG12 . VAL   B 1 144 ? 28.876 -28.575 -8.613  1.00 25.77 ?  144 VAL   B HG12 1 
ATOM   6152 H HG13 . VAL   B 1 144 ? 29.549 -27.662 -9.729  1.00 25.77 ?  144 VAL   B HG13 1 
ATOM   6153 H HG21 . VAL   B 1 144 ? 32.047 -29.639 -9.481  1.00 22.00 ?  144 VAL   B HG21 1 
ATOM   6154 H HG22 . VAL   B 1 144 ? 32.303 -28.112 -9.835  1.00 22.00 ?  144 VAL   B HG22 1 
ATOM   6155 H HG23 . VAL   B 1 144 ? 32.922 -28.735 -8.511  1.00 22.00 ?  144 VAL   B HG23 1 
ATOM   6156 N N    . ASP   B 1 145 ? 29.249 -26.600 -6.144  1.00 15.55 ?  145 ASP   B N    1 
ATOM   6157 C CA   . ASP   B 1 145 ? 27.946 -26.117 -5.708  1.00 16.29 ?  145 ASP   B CA   1 
ATOM   6158 C C    . ASP   B 1 145 ? 27.980 -24.690 -5.170  1.00 15.66 ?  145 ASP   B C    1 
ATOM   6159 O O    . ASP   B 1 145 ? 26.921 -24.146 -4.841  1.00 17.54 ?  145 ASP   B O    1 
ATOM   6160 C CB   . ASP   B 1 145 ? 27.366 -27.034 -4.624  1.00 17.88 ?  145 ASP   B CB   1 
ATOM   6161 C CG   . ASP   B 1 145 ? 26.988 -28.409 -5.138  1.00 19.56 ?  145 ASP   B CG   1 
ATOM   6162 O OD1  . ASP   B 1 145 ? 26.876 -28.602 -6.367  1.00 19.77 ?  145 ASP   B OD1  1 
ATOM   6163 O OD2  . ASP   B 1 145 ? 26.780 -29.295 -4.288  1.00 21.95 -1 145 ASP   B OD2  1 
ATOM   6164 H H    . ASP   B 1 145 ? 29.683 -27.041 -5.548  1.00 18.80 ?  145 ASP   B H    1 
ATOM   6165 H HA   . ASP   B 1 145 ? 27.349 -26.112 -6.465  1.00 19.70 ?  145 ASP   B HA   1 
ATOM   6166 H HB2  . ASP   B 1 145 ? 28.022 -27.151 -3.927  1.00 21.61 ?  145 ASP   B HB2  1 
ATOM   6167 H HB3  . ASP   B 1 145 ? 26.566 -26.614 -4.265  1.00 21.61 ?  145 ASP   B HB3  1 
ATOM   6168 N N    . THR   B 1 146 ? 29.154 -24.078 -5.057  1.00 14.13 ?  146 THR   B N    1 
ATOM   6169 C CA   . THR   B 1 146 ? 29.292 -22.757 -4.448  1.00 14.17 ?  146 THR   B CA   1 
ATOM   6170 C C    . THR   B 1 146 ? 29.927 -21.730 -5.368  1.00 13.90 ?  146 THR   B C    1 
ATOM   6171 O O    . THR   B 1 146 ? 29.464 -20.574 -5.422  1.00 14.28 ?  146 THR   B O    1 
ATOM   6172 C CB   . THR   B 1 146 ? 30.124 -22.863 -3.161  1.00 14.57 ?  146 THR   B CB   1 
ATOM   6173 O OG1  . THR   B 1 146 ? 29.553 -23.854 -2.298  1.00 14.57 ?  146 THR   B OG1  1 
ATOM   6174 C CG2  . THR   B 1 146 ? 30.198 -21.511 -2.444  1.00 14.67 ?  146 THR   B CG2  1 
ATOM   6175 H H    . THR   B 1 146 ? 29.905 -24.407 -5.332  1.00 17.11 ?  146 THR   B H    1 
ATOM   6176 H HA   . THR   B 1 146 ? 28.421 -22.425 -4.206  1.00 17.15 ?  146 THR   B HA   1 
ATOM   6177 H HB   . THR   B 1 146 ? 31.032 -23.125 -3.389  1.00 17.63 ?  146 THR   B HB   1 
ATOM   6178 H HG1  . THR   B 1 146 ? 29.580 -24.611 -2.679  1.00 17.64 ?  146 THR   B HG1  1 
ATOM   6179 H HG21 . THR   B 1 146 ? 30.542 -21.635 -1.547  1.00 17.75 ?  146 THR   B HG21 1 
ATOM   6180 H HG22 . THR   B 1 146 ? 30.789 -20.911 -2.927  1.00 17.75 ?  146 THR   B HG22 1 
ATOM   6181 H HG23 . THR   B 1 146 ? 29.316 -21.117 -2.394  1.00 17.75 ?  146 THR   B HG23 1 
ATOM   6182 N N    . VAL   B 1 147 ? 30.986 -22.102 -6.073  1.00 13.53 ?  147 VAL   B N    1 
ATOM   6183 C CA   . VAL   B 1 147 ? 31.711 -21.155 -6.909  1.00 13.13 ?  147 VAL   B CA   1 
ATOM   6184 C C    . VAL   B 1 147 ? 30.981 -21.013 -8.232  1.00 13.56 ?  147 VAL   B C    1 
ATOM   6185 O O    . VAL   B 1 147 ? 30.608 -22.013 -8.864  1.00 14.32 ?  147 VAL   B O    1 
ATOM   6186 C CB   . VAL   B 1 147 ? 33.164 -21.614 -7.118  1.00 13.29 ?  147 VAL   B CB   1 
ATOM   6187 C CG1  . VAL   B 1 147 ? 33.924 -20.591 -7.936  1.00 13.38 ?  147 VAL   B CG1  1 
ATOM   6188 C CG2  . VAL   B 1 147 ? 33.848 -21.833 -5.780  1.00 13.59 ?  147 VAL   B CG2  1 
ATOM   6189 H H    . VAL   B 1 147 ? 31.311 -22.904 -6.090  1.00 16.38 ?  147 VAL   B H    1 
ATOM   6190 H HA   . VAL   B 1 147 ? 31.732 -20.292 -6.476  1.00 15.91 ?  147 VAL   B HA   1 
ATOM   6191 H HB   . VAL   B 1 147 ? 33.174 -22.457 -7.605  1.00 16.09 ?  147 VAL   B HB   1 
ATOM   6192 H HG11 . VAL   B 1 147 ? 34.871 -20.807 -7.923  1.00 16.20 ?  147 VAL   B HG11 1 
ATOM   6193 H HG12 . VAL   B 1 147 ? 33.599 -20.599 -8.850  1.00 16.20 ?  147 VAL   B HG12 1 
ATOM   6194 H HG13 . VAL   B 1 147 ? 33.788 -19.709 -7.546  1.00 16.20 ?  147 VAL   B HG13 1 
ATOM   6195 H HG21 . VAL   B 1 147 ? 34.788 -22.028 -5.931  1.00 16.46 ?  147 VAL   B HG21 1 
ATOM   6196 H HG22 . VAL   B 1 147 ? 33.762 -21.027 -5.248  1.00 16.46 ?  147 VAL   B HG22 1 
ATOM   6197 H HG23 . VAL   B 1 147 ? 33.426 -22.578 -5.325  1.00 16.46 ?  147 VAL   B HG23 1 
ATOM   6198 N N    . ARG   B 1 148 ? 30.766 -19.756 -8.644  1.00 13.48 ?  148 ARG   B N    1 
ATOM   6199 C CA   . ARG   B 1 148 ? 30.143 -19.433 -9.918  1.00 13.83 ?  148 ARG   B CA   1 
ATOM   6200 C C    . ARG   B 1 148 ? 31.100 -18.766 -10.895 1.00 13.72 ?  148 ARG   B C    1 
ATOM   6201 O O    . ARG   B 1 148 ? 30.812 -18.742 -12.094 1.00 14.99 ?  148 ARG   B O    1 
ATOM   6202 C CB   . ARG   B 1 148 ? 28.904 -18.549 -9.702  1.00 14.38 ?  148 ARG   B CB   1 
ATOM   6203 C CG   . ARG   B 1 148 ? 27.831 -19.257 -8.886  1.00 15.02 ?  148 ARG   B CG   1 
ATOM   6204 C CD   . ARG   B 1 148 ? 26.618 -18.385 -8.573  1.00 15.66 ?  148 ARG   B CD   1 
ATOM   6205 N NE   . ARG   B 1 148 ? 26.993 -17.181 -7.843  1.00 15.25 ?  148 ARG   B NE   1 
ATOM   6206 C CZ   . ARG   B 1 148 ? 27.296 -17.147 -6.552  1.00 14.67 ?  148 ARG   B CZ   1 
ATOM   6207 N NH1  . ARG   B 1 148 ? 27.228 -18.232 -5.794  1.00 15.04 ?  148 ARG   B NH1  1 
ATOM   6208 N NH2  . ARG   B 1 148 ? 27.690 -15.998 -6.010  1.00 14.94 ?  148 ARG   B NH2  1 
ATOM   6209 H H    . ARG   B 1 148 ? 30.988 -19.058 -8.185  1.00 16.32 ?  148 ARG   B H    1 
ATOM   6210 H HA   . ARG   B 1 148 ? 29.843 -20.260 -10.326 1.00 16.74 ?  148 ARG   B HA   1 
ATOM   6211 H HB2  . ARG   B 1 148 ? 29.170 -17.748 -9.223  1.00 17.40 ?  148 ARG   B HB2  1 
ATOM   6212 H HB3  . ARG   B 1 148 ? 28.530 -18.317 -10.563 1.00 17.40 ?  148 ARG   B HB3  1 
ATOM   6213 H HG2  . ARG   B 1 148 ? 27.523 -20.030 -9.386  1.00 18.17 ?  148 ARG   B HG2  1 
ATOM   6214 H HG3  . ARG   B 1 148 ? 28.217 -19.544 -8.045  1.00 18.17 ?  148 ARG   B HG3  1 
ATOM   6215 H HD2  . ARG   B 1 148 ? 26.196 -18.118 -9.404  1.00 18.94 ?  148 ARG   B HD2  1 
ATOM   6216 H HD3  . ARG   B 1 148 ? 25.994 -18.893 -8.030  1.00 18.94 ?  148 ARG   B HD3  1 
ATOM   6217 H HE   . ARG   B 1 148 ? 27.025 -16.445 -8.280  1.00 18.45 ?  148 ARG   B HE   1 
ATOM   6218 H HH11 . ARG   B 1 148 ? 26.972 -18.983 -6.128  1.00 18.19 ?  148 ARG   B HH11 1 
ATOM   6219 H HH12 . ARG   B 1 148 ? 27.423 -18.185 -4.955  1.00 18.19 ?  148 ARG   B HH12 1 
ATOM   6220 H HH21 . ARG   B 1 148 ? 27.742 -15.290 -6.495  1.00 18.08 ?  148 ARG   B HH21 1 
ATOM   6221 H HH22 . ARG   B 1 148 ? 27.887 -15.960 -5.174  1.00 18.08 ?  148 ARG   B HH22 1 
ATOM   6222 N N    . THR   B 1 149 ? 32.207 -18.206 -10.410 1.00 13.74 ?  149 THR   B N    1 
ATOM   6223 C CA   . THR   B 1 149 ? 33.251 -17.647 -11.256 1.00 13.79 ?  149 THR   B CA   1 
ATOM   6224 C C    . THR   B 1 149 ? 34.133 -18.786 -11.771 1.00 13.49 ?  149 THR   B C    1 
ATOM   6225 O O    . THR   B 1 149 ? 33.929 -19.961 -11.446 1.00 14.20 ?  149 THR   B O    1 
ATOM   6226 C CB   . THR   B 1 149 ? 34.024 -16.602 -10.465 1.00 13.77 ?  149 THR   B CB   1 
ATOM   6227 O OG1  . THR   B 1 149 ? 34.477 -17.203 -9.254  1.00 13.69 ?  149 THR   B OG1  1 
ATOM   6228 C CG2  . THR   B 1 149 ? 33.126 -15.410 -10.157 1.00 14.07 ?  149 THR   B CG2  1 
ATOM   6229 H H    . THR   B 1 149 ? 32.369 -18.127 -9.571  1.00 16.64 ?  149 THR   B H    1 
ATOM   6230 H HA   . THR   B 1 149 ? 32.844 -17.209 -12.019 1.00 16.70 ?  149 THR   B HA   1 
ATOM   6231 H HB   . THR   B 1 149 ? 34.783 -16.298 -10.982 1.00 16.68 ?  149 THR   B HB   1 
ATOM   6232 H HG1  . THR   B 1 149 ? 34.904 -16.636 -8.793  1.00 16.57 ?  149 THR   B HG1  1 
ATOM   6233 H HG21 . THR   B 1 149 ? 33.629 -14.732 -9.678  1.00 17.03 ?  149 THR   B HG21 1 
ATOM   6234 H HG22 . THR   B 1 149 ? 32.789 -15.027 -10.982 1.00 17.03 ?  149 THR   B HG22 1 
ATOM   6235 H HG23 . THR   B 1 149 ? 32.375 -15.689 -9.610  1.00 17.03 ?  149 THR   B HG23 1 
ATOM   6236 N N    . ASN   B 1 150 ? 35.101 -18.464 -12.616 1.00 13.56 ?  150 ASN   B N    1 
ATOM   6237 C CA   . ASN   B 1 150 ? 35.871 -19.485 -13.319 1.00 13.92 ?  150 ASN   B CA   1 
ATOM   6238 C C    . ASN   B 1 150 ? 37.037 -19.939 -12.448 1.00 13.61 ?  150 ASN   B C    1 
ATOM   6239 O O    . ASN   B 1 150 ? 37.966 -19.170 -12.188 1.00 14.36 ?  150 ASN   B O    1 
ATOM   6240 C CB   . ASN   B 1 150 ? 36.341 -18.943 -14.661 1.00 15.94 ?  150 ASN   B CB   1 
ATOM   6241 C CG   . ASN   B 1 150 ? 35.197 -18.743 -15.615 1.00 18.71 ?  150 ASN   B CG   1 
ATOM   6242 O OD1  . ASN   B 1 150 ? 34.317 -19.591 -15.717 1.00 19.84 ?  150 ASN   B OD1  1 
ATOM   6243 N ND2  . ASN   B 1 150 ? 35.175 -17.607 -16.291 1.00 20.64 ?  150 ASN   B ND2  1 
ATOM   6244 H H    . ASN   B 1 150 ? 35.344 -17.657 -12.795 1.00 16.42 ?  150 ASN   B H    1 
ATOM   6245 H HA   . ASN   B 1 150 ? 35.296 -20.252 -13.488 1.00 16.85 ?  150 ASN   B HA   1 
ATOM   6246 H HB2  . ASN   B 1 150 ? 36.773 -18.082 -14.519 1.00 19.27 ?  150 ASN   B HB2  1 
ATOM   6247 H HB3  . ASN   B 1 150 ? 36.965 -19.567 -15.057 1.00 19.27 ?  150 ASN   B HB3  1 
ATOM   6248 H HD21 . ASN   B 1 150 ? 34.538 -17.449 -16.850 1.00 24.91 ?  150 ASN   B HD21 1 
ATOM   6249 H HD22 . ASN   B 1 150 ? 35.802 -17.026 -16.185 1.00 24.91 ?  150 ASN   B HD22 1 
ATOM   6250 N N    . VAL   B 1 151 ? 36.989 -21.187 -11.993 1.00 13.09 ?  151 VAL   B N    1 
ATOM   6251 C CA   . VAL   B 1 151 ? 38.007 -21.726 -11.103 1.00 13.18 ?  151 VAL   B CA   1 
ATOM   6252 C C    . VAL   B 1 151 ? 38.719 -22.895 -11.780 1.00 12.90 ?  151 VAL   B C    1 
ATOM   6253 O O    . VAL   B 1 151 ? 38.081 -23.829 -12.284 1.00 13.84 ?  151 VAL   B O    1 
ATOM   6254 C CB   . VAL   B 1 151 ? 37.447 -22.065 -9.707  1.00 14.40 ?  151 VAL   B CB   1 
ATOM   6255 C CG1  . VAL   B 1 151 ? 36.275 -23.050 -9.786  1.00 15.61 ?  151 VAL   B CG1  1 
ATOM   6256 C CG2  . VAL   B 1 151 ? 38.552 -22.563 -8.792  1.00 15.04 ?  151 VAL   B CG2  1 
ATOM   6257 H H    . VAL   B 1 151 ? 36.360 -21.748 -12.192 1.00 15.86 ?  151 VAL   B H    1 
ATOM   6258 H HA   . VAL   B 1 151 ? 38.672 -21.033 -10.974 1.00 15.96 ?  151 VAL   B HA   1 
ATOM   6259 H HB   . VAL   B 1 151 ? 37.104 -21.241 -9.314  1.00 17.43 ?  151 VAL   B HB   1 
ATOM   6260 H HG11 . VAL   B 1 151 ? 35.960 -23.243 -8.886  1.00 18.88 ?  151 VAL   B HG11 1 
ATOM   6261 H HG12 . VAL   B 1 151 ? 35.554 -22.651 -10.304 1.00 18.88 ?  151 VAL   B HG12 1 
ATOM   6262 H HG13 . VAL   B 1 151 ? 36.573 -23.868 -10.212 1.00 18.88 ?  151 VAL   B HG13 1 
ATOM   6263 H HG21 . VAL   B 1 151 ? 38.201 -22.641 -7.890  1.00 18.20 ?  151 VAL   B HG21 1 
ATOM   6264 H HG22 . VAL   B 1 151 ? 38.854 -23.429 -9.104  1.00 18.20 ?  151 VAL   B HG22 1 
ATOM   6265 H HG23 . VAL   B 1 151 ? 39.287 -21.929 -8.805  1.00 18.20 ?  151 VAL   B HG23 1 
ATOM   6266 N N    . TYR   B 1 152 ? 40.050 -22.813 -11.791 1.00 12.74 ?  152 TYR   B N    1 
ATOM   6267 C CA   . TYR   B 1 152 ? 40.953 -23.792 -12.377 1.00 12.77 ?  152 TYR   B CA   1 
ATOM   6268 C C    . TYR   B 1 152 ? 41.673 -24.473 -11.218 1.00 11.97 ?  152 TYR   B C    1 
ATOM   6269 O O    . TYR   B 1 152 ? 42.522 -23.865 -10.565 1.00 13.06 ?  152 TYR   B O    1 
ATOM   6270 C CB   . TYR   B 1 152 ? 41.922 -23.083 -13.325 1.00 13.75 ?  152 TYR   B CB   1 
ATOM   6271 C CG   . TYR   B 1 152 ? 41.246 -22.624 -14.593 1.00 14.47 ?  152 TYR   B CG   1 
ATOM   6272 C CD1  . TYR   B 1 152 ? 40.576 -21.405 -14.656 1.00 14.83 ?  152 TYR   B CD1  1 
ATOM   6273 C CD2  . TYR   B 1 152 ? 41.253 -23.423 -15.723 1.00 15.50 ?  152 TYR   B CD2  1 
ATOM   6274 C CE1  . TYR   B 1 152 ? 39.938 -21.001 -15.814 1.00 16.10 ?  152 TYR   B CE1  1 
ATOM   6275 C CE2  . TYR   B 1 152 ? 40.617 -23.032 -16.881 1.00 16.66 ?  152 TYR   B CE2  1 
ATOM   6276 C CZ   . TYR   B 1 152 ? 39.961 -21.822 -16.924 1.00 16.69 ?  152 TYR   B CZ   1 
ATOM   6277 O OH   . TYR   B 1 152 ? 39.339 -21.442 -18.087 1.00 19.49 ?  152 TYR   B OH   1 
ATOM   6278 H H    . TYR   B 1 152 ? 40.477 -22.156 -11.433 1.00 15.43 ?  152 TYR   B H    1 
ATOM   6279 H HA   . TYR   B 1 152 ? 40.447 -24.456 -12.877 1.00 15.47 ?  152 TYR   B HA   1 
ATOM   6280 H HB2  . TYR   B 1 152 ? 42.283 -22.300 -12.873 1.00 16.64 ?  152 TYR   B HB2  1 
ATOM   6281 H HB3  . TYR   B 1 152 ? 42.637 -23.688 -13.562 1.00 16.64 ?  152 TYR   B HB3  1 
ATOM   6282 H HD1  . TYR   B 1 152 ? 40.551 -20.854 -13.905 1.00 17.94 ?  152 TYR   B HD1  1 
ATOM   6283 H HD2  . TYR   B 1 152 ? 41.688 -24.247 -15.695 1.00 18.75 ?  152 TYR   B HD2  1 
ATOM   6284 H HE1  . TYR   B 1 152 ? 39.494 -20.185 -15.847 1.00 19.46 ?  152 TYR   B HE1  1 
ATOM   6285 H HE2  . TYR   B 1 152 ? 40.637 -23.581 -17.631 1.00 20.14 ?  152 TYR   B HE2  1 
ATOM   6286 H HH   . TYR   B 1 152 ? 39.442 -22.038 -18.673 1.00 23.54 ?  152 TYR   B HH   1 
ATOM   6287 N N    . LEU   B 1 153 ? 41.309 -25.730 -10.953 1.00 12.50 ?  153 LEU   B N    1 
ATOM   6288 C CA   . LEU   B 1 153 ? 41.816 -26.482 -9.812  1.00 12.13 ?  153 LEU   B CA   1 
ATOM   6289 C C    . LEU   B 1 153 ? 43.046 -27.285 -10.208 1.00 12.62 ?  153 LEU   B C    1 
ATOM   6290 O O    . LEU   B 1 153 ? 43.024 -28.009 -11.207 1.00 13.71 ?  153 LEU   B O    1 
ATOM   6291 C CB   . LEU   B 1 153 ? 40.738 -27.439 -9.296  1.00 12.69 ?  153 LEU   B CB   1 
ATOM   6292 C CG   . LEU   B 1 153 ? 39.476 -26.791 -8.729  1.00 13.68 ?  153 LEU   B CG   1 
ATOM   6293 C CD1  . LEU   B 1 153 ? 38.382 -27.834 -8.585  1.00 14.60 ?  153 LEU   B CD1  1 
ATOM   6294 C CD2  . LEU   B 1 153 ? 39.775 -26.140 -7.384  1.00 13.83 ?  153 LEU   B CD2  1 
ATOM   6295 H H    . LEU   B 1 153 ? 40.737 -26.177 -11.432 1.00 15.14 ?  153 LEU   B H    1 
ATOM   6296 H HA   . LEU   B 1 153 ? 42.043 -25.866 -9.104  1.00 14.71 ?  153 LEU   B HA   1 
ATOM   6297 H HB2  . LEU   B 1 153 ? 40.458 -28.013 -10.026 1.00 15.38 ?  153 LEU   B HB2  1 
ATOM   6298 H HB3  . LEU   B 1 153 ? 41.123 -27.980 -8.589  1.00 15.38 ?  153 LEU   B HB3  1 
ATOM   6299 H HG   . LEU   B 1 153 ? 39.166 -26.098 -9.335  1.00 16.56 ?  153 LEU   B HG   1 
ATOM   6300 H HD11 . LEU   B 1 153 ? 37.582 -27.405 -8.245  1.00 17.67 ?  153 LEU   B HD11 1 
ATOM   6301 H HD12 . LEU   B 1 153 ? 38.208 -28.223 -9.454  1.00 17.67 ?  153 LEU   B HD12 1 
ATOM   6302 H HD13 . LEU   B 1 153 ? 38.682 -28.517 -7.966  1.00 17.67 ?  153 LEU   B HD13 1 
ATOM   6303 H HD21 . LEU   B 1 153 ? 38.963 -25.764 -7.018  1.00 16.74 ?  153 LEU   B HD21 1 
ATOM   6304 H HD22 . LEU   B 1 153 ? 40.130 -26.814 -6.778  1.00 16.74 ?  153 LEU   B HD22 1 
ATOM   6305 H HD23 . LEU   B 1 153 ? 40.438 -25.437 -7.508  1.00 16.74 ?  153 LEU   B HD23 1 
ATOM   6306 N N    . ALA   B 1 154 ? 44.099 -27.184 -9.402  1.00 12.75 ?  154 ALA   B N    1 
ATOM   6307 C CA   . ALA   B 1 154 ? 45.327 -27.945 -9.592  1.00 13.77 ?  154 ALA   B CA   1 
ATOM   6308 C C    . ALA   B 1 154 ? 45.405 -29.021 -8.514  1.00 14.54 ?  154 ALA   B C    1 
ATOM   6309 O O    . ALA   B 1 154 ? 45.336 -28.715 -7.316  1.00 16.12 ?  154 ALA   B O    1 
ATOM   6310 C CB   . ALA   B 1 154 ? 46.547 -27.031 -9.542  1.00 14.84 ?  154 ALA   B CB   1 
ATOM   6311 H H    . ALA   B 1 154 ? 44.112 -26.662 -8.712  1.00 15.45 ?  154 ALA   B H    1 
ATOM   6312 H HA   . ALA   B 1 154 ? 45.301 -28.377 -10.453 1.00 16.67 ?  154 ALA   B HA   1 
ATOM   6313 H HB1  . ALA   B 1 154 ? 47.344 -27.566 -9.670  1.00 17.96 ?  154 ALA   B HB1  1 
ATOM   6314 H HB2  . ALA   B 1 154 ? 46.475 -26.368 -10.247 1.00 17.96 ?  154 ALA   B HB2  1 
ATOM   6315 H HB3  . ALA   B 1 154 ? 46.580 -26.588 -8.677  1.00 17.96 ?  154 ALA   B HB3  1 
ATOM   6316 N N    . VAL   B 1 155 ? 45.523 -30.273 -8.944  1.00 13.81 ?  155 VAL   B N    1 
ATOM   6317 C CA   . VAL   B 1 155 ? 45.630 -31.425 -8.055  1.00 13.79 ?  155 VAL   B CA   1 
ATOM   6318 C C    . VAL   B 1 155 ? 46.971 -32.095 -8.332  1.00 13.86 ?  155 VAL   B C    1 
ATOM   6319 O O    . VAL   B 1 155 ? 47.211 -32.584 -9.443  1.00 15.80 ?  155 VAL   B O    1 
ATOM   6320 C CB   . VAL   B 1 155 ? 44.466 -32.412 -8.257  1.00 15.48 ?  155 VAL   B CB   1 
ATOM   6321 C CG1  . VAL   B 1 155 ? 44.637 -33.623 -7.352  1.00 15.70 ?  155 VAL   B CG1  1 
ATOM   6322 C CG2  . VAL   B 1 155 ? 43.118 -31.712 -8.003  1.00 16.54 ?  155 VAL   B CG2  1 
ATOM   6323 H H    . VAL   B 1 155 ? 45.553 -30.485 -9.777  1.00 16.72 ?  155 VAL   B H    1 
ATOM   6324 H HA   . VAL   B 1 155 ? 45.619 -31.129 -7.134  1.00 16.70 ?  155 VAL   B HA   1 
ATOM   6325 H HB   . VAL   B 1 155 ? 44.465 -32.719 -9.179  1.00 18.73 ?  155 VAL   B HB   1 
ATOM   6326 H HG11 . VAL   B 1 155 ? 43.809 -34.129 -7.336  1.00 18.98 ?  155 VAL   B HG11 1 
ATOM   6327 H HG12 . VAL   B 1 155 ? 45.354 -34.180 -7.699  1.00 18.98 ?  155 VAL   B HG12 1 
ATOM   6328 H HG13 . VAL   B 1 155 ? 44.856 -33.321 -6.457  1.00 18.98 ?  155 VAL   B HG13 1 
ATOM   6329 H HG21 . VAL   B 1 155 ? 42.403 -32.360 -8.095  1.00 20.00 ?  155 VAL   B HG21 1 
ATOM   6330 H HG22 . VAL   B 1 155 ? 43.120 -31.346 -7.104  1.00 20.00 ?  155 VAL   B HG22 1 
ATOM   6331 H HG23 . VAL   B 1 155 ? 43.004 -30.998 -8.650  1.00 20.00 ?  155 VAL   B HG23 1 
ATOM   6332 N N    . PHE   B 1 156 ? 47.836 -32.136 -7.317  1.00 14.46 ?  156 PHE   B N    1 
ATOM   6333 C CA   . PHE   B 1 156 ? 49.214 -32.591 -7.517  1.00 15.62 ?  156 PHE   B CA   1 
ATOM   6334 C C    . PHE   B 1 156 ? 49.307 -34.091 -7.805  1.00 16.35 ?  156 PHE   B C    1 
ATOM   6335 O O    . PHE   B 1 156 ? 50.044 -34.516 -8.705  1.00 18.47 ?  156 PHE   B O    1 
ATOM   6336 C CB   . PHE   B 1 156 ? 50.044 -32.224 -6.288  1.00 15.72 ?  156 PHE   B CB   1 
ATOM   6337 C CG   . PHE   B 1 156 ? 51.464 -32.689 -6.351  1.00 16.42 ?  156 PHE   B CG   1 
ATOM   6338 C CD1  . PHE   B 1 156 ? 52.335 -32.153 -7.276  1.00 17.85 ?  156 PHE   B CD1  1 
ATOM   6339 C CD2  . PHE   B 1 156 ? 51.928 -33.651 -5.478  1.00 16.79 ?  156 PHE   B CD2  1 
ATOM   6340 C CE1  . PHE   B 1 156 ? 53.656 -32.567 -7.332  1.00 18.86 ?  156 PHE   B CE1  1 
ATOM   6341 C CE2  . PHE   B 1 156 ? 53.246 -34.075 -5.530  1.00 18.13 ?  156 PHE   B CE2  1 
ATOM   6342 C CZ   . PHE   B 1 156 ? 54.103 -33.532 -6.463  1.00 18.79 ?  156 PHE   B CZ   1 
ATOM   6343 H H    . PHE   B 1 156 ? 47.651 -31.901 -6.510  1.00 17.50 ?  156 PHE   B H    1 
ATOM   6344 H HA   . PHE   B 1 156 ? 49.589 -32.120 -8.275  1.00 18.89 ?  156 PHE   B HA   1 
ATOM   6345 H HB2  . PHE   B 1 156 ? 50.051 -31.259 -6.196  1.00 19.01 ?  156 PHE   B HB2  1 
ATOM   6346 H HB3  . PHE   B 1 156 ? 49.638 -32.626 -5.504  1.00 19.01 ?  156 PHE   B HB3  1 
ATOM   6347 H HD1  . PHE   B 1 156 ? 52.035 -31.493 -7.868  1.00 21.57 ?  156 PHE   B HD1  1 
ATOM   6348 H HD2  . PHE   B 1 156 ? 51.348 -34.022 -4.853  1.00 20.30 ?  156 PHE   B HD2  1 
ATOM   6349 H HE1  . PHE   B 1 156 ? 54.236 -32.198 -7.961  1.00 22.78 ?  156 PHE   B HE1  1 
ATOM   6350 H HE2  . PHE   B 1 156 ? 53.549 -34.731 -4.943  1.00 21.91 ?  156 PHE   B HE2  1 
ATOM   6351 H HZ   . PHE   B 1 156 ? 54.988 -33.817 -6.498  1.00 22.69 ?  156 PHE   B HZ   1 
ATOM   6352 N N    . ASP   B 1 157 ? 48.632 -34.911 -7.014  1.00 17.15 ?  157 ASP   B N    1 
ATOM   6353 C CA   . ASP   B 1 157 ? 48.786 -36.360 -7.108  1.00 18.45 ?  157 ASP   B CA   1 
ATOM   6354 C C    . ASP   B 1 157 ? 47.870 -36.912 -8.195  1.00 18.17 ?  157 ASP   B C    1 
ATOM   6355 O O    . ASP   B 1 157 ? 46.645 -36.798 -8.089  1.00 17.74 ?  157 ASP   B O    1 
ATOM   6356 C CB   . ASP   B 1 157 ? 48.429 -36.967 -5.758  1.00 20.04 ?  157 ASP   B CB   1 
ATOM   6357 C CG   . ASP   B 1 157 ? 48.566 -38.475 -5.737  1.00 22.53 ?  157 ASP   B CG   1 
ATOM   6358 O OD1  . ASP   B 1 157 ? 48.922 -39.077 -6.776  1.00 22.83 ?  157 ASP   B OD1  1 
ATOM   6359 O OD2  . ASP   B 1 157 ? 48.327 -39.056 -4.663  1.00 24.74 -1 157 ASP   B OD2  1 
ATOM   6360 H H    . ASP   B 1 157 ? 48.083 -34.657 -6.409  1.00 20.73 ?  157 ASP   B H    1 
ATOM   6361 H HA   . ASP   B 1 157 ? 49.707 -36.588 -7.323  1.00 22.29 ?  157 ASP   B HA   1 
ATOM   6362 H HB2  . ASP   B 1 157 ? 49.010 -36.590 -5.080  1.00 24.20 ?  157 ASP   B HB2  1 
ATOM   6363 H HB3  . ASP   B 1 157 ? 47.504 -36.751 -5.555  1.00 24.20 ?  157 ASP   B HB3  1 
ATOM   6364 N N    . LYS   B 1 158 ? 48.458 -37.535 -9.223  1.00 19.06 ?  158 LYS   B N    1 
ATOM   6365 C CA   . LYS   B 1 158 ? 47.676 -38.133 -10.308 1.00 20.40 ?  158 LYS   B CA   1 
ATOM   6366 C C    . LYS   B 1 158 ? 46.621 -39.110 -9.790  1.00 20.28 ?  158 LYS   B C    1 
ATOM   6367 O O    . LYS   B 1 158 ? 45.520 -39.203 -10.346 1.00 20.83 ?  158 LYS   B O    1 
ATOM   6368 C CB   . LYS   B 1 158 ? 48.622 -38.838 -11.289 1.00 22.59 ?  158 LYS   B CB   1 
ATOM   6369 C CG   . LYS   B 1 158 ? 47.948 -39.752 -12.304 1.00 24.97 ?  158 LYS   B CG   1 
ATOM   6370 C CD   . LYS   B 1 158 ? 47.114 -38.982 -13.306 1.00 27.63 ?  158 LYS   B CD   1 
ATOM   6371 C CE   . LYS   B 1 158 ? 46.491 -39.921 -14.330 1.00 29.73 ?  158 LYS   B CE   1 
ATOM   6372 N NZ   . LYS   B 1 158 ? 45.430 -39.251 -15.136 1.00 30.24 ?  158 LYS   B NZ   1 
ATOM   6373 H H    . LYS   B 1 158 ? 49.312 -37.630 -9.314  1.00 23.02 ?  158 LYS   B H    1 
ATOM   6374 H HA   . LYS   B 1 158 ? 47.223 -37.426 -10.796 1.00 24.63 ?  158 LYS   B HA   1 
ATOM   6375 H HB2  . LYS   B 1 158 ? 49.110 -38.164 -11.793 1.00 27.26 ?  158 LYS   B HB2  1 
ATOM   6376 H HB3  . LYS   B 1 158 ? 49.249 -39.378 -10.785 1.00 27.26 ?  158 LYS   B HB3  1 
ATOM   6377 H HG2  . LYS   B 1 158 ? 48.634 -40.229 -12.798 1.00 30.11 ?  158 LYS   B HG2  1 
ATOM   6378 H HG3  . LYS   B 1 158 ? 47.374 -40.393 -11.852 1.00 30.11 ?  158 LYS   B HG3  1 
ATOM   6379 H HD2  . LYS   B 1 158 ? 46.399 -38.517 -12.843 1.00 33.30 ?  158 LYS   B HD2  1 
ATOM   6380 H HD3  . LYS   B 1 158 ? 47.679 -38.350 -13.777 1.00 33.30 ?  158 LYS   B HD3  1 
ATOM   6381 H HE2  . LYS   B 1 158 ? 47.178 -40.232 -14.938 1.00 35.83 ?  158 LYS   B HE2  1 
ATOM   6382 H HE3  . LYS   B 1 158 ? 46.089 -40.675 -13.870 1.00 35.83 ?  158 LYS   B HE3  1 
ATOM   6383 H HZ1  . LYS   B 1 158 ? 45.084 -39.823 -15.723 1.00 36.44 ?  158 LYS   B HZ1  1 
ATOM   6384 H HZ2  . LYS   B 1 158 ? 44.780 -38.958 -14.602 1.00 36.44 ?  158 LYS   B HZ2  1 
ATOM   6385 H HZ3  . LYS   B 1 158 ? 45.775 -38.558 -15.576 1.00 36.44 ?  158 LYS   B HZ3  1 
ATOM   6386 N N    A ASN   B 1 159 ? 46.942 -39.865 -8.737  0.86 20.26 ?  159 ASN   B N    1 
ATOM   6387 N N    B ASN   B 1 159 ? 46.943 -39.856 -8.732  0.14 19.69 ?  159 ASN   B N    1 
ATOM   6388 C CA   A ASN   B 1 159 ? 45.986 -40.845 -8.231  0.86 21.12 ?  159 ASN   B CA   1 
ATOM   6389 C CA   B ASN   B 1 159 ? 45.997 -40.844 -8.223  0.14 19.36 ?  159 ASN   B CA   1 
ATOM   6390 C C    A ASN   B 1 159 ? 44.790 -40.174 -7.554  0.86 20.04 ?  159 ASN   B C    1 
ATOM   6391 C C    B ASN   B 1 159 ? 44.804 -40.189 -7.534  0.14 19.17 ?  159 ASN   B C    1 
ATOM   6392 O O    A ASN   B 1 159 ? 43.656 -40.667 -7.659  0.86 20.50 ?  159 ASN   B O    1 
ATOM   6393 O O    B ASN   B 1 159 ? 43.688 -40.719 -7.600  0.14 19.03 ?  159 ASN   B O    1 
ATOM   6394 C CB   A ASN   B 1 159 ? 46.693 -41.831 -7.302  0.86 23.02 ?  159 ASN   B CB   1 
ATOM   6395 C CB   B ASN   B 1 159 ? 46.713 -41.824 -7.293  0.14 19.41 ?  159 ASN   B CB   1 
ATOM   6396 C CG   A ASN   B 1 159 ? 47.716 -42.681 -8.031  0.86 25.27 ?  159 ASN   B CG   1 
ATOM   6397 C CG   B ASN   B 1 159 ? 47.732 -42.680 -8.023  0.14 19.81 ?  159 ASN   B CG   1 
ATOM   6398 O OD1  A ASN   B 1 159 ? 47.462 -43.169 -9.137  0.86 25.90 ?  159 ASN   B OD1  1 
ATOM   6399 O OD1  B ASN   B 1 159 ? 47.507 -43.099 -9.160  0.14 19.92 ?  159 ASN   B OD1  1 
ATOM   6400 N ND2  A ASN   B 1 159 ? 48.881 -42.862 -7.419  0.86 26.20 ?  159 ASN   B ND2  1 
ATOM   6401 N ND2  B ASN   B 1 159 ? 48.860 -42.942 -7.374  0.14 20.04 ?  159 ASN   B ND2  1 
ATOM   6402 H H    A ASN   B 1 159 ? 47.685 -39.815 -8.310  0.86 24.46 ?  159 ASN   B H    1 
ATOM   6403 H H    B ASN   B 1 159 ? 47.686 -39.808 -8.306  0.14 23.77 ?  159 ASN   B H    1 
ATOM   6404 H HA   A ASN   B 1 159 ? 45.651 -41.350 -8.989  0.86 25.50 ?  159 ASN   B HA   1 
ATOM   6405 H HA   B ASN   B 1 159 ? 45.656 -41.355 -8.976  0.14 23.38 ?  159 ASN   B HA   1 
ATOM   6406 H HB2  A ASN   B 1 159 ? 47.153 -41.338 -6.607  0.86 27.77 ?  159 ASN   B HB2  1 
ATOM   6407 H HB2  B ASN   B 1 159 ? 47.178 -41.326 -6.605  0.14 23.45 ?  159 ASN   B HB2  1 
ATOM   6408 H HB3  A ASN   B 1 159 ? 46.035 -42.426 -6.917  0.86 27.77 ?  159 ASN   B HB3  1 
ATOM   6409 H HB3  B ASN   B 1 159 ? 46.057 -42.416 -6.894  0.14 23.45 ?  159 ASN   B HB3  1 
ATOM   6410 H HD21 A ASN   B 1 159 ? 49.496 -43.336 -7.792  0.86 31.59 ?  159 ASN   B HD21 1 
ATOM   6411 H HD21 B ASN   B 1 159 ? 49.469 -43.424 -7.746  0.14 24.20 ?  159 ASN   B HD21 1 
ATOM   6412 H HD22 A ASN   B 1 159 ? 49.018 -42.517 -6.643  0.86 31.59 ?  159 ASN   B HD22 1 
ATOM   6413 H HD22 B ASN   B 1 159 ? 48.981 -42.633 -6.582  0.14 24.20 ?  159 ASN   B HD22 1 
ATOM   6414 N N    . LEU   B 1 160 ? 45.008 -39.044 -6.875  1.00 19.41 ?  160 LEU   B N    1 
ATOM   6415 C CA   . LEU   B 1 160 ? 43.876 -38.312 -6.319  1.00 18.30 ?  160 LEU   B CA   1 
ATOM   6416 C C    . LEU   B 1 160 ? 43.082 -37.644 -7.430  1.00 17.62 ?  160 LEU   B C    1 
ATOM   6417 O O    . LEU   B 1 160 ? 41.843 -37.648 -7.410  1.00 17.22 ?  160 LEU   B O    1 
ATOM   6418 C CB   . LEU   B 1 160 ? 44.343 -37.282 -5.289  1.00 17.75 ?  160 LEU   B CB   1 
ATOM   6419 C CG   . LEU   B 1 160 ? 43.218 -36.387 -4.745  1.00 17.35 ?  160 LEU   B CG   1 
ATOM   6420 C CD1  . LEU   B 1 160 ? 42.102 -37.214 -4.116  1.00 18.50 ?  160 LEU   B CD1  1 
ATOM   6421 C CD2  . LEU   B 1 160 ? 43.760 -35.377 -3.742  1.00 17.55 ?  160 LEU   B CD2  1 
ATOM   6422 H H    A LEU   B 1 160 ? 45.781 -38.693 -6.730  0.86 23.43 ?  160 LEU   B H    1 
ATOM   6423 H H    B LEU   B 1 160 ? 45.778 -38.680 -6.748  0.14 23.43 ?  160 LEU   B H    1 
ATOM   6424 H HA   . LEU   B 1 160 ? 43.290 -38.939 -5.874  1.00 22.11 ?  160 LEU   B HA   1 
ATOM   6425 H HB2  . LEU   B 1 160 ? 44.743 -37.757 -4.540  1.00 21.44 ?  160 LEU   B HB2  1 
ATOM   6426 H HB3  . LEU   B 1 160 ? 45.012 -36.710 -5.703  1.00 21.44 ?  160 LEU   B HB3  1 
ATOM   6427 H HG   . LEU   B 1 160 ? 42.838 -35.891 -5.482  1.00 20.96 ?  160 LEU   B HG   1 
ATOM   6428 H HD11 . LEU   B 1 160 ? 41.471 -36.617 -3.691  1.00 22.35 ?  160 LEU   B HD11 1 
ATOM   6429 H HD12 . LEU   B 1 160 ? 41.655 -37.729 -4.809  1.00 22.35 ?  160 LEU   B HD12 1 
ATOM   6430 H HD13 . LEU   B 1 160 ? 42.484 -37.817 -3.456  1.00 22.35 ?  160 LEU   B HD13 1 
ATOM   6431 H HD21 . LEU   B 1 160 ? 43.033 -34.805 -3.453  1.00 21.21 ?  160 LEU   B HD21 1 
ATOM   6432 H HD22 . LEU   B 1 160 ? 44.133 -35.850 -2.983  1.00 21.21 ?  160 LEU   B HD22 1 
ATOM   6433 H HD23 . LEU   B 1 160 ? 44.449 -34.843 -4.172  1.00 21.21 ?  160 LEU   B HD23 1 
ATOM   6434 N N    . TYR   B 1 161 ? 43.779 -37.075 -8.417  1.00 17.63 ?  161 TYR   B N    1 
ATOM   6435 C CA   . TYR   B 1 161 ? 43.105 -36.500 -9.576  1.00 17.14 ?  161 TYR   B CA   1 
ATOM   6436 C C    . TYR   B 1 161 ? 42.164 -37.521 -10.204 1.00 17.13 ?  161 TYR   B C    1 
ATOM   6437 O O    . TYR   B 1 161 ? 40.999 -37.220 -10.479 1.00 17.07 ?  161 TYR   B O    1 
ATOM   6438 C CB   . TYR   B 1 161 ? 44.147 -36.017 -10.594 1.00 18.11 ?  161 TYR   B CB   1 
ATOM   6439 C CG   . TYR   B 1 161 ? 43.568 -35.549 -11.908 1.00 19.00 ?  161 TYR   B CG   1 
ATOM   6440 C CD1  . TYR   B 1 161 ? 43.167 -34.230 -12.073 1.00 18.86 ?  161 TYR   B CD1  1 
ATOM   6441 C CD2  . TYR   B 1 161 ? 43.412 -36.424 -12.981 1.00 19.56 ?  161 TYR   B CD2  1 
ATOM   6442 C CE1  . TYR   B 1 161 ? 42.636 -33.793 -13.260 1.00 20.07 ?  161 TYR   B CE1  1 
ATOM   6443 C CE2  . TYR   B 1 161 ? 42.868 -35.995 -14.172 1.00 20.60 ?  161 TYR   B CE2  1 
ATOM   6444 C CZ   . TYR   B 1 161 ? 42.484 -34.678 -14.306 1.00 20.58 ?  161 TYR   B CZ   1 
ATOM   6445 O OH   . TYR   B 1 161 ? 41.944 -34.242 -15.490 1.00 22.50 ?  161 TYR   B OH   1 
ATOM   6446 H H    . TYR   B 1 161 ? 44.634 -37.008 -8.440  1.00 21.30 ?  161 TYR   B H    1 
ATOM   6447 H HA   . TYR   B 1 161 ? 42.578 -35.736 -9.297  1.00 20.72 ?  161 TYR   B HA   1 
ATOM   6448 H HB2  . TYR   B 1 161 ? 44.636 -35.272 -10.209 1.00 21.88 ?  161 TYR   B HB2  1 
ATOM   6449 H HB3  . TYR   B 1 161 ? 44.756 -36.743 -10.788 1.00 21.88 ?  161 TYR   B HB3  1 
ATOM   6450 H HD1  . TYR   B 1 161 ? 43.269 -33.624 -11.370 1.00 22.78 ?  161 TYR   B HD1  1 
ATOM   6451 H HD2  . TYR   B 1 161 ? 43.664 -37.311 -12.891 1.00 23.62 ?  161 TYR   B HD2  1 
ATOM   6452 H HE1  . TYR   B 1 161 ? 42.376 -32.900 -13.353 1.00 24.23 ?  161 TYR   B HE1  1 
ATOM   6453 H HE2  . TYR   B 1 161 ? 42.766 -36.584 -14.884 1.00 24.86 ?  161 TYR   B HE2  1 
ATOM   6454 H HH   . TYR   B 1 161 ? 41.912 -34.873 -16.042 1.00 27.15 ?  161 TYR   B HH   1 
ATOM   6455 N N    . ASP   B 1 162 ? 42.652 -38.749 -10.415 1.00 17.50 ?  162 ASP   B N    1 
ATOM   6456 C CA   . ASP   B 1 162 ? 41.826 -39.779 -11.039 1.00 18.12 ?  162 ASP   B CA   1 
ATOM   6457 C C    . ASP   B 1 162 ? 40.616 -40.122 -10.176 1.00 17.44 ?  162 ASP   B C    1 
ATOM   6458 O O    . ASP   B 1 162 ? 39.514 -40.335 -10.696 1.00 17.93 ?  162 ASP   B O    1 
ATOM   6459 C CB   . ASP   B 1 162 ? 42.654 -41.041 -11.298 1.00 19.79 ?  162 ASP   B CB   1 
ATOM   6460 C CG   . ASP   B 1 162 ? 43.660 -40.877 -12.431 1.00 21.54 ?  162 ASP   B CG   1 
ATOM   6461 O OD1  . ASP   B 1 162 ? 43.530 -39.932 -13.231 1.00 21.77 ?  162 ASP   B OD1  1 
ATOM   6462 O OD2  . ASP   B 1 162 ? 44.566 -41.732 -12.544 1.00 23.23 -1 162 ASP   B OD2  1 
ATOM   6463 H H    . ASP   B 1 162 ? 43.447 -39.004 -10.213 1.00 21.15 ?  162 ASP   B H    1 
ATOM   6464 H HA   . ASP   B 1 162 ? 41.498 -39.453 -11.890 1.00 21.89 ?  162 ASP   B HA   1 
ATOM   6465 H HB2  . ASP   B 1 162 ? 43.144 -41.266 -10.493 1.00 23.89 ?  162 ASP   B HB2  1 
ATOM   6466 H HB3  . ASP   B 1 162 ? 42.055 -41.766 -11.537 1.00 23.89 ?  162 ASP   B HB3  1 
ATOM   6467 N N    A LYS   B 1 163 ? 40.805 -40.200 -8.858  0.86 16.96 ?  163 LYS   B N    1 
ATOM   6468 N N    B LYS   B 1 163 ? 40.796 -40.174 -8.853  0.14 18.25 ?  163 LYS   B N    1 
ATOM   6469 C CA   A LYS   B 1 163 ? 39.684 -40.473 -7.966  0.86 17.39 ?  163 LYS   B CA   1 
ATOM   6470 C CA   B LYS   B 1 163 ? 39.672 -40.476 -7.970  0.14 19.30 ?  163 LYS   B CA   1 
ATOM   6471 C C    A LYS   B 1 163 ? 38.641 -39.364 -8.033  0.86 16.38 ?  163 LYS   B C    1 
ATOM   6472 C C    B LYS   B 1 163 ? 38.637 -39.356 -7.988  0.14 17.32 ?  163 LYS   B C    1 
ATOM   6473 O O    A LYS   B 1 163 ? 37.431 -39.636 -8.046  0.86 17.48 ?  163 LYS   B O    1 
ATOM   6474 O O    B LYS   B 1 163 ? 37.430 -39.615 -7.915  0.14 17.37 ?  163 LYS   B O    1 
ATOM   6475 C CB   A LYS   B 1 163 ? 40.176 -40.652 -6.532  0.86 19.96 ?  163 LYS   B CB   1 
ATOM   6476 C CB   B LYS   B 1 163 ? 40.172 -40.723 -6.547  0.14 22.44 ?  163 LYS   B CB   1 
ATOM   6477 C CG   A LYS   B 1 163 ? 39.084 -41.148 -5.607  0.86 25.23 ?  163 LYS   B CG   1 
ATOM   6478 C CG   B LYS   B 1 163 ? 39.092 -41.237 -5.613  0.14 25.75 ?  163 LYS   B CG   1 
ATOM   6479 C CD   A LYS   B 1 163 ? 39.533 -41.279 -4.165  0.86 30.08 ?  163 LYS   B CD   1 
ATOM   6480 C CD   B LYS   B 1 163 ? 39.598 -41.419 -4.194  0.14 29.03 ?  163 LYS   B CD   1 
ATOM   6481 C CE   A LYS   B 1 163 ? 38.450 -41.965 -3.340  0.86 33.56 ?  163 LYS   B CE   1 
ATOM   6482 C CE   B LYS   B 1 163 ? 38.541 -42.103 -3.341  0.14 31.42 ?  163 LYS   B CE   1 
ATOM   6483 N NZ   A LYS   B 1 163 ? 38.520 -41.628 -1.891  0.86 35.71 ?  163 LYS   B NZ   1 
ATOM   6484 N NZ   B LYS   B 1 163 ? 38.652 -41.742 -1.903  0.14 32.37 ?  163 LYS   B NZ   1 
ATOM   6485 H H    A LYS   B 1 163 ? 41.564 -40.098 -8.464  0.86 20.49 ?  163 LYS   B H    1 
ATOM   6486 H H    B LYS   B 1 163 ? 41.546 -40.045 -8.451  0.14 22.05 ?  163 LYS   B H    1 
ATOM   6487 H HA   A LYS   B 1 163 ? 39.260 -41.297 -8.241  0.86 21.02 ?  163 LYS   B HA   1 
ATOM   6488 H HA   B LYS   B 1 163 ? 39.237 -41.285 -8.277  0.14 23.31 ?  163 LYS   B HA   1 
ATOM   6489 H HB2  A LYS   B 1 163 ? 40.898 -41.304 -6.524  0.86 24.10 ?  163 LYS   B HB2  1 
ATOM   6490 H HB2  B LYS   B 1 163 ? 40.882 -41.385 -6.571  0.14 27.07 ?  163 LYS   B HB2  1 
ATOM   6491 H HB3  A LYS   B 1 163 ? 40.495 -39.802 -6.194  0.86 24.10 ?  163 LYS   B HB3  1 
ATOM   6492 H HB3  B LYS   B 1 163 ? 40.510 -39.891 -6.179  0.14 27.07 ?  163 LYS   B HB3  1 
ATOM   6493 H HG2  A LYS   B 1 163 ? 38.341 -40.527 -5.631  0.86 30.43 ?  163 LYS   B HG2  1 
ATOM   6494 H HG2  B LYS   B 1 163 ? 38.360 -40.601 -5.590  0.14 31.05 ?  163 LYS   B HG2  1 
ATOM   6495 H HG3  A LYS   B 1 163 ? 38.791 -42.024 -5.909  0.86 30.43 ?  163 LYS   B HG3  1 
ATOM   6496 H HG3  B LYS   B 1 163 ? 38.778 -42.097 -5.934  0.14 31.05 ?  163 LYS   B HG3  1 
ATOM   6497 H HD2  A LYS   B 1 163 ? 40.339 -41.818 -4.123  0.86 36.25 ?  163 LYS   B HD2  1 
ATOM   6498 H HD2  B LYS   B 1 163 ? 40.395 -41.974 -4.201  0.14 34.98 ?  163 LYS   B HD2  1 
ATOM   6499 H HD3  A LYS   B 1 163 ? 39.693 -40.398 -3.794  0.86 36.25 ?  163 LYS   B HD3  1 
ATOM   6500 H HD3  B LYS   B 1 163 ? 39.794 -40.552 -3.804  0.14 34.98 ?  163 LYS   B HD3  1 
ATOM   6501 H HE2  A LYS   B 1 163 ? 37.578 -41.702 -3.673  0.86 40.42 ?  163 LYS   B HE2  1 
ATOM   6502 H HE2  B LYS   B 1 163 ? 37.662 -41.839 -3.655  0.14 37.85 ?  163 LYS   B HE2  1 
ATOM   6503 H HE3  A LYS   B 1 163 ? 38.555 -42.924 -3.426  0.86 40.42 ?  163 LYS   B HE3  1 
ATOM   6504 H HE3  B LYS   B 1 163 ? 38.646 -43.065 -3.420  0.14 37.85 ?  163 LYS   B HE3  1 
ATOM   6505 H HZ1  A LYS   B 1 163 ? 37.870 -42.048 -1.450  0.86 43.00 ?  163 LYS   B HZ1  1 
ATOM   6506 H HZ1  B LYS   B 1 163 ? 38.019 -42.158 -1.436  0.14 38.99 ?  163 LYS   B HZ1  1 
ATOM   6507 H HZ2  A LYS   B 1 163 ? 39.305 -41.880 -1.558  0.86 43.00 ?  163 LYS   B HZ2  1 
ATOM   6508 H HZ2  B LYS   B 1 163 ? 39.449 -41.981 -1.590  0.14 38.99 ?  163 LYS   B HZ2  1 
ATOM   6509 H HZ3  A LYS   B 1 163 ? 38.425 -40.750 -1.778  0.86 43.00 ?  163 LYS   B HZ3  1 
ATOM   6510 H HZ3  B LYS   B 1 163 ? 38.553 -40.862 -1.804  0.14 38.99 ?  163 LYS   B HZ3  1 
ATOM   6511 N N    . LEU   B 1 164 ? 39.093 -38.106 -8.081  1.00 15.58 ?  164 LEU   B N    1 
ATOM   6512 C CA   . LEU   B 1 164 ? 38.181 -36.966 -8.131  1.00 15.22 ?  164 LEU   B CA   1 
ATOM   6513 C C    . LEU   B 1 164 ? 37.394 -36.948 -9.437  1.00 15.11 ?  164 LEU   B C    1 
ATOM   6514 O O    . LEU   B 1 164 ? 36.172 -36.739 -9.437  1.00 16.25 ?  164 LEU   B O    1 
ATOM   6515 C CB   . LEU   B 1 164 ? 38.984 -35.670 -7.967  1.00 14.61 ?  164 LEU   B CB   1 
ATOM   6516 C CG   . LEU   B 1 164 ? 39.529 -35.399 -6.571  1.00 15.79 ?  164 LEU   B CG   1 
ATOM   6517 C CD1  . LEU   B 1 164 ? 40.618 -34.343 -6.638  1.00 15.94 ?  164 LEU   B CD1  1 
ATOM   6518 C CD2  . LEU   B 1 164 ? 38.426 -34.968 -5.621  1.00 17.65 ?  164 LEU   B CD2  1 
ATOM   6519 H H    A LEU   B 1 164 ? 39.931 -37.886 -8.086  0.86 18.85 ?  164 LEU   B H    1 
ATOM   6520 H H    B LEU   B 1 164 ? 39.931 -37.891 -8.123  0.14 18.85 ?  164 LEU   B H    1 
ATOM   6521 H HA   . LEU   B 1 164 ? 37.555 -37.027 -7.401  1.00 18.41 ?  164 LEU   B HA   1 
ATOM   6522 H HB2  . LEU   B 1 164 ? 39.746 -35.700 -8.572  1.00 17.68 ?  164 LEU   B HB2  1 
ATOM   6523 H HB3  . LEU   B 1 164 ? 38.416 -34.923 -8.207  1.00 17.68 ?  164 LEU   B HB3  1 
ATOM   6524 H HG   . LEU   B 1 164 ? 39.924 -36.211 -6.225  1.00 19.10 ?  164 LEU   B HG   1 
ATOM   6525 H HD11 . LEU   B 1 164 ? 40.949 -34.167 -5.742  1.00 19.28 ?  164 LEU   B HD11 1 
ATOM   6526 H HD12 . LEU   B 1 164 ? 41.347 -34.669 -7.196  1.00 19.28 ?  164 LEU   B HD12 1 
ATOM   6527 H HD13 . LEU   B 1 164 ? 40.256 -33.528 -7.020  1.00 19.28 ?  164 LEU   B HD13 1 
ATOM   6528 H HD21 . LEU   B 1 164 ? 38.814 -34.761 -4.758  1.00 21.32 ?  164 LEU   B HD21 1 
ATOM   6529 H HD22 . LEU   B 1 164 ? 37.983 -34.185 -5.982  1.00 21.32 ?  164 LEU   B HD22 1 
ATOM   6530 H HD23 . LEU   B 1 164 ? 37.787 -35.695 -5.531  1.00 21.32 ?  164 LEU   B HD23 1 
ATOM   6531 N N    . VAL   B 1 165 ? 38.080 -37.132 -10.565 1.00 16.79 ?  165 VAL   B N    1 
ATOM   6532 C CA   . VAL   B 1 165 ? 37.421 -37.059 -11.866 1.00 18.10 ?  165 VAL   B CA   1 
ATOM   6533 C C    . VAL   B 1 165 ? 36.503 -38.258 -12.058 1.00 20.06 ?  165 VAL   B C    1 
ATOM   6534 O O    . VAL   B 1 165 ? 35.344 -38.124 -12.475 1.00 21.04 ?  165 VAL   B O    1 
ATOM   6535 C CB   . VAL   B 1 165 ? 38.461 -36.965 -12.997 1.00 19.32 ?  165 VAL   B CB   1 
ATOM   6536 C CG1  . VAL   B 1 165 ? 37.785 -37.059 -14.348 1.00 20.88 ?  165 VAL   B CG1  1 
ATOM   6537 C CG2  . VAL   B 1 165 ? 39.259 -35.676 -12.886 1.00 19.24 ?  165 VAL   B CG2  1 
ATOM   6538 H H    . VAL   B 1 165 ? 38.927 -37.290 -10.605 1.00 20.30 ?  165 VAL   B H    1 
ATOM   6539 H HA   . VAL   B 1 165 ? 36.877 -36.259 -11.900 1.00 21.86 ?  165 VAL   B HA   1 
ATOM   6540 H HB   . VAL   B 1 165 ? 39.086 -37.701 -12.920 1.00 23.33 ?  165 VAL   B HB   1 
ATOM   6541 H HG11 . VAL   B 1 165 ? 38.393 -36.740 -15.030 1.00 25.21 ?  165 VAL   B HG11 1 
ATOM   6542 H HG12 . VAL   B 1 165 ? 37.559 -37.988 -14.519 1.00 25.21 ?  165 VAL   B HG12 1 
ATOM   6543 H HG13 . VAL   B 1 165 ? 36.982 -36.518 -14.338 1.00 25.21 ?  165 VAL   B HG13 1 
ATOM   6544 H HG21 . VAL   B 1 165 ? 39.894 -35.628 -13.620 1.00 23.23 ?  165 VAL   B HG21 1 
ATOM   6545 H HG22 . VAL   B 1 165 ? 38.650 -34.920 -12.930 1.00 23.23 ?  165 VAL   B HG22 1 
ATOM   6546 H HG23 . VAL   B 1 165 ? 39.734 -35.666 -12.039 1.00 23.23 ?  165 VAL   B HG23 1 
ATOM   6547 N N    . SER   B 1 166 ? 37.017 -39.456 -11.767 1.00 20.95 ?  166 SER   B N    1 
ATOM   6548 C CA   . SER   B 1 166 ? 36.257 -40.665 -12.047 1.00 22.21 ?  166 SER   B CA   1 
ATOM   6549 C C    . SER   B 1 166 ? 35.000 -40.746 -11.193 1.00 22.34 ?  166 SER   B C    1 
ATOM   6550 O O    . SER   B 1 166 ? 34.020 -41.359 -11.616 1.00 23.95 ?  166 SER   B O    1 
ATOM   6551 C CB   . SER   B 1 166 ? 37.127 -41.922 -11.894 1.00 23.18 ?  166 SER   B CB   1 
ATOM   6552 O OG   . SER   B 1 166 ? 37.503 -42.153 -10.546 1.00 22.94 ?  166 SER   B OG   1 
ATOM   6553 H H    . SER   B 1 166 ? 37.801 -39.589 -11.427 1.00 25.29 ?  166 SER   B H    1 
ATOM   6554 H HA   . SER   B 1 166 ? 35.975 -40.637 -12.973 1.00 26.79 ?  166 SER   B HA   1 
ATOM   6555 H HB2  . SER   B 1 166 ? 36.628 -42.690 -12.213 1.00 27.96 ?  166 SER   B HB2  1 
ATOM   6556 H HB3  . SER   B 1 166 ? 37.932 -41.814 -12.433 1.00 27.96 ?  166 SER   B HB3  1 
ATOM   6557 H HG   . SER   B 1 166 ? 37.958 -41.507 -10.262 1.00 27.68 ?  166 SER   B HG   1 
ATOM   6558 N N    . SER   B 1 167 ? 34.986 -40.126 -10.014 1.00 21.02 ?  167 SER   B N    1 
ATOM   6559 C CA   . SER   B 1 167 ? 33.834 -40.183 -9.122  1.00 21.12 ?  167 SER   B CA   1 
ATOM   6560 C C    . SER   B 1 167 ? 32.919 -38.960 -9.213  1.00 20.56 ?  167 SER   B C    1 
ATOM   6561 O O    . SER   B 1 167 ? 31.843 -38.965 -8.600  1.00 20.56 ?  167 SER   B O    1 
ATOM   6562 C CB   . SER   B 1 167 ? 34.285 -40.374 -7.668  1.00 20.68 ?  167 SER   B CB   1 
ATOM   6563 O OG   . SER   B 1 167 ? 34.951 -39.214 -7.189  1.00 20.41 ?  167 SER   B OG   1 
ATOM   6564 H H    . SER   B 1 167 ? 35.641 -39.667 -9.707  1.00 25.38 ?  167 SER   B H    1 
ATOM   6565 H HA   . SER   B 1 167 ? 33.303 -40.960 -9.364  1.00 25.49 ?  167 SER   B HA   1 
ATOM   6566 H HB2  . SER   B 1 167 ? 33.502 -40.542 -7.119  1.00 24.97 ?  167 SER   B HB2  1 
ATOM   6567 H HB3  . SER   B 1 167 ? 34.886 -41.138 -7.624  1.00 24.97 ?  167 SER   B HB3  1 
ATOM   6568 H HG   . SER   B 1 167 ? 35.636 -39.071 -7.656  1.00 24.64 ?  167 SER   B HG   1 
ATOM   6569 N N    . PHE   B 1 168 ? 33.299 -37.923 -9.964  1.00 20.02 ?  168 PHE   B N    1 
ATOM   6570 C CA   . PHE   B 1 168 ? 32.470 -36.720 -10.030 1.00 19.45 ?  168 PHE   B CA   1 
ATOM   6571 C C    . PHE   B 1 168 ? 31.152 -36.986 -10.756 1.00 17.11 ?  168 PHE   B C    1 
ATOM   6572 O O    . PHE   B 1 168 ? 30.110 -36.397 -10.411 1.00 17.65 ?  168 PHE   B O    1 
ATOM   6573 C CB   . PHE   B 1 168 ? 33.234 -35.579 -10.705 1.00 20.02 ?  168 PHE   B CB   1 
ATOM   6574 C CG   . PHE   B 1 168 ? 32.427 -34.329 -10.842 1.00 19.92 ?  168 PHE   B CG   1 
ATOM   6575 C CD1  . PHE   B 1 168 ? 32.090 -33.590 -9.717  1.00 21.32 ?  168 PHE   B CD1  1 
ATOM   6576 C CD2  . PHE   B 1 168 ? 31.974 -33.908 -12.077 1.00 19.39 ?  168 PHE   B CD2  1 
ATOM   6577 C CE1  . PHE   B 1 168 ? 31.322 -32.446 -9.819  1.00 21.82 ?  168 PHE   B CE1  1 
ATOM   6578 C CE2  . PHE   B 1 168 ? 31.215 -32.746 -12.196 1.00 20.50 ?  168 PHE   B CE2  1 
ATOM   6579 C CZ   . PHE   B 1 168 ? 30.883 -32.015 -11.062 1.00 20.97 ?  168 PHE   B CZ   1 
ATOM   6580 H H    . PHE   B 1 168 ? 34.024 -37.892 -10.434 1.00 24.17 ?  168 PHE   B H    1 
ATOM   6581 H HA   . PHE   B 1 168 ? 32.258 -36.441 -9.131  1.00 23.49 ?  168 PHE   B HA   1 
ATOM   6582 H HB2  . PHE   B 1 168 ? 34.017 -35.365 -10.172 1.00 24.17 ?  168 PHE   B HB2  1 
ATOM   6583 H HB3  . PHE   B 1 168 ? 33.504 -35.856 -11.593 1.00 24.17 ?  168 PHE   B HB3  1 
ATOM   6584 H HD1  . PHE   B 1 168 ? 32.378 -33.881 -8.881  1.00 25.73 ?  168 PHE   B HD1  1 
ATOM   6585 H HD2  . PHE   B 1 168 ? 32.192 -34.392 -12.839 1.00 23.41 ?  168 PHE   B HD2  1 
ATOM   6586 H HE1  . PHE   B 1 168 ? 31.106 -31.964 -9.054  1.00 26.34 ?  168 PHE   B HE1  1 
ATOM   6587 H HE2  . PHE   B 1 168 ? 30.915 -32.468 -13.033 1.00 24.75 ?  168 PHE   B HE2  1 
ATOM   6588 H HZ   . PHE   B 1 168 ? 30.366 -31.244 -11.138 1.00 25.31 ?  168 PHE   B HZ   1 
ATOM   6589 N N    . LEU   B 1 169 ? 31.183 -37.860 -11.758 1.00 18.03 ?  169 LEU   B N    1 
ATOM   6590 C CA   . LEU   B 1 169 ? 30.007 -38.170 -12.561 1.00 20.62 ?  169 LEU   B CA   1 
ATOM   6591 C C    . LEU   B 1 169 ? 29.996 -39.617 -13.044 1.00 23.79 ?  169 LEU   B C    1 
ATOM   6592 O O    . LEU   B 1 169 ? 29.103 -40.051 -13.774 1.00 26.28 ?  169 LEU   B O    1 
ATOM   6593 C CB   . LEU   B 1 169 ? 29.935 -37.239 -13.771 1.00 22.57 ?  169 LEU   B CB   1 
ATOM   6594 C CG   . LEU   B 1 169 ? 28.675 -36.377 -13.863 1.00 25.95 ?  169 LEU   B CG   1 
ATOM   6595 C CD1  . LEU   B 1 169 ? 28.618 -35.677 -15.207 1.00 27.16 ?  169 LEU   B CD1  1 
ATOM   6596 C CD2  . LEU   B 1 169 ? 27.414 -37.194 -13.627 1.00 26.30 ?  169 LEU   B CD2  1 
ATOM   6597 O OXT  . LEU   B 1 169 ? 30.897 -40.383 -12.726 1.00 24.64 -1 169 LEU   B OXT  1 
ATOM   6598 H H    . LEU   B 1 169 ? 31.889 -38.286 -12.007 1.00 21.79 ?  169 LEU   B H    1 
ATOM   6599 H HA   . LEU   B 1 169 ? 29.221 -38.024 -12.018 1.00 24.89 ?  169 LEU   B HA   1 
ATOM   6600 H HB2  . LEU   B 1 169 ? 30.696 -36.636 -13.746 1.00 27.23 ?  169 LEU   B HB2  1 
ATOM   6601 H HB3  . LEU   B 1 169 ? 29.975 -37.773 -14.581 1.00 27.23 ?  169 LEU   B HB3  1 
ATOM   6602 H HG   . LEU   B 1 169 ? 28.716 -35.690 -13.177 1.00 31.29 ?  169 LEU   B HG   1 
ATOM   6603 H HD11 . LEU   B 1 169 ? 27.828 -35.115 -15.237 1.00 32.74 ?  169 LEU   B HD11 1 
ATOM   6604 H HD12 . LEU   B 1 169 ? 29.415 -35.134 -15.313 1.00 32.74 ?  169 LEU   B HD12 1 
ATOM   6605 H HD13 . LEU   B 1 169 ? 28.576 -36.346 -15.907 1.00 32.74 ?  169 LEU   B HD13 1 
ATOM   6606 H HD21 . LEU   B 1 169 ? 26.665 -36.754 -14.054 1.00 31.71 ?  169 LEU   B HD21 1 
ATOM   6607 H HD22 . LEU   B 1 169 ? 27.538 -38.080 -14.007 1.00 31.71 ?  169 LEU   B HD22 1 
ATOM   6608 H HD23 . LEU   B 1 169 ? 27.258 -37.264 -12.673 1.00 31.71 ?  169 LEU   B HD23 1 
HETATM 6609 N N2   B A1BBU C 2 .   ? 14.840 0.139   4.058   0.14 16.65 ?  201 A1BBU A N2   1 
HETATM 6610 C C3   B A1BBU C 2 .   ? 12.080 1.473   0.983   0.14 19.50 ?  201 A1BBU A C3   1 
HETATM 6611 C C6   B A1BBU C 2 .   ? 15.021 0.545   -0.215  0.14 19.02 ?  201 A1BBU A C6   1 
HETATM 6612 C C9   B A1BBU C 2 .   ? 14.954 1.350   3.456   0.14 16.62 ?  201 A1BBU A C9   1 
HETATM 6613 C C12  B A1BBU C 2 .   ? 15.212 2.510   4.262   0.14 15.33 ?  201 A1BBU A C12  1 
HETATM 6614 C C14  B A1BBU C 2 .   ? 15.627 4.491   5.331   0.14 13.57 ?  201 A1BBU A C14  1 
HETATM 6615 C C1   B A1BBU C 2 .   ? 12.460 -0.595  -0.344  0.14 19.32 ?  201 A1BBU A C1   1 
HETATM 6616 C C10  B A1BBU C 2 .   ? 14.970 0.081   5.428   0.14 16.19 ?  201 A1BBU A C10  1 
HETATM 6617 C C11  B A1BBU C 2 .   ? 15.326 2.285   5.670   0.14 15.01 ?  201 A1BBU A C11  1 
HETATM 6618 C C13  B A1BBU C 2 .   ? 15.412 3.919   4.092   0.14 14.65 ?  201 A1BBU A C13  1 
HETATM 6619 C C2   B A1BBU C 2 .   ? 12.785 0.121   0.981   0.14 19.36 ?  201 A1BBU A C2   1 
HETATM 6620 C C4   B A1BBU C 2 .   ? 12.276 -0.754  2.119   0.14 19.46 ?  201 A1BBU A C4   1 
HETATM 6621 C C5   B A1BBU C 2 .   ? 14.316 0.315   1.153   0.14 18.93 ?  201 A1BBU A C5   1 
HETATM 6622 C C7   B A1BBU C 2 .   ? 15.622 1.916   -0.176  0.14 19.00 ?  201 A1BBU A C7   1 
HETATM 6623 C C8   B A1BBU C 2 .   ? 15.819 2.214   1.297   0.14 18.65 ?  201 A1BBU A C8   1 
HETATM 6624 N N1   B A1BBU C 2 .   ? 14.825 1.412   2.029   0.14 18.09 ?  201 A1BBU A N1   1 
HETATM 6625 N N3   B A1BBU C 2 .   ? 15.206 1.077   6.284   0.14 15.67 ?  201 A1BBU A N3   1 
HETATM 6626 N N4   B A1BBU C 2 .   ? 15.576 3.499   6.310   0.14 14.32 ?  201 A1BBU A N4   1 
HETATM 6627 H H7   B A1BBU C 2 .   ? 12.288 2.059   0.079   0.14 23.55 ?  201 A1BBU A H7   1 
HETATM 6628 H H6   B A1BBU C 2 .   ? 12.378 2.110   1.827   0.14 23.55 ?  201 A1BBU A H6   1 
HETATM 6629 H H5   B A1BBU C 2 .   ? 10.994 1.354   1.048   0.14 23.55 ?  201 A1BBU A H5   1 
HETATM 6630 H H12  B A1BBU C 2 .   ? 15.774 -0.242  -0.356  0.14 22.98 ?  201 A1BBU A H12  1 
HETATM 6631 H H11  B A1BBU C 2 .   ? 14.427 0.464   -1.122  0.14 22.98 ?  201 A1BBU A H11  1 
HETATM 6632 H H19  B A1BBU C 2 .   ? 15.802 5.537   5.595   0.14 16.43 ?  201 A1BBU A H19  1 
HETATM 6633 H H2   B A1BBU C 2 .   ? 12.379 0.093   -1.206  0.14 23.33 ?  201 A1BBU A H2   1 
HETATM 6634 H H3   B A1BBU C 2 .   ? 11.530 -1.133  -0.306  0.14 23.33 ?  201 A1BBU A H3   1 
HETATM 6635 H H4   B A1BBU C 2 .   ? 13.214 -1.358  -0.626  0.14 23.33 ?  201 A1BBU A H4   1 
HETATM 6636 H H17  B A1BBU C 2 .   ? 14.873 -0.902  5.935   0.14 19.58 ?  201 A1BBU A H17  1 
HETATM 6637 H H18  B A1BBU C 2 .   ? 15.391 4.430   3.162   0.14 17.73 ?  201 A1BBU A H18  1 
HETATM 6638 H H8   B A1BBU C 2 .   ? 11.258 -1.111  1.943   0.14 23.50 ?  201 A1BBU A H8   1 
HETATM 6639 H H10  B A1BBU C 2 .   ? 12.248 -0.219  3.069   0.14 23.50 ?  201 A1BBU A H10  1 
HETATM 6640 H H9   B A1BBU C 2 .   ? 12.907 -1.637  2.293   0.14 23.50 ?  201 A1BBU A H9   1 
HETATM 6641 H H1   B A1BBU C 2 .   ? 14.734 -0.622  1.630   0.14 22.86 ?  201 A1BBU A H1   1 
HETATM 6642 H H13  B A1BBU C 2 .   ? 14.974 2.655   -0.686  0.14 22.95 ?  201 A1BBU A H13  1 
HETATM 6643 H H14  B A1BBU C 2 .   ? 16.557 1.944   -0.742  0.14 22.95 ?  201 A1BBU A H14  1 
HETATM 6644 H H16  B A1BBU C 2 .   ? 15.814 3.300   1.487   0.14 22.53 ?  201 A1BBU A H16  1 
HETATM 6645 H H15  B A1BBU C 2 .   ? 16.815 1.854   1.603   0.14 22.53 ?  201 A1BBU A H15  1 
HETATM 6646 H H20  B A1BBU C 2 .   ? 15.692 3.613   7.293   0.14 17.33 ?  201 A1BBU A H20  1 
HETATM 6647 O O    . HOH   D 3 .   ? 17.559 -1.692  0.450   1.00 19.66 ?  301 HOH   A O    1 
HETATM 6648 O O    . HOH   D 3 .   ? 4.778  3.875   0.692   1.00 26.98 ?  302 HOH   A O    1 
HETATM 6649 O O    . HOH   D 3 .   ? 14.809 -4.816  20.547  1.00 42.97 ?  303 HOH   A O    1 
HETATM 6650 O O    . HOH   D 3 .   ? 10.493 -22.207 -1.269  1.00 46.46 ?  304 HOH   A O    1 
HETATM 6651 O O    . HOH   D 3 .   ? 7.717  -6.221  -6.612  1.00 40.80 ?  305 HOH   A O    1 
HETATM 6652 O O    . HOH   D 3 .   ? 26.864 11.419  1.661   1.00 17.88 ?  306 HOH   A O    1 
HETATM 6653 O O    . HOH   D 3 .   ? 12.183 0.293   14.941  1.00 35.22 ?  307 HOH   A O    1 
HETATM 6654 O O    . HOH   D 3 .   ? 3.619  -9.391  10.004  1.00 37.36 ?  308 HOH   A O    1 
HETATM 6655 O O    . HOH   D 3 .   ? 15.233 -12.254 18.792  1.00 35.03 ?  309 HOH   A O    1 
HETATM 6656 O O    . HOH   D 3 .   ? 9.054  -10.181 19.375  1.00 43.60 ?  310 HOH   A O    1 
HETATM 6657 O O    . HOH   D 3 .   ? 34.481 -1.838  12.510  1.00 40.79 ?  311 HOH   A O    1 
HETATM 6658 O O    . HOH   D 3 .   ? 28.950 0.478   -9.753  1.00 22.86 ?  312 HOH   A O    1 
HETATM 6659 O O    . HOH   D 3 .   ? 6.948  -8.187  11.897  1.00 22.38 ?  313 HOH   A O    1 
HETATM 6660 O O    A HOH   D 3 .   ? 28.264 -0.198  -13.318 0.86 34.43 ?  314 HOH   A O    1 
HETATM 6661 O O    . HOH   D 3 .   ? 19.931 -12.544 -8.963  1.00 27.70 ?  315 HOH   A O    1 
HETATM 6662 O O    . HOH   D 3 .   ? 18.701 -19.424 13.545  1.00 35.56 ?  316 HOH   A O    1 
HETATM 6663 O O    . HOH   D 3 .   ? 42.465 10.569  5.155   1.00 21.09 ?  317 HOH   A O    1 
HETATM 6664 O O    . HOH   D 3 .   ? 14.783 -14.026 16.748  1.00 25.03 ?  318 HOH   A O    1 
HETATM 6665 O O    . HOH   D 3 .   ? 28.363 -6.380  19.621  1.00 44.41 ?  319 HOH   A O    1 
HETATM 6666 O O    . HOH   D 3 .   ? 30.299 -13.322 -8.571  1.00 24.39 ?  320 HOH   A O    1 
HETATM 6667 O O    . HOH   D 3 .   ? 36.192 -5.090  -0.569  1.00 29.92 ?  321 HOH   A O    1 
HETATM 6668 O O    . HOH   D 3 .   ? 0.728  -4.493  0.329   1.00 33.91 ?  322 HOH   A O    1 
HETATM 6669 O O    . HOH   D 3 .   ? 7.971  -12.621 -0.834  1.00 22.36 ?  323 HOH   A O    1 
HETATM 6670 O O    . HOH   D 3 .   ? 17.151 -18.088 15.089  1.00 26.42 ?  324 HOH   A O    1 
HETATM 6671 O O    . HOH   D 3 .   ? 27.952 0.832   -7.187  1.00 15.53 ?  325 HOH   A O    1 
HETATM 6672 O O    . HOH   D 3 .   ? 37.600 2.839   10.238  1.00 29.12 ?  326 HOH   A O    1 
HETATM 6673 O O    . HOH   D 3 .   ? 34.043 -0.995  -8.931  1.00 28.80 ?  327 HOH   A O    1 
HETATM 6674 O O    . HOH   D 3 .   ? 31.070 -18.166 7.757   1.00 20.67 ?  328 HOH   A O    1 
HETATM 6675 O O    . HOH   D 3 .   ? 26.552 -19.361 -1.809  1.00 15.29 ?  329 HOH   A O    1 
HETATM 6676 O O    . HOH   D 3 .   ? 38.309 10.128  7.140   1.00 43.07 ?  330 HOH   A O    1 
HETATM 6677 O O    . HOH   D 3 .   ? 18.967 -22.001 6.873   1.00 34.85 ?  331 HOH   A O    1 
HETATM 6678 O O    . HOH   D 3 .   ? 14.123 -4.518  -11.858 1.00 31.68 ?  332 HOH   A O    1 
HETATM 6679 O O    . HOH   D 3 .   ? 11.635 -10.838 -10.096 1.00 42.10 ?  333 HOH   A O    1 
HETATM 6680 O O    . HOH   D 3 .   ? 22.279 -19.395 11.326  1.00 32.93 ?  334 HOH   A O    1 
HETATM 6681 O O    . HOH   D 3 .   ? 20.672 -19.801 -5.059  1.00 31.89 ?  335 HOH   A O    1 
HETATM 6682 O O    . HOH   D 3 .   ? 8.165  -21.605 3.967   1.00 49.19 ?  336 HOH   A O    1 
HETATM 6683 O O    . HOH   D 3 .   ? 22.464 5.341   19.096  1.00 42.20 ?  337 HOH   A O    1 
HETATM 6684 O O    . HOH   D 3 .   ? 24.611 1.987   -7.040  1.00 20.63 ?  338 HOH   A O    1 
HETATM 6685 O O    . HOH   D 3 .   ? 27.339 13.797  2.897   1.00 30.77 ?  339 HOH   A O    1 
HETATM 6686 O O    . HOH   D 3 .   ? 21.252 -2.396  -2.107  1.00 16.90 ?  340 HOH   A O    1 
HETATM 6687 O O    . HOH   D 3 .   ? 38.618 4.951   6.970   1.00 16.79 ?  341 HOH   A O    1 
HETATM 6688 O O    . HOH   D 3 .   ? 21.386 3.140   -0.317  1.00 14.94 ?  342 HOH   A O    1 
HETATM 6689 O O    . HOH   D 3 .   ? 24.074 -2.107  -2.076  1.00 12.13 ?  343 HOH   A O    1 
HETATM 6690 O O    . HOH   D 3 .   ? 17.201 -17.866 -5.066  1.00 28.97 ?  344 HOH   A O    1 
HETATM 6691 O O    . HOH   D 3 .   ? 30.945 6.217   -12.343 1.00 31.29 ?  345 HOH   A O    1 
HETATM 6692 O O    . HOH   D 3 .   ? 15.567 11.974  7.978   1.00 33.77 ?  346 HOH   A O    1 
HETATM 6693 O O    . HOH   D 3 .   ? 15.099 3.859   17.836  1.00 40.74 ?  347 HOH   A O    1 
HETATM 6694 O O    . HOH   D 3 .   ? 31.745 8.186   14.883  1.00 25.52 ?  348 HOH   A O    1 
HETATM 6695 O O    . HOH   D 3 .   ? 35.847 -12.699 6.818   1.00 16.61 ?  349 HOH   A O    1 
HETATM 6696 O O    . HOH   D 3 .   ? 31.120 -13.966 -2.511  1.00 15.13 ?  350 HOH   A O    1 
HETATM 6697 O O    . HOH   D 3 .   ? 44.399 7.131   6.480   1.00 28.19 ?  351 HOH   A O    1 
HETATM 6698 O O    . HOH   D 3 .   ? 8.894  -12.116 17.232  1.00 43.05 ?  352 HOH   A O    1 
HETATM 6699 O O    A HOH   D 3 .   ? 14.333 0.533   6.833   0.86 21.21 ?  353 HOH   A O    1 
HETATM 6700 O O    . HOH   D 3 .   ? 39.827 -0.995  -5.221  1.00 21.44 ?  354 HOH   A O    1 
HETATM 6701 O O    . HOH   D 3 .   ? -0.582 -8.495  2.201   1.00 44.21 ?  355 HOH   A O    1 
HETATM 6702 O O    . HOH   D 3 .   ? 42.658 4.277   5.400   1.00 34.72 ?  356 HOH   A O    1 
HETATM 6703 O O    . HOH   D 3 .   ? 9.910  -21.408 5.727   1.00 20.53 ?  357 HOH   A O    1 
HETATM 6704 O O    . HOH   D 3 .   ? 33.710 -7.157  4.262   1.00 17.88 ?  358 HOH   A O    1 
HETATM 6705 O O    . HOH   D 3 .   ? 18.578 9.457   9.028   1.00 22.83 ?  359 HOH   A O    1 
HETATM 6706 O O    . HOH   D 3 .   ? 31.886 -9.337  -6.698  1.00 23.16 ?  360 HOH   A O    1 
HETATM 6707 O O    . HOH   D 3 .   ? 37.386 11.957  4.970   1.00 32.54 ?  361 HOH   A O    1 
HETATM 6708 O O    A HOH   D 3 .   ? -0.422 -3.130  3.139   0.86 36.04 ?  362 HOH   A O    1 
HETATM 6709 O O    A HOH   D 3 .   ? 14.691 -3.688  3.123   0.86 18.15 ?  363 HOH   A O    1 
HETATM 6710 O O    . HOH   D 3 .   ? 30.870 3.083   8.276   1.00 13.26 ?  364 HOH   A O    1 
HETATM 6711 O O    . HOH   D 3 .   ? 13.568 -15.280 -7.554  1.00 29.93 ?  365 HOH   A O    1 
HETATM 6712 O O    . HOH   D 3 .   ? 14.377 -21.275 -4.288  1.00 31.00 ?  366 HOH   A O    1 
HETATM 6713 O O    . HOH   D 3 .   ? 22.782 12.525  1.634   1.00 16.45 ?  367 HOH   A O    1 
HETATM 6714 O O    . HOH   D 3 .   ? 21.931 -21.968 8.422   1.00 30.43 ?  368 HOH   A O    1 
HETATM 6715 O O    . HOH   D 3 .   ? 37.285 -2.859  9.744   1.00 42.32 ?  369 HOH   A O    1 
HETATM 6716 O O    . HOH   D 3 .   ? 27.566 -10.650 14.065  1.00 18.16 ?  370 HOH   A O    1 
HETATM 6717 O O    . HOH   D 3 .   ? 13.317 -1.436  -6.594  1.00 19.42 ?  371 HOH   A O    1 
HETATM 6718 O O    . HOH   D 3 .   ? 17.064 -19.349 4.899   1.00 16.43 ?  372 HOH   A O    1 
HETATM 6719 O O    . HOH   D 3 .   ? 24.415 3.604   -1.807  1.00 17.50 ?  373 HOH   A O    1 
HETATM 6720 O O    . HOH   D 3 .   ? 14.026 -5.011  17.596  1.00 26.61 ?  374 HOH   A O    1 
HETATM 6721 O O    . HOH   D 3 .   ? 16.508 -22.107 0.962   1.00 29.91 ?  375 HOH   A O    1 
HETATM 6722 O O    . HOH   D 3 .   ? 15.198 -8.077  -9.662  1.00 24.23 ?  376 HOH   A O    1 
HETATM 6723 O O    . HOH   D 3 .   ? 24.764 -17.569 12.741  1.00 26.60 ?  377 HOH   A O    1 
HETATM 6724 O O    . HOH   D 3 .   ? 44.008 8.506   -3.082  1.00 28.79 ?  378 HOH   A O    1 
HETATM 6725 O O    B HOH   D 3 .   ? 15.107 -2.803  3.566   0.14 15.50 ?  379 HOH   A O    1 
HETATM 6726 O O    . HOH   D 3 .   ? 6.482  -5.637  11.193  1.00 21.47 ?  380 HOH   A O    1 
HETATM 6727 O O    . HOH   D 3 .   ? 31.802 -7.270  -9.886  1.00 22.68 ?  381 HOH   A O    1 
HETATM 6728 O O    . HOH   D 3 .   ? 43.426 7.850   2.698   1.00 30.82 ?  382 HOH   A O    1 
HETATM 6729 O O    . HOH   D 3 .   ? 25.755 -0.774  -7.346  1.00 17.29 ?  383 HOH   A O    1 
HETATM 6730 O O    . HOH   D 3 .   ? 14.467 -24.751 11.620  1.00 37.67 ?  384 HOH   A O    1 
HETATM 6731 O O    . HOH   D 3 .   ? 33.559 -17.045 8.022   1.00 19.81 ?  385 HOH   A O    1 
HETATM 6732 O O    A HOH   D 3 .   ? 20.143 4.529   -7.510  0.86 19.56 ?  386 HOH   A O    1 
HETATM 6733 O O    . HOH   D 3 .   ? 18.985 -0.666  -1.655  1.00 14.93 ?  387 HOH   A O    1 
HETATM 6734 O O    . HOH   D 3 .   ? 24.026 -15.678 -9.177  1.00 37.91 ?  388 HOH   A O    1 
HETATM 6735 O O    . HOH   D 3 .   ? 24.312 -7.821  14.484  1.00 18.44 ?  389 HOH   A O    1 
HETATM 6736 O O    . HOH   D 3 .   ? 22.719 -11.980 21.892  1.00 43.27 ?  390 HOH   A O    1 
HETATM 6737 O O    . HOH   D 3 .   ? 21.225 10.235  15.085  1.00 38.41 ?  391 HOH   A O    1 
HETATM 6738 O O    . HOH   D 3 .   ? 28.640 -10.612 -14.095 1.00 45.28 ?  392 HOH   A O    1 
HETATM 6739 O O    . HOH   D 3 .   ? 30.739 1.862   16.724  1.00 22.50 ?  393 HOH   A O    1 
HETATM 6740 O O    . HOH   D 3 .   ? 24.051 3.942   -4.854  1.00 24.67 ?  394 HOH   A O    1 
HETATM 6741 O O    . HOH   D 3 .   ? 27.571 -6.087  -14.021 1.00 40.40 ?  395 HOH   A O    1 
HETATM 6742 O O    . HOH   D 3 .   ? 20.609 -20.074 2.778   1.00 19.51 ?  396 HOH   A O    1 
HETATM 6743 O O    . HOH   D 3 .   ? 23.495 11.368  4.138   1.00 13.65 ?  397 HOH   A O    1 
HETATM 6744 O O    . HOH   D 3 .   ? 16.015 6.959   3.007   1.00 17.11 ?  398 HOH   A O    1 
HETATM 6745 O O    . HOH   D 3 .   ? 37.623 -2.057  5.787   1.00 28.06 ?  399 HOH   A O    1 
HETATM 6746 O O    . HOH   D 3 .   ? 21.860 -13.846 -8.158  1.00 41.67 ?  400 HOH   A O    1 
HETATM 6747 O O    . HOH   D 3 .   ? 26.978 4.158   -0.647  1.00 13.91 ?  401 HOH   A O    1 
HETATM 6748 O O    A HOH   D 3 .   ? 15.857 -0.983  5.300   0.86 24.56 ?  402 HOH   A O    1 
HETATM 6749 O O    . HOH   D 3 .   ? 27.340 2.298   18.747  1.00 30.72 ?  403 HOH   A O    1 
HETATM 6750 O O    . HOH   D 3 .   ? 15.251 -21.623 14.228  1.00 19.25 ?  404 HOH   A O    1 
HETATM 6751 O O    . HOH   D 3 .   ? 32.830 -9.281  5.897   1.00 20.32 ?  405 HOH   A O    1 
HETATM 6752 O O    . HOH   D 3 .   ? 19.513 -11.213 24.129  1.00 67.54 ?  406 HOH   A O    1 
HETATM 6753 O O    . HOH   D 3 .   ? 9.464  -16.321 -2.168  1.00 43.35 ?  407 HOH   A O    1 
HETATM 6754 O O    . HOH   D 3 .   ? 30.135 -10.164 13.028  1.00 23.78 ?  408 HOH   A O    1 
HETATM 6755 O O    . HOH   D 3 .   ? 41.682 1.566   4.933   1.00 38.03 ?  409 HOH   A O    1 
HETATM 6756 O O    . HOH   D 3 .   ? 32.608 -10.640 3.144   1.00 32.01 ?  410 HOH   A O    1 
HETATM 6757 O O    . HOH   D 3 .   ? 45.024 -0.683  2.898   1.00 42.52 ?  411 HOH   A O    1 
HETATM 6758 O O    . HOH   D 3 .   ? 14.083 -23.114 7.419   1.00 19.62 ?  412 HOH   A O    1 
HETATM 6759 O O    . HOH   D 3 .   ? 11.051 1.603   12.838  1.00 26.13 ?  413 HOH   A O    1 
HETATM 6760 O O    . HOH   D 3 .   ? 27.136 -3.315  19.399  1.00 38.75 ?  414 HOH   A O    1 
HETATM 6761 O O    . HOH   D 3 .   ? 16.243 16.689  8.703   1.00 31.22 ?  415 HOH   A O    1 
HETATM 6762 O O    . HOH   D 3 .   ? 40.959 -8.256  -6.768  1.00 36.98 ?  416 HOH   A O    1 
HETATM 6763 O O    . HOH   D 3 .   ? 38.164 -1.345  -1.978  1.00 20.46 ?  417 HOH   A O    1 
HETATM 6764 O O    . HOH   D 3 .   ? 14.509 -0.486  -12.117 1.00 28.23 ?  418 HOH   A O    1 
HETATM 6765 O O    . HOH   D 3 .   ? 29.936 -1.914  -12.752 1.00 47.35 ?  419 HOH   A O    1 
HETATM 6766 O O    . HOH   D 3 .   ? 6.711  -3.376  13.009  1.00 32.00 ?  420 HOH   A O    1 
HETATM 6767 O O    . HOH   D 3 .   ? 23.996 -20.327 -1.358  1.00 18.04 ?  421 HOH   A O    1 
HETATM 6768 O O    . HOH   D 3 .   ? 35.129 -5.221  -3.109  1.00 18.94 ?  422 HOH   A O    1 
HETATM 6769 O O    . HOH   D 3 .   ? 15.942 2.149   24.814  1.00 51.46 ?  423 HOH   A O    1 
HETATM 6770 O O    . HOH   D 3 .   ? 36.758 -5.025  5.354   1.00 25.55 ?  424 HOH   A O    1 
HETATM 6771 O O    A HOH   D 3 .   ? 18.612 -2.462  -16.314 0.86 39.13 ?  425 HOH   A O    1 
HETATM 6772 O O    . HOH   D 3 .   ? 5.201  2.674   5.167   1.00 34.27 ?  426 HOH   A O    1 
HETATM 6773 O O    . HOH   D 3 .   ? 10.421 -13.797 -1.678  1.00 19.52 ?  427 HOH   A O    1 
HETATM 6774 O O    . HOH   D 3 .   ? 32.696 -4.322  -9.950  1.00 29.66 ?  428 HOH   A O    1 
HETATM 6775 O O    . HOH   D 3 .   ? 30.442 -12.976 13.517  1.00 21.15 ?  429 HOH   A O    1 
HETATM 6776 O O    . HOH   D 3 .   ? 22.720 8.080   18.430  1.00 41.11 ?  430 HOH   A O    1 
HETATM 6777 O O    . HOH   D 3 .   ? 16.237 -14.221 20.299  1.00 47.40 ?  431 HOH   A O    1 
HETATM 6778 O O    A HOH   D 3 .   ? 11.121 -0.413  1.968   0.86 23.72 ?  432 HOH   A O    1 
HETATM 6779 O O    . HOH   D 3 .   ? 11.695 -10.835 17.035  1.00 27.01 ?  433 HOH   A O    1 
HETATM 6780 O O    . HOH   D 3 .   ? 20.680 -17.718 24.838  1.00 47.42 ?  434 HOH   A O    1 
HETATM 6781 O O    . HOH   D 3 .   ? 21.341 -9.293  21.339  1.00 45.75 ?  435 HOH   A O    1 
HETATM 6782 O O    . HOH   D 3 .   ? 18.481 -16.039 16.312  1.00 37.23 ?  436 HOH   A O    1 
HETATM 6783 O O    . HOH   D 3 .   ? 18.863 2.031   -0.729  1.00 15.17 ?  437 HOH   A O    1 
HETATM 6784 O O    A HOH   D 3 .   ? 16.308 2.922   -1.405  0.86 17.24 ?  438 HOH   A O    1 
HETATM 6785 O O    . HOH   D 3 .   ? 18.448 4.744   -15.206 1.00 52.69 ?  439 HOH   A O    1 
HETATM 6786 O O    . HOH   D 3 .   ? 23.404 -21.012 1.278   1.00 19.71 ?  440 HOH   A O    1 
HETATM 6787 O O    . HOH   D 3 .   ? 37.788 -8.833  -3.500  1.00 25.47 ?  441 HOH   A O    1 
HETATM 6788 O O    . HOH   D 3 .   ? 23.600 -8.092  17.102  1.00 22.40 ?  442 HOH   A O    1 
HETATM 6789 O O    . HOH   D 3 .   ? 23.233 7.578   -3.224  1.00 31.83 ?  443 HOH   A O    1 
HETATM 6790 O O    . HOH   D 3 .   ? 34.493 -8.079  -0.571  1.00 31.34 ?  444 HOH   A O    1 
HETATM 6791 O O    . HOH   D 3 .   ? -1.371 -5.008  7.745   1.00 42.17 ?  445 HOH   A O    1 
HETATM 6792 O O    . HOH   D 3 .   ? 31.408 -12.825 -0.009  1.00 21.57 ?  446 HOH   A O    1 
HETATM 6793 O O    . HOH   D 3 .   ? 30.601 14.772  2.802   1.00 20.11 ?  447 HOH   A O    1 
HETATM 6794 O O    . HOH   D 3 .   ? 21.602 -14.803 18.040  1.00 49.08 ?  448 HOH   A O    1 
HETATM 6795 O O    A HOH   D 3 .   ? 14.082 -0.373  3.494   0.86 21.10 ?  449 HOH   A O    1 
HETATM 6796 O O    . HOH   D 3 .   ? 25.445 8.270   -4.795  1.00 26.66 ?  450 HOH   A O    1 
HETATM 6797 O O    . HOH   D 3 .   ? 29.912 -16.133 10.692  1.00 37.38 ?  451 HOH   A O    1 
HETATM 6798 O O    . HOH   D 3 .   ? 27.867 7.092   -6.363  1.00 37.01 ?  452 HOH   A O    1 
HETATM 6799 O O    . HOH   D 3 .   ? 32.523 -15.958 10.836  1.00 35.42 ?  453 HOH   A O    1 
HETATM 6800 O O    . HOH   D 3 .   ? 19.972 -17.395 -5.136  1.00 26.29 ?  454 HOH   A O    1 
HETATM 6801 O O    . HOH   D 3 .   ? 24.859 5.588   20.758  1.00 53.53 ?  455 HOH   A O    1 
HETATM 6802 O O    . HOH   D 3 .   ? 24.627 14.578  7.906   1.00 36.83 ?  456 HOH   A O    1 
HETATM 6803 O O    . HOH   D 3 .   ? 23.269 -22.418 -3.376  1.00 38.02 ?  457 HOH   A O    1 
HETATM 6804 O O    . HOH   D 3 .   ? 11.007 -14.988 -6.067  1.00 36.11 ?  458 HOH   A O    1 
HETATM 6805 O O    . HOH   D 3 .   ? 12.419 1.632   17.335  1.00 42.66 ?  459 HOH   A O    1 
HETATM 6806 O O    . HOH   D 3 .   ? 26.978 11.650  -1.384  1.00 30.97 ?  460 HOH   A O    1 
HETATM 6807 O O    . HOH   D 3 .   ? 8.146  -3.094  -5.676  1.00 44.68 ?  461 HOH   A O    1 
HETATM 6808 O O    . HOH   D 3 .   ? 15.788 -21.561 3.698   1.00 24.34 ?  462 HOH   A O    1 
HETATM 6809 O O    . HOH   D 3 .   ? 23.524 13.724  5.531   1.00 20.45 ?  463 HOH   A O    1 
HETATM 6810 O O    . HOH   D 3 .   ? 18.785 10.820  11.415  1.00 35.16 ?  464 HOH   A O    1 
HETATM 6811 O O    . HOH   D 3 .   ? 18.153 -16.249 -8.825  1.00 42.63 ?  465 HOH   A O    1 
HETATM 6812 O O    . HOH   D 3 .   ? 27.596 -11.490 16.522  1.00 36.82 ?  466 HOH   A O    1 
HETATM 6813 O O    . HOH   D 3 .   ? 12.021 -13.432 16.357  1.00 46.55 ?  467 HOH   A O    1 
HETATM 6814 O O    A HOH   D 3 .   ? 22.010 5.251   -5.800  0.86 28.80 ?  468 HOH   A O    1 
HETATM 6815 O O    . HOH   D 3 .   ? 25.871 10.795  -3.687  1.00 26.51 ?  469 HOH   A O    1 
HETATM 6816 O O    . HOH   D 3 .   ? 39.710 -6.974  -3.418  1.00 44.51 ?  470 HOH   A O    1 
HETATM 6817 O O    . HOH   D 3 .   ? 28.665 -4.733  -12.291 1.00 41.30 ?  471 HOH   A O    1 
HETATM 6818 O O    . HOH   D 3 .   ? 28.907 8.912   17.502  1.00 39.04 ?  472 HOH   A O    1 
HETATM 6819 O O    . HOH   D 3 .   ? 35.239 7.396   12.242  1.00 46.64 ?  473 HOH   A O    1 
HETATM 6820 O O    . HOH   D 3 .   ? 14.019 -10.331 -10.933 1.00 34.39 ?  474 HOH   A O    1 
HETATM 6821 O O    . HOH   D 3 .   ? 31.516 -0.595  -10.569 1.00 29.38 ?  475 HOH   A O    1 
HETATM 6822 O O    . HOH   D 3 .   ? 30.849 0.690   19.217  1.00 41.67 ?  476 HOH   A O    1 
HETATM 6823 O O    . HOH   D 3 .   ? 23.177 11.837  -4.055  1.00 21.39 ?  477 HOH   A O    1 
HETATM 6824 O O    . HOH   D 3 .   ? 16.013 -6.696  -11.796 1.00 43.39 ?  478 HOH   A O    1 
HETATM 6825 O O    . HOH   D 3 .   ? 17.489 -18.864 19.815  1.00 46.70 ?  479 HOH   A O    1 
HETATM 6826 O O    . HOH   D 3 .   ? 15.758 -17.213 -7.049  1.00 34.01 ?  480 HOH   A O    1 
HETATM 6827 O O    . HOH   D 3 .   ? 41.046 -3.984  -0.386  1.00 39.24 ?  481 HOH   A O    1 
HETATM 6828 O O    . HOH   D 3 .   ? 16.855 -20.622 16.171  1.00 29.39 ?  482 HOH   A O    1 
HETATM 6829 O O    . HOH   D 3 .   ? 28.689 -7.876  -15.339 1.00 46.24 ?  483 HOH   A O    1 
HETATM 6830 O O    . HOH   D 3 .   ? 41.773 9.326   -4.087  1.00 33.42 ?  484 HOH   A O    1 
HETATM 6831 O O    . HOH   D 3 .   ? 23.315 -12.875 19.373  1.00 45.85 ?  485 HOH   A O    1 
HETATM 6832 O O    . HOH   D 3 .   ? 44.569 10.496  -1.580  1.00 33.24 ?  486 HOH   A O    1 
HETATM 6833 O O    . HOH   D 3 .   ? 39.249 2.359   7.508   1.00 32.66 ?  487 HOH   A O    1 
HETATM 6834 O O    . HOH   D 3 .   ? 18.582 -23.256 1.886   1.00 51.29 ?  488 HOH   A O    1 
HETATM 6835 O O    . HOH   D 3 .   ? 30.843 5.779   -14.776 1.00 37.23 ?  489 HOH   A O    1 
HETATM 6836 O O    . HOH   D 3 .   ? 40.561 -0.230  -7.851  1.00 33.57 ?  490 HOH   A O    1 
HETATM 6837 O O    . HOH   D 3 .   ? 20.043 -22.393 4.161   1.00 28.83 ?  491 HOH   A O    1 
HETATM 6838 O O    . HOH   D 3 .   ? 14.077 -25.362 8.924   1.00 31.19 ?  492 HOH   A O    1 
HETATM 6839 O O    . HOH   D 3 .   ? 16.193 -23.442 5.749   1.00 29.67 ?  493 HOH   A O    1 
HETATM 6840 O O    . HOH   D 3 .   ? 30.778 -5.800  -11.841 1.00 47.50 ?  494 HOH   A O    1 
HETATM 6841 O O    . HOH   D 3 .   ? 37.442 -6.657  7.563   1.00 26.02 ?  495 HOH   A O    1 
HETATM 6842 O O    . HOH   D 3 .   ? 23.179 -23.824 1.619   1.00 33.41 ?  496 HOH   A O    1 
HETATM 6843 O O    . HOH   D 3 .   ? 20.585 -16.093 -7.403  1.00 31.23 ?  497 HOH   A O    1 
HETATM 6844 O O    . HOH   D 3 .   ? 39.659 0.002   6.583   1.00 29.79 ?  498 HOH   A O    1 
HETATM 6845 O O    . HOH   D 3 .   ? 29.049 14.485  0.895   1.00 45.04 ?  499 HOH   A O    1 
HETATM 6846 O O    . HOH   D 3 .   ? 38.064 13.959  6.724   1.00 44.72 ?  500 HOH   A O    1 
HETATM 6847 O O    . HOH   D 3 .   ? 14.932 8.571   5.026   1.00 40.31 ?  501 HOH   A O    1 
HETATM 6848 O O    . HOH   D 3 .   ? 36.474 -6.591  10.107  1.00 45.05 ?  502 HOH   A O    1 
HETATM 6849 O O    . HOH   D 3 .   ? 22.060 -24.110 4.475   1.00 28.37 ?  503 HOH   A O    1 
HETATM 6850 O O    . HOH   D 3 .   ? 17.374 -6.943  -14.263 1.00 41.18 ?  504 HOH   A O    1 
HETATM 6851 O O    . HOH   D 3 .   ? 24.104 8.978   -7.310  1.00 37.26 ?  505 HOH   A O    1 
HETATM 6852 O O    . HOH   D 3 .   ? 16.460 -21.172 18.795  1.00 36.02 ?  506 HOH   A O    1 
HETATM 6853 O O    . HOH   D 3 .   ? 15.914 -12.348 27.518  1.00 44.99 ?  507 HOH   A O    1 
HETATM 6854 O O    . HOH   D 3 .   ? 14.719 -22.779 19.898  1.00 36.10 ?  508 HOH   A O    1 
HETATM 6855 O O    . HOH   E 3 .   ? 29.905 -22.432 5.464   1.00 22.38 ?  201 HOH   B O    1 
HETATM 6856 O O    . HOH   E 3 .   ? 59.292 -18.750 6.784   1.00 39.85 ?  202 HOH   B O    1 
HETATM 6857 O O    . HOH   E 3 .   ? 49.507 -22.655 -19.739 1.00 49.49 ?  203 HOH   B O    1 
HETATM 6858 O O    . HOH   E 3 .   ? 48.229 -6.938  15.585  1.00 32.69 ?  204 HOH   B O    1 
HETATM 6859 O O    . HOH   E 3 .   ? 38.022 -39.520 -0.199  1.00 45.87 ?  205 HOH   B O    1 
HETATM 6860 O O    . HOH   E 3 .   ? 41.834 -35.941 -17.460 1.00 31.73 ?  206 HOH   B O    1 
HETATM 6861 O O    . HOH   E 3 .   ? 27.779 -29.210 -1.868  1.00 36.18 ?  207 HOH   B O    1 
HETATM 6862 O O    . HOH   E 3 .   ? 54.581 -9.399  -8.773  1.00 20.46 ?  208 HOH   B O    1 
HETATM 6863 O O    . HOH   E 3 .   ? 50.412 -3.312  7.196   1.00 34.78 ?  209 HOH   B O    1 
HETATM 6864 O O    . HOH   E 3 .   ? 58.299 -13.041 8.367   1.00 35.73 ?  210 HOH   B O    1 
HETATM 6865 O O    . HOH   E 3 .   ? 41.485 -7.726  5.430   1.00 39.21 ?  211 HOH   B O    1 
HETATM 6866 O O    . HOH   E 3 .   ? 56.453 -19.772 7.236   1.00 33.57 ?  212 HOH   B O    1 
HETATM 6867 O O    . HOH   E 3 .   ? 27.881 -41.870 -15.247 1.00 36.87 ?  213 HOH   B O    1 
HETATM 6868 O O    . HOH   E 3 .   ? 30.262 -41.058 -8.168  1.00 17.74 ?  214 HOH   B O    1 
HETATM 6869 O O    . HOH   E 3 .   ? 47.471 -7.366  -3.928  1.00 42.59 ?  215 HOH   B O    1 
HETATM 6870 O O    . HOH   E 3 .   ? 57.835 -24.513 5.021   1.00 39.83 ?  216 HOH   B O    1 
HETATM 6871 O O    . HOH   E 3 .   ? 29.987 -26.363 3.993   1.00 28.19 ?  217 HOH   B O    1 
HETATM 6872 O O    . HOH   E 3 .   ? 29.906 -34.296 -0.441  1.00 36.05 ?  218 HOH   B O    1 
HETATM 6873 O O    . HOH   E 3 .   ? 53.071 -13.468 -20.419 1.00 37.84 ?  219 HOH   B O    1 
HETATM 6874 O O    . HOH   E 3 .   ? 34.618 -36.431 -7.260  1.00 19.30 ?  220 HOH   B O    1 
HETATM 6875 O O    . HOH   E 3 .   ? 56.786 -30.825 -7.807  1.00 32.28 ?  221 HOH   B O    1 
HETATM 6876 O O    . HOH   E 3 .   ? 50.840 -6.099  0.184   1.00 30.10 ?  222 HOH   B O    1 
HETATM 6877 O O    . HOH   E 3 .   ? 48.630 -36.520 -15.560 1.00 41.50 ?  223 HOH   B O    1 
HETATM 6878 O O    . HOH   E 3 .   ? 44.550 -7.274  2.113   1.00 35.84 ?  224 HOH   B O    1 
HETATM 6879 O O    . HOH   E 3 .   ? 30.946 -28.825 4.265   1.00 27.18 ?  225 HOH   B O    1 
HETATM 6880 O O    . HOH   E 3 .   ? 57.254 -26.872 -7.619  1.00 38.49 ?  226 HOH   B O    1 
HETATM 6881 O O    . HOH   E 3 .   ? 57.499 -16.257 -12.256 1.00 20.34 ?  227 HOH   B O    1 
HETATM 6882 O O    . HOH   E 3 .   ? 39.403 -10.936 6.104   1.00 28.20 ?  228 HOH   B O    1 
HETATM 6883 O O    . HOH   E 3 .   ? 45.181 -35.020 6.854   1.00 40.91 ?  229 HOH   B O    1 
HETATM 6884 O O    . HOH   E 3 .   ? 55.415 -16.436 -14.398 1.00 33.16 ?  230 HOH   B O    1 
HETATM 6885 O O    . HOH   E 3 .   ? 25.505 -25.991 -1.395  1.00 35.75 ?  231 HOH   B O    1 
HETATM 6886 O O    . HOH   E 3 .   ? 43.145 -43.306 -8.275  1.00 30.50 ?  232 HOH   B O    1 
HETATM 6887 O O    . HOH   E 3 .   ? 50.841 -12.996 -0.497  1.00 13.43 ?  233 HOH   B O    1 
HETATM 6888 O O    . HOH   E 3 .   ? 41.570 -39.215 -14.991 1.00 23.75 ?  234 HOH   B O    1 
HETATM 6889 O O    . HOH   E 3 .   ? 41.436 -9.666  13.064  1.00 24.09 ?  235 HOH   B O    1 
HETATM 6890 O O    . HOH   E 3 .   ? 40.664 -16.095 14.126  1.00 25.98 ?  236 HOH   B O    1 
HETATM 6891 O O    . HOH   E 3 .   ? 35.976 -43.305 -8.592  1.00 34.80 ?  237 HOH   B O    1 
HETATM 6892 O O    . HOH   E 3 .   ? 35.184 -8.006  -3.063  1.00 19.27 ?  238 HOH   B O    1 
HETATM 6893 O O    . HOH   E 3 .   ? 45.063 -43.589 -10.580 1.00 28.95 ?  239 HOH   B O    1 
HETATM 6894 O O    . HOH   E 3 .   ? 32.856 -43.839 -11.387 1.00 21.74 ?  240 HOH   B O    1 
HETATM 6895 O O    . HOH   E 3 .   ? 46.435 -1.595  13.273  1.00 27.69 ?  241 HOH   B O    1 
HETATM 6896 O O    . HOH   E 3 .   ? 57.724 -24.410 -3.854  1.00 21.98 ?  242 HOH   B O    1 
HETATM 6897 O O    . HOH   E 3 .   ? 28.462 -19.703 -13.177 1.00 25.64 ?  243 HOH   B O    1 
HETATM 6898 O O    . HOH   E 3 .   ? 44.609 -27.838 -0.765  1.00 23.58 ?  244 HOH   B O    1 
HETATM 6899 O O    . HOH   E 3 .   ? 42.649 -25.414 2.638   1.00 16.18 ?  245 HOH   B O    1 
HETATM 6900 O O    . HOH   E 3 .   ? 42.719 -22.912 3.834   1.00 12.84 ?  246 HOH   B O    1 
HETATM 6901 O O    . HOH   E 3 .   ? 51.751 -6.524  4.377   1.00 21.38 ?  247 HOH   B O    1 
HETATM 6902 O O    . HOH   E 3 .   ? 37.139 -19.750 -18.117 1.00 43.95 ?  248 HOH   B O    1 
HETATM 6903 O O    . HOH   E 3 .   ? 51.039 -40.035 -8.295  1.00 31.74 ?  249 HOH   B O    1 
HETATM 6904 O O    . HOH   E 3 .   ? 39.564 -11.133 0.293   1.00 18.58 ?  250 HOH   B O    1 
HETATM 6905 O O    . HOH   E 3 .   ? 40.421 -12.764 -11.554 1.00 16.42 ?  251 HOH   B O    1 
HETATM 6906 O O    . HOH   E 3 .   ? 30.920 -15.767 2.634   1.00 14.61 ?  252 HOH   B O    1 
HETATM 6907 O O    . HOH   E 3 .   ? 34.299 -18.515 11.423  1.00 25.49 ?  253 HOH   B O    1 
HETATM 6908 O O    . HOH   E 3 .   ? 43.260 -32.411 -17.149 1.00 24.90 ?  254 HOH   B O    1 
HETATM 6909 O O    . HOH   E 3 .   ? 29.780 -25.234 -10.858 1.00 17.56 ?  255 HOH   B O    1 
HETATM 6910 O O    . HOH   E 3 .   ? 48.121 -24.513 -17.858 1.00 32.85 ?  256 HOH   B O    1 
HETATM 6911 O O    . HOH   E 3 .   ? 49.866 -0.566  10.274  1.00 34.64 ?  257 HOH   B O    1 
HETATM 6912 O O    . HOH   E 3 .   ? 41.952 -23.562 9.304   1.00 18.81 ?  258 HOH   B O    1 
HETATM 6913 O O    . HOH   E 3 .   ? 34.963 -24.691 13.869  1.00 30.96 ?  259 HOH   B O    1 
HETATM 6914 O O    . HOH   E 3 .   ? 58.277 -10.649 -4.103  1.00 22.08 ?  260 HOH   B O    1 
HETATM 6915 O O    . HOH   E 3 .   ? 34.558 -12.814 2.581   1.00 27.89 ?  261 HOH   B O    1 
HETATM 6916 O O    . HOH   E 3 .   ? 48.099 -22.821 5.813   1.00 18.50 ?  262 HOH   B O    1 
HETATM 6917 O O    . HOH   E 3 .   ? 27.175 -31.855 -10.039 1.00 23.09 ?  263 HOH   B O    1 
HETATM 6918 O O    . HOH   E 3 .   ? 49.397 -28.755 -6.967  1.00 16.67 ?  264 HOH   B O    1 
HETATM 6919 O O    . HOH   E 3 .   ? 28.551 -30.860 -14.847 1.00 32.08 ?  265 HOH   B O    1 
HETATM 6920 O O    . HOH   E 3 .   ? 51.606 -13.840 10.996  1.00 30.51 ?  266 HOH   B O    1 
HETATM 6921 O O    . HOH   E 3 .   ? 43.461 -15.804 -12.232 1.00 15.18 ?  267 HOH   B O    1 
HETATM 6922 O O    . HOH   E 3 .   ? 38.507 -11.107 -2.231  1.00 20.06 ?  268 HOH   B O    1 
HETATM 6923 O O    . HOH   E 3 .   ? 38.975 -12.045 12.363  1.00 34.91 ?  269 HOH   B O    1 
HETATM 6924 O O    . HOH   E 3 .   ? 57.227 -12.184 12.339  1.00 38.62 ?  270 HOH   B O    1 
HETATM 6925 O O    . HOH   E 3 .   ? 42.418 -9.931  9.354   1.00 22.40 ?  271 HOH   B O    1 
HETATM 6926 O O    . HOH   E 3 .   ? 57.049 -8.672  8.411   1.00 21.41 ?  272 HOH   B O    1 
HETATM 6927 O O    . HOH   E 3 .   ? 46.715 -31.292 -4.850  1.00 21.54 ?  273 HOH   B O    1 
HETATM 6928 O O    . HOH   E 3 .   ? 31.896 -17.961 -14.599 1.00 32.89 ?  274 HOH   B O    1 
HETATM 6929 O O    . HOH   E 3 .   ? 28.307 -34.394 -9.511  1.00 22.52 ?  275 HOH   B O    1 
HETATM 6930 O O    . HOH   E 3 .   ? 57.622 -9.250  1.398   1.00 20.66 ?  276 HOH   B O    1 
HETATM 6931 O O    . HOH   E 3 .   ? 48.493 -25.095 3.084   1.00 14.43 ?  277 HOH   B O    1 
HETATM 6932 O O    . HOH   E 3 .   ? 33.623 -15.327 -14.023 1.00 22.09 ?  278 HOH   B O    1 
HETATM 6933 O O    . HOH   E 3 .   ? 42.474 -34.766 3.756   1.00 26.95 ?  279 HOH   B O    1 
HETATM 6934 O O    . HOH   E 3 .   ? 56.301 -23.530 -14.821 1.00 28.23 ?  280 HOH   B O    1 
HETATM 6935 O O    . HOH   E 3 .   ? 36.915 -12.806 -1.547  1.00 28.59 ?  281 HOH   B O    1 
HETATM 6936 O O    . HOH   E 3 .   ? 41.241 -5.532  11.507  1.00 43.84 ?  282 HOH   B O    1 
HETATM 6937 O O    . HOH   E 3 .   ? 42.956 -20.296 -20.791 1.00 37.53 ?  283 HOH   B O    1 
HETATM 6938 O O    . HOH   E 3 .   ? 46.948 -29.600 9.827   1.00 31.41 ?  284 HOH   B O    1 
HETATM 6939 O O    . HOH   E 3 .   ? 28.001 -22.915 -8.055  1.00 18.65 ?  285 HOH   B O    1 
HETATM 6940 O O    . HOH   E 3 .   ? 35.013 -33.406 -19.316 1.00 30.41 ?  286 HOH   B O    1 
HETATM 6941 O O    . HOH   E 3 .   ? 48.803 -20.076 5.919   1.00 15.05 ?  287 HOH   B O    1 
HETATM 6942 O O    . HOH   E 3 .   ? 42.410 -9.942  -14.922 1.00 37.52 ?  288 HOH   B O    1 
HETATM 6943 O O    . HOH   E 3 .   ? 27.643 -26.760 -15.692 1.00 35.23 ?  289 HOH   B O    1 
HETATM 6944 O O    . HOH   E 3 .   ? 37.424 -35.710 7.209   1.00 36.14 ?  290 HOH   B O    1 
HETATM 6945 O O    . HOH   E 3 .   ? 51.317 -37.693 -9.664  1.00 27.31 ?  291 HOH   B O    1 
HETATM 6946 O O    . HOH   E 3 .   ? 47.162 -34.026 -4.678  1.00 18.75 ?  292 HOH   B O    1 
HETATM 6947 O O    . HOH   E 3 .   ? 45.985 -40.485 -3.691  1.00 29.75 ?  293 HOH   B O    1 
HETATM 6948 O O    . HOH   E 3 .   ? 45.433 -33.426 -16.040 1.00 24.83 ?  294 HOH   B O    1 
HETATM 6949 O O    . HOH   E 3 .   ? 57.749 -22.151 3.092   1.00 28.76 ?  295 HOH   B O    1 
HETATM 6950 O O    . HOH   E 3 .   ? 50.038 -24.707 5.810   1.00 37.69 ?  296 HOH   B O    1 
HETATM 6951 O O    . HOH   E 3 .   ? 35.134 -33.643 4.464   1.00 29.19 ?  297 HOH   B O    1 
HETATM 6952 O O    . HOH   E 3 .   ? 44.703 -27.510 1.953   1.00 16.71 ?  298 HOH   B O    1 
HETATM 6953 O O    . HOH   E 3 .   ? 52.692 -35.754 -8.657  1.00 29.37 ?  299 HOH   B O    1 
HETATM 6954 O O    . HOH   E 3 .   ? 30.547 -42.391 -10.628 1.00 31.54 ?  300 HOH   B O    1 
HETATM 6955 O O    . HOH   E 3 .   ? 52.612 -10.445 13.044  1.00 23.87 ?  301 HOH   B O    1 
HETATM 6956 O O    . HOH   E 3 .   ? 40.323 -10.835 -9.578  1.00 18.12 ?  302 HOH   B O    1 
HETATM 6957 O O    . HOH   E 3 .   ? 59.870 -15.371 8.202   1.00 33.75 ?  303 HOH   B O    1 
HETATM 6958 O O    . HOH   E 3 .   ? 44.129 -29.393 -4.719  1.00 24.84 ?  304 HOH   B O    1 
HETATM 6959 O O    . HOH   E 3 .   ? 41.290 -24.528 15.794  1.00 45.97 ?  305 HOH   B O    1 
HETATM 6960 O O    . HOH   E 3 .   ? 42.745 -12.262 -18.561 1.00 30.34 ?  306 HOH   B O    1 
HETATM 6961 O O    . HOH   E 3 .   ? 53.550 -30.260 4.527   1.00 20.08 ?  307 HOH   B O    1 
HETATM 6962 O O    . HOH   E 3 .   ? 37.625 -18.203 13.149  1.00 30.85 ?  308 HOH   B O    1 
HETATM 6963 O O    . HOH   E 3 .   ? 32.893 -34.640 -5.967  1.00 18.01 ?  309 HOH   B O    1 
HETATM 6964 O O    . HOH   E 3 .   ? 52.671 -29.312 -13.089 1.00 25.64 ?  310 HOH   B O    1 
HETATM 6965 O O    . HOH   E 3 .   ? 37.922 -10.243 -10.792 1.00 18.44 ?  311 HOH   B O    1 
HETATM 6966 O O    . HOH   E 3 .   ? 53.183 -16.035 -12.791 1.00 29.63 ?  312 HOH   B O    1 
HETATM 6967 O O    . HOH   E 3 .   ? 26.004 -21.506 -3.574  1.00 18.06 ?  313 HOH   B O    1 
HETATM 6968 O O    . HOH   E 3 .   ? 38.447 -9.409  -13.325 1.00 30.38 ?  314 HOH   B O    1 
HETATM 6969 O O    . HOH   E 3 .   ? 51.454 -32.971 -10.819 1.00 40.76 ?  315 HOH   B O    1 
HETATM 6970 O O    . HOH   E 3 .   ? 43.287 -21.480 10.672  1.00 16.94 ?  316 HOH   B O    1 
HETATM 6971 O O    . HOH   E 3 .   ? 43.582 -15.406 18.208  1.00 30.81 ?  317 HOH   B O    1 
HETATM 6972 O O    . HOH   E 3 .   ? 44.631 -24.686 9.589   1.00 21.05 ?  318 HOH   B O    1 
HETATM 6973 O O    . HOH   E 3 .   ? 37.154 -30.628 -21.094 1.00 32.75 ?  319 HOH   B O    1 
HETATM 6974 O O    . HOH   E 3 .   ? 62.795 -13.588 4.671   1.00 27.56 ?  320 HOH   B O    1 
HETATM 6975 O O    . HOH   E 3 .   ? 38.423 -12.791 7.916   1.00 19.82 ?  321 HOH   B O    1 
HETATM 6976 O O    . HOH   E 3 .   ? 26.405 -21.060 -6.304  1.00 17.49 ?  322 HOH   B O    1 
HETATM 6977 O O    . HOH   E 3 .   ? 48.247 -32.706 -16.701 1.00 46.44 ?  323 HOH   B O    1 
HETATM 6978 O O    . HOH   E 3 .   ? 60.033 -17.219 -10.529 1.00 36.80 ?  324 HOH   B O    1 
HETATM 6979 O O    . HOH   E 3 .   ? 41.799 -8.089  1.378   1.00 27.40 ?  325 HOH   B O    1 
HETATM 6980 O O    . HOH   E 3 .   ? 63.006 -20.235 -0.861  1.00 40.98 ?  326 HOH   B O    1 
HETATM 6981 O O    . HOH   E 3 .   ? 51.819 -5.973  -7.919  1.00 44.95 ?  327 HOH   B O    1 
HETATM 6982 O O    . HOH   E 3 .   ? 36.788 -12.459 4.259   1.00 19.68 ?  328 HOH   B O    1 
HETATM 6983 O O    . HOH   E 3 .   ? 44.297 -1.789  7.539   1.00 45.40 ?  329 HOH   B O    1 
HETATM 6984 O O    . HOH   E 3 .   ? 47.265 -24.540 8.138   1.00 26.87 ?  330 HOH   B O    1 
HETATM 6985 O O    . HOH   E 3 .   ? 33.775 -31.200 11.079  1.00 38.75 ?  331 HOH   B O    1 
HETATM 6986 O O    . HOH   E 3 .   ? 27.941 -14.779 -9.492  1.00 36.67 ?  332 HOH   B O    1 
HETATM 6987 O O    . HOH   E 3 .   ? 53.740 -12.580 -22.355 1.00 37.07 ?  333 HOH   B O    1 
HETATM 6988 O O    . HOH   E 3 .   ? 43.201 -34.725 0.078   1.00 22.14 ?  334 HOH   B O    1 
HETATM 6989 O O    . HOH   E 3 .   ? 37.137 -45.144 -9.841  1.00 38.45 ?  335 HOH   B O    1 
HETATM 6990 O O    . HOH   E 3 .   ? 47.572 -27.490 1.982   1.00 16.03 ?  336 HOH   B O    1 
HETATM 6991 O O    . HOH   E 3 .   ? 42.876 -43.562 -14.397 1.00 43.56 ?  337 HOH   B O    1 
HETATM 6992 O O    . HOH   E 3 .   ? 39.583 -23.536 -20.367 1.00 38.05 ?  338 HOH   B O    1 
HETATM 6993 O O    . HOH   E 3 .   ? 48.693 -11.947 -13.971 1.00 28.77 ?  339 HOH   B O    1 
HETATM 6994 O O    . HOH   E 3 .   ? 45.807 -36.315 -16.198 1.00 34.97 ?  340 HOH   B O    1 
HETATM 6995 O O    . HOH   E 3 .   ? 46.906 -19.938 12.295  1.00 31.50 ?  341 HOH   B O    1 
HETATM 6996 O O    . HOH   E 3 .   ? 38.455 -12.222 -16.308 1.00 43.73 ?  342 HOH   B O    1 
HETATM 6997 O O    . HOH   E 3 .   ? 28.919 -42.918 -12.409 1.00 40.03 ?  343 HOH   B O    1 
HETATM 6998 O O    . HOH   E 3 .   ? 37.156 -15.099 -16.584 1.00 39.47 ?  344 HOH   B O    1 
HETATM 6999 O O    . HOH   E 3 .   ? 39.870 -44.288 -11.289 1.00 40.83 ?  345 HOH   B O    1 
HETATM 7000 O O    . HOH   E 3 .   ? 33.055 -14.702 1.019   1.00 20.49 ?  346 HOH   B O    1 
HETATM 7001 O O    . HOH   E 3 .   ? 40.469 -43.540 -9.262  1.00 27.60 ?  347 HOH   B O    1 
HETATM 7002 O O    . HOH   E 3 .   ? 38.617 -22.306 15.071  1.00 42.72 ?  348 HOH   B O    1 
HETATM 7003 O O    . HOH   E 3 .   ? 27.805 -26.691 -0.655  1.00 32.21 ?  349 HOH   B O    1 
HETATM 7004 O O    . HOH   E 3 .   ? 33.828 -9.266  -8.853  1.00 32.67 ?  350 HOH   B O    1 
HETATM 7005 O O    . HOH   E 3 .   ? 55.773 -8.270  10.819  1.00 25.20 ?  351 HOH   B O    1 
HETATM 7006 O O    . HOH   E 3 .   ? 23.266 -23.732 6.737   1.00 35.73 ?  352 HOH   B O    1 
HETATM 7007 O O    . HOH   E 3 .   ? 34.662 -10.357 7.529   1.00 25.22 ?  353 HOH   B O    1 
HETATM 7008 O O    . HOH   E 3 .   ? 62.731 -20.169 -4.929  1.00 45.61 ?  354 HOH   B O    1 
HETATM 7009 O O    . HOH   E 3 .   ? 56.707 -7.349  3.111   1.00 30.26 ?  355 HOH   B O    1 
HETATM 7010 O O    . HOH   E 3 .   ? 36.242 -8.514  -9.712  1.00 37.43 ?  356 HOH   B O    1 
HETATM 7011 O O    . HOH   E 3 .   ? 44.249 -37.393 -17.919 1.00 36.84 ?  357 HOH   B O    1 
HETATM 7012 O O    . HOH   E 3 .   ? 34.024 -7.884  11.519  1.00 42.24 ?  358 HOH   B O    1 
HETATM 7013 O O    . HOH   E 3 .   ? 61.632 -19.900 1.578   1.00 35.07 ?  359 HOH   B O    1 
HETATM 7014 O O    . HOH   E 3 .   ? 43.282 -12.725 -21.263 1.00 40.33 ?  360 HOH   B O    1 
HETATM 7015 O O    . HOH   E 3 .   ? 57.030 -21.584 -16.488 1.00 41.61 ?  361 HOH   B O    1 
HETATM 7016 O O    . HOH   E 3 .   ? 40.296 -8.859  9.901   1.00 37.78 ?  362 HOH   B O    1 
HETATM 7017 O O    . HOH   E 3 .   ? 27.216 -26.002 -11.492 1.00 34.21 ?  363 HOH   B O    1 
HETATM 7018 O O    . HOH   E 3 .   ? 54.269 -5.747  2.956   1.00 37.75 ?  364 HOH   B O    1 
HETATM 7019 O O    . HOH   E 3 .   ? 32.602 -23.693 14.072  1.00 41.67 ?  365 HOH   B O    1 
HETATM 7020 O O    . HOH   E 3 .   ? 40.213 -11.369 -13.962 1.00 35.84 ?  366 HOH   B O    1 
HETATM 7021 O O    . HOH   E 3 .   ? 36.297 -8.790  8.962   1.00 38.68 ?  367 HOH   B O    1 
HETATM 7022 O O    . HOH   E 3 .   ? 56.179 -7.866  -0.610  1.00 40.01 ?  368 HOH   B O    1 
HETATM 7023 O O    . HOH   E 3 .   ? 39.929 -7.044  7.828   1.00 42.99 ?  369 HOH   B O    1 
HETATM 7024 O O    . HOH   E 3 .   ? 41.891 -10.039 -17.420 1.00 60.22 ?  370 HOH   B O    1 
HETATM 7025 O O    . HOH   E 3 .   ? 48.506 -26.538 8.780   1.00 40.37 ?  371 HOH   B O    1 
HETATM 7026 O O    . HOH   E 3 .   ? 59.137 -10.419 9.157   1.00 40.50 ?  372 HOH   B O    1 
HETATM 7027 O O    . HOH   E 3 .   ? 44.252 -5.654  -3.600  1.00 41.16 ?  373 HOH   B O    1 
HETATM 7028 O O    . HOH   E 3 .   ? 36.642 -22.842 13.315  1.00 27.20 ?  374 HOH   B O    1 
HETATM 7029 O O    . HOH   E 3 .   ? 52.112 -12.923 13.348  1.00 31.98 ?  375 HOH   B O    1 
HETATM 7030 O O    . HOH   E 3 .   ? 63.218 -12.463 6.902   1.00 38.10 ?  376 HOH   B O    1 
HETATM 7031 O O    . HOH   E 3 .   ? 38.092 -10.603 10.094  1.00 31.55 ?  377 HOH   B O    1 
HETATM 7032 O O    . HOH   E 3 .   ? 41.941 -6.838  -4.870  1.00 51.10 ?  378 HOH   B O    1 
HETATM 7033 O O    . HOH   E 3 .   ? 40.226 -7.673  3.242   1.00 37.02 ?  379 HOH   B O    1 
HETATM 7034 O O    . HOH   E 3 .   ? 42.706 -17.028 -23.272 1.00 43.28 ?  380 HOH   B O    1 
HETATM 7035 O O    . HOH   E 3 .   ? 39.750 -14.132 15.696  1.00 50.61 ?  381 HOH   B O    1 
HETATM 7036 O O    . HOH   E 3 .   ? 52.961 -29.964 7.163   1.00 24.35 ?  382 HOH   B O    1 
HETATM 7037 O O    . HOH   E 3 .   ? 60.579 -22.272 2.800   1.00 47.83 ?  383 HOH   B O    1 
HETATM 7038 O O    . HOH   E 3 .   ? 35.526 -33.833 7.279   1.00 42.75 ?  384 HOH   B O    1 
HETATM 7039 O O    . HOH   E 3 .   ? 46.879 -5.434  2.919   1.00 40.40 ?  385 HOH   B O    1 
HETATM 7040 O O    . HOH   E 3 .   ? 41.056 -9.867  15.834  1.00 50.97 ?  386 HOH   B O    1 
HETATM 7041 O O    . HOH   E 3 .   ? 25.810 -18.933 -11.924 1.00 39.55 ?  387 HOH   B O    1 
HETATM 7042 O O    . HOH   E 3 .   ? 23.940 -20.821 -7.739  1.00 29.55 ?  388 HOH   B O    1 
HETATM 7043 O O    . HOH   E 3 .   ? 35.451 -20.364 13.387  1.00 31.76 ?  389 HOH   B O    1 
HETATM 7044 O O    . HOH   E 3 .   ? 40.764 -6.633  -0.861  1.00 27.37 ?  390 HOH   B O    1 
HETATM 7045 O O    . HOH   E 3 .   ? 44.259 -31.797 -3.875  1.00 36.66 ?  391 HOH   B O    1 
HETATM 7046 O O    . HOH   E 3 .   ? 28.053 -27.155 2.208   1.00 32.81 ?  392 HOH   B O    1 
HETATM 7047 O O    . HOH   E 3 .   ? 26.669 -28.017 -13.546 1.00 38.57 ?  393 HOH   B O    1 
HETATM 7048 O O    . HOH   E 3 .   ? 50.712 -30.827 8.650   1.00 28.95 ?  394 HOH   B O    1 
HETATM 7049 O O    . HOH   E 3 .   ? 24.621 -20.679 -10.501 1.00 39.75 ?  395 HOH   B O    1 
HETATM 7050 O O    . HOH   E 3 .   ? 34.452 -33.537 9.535   1.00 33.86 ?  396 HOH   B O    1 
HETATM 7051 O O    . HOH   E 3 .   ? 26.861 -30.695 -12.729 1.00 30.75 ?  397 HOH   B O    1 
HETATM 7052 O O    . HOH   E 3 .   ? 45.814 -20.327 15.227  1.00 52.56 ?  398 HOH   B O    1 
HETATM 7053 O O    . HOH   E 3 .   ? 57.635 -6.382  -2.358  1.00 36.34 ?  399 HOH   B O    1 
HETATM 7054 O O    . HOH   E 3 .   ? 40.957 -11.796 -22.365 1.00 42.84 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.6575 0.6477 0.7146 0.0034  -0.0270 0.0831  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6513 0.6465 0.6711 -0.0053 -0.0139 0.0463  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6550 0.6453 0.7064 0.0014  -0.0243 0.0817  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6489 0.6442 0.6669 -0.0060 -0.0138 0.0482  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6389 0.6333 0.6759 -0.0049 -0.0226 0.0810  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6367 0.6332 0.6519 -0.0093 -0.0163 0.0611  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6402 0.6353 0.6873 -0.0024 -0.0242 0.0839  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6396 0.6357 0.6602 -0.0087 -0.0170 0.0604  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6660 0.6526 0.7202 0.0040  -0.0236 0.0820  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6561 0.6507 0.6736 -0.0040 -0.0114 0.0395  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6703 0.6548 0.7223 0.0048  -0.0235 0.0817  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6585 0.6528 0.6747 -0.0033 -0.0106 0.0363  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6695 0.6553 0.7230 0.0048  -0.0232 0.0840  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6584 0.6529 0.6748 -0.0032 -0.0106 0.0368  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.6186 0.6170 0.6237 -0.0134 -0.0183 0.0758  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5778 0.5816 0.5360 -0.0269 -0.0143 0.0830  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.5284 0.5421 0.4794 -0.0372 -0.0014 0.0642  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.5282 0.5424 0.4594 -0.0407 -0.0028 0.0714  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5836 0.5836 0.4978 -0.0300 -0.0224 0.1074  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5872 0.5833 0.4607 -0.0339 -0.0312 0.1306  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5909 0.5829 0.4521 -0.0357 -0.0361 0.1370  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5861 0.5822 0.4502 -0.0339 -0.0323 0.1436  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4770 0.4980 0.4369 -0.0448 0.0105  0.0388  5   SER   A N   
47   C CA  . SER   A 5   ? 0.4255 0.4580 0.3982 -0.0502 0.0242  0.0122  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3680 0.4009 0.3374 -0.0465 0.0359  -0.0074 5   SER   A C   
49   O O   . SER   A 5   ? 0.3793 0.4144 0.3338 -0.0310 0.0345  -0.0265 5   SER   A O   
50   C CB  . SER   A 5   ? 0.4337 0.4724 0.4316 -0.0575 0.0241  0.0035  5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4375 0.4750 0.4462 -0.0639 0.0270  -0.0030 5   SER   A OG  
57   N N   A PHE   A 6   ? 0.3188 0.3561 0.2965 -0.0658 0.0574  0.0016  6   PHE   A N   
58   N N   B PHE   A 6   ? 0.3428 0.3730 0.3170 -0.0413 0.0308  -0.0093 6   PHE   A N   
59   C CA  A PHE   A 6   ? 0.2760 0.3147 0.2557 -0.0775 0.0700  0.0225  6   PHE   A CA  
60   C CA  B PHE   A 6   ? 0.3176 0.3448 0.2926 -0.0361 0.0241  -0.0090 6   PHE   A CA  
61   C C   A PHE   A 6   ? 0.2698 0.3170 0.2717 -0.0887 0.0852  0.0245  6   PHE   A C   
62   C C   B PHE   A 6   ? 0.3020 0.3297 0.2929 -0.0348 0.0220  -0.0102 6   PHE   A C   
63   O O   A PHE   A 6   ? 0.2757 0.3281 0.2994 -0.0938 0.0743  0.0380  6   PHE   A O   
64   O O   B PHE   A 6   ? 0.3024 0.3313 0.3012 -0.0362 0.0183  -0.0112 6   PHE   A O   
65   C CB  A PHE   A 6   ? 0.2595 0.2750 0.2317 -0.0657 0.0536  0.0333  6   PHE   A CB  
66   C CB  B PHE   A 6   ? 0.3095 0.3315 0.2717 -0.0320 0.0206  -0.0086 6   PHE   A CB  
67   C CG  A PHE   A 6   ? 0.2446 0.2500 0.2184 -0.0544 0.0425  0.0332  6   PHE   A CG  
68   C CG  B PHE   A 6   ? 0.3022 0.3196 0.2524 -0.0290 0.0170  -0.0086 6   PHE   A CG  
69   C CD1 A PHE   A 6   ? 0.2374 0.2398 0.2229 -0.0428 0.0350  0.0382  6   PHE   A CD1 
70   C CD1 B PHE   A 6   ? 0.2989 0.3149 0.2439 -0.0269 0.0154  -0.0073 6   PHE   A CD1 
71   C CD2 A PHE   A 6   ? 0.2487 0.2423 0.2236 -0.0381 0.0422  0.0290  6   PHE   A CD2 
72   C CD2 B PHE   A 6   ? 0.3003 0.3147 0.2451 -0.0267 0.0167  -0.0086 6   PHE   A CD2 
73   C CE1 A PHE   A 6   ? 0.2383 0.2349 0.2345 -0.0366 0.0340  0.0373  6   PHE   A CE1 
74   C CE1 B PHE   A 6   ? 0.2977 0.3122 0.2391 -0.0258 0.0157  -0.0056 6   PHE   A CE1 
75   C CE2 A PHE   A 6   ? 0.2451 0.2352 0.2368 -0.0321 0.0398  0.0213  6   PHE   A CE2 
76   C CE2 B PHE   A 6   ? 0.2988 0.3115 0.2389 -0.0255 0.0176  -0.0075 6   PHE   A CE2 
77   C CZ  A PHE   A 6   ? 0.2444 0.2289 0.2331 -0.0332 0.0312  0.0233  6   PHE   A CZ  
78   C CZ  B PHE   A 6   ? 0.2981 0.3106 0.2376 -0.0253 0.0160  -0.0063 6   PHE   A CZ  
97   N N   A SER   A 7   ? 0.2607 0.3089 0.2817 -0.0904 0.0914  0.0132  7   SER   A N   
98   N N   B SER   A 7   ? 0.2859 0.3134 0.2861 -0.0319 0.0216  -0.0107 7   SER   A N   
99   C CA  A SER   A 7   ? 0.2704 0.3125 0.3066 -0.0745 0.0908  -0.0033 7   SER   A CA  
100  C CA  B SER   A 7   ? 0.2712 0.2973 0.2804 -0.0290 0.0206  -0.0111 7   SER   A CA  
101  C C   A SER   A 7   ? 0.2545 0.2813 0.2949 -0.0696 0.1015  -0.0018 7   SER   A C   
102  C C   B SER   A 7   ? 0.2585 0.2797 0.2672 -0.0258 0.0202  -0.0101 7   SER   A C   
103  O O   A SER   A 7   ? 0.2648 0.2686 0.2912 -0.0724 0.0947  0.0033  7   SER   A O   
104  O O   B SER   A 7   ? 0.2581 0.2784 0.2663 -0.0272 0.0216  -0.0126 7   SER   A O   
105  C CB  A SER   A 7   ? 0.2909 0.3477 0.3279 -0.0582 0.0946  -0.0004 7   SER   A CB  
106  C CB  B SER   A 7   ? 0.2710 0.2986 0.2878 -0.0277 0.0182  -0.0132 7   SER   A CB  
107  O OG  A SER   A 7   ? 0.3059 0.3659 0.3691 -0.0512 0.0831  -0.0013 7   SER   A OG  
108  O OG  B SER   A 7   ? 0.2698 0.3010 0.2912 -0.0263 0.0162  -0.0144 7   SER   A OG  
119  N N   A GLY   A 8   ? 0.2372 0.2672 0.2974 -0.0633 0.0994  -0.0143 8   GLY   A N   
120  N N   B GLY   A 8   ? 0.2464 0.2643 0.2551 -0.0225 0.0177  -0.0081 8   GLY   A N   
121  C CA  A GLY   A 8   ? 0.2248 0.2462 0.3066 -0.0461 0.0976  -0.0183 8   GLY   A CA  
122  C CA  B GLY   A 8   ? 0.2349 0.2494 0.2470 -0.0167 0.0149  -0.0048 8   GLY   A CA  
123  C C   A GLY   A 8   ? 0.2096 0.2320 0.2953 -0.0341 0.0825  -0.0129 8   GLY   A C   
124  C C   B GLY   A 8   ? 0.2219 0.2359 0.2338 -0.0123 0.0089  -0.0010 8   GLY   A C   
125  O O   A GLY   A 8   ? 0.2060 0.2387 0.3228 -0.0182 0.0696  -0.0260 8   GLY   A O   
126  O O   B GLY   A 8   ? 0.2219 0.2355 0.2372 -0.0107 0.0057  -0.0028 8   GLY   A O   
133  N N   A TYR   A 9   ? 0.1881 0.2152 0.2677 -0.0288 0.0735  0.0148  9   TYR   A N   
134  N N   B TYR   A 9   ? 0.2078 0.2235 0.2218 -0.0083 0.0041  0.0056  9   TYR   A N   
135  C CA  A TYR   A 9   ? 0.1851 0.1985 0.2340 -0.0258 0.0561  0.0220  9   TYR   A CA  
136  C CA  B TYR   A 9   ? 0.1963 0.2117 0.2070 -0.0071 0.0022  0.0060  9   TYR   A CA  
137  C C   A TYR   A 9   ? 0.1864 0.1881 0.2393 -0.0204 0.0560  0.0511  9   TYR   A C   
138  C C   B TYR   A 9   ? 0.1847 0.2026 0.2022 -0.0022 0.0056  0.0090  9   TYR   A C   
139  O O   A TYR   A 9   ? 0.2085 0.2124 0.2618 -0.0321 0.0527  0.0494  9   TYR   A O   
140  O O   B TYR   A 9   ? 0.1860 0.2070 0.2069 -0.0008 0.0102  0.0110  9   TYR   A O   
141  C CB  A TYR   A 9   ? 0.1793 0.2080 0.2368 -0.0155 0.0467  0.0117  9   TYR   A CB  
142  C CB  B TYR   A 9   ? 0.1975 0.2130 0.2062 -0.0091 -0.0021 0.0032  9   TYR   A CB  
143  C CG  A TYR   A 9   ? 0.1751 0.2141 0.2319 -0.0033 0.0551  0.0031  9   TYR   A CG  
144  C CG  B TYR   A 9   ? 0.1992 0.2136 0.2020 -0.0099 -0.0018 0.0006  9   TYR   A CG  
145  C CD1 A TYR   A 9   ? 0.1797 0.2233 0.2423 -0.0173 0.0653  0.0068  9   TYR   A CD1 
146  C CD1 B TYR   A 9   ? 0.2019 0.2156 0.2047 -0.0133 0.0011  0.0007  9   TYR   A CD1 
147  C CD2 A TYR   A 9   ? 0.1722 0.2036 0.2251 -0.0006 0.0487  0.0194  9   TYR   A CD2 
148  C CD2 B TYR   A 9   ? 0.1991 0.2113 0.1971 -0.0097 -0.0022 0.0008  9   TYR   A CD2 
149  C CE1 A TYR   A 9   ? 0.1789 0.2269 0.2537 -0.0158 0.0691  0.0017  9   TYR   A CE1 
150  C CE1 B TYR   A 9   ? 0.2026 0.2161 0.2042 -0.0135 0.0020  -0.0013 9   TYR   A CE1 
151  C CE2 A TYR   A 9   ? 0.1718 0.2060 0.2315 -0.0058 0.0560  0.0061  9   TYR   A CE2 
152  C CE2 B TYR   A 9   ? 0.2012 0.2124 0.1995 -0.0111 0.0004  -0.0018 9   TYR   A CE2 
153  C CZ  A TYR   A 9   ? 0.1742 0.2197 0.2536 -0.0236 0.0721  0.0041  9   TYR   A CZ  
154  C CZ  B TYR   A 9   ? 0.2035 0.2151 0.2055 -0.0146 0.0034  -0.0014 9   TYR   A CZ  
155  O OH  A TYR   A 9   ? 0.1766 0.2312 0.2760 -0.0380 0.0622  -0.0001 9   TYR   A OH  
156  O OH  B TYR   A 9   ? 0.2091 0.2179 0.2109 -0.0168 0.0029  -0.0007 9   TYR   A OH  
175  N N   A LEU   A 10  ? 0.1664 0.1762 0.2421 -0.0170 0.0400  0.0476  10  LEU   A N   
176  N N   B LEU   A 10  ? 0.1723 0.1934 0.1959 -0.0019 0.0028  0.0050  10  LEU   A N   
177  C CA  A LEU   A 10  ? 0.1673 0.1790 0.2514 -0.0244 0.0265  0.0601  10  LEU   A CA  
178  C CA  B LEU   A 10  ? 0.1635 0.1875 0.1912 -0.0035 -0.0016 0.0038  10  LEU   A CA  
179  C C   A LEU   A 10  ? 0.1624 0.1706 0.2293 -0.0322 0.0152  0.0571  10  LEU   A C   
180  C C   B LEU   A 10  ? 0.1633 0.1742 0.1829 -0.0080 -0.0037 0.0152  10  LEU   A C   
181  O O   A LEU   A 10  ? 0.1627 0.1588 0.2356 -0.0341 0.0298  0.0485  10  LEU   A O   
182  O O   B LEU   A 10  ? 0.1632 0.1719 0.1884 -0.0066 -0.0043 0.0214  10  LEU   A O   
183  C CB  A LEU   A 10  ? 0.1756 0.1911 0.2886 -0.0231 0.0101  0.0863  10  LEU   A CB  
184  C CB  B LEU   A 10  ? 0.1555 0.1958 0.1954 -0.0026 -0.0056 -0.0039 10  LEU   A CB  
185  C CG  A LEU   A 10  ? 0.2040 0.1980 0.3362 -0.0197 -0.0365 0.1050  10  LEU   A CG  
186  C CG  B LEU   A 10  ? 0.1488 0.2052 0.2028 -0.0028 -0.0156 -0.0139 10  LEU   A CG  
187  C CD1 A LEU   A 10  ? 0.2239 0.2043 0.3755 -0.0254 -0.0347 0.0967  10  LEU   A CD1 
188  C CD1 B LEU   A 10  ? 0.1450 0.2102 0.2043 -0.0050 -0.0116 -0.0203 10  LEU   A CD1 
189  C CD2 A LEU   A 10  ? 0.2302 0.2225 0.3642 -0.0126 -0.0181 0.0766  10  LEU   A CD2 
190  C CD2 B LEU   A 10  ? 0.1480 0.2118 0.2059 -0.0013 -0.0167 -0.0215 10  LEU   A CD2 
213  N N   A LYS   A 11  ? 0.1628 0.1772 0.2159 -0.0301 0.0175  0.0594  11  LYS   A N   
214  N N   B LYS   A 11  ? 0.1651 0.1645 0.1728 -0.0124 -0.0023 0.0200  11  LYS   A N   
215  C CA  A LYS   A 11  ? 0.1602 0.1777 0.2190 -0.0306 0.0052  0.0572  11  LYS   A CA  
216  C CA  B LYS   A 11  ? 0.1666 0.1537 0.1653 -0.0163 0.0017  0.0248  11  LYS   A CA  
217  C C   A LYS   A 11  ? 0.1565 0.1783 0.2142 -0.0362 0.0131  0.0514  11  LYS   A C   
218  C C   B LYS   A 11  ? 0.1666 0.1411 0.1548 -0.0130 0.0052  0.0235  11  LYS   A C   
219  O O   A LYS   A 11  ? 0.1724 0.2060 0.2432 -0.0631 0.0205  0.0316  11  LYS   A O   
220  O O   B LYS   A 11  ? 0.1641 0.1261 0.1501 -0.0120 0.0035  0.0184  11  LYS   A O   
221  C CB  A LYS   A 11  ? 0.1639 0.1728 0.2081 -0.0303 0.0052  0.0379  11  LYS   A CB  
222  C CB  B LYS   A 11  ? 0.1709 0.1547 0.1666 -0.0208 0.0032  0.0235  11  LYS   A CB  
223  C CG  A LYS   A 11  ? 0.1828 0.1714 0.2053 -0.0304 0.0162  0.0433  11  LYS   A CG  
224  C CG  B LYS   A 11  ? 0.1761 0.1570 0.1726 -0.0233 0.0071  0.0213  11  LYS   A CG  
225  C CD  A LYS   A 11  ? 0.1936 0.1704 0.2072 -0.0267 0.0151  0.0334  11  LYS   A CD  
226  C CD  B LYS   A 11  ? 0.1804 0.1596 0.1793 -0.0236 0.0105  0.0166  11  LYS   A CD  
227  C CE  A LYS   A 11  ? 0.2052 0.1695 0.2097 -0.0208 0.0143  0.0376  11  LYS   A CE  
228  C CE  B LYS   A 11  ? 0.1809 0.1591 0.1837 -0.0256 0.0088  0.0125  11  LYS   A CE  
229  N NZ  A LYS   A 11  ? 0.2053 0.1724 0.2155 -0.0021 0.0027  0.0412  11  LYS   A NZ  
230  N NZ  B LYS   A 11  ? 0.1798 0.1592 0.1880 -0.0247 0.0061  0.0113  11  LYS   A NZ  
257  N N   A LEU   A 12  ? 0.1424 0.1794 0.2083 -0.0326 0.0085  0.0427  12  LEU   A N   
258  N N   B LEU   A 12  ? 0.1682 0.1518 0.1583 -0.0090 0.0029  0.0201  12  LEU   A N   
259  C CA  A LEU   A 12  ? 0.1393 0.1961 0.2084 -0.0258 0.0015  0.0545  12  LEU   A CA  
260  C CA  B LEU   A 12  ? 0.1718 0.1681 0.1660 -0.0039 0.0018  0.0167  12  LEU   A CA  
261  C C   A LEU   A 12  ? 0.1533 0.1847 0.2102 -0.0362 0.0040  0.0555  12  LEU   A C   
262  C C   B LEU   A 12  ? 0.1768 0.1756 0.1701 -0.0040 0.0025  0.0148  12  LEU   A C   
263  O O   A LEU   A 12  ? 0.1608 0.1947 0.2258 -0.0387 0.0097  0.0472  12  LEU   A O   
264  O O   B LEU   A 12  ? 0.1774 0.1777 0.1699 -0.0035 0.0018  0.0141  12  LEU   A O   
265  C CB  A LEU   A 12  ? 0.1596 0.1962 0.2208 -0.0250 0.0048  0.0604  12  LEU   A CB  
266  C CB  B LEU   A 12  ? 0.1754 0.1718 0.1738 0.0002  0.0026  0.0149  12  LEU   A CB  
267  C CG  A LEU   A 12  ? 0.1677 0.1995 0.2505 -0.0181 0.0181  0.0643  12  LEU   A CG  
268  C CG  B LEU   A 12  ? 0.1763 0.1720 0.1818 0.0023  0.0058  0.0128  12  LEU   A CG  
269  C CD1 A LEU   A 12  ? 0.1854 0.2078 0.2643 -0.0102 0.0290  0.0765  12  LEU   A CD1 
270  C CD1 B LEU   A 12  ? 0.1780 0.1744 0.1806 0.0025  0.0062  0.0098  12  LEU   A CD1 
271  C CD2 A LEU   A 12  ? 0.1660 0.2038 0.2574 -0.0193 0.0110  0.0464  12  LEU   A CD2 
272  C CD2 B LEU   A 12  ? 0.1775 0.1717 0.1900 0.0043  0.0053  0.0151  12  LEU   A CD2 
295  N N   A THR   A 13  ? 0.1505 0.1709 0.2127 -0.0260 0.0028  0.0457  13  THR   A N   
296  N N   B THR   A 13  ? 0.1788 0.1793 0.1768 -0.0016 0.0048  0.0111  13  THR   A N   
297  C CA  A THR   A 13  ? 0.1557 0.1737 0.2151 -0.0221 0.0069  0.0359  13  THR   A CA  
298  C CA  B THR   A 13  ? 0.1803 0.1847 0.1832 -0.0011 0.0068  0.0072  13  THR   A CA  
299  C C   A THR   A 13  ? 0.1557 0.1674 0.2124 -0.0292 0.0075  0.0408  13  THR   A C   
300  C C   B THR   A 13  ? 0.1802 0.1848 0.1884 -0.0036 0.0060  0.0089  13  THR   A C   
301  O O   A THR   A 13  ? 0.1581 0.1626 0.2154 -0.0217 0.0074  0.0401  13  THR   A O   
302  O O   B THR   A 13  ? 0.1804 0.1857 0.1890 -0.0020 0.0082  0.0096  13  THR   A O   
303  C CB  A THR   A 13  ? 0.1659 0.1928 0.2286 -0.0245 0.0154  0.0370  13  THR   A CB  
304  C CB  B THR   A 13  ? 0.1836 0.1921 0.1877 0.0011  0.0101  0.0050  13  THR   A CB  
305  O OG1 A THR   A 13  ? 0.1616 0.1861 0.2380 -0.0329 0.0122  0.0480  13  THR   A OG1 
306  O OG1 B THR   A 13  ? 0.1850 0.1935 0.1930 0.0010  0.0108  0.0029  13  THR   A OG1 
307  C CG2 A THR   A 13  ? 0.1774 0.2123 0.2569 -0.0257 0.0236  0.0247  13  THR   A CG2 
308  C CG2 B THR   A 13  ? 0.1861 0.1967 0.1925 0.0017  0.0112  0.0037  13  THR   A CG2 
323  N N   A ASP   A 14  ? 0.1597 0.1717 0.2255 -0.0318 0.0138  0.0423  14  ASP   A N   
324  N N   B ASP   A 14  ? 0.1810 0.1848 0.1991 -0.0044 0.0039  0.0095  14  ASP   A N   
325  C CA  A ASP   A 14  ? 0.1584 0.1838 0.2447 -0.0231 0.0057  0.0517  14  ASP   A CA  
326  C CA  B ASP   A 14  ? 0.1804 0.1850 0.2105 -0.0050 0.0029  0.0157  14  ASP   A CA  
327  C C   A ASP   A 14  ? 0.1550 0.1759 0.2143 -0.0186 0.0023  0.0532  14  ASP   A C   
328  C C   B ASP   A 14  ? 0.1689 0.1735 0.1965 -0.0101 0.0044  0.0276  14  ASP   A C   
329  O O   A ASP   A 14  ? 0.1775 0.1897 0.2344 -0.0307 -0.0071 0.0550  14  ASP   A O   
330  O O   B ASP   A 14  ? 0.1700 0.1741 0.1901 -0.0037 -0.0014 0.0211  14  ASP   A O   
331  C CB  A ASP   A 14  ? 0.1827 0.2182 0.3115 -0.0264 0.0057  0.0679  14  ASP   A CB  
332  C CB  B ASP   A 14  ? 0.1951 0.1985 0.2408 -0.0015 0.0012  0.0139  14  ASP   A CB  
333  C CG  A ASP   A 14  ? 0.2169 0.2690 0.3969 -0.0291 0.0140  0.0701  14  ASP   A CG  
334  C CG  B ASP   A 14  ? 0.2056 0.2120 0.2708 0.0003  0.0018  0.0148  14  ASP   A CG  
335  O OD1 A ASP   A 14  ? 0.2252 0.2783 0.4122 -0.0187 0.0013  0.0805  14  ASP   A OD1 
336  O OD1 B ASP   A 14  ? 0.2067 0.2124 0.2779 -0.0000 0.0016  0.0182  14  ASP   A OD1 
337  O OD2 A ASP   A 14  ? 0.2482 0.3136 0.4480 -0.0203 0.0081  0.0532  14  ASP   A OD2 
338  O OD2 B ASP   A 14  ? 0.2143 0.2234 0.2826 0.0024  -0.0004 0.0135  14  ASP   A OD2 
347  N N   . ASN   A 15  ? 0.1603 0.1649 0.2012 -0.0264 0.0113  0.0485  15  ASN   A N   
348  C CA  . ASN   A 15  ? 0.1574 0.1646 0.2159 -0.0182 -0.0002 0.0423  15  ASN   A CA  
349  C C   . ASN   A 15  ? 0.1581 0.1626 0.2332 -0.0172 0.0097  0.0450  15  ASN   A C   
350  O O   . ASN   A 15  ? 0.1652 0.1589 0.2954 -0.0208 -0.0131 0.0448  15  ASN   A O   
351  C CB  . ASN   A 15  ? 0.1543 0.1647 0.2150 -0.0136 -0.0017 0.0350  15  ASN   A CB  
352  C CG  . ASN   A 15  ? 0.1468 0.1704 0.2236 -0.0143 0.0019  0.0241  15  ASN   A CG  
353  O OD1 . ASN   A 15  ? 0.1671 0.1791 0.2469 -0.0283 0.0071  0.0227  15  ASN   A OD1 
354  N ND2 . ASN   A 15  ? 0.1588 0.1760 0.2140 -0.0221 0.0133  0.0281  15  ASN   A ND2 
362  N N   A VAL   A 16  ? 0.1592 0.1647 0.2296 -0.0101 0.0066  0.0491  16  VAL   A N   
363  N N   B VAL   A 16  ? 0.1603 0.1655 0.2111 -0.0163 0.0076  0.0355  16  VAL   A N   
364  C CA  A VAL   A 16  ? 0.1631 0.1613 0.2375 -0.0033 0.0074  0.0555  16  VAL   A CA  
365  C CA  B VAL   A 16  ? 0.1634 0.1671 0.1930 -0.0157 0.0059  0.0256  16  VAL   A CA  
366  C C   A VAL   A 16  ? 0.1530 0.1542 0.2214 -0.0168 0.0110  0.0501  16  VAL   A C   
367  C C   B VAL   A 16  ? 0.1660 0.1648 0.1775 -0.0135 0.0015  0.0170  16  VAL   A C   
368  O O   A VAL   A 16  ? 0.1513 0.1508 0.2286 -0.0200 0.0180  0.0322  16  VAL   A O   
369  O O   B VAL   A 16  ? 0.1657 0.1648 0.1775 -0.0112 -0.0002 0.0162  16  VAL   A O   
370  C CB  A VAL   A 16  ? 0.1734 0.1708 0.2487 0.0101  0.0249  0.0557  16  VAL   A CB  
371  C CB  B VAL   A 16  ? 0.1632 0.1717 0.1914 -0.0183 0.0112  0.0231  16  VAL   A CB  
372  C CG1 A VAL   A 16  ? 0.1789 0.1837 0.2517 0.0174  0.0370  0.0544  16  VAL   A CG1 
373  C CG1 B VAL   A 16  ? 0.1651 0.1760 0.1927 -0.0153 0.0118  0.0223  16  VAL   A CG1 
374  C CG2 A VAL   A 16  ? 0.1768 0.1796 0.2614 0.0147  0.0320  0.0566  16  VAL   A CG2 
375  C CG2 B VAL   A 16  ? 0.1614 0.1734 0.1938 -0.0243 0.0133  0.0203  16  VAL   A CG2 
394  N N   A TYR   A 17  ? 0.1454 0.1490 0.2312 -0.0147 0.0185  0.0465  17  TYR   A N   
395  N N   B TYR   A 17  ? 0.1682 0.1622 0.1683 -0.0111 0.0000  0.0076  17  TYR   A N   
396  C CA  A TYR   A 17  ? 0.1533 0.1546 0.2223 -0.0169 0.0240  0.0465  17  TYR   A CA  
397  C CA  B TYR   A 17  ? 0.1720 0.1608 0.1603 -0.0116 0.0001  0.0016  17  TYR   A CA  
398  C C   A TYR   A 17  ? 0.1616 0.1494 0.2330 -0.0092 0.0240  0.0479  17  TYR   A C   
399  C C   B TYR   A 17  ? 0.1703 0.1611 0.1540 -0.0112 0.0031  -0.0044 17  TYR   A C   
400  O O   A TYR   A 17  ? 0.1534 0.1446 0.2282 -0.0177 0.0219  0.0542  17  TYR   A O   
401  O O   B TYR   A 17  ? 0.1671 0.1573 0.1626 -0.0110 0.0139  -0.0059 17  TYR   A O   
402  C CB  A TYR   A 17  ? 0.1689 0.1610 0.2294 -0.0273 0.0141  0.0477  17  TYR   A CB  
403  C CB  B TYR   A 17  ? 0.1807 0.1606 0.1647 -0.0107 -0.0050 0.0030  17  TYR   A CB  
404  C CG  A TYR   A 17  ? 0.1927 0.1704 0.2221 -0.0303 0.0093  0.0431  17  TYR   A CG  
405  C CG  B TYR   A 17  ? 0.1914 0.1607 0.1681 -0.0089 -0.0103 0.0053  17  TYR   A CG  
406  C CD1 A TYR   A 17  ? 0.2071 0.1806 0.2287 -0.0191 -0.0006 0.0397  17  TYR   A CD1 
407  C CD1 B TYR   A 17  ? 0.1956 0.1593 0.1699 -0.0065 -0.0128 0.0097  17  TYR   A CD1 
408  C CD2 A TYR   A 17  ? 0.2071 0.1801 0.2151 -0.0420 0.0106  0.0455  17  TYR   A CD2 
409  C CD2 B TYR   A 17  ? 0.1986 0.1644 0.1733 -0.0101 -0.0111 0.0072  17  TYR   A CD2 
410  C CE1 A TYR   A 17  ? 0.2197 0.1757 0.2266 -0.0171 -0.0095 0.0374  17  TYR   A CE1 
411  C CE1 B TYR   A 17  ? 0.1999 0.1583 0.1767 -0.0065 -0.0150 0.0108  17  TYR   A CE1 
412  C CE2 A TYR   A 17  ? 0.2270 0.1769 0.2195 -0.0421 0.0048  0.0311  17  TYR   A CE2 
413  C CE2 B TYR   A 17  ? 0.2043 0.1631 0.1772 -0.0118 -0.0131 0.0059  17  TYR   A CE2 
414  C CZ  A TYR   A 17  ? 0.2355 0.1704 0.2169 -0.0301 -0.0074 0.0480  17  TYR   A CZ  
415  C CZ  B TYR   A 17  ? 0.2066 0.1605 0.1771 -0.0098 -0.0155 0.0104  17  TYR   A CZ  
416  O OH  A TYR   A 17  ? 0.2481 0.1790 0.2263 -0.0258 -0.0018 0.0406  17  TYR   A OH  
417  O OH  B TYR   A 17  ? 0.2129 0.1607 0.1796 -0.0088 -0.0170 0.0051  17  TYR   A OH  
436  N N   A ILE   A 18  ? 0.1543 0.1546 0.2332 -0.0098 0.0273  0.0592  18  ILE   A N   
437  N N   B ILE   A 18  ? 0.1672 0.1663 0.1423 -0.0168 -0.0064 -0.0029 18  ILE   A N   
438  C CA  A ILE   A 18  ? 0.1542 0.1627 0.2392 -0.0136 0.0272  0.0459  18  ILE   A CA  
439  C CA  B ILE   A 18  ? 0.1670 0.1747 0.1375 -0.0129 -0.0152 -0.0038 18  ILE   A CA  
440  C C   A ILE   A 18  ? 0.1598 0.1631 0.2557 -0.0260 0.0256  0.0628  18  ILE   A C   
441  C C   B ILE   A 18  ? 0.1687 0.1865 0.1330 -0.0102 -0.0210 -0.0086 18  ILE   A C   
442  O O   A ILE   A 18  ? 0.1563 0.1775 0.2532 -0.0296 0.0287  0.0654  18  ILE   A O   
443  O O   B ILE   A 18  ? 0.1656 0.1930 0.1337 -0.0106 -0.0202 -0.0092 18  ILE   A O   
444  C CB  A ILE   A 18  ? 0.1709 0.1690 0.2172 -0.0116 0.0220  0.0672  18  ILE   A CB  
445  C CB  B ILE   A 18  ? 0.1655 0.1715 0.1287 -0.0160 -0.0134 0.0112  18  ILE   A CB  
446  C CG1 A ILE   A 18  ? 0.1799 0.1826 0.2263 -0.0034 0.0121  0.0707  18  ILE   A CG1 
447  C CG1 B ILE   A 18  ? 0.1654 0.1714 0.1301 -0.0178 -0.0032 0.0229  18  ILE   A CG1 
448  C CG2 A ILE   A 18  ? 0.1875 0.1783 0.2297 -0.0196 0.0170  0.0563  18  ILE   A CG2 
449  C CG2 B ILE   A 18  ? 0.1683 0.1747 0.1316 -0.0173 -0.0180 0.0154  18  ILE   A CG2 
450  C CD1 A ILE   A 18  ? 0.2008 0.1945 0.2456 0.0095  0.0083  0.0645  18  ILE   A CD1 
451  C CD1 B ILE   A 18  ? 0.1665 0.1742 0.1304 -0.0184 0.0052  0.0250  18  ILE   A CD1 
474  N N   A LYS   A 19  ? 0.1593 0.1750 0.2715 -0.0114 0.0594  0.0566  19  LYS   A N   
475  N N   B LYS   A 19  ? 0.1736 0.1920 0.1390 -0.0025 -0.0177 -0.0132 19  LYS   A N   
476  C CA  A LYS   A 19  ? 0.1833 0.1783 0.2885 -0.0003 0.0671  0.0582  19  LYS   A CA  
477  C CA  B LYS   A 19  ? 0.1817 0.1982 0.1661 0.0030  -0.0071 -0.0157 19  LYS   A CA  
478  C C   A LYS   A 19  ? 0.1691 0.1660 0.2975 0.0090  0.0628  0.0589  19  LYS   A C   
479  C C   B LYS   A 19  ? 0.1850 0.2006 0.1812 0.0074  -0.0051 -0.0107 19  LYS   A C   
480  O O   A LYS   A 19  ? 0.1687 0.1641 0.3023 0.0024  0.0440  0.0644  19  LYS   A O   
481  O O   B LYS   A 19  ? 0.1856 0.2002 0.1792 0.0079  -0.0078 -0.0077 19  LYS   A O   
482  C CB  A LYS   A 19  ? 0.1913 0.2088 0.2963 -0.0002 0.0810  0.0466  19  LYS   A CB  
483  C CB  B LYS   A 19  ? 0.1842 0.2040 0.1798 0.0049  0.0027  -0.0209 19  LYS   A CB  
484  C CG  A LYS   A 19  ? 0.2305 0.2297 0.3064 -0.0014 0.0756  0.0346  19  LYS   A CG  
485  C CG  B LYS   A 19  ? 0.1921 0.2080 0.1956 0.0077  0.0117  -0.0219 19  LYS   A CG  
486  C CD  A LYS   A 19  ? 0.2647 0.2479 0.3078 0.0030  0.0766  0.0293  19  LYS   A CD  
487  C CD  B LYS   A 19  ? 0.1994 0.2123 0.2102 0.0102  0.0212  -0.0210 19  LYS   A CD  
488  C CE  A LYS   A 19  ? 0.2857 0.2500 0.3126 -0.0017 0.0740  0.0240  19  LYS   A CE  
489  C CE  B LYS   A 19  ? 0.2039 0.2150 0.2211 0.0092  0.0282  -0.0198 19  LYS   A CE  
490  N NZ  A LYS   A 19  ? 0.3023 0.2521 0.3001 -0.0121 0.0927  0.0142  19  LYS   A NZ  
491  N NZ  B LYS   A 19  ? 0.2053 0.2168 0.2259 0.0092  0.0320  -0.0202 19  LYS   A NZ  
518  N N   A ASN   A 20  ? 0.1795 0.1764 0.3305 0.0119  0.0663  0.0672  20  ASN   A N   
519  N N   B ASN   A 20  ? 0.1918 0.2045 0.2036 0.0097  0.0051  -0.0105 20  ASN   A N   
520  C CA  A ASN   A 20  ? 0.1857 0.1985 0.3575 0.0324  0.0690  0.0608  20  ASN   A CA  
521  C CA  B ASN   A 20  ? 0.1977 0.2102 0.2286 0.0123  0.0150  -0.0068 20  ASN   A CA  
522  C C   A ASN   A 20  ? 0.2128 0.2027 0.3548 0.0203  0.0807  0.0409  20  ASN   A C   
523  C C   B ASN   A 20  ? 0.2021 0.2053 0.2311 0.0026  0.0259  -0.0043 20  ASN   A C   
524  O O   A ASN   A 20  ? 0.2276 0.2156 0.3521 0.0019  0.0820  0.0288  20  ASN   A O   
525  O O   B ASN   A 20  ? 0.2051 0.2072 0.2343 0.0025  0.0327  -0.0044 20  ASN   A O   
526  C CB  A ASN   A 20  ? 0.1814 0.2108 0.3869 0.0443  0.0753  0.0767  20  ASN   A CB  
527  C CB  B ASN   A 20  ? 0.2004 0.2182 0.2513 0.0223  0.0163  -0.0036 20  ASN   A CB  
528  C CG  A ASN   A 20  ? 0.2010 0.2246 0.4338 0.0570  0.0813  0.0886  20  ASN   A CG  
529  C CG  B ASN   A 20  ? 0.2062 0.2247 0.2748 0.0314  0.0185  -0.0011 20  ASN   A CG  
530  O OD1 A ASN   A 20  ? 0.2383 0.2401 0.4824 0.0681  0.1067  0.0844  20  ASN   A OD1 
531  O OD1 B ASN   A 20  ? 0.2152 0.2278 0.2953 0.0374  0.0247  -0.0022 20  ASN   A OD1 
532  N ND2 A ASN   A 20  ? 0.2160 0.2279 0.4472 0.0507  0.0637  0.0925  20  ASN   A ND2 
533  N ND2 B ASN   A 20  ? 0.2071 0.2251 0.2791 0.0319  0.0151  0.0020  20  ASN   A ND2 
546  N N   A ALA   A 21  ? 0.2174 0.1977 0.3575 0.0181  0.0715  0.0297  21  ALA   A N   
547  N N   B ALA   A 21  ? 0.2014 0.1974 0.2302 -0.0082 0.0232  -0.0018 21  ALA   A N   
548  C CA  A ALA   A 21  ? 0.2231 0.1995 0.3454 0.0136  0.0740  0.0371  21  ALA   A CA  
549  C CA  B ALA   A 21  ? 0.2004 0.1901 0.2268 -0.0193 0.0272  0.0034  21  ALA   A CA  
550  C C   A ALA   A 21  ? 0.2137 0.2073 0.3400 0.0103  0.0721  0.0328  21  ALA   A C   
551  C C   B ALA   A 21  ? 0.1938 0.1844 0.2185 -0.0290 0.0374  0.0097  21  ALA   A C   
552  O O   A ALA   A 21  ? 0.2125 0.2154 0.3309 0.0136  0.0701  0.0351  21  ALA   A O   
553  O O   B ALA   A 21  ? 0.1901 0.1740 0.2134 -0.0350 0.0432  0.0105  21  ALA   A O   
554  C CB  A ALA   A 21  ? 0.2404 0.2079 0.3610 0.0106  0.0636  0.0464  21  ALA   A CB  
555  C CB  B ALA   A 21  ? 0.2021 0.1899 0.2364 -0.0150 0.0217  -0.0016 21  ALA   A CB  
566  N N   A ASP   A 22  ? 0.2200 0.1980 0.3389 0.0008  0.0739  0.0396  22  ASP   A N   
567  N N   B ASP   A 22  ? 0.1939 0.1867 0.2140 -0.0318 0.0458  0.0169  22  ASP   A N   
568  C CA  A ASP   A 22  ? 0.2182 0.1955 0.3287 0.0029  0.0571  0.0378  22  ASP   A CA  
569  C CA  B ASP   A 22  ? 0.1957 0.1909 0.2144 -0.0314 0.0408  0.0169  22  ASP   A CA  
570  C C   A ASP   A 22  ? 0.2013 0.2011 0.2810 -0.0075 0.0646  0.0367  22  ASP   A C   
571  C C   B ASP   A 22  ? 0.1940 0.1914 0.2011 -0.0367 0.0383  0.0148  22  ASP   A C   
572  O O   A ASP   A 22  ? 0.2095 0.2130 0.2829 -0.0133 0.0654  0.0367  22  ASP   A O   
573  O O   B ASP   A 22  ? 0.1933 0.1887 0.2007 -0.0461 0.0416  0.0142  22  ASP   A O   
574  C CB  A ASP   A 22  ? 0.2430 0.2034 0.3850 0.0045  0.0539  0.0290  22  ASP   A CB  
575  C CB  B ASP   A 22  ? 0.1978 0.1957 0.2278 -0.0224 0.0434  0.0168  22  ASP   A CB  
576  C CG  A ASP   A 22  ? 0.2597 0.2107 0.4423 -0.0007 0.0392  0.0375  22  ASP   A CG  
577  C CG  B ASP   A 22  ? 0.1993 0.1961 0.2371 -0.0171 0.0447  0.0210  22  ASP   A CG  
578  O OD1 A ASP   A 22  ? 0.2558 0.2020 0.4541 -0.0166 0.0240  0.0674  22  ASP   A OD1 
579  O OD1 B ASP   A 22  ? 0.2016 0.1888 0.2359 -0.0156 0.0504  0.0243  22  ASP   A OD1 
580  O OD2 A ASP   A 22  ? 0.2791 0.2256 0.4833 0.0109  0.0445  0.0218  22  ASP   A OD2 
581  O OD2 B ASP   A 22  ? 0.1978 0.2044 0.2452 -0.0161 0.0418  0.0235  22  ASP   A OD2 
590  N N   A ILE   A 23  ? 0.1980 0.2036 0.2622 -0.0081 0.0550  0.0281  23  ILE   A N   
591  N N   B ILE   A 23  ? 0.1956 0.1956 0.1939 -0.0276 0.0301  0.0146  23  ILE   A N   
592  C CA  A ILE   A 23  ? 0.1911 0.2017 0.2340 -0.0098 0.0450  0.0292  23  ILE   A CA  
593  C CA  B ILE   A 23  ? 0.1969 0.2021 0.1919 -0.0225 0.0165  0.0139  23  ILE   A CA  
594  C C   A ILE   A 23  ? 0.1855 0.2118 0.2307 -0.0072 0.0698  0.0248  23  ILE   A C   
595  C C   B ILE   A 23  ? 0.2052 0.2105 0.1989 -0.0224 0.0206  0.0111  23  ILE   A C   
596  O O   A ILE   A 23  ? 0.2004 0.2091 0.2206 -0.0029 0.0640  0.0210  23  ILE   A O   
597  O O   B ILE   A 23  ? 0.2062 0.2084 0.1977 -0.0212 0.0211  0.0068  23  ILE   A O   
598  C CB  A ILE   A 23  ? 0.2004 0.1939 0.2052 -0.0052 0.0437  0.0262  23  ILE   A CB  
599  C CB  B ILE   A 23  ? 0.1936 0.1965 0.1824 -0.0174 0.0061  0.0159  23  ILE   A CB  
600  C CG1 A ILE   A 23  ? 0.2022 0.1957 0.1997 -0.0055 0.0381  0.0108  23  ILE   A CG1 
601  C CG1 B ILE   A 23  ? 0.1913 0.1962 0.1777 -0.0151 -0.0048 0.0144  23  ILE   A CG1 
602  C CG2 A ILE   A 23  ? 0.2062 0.1974 0.2069 -0.0023 0.0527  0.0261  23  ILE   A CG2 
603  C CG2 B ILE   A 23  ? 0.1924 0.1948 0.1822 -0.0136 0.0052  0.0155  23  ILE   A CG2 
604  C CD1 A ILE   A 23  ? 0.2126 0.1960 0.2080 -0.0030 0.0162  0.0001  23  ILE   A CD1 
605  C CD1 B ILE   A 23  ? 0.1875 0.1947 0.1782 -0.0127 -0.0141 0.0112  23  ILE   A CD1 
628  N N   A VAL   A 24  ? 0.2010 0.2210 0.2528 -0.0251 0.0676  0.0157  24  VAL   A N   
629  N N   B VAL   A 24  ? 0.2165 0.2229 0.2154 -0.0226 0.0196  0.0093  24  VAL   A N   
630  C CA  A VAL   A 24  ? 0.2241 0.2251 0.2702 -0.0303 0.0643  0.0102  24  VAL   A CA  
631  C CA  B VAL   A 24  ? 0.2293 0.2341 0.2295 -0.0179 0.0193  0.0075  24  VAL   A CA  
632  C C   A VAL   A 24  ? 0.2274 0.2416 0.2697 -0.0344 0.0685  -0.0025 24  VAL   A C   
633  C C   B VAL   A 24  ? 0.2386 0.2449 0.2383 -0.0154 0.0203  0.0024  24  VAL   A C   
634  O O   A VAL   A 24  ? 0.2410 0.2375 0.2720 -0.0216 0.0706  -0.0035 24  VAL   A O   
635  O O   B VAL   A 24  ? 0.2407 0.2457 0.2390 -0.0125 0.0210  0.0023  24  VAL   A O   
636  C CB  A VAL   A 24  ? 0.2355 0.2257 0.2957 -0.0349 0.0664  0.0176  24  VAL   A CB  
637  C CB  B VAL   A 24  ? 0.2322 0.2375 0.2377 -0.0176 0.0161  0.0123  24  VAL   A CB  
638  C CG1 A VAL   A 24  ? 0.2481 0.2319 0.3173 -0.0237 0.0634  0.0043  24  VAL   A CG1 
639  C CG1 B VAL   A 24  ? 0.2363 0.2408 0.2471 -0.0160 0.0136  0.0147  24  VAL   A CG1 
640  C CG2 A VAL   A 24  ? 0.2504 0.2357 0.3101 -0.0203 0.0793  0.0334  24  VAL   A CG2 
641  C CG2 B VAL   A 24  ? 0.2338 0.2382 0.2374 -0.0171 0.0153  0.0121  24  VAL   A CG2 
660  N N   A GLU   A 25  ? 0.2327 0.2776 0.2760 -0.0380 0.0875  -0.0131 25  GLU   A N   
661  N N   B GLU   A 25  ? 0.2469 0.2559 0.2504 -0.0154 0.0233  -0.0013 25  GLU   A N   
662  C CA  A GLU   A 25  ? 0.2558 0.3100 0.2792 -0.0285 0.1017  -0.0183 25  GLU   A CA  
663  C CA  B GLU   A 25  ? 0.2573 0.2671 0.2671 -0.0170 0.0246  -0.0014 25  GLU   A CA  
664  C C   A GLU   A 25  ? 0.2506 0.3105 0.2503 -0.0432 0.1004  -0.0145 25  GLU   A C   
665  C C   B GLU   A 25  ? 0.2576 0.2691 0.2541 -0.0201 0.0242  -0.0033 25  GLU   A C   
666  O O   A GLU   A 25  ? 0.2616 0.3205 0.2513 -0.0498 0.1073  -0.0186 25  GLU   A O   
667  O O   B GLU   A 25  ? 0.2590 0.2702 0.2561 -0.0219 0.0224  -0.0055 25  GLU   A O   
668  C CB  A GLU   A 25  ? 0.2871 0.3401 0.3229 -0.0180 0.1087  -0.0134 25  GLU   A CB  
669  C CB  B GLU   A 25  ? 0.2673 0.2752 0.2948 -0.0164 0.0271  0.0002  25  GLU   A CB  
670  C CG  A GLU   A 25  ? 0.3251 0.3693 0.3832 -0.0143 0.0929  -0.0121 25  GLU   A CG  
671  C CG  B GLU   A 25  ? 0.2786 0.2834 0.3237 -0.0159 0.0282  0.0023  25  GLU   A CG  
672  C CD  A GLU   A 25  ? 0.3577 0.3958 0.4420 -0.0105 0.0783  -0.0066 25  GLU   A CD  
673  C CD  B GLU   A 25  ? 0.2880 0.2894 0.3477 -0.0162 0.0279  0.0038  25  GLU   A CD  
674  O OE1 A GLU   A 25  ? 0.3719 0.4065 0.4582 -0.0038 0.0584  -0.0106 25  GLU   A OE1 
675  O OE1 B GLU   A 25  ? 0.2908 0.2907 0.3537 -0.0155 0.0272  0.0068  25  GLU   A OE1 
676  O OE2 A GLU   A 25  ? 0.3678 0.4060 0.4721 -0.0113 0.0758  -0.0148 25  GLU   A OE2 
677  O OE2 B GLU   A 25  ? 0.2923 0.2909 0.3586 -0.0181 0.0292  0.0024  25  GLU   A OE2 
690  N N   A GLU   A 26  ? 0.2360 0.2966 0.2485 -0.0618 0.1016  -0.0126 26  GLU   A N   
691  N N   B GLU   A 26  ? 0.2584 0.2705 0.2448 -0.0219 0.0285  -0.0067 26  GLU   A N   
692  C CA  A GLU   A 26  ? 0.2544 0.2870 0.2274 -0.0760 0.0911  0.0038  26  GLU   A CA  
693  C CA  B GLU   A 26  ? 0.2619 0.2716 0.2368 -0.0236 0.0284  -0.0098 26  GLU   A CA  
694  C C   A GLU   A 26  ? 0.2523 0.2659 0.2054 -0.0718 0.0795  -0.0021 26  GLU   A C   
695  C C   B GLU   A 26  ? 0.2684 0.2765 0.2298 -0.0177 0.0280  -0.0076 26  GLU   A C   
696  O O   A GLU   A 26  ? 0.2621 0.2625 0.2087 -0.0866 0.0704  -0.0065 26  GLU   A O   
697  O O   B GLU   A 26  ? 0.2686 0.2745 0.2291 -0.0165 0.0325  -0.0081 26  GLU   A O   
698  C CB  A GLU   A 26  ? 0.2801 0.2894 0.2614 -0.0877 0.0702  0.0095  26  GLU   A CB  
699  C CB  B GLU   A 26  ? 0.2593 0.2691 0.2386 -0.0315 0.0254  -0.0159 26  GLU   A CB  
700  C CG  A GLU   A 26  ? 0.2997 0.2956 0.3180 -0.0954 0.0744  -0.0023 26  GLU   A CG  
701  C CG  B GLU   A 26  ? 0.2564 0.2638 0.2416 -0.0398 0.0280  -0.0192 26  GLU   A CG  
702  C CD  A GLU   A 26  ? 0.3054 0.2947 0.3395 -0.1055 0.1002  -0.0096 26  GLU   A CD  
703  C CD  B GLU   A 26  ? 0.2529 0.2582 0.2418 -0.0485 0.0318  -0.0229 26  GLU   A CD  
704  O OE1 A GLU   A 26  ? 0.2889 0.3228 0.3406 -0.0823 0.1300  -0.0670 26  GLU   A OE1 
705  O OE1 B GLU   A 26  ? 0.2532 0.2611 0.2527 -0.0469 0.0384  -0.0275 26  GLU   A OE1 
706  O OE2 A GLU   A 26  ? 0.3295 0.3014 0.3522 -0.1022 0.0982  0.0101  26  GLU   A OE2 
707  O OE2 B GLU   A 26  ? 0.2497 0.2545 0.2249 -0.0550 0.0321  -0.0282 26  GLU   A OE2 
720  N N   A ALA   A 27  ? 0.2319 0.2406 0.2012 -0.0702 0.0660  -0.0032 27  ALA   A N   
721  N N   B ALA   A 27  ? 0.2746 0.2835 0.2276 -0.0155 0.0228  -0.0056 27  ALA   A N   
722  C CA  A ALA   A 27  ? 0.2360 0.2415 0.1899 -0.0584 0.0648  -0.0066 27  ALA   A CA  
723  C CA  B ALA   A 27  ? 0.2843 0.2939 0.2273 -0.0135 0.0209  -0.0053 27  ALA   A CA  
724  C C   A ALA   A 27  ? 0.2605 0.2574 0.1971 -0.0586 0.0732  -0.0231 27  ALA   A C   
725  C C   B ALA   A 27  ? 0.2983 0.3078 0.2374 -0.0150 0.0244  -0.0072 27  ALA   A C   
726  O O   A ALA   A 27  ? 0.2621 0.2491 0.2042 -0.0636 0.0539  -0.0260 27  ALA   A O   
727  O O   B ALA   A 27  ? 0.2984 0.3071 0.2332 -0.0131 0.0190  -0.0073 27  ALA   A O   
728  C CB  A ALA   A 27  ? 0.2146 0.2278 0.1990 -0.0622 0.0544  -0.0010 27  ALA   A CB  
729  C CB  B ALA   A 27  ? 0.2814 0.2917 0.2247 -0.0122 0.0181  -0.0045 27  ALA   A CB  
740  N N   A LYS   A 28  ? 0.2919 0.2794 0.2109 -0.0546 0.0744  -0.0499 28  LYS   A N   
741  N N   B LYS   A 28  ? 0.3135 0.3219 0.2542 -0.0194 0.0333  -0.0112 28  LYS   A N   
742  C CA  A LYS   A 28  ? 0.3303 0.3120 0.2563 -0.0461 0.0673  -0.0713 28  LYS   A CA  
743  C CA  B LYS   A 28  ? 0.3294 0.3368 0.2752 -0.0244 0.0441  -0.0173 28  LYS   A CA  
744  C C   A LYS   A 28  ? 0.3470 0.3420 0.2534 -0.0513 0.0762  -0.0566 28  LYS   A C   
745  C C   B LYS   A 28  ? 0.3423 0.3486 0.2615 -0.0380 0.0670  -0.0228 28  LYS   A C   
746  O O   A LYS   A 28  ? 0.3553 0.3537 0.3024 -0.0563 0.0659  -0.0518 28  LYS   A O   
747  O O   B LYS   A 28  ? 0.3439 0.3497 0.2694 -0.0370 0.0653  -0.0237 28  LYS   A O   
748  C CB  A LYS   A 28  ? 0.3503 0.3225 0.3072 -0.0329 0.0561  -0.0859 28  LYS   A CB  
749  C CB  B LYS   A 28  ? 0.3328 0.3406 0.3061 -0.0173 0.0337  -0.0167 28  LYS   A CB  
750  C CG  A LYS   A 28  ? 0.3681 0.3334 0.3570 -0.0209 0.0497  -0.0829 28  LYS   A CG  
751  C CG  B LYS   A 28  ? 0.3366 0.3441 0.3347 -0.0114 0.0254  -0.0150 28  LYS   A CG  
752  C CD  A LYS   A 28  ? 0.3857 0.3546 0.4222 -0.0081 0.0419  -0.0729 28  LYS   A CD  
753  C CD  B LYS   A 28  ? 0.3410 0.3494 0.3650 -0.0068 0.0177  -0.0135 28  LYS   A CD  
754  C CE  A LYS   A 28  ? 0.3969 0.3668 0.4636 -0.0024 0.0386  -0.0675 28  LYS   A CE  
755  C CE  B LYS   A 28  ? 0.3444 0.3527 0.3846 -0.0049 0.0122  -0.0132 28  LYS   A CE  
756  N NZ  A LYS   A 28  ? 0.4055 0.3738 0.4913 0.0040  0.0389  -0.0675 28  LYS   A NZ  
757  N NZ  B LYS   A 28  ? 0.3464 0.3544 0.3977 -0.0035 0.0094  -0.0136 28  LYS   A NZ  
784  N N   . LYS   A 29  ? 0.3523 0.3579 0.2451 -0.0542 0.0926  -0.0272 29  LYS   A N   
785  C CA  . LYS   A 29  ? 0.3808 0.3925 0.2645 -0.0636 0.1087  -0.0182 29  LYS   A CA  
786  C C   . LYS   A 29  ? 0.3854 0.3941 0.2403 -0.0750 0.1043  -0.0184 29  LYS   A C   
787  O O   . LYS   A 29  ? 0.3998 0.4089 0.2560 -0.0664 0.1008  -0.0269 29  LYS   A O   
788  C CB  . LYS   A 29  ? 0.4008 0.4245 0.3339 -0.0563 0.1218  -0.0109 29  LYS   A CB  
789  C CG  . LYS   A 29  ? 0.4205 0.4503 0.4143 -0.0509 0.1197  -0.0037 29  LYS   A CG  
790  C CD  . LYS   A 29  ? 0.4385 0.4735 0.4948 -0.0471 0.1147  -0.0028 29  LYS   A CD  
791  C CE  . LYS   A 29  ? 0.4526 0.4899 0.5474 -0.0437 0.1125  -0.0043 29  LYS   A CE  
792  N NZ  . LYS   A 29  ? 0.4583 0.4999 0.5818 -0.0404 0.1096  -0.0075 29  LYS   A NZ  
807  N N   . VAL   A 30  ? 0.3694 0.3758 0.2193 -0.0932 0.1064  -0.0139 30  VAL   A N   
808  C CA  . VAL   A 30  ? 0.3648 0.3583 0.2094 -0.1088 0.0818  0.0006  30  VAL   A CA  
809  C C   . VAL   A 30  ? 0.3675 0.3427 0.1716 -0.1098 0.0680  0.0011  30  VAL   A C   
810  O O   . VAL   A 30  ? 0.3775 0.3461 0.1809 -0.1121 0.0641  0.0025  30  VAL   A O   
811  C CB  . VAL   A 30  ? 0.3588 0.3524 0.2453 -0.1236 0.0541  0.0051  30  VAL   A CB  
812  C CG1 . VAL   A 30  ? 0.3591 0.3543 0.2612 -0.1220 0.0271  0.0022  30  VAL   A CG1 
813  C CG2 . VAL   A 30  ? 0.3572 0.3545 0.2774 -0.1297 0.0556  0.0026  30  VAL   A CG2 
823  N N   . LYS   A 31  ? 0.3530 0.3202 0.1435 -0.1167 0.0465  -0.0025 31  LYS   A N   
824  C CA  . LYS   A 31  ? 0.3714 0.3227 0.1568 -0.1040 0.0178  -0.0018 31  LYS   A CA  
825  C C   . LYS   A 31  ? 0.3444 0.3022 0.1102 -0.0814 0.0055  0.0352  31  LYS   A C   
826  O O   . LYS   A 31  ? 0.3530 0.3176 0.1379 -0.0753 -0.0185 0.0507  31  LYS   A O   
827  C CB  . LYS   A 31  ? 0.4195 0.3583 0.2803 -0.1027 -0.0003 -0.0206 31  LYS   A CB  
828  C CG  . LYS   A 31  ? 0.4632 0.4006 0.4315 -0.0923 -0.0198 -0.0301 31  LYS   A CG  
829  C CD  . LYS   A 31  ? 0.5021 0.4340 0.5475 -0.0839 -0.0354 -0.0378 31  LYS   A CD  
830  C CE  . LYS   A 31  ? 0.5303 0.4619 0.6173 -0.0762 -0.0504 -0.0492 31  LYS   A CE  
831  N NZ  . LYS   A 31  ? 0.5420 0.4747 0.6549 -0.0733 -0.0591 -0.0577 31  LYS   A NZ  
845  N N   . PRO   A 32  ? 0.3089 0.2718 0.0973 -0.0785 0.0121  0.0197  32  PRO   A N   
846  C CA  . PRO   A 32  ? 0.2976 0.2530 0.1537 -0.0744 0.0007  0.0251  32  PRO   A CA  
847  C C   . PRO   A 32  ? 0.2877 0.2486 0.1610 -0.0623 -0.0038 0.0384  32  PRO   A C   
848  O O   . PRO   A 32  ? 0.2810 0.2434 0.1731 -0.0631 -0.0213 0.0443  32  PRO   A O   
849  C CB  . PRO   A 32  ? 0.2980 0.2562 0.1629 -0.0739 -0.0048 0.0278  32  PRO   A CB  
850  C CG  . PRO   A 32  ? 0.2911 0.2605 0.1082 -0.0696 -0.0171 0.0261  32  PRO   A CG  
851  C CD  . PRO   A 32  ? 0.2937 0.2618 0.0974 -0.0745 -0.0037 0.0208  32  PRO   A CD  
859  N N   . THR   A 33  ? 0.2920 0.2430 0.1640 -0.0513 -0.0029 0.0413  33  THR   A N   
860  C CA  . THR   A 33  ? 0.2874 0.2477 0.1642 -0.0358 -0.0234 0.0373  33  THR   A CA  
861  C C   . THR   A 33  ? 0.2480 0.2264 0.1498 -0.0403 -0.0250 0.0287  33  THR   A C   
862  O O   . THR   A 33  ? 0.2386 0.2272 0.1706 -0.0355 -0.0367 0.0411  33  THR   A O   
863  C CB  . THR   A 33  ? 0.3136 0.2657 0.1801 -0.0272 -0.0350 0.0549  33  THR   A CB  
864  O OG1 . THR   A 33  ? 0.3379 0.2834 0.2088 -0.0101 -0.0247 0.0682  33  THR   A OG1 
865  C CG2 . THR   A 33  ? 0.3160 0.2726 0.1928 -0.0197 -0.0536 0.0513  33  THR   A CG2 
873  N N   . VAL   A 34  ? 0.2133 0.2096 0.1441 -0.0376 -0.0145 0.0327  34  VAL   A N   
874  C CA  . VAL   A 34  ? 0.1999 0.1899 0.1282 -0.0302 -0.0076 0.0349  34  VAL   A CA  
875  C C   . VAL   A 34  ? 0.1893 0.1823 0.1282 -0.0310 0.0066  0.0236  34  VAL   A C   
876  O O   . VAL   A 34  ? 0.1943 0.1796 0.1541 -0.0385 0.0033  0.0309  34  VAL   A O   
877  C CB  . VAL   A 34  ? 0.2058 0.1852 0.1523 -0.0268 -0.0044 0.0155  34  VAL   A CB  
878  C CG1 . VAL   A 34  ? 0.2076 0.1863 0.1572 -0.0299 -0.0005 0.0064  34  VAL   A CG1 
879  C CG2 . VAL   A 34  ? 0.2139 0.2015 0.1827 -0.0166 -0.0208 0.0132  34  VAL   A CG2 
889  N N   . VAL   A 35  ? 0.1792 0.1703 0.1300 -0.0288 -0.0009 0.0247  35  VAL   A N   
890  C CA  . VAL   A 35  ? 0.1658 0.1675 0.1304 -0.0264 0.0013  0.0160  35  VAL   A CA  
891  C C   . VAL   A 35  ? 0.1568 0.1551 0.1304 -0.0228 0.0045  0.0180  35  VAL   A C   
892  O O   . VAL   A 35  ? 0.1590 0.1690 0.1463 -0.0264 0.0102  0.0153  35  VAL   A O   
893  C CB  . VAL   A 35  ? 0.1772 0.1718 0.1414 -0.0161 0.0151  0.0057  35  VAL   A CB  
894  C CG1 . VAL   A 35  ? 0.1941 0.1729 0.1516 -0.0112 0.0105  0.0048  35  VAL   A CG1 
895  C CG2 . VAL   A 35  ? 0.1765 0.1771 0.1641 -0.0139 0.0224  0.0019  35  VAL   A CG2 
905  N N   . VAL   A 36  ? 0.1472 0.1477 0.1223 -0.0188 0.0136  0.0180  36  VAL   A N   
906  C CA  . VAL   A 36  ? 0.1314 0.1463 0.1352 -0.0148 0.0097  0.0123  36  VAL   A CA  
907  C C   . VAL   A 36  ? 0.1421 0.1386 0.1499 -0.0108 0.0066  0.0150  36  VAL   A C   
908  O O   . VAL   A 36  ? 0.1517 0.1365 0.1673 -0.0028 0.0240  0.0126  36  VAL   A O   
909  C CB  . VAL   A 36  ? 0.1349 0.1424 0.1389 -0.0084 0.0044  0.0082  36  VAL   A CB  
910  C CG1 . VAL   A 36  ? 0.1371 0.1421 0.1531 -0.0110 0.0004  -0.0002 36  VAL   A CG1 
911  C CG2 . VAL   A 36  ? 0.1582 0.1475 0.1505 -0.0113 0.0016  0.0209  36  VAL   A CG2 
921  N N   . ASN   A 37  ? 0.1336 0.1414 0.1270 -0.0063 -0.0009 0.0182  37  ASN   A N   
922  C CA  . ASN   A 37  ? 0.1365 0.1376 0.1247 -0.0060 0.0037  0.0142  37  ASN   A CA  
923  C C   . ASN   A 37  ? 0.1347 0.1294 0.1341 -0.0037 0.0120  0.0287  37  ASN   A C   
924  O O   . ASN   A 37  ? 0.1414 0.1453 0.1374 0.0067  0.0115  0.0105  37  ASN   A O   
925  C CB  . ASN   A 37  ? 0.1410 0.1327 0.1355 0.0031  0.0106  0.0173  37  ASN   A CB  
926  C CG  . ASN   A 37  ? 0.1444 0.1321 0.1491 0.0046  0.0084  0.0129  37  ASN   A CG  
927  O OD1 . ASN   A 37  ? 0.1463 0.1367 0.1654 0.0051  0.0106  0.0188  37  ASN   A OD1 
928  N ND2 . ASN   A 37  ? 0.1511 0.1319 0.1582 -0.0056 0.0050  0.0226  37  ASN   A ND2 
935  N N   A ALA   A 38  ? 0.1370 0.1473 0.1457 0.0062  0.0123  0.0147  38  ALA   A N   
936  N N   B ALA   A 38  ? 0.1350 0.1412 0.1407 -0.0082 0.0029  0.0202  38  ALA   A N   
937  C CA  A ALA   A 38  ? 0.1436 0.1507 0.1289 0.0033  0.0020  0.0066  38  ALA   A CA  
938  C CA  B ALA   A 38  ? 0.1356 0.1500 0.1495 -0.0142 -0.0074 0.0119  38  ALA   A CA  
939  C C   A ALA   A 38  ? 0.1374 0.1596 0.1354 0.0169  -0.0054 0.0020  38  ALA   A C   
940  C C   B ALA   A 38  ? 0.1337 0.1546 0.1518 -0.0115 -0.0124 0.0069  38  ALA   A C   
941  O O   A ALA   A 38  ? 0.1310 0.1546 0.1490 0.0121  -0.0043 0.0072  38  ALA   A O   
942  O O   B ALA   A 38  ? 0.1232 0.1542 0.1562 -0.0141 -0.0142 -0.0038 38  ALA   A O   
943  C CB  A ALA   A 38  ? 0.1484 0.1755 0.1581 -0.0113 -0.0018 0.0061  38  ALA   A CB  
944  C CB  B ALA   A 38  ? 0.1374 0.1553 0.1631 -0.0188 -0.0143 0.0063  38  ALA   A CB  
955  N N   A ALA   A 39  ? 0.1358 0.1404 0.1404 0.0117  -0.0043 0.0087  39  ALA   A N   
956  N N   B ALA   A 39  ? 0.1423 0.1535 0.1526 -0.0104 -0.0124 0.0137  39  ALA   A N   
957  C CA  A ALA   A 39  ? 0.1381 0.1377 0.1358 0.0099  0.0032  0.0147  39  ALA   A CA  
958  C CA  B ALA   A 39  ? 0.1514 0.1558 0.1540 -0.0113 -0.0179 0.0142  39  ALA   A CA  
959  C C   A ALA   A 39  ? 0.1277 0.1411 0.1406 -0.0001 -0.0030 0.0071  39  ALA   A C   
960  C C   B ALA   A 39  ? 0.1469 0.1518 0.1508 -0.0145 -0.0175 0.0112  39  ALA   A C   
961  O O   A ALA   A 39  ? 0.1459 0.1348 0.1486 -0.0050 0.0043  0.0086  39  ALA   A O   
962  O O   B ALA   A 39  ? 0.1507 0.1501 0.1483 -0.0219 -0.0137 0.0060  39  ALA   A O   
963  C CB  A ALA   A 39  ? 0.1426 0.1380 0.1440 0.0139  -0.0079 0.0027  39  ALA   A CB  
964  C CB  B ALA   A 39  ? 0.1630 0.1604 0.1557 -0.0068 -0.0237 0.0151  39  ALA   A CB  
975  N N   A ASN   A 40  ? 0.1445 0.1427 0.1314 -0.0119 0.0140  0.0056  40  ASN   A N   
976  N N   B ASN   A 40  ? 0.1452 0.1489 0.1505 -0.0095 -0.0133 0.0158  40  ASN   A N   
977  C CA  A ASN   A 40  ? 0.1513 0.1442 0.1322 -0.0011 0.0082  -0.0005 40  ASN   A CA  
978  C CA  B ASN   A 40  ? 0.1456 0.1450 0.1470 -0.0046 -0.0096 0.0180  40  ASN   A CA  
979  C C   A ASN   A 40  ? 0.1484 0.1340 0.1275 -0.0035 0.0205  0.0053  40  ASN   A C   
980  C C   B ASN   A 40  ? 0.1449 0.1437 0.1411 0.0011  -0.0085 0.0104  40  ASN   A C   
981  O O   A ASN   A 40  ? 0.1440 0.1297 0.1401 -0.0114 0.0206  0.0143  40  ASN   A O   
982  O O   B ASN   A 40  ? 0.1408 0.1423 0.1470 0.0035  -0.0157 0.0014  40  ASN   A O   
983  C CB  A ASN   A 40  ? 0.1613 0.1525 0.1523 0.0083  -0.0091 0.0083  40  ASN   A CB  
984  C CB  B ASN   A 40  ? 0.1455 0.1417 0.1480 -0.0100 0.0041  0.0201  40  ASN   A CB  
985  C CG  A ASN   A 40  ? 0.1785 0.1510 0.1967 0.0002  -0.0098 0.0112  40  ASN   A CG  
986  C CG  B ASN   A 40  ? 0.1465 0.1366 0.1476 -0.0181 0.0177  0.0186  40  ASN   A CG  
987  O OD1 A ASN   A 40  ? 0.1937 0.1501 0.2185 -0.0005 -0.0152 0.0078  40  ASN   A OD1 
988  O OD1 B ASN   A 40  ? 0.1493 0.1363 0.1431 -0.0220 0.0364  0.0164  40  ASN   A OD1 
989  N ND2 A ASN   A 40  ? 0.1834 0.1604 0.2118 0.0063  -0.0047 -0.0009 40  ASN   A ND2 
990  N ND2 B ASN   A 40  ? 0.1490 0.1341 0.1556 -0.0205 0.0171  0.0115  40  ASN   A ND2 
1003 N N   A VAL   A 41  ? 0.1623 0.1352 0.1346 -0.0011 0.0183  0.0066  41  VAL   A N   
1004 N N   B VAL   A 41  ? 0.1495 0.1462 0.1354 0.0020  -0.0011 0.0218  41  VAL   A N   
1005 C CA  A VAL   A 41  ? 0.1614 0.1447 0.1415 -0.0039 0.0256  0.0043  41  VAL   A CA  
1006 C CA  B VAL   A 41  ? 0.1539 0.1481 0.1270 -0.0017 0.0082  0.0272  41  VAL   A CA  
1007 C C   A VAL   A 41  ? 0.1587 0.1490 0.1555 0.0092  0.0229  0.0080  41  VAL   A C   
1008 C C   B VAL   A 41  ? 0.1580 0.1507 0.1294 -0.0005 0.0086  0.0297  41  VAL   A C   
1009 O O   A VAL   A 41  ? 0.1646 0.1363 0.1828 0.0075  0.0233  0.0035  41  VAL   A O   
1010 O O   B VAL   A 41  ? 0.1597 0.1470 0.1339 -0.0004 0.0099  0.0292  41  VAL   A O   
1011 C CB  A VAL   A 41  ? 0.1772 0.1507 0.1506 -0.0093 0.0375  0.0031  41  VAL   A CB  
1012 C CB  B VAL   A 41  ? 0.1542 0.1481 0.1273 -0.0079 0.0182  0.0271  41  VAL   A CB  
1013 C CG1 A VAL   A 41  ? 0.1885 0.1635 0.1656 -0.0086 0.0327  -0.0112 41  VAL   A CG1 
1014 C CG1 B VAL   A 41  ? 0.1591 0.1504 0.1324 -0.0104 0.0287  0.0245  41  VAL   A CG1 
1015 C CG2 A VAL   A 41  ? 0.1993 0.1703 0.1405 -0.0162 0.0385  -0.0009 41  VAL   A CG2 
1016 C CG2 B VAL   A 41  ? 0.1498 0.1484 0.1260 -0.0131 0.0125  0.0276  41  VAL   A CG2 
1035 N N   A TYR   A 42  ? 0.1433 0.1466 0.1581 0.0029  0.0324  0.0160  42  TYR   A N   
1036 N N   B TYR   A 42  ? 0.1597 0.1548 0.1344 -0.0003 0.0054  0.0379  42  TYR   A N   
1037 C CA  A TYR   A 42  ? 0.1512 0.1387 0.1647 -0.0078 0.0309  0.0179  42  TYR   A CA  
1038 C CA  B TYR   A 42  ? 0.1653 0.1593 0.1406 -0.0012 0.0028  0.0347  42  TYR   A CA  
1039 C C   A TYR   A 42  ? 0.1335 0.1265 0.1596 -0.0031 0.0160  0.0232  42  TYR   A C   
1040 C C   B TYR   A 42  ? 0.1644 0.1650 0.1306 -0.0002 0.0020  0.0328  42  TYR   A C   
1041 O O   A TYR   A 42  ? 0.1411 0.1329 0.1769 -0.0202 0.0125  0.0052  42  TYR   A O   
1042 O O   B TYR   A 42  ? 0.1640 0.1678 0.1230 -0.0047 0.0034  0.0278  42  TYR   A O   
1043 C CB  A TYR   A 42  ? 0.1878 0.1478 0.1560 -0.0067 0.0339  0.0346  42  TYR   A CB  
1044 C CB  B TYR   A 42  ? 0.1749 0.1594 0.1566 -0.0005 0.0018  0.0294  42  TYR   A CB  
1045 C CG  A TYR   A 42  ? 0.2138 0.1694 0.1553 -0.0082 0.0259  0.0370  42  TYR   A CG  
1046 C CG  B TYR   A 42  ? 0.1848 0.1625 0.1694 0.0009  0.0015  0.0243  42  TYR   A CG  
1047 C CD1 A TYR   A 42  ? 0.2245 0.1808 0.1607 -0.0165 0.0289  0.0320  42  TYR   A CD1 
1048 C CD1 B TYR   A 42  ? 0.1890 0.1631 0.1716 -0.0005 0.0003  0.0212  42  TYR   A CD1 
1049 C CD2 A TYR   A 42  ? 0.2264 0.1932 0.1740 -0.0059 0.0230  0.0189  42  TYR   A CD2 
1050 C CD2 B TYR   A 42  ? 0.1897 0.1665 0.1772 0.0019  0.0037  0.0185  42  TYR   A CD2 
1051 C CE1 A TYR   A 42  ? 0.2335 0.1940 0.1709 -0.0279 0.0399  0.0269  42  TYR   A CE1 
1052 C CE1 B TYR   A 42  ? 0.1930 0.1659 0.1799 -0.0030 0.0022  0.0157  42  TYR   A CE1 
1053 C CE2 A TYR   A 42  ? 0.2410 0.2061 0.1847 -0.0246 0.0250  0.0245  42  TYR   A CE2 
1054 C CE2 B TYR   A 42  ? 0.1954 0.1686 0.1883 -0.0027 0.0036  0.0185  42  TYR   A CE2 
1055 C CZ  A TYR   A 42  ? 0.2511 0.2110 0.1703 -0.0314 0.0389  0.0248  42  TYR   A CZ  
1056 C CZ  B TYR   A 42  ? 0.1973 0.1699 0.1879 -0.0057 0.0044  0.0143  42  TYR   A CZ  
1057 O OH  A TYR   A 42  ? 0.2655 0.2304 0.2055 -0.0420 0.0365  0.0089  42  TYR   A OH  
1058 O OH  B TYR   A 42  ? 0.1997 0.1752 0.1995 -0.0111 0.0034  0.0118  42  TYR   A OH  
1077 N N   A LEU   A 43  ? 0.1411 0.1259 0.1640 -0.0095 0.0172  0.0056  43  LEU   A N   
1078 N N   B LEU   A 43  ? 0.1656 0.1694 0.1337 0.0035  -0.0027 0.0267  43  LEU   A N   
1079 C CA  A LEU   A 43  ? 0.1329 0.1230 0.1527 -0.0071 0.0175  0.0099  43  LEU   A CA  
1080 C CA  B LEU   A 43  ? 0.1676 0.1734 0.1350 0.0096  -0.0058 0.0227  43  LEU   A CA  
1081 C C   A LEU   A 43  ? 0.1348 0.1286 0.1519 -0.0011 0.0090  0.0040  43  LEU   A C   
1082 C C   B LEU   A 43  ? 0.1727 0.1824 0.1467 0.0076  -0.0104 0.0164  43  LEU   A C   
1083 O O   A LEU   A 43  ? 0.1539 0.1466 0.1611 -0.0003 -0.0045 -0.0010 43  LEU   A O   
1084 O O   B LEU   A 43  ? 0.1716 0.1847 0.1399 0.0102  -0.0167 0.0157  43  LEU   A O   
1085 C CB  A LEU   A 43  ? 0.1457 0.1302 0.1666 -0.0127 0.0255  0.0108  43  LEU   A CB  
1086 C CB  B LEU   A 43  ? 0.1699 0.1681 0.1370 0.0153  -0.0050 0.0273  43  LEU   A CB  
1087 C CG  A LEU   A 43  ? 0.1522 0.1282 0.1687 -0.0032 0.0056  0.0100  43  LEU   A CG  
1088 C CG  B LEU   A 43  ? 0.1715 0.1630 0.1395 0.0199  -0.0072 0.0249  43  LEU   A CG  
1089 C CD1 A LEU   A 43  ? 0.1583 0.1362 0.1791 -0.0028 0.0003  0.0113  43  LEU   A CD1 
1090 C CD1 B LEU   A 43  ? 0.1728 0.1623 0.1359 0.0203  -0.0079 0.0277  43  LEU   A CD1 
1091 C CD2 A LEU   A 43  ? 0.1772 0.1328 0.1639 -0.0073 0.0075  0.0223  43  LEU   A CD2 
1092 C CD2 B LEU   A 43  ? 0.1766 0.1607 0.1414 0.0210  -0.0057 0.0295  43  LEU   A CD2 
1115 N N   A LYS   A 44  ? 0.1368 0.1329 0.1582 -0.0012 0.0070  0.0051  44  LYS   A N   
1116 N N   B LYS   A 44  ? 0.1801 0.1900 0.1642 0.0048  -0.0103 0.0113  44  LYS   A N   
1117 C CA  A LYS   A 44  ? 0.1536 0.1358 0.1554 -0.0065 0.0184  0.0169  44  LYS   A CA  
1118 C CA  B LYS   A 44  ? 0.1904 0.1963 0.1805 -0.0003 -0.0115 0.0080  44  LYS   A CA  
1119 C C   A LYS   A 44  ? 0.1442 0.1321 0.1404 -0.0036 0.0141  0.0046  44  LYS   A C   
1120 C C   B LYS   A 44  ? 0.1800 0.1883 0.1637 -0.0020 -0.0153 0.0076  44  LYS   A C   
1121 O O   A LYS   A 44  ? 0.1564 0.1407 0.1696 0.0022  0.0060  -0.0055 44  LYS   A O   
1122 O O   B LYS   A 44  ? 0.1834 0.1894 0.1597 -0.0040 -0.0178 0.0065  44  LYS   A O   
1123 C CB  A LYS   A 44  ? 0.1810 0.1541 0.2050 -0.0022 0.0281  0.0226  44  LYS   A CB  
1124 C CB  B LYS   A 44  ? 0.2094 0.2129 0.2251 -0.0007 -0.0078 0.0055  44  LYS   A CB  
1125 C CG  A LYS   A 44  ? 0.2129 0.1850 0.2900 -0.0156 0.0501  0.0276  44  LYS   A CG  
1126 C CG  B LYS   A 44  ? 0.2269 0.2291 0.2719 -0.0020 -0.0041 0.0042  44  LYS   A CG  
1127 C CD  A LYS   A 44  ? 0.2540 0.2502 0.4029 -0.0193 0.0385  0.0293  44  LYS   A CD  
1128 C CD  B LYS   A 44  ? 0.2433 0.2482 0.3171 -0.0052 -0.0052 0.0041  44  LYS   A CD  
1129 C CE  A LYS   A 44  ? 0.2723 0.2892 0.4756 -0.0198 0.0306  0.0322  44  LYS   A CE  
1130 C CE  B LYS   A 44  ? 0.2544 0.2614 0.3489 -0.0081 -0.0063 0.0056  44  LYS   A CE  
1131 N NZ  A LYS   A 44  ? 0.2810 0.3170 0.5086 -0.0191 0.0280  0.0364  44  LYS   A NZ  
1132 N NZ  B LYS   A 44  ? 0.2613 0.2696 0.3652 -0.0117 -0.0070 0.0063  44  LYS   A NZ  
1159 N N   A HIS   A 45  ? 0.1349 0.1302 0.1561 0.0049  0.0089  0.0214  45  HIS   A N   
1160 N N   B HIS   A 45  ? 0.1675 0.1799 0.1578 -0.0017 -0.0189 0.0086  45  HIS   A N   
1161 C CA  A HIS   A 45  ? 0.1312 0.1400 0.1569 0.0049  0.0093  0.0148  45  HIS   A CA  
1162 C CA  B HIS   A 45  ? 0.1549 0.1727 0.1515 -0.0007 -0.0179 0.0076  45  HIS   A CA  
1163 C C   A HIS   A 45  ? 0.1368 0.1553 0.1616 0.0070  0.0107  0.0217  45  HIS   A C   
1164 C C   B HIS   A 45  ? 0.1523 0.1709 0.1487 0.0014  -0.0141 0.0122  45  HIS   A C   
1165 O O   A HIS   A 45  ? 0.1504 0.1518 0.1892 0.0171  0.0115  0.0108  45  HIS   A O   
1166 O O   B HIS   A 45  ? 0.1541 0.1710 0.1542 0.0062  -0.0119 0.0189  45  HIS   A O   
1167 C CB  A HIS   A 45  ? 0.1319 0.1343 0.1465 0.0019  -0.0012 0.0041  45  HIS   A CB  
1168 C CB  B HIS   A 45  ? 0.1449 0.1663 0.1419 0.0012  -0.0229 0.0035  45  HIS   A CB  
1169 C CG  A HIS   A 45  ? 0.1375 0.1326 0.1431 -0.0064 0.0017  0.0069  45  HIS   A CG  
1170 C CG  B HIS   A 45  ? 0.1337 0.1593 0.1246 -0.0001 -0.0201 0.0027  45  HIS   A CG  
1171 N ND1 A HIS   A 45  ? 0.1422 0.1376 0.1558 0.0012  0.0099  0.0070  45  HIS   A ND1 
1172 N ND1 B HIS   A 45  ? 0.1312 0.1586 0.1231 0.0015  -0.0259 0.0043  45  HIS   A ND1 
1173 C CD2 A HIS   A 45  ? 0.1374 0.1405 0.1448 -0.0025 0.0006  0.0223  45  HIS   A CD2 
1174 C CD2 B HIS   A 45  ? 0.1279 0.1537 0.1144 -0.0012 -0.0187 -0.0014 45  HIS   A CD2 
1175 C CE1 A HIS   A 45  ? 0.1424 0.1288 0.1522 -0.0061 0.0089  0.0191  45  HIS   A CE1 
1176 C CE1 B HIS   A 45  ? 0.1265 0.1511 0.1075 0.0010  -0.0254 -0.0043 45  HIS   A CE1 
1177 N NE2 A HIS   A 45  ? 0.1331 0.1402 0.1505 0.0025  0.0069  0.0195  45  HIS   A NE2 
1178 N NE2 B HIS   A 45  ? 0.1234 0.1524 0.1067 -0.0016 -0.0237 -0.0061 45  HIS   A NE2 
1193 N N   A GLY   A 46  ? 0.1513 0.1709 0.1783 0.0180  -0.0110 0.0296  46  GLY   A N   
1194 N N   B GLY   A 46  ? 0.1500 0.1681 0.1432 -0.0006 -0.0090 0.0074  46  GLY   A N   
1195 C CA  A GLY   A 46  ? 0.1591 0.1862 0.1898 0.0177  -0.0180 0.0376  46  GLY   A CA  
1196 C CA  B GLY   A 46  ? 0.1434 0.1700 0.1434 -0.0015 -0.0001 0.0016  46  GLY   A CA  
1197 C C   A GLY   A 46  ? 0.1523 0.1778 0.1967 0.0264  -0.0166 0.0453  46  GLY   A C   
1198 C C   B GLY   A 46  ? 0.1374 0.1690 0.1451 0.0002  0.0110  -0.0016 46  GLY   A C   
1199 O O   A GLY   A 46  ? 0.1652 0.1840 0.2338 0.0273  -0.0269 0.0392  46  GLY   A O   
1200 O O   B GLY   A 46  ? 0.1431 0.1694 0.1498 -0.0026 0.0125  -0.0083 46  GLY   A O   
1207 N N   A GLY   A 47  ? 0.1614 0.1742 0.1866 0.0215  -0.0127 0.0380  47  GLY   A N   
1208 N N   B GLY   A 47  ? 0.1369 0.1668 0.1405 0.0013  0.0094  -0.0034 47  GLY   A N   
1209 C CA  A GLY   A 47  ? 0.1655 0.1852 0.1903 0.0234  -0.0263 0.0263  47  GLY   A CA  
1210 C CA  B GLY   A 47  ? 0.1317 0.1626 0.1322 -0.0025 0.0026  0.0027  47  GLY   A CA  
1211 C C   A GLY   A 47  ? 0.1592 0.1691 0.1689 0.0263  -0.0252 0.0101  47  GLY   A C   
1212 C C   B GLY   A 47  ? 0.1285 0.1501 0.1170 0.0025  0.0035  0.0006  47  GLY   A C   
1213 O O   A GLY   A 47  ? 0.1643 0.1599 0.1825 0.0270  -0.0219 0.0179  47  GLY   A O   
1214 O O   B GLY   A 47  ? 0.1206 0.1466 0.1179 0.0079  -0.0024 0.0058  47  GLY   A O   
1221 N N   A GLY   A 48  ? 0.1587 0.1745 0.1638 0.0236  -0.0288 0.0060  48  GLY   A N   
1222 N N   B GLY   A 48  ? 0.1298 0.1462 0.1162 -0.0038 0.0073  -0.0008 48  GLY   A N   
1223 C CA  A GLY   A 48  ? 0.1519 0.1706 0.1680 0.0120  -0.0240 -0.0127 48  GLY   A CA  
1224 C CA  B GLY   A 48  ? 0.1301 0.1374 0.1046 -0.0044 0.0078  -0.0079 48  GLY   A CA  
1225 C C   A GLY   A 48  ? 0.1435 0.1617 0.1483 0.0076  -0.0067 -0.0052 48  GLY   A C   
1226 C C   B GLY   A 48  ? 0.1326 0.1355 0.1064 -0.0024 0.0031  -0.0027 48  GLY   A C   
1227 O O   A GLY   A 48  ? 0.1615 0.1584 0.1603 0.0059  -0.0012 -0.0021 48  GLY   A O   
1228 O O   B GLY   A 48  ? 0.1420 0.1339 0.0882 0.0003  0.0141  0.0020  48  GLY   A O   
1235 N N   A VAL   A 49  ? 0.1376 0.1574 0.1720 -0.0038 -0.0102 0.0014  49  VAL   A N   
1236 N N   B VAL   A 49  ? 0.1242 0.1323 0.1121 -0.0003 -0.0069 -0.0049 49  VAL   A N   
1237 C CA  A VAL   A 49  ? 0.1548 0.1403 0.1669 -0.0135 -0.0000 0.0016  49  VAL   A CA  
1238 C CA  B VAL   A 49  ? 0.1235 0.1310 0.1232 0.0052  -0.0139 -0.0064 49  VAL   A CA  
1239 C C   A VAL   A 49  ? 0.1539 0.1292 0.1460 -0.0055 0.0056  -0.0009 49  VAL   A C   
1240 C C   B VAL   A 49  ? 0.1220 0.1244 0.1206 0.0081  -0.0081 -0.0276 49  VAL   A C   
1241 O O   A VAL   A 49  ? 0.1425 0.1370 0.1629 -0.0114 0.0032  -0.0030 49  VAL   A O   
1242 O O   B VAL   A 49  ? 0.1150 0.1218 0.1234 0.0183  -0.0062 -0.0273 49  VAL   A O   
1243 C CB  A VAL   A 49  ? 0.1715 0.1407 0.1933 -0.0157 -0.0092 0.0026  49  VAL   A CB  
1244 C CB  B VAL   A 49  ? 0.1236 0.1333 0.1349 0.0144  -0.0277 0.0093  49  VAL   A CB  
1245 C CG1 A VAL   A 49  ? 0.1799 0.1434 0.2109 -0.0134 -0.0060 0.0052  49  VAL   A CG1 
1246 C CG1 B VAL   A 49  ? 0.1116 0.1316 0.1344 0.0234  -0.0325 0.0223  49  VAL   A CG1 
1247 C CG2 A VAL   A 49  ? 0.1870 0.1592 0.2338 -0.0377 -0.0121 0.0045  49  VAL   A CG2 
1248 C CG2 B VAL   A 49  ? 0.1334 0.1335 0.1420 0.0112  -0.0395 0.0124  49  VAL   A CG2 
1267 N N   A ALA   A 50  ? 0.1497 0.1322 0.1429 -0.0073 -0.0134 0.0103  50  ALA   A N   
1268 N N   B ALA   A 50  ? 0.1263 0.1219 0.1203 0.0011  -0.0071 -0.0337 50  ALA   A N   
1269 C CA  A ALA   A 50  ? 0.1450 0.1372 0.1521 -0.0098 -0.0075 0.0112  50  ALA   A CA  
1270 C CA  B ALA   A 50  ? 0.1254 0.1199 0.1159 0.0002  -0.0017 -0.0422 50  ALA   A CA  
1271 C C   A ALA   A 50  ? 0.1271 0.1300 0.1548 -0.0090 -0.0031 -0.0017 50  ALA   A C   
1272 C C   B ALA   A 50  ? 0.1255 0.1181 0.1112 -0.0019 -0.0028 -0.0411 50  ALA   A C   
1273 O O   A ALA   A 50  ? 0.1305 0.1436 0.1689 -0.0029 -0.0046 0.0050  50  ALA   A O   
1274 O O   B ALA   A 50  ? 0.1246 0.1245 0.1016 -0.0018 -0.0001 -0.0344 50  ALA   A O   
1275 C CB  A ALA   A 50  ? 0.1430 0.1433 0.1476 0.0072  0.0036  0.0137  50  ALA   A CB  
1276 C CB  B ALA   A 50  ? 0.1208 0.1175 0.1149 0.0014  0.0092  -0.0560 50  ALA   A CB  
1287 N N   A GLY   A 51  ? 0.1324 0.1344 0.1689 0.0116  -0.0135 0.0054  51  GLY   A N   
1288 N N   B GLY   A 51  ? 0.1319 0.1225 0.1292 -0.0009 -0.0092 -0.0402 51  GLY   A N   
1289 C CA  A GLY   A 51  ? 0.1439 0.1332 0.1720 0.0148  -0.0114 0.0027  51  GLY   A CA  
1290 C CA  B GLY   A 51  ? 0.1380 0.1265 0.1302 -0.0022 -0.0097 -0.0402 51  GLY   A CA  
1291 C C   A GLY   A 51  ? 0.1333 0.1395 0.1633 0.0090  -0.0094 -0.0106 51  GLY   A C   
1292 C C   B GLY   A 51  ? 0.1387 0.1361 0.1389 -0.0046 -0.0119 -0.0333 51  GLY   A C   
1293 O O   A GLY   A 51  ? 0.1384 0.1526 0.1851 0.0069  -0.0088 -0.0154 51  GLY   A O   
1294 O O   B GLY   A 51  ? 0.1419 0.1394 0.1469 -0.0041 -0.0094 -0.0359 51  GLY   A O   
1301 N N   A ALA   A 52  ? 0.1330 0.1516 0.1608 0.0025  -0.0035 -0.0168 52  ALA   A N   
1302 N N   B ALA   A 52  ? 0.1411 0.1422 0.1419 -0.0070 -0.0106 -0.0305 52  ALA   A N   
1303 C CA  A ALA   A 52  ? 0.1377 0.1593 0.1765 0.0026  -0.0024 -0.0139 52  ALA   A CA  
1304 C CA  B ALA   A 52  ? 0.1435 0.1479 0.1466 -0.0080 -0.0075 -0.0253 52  ALA   A CA  
1305 C C   A ALA   A 52  ? 0.1343 0.1621 0.1536 -0.0063 0.0058  -0.0031 52  ALA   A C   
1306 C C   B ALA   A 52  ? 0.1414 0.1474 0.1366 -0.0145 -0.0007 -0.0294 52  ALA   A C   
1307 O O   A ALA   A 52  ? 0.1522 0.1669 0.1757 -0.0053 0.0079  -0.0062 52  ALA   A O   
1308 O O   B ALA   A 52  ? 0.1454 0.1454 0.1389 -0.0194 0.0060  -0.0346 52  ALA   A O   
1309 C CB  A ALA   A 52  ? 0.1547 0.1836 0.1984 -0.0044 -0.0078 -0.0046 52  ALA   A CB  
1310 C CB  B ALA   A 52  ? 0.1491 0.1571 0.1572 -0.0072 -0.0097 -0.0176 52  ALA   A CB  
1321 N N   A LEU   A 53  ? 0.1359 0.1520 0.1625 -0.0025 0.0032  -0.0023 53  LEU   A N   
1322 N N   B LEU   A 53  ? 0.1403 0.1471 0.1383 -0.0152 -0.0034 -0.0281 53  LEU   A N   
1323 C CA  A LEU   A 53  ? 0.1513 0.1554 0.1463 -0.0032 0.0090  0.0091  53  LEU   A CA  
1324 C CA  B LEU   A 53  ? 0.1439 0.1520 0.1394 -0.0147 -0.0031 -0.0208 53  LEU   A CA  
1325 C C   A LEU   A 53  ? 0.1463 0.1515 0.1130 0.0062  0.0133  0.0024  53  LEU   A C   
1326 C C   B LEU   A 53  ? 0.1448 0.1530 0.1357 -0.0120 -0.0004 -0.0159 53  LEU   A C   
1327 O O   A LEU   A 53  ? 0.1649 0.1614 0.1371 -0.0081 0.0100  -0.0019 53  LEU   A O   
1328 O O   B LEU   A 53  ? 0.1481 0.1542 0.1392 -0.0159 -0.0001 -0.0157 53  LEU   A O   
1329 C CB  A LEU   A 53  ? 0.1535 0.1633 0.1495 -0.0063 0.0097  0.0114  53  LEU   A CB  
1330 C CB  B LEU   A 53  ? 0.1444 0.1554 0.1433 -0.0184 -0.0045 -0.0223 53  LEU   A CB  
1331 C CG  A LEU   A 53  ? 0.1842 0.1559 0.1501 -0.0197 0.0191  0.0051  53  LEU   A CG  
1332 C CG  B LEU   A 53  ? 0.1501 0.1564 0.1444 -0.0244 -0.0060 -0.0273 53  LEU   A CG  
1333 C CD1 A LEU   A 53  ? 0.1852 0.1684 0.1598 0.0001  0.0030  0.0017  53  LEU   A CD1 
1334 C CD1 B LEU   A 53  ? 0.1515 0.1597 0.1426 -0.0196 -0.0093 -0.0345 53  LEU   A CD1 
1335 C CD2 A LEU   A 53  ? 0.2203 0.1759 0.1776 -0.0369 0.0283  -0.0033 53  LEU   A CD2 
1336 C CD2 B LEU   A 53  ? 0.1576 0.1597 0.1556 -0.0346 -0.0030 -0.0238 53  LEU   A CD2 
1359 N N   A ASN   A 54  ? 0.1430 0.1431 0.1246 -0.0024 -0.0015 0.0094  54  ASN   A N   
1360 N N   B ASN   A 54  ? 0.1436 0.1545 0.1414 -0.0085 -0.0016 -0.0098 54  ASN   A N   
1361 C CA  A ASN   A 54  ? 0.1303 0.1373 0.1377 -0.0035 -0.0013 0.0025  54  ASN   A CA  
1362 C CA  B ASN   A 54  ? 0.1413 0.1554 0.1456 -0.0038 -0.0027 -0.0070 54  ASN   A CA  
1363 C C   A ASN   A 54  ? 0.1416 0.1439 0.1426 -0.0026 0.0054  -0.0104 54  ASN   A C   
1364 C C   B ASN   A 54  ? 0.1416 0.1526 0.1490 0.0008  -0.0009 -0.0076 54  ASN   A C   
1365 O O   A ASN   A 54  ? 0.1481 0.1462 0.1572 -0.0068 -0.0015 -0.0139 54  ASN   A O   
1366 O O   B ASN   A 54  ? 0.1442 0.1511 0.1451 0.0022  -0.0072 0.0006  54  ASN   A O   
1367 C CB  A ASN   A 54  ? 0.1276 0.1444 0.1451 0.0003  -0.0131 -0.0028 54  ASN   A CB  
1368 C CB  B ASN   A 54  ? 0.1419 0.1601 0.1490 -0.0008 -0.0058 -0.0029 54  ASN   A CB  
1369 C CG  A ASN   A 54  ? 0.1356 0.1542 0.1515 0.0013  -0.0102 0.0048  54  ASN   A CG  
1370 C CG  B ASN   A 54  ? 0.1449 0.1639 0.1524 0.0004  -0.0120 0.0017  54  ASN   A CG  
1371 O OD1 A ASN   A 54  ? 0.1376 0.1492 0.1511 -0.0029 -0.0029 0.0051  54  ASN   A OD1 
1372 O OD1 B ASN   A 54  ? 0.1463 0.1670 0.1596 -0.0016 -0.0144 0.0078  54  ASN   A OD1 
1373 N ND2 A ASN   A 54  ? 0.1357 0.1609 0.1729 -0.0092 -0.0075 0.0195  54  ASN   A ND2 
1374 N ND2 B ASN   A 54  ? 0.1446 0.1627 0.1534 -0.0003 -0.0164 0.0012  54  ASN   A ND2 
1387 N N   . LYS   A 55  ? 0.1392 0.1496 0.1637 0.0032  0.0054  -0.0189 55  LYS   A N   
1388 C CA  . LYS   A 55  ? 0.1501 0.1591 0.1627 0.0079  -0.0091 -0.0180 55  LYS   A CA  
1389 C C   . LYS   A 55  ? 0.1499 0.1709 0.1590 -0.0086 -0.0075 -0.0210 55  LYS   A C   
1390 O O   . LYS   A 55  ? 0.1664 0.1814 0.1700 0.0011  -0.0069 -0.0269 55  LYS   A O   
1391 C CB  . LYS   A 55  ? 0.1572 0.1641 0.1851 0.0191  0.0006  -0.0233 55  LYS   A CB  
1392 C CG  . LYS   A 55  ? 0.1698 0.1950 0.2056 0.0224  -0.0108 -0.0295 55  LYS   A CG  
1393 C CD  . LYS   A 55  ? 0.1758 0.2211 0.2100 0.0382  -0.0024 -0.0282 55  LYS   A CD  
1394 C CE  . LYS   A 55  ? 0.2022 0.2526 0.2314 0.0491  -0.0193 -0.0248 55  LYS   A CE  
1395 N NZ  . LYS   A 55  ? 0.2088 0.2628 0.2410 0.0565  -0.0241 -0.0232 55  LYS   A NZ  
1410 N N   . ALA   A 56  ? 0.1567 0.1757 0.1629 -0.0091 0.0087  -0.0184 56  ALA   A N   
1411 C CA  . ALA   A 56  ? 0.1730 0.1967 0.1695 -0.0062 0.0073  -0.0224 56  ALA   A CA  
1412 C C   . ALA   A 56  ? 0.1809 0.2018 0.1340 -0.0102 0.0115  -0.0351 56  ALA   A C   
1413 O O   . ALA   A 56  ? 0.1836 0.2286 0.1549 0.0005  0.0215  -0.0247 56  ALA   A O   
1414 C CB  . ALA   A 56  ? 0.1765 0.2043 0.1848 -0.0127 0.0135  -0.0121 56  ALA   A CB  
1420 N N   . THR   A 57  ? 0.1683 0.1853 0.1364 -0.0053 0.0164  -0.0233 57  THR   A N   
1421 C CA  . THR   A 57  ? 0.1648 0.1785 0.1465 -0.0131 -0.0037 -0.0189 57  THR   A CA  
1422 C C   . THR   A 57  ? 0.1594 0.1827 0.1596 -0.0093 -0.0054 -0.0167 57  THR   A C   
1423 O O   . THR   A 57  ? 0.1599 0.1825 0.1813 -0.0119 -0.0084 -0.0314 57  THR   A O   
1424 C CB  . THR   A 57  ? 0.1636 0.1742 0.1476 -0.0094 0.0039  -0.0132 57  THR   A CB  
1425 O OG1 . THR   A 57  ? 0.1436 0.1773 0.1623 -0.0044 0.0106  -0.0113 57  THR   A OG1 
1426 C CG2 . THR   A 57  ? 0.1658 0.1788 0.1436 -0.0074 -0.0013 -0.0019 57  THR   A CG2 
1434 N N   . ASN   A 58  ? 0.1488 0.1780 0.1780 -0.0122 0.0059  -0.0367 58  ASN   A N   
1435 C CA  . ASN   A 58  ? 0.1768 0.1715 0.1941 -0.0121 0.0123  -0.0438 58  ASN   A CA  
1436 C C   . ASN   A 58  ? 0.1615 0.1569 0.1780 -0.0025 0.0004  -0.0251 58  ASN   A C   
1437 O O   . ASN   A 58  ? 0.1640 0.1649 0.1974 -0.0146 -0.0000 -0.0285 58  ASN   A O   
1438 C CB  . ASN   A 58  ? 0.2238 0.1896 0.2159 -0.0226 0.0360  -0.0578 58  ASN   A CB  
1439 C CG  . ASN   A 58  ? 0.2668 0.2161 0.2904 -0.0181 0.0354  -0.0423 58  ASN   A CG  
1440 O OD1 . ASN   A 58  ? 0.2952 0.2080 0.3444 0.0186  0.0667  -0.0361 58  ASN   A OD1 
1441 N ND2 . ASN   A 58  ? 0.2750 0.2336 0.3130 -0.0214 0.0170  -0.0459 58  ASN   A ND2 
1448 N N   . ASN   A 59  ? 0.1563 0.1534 0.1579 -0.0012 -0.0046 -0.0247 59  ASN   A N   
1449 C CA  . ASN   A 59  ? 0.1562 0.1462 0.1560 -0.0029 -0.0051 -0.0213 59  ASN   A CA  
1450 C C   . ASN   A 59  ? 0.1575 0.1435 0.1486 -0.0089 -0.0030 -0.0071 59  ASN   A C   
1451 O O   . ASN   A 59  ? 0.1543 0.1555 0.1585 -0.0094 -0.0037 0.0005  59  ASN   A O   
1452 C CB  . ASN   A 59  ? 0.1570 0.1393 0.1709 -0.0025 -0.0128 -0.0235 59  ASN   A CB  
1453 C CG  . ASN   A 59  ? 0.1590 0.1359 0.1840 -0.0041 -0.0246 -0.0019 59  ASN   A CG  
1454 O OD1 . ASN   A 59  ? 0.1676 0.1500 0.1746 -0.0106 -0.0263 -0.0005 59  ASN   A OD1 
1455 N ND2 . ASN   A 59  ? 0.1649 0.1484 0.1940 -0.0144 -0.0250 0.0053  59  ASN   A ND2 
1462 N N   . ALA   A 60  ? 0.1423 0.1477 0.1551 0.0002  0.0006  -0.0055 60  ALA   A N   
1463 C CA  . ALA   A 60  ? 0.1504 0.1512 0.1591 0.0029  -0.0000 -0.0010 60  ALA   A CA  
1464 C C   . ALA   A 60  ? 0.1556 0.1451 0.1612 0.0036  0.0019  -0.0144 60  ALA   A C   
1465 O O   . ALA   A 60  ? 0.1458 0.1480 0.1856 -0.0015 -0.0059 -0.0154 60  ALA   A O   
1466 C CB  . ALA   A 60  ? 0.1656 0.1585 0.1560 0.0011  -0.0065 -0.0211 60  ALA   A CB  
1472 N N   . MET   A 61  ? 0.1495 0.1353 0.1601 -0.0113 -0.0007 -0.0083 61  MET   A N   
1473 C CA  . MET   A 61  ? 0.1392 0.1340 0.1633 -0.0099 0.0083  -0.0007 61  MET   A CA  
1474 C C   . MET   A 61  ? 0.1280 0.1300 0.1774 -0.0068 -0.0079 -0.0073 61  MET   A C   
1475 O O   . MET   A 61  ? 0.1412 0.1327 0.1770 -0.0024 0.0099  0.0008  61  MET   A O   
1476 C CB  . MET   A 61  ? 0.1425 0.1404 0.1491 -0.0085 0.0010  -0.0035 61  MET   A CB  
1477 C CG  . MET   A 61  ? 0.1404 0.1547 0.1553 0.0019  -0.0032 0.0003  61  MET   A CG  
1478 S SD  . MET   A 61  ? 0.1515 0.1545 0.1888 -0.0091 0.0037  -0.0188 61  MET   A SD  
1479 C CE  . MET   A 61  ? 0.1756 0.1600 0.2288 -0.0210 0.0156  -0.0197 61  MET   A CE  
1489 N N   . GLN   A 62  ? 0.1338 0.1324 0.1756 -0.0017 0.0014  -0.0054 62  GLN   A N   
1490 C CA  . GLN   A 62  ? 0.1362 0.1396 0.1727 -0.0048 0.0031  0.0013  62  GLN   A CA  
1491 C C   . GLN   A 62  ? 0.1370 0.1258 0.1827 -0.0010 0.0015  0.0003  62  GLN   A C   
1492 O O   . GLN   A 62  ? 0.1364 0.1445 0.1829 0.0011  0.0044  0.0004  62  GLN   A O   
1493 C CB  . GLN   A 62  ? 0.1338 0.1329 0.1781 -0.0041 0.0014  0.0016  62  GLN   A CB  
1494 C CG  . GLN   A 62  ? 0.1349 0.1293 0.1777 -0.0080 -0.0048 0.0142  62  GLN   A CG  
1495 C CD  . GLN   A 62  ? 0.1555 0.1345 0.1714 -0.0070 0.0064  0.0016  62  GLN   A CD  
1496 O OE1 . GLN   A 62  ? 0.1540 0.1482 0.1811 -0.0098 0.0031  0.0012  62  GLN   A OE1 
1497 N NE2 . GLN   A 62  ? 0.1616 0.1367 0.1873 0.0005  0.0037  -0.0118 62  GLN   A NE2 
1506 N N   . VAL   A 63  ? 0.1389 0.1291 0.1921 -0.0111 0.0040  -0.0201 63  VAL   A N   
1507 C CA  . VAL   A 63  ? 0.1370 0.1551 0.2005 -0.0170 -0.0002 -0.0252 63  VAL   A CA  
1508 C C   . VAL   A 63  ? 0.1296 0.1552 0.1821 -0.0178 0.0036  -0.0226 63  VAL   A C   
1509 O O   . VAL   A 63  ? 0.1394 0.1492 0.1992 -0.0191 0.0033  -0.0114 63  VAL   A O   
1510 C CB  . VAL   A 63  ? 0.1545 0.1744 0.2360 -0.0135 -0.0095 -0.0430 63  VAL   A CB  
1511 C CG1 . VAL   A 63  ? 0.1578 0.1988 0.2670 -0.0133 -0.0114 -0.0682 63  VAL   A CG1 
1512 C CG2 . VAL   A 63  ? 0.1582 0.1708 0.2487 -0.0119 0.0072  -0.0369 63  VAL   A CG2 
1522 N N   . GLU   A 64  ? 0.1288 0.1611 0.1849 -0.0091 -0.0001 -0.0109 64  GLU   A N   
1523 C CA  . GLU   A 64  ? 0.1361 0.1557 0.1738 -0.0051 -0.0083 -0.0025 64  GLU   A CA  
1524 C C   . GLU   A 64  ? 0.1391 0.1379 0.1687 -0.0036 -0.0030 0.0044  64  GLU   A C   
1525 O O   . GLU   A 64  ? 0.1454 0.1522 0.1761 0.0038  0.0006  -0.0053 64  GLU   A O   
1526 C CB  . GLU   A 64  ? 0.1411 0.1717 0.1886 -0.0040 -0.0003 -0.0045 64  GLU   A CB  
1527 C CG  . GLU   A 64  ? 0.1496 0.1771 0.1997 -0.0020 0.0023  0.0030  64  GLU   A CG  
1528 C CD  . GLU   A 64  ? 0.1683 0.1862 0.2079 -0.0094 0.0047  0.0012  64  GLU   A CD  
1529 O OE1 . GLU   A 64  ? 0.1741 0.1945 0.2259 -0.0226 0.0209  -0.0090 64  GLU   A OE1 
1530 O OE2 . GLU   A 64  ? 0.1789 0.1884 0.2021 -0.0264 -0.0081 0.0027  64  GLU   A OE2 
1537 N N   . SER   A 65  ? 0.1419 0.1461 0.1606 -0.0012 -0.0054 0.0037  65  SER   A N   
1538 C CA  . SER   A 65  ? 0.1442 0.1375 0.1541 -0.0043 -0.0033 0.0021  65  SER   A CA  
1539 C C   . SER   A 65  ? 0.1410 0.1454 0.1683 -0.0048 -0.0083 0.0020  65  SER   A C   
1540 O O   . SER   A 65  ? 0.1420 0.1501 0.1924 0.0029  0.0096  -0.0029 65  SER   A O   
1541 C CB  . SER   A 65  ? 0.1380 0.1478 0.1654 -0.0124 -0.0015 0.0161  65  SER   A CB  
1542 O OG  . SER   A 65  ? 0.1390 0.1509 0.1753 -0.0081 -0.0065 0.0141  65  SER   A OG  
1548 N N   . ASP   A 66  ? 0.1402 0.1377 0.1848 -0.0045 0.0157  0.0057  66  ASP   A N   
1549 C CA  . ASP   A 66  ? 0.1504 0.1479 0.1936 0.0033  0.0142  0.0166  66  ASP   A CA  
1550 C C   . ASP   A 66  ? 0.1449 0.1544 0.1835 -0.0020 0.0143  0.0119  66  ASP   A C   
1551 O O   . ASP   A 66  ? 0.1532 0.1645 0.2055 -0.0010 0.0277  0.0203  66  ASP   A O   
1552 C CB  . ASP   A 66  ? 0.1655 0.1612 0.2227 0.0077  0.0169  0.0284  66  ASP   A CB  
1553 C CG  . ASP   A 66  ? 0.1881 0.1684 0.2652 0.0065  0.0075  0.0548  66  ASP   A CG  
1554 O OD1 . ASP   A 66  ? 0.1825 0.1994 0.2468 -0.0057 0.0128  0.0530  66  ASP   A OD1 
1555 O OD2 . ASP   A 66  ? 0.2044 0.1946 0.3449 0.0268  -0.0135 0.0272  66  ASP   A OD2 
1560 N N   . ASP   A 67  ? 0.1318 0.1540 0.2010 0.0016  0.0066  0.0151  67  ASP   A N   
1561 C CA  . ASP   A 67  ? 0.1448 0.1681 0.2104 -0.0008 -0.0008 0.0220  67  ASP   A CA  
1562 C C   . ASP   A 67  ? 0.1504 0.1627 0.2084 0.0072  0.0112  0.0221  67  ASP   A C   
1563 O O   . ASP   A 67  ? 0.1487 0.1725 0.2317 0.0096  0.0319  0.0292  67  ASP   A O   
1564 C CB  . ASP   A 67  ? 0.1539 0.1860 0.2438 -0.0070 -0.0162 0.0359  67  ASP   A CB  
1565 C CG  . ASP   A 67  ? 0.1589 0.1973 0.2814 -0.0133 -0.0222 0.0459  67  ASP   A CG  
1566 O OD1 . ASP   A 67  ? 0.1628 0.2117 0.3729 -0.0144 -0.0369 0.0562  67  ASP   A OD1 
1567 O OD2 . ASP   A 67  ? 0.1569 0.1984 0.2660 0.0040  -0.0129 0.0325  67  ASP   A OD2 
1572 N N   . TYR   A 68  ? 0.1487 0.1506 0.1997 0.0060  0.0132  0.0325  68  TYR   A N   
1573 C CA  . TYR   A 68  ? 0.1565 0.1513 0.1924 0.0042  0.0288  0.0175  68  TYR   A CA  
1574 C C   . TYR   A 68  ? 0.1476 0.1495 0.1920 0.0037  0.0351  0.0119  68  TYR   A C   
1575 O O   . TYR   A 68  ? 0.1596 0.1566 0.2012 0.0147  0.0356  0.0198  68  TYR   A O   
1576 C CB  . TYR   A 68  ? 0.1611 0.1457 0.2154 0.0114  0.0398  0.0255  68  TYR   A CB  
1577 C CG  . TYR   A 68  ? 0.1584 0.1704 0.2490 0.0122  0.0595  0.0162  68  TYR   A CG  
1578 C CD1 . TYR   A 68  ? 0.1810 0.1815 0.2769 -0.0168 0.0572  -0.0230 68  TYR   A CD1 
1579 C CD2 . TYR   A 68  ? 0.1817 0.1824 0.3054 0.0134  0.0617  0.0202  68  TYR   A CD2 
1580 C CE1 . TYR   A 68  ? 0.1843 0.1915 0.3152 -0.0123 0.0637  -0.0257 68  TYR   A CE1 
1581 C CE2 . TYR   A 68  ? 0.1824 0.1828 0.3265 0.0086  0.0756  -0.0082 68  TYR   A CE2 
1582 C CZ  . TYR   A 68  ? 0.1902 0.1852 0.3390 -0.0139 0.0656  -0.0311 68  TYR   A CZ  
1583 O OH  . TYR   A 68  ? 0.2178 0.1919 0.3770 -0.0151 0.0402  -0.0612 68  TYR   A OH  
1593 N N   . ILE   A 69  ? 0.1415 0.1466 0.1954 0.0061  0.0198  0.0136  69  ILE   A N   
1594 C CA  . ILE   A 69  ? 0.1511 0.1520 0.1950 0.0012  0.0104  -0.0004 69  ILE   A CA  
1595 C C   . ILE   A 69  ? 0.1455 0.1545 0.1856 0.0021  0.0166  0.0165  69  ILE   A C   
1596 O O   . ILE   A 69  ? 0.1558 0.1612 0.1837 0.0066  0.0249  0.0229  69  ILE   A O   
1597 C CB  . ILE   A 69  ? 0.1605 0.1721 0.1904 0.0018  0.0122  -0.0065 69  ILE   A CB  
1598 C CG1 . ILE   A 69  ? 0.1633 0.1834 0.2081 0.0009  0.0124  -0.0219 69  ILE   A CG1 
1599 C CG2 . ILE   A 69  ? 0.1808 0.1935 0.2019 0.0156  -0.0027 -0.0252 69  ILE   A CG2 
1600 C CD1 . ILE   A 69  ? 0.1620 0.1954 0.2246 -0.0078 0.0209  -0.0258 69  ILE   A CD1 
1612 N N   . ALA   A 70  ? 0.1511 0.1534 0.1897 -0.0094 0.0178  0.0188  70  ALA   A N   
1613 C CA  . ALA   A 70  ? 0.1677 0.1641 0.2062 -0.0173 0.0282  0.0218  70  ALA   A CA  
1614 C C   . ALA   A 70  ? 0.1644 0.1791 0.2051 -0.0145 0.0384  0.0181  70  ALA   A C   
1615 O O   . ALA   A 70  ? 0.1847 0.2200 0.2249 0.0061  0.0591  0.0349  70  ALA   A O   
1616 C CB  . ALA   A 70  ? 0.1698 0.1635 0.2305 -0.0222 0.0184  0.0112  70  ALA   A CB  
1622 N N   . THR   A 71  ? 0.1588 0.1710 0.1982 -0.0040 0.0260  0.0286  71  THR   A N   
1623 C CA  . THR   A 71  ? 0.1780 0.1869 0.2222 0.0082  0.0243  0.0269  71  THR   A CA  
1624 C C   . THR   A 71  ? 0.1636 0.1834 0.2501 0.0145  0.0381  0.0156  71  THR   A C   
1625 O O   . THR   A 71  ? 0.1693 0.2079 0.2940 0.0127  0.0513  -0.0039 71  THR   A O   
1626 C CB  . THR   A 71  ? 0.2044 0.2142 0.2556 0.0171  -0.0123 0.0313  71  THR   A CB  
1627 O OG1 . THR   A 71  ? 0.2302 0.2341 0.2716 0.0129  -0.0372 0.0230  71  THR   A OG1 
1628 C CG2 . THR   A 71  ? 0.2138 0.2338 0.2845 0.0248  -0.0257 0.0511  71  THR   A CG2 
1636 N N   . ASN   A 72  ? 0.1575 0.1690 0.2296 0.0120  0.0288  0.0255  72  ASN   A N   
1637 C CA  . ASN   A 72  ? 0.1642 0.1728 0.2247 0.0182  0.0424  0.0311  72  ASN   A CA  
1638 C C   . ASN   A 72  ? 0.1771 0.1779 0.2217 0.0146  0.0486  0.0139  72  ASN   A C   
1639 O O   . ASN   A 72  ? 0.1961 0.1857 0.2522 0.0195  0.0473  0.0001  72  ASN   A O   
1640 C CB  . ASN   A 72  ? 0.1840 0.1859 0.2225 0.0229  0.0431  0.0276  72  ASN   A CB  
1641 C CG  . ASN   A 72  ? 0.2057 0.1942 0.2244 0.0303  0.0421  0.0353  72  ASN   A CG  
1642 O OD1 . ASN   A 72  ? 0.2216 0.2254 0.2497 0.0269  0.0471  0.0308  72  ASN   A OD1 
1643 N ND2 . ASN   A 72  ? 0.2291 0.1977 0.2340 0.0619  0.0235  0.0265  72  ASN   A ND2 
1650 N N   . GLY   A 73  ? 0.1754 0.1704 0.2058 0.0065  0.0510  0.0045  73  GLY   A N   
1651 C CA  . GLY   A 73  ? 0.1787 0.1640 0.1985 -0.0072 0.0396  0.0101  73  GLY   A CA  
1652 C C   . GLY   A 73  ? 0.1783 0.1524 0.1816 0.0007  0.0516  0.0335  73  GLY   A C   
1653 O O   . GLY   A 73  ? 0.1789 0.1588 0.2087 0.0102  0.0345  0.0298  73  GLY   A O   
1657 N N   . PRO   A 74  ? 0.1937 0.1594 0.1865 -0.0135 0.0518  0.0208  74  PRO   A N   
1658 C CA  . PRO   A 74  ? 0.1874 0.1504 0.1980 -0.0025 0.0477  0.0177  74  PRO   A CA  
1659 C C   . PRO   A 74  ? 0.1771 0.1327 0.1930 -0.0023 0.0301  0.0093  74  PRO   A C   
1660 O O   . PRO   A 74  ? 0.1812 0.1496 0.2145 0.0027  0.0357  -0.0086 74  PRO   A O   
1661 C CB  . PRO   A 74  ? 0.2032 0.1815 0.2285 0.0038  0.0483  0.0289  74  PRO   A CB  
1662 C CG  . PRO   A 74  ? 0.2320 0.2170 0.2751 -0.0174 0.0348  0.0214  74  PRO   A CG  
1663 C CD  . PRO   A 74  ? 0.2119 0.1917 0.2141 -0.0257 0.0387  0.0082  74  PRO   A CD  
1671 N N   . LEU   A 75  ? 0.1775 0.1420 0.1717 -0.0061 0.0346  0.0065  75  LEU   A N   
1672 C CA  . LEU   A 75  ? 0.1777 0.1460 0.1458 -0.0052 0.0147  0.0133  75  LEU   A CA  
1673 C C   . LEU   A 75  ? 0.1870 0.1527 0.1555 0.0012  0.0201  0.0134  75  LEU   A C   
1674 O O   . LEU   A 75  ? 0.2176 0.1668 0.1658 0.0118  0.0104  0.0055  75  LEU   A O   
1675 C CB  . LEU   A 75  ? 0.1872 0.1467 0.1435 -0.0149 0.0149  0.0186  75  LEU   A CB  
1676 C CG  . LEU   A 75  ? 0.2036 0.1771 0.1675 -0.0386 0.0151  0.0119  75  LEU   A CG  
1677 C CD1 . LEU   A 75  ? 0.2115 0.2311 0.1723 -0.0418 0.0136  -0.0049 75  LEU   A CD1 
1678 C CD2 . LEU   A 75  ? 0.2407 0.2179 0.2295 -0.0139 0.0193  0.0157  75  LEU   A CD2 
1690 N N   . LYS   A 76  ? 0.1812 0.1491 0.1827 -0.0130 0.0106  -0.0029 76  LYS   A N   
1691 C CA  . LYS   A 76  ? 0.1728 0.1688 0.1860 -0.0070 0.0129  -0.0098 76  LYS   A CA  
1692 C C   . LYS   A 76  ? 0.1715 0.1607 0.1572 0.0002  0.0108  0.0015  76  LYS   A C   
1693 O O   . LYS   A 76  ? 0.1754 0.1508 0.1588 -0.0015 0.0178  0.0073  76  LYS   A O   
1694 C CB  . LYS   A 76  ? 0.1759 0.1947 0.2249 0.0112  0.0188  -0.0367 76  LYS   A CB  
1695 C CG  . LYS   A 76  ? 0.1920 0.1942 0.2711 0.0178  0.0111  -0.0389 76  LYS   A CG  
1696 C CD  . LYS   A 76  ? 0.1985 0.2037 0.3094 0.0233  -0.0018 -0.0389 76  LYS   A CD  
1697 C CE  . LYS   A 76  ? 0.2108 0.2191 0.3729 0.0070  0.0139  -0.0529 76  LYS   A CE  
1698 N NZ  . LYS   A 76  ? 0.2097 0.2107 0.4195 -0.0069 0.0112  -0.0631 76  LYS   A NZ  
1712 N N   . VAL   A 77  ? 0.1882 0.1593 0.1450 -0.0003 0.0219  0.0132  77  VAL   A N   
1713 C CA  . VAL   A 77  ? 0.1784 0.1589 0.1490 0.0049  0.0248  0.0130  77  VAL   A CA  
1714 C C   . VAL   A 77  ? 0.1666 0.1565 0.1576 0.0078  0.0169  0.0045  77  VAL   A C   
1715 O O   . VAL   A 77  ? 0.1741 0.1690 0.1606 0.0134  0.0257  -0.0113 77  VAL   A O   
1716 C CB  . VAL   A 77  ? 0.1998 0.1801 0.1690 0.0031  0.0153  0.0201  77  VAL   A CB  
1717 C CG1 . VAL   A 77  ? 0.1999 0.1975 0.1885 0.0093  -0.0001 0.0114  77  VAL   A CG1 
1718 C CG2 . VAL   A 77  ? 0.2249 0.1860 0.1957 -0.0049 0.0020  0.0262  77  VAL   A CG2 
1728 N N   . GLY   A 78  ? 0.1676 0.1555 0.1431 0.0066  0.0215  0.0129  78  GLY   A N   
1729 C CA  . GLY   A 78  ? 0.1710 0.1529 0.1495 0.0054  0.0216  0.0138  78  GLY   A CA  
1730 C C   . GLY   A 78  ? 0.1582 0.1473 0.1453 0.0049  0.0262  0.0127  78  GLY   A C   
1731 O O   . GLY   A 78  ? 0.1604 0.1509 0.1799 0.0033  0.0204  0.0291  78  GLY   A O   
1735 N N   . GLY   A 79  ? 0.1587 0.1442 0.1494 0.0060  0.0201  0.0156  79  GLY   A N   
1736 C CA  . GLY   A 79  ? 0.1569 0.1490 0.1698 0.0053  0.0112  0.0153  79  GLY   A CA  
1737 C C   . GLY   A 79  ? 0.1430 0.1348 0.1515 0.0041  0.0135  0.0071  79  GLY   A C   
1738 O O   . GLY   A 79  ? 0.1504 0.1455 0.1666 0.0235  0.0152  0.0052  79  GLY   A O   
1742 N N   . SER   A 80  ? 0.1415 0.1494 0.1697 0.0030  0.0148  -0.0006 80  SER   A N   
1743 C CA  . SER   A 80  ? 0.1426 0.1409 0.1592 -0.0028 0.0063  -0.0047 80  SER   A CA  
1744 C C   . SER   A 80  ? 0.1491 0.1441 0.1484 0.0002  0.0163  0.0112  80  SER   A C   
1745 O O   . SER   A 80  ? 0.1512 0.1647 0.1855 0.0136  0.0178  -0.0050 80  SER   A O   
1746 C CB  . SER   A 80  ? 0.1493 0.1436 0.1960 -0.0059 0.0096  0.0080  80  SER   A CB  
1747 O OG  . SER   A 80  ? 0.1776 0.1568 0.2300 0.0062  -0.0018 0.0204  80  SER   A OG  
1753 N N   . CYS   A 81  ? 0.1428 0.1439 0.1466 0.0051  0.0018  0.0114  81  CYS   A N   
1754 C CA  . CYS   A 81  ? 0.1429 0.1542 0.1393 -0.0066 -0.0092 0.0251  81  CYS   A CA  
1755 C C   . CYS   A 81  ? 0.1398 0.1546 0.1391 -0.0070 -0.0001 0.0289  81  CYS   A C   
1756 O O   . CYS   A 81  ? 0.1358 0.1733 0.1809 0.0009  0.0095  0.0349  81  CYS   A O   
1757 C CB  . CYS   A 81  ? 0.1470 0.1539 0.1843 -0.0145 -0.0009 0.0244  81  CYS   A CB  
1758 S SG  . CYS   A 81  ? 0.1608 0.1498 0.1714 -0.0141 0.0050  0.0138  81  CYS   A SG  
1764 N N   . VAL   A 82  ? 0.1389 0.1646 0.1478 -0.0015 -0.0120 0.0134  82  VAL   A N   
1765 C CA  . VAL   A 82  ? 0.1447 0.1742 0.1446 -0.0022 -0.0069 0.0278  82  VAL   A CA  
1766 C C   . VAL   A 82  ? 0.1458 0.1706 0.1597 -0.0103 -0.0070 0.0258  82  VAL   A C   
1767 O O   . VAL   A 82  ? 0.1493 0.1739 0.1899 -0.0061 0.0001  -0.0071 82  VAL   A O   
1768 C CB  . VAL   A 82  ? 0.1801 0.1815 0.1659 0.0005  -0.0038 0.0318  82  VAL   A CB  
1769 C CG1 . VAL   A 82  ? 0.2068 0.1946 0.1726 0.0044  0.0089  0.0241  82  VAL   A CG1 
1770 C CG2 . VAL   A 82  ? 0.1859 0.1837 0.2063 -0.0108 -0.0067 0.0324  82  VAL   A CG2 
1780 N N   . LEU   A 83  ? 0.1425 0.1726 0.1587 -0.0150 -0.0100 0.0090  83  LEU   A N   
1781 C CA  . LEU   A 83  ? 0.1500 0.1750 0.1461 -0.0087 -0.0136 0.0044  83  LEU   A CA  
1782 C C   . LEU   A 83  ? 0.1561 0.1707 0.1533 -0.0138 -0.0166 0.0100  83  LEU   A C   
1783 O O   . LEU   A 83  ? 0.1646 0.1699 0.1667 -0.0140 -0.0049 0.0159  83  LEU   A O   
1784 C CB  . LEU   A 83  ? 0.1557 0.1806 0.1464 -0.0063 -0.0170 0.0183  83  LEU   A CB  
1785 C CG  . LEU   A 83  ? 0.1687 0.1925 0.1621 -0.0094 -0.0029 0.0082  83  LEU   A CG  
1786 C CD1 . LEU   A 83  ? 0.1801 0.1915 0.1608 -0.0225 -0.0047 0.0289  83  LEU   A CD1 
1787 C CD2 . LEU   A 83  ? 0.1715 0.1954 0.1891 -0.0098 0.0147  0.0165  83  LEU   A CD2 
1799 N N   . SER   A 84  ? 0.1736 0.1733 0.1592 -0.0124 -0.0120 0.0122  84  SER   A N   
1800 C CA  . SER   A 84  ? 0.1807 0.1828 0.1466 -0.0130 -0.0114 0.0065  84  SER   A CA  
1801 C C   . SER   A 84  ? 0.1813 0.1744 0.1328 -0.0187 0.0005  0.0124  84  SER   A C   
1802 O O   . SER   A 84  ? 0.1824 0.1888 0.1373 -0.0088 -0.0069 0.0048  84  SER   A O   
1803 C CB  . SER   A 84  ? 0.1869 0.2052 0.1617 -0.0140 -0.0088 0.0010  84  SER   A CB  
1804 O OG  . SER   A 84  ? 0.1926 0.2226 0.1701 -0.0064 -0.0215 -0.0092 84  SER   A OG  
1810 N N   . GLY   A 85  ? 0.1963 0.1918 0.1362 -0.0157 0.0101  0.0027  85  GLY   A N   
1811 C CA  . GLY   A 85  ? 0.2031 0.2001 0.1587 -0.0168 0.0134  -0.0074 85  GLY   A CA  
1812 C C   . GLY   A 85  ? 0.2026 0.1970 0.1451 -0.0147 0.0026  -0.0063 85  GLY   A C   
1813 O O   . GLY   A 85  ? 0.2064 0.2037 0.1655 -0.0299 0.0252  -0.0135 85  GLY   A O   
1817 N N   . HIS   A 86  ? 0.2002 0.1916 0.1426 -0.0142 -0.0014 -0.0064 86  HIS   A N   
1818 C CA  . HIS   A 86  ? 0.2167 0.2021 0.1478 -0.0177 0.0015  -0.0036 86  HIS   A CA  
1819 C C   . HIS   A 86  ? 0.2386 0.2080 0.1409 -0.0181 0.0004  0.0001  86  HIS   A C   
1820 O O   . HIS   A 86  ? 0.2490 0.2251 0.1569 -0.0067 0.0121  -0.0029 86  HIS   A O   
1821 C CB  . HIS   A 86  ? 0.2146 0.1936 0.1490 -0.0133 0.0105  0.0004  86  HIS   A CB  
1822 C CG  . HIS   A 86  ? 0.2032 0.1961 0.1587 -0.0094 0.0170  0.0134  86  HIS   A CG  
1823 N ND1 . HIS   A 86  ? 0.2034 0.1999 0.2013 -0.0198 0.0052  0.0085  86  HIS   A ND1 
1824 C CD2 . HIS   A 86  ? 0.2080 0.1907 0.1509 0.0011  0.0189  0.0202  86  HIS   A CD2 
1825 C CE1 . HIS   A 86  ? 0.2058 0.2021 0.1921 -0.0092 0.0262  0.0159  86  HIS   A CE1 
1826 N NE2 . HIS   A 86  ? 0.2096 0.1945 0.1733 0.0064  0.0263  0.0373  86  HIS   A NE2 
1834 N N   . ASN   A 87  ? 0.2505 0.2219 0.1555 -0.0126 0.0252  -0.0134 87  ASN   A N   
1835 C CA  . ASN   A 87  ? 0.2718 0.2363 0.1600 -0.0102 0.0517  -0.0194 87  ASN   A CA  
1836 C C   . ASN   A 87  ? 0.2681 0.2471 0.2009 -0.0180 0.0715  -0.0068 87  ASN   A C   
1837 O O   . ASN   A 87  ? 0.2936 0.2654 0.2436 -0.0345 0.1054  -0.0119 87  ASN   A O   
1838 C CB  . ASN   A 87  ? 0.2904 0.2438 0.1725 -0.0002 0.0510  -0.0222 87  ASN   A CB  
1839 C CG  . ASN   A 87  ? 0.3028 0.2487 0.1777 0.0060  0.0668  -0.0127 87  ASN   A CG  
1840 O OD1 . ASN   A 87  ? 0.3193 0.2438 0.1858 0.0256  0.0557  0.0080  87  ASN   A OD1 
1841 N ND2 . ASN   A 87  ? 0.3066 0.2749 0.1871 0.0021  0.0651  -0.0109 87  ASN   A ND2 
1848 N N   . LEU   A 88  ? 0.2446 0.2287 0.1949 -0.0269 0.0427  0.0073  88  LEU   A N   
1849 C CA  . LEU   A 88  ? 0.2344 0.2224 0.2041 -0.0361 0.0367  0.0159  88  LEU   A CA  
1850 C C   . LEU   A 88  ? 0.2308 0.2257 0.1958 -0.0320 0.0418  0.0314  88  LEU   A C   
1851 O O   . LEU   A 88  ? 0.2334 0.2353 0.2330 -0.0344 0.0482  0.0499  88  LEU   A O   
1852 C CB  . LEU   A 88  ? 0.2310 0.2333 0.2219 -0.0429 0.0022  0.0192  88  LEU   A CB  
1853 C CG  . LEU   A 88  ? 0.2457 0.2465 0.2615 -0.0391 -0.0103 0.0189  88  LEU   A CG  
1854 C CD1 . LEU   A 88  ? 0.2541 0.2511 0.2482 -0.0391 -0.0125 0.0003  88  LEU   A CD1 
1855 C CD2 . LEU   A 88  ? 0.2601 0.2647 0.3127 -0.0349 -0.0100 0.0124  88  LEU   A CD2 
1867 N N   . ALA   A 89  ? 0.2279 0.2187 0.1706 -0.0269 0.0284  0.0071  89  ALA   A N   
1868 C CA  . ALA   A 89  ? 0.2308 0.2194 0.1537 -0.0190 0.0131  0.0210  89  ALA   A CA  
1869 C C   . ALA   A 89  ? 0.2293 0.2232 0.1620 -0.0166 -0.0027 0.0199  89  ALA   A C   
1870 O O   . ALA   A 89  ? 0.2303 0.2230 0.2008 -0.0274 -0.0024 -0.0104 89  ALA   A O   
1871 C CB  . ALA   A 89  ? 0.2156 0.2205 0.1429 -0.0175 0.0108  0.0258  89  ALA   A CB  
1877 N N   . LYS   A 90  ? 0.2399 0.2394 0.1571 -0.0283 -0.0219 0.0227  90  LYS   A N   
1878 C CA  . LYS   A 90  ? 0.2488 0.2541 0.1605 -0.0230 -0.0264 0.0201  90  LYS   A CA  
1879 C C   . LYS   A 90  ? 0.2273 0.2371 0.1522 -0.0260 -0.0252 0.0096  90  LYS   A C   
1880 O O   . LYS   A 90  ? 0.2317 0.2585 0.1903 -0.0319 -0.0328 -0.0012 90  LYS   A O   
1881 C CB  . LYS   A 90  ? 0.2753 0.2867 0.2134 -0.0223 -0.0301 0.0464  90  LYS   A CB  
1882 C CG  . LYS   A 90  ? 0.3138 0.3224 0.3078 -0.0206 -0.0243 0.0543  90  LYS   A CG  
1883 C CD  . LYS   A 90  ? 0.3576 0.3642 0.4087 -0.0202 -0.0115 0.0593  90  LYS   A CD  
1884 C CE  . LYS   A 90  ? 0.3922 0.3992 0.4796 -0.0212 -0.0021 0.0559  90  LYS   A CE  
1885 N NZ  . LYS   A 90  ? 0.4059 0.4142 0.5311 -0.0228 0.0020  0.0513  90  LYS   A NZ  
1899 N N   . HIS   A 91  ? 0.2183 0.2064 0.1100 -0.0209 -0.0299 0.0098  91  HIS   A N   
1900 C CA  . HIS   A 91  ? 0.2038 0.1913 0.1172 -0.0157 -0.0253 0.0159  91  HIS   A CA  
1901 C C   . HIS   A 91  ? 0.1779 0.1752 0.1034 -0.0167 -0.0148 0.0154  91  HIS   A C   
1902 O O   . HIS   A 91  ? 0.1699 0.1933 0.1422 -0.0188 0.0003  0.0209  91  HIS   A O   
1903 C CB  . HIS   A 91  ? 0.2207 0.2202 0.1794 0.0075  -0.0346 0.0145  91  HIS   A CB  
1904 C CG  . HIS   A 91  ? 0.2631 0.2702 0.2559 0.0134  -0.0609 0.0127  91  HIS   A CG  
1905 N ND1 . HIS   A 91  ? 0.2738 0.2979 0.2936 0.0155  -0.0732 -0.0078 91  HIS   A ND1 
1906 C CD2 . HIS   A 91  ? 0.2858 0.2928 0.2789 0.0201  -0.0771 0.0246  91  HIS   A CD2 
1907 C CE1 . HIS   A 91  ? 0.2825 0.3072 0.3065 0.0201  -0.0752 0.0095  91  HIS   A CE1 
1908 N NE2 . HIS   A 91  ? 0.2957 0.3080 0.3074 0.0255  -0.0830 0.0167  91  HIS   A NE2 
1916 N N   . CYS   A 92  ? 0.1646 0.1689 0.1214 -0.0135 -0.0074 0.0181  92  CYS   A N   
1917 C CA  . CYS   A 92  ? 0.1571 0.1682 0.1358 -0.0117 -0.0021 0.0222  92  CYS   A CA  
1918 C C   . CYS   A 92  ? 0.1478 0.1586 0.1389 -0.0216 0.0119  0.0142  92  CYS   A C   
1919 O O   . CYS   A 92  ? 0.1588 0.1675 0.1525 -0.0255 0.0016  0.0130  92  CYS   A O   
1920 C CB  . CYS   A 92  ? 0.1691 0.1686 0.1531 -0.0046 -0.0002 0.0177  92  CYS   A CB  
1921 S SG  . CYS   A 92  ? 0.1599 0.1582 0.1512 -0.0120 -0.0013 0.0077  92  CYS   A SG  
1927 N N   . LEU   A 93  ? 0.1364 0.1491 0.1467 -0.0082 0.0173  0.0097  93  LEU   A N   
1928 C CA  . LEU   A 93  ? 0.1244 0.1415 0.1446 -0.0061 0.0029  0.0066  93  LEU   A CA  
1929 C C   . LEU   A 93  ? 0.1364 0.1299 0.1409 -0.0017 0.0059  0.0109  93  LEU   A C   
1930 O O   . LEU   A 93  ? 0.1341 0.1474 0.1417 -0.0007 0.0042  0.0112  93  LEU   A O   
1931 C CB  . LEU   A 93  ? 0.1415 0.1482 0.1524 -0.0009 -0.0008 0.0188  93  LEU   A CB  
1932 C CG  . LEU   A 93  ? 0.1508 0.1489 0.1556 -0.0070 0.0071  0.0263  93  LEU   A CG  
1933 C CD1 . LEU   A 93  ? 0.1574 0.1473 0.1925 0.0064  0.0192  0.0167  93  LEU   A CD1 
1934 C CD2 . LEU   A 93  ? 0.1635 0.1538 0.1769 -0.0048 -0.0046 0.0221  93  LEU   A CD2 
1946 N N   . HIS   A 94  ? 0.1301 0.1262 0.1497 0.0025  0.0033  0.0142  94  HIS   A N   
1947 C CA  . HIS   A 94  ? 0.1257 0.1373 0.1393 -0.0074 -0.0058 0.0138  94  HIS   A CA  
1948 C C   . HIS   A 94  ? 0.1329 0.1324 0.1389 -0.0073 0.0011  -0.0022 94  HIS   A C   
1949 O O   . HIS   A 94  ? 0.1332 0.1489 0.1828 0.0051  0.0106  -0.0180 94  HIS   A O   
1950 C CB  . HIS   A 94  ? 0.1267 0.1351 0.1424 -0.0010 -0.0079 0.0115  94  HIS   A CB  
1951 C CG  . HIS   A 94  ? 0.1281 0.1357 0.1456 -0.0030 -0.0059 0.0076  94  HIS   A CG  
1952 N ND1 . HIS   A 94  ? 0.1335 0.1314 0.1458 -0.0085 0.0012  0.0139  94  HIS   A ND1 
1953 C CD2 . HIS   A 94  ? 0.1353 0.1523 0.1608 -0.0034 -0.0050 0.0003  94  HIS   A CD2 
1954 C CE1 . HIS   A 94  ? 0.1442 0.1326 0.1548 -0.0073 -0.0114 0.0056  94  HIS   A CE1 
1955 N NE2 . HIS   A 94  ? 0.1489 0.1459 0.1506 -0.0063 -0.0015 -0.0020 94  HIS   A NE2 
1963 N N   . VAL   A 95  ? 0.1382 0.1281 0.1241 -0.0057 0.0020  -0.0042 95  VAL   A N   
1964 C CA  . VAL   A 95  ? 0.1371 0.1433 0.1131 -0.0030 -0.0012 0.0100  95  VAL   A CA  
1965 C C   . VAL   A 95  ? 0.1278 0.1341 0.1096 -0.0185 0.0011  0.0012  95  VAL   A C   
1966 O O   . VAL   A 95  ? 0.1397 0.1399 0.1382 0.0089  0.0110  0.0067  95  VAL   A O   
1967 C CB  . VAL   A 95  ? 0.1353 0.1452 0.1446 -0.0113 0.0016  0.0077  95  VAL   A CB  
1968 C CG1 . VAL   A 95  ? 0.1477 0.1568 0.1560 -0.0189 0.0035  -0.0114 95  VAL   A CG1 
1969 C CG2 . VAL   A 95  ? 0.1426 0.1323 0.1525 -0.0136 0.0024  0.0158  95  VAL   A CG2 
1979 N N   . VAL   A 96  ? 0.1387 0.1348 0.1133 -0.0037 0.0080  0.0056  96  VAL   A N   
1980 C CA  . VAL   A 96  ? 0.1431 0.1338 0.1329 -0.0024 0.0111  0.0228  96  VAL   A CA  
1981 C C   . VAL   A 96  ? 0.1460 0.1431 0.1529 0.0070  0.0202  0.0214  96  VAL   A C   
1982 O O   . VAL   A 96  ? 0.1503 0.1529 0.1638 -0.0008 0.0234  0.0002  96  VAL   A O   
1983 C CB  . VAL   A 96  ? 0.1504 0.1427 0.1393 -0.0022 0.0192  0.0180  96  VAL   A CB  
1984 C CG1 . VAL   A 96  ? 0.1558 0.1469 0.1358 -0.0022 0.0102  0.0109  96  VAL   A CG1 
1985 C CG2 . VAL   A 96  ? 0.1460 0.1559 0.1637 -0.0115 0.0145  0.0142  96  VAL   A CG2 
1995 N N   A GLY   A 97  ? 0.1469 0.1433 0.1486 0.0005  0.0120  0.0120  97  GLY   A N   
1996 N N   B GLY   A 97  ? 0.1495 0.1490 0.1526 0.0048  0.0149  0.0149  97  GLY   A N   
1997 C CA  A GLY   A 97  ? 0.1570 0.1608 0.1501 -0.0069 -0.0016 0.0029  97  GLY   A CA  
1998 C CA  B GLY   A 97  ? 0.1542 0.1541 0.1535 0.0032  0.0101  0.0148  97  GLY   A CA  
1999 C C   A GLY   A 97  ? 0.1514 0.1764 0.1310 -0.0159 0.0025  0.0003  97  GLY   A C   
2000 C C   B GLY   A 97  ? 0.1566 0.1588 0.1531 -0.0001 0.0095  0.0198  97  GLY   A C   
2001 O O   A GLY   A 97  ? 0.1668 0.1786 0.1517 -0.0116 0.0004  0.0028  97  GLY   A O   
2002 O O   B GLY   A 97  ? 0.1558 0.1612 0.1517 -0.0037 0.0143  0.0270  97  GLY   A O   
2009 N N   A PRO   A 98  ? 0.1674 0.1706 0.1227 -0.0056 0.0000  0.0156  98  PRO   A N   
2010 N N   B PRO   A 98  ? 0.1648 0.1586 0.1572 0.0017  0.0053  0.0230  98  PRO   A N   
2011 C CA  A PRO   A 98  ? 0.1759 0.1950 0.1196 -0.0038 0.0025  -0.0022 98  PRO   A CA  
2012 C CA  B PRO   A 98  ? 0.1725 0.1604 0.1619 0.0018  0.0002  0.0188  98  PRO   A CA  
2013 C C   A PRO   A 98  ? 0.1798 0.2089 0.1237 -0.0139 0.0125  0.0177  98  PRO   A C   
2014 C C   B PRO   A 98  ? 0.1842 0.1594 0.1619 0.0019  0.0031  0.0273  98  PRO   A C   
2015 O O   A PRO   A 98  ? 0.1771 0.1901 0.1447 -0.0082 0.0139  0.0167  98  PRO   A O   
2016 O O   B PRO   A 98  ? 0.1854 0.1604 0.1726 -0.0011 0.0087  0.0293  98  PRO   A O   
2017 C CB  A PRO   A 98  ? 0.1868 0.2053 0.1188 0.0086  0.0021  -0.0061 98  PRO   A CB  
2018 C CB  B PRO   A 98  ? 0.1707 0.1578 0.1554 0.0047  0.0002  0.0159  98  PRO   A CB  
2019 C CG  A PRO   A 98  ? 0.1935 0.1895 0.1326 0.0125  -0.0046 -0.0136 98  PRO   A CG  
2020 C CG  B PRO   A 98  ? 0.1726 0.1575 0.1572 0.0041  0.0022  0.0144  98  PRO   A CG  
2021 C CD  A PRO   A 98  ? 0.1815 0.1746 0.1248 0.0067  -0.0092 0.0009  98  PRO   A CD  
2022 C CD  B PRO   A 98  ? 0.1679 0.1578 0.1552 0.0038  0.0015  0.0194  98  PRO   A CD  
2037 N N   A ASN   A 99  ? 0.1791 0.2307 0.1277 -0.0083 0.0091  0.0389  99  ASN   A N   
2038 N N   B ASN   A 99  ? 0.1962 0.1558 0.1509 0.0089  0.0004  0.0359  99  ASN   A N   
2039 C CA  A ASN   A 99  ? 0.2008 0.2426 0.1257 -0.0078 0.0066  0.0510  99  ASN   A CA  
2040 C CA  B ASN   A 99  ? 0.2089 0.1548 0.1543 0.0165  0.0001  0.0377  99  ASN   A CA  
2041 C C   A ASN   A 99  ? 0.2244 0.2800 0.1262 -0.0129 0.0107  0.0603  99  ASN   A C   
2042 C C   B ASN   A 99  ? 0.2162 0.1534 0.1642 0.0215  -0.0104 0.0395  99  ASN   A C   
2043 O O   A ASN   A 99  ? 0.2412 0.3098 0.1478 -0.0037 0.0024  0.0461  99  ASN   A O   
2044 O O   B ASN   A 99  ? 0.2149 0.1430 0.1567 0.0262  -0.0173 0.0398  99  ASN   A O   
2045 C CB  A ASN   A 99  ? 0.1995 0.2259 0.1652 -0.0096 -0.0081 0.0632  99  ASN   A CB  
2046 C CB  B ASN   A 99  ? 0.2111 0.1520 0.1458 0.0210  0.0060  0.0348  99  ASN   A CB  
2047 C CG  A ASN   A 99  ? 0.2025 0.2213 0.2072 -0.0013 -0.0147 0.0454  99  ASN   A CG  
2048 C CG  B ASN   A 99  ? 0.2165 0.1548 0.1490 0.0231  0.0111  0.0277  99  ASN   A CG  
2049 O OD1 A ASN   A 99  ? 0.2171 0.2274 0.2206 0.0100  -0.0074 0.0333  99  ASN   A OD1 
2050 O OD1 B ASN   A 99  ? 0.2152 0.1527 0.1393 0.0308  0.0144  0.0268  99  ASN   A OD1 
2051 N ND2 A ASN   A 99  ? 0.2075 0.2139 0.2375 -0.0015 -0.0163 0.0507  99  ASN   A ND2 
2052 N ND2 B ASN   A 99  ? 0.2187 0.1599 0.1654 0.0201  0.0098  0.0208  99  ASN   A ND2 
2065 N N   A VAL   A 100 ? 0.2385 0.2885 0.1277 -0.0300 -0.0169 0.0428  100 VAL   A N   
2066 N N   B VAL   A 100 ? 0.2273 0.1729 0.1848 0.0201  -0.0164 0.0378  100 VAL   A N   
2067 C CA  A VAL   A 100 ? 0.2645 0.3129 0.1605 -0.0346 -0.0158 0.0426  100 VAL   A CA  
2068 C CA  B VAL   A 100 ? 0.2399 0.1925 0.2129 0.0181  -0.0200 0.0245  100 VAL   A CA  
2069 C C   A VAL   A 100 ? 0.2790 0.3318 0.1702 -0.0397 -0.0256 0.0672  100 VAL   A C   
2070 C C   B VAL   A 100 ? 0.2473 0.1991 0.2256 0.0243  -0.0180 0.0123  100 VAL   A C   
2071 O O   A VAL   A 100 ? 0.2879 0.3422 0.1934 -0.0333 -0.0103 0.0672  100 VAL   A O   
2072 O O   B VAL   A 100 ? 0.2469 0.1956 0.2241 0.0246  -0.0198 -0.0016 100 VAL   A O   
2073 C CB  A VAL   A 100 ? 0.2831 0.3183 0.2035 -0.0409 -0.0293 0.0353  100 VAL   A CB  
2074 C CB  B VAL   A 100 ? 0.2439 0.2036 0.2258 0.0129  -0.0221 0.0204  100 VAL   A CB  
2075 C CG1 A VAL   A 100 ? 0.2849 0.3228 0.2246 -0.0458 -0.0278 0.0287  100 VAL   A CG1 
2076 C CG1 B VAL   A 100 ? 0.2446 0.2048 0.2290 0.0105  -0.0226 0.0174  100 VAL   A CG1 
2077 C CG2 A VAL   A 100 ? 0.2983 0.3269 0.2128 -0.0429 -0.0242 0.0386  100 VAL   A CG2 
2078 C CG2 B VAL   A 100 ? 0.2448 0.2091 0.2332 0.0132  -0.0221 0.0184  100 VAL   A CG2 
2097 N N   A ASN   A 101 ? 0.2845 0.3382 0.1924 -0.0491 -0.0412 0.0970  101 ASN   A N   
2098 N N   B ASN   A 101 ? 0.2573 0.2102 0.2347 0.0273  -0.0164 0.0107  101 ASN   A N   
2099 C CA  A ASN   A 101 ? 0.3107 0.3485 0.2177 -0.0535 -0.0394 0.1257  101 ASN   A CA  
2100 C CA  B ASN   A 101 ? 0.2683 0.2220 0.2451 0.0320  -0.0146 0.0108  101 ASN   A CA  
2101 C C   A ASN   A 101 ? 0.3360 0.3814 0.2423 -0.0612 -0.0137 0.1551  101 ASN   A C   
2102 C C   B ASN   A 101 ? 0.2834 0.2418 0.2597 0.0260  -0.0138 0.0117  101 ASN   A C   
2103 O O   A ASN   A 101 ? 0.3569 0.3865 0.2979 -0.0540 -0.0214 0.1431  101 ASN   A O   
2104 O O   B ASN   A 101 ? 0.2852 0.2432 0.2552 0.0251  -0.0182 0.0163  101 ASN   A O   
2105 C CB  A ASN   A 101 ? 0.3135 0.3316 0.2287 -0.0506 -0.0604 0.1029  101 ASN   A CB  
2106 C CB  B ASN   A 101 ? 0.2638 0.2165 0.2446 0.0405  -0.0142 0.0098  101 ASN   A CB  
2107 C CG  A ASN   A 101 ? 0.3151 0.3170 0.2315 -0.0506 -0.0735 0.0608  101 ASN   A CG  
2108 C CG  B ASN   A 101 ? 0.2610 0.2144 0.2494 0.0462  -0.0145 0.0095  101 ASN   A CG  
2109 O OD1 A ASN   A 101 ? 0.3127 0.3250 0.2372 -0.0290 -0.0727 0.0223  101 ASN   A OD1 
2110 O OD1 B ASN   A 101 ? 0.2637 0.2149 0.2594 0.0482  -0.0133 0.0125  101 ASN   A OD1 
2111 N ND2 A ASN   A 101 ? 0.3185 0.3053 0.2307 -0.0597 -0.0794 0.0688  101 ASN   A ND2 
2112 N ND2 B ASN   A 101 ? 0.2585 0.2119 0.2470 0.0500  -0.0120 0.0035  101 ASN   A ND2 
2125 N N   A LYS   A 102 ? 0.3348 0.4124 0.2696 -0.0769 0.0122  0.1530  102 LYS   A N   
2126 N N   B LYS   A 102 ? 0.2952 0.2578 0.2821 0.0230  -0.0098 0.0097  102 LYS   A N   
2127 C CA  A LYS   A 102 ? 0.3447 0.4403 0.2720 -0.0813 0.0126  0.1402  102 LYS   A CA  
2128 C CA  B LYS   A 102 ? 0.3062 0.2750 0.2955 0.0164  -0.0077 0.0103  102 LYS   A CA  
2129 C C   A LYS   A 102 ? 0.3585 0.4680 0.2547 -0.0689 0.0083  0.1273  102 LYS   A C   
2130 C C   B LYS   A 102 ? 0.3110 0.2812 0.2913 0.0132  -0.0072 0.0152  102 LYS   A C   
2131 O O   A LYS   A 102 ? 0.3667 0.4861 0.2706 -0.0639 0.0118  0.1123  102 LYS   A O   
2132 O O   B LYS   A 102 ? 0.3109 0.2787 0.2886 0.0139  -0.0058 0.0188  102 LYS   A O   
2133 C CB  A LYS   A 102 ? 0.3491 0.4413 0.3102 -0.0936 0.0048  0.1266  102 LYS   A CB  
2134 C CB  B LYS   A 102 ? 0.3111 0.2834 0.3112 0.0149  -0.0074 0.0064  102 LYS   A CB  
2135 C CG  A LYS   A 102 ? 0.3541 0.4403 0.3410 -0.1029 -0.0029 0.1086  102 LYS   A CG  
2136 C CG  B LYS   A 102 ? 0.3167 0.2915 0.3286 0.0127  -0.0080 0.0035  102 LYS   A CG  
2137 C CD  A LYS   A 102 ? 0.3646 0.4416 0.3765 -0.1060 -0.0135 0.0840  102 LYS   A CD  
2138 C CD  B LYS   A 102 ? 0.3217 0.2984 0.3463 0.0111  -0.0077 0.0012  102 LYS   A CD  
2139 C CE  A LYS   A 102 ? 0.3769 0.4446 0.4086 -0.1020 -0.0217 0.0657  102 LYS   A CE  
2140 C CE  B LYS   A 102 ? 0.3259 0.3035 0.3621 0.0106  -0.0078 -0.0003 102 LYS   A CE  
2141 N NZ  A LYS   A 102 ? 0.3838 0.4442 0.4201 -0.1055 -0.0245 0.0533  102 LYS   A NZ  
2142 N NZ  B LYS   A 102 ? 0.3284 0.3053 0.3709 0.0104  -0.0087 -0.0002 102 LYS   A NZ  
2169 N N   A GLY   A 103 ? 0.3612 0.4834 0.2556 -0.0527 -0.0054 0.0989  103 GLY   A N   
2170 N N   B GLY   A 103 ? 0.3155 0.2908 0.2906 0.0121  -0.0110 0.0115  103 GLY   A N   
2171 C CA  A GLY   A 103 ? 0.3655 0.4919 0.2441 -0.0373 -0.0081 0.0768  103 GLY   A CA  
2172 C CA  B GLY   A 103 ? 0.3198 0.2987 0.2959 0.0120  -0.0128 0.0115  103 GLY   A CA  
2173 C C   A GLY   A 103 ? 0.3634 0.5003 0.2483 -0.0277 0.0029  0.0525  103 GLY   A C   
2174 C C   B GLY   A 103 ? 0.3226 0.3053 0.2977 0.0107  -0.0129 0.0109  103 GLY   A C   
2175 O O   A GLY   A 103 ? 0.3760 0.5125 0.2728 -0.0203 0.0038  0.0352  103 GLY   A O   
2176 O O   B GLY   A 103 ? 0.3244 0.3063 0.3004 0.0133  -0.0143 0.0100  103 GLY   A O   
2183 N N   A GLU   A 104 ? 0.3426 0.4905 0.2006 -0.0335 0.0140  0.0435  104 GLU   A N   
2184 N N   B GLU   A 104 ? 0.3217 0.3084 0.2919 0.0059  -0.0151 0.0150  104 GLU   A N   
2185 C CA  A GLU   A 104 ? 0.3152 0.4761 0.1802 -0.0492 0.0208  0.0377  104 GLU   A CA  
2186 C CA  B GLU   A 104 ? 0.3212 0.3113 0.2879 -0.0009 -0.0162 0.0161  104 GLU   A CA  
2187 C C   A GLU   A 104 ? 0.3081 0.4817 0.1803 -0.0596 0.0250  0.0153  104 GLU   A C   
2188 C C   B GLU   A 104 ? 0.3254 0.3183 0.2954 -0.0003 -0.0135 0.0147  104 GLU   A C   
2189 O O   A GLU   A 104 ? 0.2957 0.4822 0.2059 -0.0669 0.0075  0.0111  104 GLU   A O   
2190 O O   B GLU   A 104 ? 0.3247 0.3144 0.2930 -0.0008 -0.0167 0.0180  104 GLU   A O   
2191 C CB  A GLU   A 104 ? 0.2907 0.4540 0.1596 -0.0558 0.0297  0.0608  104 GLU   A CB  
2192 C CB  B GLU   A 104 ? 0.3174 0.3075 0.2821 -0.0084 -0.0183 0.0176  104 GLU   A CB  
2193 C CG  A GLU   A 104 ? 0.2782 0.4357 0.1777 -0.0544 0.0119  0.0692  104 GLU   A CG  
2194 C CG  B GLU   A 104 ? 0.3148 0.3046 0.2792 -0.0148 -0.0208 0.0182  104 GLU   A CG  
2195 C CD  A GLU   A 104 ? 0.2585 0.4186 0.1785 -0.0557 0.0079  0.0803  104 GLU   A CD  
2196 C CD  B GLU   A 104 ? 0.3125 0.3021 0.2756 -0.0206 -0.0228 0.0191  104 GLU   A CD  
2197 O OE1 A GLU   A 104 ? 0.2377 0.4077 0.1533 -0.0549 0.0040  0.0775  104 GLU   A OE1 
2198 O OE1 B GLU   A 104 ? 0.3127 0.3016 0.2748 -0.0223 -0.0226 0.0197  104 GLU   A OE1 
2199 O OE2 A GLU   A 104 ? 0.2731 0.4144 0.2013 -0.0554 0.0115  0.0909  104 GLU   A OE2 
2200 O OE2 B GLU   A 104 ? 0.3116 0.2998 0.2747 -0.0229 -0.0218 0.0221  104 GLU   A OE2 
2213 N N   A ASP   A 105 ? 0.3157 0.4859 0.1985 -0.0623 0.0349  -0.0131 105 ASP   A N   
2214 N N   B ASP   A 105 ? 0.3316 0.3287 0.3124 -0.0004 -0.0089 0.0095  105 ASP   A N   
2215 C CA  A ASP   A 105 ? 0.3220 0.4894 0.2369 -0.0575 0.0398  -0.0463 105 ASP   A CA  
2216 C CA  B ASP   A 105 ? 0.3373 0.3384 0.3319 0.0012  -0.0024 0.0005  105 ASP   A CA  
2217 C C   A ASP   A 105 ? 0.2880 0.4721 0.2025 -0.0621 0.0321  -0.0642 105 ASP   A C   
2218 C C   B ASP   A 105 ? 0.3378 0.3413 0.3188 -0.0038 -0.0009 -0.0035 105 ASP   A C   
2219 O O   A ASP   A 105 ? 0.2672 0.4676 0.1522 -0.0582 0.0313  -0.0889 105 ASP   A O   
2220 O O   B ASP   A 105 ? 0.3370 0.3413 0.3097 -0.0025 -0.0023 -0.0029 105 ASP   A O   
2221 C CB  A ASP   A 105 ? 0.3555 0.5086 0.3116 -0.0474 0.0459  -0.0635 105 ASP   A CB  
2222 C CB  B ASP   A 105 ? 0.3424 0.3440 0.3652 0.0068  0.0021  -0.0045 105 ASP   A CB  
2223 C CG  A ASP   A 105 ? 0.3839 0.5240 0.3780 -0.0363 0.0446  -0.0854 105 ASP   A CG  
2224 C CG  B ASP   A 105 ? 0.3469 0.3485 0.3963 0.0124  0.0066  -0.0093 105 ASP   A CG  
2225 O OD1 A ASP   A 105 ? 0.3914 0.5298 0.3780 -0.0383 0.0425  -0.1033 105 ASP   A OD1 
2226 O OD1 B ASP   A 105 ? 0.3479 0.3497 0.4051 0.0129  0.0067  -0.0116 105 ASP   A OD1 
2227 O OD2 A ASP   A 105 ? 0.3999 0.5315 0.4276 -0.0325 0.0468  -0.0825 105 ASP   A OD2 
2228 O OD2 B ASP   A 105 ? 0.3493 0.3500 0.4084 0.0153  0.0106  -0.0107 105 ASP   A OD2 
2237 N N   A ILE   A 106 ? 0.2735 0.4578 0.2335 -0.0668 0.0076  -0.0616 106 ILE   A N   
2238 N N   B ILE   A 106 ? 0.3380 0.3440 0.3165 -0.0092 0.0003  -0.0077 106 ILE   A N   
2239 C CA  A ILE   A 106 ? 0.2483 0.4343 0.2490 -0.0776 -0.0151 -0.0756 106 ILE   A CA  
2240 C CA  B ILE   A 106 ? 0.3364 0.3455 0.3156 -0.0163 0.0020  -0.0129 106 ILE   A CA  
2241 C C   A ILE   A 106 ? 0.2327 0.3990 0.2491 -0.0890 -0.0147 -0.0931 106 ILE   A C   
2242 C C   B ILE   A 106 ? 0.3294 0.3404 0.3164 -0.0235 0.0091  -0.0187 106 ILE   A C   
2243 O O   A ILE   A 106 ? 0.2113 0.3819 0.2553 -0.0920 0.0011  -0.0938 106 ILE   A O   
2244 O O   B ILE   A 106 ? 0.3291 0.3403 0.3125 -0.0227 0.0089  -0.0170 106 ILE   A O   
2245 C CB  A ILE   A 106 ? 0.2526 0.4480 0.2970 -0.0665 -0.0335 -0.0456 106 ILE   A CB  
2246 C CB  B ILE   A 106 ? 0.3414 0.3513 0.3214 -0.0157 -0.0035 -0.0094 106 ILE   A CB  
2247 C CG1 A ILE   A 106 ? 0.2433 0.4502 0.3292 -0.0528 -0.0411 -0.0222 106 ILE   A CG1 
2248 C CG1 B ILE   A 106 ? 0.3419 0.3526 0.3260 -0.0141 -0.0057 -0.0060 106 ILE   A CG1 
2249 C CG2 A ILE   A 106 ? 0.2619 0.4545 0.3138 -0.0643 -0.0476 -0.0435 106 ILE   A CG2 
2250 C CG2 B ILE   A 106 ? 0.3441 0.3541 0.3228 -0.0155 -0.0061 -0.0096 106 ILE   A CG2 
2251 C CD1 A ILE   A 106 ? 0.2421 0.4476 0.3510 -0.0394 -0.0287 -0.0077 106 ILE   A CD1 
2252 C CD1 B ILE   A 106 ? 0.3423 0.3520 0.3278 -0.0125 -0.0048 -0.0037 106 ILE   A CD1 
2275 N N   A GLN   A 107 ? 0.2564 0.3800 0.2678 -0.0844 -0.0042 -0.1092 107 GLN   A N   
2276 N N   B GLN   A 107 ? 0.3220 0.3335 0.3260 -0.0308 0.0175  -0.0274 107 GLN   A N   
2277 C CA  A GLN   A 107 ? 0.2840 0.3624 0.3598 -0.0688 0.0203  -0.1080 107 GLN   A CA  
2278 C CA  B GLN   A 107 ? 0.3129 0.3261 0.3456 -0.0375 0.0255  -0.0387 107 GLN   A CA  
2279 C C   A GLN   A 107 ? 0.2587 0.3040 0.3452 -0.0616 0.0414  -0.0827 107 GLN   A C   
2280 C C   B GLN   A 107 ? 0.2732 0.2946 0.3057 -0.0479 0.0359  -0.0519 107 GLN   A C   
2281 O O   A GLN   A 107 ? 0.2638 0.2886 0.4107 -0.0516 0.0516  -0.0859 107 GLN   A O   
2282 O O   B GLN   A 107 ? 0.2759 0.2947 0.3167 -0.0481 0.0364  -0.0505 107 GLN   A O   
2283 C CB  A GLN   A 107 ? 0.3285 0.3997 0.4627 -0.0725 0.0092  -0.1155 107 GLN   A CB  
2284 C CB  B GLN   A 107 ? 0.3405 0.3487 0.4053 -0.0356 0.0214  -0.0347 107 GLN   A CB  
2285 C CG  A GLN   A 107 ? 0.3771 0.4404 0.5743 -0.0695 0.0029  -0.1067 107 GLN   A CG  
2286 C CG  B GLN   A 107 ? 0.3645 0.3682 0.4635 -0.0335 0.0177  -0.0305 107 GLN   A CG  
2287 C CD  A GLN   A 107 ? 0.4139 0.4680 0.6685 -0.0676 0.0027  -0.0944 107 GLN   A CD  
2288 C CD  B GLN   A 107 ? 0.3838 0.3837 0.5127 -0.0312 0.0156  -0.0262 107 GLN   A CD  
2289 O OE1 A GLN   A 107 ? 0.4287 0.4757 0.7074 -0.0687 0.0043  -0.0892 107 GLN   A OE1 
2290 O OE1 B GLN   A 107 ? 0.3908 0.3886 0.5310 -0.0307 0.0159  -0.0249 107 GLN   A OE1 
2291 N NE2 A GLN   A 107 ? 0.4233 0.4788 0.6995 -0.0682 -0.0006 -0.0951 107 GLN   A NE2 
2292 N NE2 B GLN   A 107 ? 0.3899 0.3896 0.5288 -0.0309 0.0144  -0.0258 107 GLN   A NE2 
2309 N N   . LEU   A 108 ? 0.2298 0.2617 0.2650 -0.0587 0.0414  -0.0700 108 LEU   A N   
2310 C CA  . LEU   A 108 ? 0.2009 0.2086 0.2216 -0.0281 0.0316  -0.0255 108 LEU   A CA  
2311 C C   . LEU   A 108 ? 0.1744 0.1736 0.2090 -0.0115 0.0218  0.0039  108 LEU   A C   
2312 O O   . LEU   A 108 ? 0.1728 0.1722 0.2290 -0.0013 0.0274  0.0076  108 LEU   A O   
2313 C CB  . LEU   A 108 ? 0.2099 0.2164 0.1932 -0.0295 0.0340  -0.0216 108 LEU   A CB  
2314 C CG  . LEU   A 108 ? 0.2315 0.2359 0.2301 -0.0241 0.0369  -0.0309 108 LEU   A CG  
2315 C CD1 . LEU   A 108 ? 0.2535 0.2417 0.2406 -0.0320 0.0525  -0.0288 108 LEU   A CD1 
2316 C CD2 . LEU   A 108 ? 0.2319 0.2652 0.2798 -0.0144 0.0348  -0.0168 108 LEU   A CD2 
2329 N N   . LEU   A 109 ? 0.1611 0.1716 0.2101 0.0008  0.0219  0.0143  109 LEU   A N   
2330 C CA  . LEU   A 109 ? 0.1615 0.1685 0.1861 0.0055  0.0053  0.0170  109 LEU   A CA  
2331 C C   . LEU   A 109 ? 0.1519 0.1602 0.1773 -0.0069 0.0014  -0.0059 109 LEU   A C   
2332 O O   . LEU   A 109 ? 0.1591 0.1422 0.2013 -0.0050 0.0055  -0.0007 109 LEU   A O   
2333 C CB  . LEU   A 109 ? 0.1686 0.1687 0.2043 0.0096  -0.0082 0.0271  109 LEU   A CB  
2334 C CG  . LEU   A 109 ? 0.1673 0.1773 0.2091 0.0057  -0.0039 0.0355  109 LEU   A CG  
2335 C CD1 . LEU   A 109 ? 0.1616 0.1672 0.2211 -0.0045 0.0068  0.0045  109 LEU   A CD1 
2336 C CD2 . LEU   A 109 ? 0.1637 0.1926 0.2351 0.0039  -0.0076 0.0349  109 LEU   A CD2 
2348 N N   . LYS   A 110 ? 0.1496 0.1578 0.1828 -0.0059 -0.0092 0.0048  110 LYS   A N   
2349 C CA  . LYS   A 110 ? 0.1540 0.1506 0.1902 -0.0075 -0.0131 0.0047  110 LYS   A CA  
2350 C C   . LYS   A 110 ? 0.1593 0.1423 0.1661 -0.0130 -0.0031 0.0020  110 LYS   A C   
2351 O O   . LYS   A 110 ? 0.1429 0.1416 0.1833 -0.0123 0.0059  -0.0061 110 LYS   A O   
2352 C CB  . LYS   A 110 ? 0.1644 0.1602 0.2075 -0.0053 -0.0201 -0.0079 110 LYS   A CB  
2353 C CG  . LYS   A 110 ? 0.1667 0.1537 0.2065 -0.0064 -0.0110 -0.0124 110 LYS   A CG  
2354 C CD  . LYS   A 110 ? 0.1758 0.1645 0.2216 -0.0146 -0.0041 -0.0058 110 LYS   A CD  
2355 C CE  . LYS   A 110 ? 0.1929 0.1755 0.2371 -0.0153 0.0155  -0.0034 110 LYS   A CE  
2356 N NZ  . LYS   A 110 ? 0.1887 0.1700 0.2483 -0.0235 0.0222  -0.0041 110 LYS   A NZ  
2370 N N   . SER   A 111 ? 0.1608 0.1446 0.1774 -0.0076 -0.0107 0.0058  111 SER   A N   
2371 C CA  . SER   A 111 ? 0.1547 0.1539 0.1754 -0.0029 0.0000  -0.0009 111 SER   A CA  
2372 C C   . SER   A 111 ? 0.1404 0.1463 0.1628 -0.0044 0.0083  0.0048  111 SER   A C   
2373 O O   . SER   A 111 ? 0.1490 0.1390 0.1953 -0.0007 0.0064  0.0081  111 SER   A O   
2374 C CB  . SER   A 111 ? 0.1651 0.1689 0.1957 -0.0012 0.0175  -0.0115 111 SER   A CB  
2375 O OG  . SER   A 111 ? 0.2172 0.1881 0.2132 0.0026  0.0269  -0.0166 111 SER   A OG  
2381 N N   . ALA   A 112 ? 0.1380 0.1375 0.1867 0.0037  0.0110  0.0061  112 ALA   A N   
2382 C CA  . ALA   A 112 ? 0.1457 0.1330 0.1571 -0.0041 0.0230  -0.0012 112 ALA   A CA  
2383 C C   . ALA   A 112 ? 0.1427 0.1237 0.1755 -0.0007 0.0126  -0.0055 112 ALA   A C   
2384 O O   . ALA   A 112 ? 0.1512 0.1304 0.1825 -0.0108 0.0141  0.0018  112 ALA   A O   
2385 C CB  . ALA   A 112 ? 0.1579 0.1355 0.1759 -0.0055 0.0110  0.0095  112 ALA   A CB  
2391 N N   . TYR   A 113 ? 0.1365 0.1300 0.2014 -0.0067 0.0117  0.0142  113 TYR   A N   
2392 C CA  . TYR   A 113 ? 0.1331 0.1281 0.1778 -0.0058 0.0136  0.0104  113 TYR   A CA  
2393 C C   . TYR   A 113 ? 0.1317 0.1279 0.1672 -0.0134 0.0007  0.0013  113 TYR   A C   
2394 O O   . TYR   A 113 ? 0.1382 0.1375 0.1812 -0.0051 0.0147  0.0009  113 TYR   A O   
2395 C CB  . TYR   A 113 ? 0.1400 0.1442 0.1829 -0.0031 0.0008  0.0186  113 TYR   A CB  
2396 C CG  . TYR   A 113 ? 0.1362 0.1413 0.1777 -0.0098 0.0077  0.0204  113 TYR   A CG  
2397 C CD1 . TYR   A 113 ? 0.1334 0.1545 0.1784 -0.0029 0.0082  0.0249  113 TYR   A CD1 
2398 C CD2 . TYR   A 113 ? 0.1481 0.1491 0.1747 -0.0116 -0.0002 0.0183  113 TYR   A CD2 
2399 C CE1 . TYR   A 113 ? 0.1411 0.1626 0.1711 -0.0078 0.0108  0.0309  113 TYR   A CE1 
2400 C CE2 . TYR   A 113 ? 0.1420 0.1561 0.1716 -0.0110 -0.0026 0.0222  113 TYR   A CE2 
2401 C CZ  . TYR   A 113 ? 0.1365 0.1572 0.1691 0.0057  0.0167  0.0275  113 TYR   A CZ  
2402 O OH  . TYR   A 113 ? 0.1463 0.1694 0.1964 0.0151  0.0128  0.0321  113 TYR   A OH  
2412 N N   . GLU   A 114 ? 0.1354 0.1305 0.1812 -0.0025 0.0121  0.0081  114 GLU   A N   
2413 C CA  . GLU   A 114 ? 0.1377 0.1197 0.1899 0.0031  0.0093  0.0119  114 GLU   A CA  
2414 C C   . GLU   A 114 ? 0.1271 0.1288 0.1830 0.0037  0.0133  0.0047  114 GLU   A C   
2415 O O   . GLU   A 114 ? 0.1444 0.1374 0.1830 0.0023  0.0050  0.0096  114 GLU   A O   
2416 C CB  . GLU   A 114 ? 0.1383 0.1294 0.1915 -0.0033 0.0113  0.0123  114 GLU   A CB  
2417 C CG  . GLU   A 114 ? 0.1398 0.1386 0.2032 0.0006  0.0103  -0.0040 114 GLU   A CG  
2418 C CD  . GLU   A 114 ? 0.1554 0.1415 0.2078 -0.0103 0.0016  0.0013  114 GLU   A CD  
2419 O OE1 . GLU   A 114 ? 0.1618 0.1345 0.2185 -0.0066 0.0121  -0.0035 114 GLU   A OE1 
2420 O OE2 . GLU   A 114 ? 0.1705 0.1511 0.2225 -0.0138 0.0099  -0.0169 114 GLU   A OE2 
2427 N N   . ASN   A 115 ? 0.1311 0.1347 0.1718 -0.0051 0.0095  0.0011  115 ASN   A N   
2428 C CA  . ASN   A 115 ? 0.1410 0.1389 0.1698 -0.0106 0.0111  0.0091  115 ASN   A CA  
2429 C C   . ASN   A 115 ? 0.1416 0.1434 0.1565 -0.0130 0.0048  0.0020  115 ASN   A C   
2430 O O   . ASN   A 115 ? 0.1427 0.1525 0.1708 -0.0106 0.0172  0.0092  115 ASN   A O   
2431 C CB  . ASN   A 115 ? 0.1451 0.1454 0.1625 -0.0108 0.0043  0.0126  115 ASN   A CB  
2432 C CG  . ASN   A 115 ? 0.1459 0.1656 0.1823 -0.0144 0.0147  0.0104  115 ASN   A CG  
2433 O OD1 . ASN   A 115 ? 0.1529 0.2636 0.2042 -0.0153 0.0226  0.0227  115 ASN   A OD1 
2434 N ND2 . ASN   A 115 ? 0.1398 0.1552 0.1846 -0.0112 0.0281  0.0098  115 ASN   A ND2 
2441 N N   . PHE   A 116 ? 0.1303 0.1481 0.1770 0.0026  0.0150  0.0118  116 PHE   A N   
2442 C CA  . PHE   A 116 ? 0.1318 0.1530 0.1648 0.0090  0.0142  0.0140  116 PHE   A CA  
2443 C C   . PHE   A 116 ? 0.1315 0.1609 0.1673 -0.0019 0.0242  0.0127  116 PHE   A C   
2444 O O   . PHE   A 116 ? 0.1398 0.1591 0.1762 0.0089  0.0190  0.0189  116 PHE   A O   
2445 C CB  . PHE   A 116 ? 0.1285 0.1450 0.1862 0.0003  0.0187  0.0147  116 PHE   A CB  
2446 C CG  . PHE   A 116 ? 0.1285 0.1438 0.1781 -0.0048 0.0161  0.0063  116 PHE   A CG  
2447 C CD1 . PHE   A 116 ? 0.1337 0.1450 0.1785 -0.0087 0.0172  0.0134  116 PHE   A CD1 
2448 C CD2 . PHE   A 116 ? 0.1405 0.1520 0.1831 -0.0002 0.0144  0.0071  116 PHE   A CD2 
2449 C CE1 . PHE   A 116 ? 0.1369 0.1438 0.1877 -0.0119 0.0087  0.0024  116 PHE   A CE1 
2450 C CE2 . PHE   A 116 ? 0.1338 0.1517 0.1896 -0.0064 0.0187  0.0039  116 PHE   A CE2 
2451 C CZ  . PHE   A 116 ? 0.1370 0.1407 0.1837 -0.0056 0.0063  0.0066  116 PHE   A CZ  
2461 N N   . ASN   A 117 ? 0.1379 0.1520 0.1724 0.0018  0.0156  0.0253  117 ASN   A N   
2462 C CA  . ASN   A 117 ? 0.1442 0.1536 0.1781 0.0048  0.0081  0.0227  117 ASN   A CA  
2463 C C   . ASN   A 117 ? 0.1356 0.1552 0.1992 0.0019  0.0100  0.0249  117 ASN   A C   
2464 O O   . ASN   A 117 ? 0.1525 0.1601 0.2237 -0.0058 -0.0067 0.0377  117 ASN   A O   
2465 C CB  . ASN   A 117 ? 0.1481 0.1562 0.1829 -0.0014 0.0064  0.0266  117 ASN   A CB  
2466 C CG  . ASN   A 117 ? 0.1415 0.1524 0.1891 -0.0054 0.0047  0.0260  117 ASN   A CG  
2467 O OD1 . ASN   A 117 ? 0.1539 0.1707 0.1918 -0.0117 0.0150  0.0214  117 ASN   A OD1 
2468 N ND2 . ASN   A 117 ? 0.1310 0.1461 0.2035 -0.0051 0.0036  0.0284  117 ASN   A ND2 
2475 N N   . GLN   A 118 ? 0.1352 0.1515 0.2076 -0.0066 -0.0024 0.0284  118 GLN   A N   
2476 C CA  . GLN   A 118 ? 0.1470 0.1587 0.2004 -0.0057 -0.0114 0.0235  118 GLN   A CA  
2477 C C   . GLN   A 118 ? 0.1469 0.1633 0.1912 -0.0069 -0.0049 0.0282  118 GLN   A C   
2478 O O   . GLN   A 118 ? 0.1522 0.1980 0.2258 0.0040  -0.0080 0.0093  118 GLN   A O   
2479 C CB  . GLN   A 118 ? 0.1461 0.1579 0.2044 -0.0050 0.0054  0.0227  118 GLN   A CB  
2480 C CG  . GLN   A 118 ? 0.1391 0.1700 0.2124 0.0025  0.0061  0.0253  118 GLN   A CG  
2481 C CD  . GLN   A 118 ? 0.1460 0.1786 0.2133 0.0010  0.0060  0.0157  118 GLN   A CD  
2482 O OE1 . GLN   A 118 ? 0.1512 0.1855 0.2286 0.0126  -0.0005 0.0088  118 GLN   A OE1 
2483 N NE2 . GLN   A 118 ? 0.1493 0.1731 0.2149 0.0048  0.0018  0.0227  118 GLN   A NE2 
2492 N N   . HIS   A 119 ? 0.1513 0.1595 0.1868 0.0001  0.0078  0.0287  119 HIS   A N   
2493 C CA  . HIS   A 119 ? 0.1580 0.1710 0.1860 0.0012  0.0074  0.0346  119 HIS   A CA  
2494 C C   . HIS   A 119 ? 0.1784 0.1753 0.1771 -0.0110 0.0090  0.0347  119 HIS   A C   
2495 O O   . HIS   A 119 ? 0.1804 0.1819 0.1970 -0.0340 -0.0024 0.0284  119 HIS   A O   
2496 C CB  . HIS   A 119 ? 0.1603 0.1740 0.2016 -0.0001 0.0224  0.0333  119 HIS   A CB  
2497 C CG  . HIS   A 119 ? 0.1641 0.1700 0.2517 0.0005  0.0159  0.0392  119 HIS   A CG  
2498 N ND1 . HIS   A 119 ? 0.1709 0.1939 0.3085 -0.0161 0.0045  0.0346  119 HIS   A ND1 
2499 C CD2 . HIS   A 119 ? 0.1808 0.1769 0.2745 0.0100  0.0248  0.0575  119 HIS   A CD2 
2500 C CE1 . HIS   A 119 ? 0.1705 0.1965 0.3254 -0.0180 0.0198  0.0498  119 HIS   A CE1 
2501 N NE2 . HIS   A 119 ? 0.1830 0.1891 0.3164 -0.0029 0.0441  0.0602  119 HIS   A NE2 
2509 N N   . GLU   A 120 ? 0.1868 0.1929 0.1878 -0.0007 0.0050  0.0477  120 GLU   A N   
2510 C CA  . GLU   A 120 ? 0.2086 0.2211 0.2106 0.0068  0.0072  0.0777  120 GLU   A CA  
2511 C C   . GLU   A 120 ? 0.1916 0.2024 0.1936 -0.0113 0.0051  0.0712  120 GLU   A C   
2512 O O   . GLU   A 120 ? 0.1916 0.1907 0.2025 -0.0118 -0.0002 0.0621  120 GLU   A O   
2513 C CB  . GLU   A 120 ? 0.2683 0.2853 0.2696 0.0287  0.0044  0.1335  120 GLU   A CB  
2514 C CG  . GLU   A 120 ? 0.3593 0.3639 0.3894 0.0410  0.0021  0.1327  120 GLU   A CG  
2515 C CD  . GLU   A 120 ? 0.4384 0.4262 0.5099 0.0495  0.0088  0.1240  120 GLU   A CD  
2516 O OE1 . GLU   A 120 ? 0.4640 0.4471 0.5326 0.0509  0.0095  0.1190  120 GLU   A OE1 
2517 O OE2 . GLU   A 120 ? 0.4756 0.4756 0.5710 0.0508  0.0123  0.1199  120 GLU   A OE2 
2524 N N   . VAL   A 121 ? 0.1780 0.2061 0.1802 -0.0075 0.0135  0.0512  121 VAL   A N   
2525 C CA  . VAL   A 121 ? 0.1839 0.2157 0.1663 -0.0107 0.0275  0.0518  121 VAL   A CA  
2526 C C   . VAL   A 121 ? 0.1739 0.1905 0.1561 -0.0205 0.0142  0.0428  121 VAL   A C   
2527 O O   . VAL   A 121 ? 0.1784 0.1985 0.1767 -0.0291 0.0002  0.0329  121 VAL   A O   
2528 C CB  . VAL   A 121 ? 0.2234 0.2562 0.2040 0.0010  0.0421  0.0659  121 VAL   A CB  
2529 C CG1 . VAL   A 121 ? 0.2292 0.2738 0.2061 0.0125  0.0420  0.0640  121 VAL   A CG1 
2530 C CG2 . VAL   A 121 ? 0.2429 0.2780 0.2488 -0.0113 0.0328  0.0508  121 VAL   A CG2 
2540 N N   . LEU   A 122 ? 0.1659 0.1795 0.1689 -0.0181 0.0172  0.0382  122 LEU   A N   
2541 C CA  . LEU   A 122 ? 0.1702 0.1661 0.1704 -0.0216 0.0336  0.0387  122 LEU   A CA  
2542 C C   . LEU   A 122 ? 0.1665 0.1580 0.1720 -0.0282 0.0147  0.0328  122 LEU   A C   
2543 O O   . LEU   A 122 ? 0.1661 0.1695 0.2046 -0.0285 0.0149  0.0291  122 LEU   A O   
2544 C CB  . LEU   A 122 ? 0.1895 0.1694 0.2023 -0.0162 0.0172  0.0539  122 LEU   A CB  
2545 C CG  . LEU   A 122 ? 0.1895 0.1737 0.1998 -0.0132 0.0271  0.0283  122 LEU   A CG  
2546 C CD1 . LEU   A 122 ? 0.2030 0.1843 0.2178 -0.0155 0.0224  0.0347  122 LEU   A CD1 
2547 C CD2 . LEU   A 122 ? 0.1778 0.1661 0.1913 -0.0136 0.0340  0.0194  122 LEU   A CD2 
2559 N N   A LEU   A 123 ? 0.1636 0.1548 0.1623 -0.0253 0.0121  0.0319  123 LEU   A N   
2560 N N   B LEU   A 123 ? 0.1675 0.1565 0.1610 -0.0270 0.0021  0.0197  123 LEU   A N   
2561 C CA  A LEU   A 123 ? 0.1630 0.1612 0.1551 -0.0199 0.0295  0.0293  123 LEU   A CA  
2562 C CA  B LEU   A 123 ? 0.1684 0.1567 0.1585 -0.0257 -0.0063 0.0070  123 LEU   A CA  
2563 C C   A LEU   A 123 ? 0.1629 0.1502 0.1524 -0.0154 0.0201  0.0294  123 LEU   A C   
2564 C C   B LEU   A 123 ? 0.1687 0.1513 0.1518 -0.0248 -0.0104 0.0007  123 LEU   A C   
2565 O O   A LEU   A 123 ? 0.1519 0.1529 0.1669 -0.0172 0.0163  0.0245  123 LEU   A O   
2566 O O   B LEU   A 123 ? 0.1671 0.1495 0.1514 -0.0215 -0.0102 -0.0047 123 LEU   A O   
2567 C CB  A LEU   A 123 ? 0.1684 0.1757 0.1536 -0.0156 0.0347  0.0197  123 LEU   A CB  
2568 C CB  B LEU   A 123 ? 0.1688 0.1612 0.1645 -0.0251 -0.0138 0.0034  123 LEU   A CB  
2569 C CG  A LEU   A 123 ? 0.1775 0.1857 0.1604 -0.0122 0.0290  0.0142  123 LEU   A CG  
2570 C CG  B LEU   A 123 ? 0.1703 0.1653 0.1720 -0.0256 -0.0148 0.0030  123 LEU   A CG  
2571 C CD1 A LEU   A 123 ? 0.1879 0.1875 0.1801 -0.0001 0.0195  0.0092  123 LEU   A CD1 
2572 C CD1 B LEU   A 123 ? 0.1725 0.1669 0.1795 -0.0236 -0.0147 0.0004  123 LEU   A CD1 
2573 C CD2 A LEU   A 123 ? 0.1964 0.1966 0.1717 -0.0086 0.0211  0.0113  123 LEU   A CD2 
2574 C CD2 B LEU   A 123 ? 0.1734 0.1684 0.1776 -0.0240 -0.0173 0.0016  123 LEU   A CD2 
2597 N N   A ALA   A 124 ? 0.1489 0.1406 0.1464 -0.0123 0.0157  0.0215  124 ALA   A N   
2598 N N   B ALA   A 124 ? 0.1683 0.1481 0.1478 -0.0260 -0.0125 -0.0034 124 ALA   A N   
2599 C CA  A ALA   A 124 ? 0.1339 0.1448 0.1590 -0.0090 0.0068  0.0324  124 ALA   A CA  
2600 C CA  B ALA   A 124 ? 0.1708 0.1536 0.1438 -0.0280 -0.0124 -0.0027 124 ALA   A CA  
2601 C C   A ALA   A 124 ? 0.1397 0.1426 0.1637 -0.0109 0.0260  0.0304  124 ALA   A C   
2602 C C   B ALA   A 124 ? 0.1727 0.1550 0.1353 -0.0223 -0.0174 -0.0048 124 ALA   A C   
2603 O O   A ALA   A 124 ? 0.1425 0.1545 0.1830 -0.0109 0.0259  0.0426  124 ALA   A O   
2604 O O   B ALA   A 124 ? 0.1753 0.1572 0.1285 -0.0176 -0.0223 -0.0089 124 ALA   A O   
2605 C CB  A ALA   A 124 ? 0.1360 0.1462 0.1841 -0.0065 0.0078  0.0267  124 ALA   A CB  
2606 C CB  B ALA   A 124 ? 0.1749 0.1526 0.1462 -0.0363 -0.0071 0.0018  124 ALA   A CB  
2617 N N   A PRO   A 125 ? 0.1402 0.1407 0.1630 -0.0104 0.0162  0.0361  125 PRO   A N   
2618 N N   B PRO   A 125 ? 0.1699 0.1539 0.1295 -0.0193 -0.0247 -0.0018 125 PRO   A N   
2619 C CA  A PRO   A 125 ? 0.1527 0.1523 0.1601 -0.0080 0.0092  0.0298  125 PRO   A CA  
2620 C CA  B PRO   A 125 ? 0.1721 0.1544 0.1303 -0.0207 -0.0272 -0.0040 125 PRO   A CA  
2621 C C   A PRO   A 125 ? 0.1497 0.1596 0.1554 -0.0028 0.0172  0.0277  125 PRO   A C   
2622 C C   B PRO   A 125 ? 0.1732 0.1550 0.1402 -0.0227 -0.0248 -0.0061 125 PRO   A C   
2623 O O   A PRO   A 125 ? 0.1514 0.1507 0.1862 0.0004  0.0175  0.0250  125 PRO   A O   
2624 O O   B PRO   A 125 ? 0.1689 0.1520 0.1491 -0.0291 -0.0282 -0.0026 125 PRO   A O   
2625 C CB  A PRO   A 125 ? 0.1638 0.1512 0.1604 -0.0148 0.0181  0.0291  125 PRO   A CB  
2626 C CB  B PRO   A 125 ? 0.1732 0.1552 0.1300 -0.0209 -0.0260 -0.0035 125 PRO   A CB  
2627 C CG  A PRO   A 125 ? 0.1608 0.1373 0.1673 -0.0146 0.0193  0.0282  125 PRO   A CG  
2628 C CG  B PRO   A 125 ? 0.1726 0.1567 0.1336 -0.0201 -0.0236 -0.0002 125 PRO   A CG  
2629 C CD  A PRO   A 125 ? 0.1479 0.1444 0.1718 -0.0217 0.0181  0.0259  125 PRO   A CD  
2630 C CD  B PRO   A 125 ? 0.1707 0.1565 0.1346 -0.0196 -0.0196 -0.0009 125 PRO   A CD  
2645 N N   A LEU   A 126 ? 0.1486 0.1661 0.1578 -0.0036 0.0023  0.0278  126 LEU   A N   
2646 N N   B LEU   A 126 ? 0.1816 0.1577 0.1504 -0.0176 -0.0232 -0.0068 126 LEU   A N   
2647 C CA  A LEU   A 126 ? 0.1475 0.1565 0.1765 -0.0120 0.0010  0.0354  126 LEU   A CA  
2648 C CA  B LEU   A 126 ? 0.1880 0.1564 0.1652 -0.0123 -0.0156 -0.0011 126 LEU   A CA  
2649 C C   A LEU   A 126 ? 0.1505 0.1450 0.1828 -0.0017 0.0046  0.0228  126 LEU   A C   
2650 C C   B LEU   A 126 ? 0.1827 0.1548 0.1685 -0.0068 -0.0088 0.0012  126 LEU   A C   
2651 O O   A LEU   A 126 ? 0.1565 0.1427 0.1885 -0.0041 0.0181  0.0213  126 LEU   A O   
2652 O O   B LEU   A 126 ? 0.1837 0.1528 0.1823 -0.0073 0.0038  0.0006  126 LEU   A O   
2653 C CB  A LEU   A 126 ? 0.1540 0.1661 0.1809 -0.0196 -0.0075 0.0239  126 LEU   A CB  
2654 C CB  B LEU   A 126 ? 0.2003 0.1642 0.1918 -0.0144 -0.0149 0.0064  126 LEU   A CB  
2655 C CG  A LEU   A 126 ? 0.1539 0.1987 0.1991 -0.0143 0.0079  0.0308  126 LEU   A CG  
2656 C CG  B LEU   A 126 ? 0.2085 0.1706 0.2093 -0.0119 -0.0231 0.0064  126 LEU   A CG  
2657 C CD1 A LEU   A 126 ? 0.1533 0.2183 0.2287 -0.0171 0.0066  0.0267  126 LEU   A CD1 
2658 C CD1 B LEU   A 126 ? 0.2124 0.1712 0.2166 -0.0098 -0.0215 0.0063  126 LEU   A CD1 
2659 C CD2 A LEU   A 126 ? 0.1698 0.1884 0.2106 -0.0253 0.0106  0.0490  126 LEU   A CD2 
2660 C CD2 B LEU   A 126 ? 0.2092 0.1735 0.2101 -0.0139 -0.0260 0.0070  126 LEU   A CD2 
2683 N N   A LEU   A 127 ? 0.1442 0.1486 0.1790 0.0068  0.0014  0.0289  127 LEU   A N   
2684 N N   B LEU   A 127 ? 0.1751 0.1543 0.1613 -0.0024 -0.0115 0.0094  127 LEU   A N   
2685 C CA  A LEU   A 127 ? 0.1387 0.1669 0.1661 -0.0010 -0.0056 0.0271  127 LEU   A CA  
2686 C CA  B LEU   A 127 ? 0.1675 0.1547 0.1522 0.0002  -0.0162 0.0128  127 LEU   A CA  
2687 C C   A LEU   A 127 ? 0.1297 0.1534 0.1692 -0.0010 0.0070  0.0192  127 LEU   A C   
2688 C C   B LEU   A 127 ? 0.1650 0.1530 0.1525 -0.0061 -0.0202 0.0072  127 LEU   A C   
2689 O O   A LEU   A 127 ? 0.1482 0.1515 0.1745 -0.0115 0.0011  0.0317  127 LEU   A O   
2690 O O   B LEU   A 127 ? 0.1676 0.1545 0.1455 -0.0126 -0.0193 -0.0029 127 LEU   A O   
2691 C CB  A LEU   A 127 ? 0.1515 0.1859 0.1790 0.0147  0.0028  0.0217  127 LEU   A CB  
2692 C CB  B LEU   A 127 ? 0.1649 0.1575 0.1474 0.0097  -0.0125 0.0174  127 LEU   A CB  
2693 C CG  A LEU   A 127 ? 0.1540 0.1845 0.1732 0.0184  -0.0010 0.0373  127 LEU   A CG  
2694 C CG  B LEU   A 127 ? 0.1540 0.1573 0.1312 0.0211  -0.0099 0.0268  127 LEU   A CG  
2695 C CD1 A LEU   A 127 ? 0.1647 0.1767 0.1969 0.0109  -0.0042 0.0385  127 LEU   A CD1 
2696 C CD1 B LEU   A 127 ? 0.1539 0.1561 0.1369 0.0252  -0.0055 0.0289  127 LEU   A CD1 
2697 C CD2 A LEU   A 127 ? 0.1633 0.1864 0.1859 0.0249  -0.0122 0.0361  127 LEU   A CD2 
2698 C CD2 B LEU   A 127 ? 0.1524 0.1602 0.1185 0.0256  -0.0131 0.0246  127 LEU   A CD2 
2721 N N   A SER   A 128 ? 0.1431 0.1495 0.1602 -0.0084 0.0046  0.0183  128 SER   A N   
2722 N N   B SER   A 128 ? 0.1664 0.1505 0.1570 -0.0100 -0.0202 0.0086  128 SER   A N   
2723 C CA  A SER   A 128 ? 0.1522 0.1497 0.1466 -0.0007 0.0018  0.0245  128 SER   A CA  
2724 C CA  B SER   A 128 ? 0.1686 0.1504 0.1544 -0.0092 -0.0201 0.0074  128 SER   A CA  
2725 C C   A SER   A 128 ? 0.1627 0.1522 0.1465 0.0111  -0.0062 0.0247  128 SER   A C   
2726 C C   B SER   A 128 ? 0.1666 0.1553 0.1583 -0.0045 -0.0242 0.0135  128 SER   A C   
2727 O O   A SER   A 128 ? 0.1718 0.1701 0.1665 0.0095  -0.0181 0.0139  128 SER   A O   
2728 O O   B SER   A 128 ? 0.1619 0.1536 0.1637 -0.0052 -0.0247 0.0083  128 SER   A O   
2729 C CB  A SER   A 128 ? 0.1558 0.1576 0.1495 -0.0065 0.0048  0.0177  128 SER   A CB  
2730 C CB  B SER   A 128 ? 0.1739 0.1484 0.1513 -0.0117 -0.0168 0.0071  128 SER   A CB  
2731 O OG  A SER   A 128 ? 0.1597 0.1653 0.1491 -0.0099 0.0074  0.0118  128 SER   A OG  
2732 O OG  B SER   A 128 ? 0.1785 0.1476 0.1490 -0.0139 -0.0100 0.0111  128 SER   A OG  
2743 N N   A ALA   A 129 ? 0.1529 0.1609 0.1783 0.0020  -0.0078 0.0322  129 ALA   A N   
2744 N N   B ALA   A 129 ? 0.1693 0.1677 0.1600 0.0027  -0.0278 0.0232  129 ALA   A N   
2745 C CA  A ALA   A 129 ? 0.1523 0.1543 0.1958 -0.0037 0.0029  0.0382  129 ALA   A CA  
2746 C CA  B ALA   A 129 ? 0.1759 0.1778 0.1633 0.0111  -0.0281 0.0301  129 ALA   A CA  
2747 C C   A ALA   A 129 ? 0.1608 0.1481 0.1822 -0.0088 0.0062  0.0221  129 ALA   A C   
2748 C C   B ALA   A 129 ? 0.1769 0.1838 0.1681 0.0177  -0.0246 0.0325  129 ALA   A C   
2749 O O   A ALA   A 129 ? 0.1676 0.1568 0.1644 -0.0135 0.0078  0.0214  129 ALA   A O   
2750 O O   B ALA   A 129 ? 0.1722 0.1852 0.1600 0.0240  -0.0217 0.0332  129 ALA   A O   
2751 C CB  A ALA   A 129 ? 0.1689 0.1715 0.2194 0.0081  -0.0057 0.0443  129 ALA   A CB  
2752 C CB  B ALA   A 129 ? 0.1815 0.1863 0.1655 0.0109  -0.0290 0.0276  129 ALA   A CB  
2763 N N   A GLY   A 130 ? 0.1674 0.1533 0.2206 -0.0086 0.0166  0.0134  130 GLY   A N   
2764 N N   B GLY   A 130 ? 0.1825 0.1907 0.1775 0.0191  -0.0234 0.0332  130 GLY   A N   
2765 C CA  A GLY   A 130 ? 0.1868 0.1543 0.2273 -0.0017 0.0139  0.0130  130 GLY   A CA  
2766 C CA  B GLY   A 130 ? 0.1897 0.1981 0.1874 0.0187  -0.0190 0.0270  130 GLY   A CA  
2767 C C   A GLY   A 130 ? 0.1882 0.1508 0.1986 0.0036  0.0061  0.0109  130 GLY   A C   
2768 C C   B GLY   A 130 ? 0.1973 0.2049 0.1965 0.0157  -0.0211 0.0219  130 GLY   A C   
2769 O O   A GLY   A 130 ? 0.1904 0.1470 0.2005 -0.0017 -0.0111 0.0057  130 GLY   A O   
2770 O O   B GLY   A 130 ? 0.2039 0.2078 0.2049 0.0135  -0.0237 0.0261  130 GLY   A O   
2777 N N   A ILE   A 131 ? 0.1954 0.1492 0.1794 -0.0013 0.0015  0.0174  131 ILE   A N   
2778 N N   B ILE   A 131 ? 0.1985 0.2098 0.2003 0.0144  -0.0165 0.0167  131 ILE   A N   
2779 C CA  A ILE   A 131 ? 0.2064 0.1513 0.1552 -0.0132 -0.0170 0.0201  131 ILE   A CA  
2780 C CA  B ILE   A 131 ? 0.2000 0.2143 0.2008 0.0141  -0.0129 0.0152  131 ILE   A CA  
2781 C C   A ILE   A 131 ? 0.1975 0.1504 0.1397 -0.0182 -0.0143 0.0182  131 ILE   A C   
2782 C C   B ILE   A 131 ? 0.2007 0.2119 0.1889 0.0120  -0.0141 0.0239  131 ILE   A C   
2783 O O   A ILE   A 131 ? 0.2053 0.1555 0.1658 -0.0109 -0.0183 0.0214  131 ILE   A O   
2784 O O   B ILE   A 131 ? 0.1991 0.2143 0.1814 0.0129  -0.0145 0.0270  131 ILE   A O   
2785 C CB  A ILE   A 131 ? 0.2293 0.1668 0.1661 -0.0210 -0.0245 0.0050  131 ILE   A CB  
2786 C CB  B ILE   A 131 ? 0.2028 0.2206 0.2193 0.0150  -0.0084 0.0048  131 ILE   A CB  
2787 C CG1 A ILE   A 131 ? 0.2471 0.2021 0.1768 -0.0360 -0.0353 -0.0012 131 ILE   A CG1 
2788 C CG1 B ILE   A 131 ? 0.2078 0.2265 0.2348 0.0140  -0.0132 -0.0034 131 ILE   A CG1 
2789 C CG2 A ILE   A 131 ? 0.2365 0.1591 0.1966 -0.0138 -0.0127 -0.0052 131 ILE   A CG2 
2790 C CG2 B ILE   A 131 ? 0.2022 0.2222 0.2240 0.0149  -0.0027 0.0041  131 ILE   A CG2 
2791 C CD1 A ILE   A 131 ? 0.2541 0.2167 0.2131 -0.0451 -0.0404 -0.0091 131 ILE   A CD1 
2792 C CD1 B ILE   A 131 ? 0.2107 0.2293 0.2424 0.0134  -0.0162 -0.0063 131 ILE   A CD1 
2815 N N   A PHE   A 132 ? 0.1865 0.1546 0.1357 -0.0075 -0.0083 0.0236  132 PHE   A N   
2816 N N   B PHE   A 132 ? 0.2026 0.2072 0.1786 0.0096  -0.0148 0.0252  132 PHE   A N   
2817 C CA  A PHE   A 132 ? 0.1892 0.1700 0.1347 -0.0077 0.0005  0.0077  132 PHE   A CA  
2818 C CA  B PHE   A 132 ? 0.2059 0.2034 0.1739 0.0051  -0.0171 0.0276  132 PHE   A CA  
2819 C C   A PHE   A 132 ? 0.1924 0.1839 0.1429 0.0011  -0.0018 0.0117  132 PHE   A C   
2820 C C   B PHE   A 132 ? 0.2065 0.2036 0.1742 0.0075  -0.0181 0.0264  132 PHE   A C   
2821 O O   A PHE   A 132 ? 0.2079 0.1993 0.1571 -0.0034 -0.0025 0.0111  132 PHE   A O   
2822 O O   B PHE   A 132 ? 0.2119 0.2043 0.1676 0.0062  -0.0149 0.0343  132 PHE   A O   
2823 C CB  A PHE   A 132 ? 0.1870 0.1572 0.1460 -0.0115 -0.0064 0.0099  132 PHE   A CB  
2824 C CB  B PHE   A 132 ? 0.2067 0.1994 0.1680 -0.0015 -0.0121 0.0324  132 PHE   A CB  
2825 C CG  A PHE   A 132 ? 0.1911 0.1489 0.1441 -0.0042 -0.0206 0.0093  132 PHE   A CG  
2826 C CG  B PHE   A 132 ? 0.2097 0.1982 0.1736 -0.0052 -0.0062 0.0267  132 PHE   A CG  
2827 C CD1 A PHE   A 132 ? 0.1901 0.1635 0.1737 0.0015  -0.0305 -0.0085 132 PHE   A CD1 
2828 C CD1 B PHE   A 132 ? 0.2093 0.2002 0.1780 -0.0084 -0.0048 0.0180  132 PHE   A CD1 
2829 C CD2 A PHE   A 132 ? 0.1963 0.1620 0.1424 0.0038  -0.0238 0.0021  132 PHE   A CD2 
2830 C CD2 B PHE   A 132 ? 0.2122 0.2000 0.1806 -0.0053 -0.0038 0.0221  132 PHE   A CD2 
2831 C CE1 A PHE   A 132 ? 0.1913 0.1695 0.1817 0.0085  -0.0441 -0.0087 132 PHE   A CE1 
2832 C CE1 B PHE   A 132 ? 0.2106 0.2010 0.1817 -0.0101 -0.0018 0.0109  132 PHE   A CE1 
2833 C CE2 A PHE   A 132 ? 0.1938 0.1688 0.1762 0.0100  -0.0296 0.0051  132 PHE   A CE2 
2834 C CE2 B PHE   A 132 ? 0.2121 0.2014 0.1897 -0.0060 0.0000  0.0143  132 PHE   A CE2 
2835 C CZ  A PHE   A 132 ? 0.1898 0.1674 0.1814 0.0041  -0.0426 -0.0014 132 PHE   A CZ  
2836 C CZ  B PHE   A 132 ? 0.2113 0.2007 0.1874 -0.0089 0.0010  0.0101  132 PHE   A CZ  
2855 N N   A GLY   A 133 ? 0.1925 0.1822 0.1387 0.0043  -0.0294 0.0114  133 GLY   A N   
2856 N N   B GLY   A 133 ? 0.2023 0.2023 0.1792 0.0078  -0.0201 0.0178  133 GLY   A N   
2857 C CA  A GLY   A 133 ? 0.2015 0.1887 0.1626 -0.0020 -0.0366 0.0016  133 GLY   A CA  
2858 C CA  B GLY   A 133 ? 0.1993 0.2045 0.1889 0.0071  -0.0235 0.0083  133 GLY   A CA  
2859 C C   A GLY   A 133 ? 0.2054 0.2001 0.1623 -0.0150 -0.0490 -0.0051 133 GLY   A C   
2860 C C   B GLY   A 133 ? 0.1960 0.2084 0.1989 0.0067  -0.0278 0.0019  133 GLY   A C   
2861 O O   A GLY   A 133 ? 0.2265 0.2188 0.1879 -0.0227 -0.0503 -0.0179 133 GLY   A O   
2862 O O   B GLY   A 133 ? 0.1912 0.2110 0.2016 0.0085  -0.0277 -0.0058 133 GLY   A O   
2869 N N   A ALA   A 134 ? 0.1949 0.1879 0.1528 -0.0220 -0.0262 -0.0022 134 ALA   A N   
2870 N N   B ALA   A 134 ? 0.1982 0.2084 0.2005 0.0054  -0.0266 0.0053  134 ALA   A N   
2871 C CA  A ALA   A 134 ? 0.1913 0.1919 0.1813 -0.0203 -0.0272 -0.0070 134 ALA   A CA  
2872 C CA  B ALA   A 134 ? 0.2018 0.2115 0.2035 0.0025  -0.0244 0.0091  134 ALA   A CA  
2873 C C   A ALA   A 134 ? 0.1967 0.2107 0.1858 -0.0148 -0.0201 0.0098  134 ALA   A C   
2874 C C   B ALA   A 134 ? 0.2064 0.2165 0.2113 0.0006  -0.0202 0.0204  134 ALA   A C   
2875 O O   A ALA   A 134 ? 0.2101 0.2141 0.2082 -0.0037 0.0124  0.0174  134 ALA   A O   
2876 O O   B ALA   A 134 ? 0.2103 0.2169 0.2178 0.0000  -0.0196 0.0266  134 ALA   A O   
2877 C CB  A ALA   A 134 ? 0.2003 0.1837 0.2204 -0.0151 -0.0203 -0.0073 134 ALA   A CB  
2878 C CB  B ALA   A 134 ? 0.2033 0.2104 0.2037 0.0040  -0.0245 0.0037  134 ALA   A CB  
2889 N N   A ASP   A 135 ? 0.2015 0.2274 0.1956 -0.0289 -0.0329 0.0346  135 ASP   A N   
2890 N N   B ASP   A 135 ? 0.2092 0.2206 0.2186 0.0003  -0.0165 0.0217  135 ASP   A N   
2891 C CA  A ASP   A 135 ? 0.1988 0.2418 0.2303 -0.0383 -0.0505 0.0552  135 ASP   A CA  
2892 C CA  B ASP   A 135 ? 0.2107 0.2250 0.2300 -0.0003 -0.0131 0.0231  135 ASP   A CA  
2893 C C   A ASP   A 135 ? 0.1804 0.2298 0.2361 -0.0207 -0.0363 0.0605  135 ASP   A C   
2894 C C   B ASP   A 135 ? 0.2087 0.2247 0.2213 0.0033  -0.0079 0.0232  135 ASP   A C   
2895 O O   A ASP   A 135 ? 0.1754 0.2154 0.2349 -0.0282 -0.0350 0.0605  135 ASP   A O   
2896 O O   B ASP   A 135 ? 0.2086 0.2222 0.2165 0.0007  -0.0027 0.0258  135 ASP   A O   
2897 C CB  A ASP   A 135 ? 0.2253 0.2805 0.2730 -0.0612 -0.0829 0.0480  135 ASP   A CB  
2898 C CB  B ASP   A 135 ? 0.2158 0.2320 0.2539 -0.0053 -0.0146 0.0240  135 ASP   A CB  
2899 C CG  A ASP   A 135 ? 0.2487 0.3200 0.3257 -0.0806 -0.0897 0.0418  135 ASP   A CG  
2900 C CG  B ASP   A 135 ? 0.2194 0.2400 0.2736 -0.0104 -0.0158 0.0269  135 ASP   A CG  
2901 O OD1 A ASP   A 135 ? 0.2399 0.3339 0.3158 -0.0817 -0.0915 0.0681  135 ASP   A OD1 
2902 O OD1 B ASP   A 135 ? 0.2219 0.2424 0.2853 -0.0133 -0.0109 0.0288  135 ASP   A OD1 
2903 O OD2 A ASP   A 135 ? 0.2818 0.3482 0.3839 -0.0856 -0.0707 0.0275  135 ASP   A OD2 
2904 O OD2 B ASP   A 135 ? 0.2171 0.2444 0.2799 -0.0134 -0.0227 0.0296  135 ASP   A OD2 
2913 N N   A PRO   A 136 ? 0.1718 0.2356 0.2530 0.0037  -0.0204 0.0769  136 PRO   A N   
2914 N N   B PRO   A 136 ? 0.2071 0.2266 0.2222 0.0088  -0.0076 0.0261  136 PRO   A N   
2915 C CA  A PRO   A 136 ? 0.1693 0.2325 0.2570 -0.0031 -0.0062 0.0622  136 PRO   A CA  
2916 C CA  B PRO   A 136 ? 0.2049 0.2265 0.2206 0.0088  -0.0082 0.0248  136 PRO   A CA  
2917 C C   A PRO   A 136 ? 0.1455 0.2181 0.2362 -0.0023 -0.0109 0.0466  136 PRO   A C   
2918 C C   B PRO   A 136 ? 0.1996 0.2239 0.2165 0.0093  -0.0126 0.0261  136 PRO   A C   
2919 O O   A PRO   A 136 ? 0.1479 0.2090 0.2179 -0.0002 -0.0042 0.0436  136 PRO   A O   
2920 O O   B PRO   A 136 ? 0.1989 0.2234 0.2134 0.0091  -0.0159 0.0324  136 PRO   A O   
2921 C CB  A PRO   A 136 ? 0.1926 0.2355 0.2896 0.0051  -0.0046 0.0591  136 PRO   A CB  
2922 C CB  B PRO   A 136 ? 0.2085 0.2272 0.2254 0.0115  -0.0073 0.0246  136 PRO   A CB  
2923 C CG  A PRO   A 136 ? 0.2124 0.2497 0.3144 0.0158  -0.0078 0.0626  136 PRO   A CG  
2924 C CG  B PRO   A 136 ? 0.2122 0.2297 0.2308 0.0124  -0.0078 0.0243  136 PRO   A CG  
2925 C CD  A PRO   A 136 ? 0.1922 0.2413 0.2842 0.0191  -0.0066 0.0875  136 PRO   A CD  
2926 C CD  B PRO   A 136 ? 0.2108 0.2288 0.2276 0.0120  -0.0067 0.0261  136 PRO   A CD  
2941 N N   A ILE   A 137 ? 0.1538 0.2184 0.2503 -0.0048 -0.0252 0.0460  137 ILE   A N   
2942 N N   B ILE   A 137 ? 0.1973 0.2235 0.2134 0.0072  -0.0137 0.0233  137 ILE   A N   
2943 C CA  A ILE   A 137 ? 0.1513 0.2284 0.2496 -0.0145 -0.0300 0.0500  137 ILE   A CA  
2944 C CA  B ILE   A 137 ? 0.1953 0.2237 0.2130 0.0027  -0.0152 0.0204  137 ILE   A CA  
2945 C C   A ILE   A 137 ? 0.1468 0.2159 0.2444 -0.0195 -0.0326 0.0506  137 ILE   A C   
2946 C C   B ILE   A 137 ? 0.1902 0.2186 0.2143 -0.0024 -0.0114 0.0159  137 ILE   A C   
2947 O O   A ILE   A 137 ? 0.1541 0.2157 0.2470 -0.0219 -0.0149 0.0445  137 ILE   A O   
2948 O O   B ILE   A 137 ? 0.1911 0.2178 0.2166 -0.0003 -0.0091 0.0114  137 ILE   A O   
2949 C CB  A ILE   A 137 ? 0.1636 0.2551 0.2765 -0.0185 -0.0469 0.0456  137 ILE   A CB  
2950 C CB  B ILE   A 137 ? 0.2004 0.2282 0.2153 0.0020  -0.0186 0.0196  137 ILE   A CB  
2951 C CG1 A ILE   A 137 ? 0.1850 0.2840 0.3156 -0.0098 -0.0533 0.0510  137 ILE   A CG1 
2952 C CG1 B ILE   A 137 ? 0.2047 0.2320 0.2176 0.0029  -0.0217 0.0214  137 ILE   A CG1 
2953 C CG2 A ILE   A 137 ? 0.1721 0.2596 0.2901 -0.0269 -0.0584 0.0292  137 ILE   A CG2 
2954 C CG2 B ILE   A 137 ? 0.2015 0.2289 0.2110 0.0020  -0.0193 0.0173  137 ILE   A CG2 
2955 C CD1 A ILE   A 137 ? 0.2053 0.2976 0.3407 -0.0043 -0.0417 0.0543  137 ILE   A CD1 
2956 C CD1 B ILE   A 137 ? 0.2079 0.2326 0.2191 0.0029  -0.0197 0.0283  137 ILE   A CD1 
2979 N N   A HIS   A 138 ? 0.1550 0.2251 0.2406 -0.0159 -0.0210 0.0463  138 HIS   A N   
2980 N N   B HIS   A 138 ? 0.1856 0.2171 0.2141 -0.0081 -0.0091 0.0172  138 HIS   A N   
2981 C CA  A HIS   A 138 ? 0.1650 0.2282 0.2230 -0.0176 -0.0167 0.0362  138 HIS   A CA  
2982 C CA  B HIS   A 138 ? 0.1788 0.2139 0.2091 -0.0144 -0.0101 0.0213  138 HIS   A CA  
2983 C C   A HIS   A 138 ? 0.1545 0.2155 0.2035 -0.0121 -0.0211 0.0385  138 HIS   A C   
2984 C C   B HIS   A 138 ? 0.1639 0.2057 0.2013 -0.0138 -0.0130 0.0298  138 HIS   A C   
2985 O O   A HIS   A 138 ? 0.1593 0.2176 0.2112 -0.0155 -0.0075 0.0382  138 HIS   A O   
2986 O O   B HIS   A 138 ? 0.1631 0.2057 0.1973 -0.0153 -0.0090 0.0284  138 HIS   A O   
2987 C CB  A HIS   A 138 ? 0.1802 0.2387 0.2233 -0.0162 -0.0178 0.0193  138 HIS   A CB  
2988 C CB  B HIS   A 138 ? 0.1890 0.2191 0.2183 -0.0207 -0.0132 0.0158  138 HIS   A CB  
2989 C CG  A HIS   A 138 ? 0.2030 0.2411 0.2291 -0.0214 -0.0191 0.0092  138 HIS   A CG  
2990 C CG  B HIS   A 138 ? 0.1978 0.2235 0.2278 -0.0255 -0.0096 0.0112  138 HIS   A CG  
2991 N ND1 A HIS   A 138 ? 0.2200 0.2515 0.2475 -0.0203 -0.0173 -0.0045 138 HIS   A ND1 
2992 N ND1 B HIS   A 138 ? 0.2026 0.2275 0.2357 -0.0257 -0.0066 0.0071  138 HIS   A ND1 
2993 C CD2 A HIS   A 138 ? 0.2077 0.2465 0.2283 -0.0115 -0.0195 0.0124  138 HIS   A CD2 
2994 C CD2 B HIS   A 138 ? 0.2017 0.2270 0.2309 -0.0261 -0.0101 0.0090  138 HIS   A CD2 
2995 C CE1 A HIS   A 138 ? 0.2266 0.2575 0.2515 -0.0091 -0.0206 -0.0072 138 HIS   A CE1 
2996 C CE1 B HIS   A 138 ? 0.2060 0.2303 0.2392 -0.0243 -0.0074 0.0064  138 HIS   A CE1 
2997 N NE2 A HIS   A 138 ? 0.2183 0.2562 0.2382 -0.0048 -0.0159 0.0005  138 HIS   A NE2 
2998 N NE2 B HIS   A 138 ? 0.2049 0.2299 0.2343 -0.0244 -0.0087 0.0070  138 HIS   A NE2 
3013 N N   . SER   A 139 ? 0.1505 0.1963 0.2037 -0.0152 -0.0106 0.0423  139 SER   A N   
3014 C CA  . SER   A 139 ? 0.1542 0.1858 0.2023 -0.0168 -0.0082 0.0464  139 SER   A CA  
3015 C C   . SER   A 139 ? 0.1457 0.1818 0.2040 -0.0151 0.0005  0.0294  139 SER   A C   
3016 O O   . SER   A 139 ? 0.1442 0.1746 0.2173 -0.0126 0.0006  0.0389  139 SER   A O   
3017 C CB  . SER   A 139 ? 0.1534 0.1817 0.2083 -0.0208 -0.0099 0.0475  139 SER   A CB  
3018 O OG  . SER   A 139 ? 0.1545 0.1814 0.2190 -0.0200 -0.0167 0.0510  139 SER   A OG  
3025 N N   . LEU   A 140 ? 0.1425 0.1882 0.2048 -0.0070 0.0037  0.0422  140 LEU   A N   
3026 C CA  . LEU   A 140 ? 0.1402 0.1798 0.2077 -0.0082 0.0097  0.0399  140 LEU   A CA  
3027 C C   . LEU   A 140 ? 0.1318 0.1870 0.2097 -0.0139 -0.0038 0.0351  140 LEU   A C   
3028 O O   . LEU   A 140 ? 0.1377 0.1947 0.2251 -0.0078 -0.0056 0.0414  140 LEU   A O   
3029 C CB  . LEU   A 140 ? 0.1374 0.1920 0.2290 -0.0064 0.0125  0.0402  140 LEU   A CB  
3030 C CG  . LEU   A 140 ? 0.1417 0.1952 0.2348 -0.0158 0.0161  0.0533  140 LEU   A CG  
3031 C CD1 . LEU   A 140 ? 0.1511 0.2015 0.2442 -0.0098 0.0092  0.0434  140 LEU   A CD1 
3032 C CD2 . LEU   A 140 ? 0.1567 0.2098 0.2467 -0.0100 0.0225  0.0586  140 LEU   A CD2 
3044 N N   . ARG   A 141 ? 0.1450 0.1883 0.2210 -0.0154 -0.0055 0.0365  141 ARG   A N   
3045 C CA  . ARG   A 141 ? 0.1565 0.1982 0.2347 -0.0257 -0.0163 0.0109  141 ARG   A CA  
3046 C C   . ARG   A 141 ? 0.1550 0.1789 0.2199 -0.0151 -0.0145 0.0204  141 ARG   A C   
3047 O O   . ARG   A 141 ? 0.1544 0.1799 0.2244 -0.0194 0.0047  0.0169  141 ARG   A O   
3048 C CB  . ARG   A 141 ? 0.1659 0.2258 0.2756 -0.0298 -0.0225 -0.0094 141 ARG   A CB  
3049 C CG  . ARG   A 141 ? 0.2079 0.2630 0.3217 -0.0298 -0.0118 -0.0137 141 ARG   A CG  
3050 C CD  . ARG   A 141 ? 0.2424 0.2917 0.3589 -0.0387 -0.0124 -0.0142 141 ARG   A CD  
3051 N NE  . ARG   A 141 ? 0.2310 0.3103 0.3626 -0.0394 -0.0241 -0.0114 141 ARG   A NE  
3052 C CZ  . ARG   A 141 ? 0.2228 0.3278 0.3679 -0.0568 -0.0179 -0.0089 141 ARG   A CZ  
3053 N NH1 . ARG   A 141 ? 0.2174 0.3315 0.3606 -0.0663 0.0002  -0.0259 141 ARG   A NH1 
3054 N NH2 . ARG   A 141 ? 0.2253 0.3348 0.3847 -0.0500 -0.0305 0.0012  141 ARG   A NH2 
3068 N N   . VAL   A 142 ? 0.1501 0.1798 0.2004 -0.0144 -0.0100 0.0193  142 VAL   A N   
3069 C CA  . VAL   A 142 ? 0.1489 0.1801 0.2069 -0.0124 0.0051  0.0111  142 VAL   A CA  
3070 C C   . VAL   A 142 ? 0.1332 0.1707 0.1923 -0.0151 0.0092  0.0211  142 VAL   A C   
3071 O O   . VAL   A 142 ? 0.1478 0.1627 0.2162 0.0001  0.0083  0.0162  142 VAL   A O   
3072 C CB  . VAL   A 142 ? 0.1548 0.1826 0.1991 -0.0108 -0.0002 0.0198  142 VAL   A CB  
3073 C CG1 . VAL   A 142 ? 0.1651 0.1794 0.1991 -0.0165 0.0036  0.0080  142 VAL   A CG1 
3074 C CG2 . VAL   A 142 ? 0.1681 0.2044 0.2330 -0.0030 0.0069  0.0243  142 VAL   A CG2 
3084 N N   . CYS   A 143 ? 0.1357 0.1686 0.1957 -0.0119 0.0045  0.0159  143 CYS   A N   
3085 C CA  . CYS   A 143 ? 0.1471 0.1725 0.2025 -0.0141 0.0075  0.0199  143 CYS   A CA  
3086 C C   . CYS   A 143 ? 0.1452 0.1528 0.1956 -0.0169 0.0033  0.0359  143 CYS   A C   
3087 O O   . CYS   A 143 ? 0.1475 0.1527 0.2035 -0.0073 0.0062  0.0340  143 CYS   A O   
3088 C CB  . CYS   A 143 ? 0.1418 0.1740 0.2124 -0.0092 0.0133  0.0231  143 CYS   A CB  
3089 S SG  . CYS   A 143 ? 0.1654 0.1758 0.1964 0.0041  0.0130  0.0208  143 CYS   A SG  
3095 N N   . VAL   A 144 ? 0.1469 0.1572 0.2234 -0.0150 0.0128  0.0365  144 VAL   A N   
3096 C CA  . VAL   A 144 ? 0.1470 0.1742 0.2667 -0.0167 0.0203  0.0329  144 VAL   A CA  
3097 C C   . VAL   A 144 ? 0.1478 0.1719 0.2480 -0.0199 -0.0150 0.0252  144 VAL   A C   
3098 O O   . VAL   A 144 ? 0.1648 0.1796 0.2524 -0.0082 -0.0107 0.0353  144 VAL   A O   
3099 C CB  . VAL   A 144 ? 0.1745 0.1974 0.3201 -0.0056 0.0426  0.0392  144 VAL   A CB  
3100 C CG1 . VAL   A 144 ? 0.1808 0.2243 0.3621 -0.0102 0.0260  0.0249  144 VAL   A CG1 
3101 C CG2 . VAL   A 144 ? 0.1680 0.2010 0.3267 -0.0103 0.0443  0.0522  144 VAL   A CG2 
3111 N N   . ASP   A 145 ? 0.1612 0.1678 0.2618 -0.0197 -0.0053 0.0130  145 ASP   A N   
3112 C CA  . ASP   A 145 ? 0.1663 0.1758 0.2613 -0.0255 -0.0079 0.0027  145 ASP   A CA  
3113 C C   . ASP   A 145 ? 0.1608 0.1643 0.2590 -0.0136 -0.0021 -0.0059 145 ASP   A C   
3114 O O   . ASP   A 145 ? 0.1776 0.1736 0.3169 -0.0181 -0.0042 -0.0455 145 ASP   A O   
3115 C CB  . ASP   A 145 ? 0.1822 0.2022 0.2762 -0.0264 -0.0203 -0.0032 145 ASP   A CB  
3116 C CG  . ASP   A 145 ? 0.2033 0.2372 0.3020 -0.0500 -0.0281 0.0119  145 ASP   A CG  
3117 O OD1 . ASP   A 145 ? 0.2037 0.2521 0.3218 -0.0691 -0.0224 0.0153  145 ASP   A OD1 
3118 O OD2 . ASP   A 145 ? 0.2285 0.2627 0.3063 -0.0614 -0.0513 0.0054  145 ASP   A OD2 
3123 N N   . THR   A 146 ? 0.1447 0.1512 0.2239 -0.0180 0.0099  0.0097  146 THR   A N   
3124 C CA  . THR   A 146 ? 0.1419 0.1544 0.2083 -0.0089 0.0072  0.0040  146 THR   A CA  
3125 C C   . THR   A 146 ? 0.1379 0.1495 0.2069 0.0004  0.0063  0.0130  146 THR   A C   
3126 O O   . THR   A 146 ? 0.1476 0.1536 0.2346 0.0032  -0.0001 0.0073  146 THR   A O   
3127 C CB  . THR   A 146 ? 0.1427 0.1596 0.2107 -0.0045 0.0022  0.0209  146 THR   A CB  
3128 O OG1 . THR   A 146 ? 0.1453 0.1743 0.2190 0.0022  -0.0035 0.0137  146 THR   A OG1 
3129 C CG2 . THR   A 146 ? 0.1441 0.1626 0.2309 -0.0050 0.0091  0.0155  146 THR   A CG2 
3137 N N   . VAL   A 147 ? 0.1331 0.1470 0.2025 -0.0030 0.0055  0.0181  147 VAL   A N   
3138 C CA  . VAL   A 147 ? 0.1337 0.1579 0.1997 -0.0111 0.0305  0.0168  147 VAL   A CA  
3139 C C   . VAL   A 147 ? 0.1548 0.1468 0.2024 -0.0175 0.0137  0.0259  147 VAL   A C   
3140 O O   . VAL   A 147 ? 0.1557 0.1454 0.2245 -0.0178 0.0126  0.0251  147 VAL   A O   
3141 C CB  . VAL   A 147 ? 0.1529 0.1549 0.1935 -0.0091 0.0282  0.0271  147 VAL   A CB  
3142 C CG1 . VAL   A 147 ? 0.1841 0.1660 0.1974 -0.0044 0.0274  0.0304  147 VAL   A CG1 
3143 C CG2 . VAL   A 147 ? 0.1623 0.1641 0.2064 -0.0120 0.0120  0.0244  147 VAL   A CG2 
3153 N N   . ARG   A 148 ? 0.1605 0.1447 0.2156 -0.0159 0.0197  0.0399  148 ARG   A N   
3154 C CA  . ARG   A 148 ? 0.1615 0.1443 0.2189 -0.0146 0.0085  0.0393  148 ARG   A CA  
3155 C C   . ARG   A 148 ? 0.1621 0.1491 0.2187 -0.0201 0.0160  0.0525  148 ARG   A C   
3156 O O   . ARG   A 148 ? 0.1926 0.1589 0.2434 -0.0227 0.0223  0.0448  148 ARG   A O   
3157 C CB  . ARG   A 148 ? 0.1611 0.1475 0.2307 -0.0104 0.0107  0.0325  148 ARG   A CB  
3158 C CG  . ARG   A 148 ? 0.1836 0.1493 0.2652 -0.0085 0.0248  0.0173  148 ARG   A CG  
3159 C CD  . ARG   A 148 ? 0.1980 0.1529 0.2942 -0.0106 0.0450  0.0477  148 ARG   A CD  
3160 N NE  . ARG   A 148 ? 0.1918 0.1573 0.2904 -0.0006 0.0500  0.0455  148 ARG   A NE  
3161 C CZ  . ARG   A 148 ? 0.1885 0.1484 0.2722 -0.0017 0.0549  0.0385  148 ARG   A CZ  
3162 N NH1 . ARG   A 148 ? 0.1940 0.1553 0.2862 -0.0149 0.0467  0.0138  148 ARG   A NH1 
3163 N NH2 . ARG   A 148 ? 0.1819 0.1805 0.2695 0.0131  0.0509  0.0415  148 ARG   A NH2 
3177 N N   . THR   A 149 ? 0.1583 0.1655 0.2050 -0.0194 -0.0018 0.0455  149 THR   A N   
3178 C CA  . THR   A 149 ? 0.1697 0.1652 0.2057 -0.0180 0.0063  0.0411  149 THR   A CA  
3179 C C   . THR   A 149 ? 0.1649 0.1609 0.1980 -0.0198 0.0155  0.0511  149 THR   A C   
3180 O O   . THR   A 149 ? 0.1619 0.1765 0.2165 -0.0195 0.0098  0.0461  149 THR   A O   
3181 C CB  . THR   A 149 ? 0.1743 0.1786 0.2147 -0.0104 0.0099  0.0399  149 THR   A CB  
3182 O OG1 . THR   A 149 ? 0.1677 0.1681 0.2308 -0.0209 0.0008  0.0403  149 THR   A OG1 
3183 C CG2 . THR   A 149 ? 0.1753 0.1938 0.2185 0.0013  -0.0075 0.0431  149 THR   A CG2 
3191 N N   . ASN   A 150 ? 0.1592 0.1571 0.2015 -0.0016 0.0105  0.0472  150 ASN   A N   
3192 C CA  . ASN   A 150 ? 0.1825 0.1788 0.2053 -0.0083 0.0134  0.0425  150 ASN   A CA  
3193 C C   . ASN   A 150 ? 0.1558 0.1679 0.2071 -0.0154 0.0096  0.0419  150 ASN   A C   
3194 O O   . ASN   A 150 ? 0.1680 0.1816 0.2424 -0.0183 -0.0039 0.0371  150 ASN   A O   
3195 C CB  . ASN   A 150 ? 0.2328 0.2087 0.2312 -0.0187 0.0365  0.0629  150 ASN   A CB  
3196 C CG  . ASN   A 150 ? 0.2868 0.2446 0.3046 -0.0216 0.0134  0.0668  150 ASN   A CG  
3197 O OD1 . ASN   A 150 ? 0.3046 0.2526 0.3263 -0.0312 0.0134  0.0810  150 ASN   A OD1 
3198 N ND2 . ASN   A 150 ? 0.3198 0.2716 0.3393 -0.0175 0.0040  0.0673  150 ASN   A ND2 
3205 N N   . VAL   A 151 ? 0.1609 0.1628 0.2067 -0.0161 0.0089  0.0478  151 VAL   A N   
3206 C CA  . VAL   A 151 ? 0.1602 0.1600 0.2095 -0.0140 0.0136  0.0507  151 VAL   A CA  
3207 C C   . VAL   A 151 ? 0.1598 0.1466 0.2136 -0.0266 0.0136  0.0432  151 VAL   A C   
3208 O O   . VAL   A 151 ? 0.1753 0.1578 0.2377 -0.0231 0.0153  0.0397  151 VAL   A O   
3209 C CB  . VAL   A 151 ? 0.1902 0.1857 0.2087 -0.0052 0.0136  0.0478  151 VAL   A CB  
3210 C CG1 . VAL   A 151 ? 0.1817 0.2115 0.2279 -0.0132 0.0079  0.0416  151 VAL   A CG1 
3211 C CG2 . VAL   A 151 ? 0.2065 0.1804 0.2022 -0.0020 0.0282  0.0404  151 VAL   A CG2 
3221 N N   . TYR   A 152 ? 0.1552 0.1498 0.2045 -0.0170 0.0153  0.0416  152 TYR   A N   
3222 C CA  . TYR   A 152 ? 0.1566 0.1631 0.1734 -0.0200 0.0175  0.0354  152 TYR   A CA  
3223 C C   . TYR   A 152 ? 0.1576 0.1648 0.1656 -0.0214 0.0224  0.0413  152 TYR   A C   
3224 O O   . TYR   A 152 ? 0.1599 0.1553 0.1893 -0.0220 0.0242  0.0349  152 TYR   A O   
3225 C CB  . TYR   A 152 ? 0.1818 0.1710 0.1769 -0.0220 0.0298  0.0343  152 TYR   A CB  
3226 C CG  . TYR   A 152 ? 0.1947 0.1908 0.1730 -0.0294 0.0363  0.0402  152 TYR   A CG  
3227 C CD1 . TYR   A 152 ? 0.2063 0.2115 0.2086 -0.0144 0.0337  0.0454  152 TYR   A CD1 
3228 C CD2 . TYR   A 152 ? 0.2003 0.2018 0.1737 -0.0455 0.0313  0.0294  152 TYR   A CD2 
3229 C CE1 . TYR   A 152 ? 0.2275 0.2211 0.2176 -0.0115 0.0173  0.0580  152 TYR   A CE1 
3230 C CE2 . TYR   A 152 ? 0.2215 0.2162 0.1859 -0.0419 0.0288  0.0397  152 TYR   A CE2 
3231 C CZ  . TYR   A 152 ? 0.2398 0.2115 0.1990 -0.0325 0.0176  0.0624  152 TYR   A CZ  
3232 O OH  . TYR   A 152 ? 0.2708 0.2391 0.2286 -0.0154 0.0160  0.0740  152 TYR   A OH  
3242 N N   . LEU   A 153 ? 0.1550 0.1697 0.1737 -0.0235 0.0210  0.0407  153 LEU   A N   
3243 C CA  . LEU   A 153 ? 0.1482 0.1702 0.1926 -0.0122 0.0157  0.0395  153 LEU   A CA  
3244 C C   . LEU   A 153 ? 0.1473 0.1718 0.2146 -0.0144 0.0322  0.0412  153 LEU   A C   
3245 O O   . LEU   A 153 ? 0.1603 0.1739 0.2442 -0.0090 0.0467  0.0356  153 LEU   A O   
3246 C CB  . LEU   A 153 ? 0.1396 0.1584 0.2045 -0.0047 0.0158  0.0461  153 LEU   A CB  
3247 C CG  . LEU   A 153 ? 0.1519 0.1652 0.2091 -0.0154 0.0206  0.0377  153 LEU   A CG  
3248 C CD1 . LEU   A 153 ? 0.1616 0.1694 0.1988 -0.0124 0.0027  0.0327  153 LEU   A CD1 
3249 C CD2 . LEU   A 153 ? 0.1581 0.1685 0.2130 -0.0234 0.0308  0.0167  153 LEU   A CD2 
3261 N N   A ALA   A 154 ? 0.1423 0.1633 0.2286 -0.0151 0.0428  0.0430  154 ALA   A N   
3262 N N   B ALA   A 154 ? 0.1539 0.1760 0.1973 -0.0123 0.0238  0.0394  154 ALA   A N   
3263 C CA  A ALA   A 154 ? 0.1632 0.1658 0.2500 -0.0034 0.0389  0.0365  154 ALA   A CA  
3264 C CA  B ALA   A 154 ? 0.1644 0.1817 0.1873 -0.0097 0.0164  0.0363  154 ALA   A CA  
3265 C C   A ALA   A 154 ? 0.1657 0.1615 0.2523 0.0045  0.0354  0.0498  154 ALA   A C   
3266 C C   B ALA   A 154 ? 0.1686 0.1853 0.1776 -0.0079 0.0080  0.0352  154 ALA   A C   
3267 O O   A ALA   A 154 ? 0.1736 0.1738 0.2437 -0.0013 0.0387  0.0490  154 ALA   A O   
3268 O O   B ALA   A 154 ? 0.1679 0.1799 0.1689 -0.0123 0.0058  0.0441  154 ALA   A O   
3269 C CB  A ALA   A 154 ? 0.1746 0.1614 0.2564 0.0060  0.0284  0.0343  154 ALA   A CB  
3270 C CB  B ALA   A 154 ? 0.1683 0.1817 0.1836 -0.0097 0.0153  0.0357  154 ALA   A CB  
3281 N N   A VAL   A 155 ? 0.1701 0.1672 0.2677 0.0149  0.0376  0.0650  155 VAL   A N   
3282 N N   B VAL   A 155 ? 0.1766 0.1959 0.1818 -0.0021 0.0045  0.0263  155 VAL   A N   
3283 C CA  A VAL   A 155 ? 0.1686 0.1849 0.2932 0.0170  0.0294  0.0747  155 VAL   A CA  
3284 C CA  B VAL   A 155 ? 0.1864 0.2082 0.1931 0.0016  -0.0003 0.0176  155 VAL   A CA  
3285 C C   A VAL   A 155 ? 0.1820 0.1947 0.3177 0.0308  0.0283  0.0962  155 VAL   A C   
3286 C C   B VAL   A 155 ? 0.2009 0.2171 0.2086 0.0020  0.0010  0.0121  155 VAL   A C   
3287 O O   A VAL   A 155 ? 0.1891 0.1983 0.3298 0.0465  0.0466  0.0740  155 VAL   A O   
3288 O O   B VAL   A 155 ? 0.2027 0.2185 0.2095 0.0033  0.0034  0.0109  155 VAL   A O   
3289 C CB  A VAL   A 155 ? 0.1699 0.1981 0.2868 0.0104  0.0144  0.0653  155 VAL   A CB  
3290 C CB  B VAL   A 155 ? 0.1822 0.2109 0.1941 0.0040  -0.0036 0.0155  155 VAL   A CB  
3291 C CG1 A VAL   A 155 ? 0.1915 0.2146 0.2877 0.0097  0.0126  0.0708  155 VAL   A CG1 
3292 C CG1 B VAL   A 155 ? 0.1767 0.2122 0.1917 0.0045  -0.0070 0.0159  155 VAL   A CG1 
3293 C CG2 A VAL   A 155 ? 0.1711 0.2059 0.2982 0.0249  0.0001  0.0584  155 VAL   A CG2 
3294 C CG2 B VAL   A 155 ? 0.1847 0.2121 0.1968 0.0050  -0.0052 0.0122  155 VAL   A CG2 
3313 N N   A PHE   A 156 ? 0.2009 0.2046 0.3524 0.0305  0.0329  0.1101  156 PHE   A N   
3314 N N   B PHE   A 156 ? 0.2142 0.2242 0.2222 0.0015  0.0007  0.0072  156 PHE   A N   
3315 C CA  A PHE   A 156 ? 0.2239 0.2111 0.3985 0.0396  0.0330  0.1102  156 PHE   A CA  
3316 C CA  B PHE   A 156 ? 0.2298 0.2317 0.2452 0.0018  0.0041  0.0030  156 PHE   A CA  
3317 C C   A PHE   A 156 ? 0.2272 0.2078 0.4082 0.0525  0.0440  0.1216  156 PHE   A C   
3318 C C   B PHE   A 156 ? 0.2391 0.2389 0.2539 0.0014  0.0055  0.0057  156 PHE   A C   
3319 O O   A PHE   A 156 ? 0.2327 0.2271 0.4261 0.0438  0.0448  0.1032  156 PHE   A O   
3320 O O   B PHE   A 156 ? 0.2433 0.2388 0.2574 0.0018  0.0004  0.0061  156 PHE   A O   
3321 C CB  A PHE   A 156 ? 0.2486 0.2125 0.4107 0.0326  0.0201  0.1145  156 PHE   A CB  
3322 C CB  B PHE   A 156 ? 0.2357 0.2312 0.2537 0.0014  0.0068  -0.0019 156 PHE   A CB  
3323 C CG  A PHE   A 156 ? 0.2817 0.2193 0.4298 0.0389  0.0073  0.1064  156 PHE   A CG  
3324 C CG  B PHE   A 156 ? 0.2424 0.2320 0.2649 0.0010  0.0054  -0.0073 156 PHE   A CG  
3325 C CD1 A PHE   A 156 ? 0.2984 0.2282 0.4484 0.0412  0.0122  0.0879  156 PHE   A CD1 
3326 C CD1 B PHE   A 156 ? 0.2456 0.2313 0.2684 0.0049  0.0048  -0.0132 156 PHE   A CD1 
3327 C CD2 A PHE   A 156 ? 0.2952 0.2214 0.4415 0.0518  -0.0022 0.1097  156 PHE   A CD2 
3328 C CD2 B PHE   A 156 ? 0.2438 0.2329 0.2693 -0.0026 0.0044  -0.0101 156 PHE   A CD2 
3329 C CE1 A PHE   A 156 ? 0.3125 0.2369 0.4673 0.0473  0.0116  0.0761  156 PHE   A CE1 
3330 C CE1 B PHE   A 156 ? 0.2459 0.2312 0.2692 0.0055  0.0035  -0.0175 156 PHE   A CE1 
3331 C CE2 A PHE   A 156 ? 0.3122 0.2362 0.4526 0.0573  -0.0014 0.0894  156 PHE   A CE2 
3332 C CE2 B PHE   A 156 ? 0.2461 0.2328 0.2730 -0.0023 0.0033  -0.0140 156 PHE   A CE2 
3333 C CZ  A PHE   A 156 ? 0.3158 0.2405 0.4668 0.0604  0.0045  0.0683  156 PHE   A CZ  
3334 C CZ  B PHE   A 156 ? 0.2467 0.2324 0.2700 0.0031  0.0038  -0.0182 156 PHE   A CZ  
3353 N N   A ASP   A 157 ? 0.2296 0.2167 0.3994 0.0485  0.0461  0.1355  157 ASP   A N   
3354 N N   B ASP   A 157 ? 0.2423 0.2468 0.2571 -0.0009 0.0049  0.0070  157 ASP   A N   
3355 C CA  A ASP   A 157 ? 0.2465 0.2361 0.4091 0.0556  0.0353  0.1389  157 ASP   A CA  
3356 C CA  B ASP   A 157 ? 0.2473 0.2551 0.2713 -0.0034 0.0080  0.0120  157 ASP   A CA  
3357 C C   A ASP   A 157 ? 0.2289 0.2577 0.4066 0.0649  0.0530  0.1471  157 ASP   A C   
3358 C C   B ASP   A 157 ? 0.2491 0.2609 0.2806 0.0015  0.0066  0.0150  157 ASP   A C   
3359 O O   A ASP   A 157 ? 0.2143 0.2535 0.3993 0.0623  0.0644  0.1571  157 ASP   A O   
3360 O O   B ASP   A 157 ? 0.2468 0.2612 0.2814 0.0010  0.0065  0.0136  157 ASP   A O   
3361 C CB  A ASP   A 157 ? 0.2805 0.2493 0.4356 0.0538  0.0108  0.1283  157 ASP   A CB  
3362 C CB  B ASP   A 157 ? 0.2500 0.2579 0.2782 -0.0121 0.0127  0.0162  157 ASP   A CB  
3363 C CG  A ASP   A 157 ? 0.3177 0.2638 0.4739 0.0530  -0.0152 0.1234  157 ASP   A CG  
3364 C CG  B ASP   A 157 ? 0.2540 0.2602 0.2877 -0.0194 0.0159  0.0187  157 ASP   A CG  
3365 O OD1 A ASP   A 157 ? 0.3536 0.2733 0.5109 0.0436  -0.0498 0.1019  157 ASP   A OD1 
3366 O OD1 B ASP   A 157 ? 0.2531 0.2583 0.2872 -0.0225 0.0144  0.0194  157 ASP   A OD1 
3367 O OD2 A ASP   A 157 ? 0.3125 0.2641 0.4828 0.0481  -0.0056 0.1439  157 ASP   A OD2 
3368 O OD2 B ASP   A 157 ? 0.2596 0.2631 0.2973 -0.0237 0.0185  0.0164  157 ASP   A OD2 
3377 N N   A LYS   A 158 ? 0.2361 0.2852 0.4206 0.0696  0.0548  0.1319  158 LYS   A N   
3378 N N   B LYS   A 158 ? 0.2532 0.2656 0.2860 0.0054  0.0043  0.0178  158 LYS   A N   
3379 C CA  A LYS   A 158 ? 0.2298 0.3144 0.4225 0.0716  0.0695  0.1222  158 LYS   A CA  
3380 C CA  B LYS   A 158 ? 0.2557 0.2714 0.2908 0.0085  0.0028  0.0206  158 LYS   A CA  
3381 C C   A LYS   A 158 ? 0.2065 0.3254 0.4031 0.0703  0.0644  0.1466  158 LYS   A C   
3382 C C   B LYS   A 158 ? 0.2537 0.2747 0.2916 0.0118  0.0011  0.0305  158 LYS   A C   
3383 O O   A LYS   A 158 ? 0.1945 0.3280 0.4045 0.0630  0.0639  0.1518  158 LYS   A O   
3384 O O   B LYS   A 158 ? 0.2504 0.2770 0.2917 0.0108  -0.0038 0.0332  158 LYS   A O   
3385 C CB  A LYS   A 158 ? 0.2522 0.3325 0.4377 0.0701  0.0929  0.1004  158 LYS   A CB  
3386 C CB  B LYS   A 158 ? 0.2600 0.2744 0.2933 0.0070  0.0034  0.0126  158 LYS   A CB  
3387 C CG  A LYS   A 158 ? 0.2718 0.3472 0.4496 0.0742  0.1052  0.0890  158 LYS   A CG  
3388 C CG  B LYS   A 158 ? 0.2629 0.2762 0.2949 0.0058  -0.0008 0.0066  158 LYS   A CG  
3389 C CD  A LYS   A 158 ? 0.2892 0.3645 0.4625 0.0673  0.1206  0.0916  158 LYS   A CD  
3390 C CD  B LYS   A 158 ? 0.2629 0.2776 0.2970 0.0047  -0.0034 0.0024  158 LYS   A CD  
3391 C CE  A LYS   A 158 ? 0.2984 0.3763 0.4768 0.0617  0.1326  0.0983  158 LYS   A CE  
3392 C CE  B LYS   A 158 ? 0.2606 0.2767 0.2957 0.0042  -0.0060 -0.0006 158 LYS   A CE  
3393 N NZ  A LYS   A 158 ? 0.3025 0.3829 0.4864 0.0561  0.1343  0.1075  158 LYS   A NZ  
3394 N NZ  B LYS   A 158 ? 0.2593 0.2756 0.2958 0.0045  -0.0057 -0.0047 158 LYS   A NZ  
3421 N N   A ASN   A 159 ? 0.1973 0.3399 0.4241 0.0748  0.0421  0.1447  159 ASN   A N   
3422 N N   B ASN   A 159 ? 0.2552 0.2759 0.2982 0.0149  0.0031  0.0313  159 ASN   A N   
3423 C CA  A ASN   A 159 ? 0.2047 0.3426 0.4189 0.0656  0.0197  0.1683  159 ASN   A CA  
3424 C CA  B ASN   A 159 ? 0.2575 0.2752 0.3023 0.0128  0.0046  0.0316  159 ASN   A CA  
3425 C C   A ASN   A 159 ? 0.1941 0.3376 0.3893 0.0421  0.0251  0.1621  159 ASN   A C   
3426 C C   B ASN   A 159 ? 0.2527 0.2733 0.2892 0.0087  0.0106  0.0272  159 ASN   A C   
3427 O O   A ASN   A 159 ? 0.1650 0.3465 0.3709 0.0420  0.0026  0.1487  159 ASN   A O   
3428 O O   B ASN   A 159 ? 0.2521 0.2745 0.2863 0.0078  0.0092  0.0238  159 ASN   A O   
3429 C CB  A ASN   A 159 ? 0.2244 0.3550 0.4619 0.0706  0.0139  0.1831  159 ASN   A CB  
3430 C CB  B ASN   A 159 ? 0.2646 0.2769 0.3208 0.0140  0.0001  0.0351  159 ASN   A CB  
3431 C CG  A ASN   A 159 ? 0.2533 0.3722 0.5170 0.0573  0.0187  0.1709  159 ASN   A CG  
3432 C CG  B ASN   A 159 ? 0.2708 0.2796 0.3412 0.0159  -0.0013 0.0350  159 ASN   A CG  
3433 O OD1 A ASN   A 159 ? 0.2621 0.3857 0.5442 0.0465  0.0315  0.1567  159 ASN   A OD1 
3434 O OD1 B ASN   A 159 ? 0.2709 0.2817 0.3498 0.0164  -0.0054 0.0310  159 ASN   A OD1 
3435 N ND2 A ASN   A 159 ? 0.2670 0.3806 0.5465 0.0490  0.0208  0.1586  159 ASN   A ND2 
3436 N ND2 B ASN   A 159 ? 0.2746 0.2804 0.3476 0.0163  -0.0026 0.0352  159 ASN   A ND2 
3449 N N   A LEU   A 160 ? 0.1818 0.3131 0.3786 0.0360  0.0108  0.1578  160 LEU   A N   
3450 N N   B LEU   A 160 ? 0.2444 0.2673 0.2779 0.0058  0.0113  0.0266  160 LEU   A N   
3451 C CA  A LEU   A 160 ? 0.1813 0.2923 0.3546 0.0251  0.0212  0.1548  160 LEU   A CA  
3452 C CA  B LEU   A 160 ? 0.2373 0.2612 0.2654 0.0014  0.0127  0.0275  160 LEU   A CA  
3453 C C   A LEU   A 160 ? 0.1599 0.2846 0.3381 0.0110  0.0345  0.1462  160 LEU   A C   
3454 C C   B LEU   A 160 ? 0.2294 0.2576 0.2557 0.0004  0.0119  0.0283  160 LEU   A C   
3455 O O   A LEU   A 160 ? 0.1571 0.2986 0.3609 0.0066  0.0243  0.1369  160 LEU   A O   
3456 O O   B LEU   A 160 ? 0.2279 0.2597 0.2594 -0.0007 0.0106  0.0306  160 LEU   A O   
3457 C CB  A LEU   A 160 ? 0.1979 0.2867 0.3382 0.0111  0.0264  0.1543  160 LEU   A CB  
3458 C CB  B LEU   A 160 ? 0.2380 0.2597 0.2618 -0.0044 0.0149  0.0275  160 LEU   A CB  
3459 C CG  A LEU   A 160 ? 0.2107 0.2901 0.3447 -0.0086 0.0355  0.1261  160 LEU   A CG  
3460 C CG  B LEU   A 160 ? 0.2388 0.2589 0.2606 -0.0094 0.0168  0.0240  160 LEU   A CG  
3461 C CD1 A LEU   A 160 ? 0.2248 0.3028 0.3465 -0.0097 0.0335  0.1020  160 LEU   A CD1 
3462 C CD1 B LEU   A 160 ? 0.2404 0.2603 0.2593 -0.0090 0.0171  0.0201  160 LEU   A CD1 
3463 C CD2 A LEU   A 160 ? 0.2116 0.2864 0.3456 -0.0163 0.0467  0.1139  160 LEU   A CD2 
3464 C CD2 B LEU   A 160 ? 0.2389 0.2566 0.2603 -0.0127 0.0191  0.0228  160 LEU   A CD2 
3487 N N   A TYR   A 161 ? 0.1604 0.2650 0.3290 0.0163  0.0289  0.1367  161 TYR   A N   
3488 N N   B TYR   A 161 ? 0.2253 0.2525 0.2487 0.0014  0.0105  0.0262  161 TYR   A N   
3489 C CA  A TYR   A 161 ? 0.1692 0.2525 0.3175 0.0164  0.0434  0.1360  161 TYR   A CA  
3490 C CA  B TYR   A 161 ? 0.2215 0.2493 0.2429 0.0018  0.0105  0.0281  161 TYR   A CA  
3491 C C   A TYR   A 161 ? 0.1642 0.2673 0.3272 0.0214  0.0410  0.1302  161 TYR   A C   
3492 C C   B TYR   A 161 ? 0.2201 0.2546 0.2445 0.0007  0.0088  0.0324  161 TYR   A C   
3493 O O   A TYR   A 161 ? 0.1492 0.2742 0.3296 0.0129  0.0401  0.1188  161 TYR   A O   
3494 O O   B TYR   A 161 ? 0.2174 0.2550 0.2410 0.0001  0.0103  0.0316  161 TYR   A O   
3495 C CB  A TYR   A 161 ? 0.1823 0.2425 0.3343 0.0150  0.0448  0.1074  161 TYR   A CB  
3496 C CB  B TYR   A 161 ? 0.2208 0.2433 0.2392 0.0027  0.0097  0.0235  161 TYR   A CB  
3497 C CG  A TYR   A 161 ? 0.1835 0.2316 0.3228 0.0138  0.0462  0.0869  161 TYR   A CG  
3498 C CG  B TYR   A 161 ? 0.2189 0.2385 0.2311 0.0027  0.0075  0.0192  161 TYR   A CG  
3499 C CD1 A TYR   A 161 ? 0.1760 0.2169 0.3305 0.0088  0.0336  0.0767  161 TYR   A CD1 
3500 C CD1 B TYR   A 161 ? 0.2170 0.2364 0.2307 0.0020  0.0054  0.0182  161 TYR   A CD1 
3501 C CD2 A TYR   A 161 ? 0.1911 0.2409 0.3179 0.0140  0.0439  0.0774  161 TYR   A CD2 
3502 C CD2 B TYR   A 161 ? 0.2192 0.2373 0.2272 0.0035  0.0062  0.0170  161 TYR   A CD2 
3503 C CE1 A TYR   A 161 ? 0.1822 0.2124 0.3228 0.0066  0.0351  0.0783  161 TYR   A CE1 
3504 C CE1 B TYR   A 161 ? 0.2181 0.2352 0.2286 0.0025  0.0036  0.0190  161 TYR   A CE1 
3505 C CE2 A TYR   A 161 ? 0.1939 0.2319 0.3087 0.0081  0.0398  0.0851  161 TYR   A CE2 
3506 C CE2 B TYR   A 161 ? 0.2203 0.2362 0.2267 0.0019  0.0039  0.0185  161 TYR   A CE2 
3507 C CZ  A TYR   A 161 ? 0.1994 0.2207 0.3155 0.0059  0.0322  0.0852  161 TYR   A CZ  
3508 C CZ  B TYR   A 161 ? 0.2216 0.2367 0.2294 0.0023  0.0028  0.0198  161 TYR   A CZ  
3509 O OH  A TYR   A 161 ? 0.2174 0.2269 0.3221 -0.0012 0.0213  0.0885  161 TYR   A OH  
3510 O OH  B TYR   A 161 ? 0.2264 0.2397 0.2368 0.0027  -0.0013 0.0217  161 TYR   A OH  
3529 N N   A ASP   A 162 ? 0.1651 0.2818 0.3526 0.0281  0.0478  0.1265  162 ASP   A N   
3530 N N   B ASP   A 162 ? 0.2213 0.2597 0.2536 0.0015  0.0083  0.0378  162 ASP   A N   
3531 C CA  A ASP   A 162 ? 0.1582 0.3040 0.3582 0.0112  0.0554  0.1211  162 ASP   A CA  
3532 C CA  B ASP   A 162 ? 0.2211 0.2654 0.2596 -0.0001 0.0063  0.0410  162 ASP   A CA  
3533 C C   A ASP   A 162 ? 0.1447 0.3231 0.3532 -0.0048 0.0464  0.1265  162 ASP   A C   
3534 C C   B ASP   A 162 ? 0.2273 0.2712 0.2662 -0.0058 0.0057  0.0375  162 ASP   A C   
3535 O O   A ASP   A 162 ? 0.1496 0.3279 0.3741 -0.0051 0.0410  0.1197  162 ASP   A O   
3536 O O   B ASP   A 162 ? 0.2281 0.2717 0.2688 -0.0070 0.0071  0.0360  162 ASP   A O   
3537 C CB  A ASP   A 162 ? 0.1639 0.3112 0.3704 0.0225  0.0613  0.1096  162 ASP   A CB  
3538 C CB  B ASP   A 162 ? 0.2162 0.2662 0.2633 0.0040  0.0055  0.0472  162 ASP   A CB  
3539 C CG  A ASP   A 162 ? 0.1854 0.3267 0.3904 0.0318  0.0633  0.0947  162 ASP   A CG  
3540 C CG  B ASP   A 162 ? 0.2143 0.2681 0.2640 0.0064  0.0043  0.0559  162 ASP   A CG  
3541 O OD1 A ASP   A 162 ? 0.2130 0.3374 0.3997 0.0234  0.0677  0.0894  162 ASP   A OD1 
3542 O OD1 B ASP   A 162 ? 0.2154 0.2683 0.2652 0.0094  0.0046  0.0612  162 ASP   A OD1 
3543 O OD2 A ASP   A 162 ? 0.2071 0.3350 0.4099 0.0458  0.0724  0.0803  162 ASP   A OD2 
3544 O OD2 B ASP   A 162 ? 0.2147 0.2688 0.2637 0.0060  0.0024  0.0618  162 ASP   A OD2 
3553 N N   A LYS   A 163 ? 0.1690 0.3423 0.3589 -0.0032 0.0171  0.1238  163 LYS   A N   
3554 N N   B LYS   A 163 ? 0.2348 0.2759 0.2772 -0.0091 0.0016  0.0345  163 LYS   A N   
3555 C CA  A LYS   A 163 ? 0.1828 0.3593 0.3465 -0.0056 0.0001  0.1162  163 LYS   A CA  
3556 C CA  B LYS   A 163 ? 0.2413 0.2792 0.2824 -0.0120 0.0009  0.0297  163 LYS   A CA  
3557 C C   A LYS   A 163 ? 0.1750 0.3451 0.3337 -0.0122 0.0106  0.1175  163 LYS   A C   
3558 C C   B LYS   A 163 ? 0.2380 0.2754 0.2712 -0.0144 0.0041  0.0278  163 LYS   A C   
3559 O O   A LYS   A 163 ? 0.1663 0.3626 0.3439 -0.0223 0.0107  0.1027  163 LYS   A O   
3560 O O   B LYS   A 163 ? 0.2402 0.2796 0.2714 -0.0133 0.0060  0.0286  163 LYS   A O   
3561 C CB  A LYS   A 163 ? 0.2280 0.3911 0.3846 0.0091  -0.0210 0.1059  163 LYS   A CB  
3562 C CB  B LYS   A 163 ? 0.2516 0.2858 0.3013 -0.0122 -0.0032 0.0255  163 LYS   A CB  
3563 C CG  A LYS   A 163 ? 0.2700 0.4191 0.4262 0.0157  -0.0178 0.0994  163 LYS   A CG  
3564 C CG  B LYS   A 163 ? 0.2606 0.2922 0.3185 -0.0130 -0.0054 0.0215  163 LYS   A CG  
3565 C CD  A LYS   A 163 ? 0.3169 0.4459 0.4777 0.0208  -0.0163 0.0884  163 LYS   A CD  
3566 C CD  B LYS   A 163 ? 0.2682 0.2967 0.3347 -0.0129 -0.0066 0.0178  163 LYS   A CD  
3567 C CE  A LYS   A 163 ? 0.3501 0.4637 0.5139 0.0201  -0.0132 0.0824  163 LYS   A CE  
3568 C CE  B LYS   A 163 ? 0.2739 0.3005 0.3478 -0.0137 -0.0060 0.0145  163 LYS   A CE  
3569 N NZ  A LYS   A 163 ? 0.3637 0.4706 0.5361 0.0178  -0.0111 0.0820  163 LYS   A NZ  
3570 N NZ  B LYS   A 163 ? 0.2785 0.3040 0.3527 -0.0155 -0.0079 0.0121  163 LYS   A NZ  
3597 N N   A LEU   A 164 ? 0.1562 0.3104 0.3156 -0.0219 0.0097  0.1104  164 LEU   A N   
3598 N N   B LEU   A 164 ? 0.2314 0.2671 0.2588 -0.0170 0.0037  0.0232  164 LEU   A N   
3599 C CA  A LEU   A 164 ? 0.1621 0.2815 0.2963 -0.0284 0.0206  0.0989  164 LEU   A CA  
3600 C CA  B LEU   A 164 ? 0.2281 0.2598 0.2474 -0.0190 0.0054  0.0206  164 LEU   A CA  
3601 C C   A LEU   A 164 ? 0.1663 0.2802 0.2931 -0.0270 0.0301  0.0821  164 LEU   A C   
3602 C C   B LEU   A 164 ? 0.2263 0.2591 0.2444 -0.0153 0.0039  0.0189  164 LEU   A C   
3603 O O   A LEU   A 164 ? 0.1770 0.2844 0.2937 -0.0366 0.0564  0.0599  164 LEU   A O   
3604 O O   B LEU   A 164 ? 0.2274 0.2605 0.2445 -0.0152 0.0082  0.0167  164 LEU   A O   
3605 C CB  A LEU   A 164 ? 0.1575 0.2651 0.2891 -0.0309 0.0263  0.0989  164 LEU   A CB  
3606 C CB  B LEU   A 164 ? 0.2250 0.2550 0.2394 -0.0231 0.0099  0.0215  164 LEU   A CB  
3607 C CG  A LEU   A 164 ? 0.1628 0.2600 0.3003 -0.0157 0.0160  0.0832  164 LEU   A CG  
3608 C CG  B LEU   A 164 ? 0.2245 0.2524 0.2367 -0.0263 0.0115  0.0220  164 LEU   A CG  
3609 C CD1 A LEU   A 164 ? 0.1611 0.2557 0.3041 -0.0027 0.0126  0.0771  164 LEU   A CD1 
3610 C CD1 B LEU   A 164 ? 0.2237 0.2516 0.2387 -0.0259 0.0101  0.0200  164 LEU   A CD1 
3611 C CD2 A LEU   A 164 ? 0.1679 0.2594 0.3021 -0.0214 0.0157  0.0754  164 LEU   A CD2 
3612 C CD2 B LEU   A 164 ? 0.2243 0.2510 0.2320 -0.0295 0.0157  0.0245  164 LEU   A CD2 
3635 N N   A VAL   A 165 ? 0.1696 0.2746 0.2779 -0.0275 0.0324  0.0843  165 VAL   A N   
3636 N N   B VAL   A 165 ? 0.2237 0.2582 0.2438 -0.0133 0.0003  0.0186  165 VAL   A N   
3637 C CA  A VAL   A 165 ? 0.1766 0.2718 0.2683 -0.0269 0.0366  0.0923  165 VAL   A CA  
3638 C CA  B VAL   A 165 ? 0.2217 0.2564 0.2421 -0.0133 -0.0044 0.0206  165 VAL   A CA  
3639 C C   A VAL   A 165 ? 0.1646 0.2878 0.2748 -0.0230 0.0453  0.0926  165 VAL   A C   
3640 C C   B VAL   A 165 ? 0.2151 0.2554 0.2469 -0.0158 -0.0052 0.0265  165 VAL   A C   
3641 O O   A VAL   A 165 ? 0.1593 0.2856 0.2639 -0.0223 0.0381  0.0923  165 VAL   A O   
3642 O O   B VAL   A 165 ? 0.2180 0.2588 0.2598 -0.0162 -0.0098 0.0296  165 VAL   A O   
3643 C CB  A VAL   A 165 ? 0.1906 0.2616 0.2653 -0.0257 0.0370  0.0791  165 VAL   A CB  
3644 C CB  B VAL   A 165 ? 0.2263 0.2576 0.2350 -0.0105 -0.0060 0.0161  165 VAL   A CB  
3645 C CG1 A VAL   A 165 ? 0.1928 0.2648 0.2754 -0.0198 0.0360  0.0684  165 VAL   A CG1 
3646 C CG1 B VAL   A 165 ? 0.2287 0.2595 0.2323 -0.0107 -0.0071 0.0136  165 VAL   A CG1 
3647 C CG2 A VAL   A 165 ? 0.2011 0.2576 0.2703 -0.0240 0.0341  0.0756  165 VAL   A CG2 
3648 C CG2 B VAL   A 165 ? 0.2283 0.2575 0.2358 -0.0079 -0.0042 0.0135  165 VAL   A CG2 
3667 N N   A SER   A 166 ? 0.1674 0.3043 0.3008 -0.0173 0.0433  0.0962  166 SER   A N   
3668 N N   B SER   A 166 ? 0.2058 0.2515 0.2384 -0.0173 -0.0012 0.0317  166 SER   A N   
3669 C CA  A SER   A 166 ? 0.1639 0.3276 0.3220 -0.0191 0.0355  0.0837  166 SER   A CA  
3670 C CA  B SER   A 166 ? 0.1967 0.2481 0.2291 -0.0211 0.0003  0.0365  166 SER   A CA  
3671 C C   A SER   A 166 ? 0.1630 0.3466 0.3172 -0.0252 0.0131  0.0804  166 SER   A C   
3672 C C   B SER   A 166 ? 0.2116 0.2571 0.2344 -0.0289 0.0090  0.0383  166 SER   A C   
3673 O O   A SER   A 166 ? 0.1849 0.3642 0.3453 -0.0380 0.0105  0.0568  166 SER   A O   
3674 O O   B SER   A 166 ? 0.2096 0.2571 0.2298 -0.0384 0.0118  0.0455  166 SER   A O   
3675 C CB  A SER   A 166 ? 0.1864 0.3418 0.3623 -0.0000 0.0179  0.0636  166 SER   A CB  
3676 C CB  B SER   A 166 ? 0.1738 0.2383 0.2194 -0.0134 -0.0108 0.0399  166 SER   A CB  
3677 O OG  A SER   A 166 ? 0.2245 0.3481 0.3830 -0.0039 0.0162  0.0657  166 SER   A OG  
3678 O OG  B SER   A 166 ? 0.1535 0.2273 0.2058 -0.0115 -0.0174 0.0513  166 SER   A OG  
3689 N N   A SER   A 167 ? 0.1602 0.3503 0.2834 -0.0082 -0.0143 0.0880  167 SER   A N   
3690 N N   B SER   A 167 ? 0.2305 0.2664 0.2471 -0.0259 0.0109  0.0342  167 SER   A N   
3691 C CA  A SER   A 167 ? 0.1841 0.3531 0.2639 0.0023  -0.0178 0.0682  167 SER   A CA  
3692 C CA  B SER   A 167 ? 0.2468 0.2765 0.2588 -0.0227 0.0140  0.0235  167 SER   A CA  
3693 C C   A SER   A 167 ? 0.1910 0.3472 0.2534 0.0111  -0.0011 0.0592  167 SER   A C   
3694 C C   B SER   A 167 ? 0.2562 0.2835 0.2686 -0.0211 0.0115  0.0164  167 SER   A C   
3695 O O   A SER   A 167 ? 0.2159 0.3468 0.2770 0.0167  -0.0145 0.0569  167 SER   A O   
3696 O O   B SER   A 167 ? 0.2578 0.2855 0.2684 -0.0214 0.0111  0.0162  167 SER   A O   
3697 C CB  A SER   A 167 ? 0.2030 0.3627 0.2683 0.0066  -0.0142 0.0676  167 SER   A CB  
3698 C CB  B SER   A 167 ? 0.2527 0.2803 0.2627 -0.0207 0.0153  0.0195  167 SER   A CB  
3699 O OG  A SER   A 167 ? 0.2057 0.3672 0.2741 0.0034  0.0016  0.0721  167 SER   A OG  
3700 O OG  B SER   A 167 ? 0.2571 0.2833 0.2658 -0.0197 0.0160  0.0171  167 SER   A OG  
3711 N N   A PHE   A 168 ? 0.1869 0.3402 0.2435 0.0197  0.0012  0.0483  168 PHE   A N   
3712 N N   B PHE   A 168 ? 0.2640 0.2890 0.2828 -0.0182 0.0105  0.0098  168 PHE   A N   
3713 C CA  A PHE   A 168 ? 0.1902 0.3384 0.2563 0.0126  0.0105  0.0294  168 PHE   A CA  
3714 C CA  B PHE   A 168 ? 0.2735 0.2928 0.2959 -0.0164 0.0083  0.0034  168 PHE   A CA  
3715 C C   A PHE   A 168 ? 0.2034 0.3621 0.2850 0.0032  0.0518  0.0159  168 PHE   A C   
3716 C C   B PHE   A 168 ? 0.2858 0.3056 0.3233 -0.0125 0.0086  0.0004  168 PHE   A C   
3717 O O   A PHE   A 168 ? 0.2202 0.3645 0.3267 -0.0183 0.0549  0.0287  168 PHE   A O   
3718 O O   B PHE   A 168 ? 0.2875 0.3057 0.3217 -0.0139 0.0082  -0.0009 168 PHE   A O   
3719 C CB  A PHE   A 168 ? 0.1851 0.3110 0.2286 0.0020  -0.0083 0.0288  168 PHE   A CB  
3720 C CB  B PHE   A 168 ? 0.2700 0.2839 0.2829 -0.0184 0.0048  0.0033  168 PHE   A CB  
3721 C CG  A PHE   A 168 ? 0.1808 0.2890 0.2118 -0.0092 -0.0165 0.0284  168 PHE   A CG  
3722 C CG  B PHE   A 168 ? 0.2675 0.2759 0.2696 -0.0203 0.0039  0.0014  168 PHE   A CG  
3723 C CD1 A PHE   A 168 ? 0.1823 0.2888 0.2213 -0.0150 -0.0201 0.0452  168 PHE   A CD1 
3724 C CD1 B PHE   A 168 ? 0.2667 0.2730 0.2627 -0.0214 0.0016  -0.0007 168 PHE   A CD1 
3725 C CD2 A PHE   A 168 ? 0.1806 0.2777 0.1978 -0.0064 -0.0062 0.0167  168 PHE   A CD2 
3726 C CD2 B PHE   A 168 ? 0.2663 0.2723 0.2638 -0.0207 0.0044  0.0007  168 PHE   A CD2 
3727 C CE1 A PHE   A 168 ? 0.1766 0.2840 0.2072 -0.0136 -0.0257 0.0559  168 PHE   A CE1 
3728 C CE1 B PHE   A 168 ? 0.2663 0.2711 0.2579 -0.0223 0.0009  -0.0004 168 PHE   A CE1 
3729 C CE2 A PHE   A 168 ? 0.1853 0.2696 0.2028 -0.0115 -0.0025 0.0384  168 PHE   A CE2 
3730 C CE2 B PHE   A 168 ? 0.2658 0.2699 0.2585 -0.0218 0.0033  0.0005  168 PHE   A CE2 
3731 C CZ  A PHE   A 168 ? 0.1859 0.2751 0.2037 -0.0136 -0.0136 0.0539  168 PHE   A CZ  
3732 C CZ  B PHE   A 168 ? 0.2660 0.2705 0.2567 -0.0208 0.0010  -0.0006 168 PHE   A CZ  
3751 N N   A LEU   A 169 ? 0.2409 0.3818 0.3284 0.0009  0.0577  -0.0138 169 LEU   A N   
3752 N N   B LEU   A 169 ? 0.2965 0.3171 0.3501 -0.0077 0.0081  -0.0005 169 LEU   A N   
3753 C CA  A LEU   A 169 ? 0.3041 0.4076 0.4212 0.0082  0.0154  -0.0255 169 LEU   A CA  
3754 C CA  B LEU   A 169 ? 0.3068 0.3288 0.3750 -0.0034 0.0061  -0.0013 169 LEU   A CA  
3755 C C   A LEU   A 169 ? 0.3170 0.4099 0.4619 0.0065  0.0068  -0.0165 169 LEU   A C   
3756 C C   B LEU   A 169 ? 0.3069 0.3333 0.3803 -0.0021 0.0075  -0.0023 169 LEU   A C   
3757 O O   A LEU   A 169 ? 0.3253 0.4116 0.4713 0.0033  0.0073  -0.0194 169 LEU   A O   
3758 O O   B LEU   A 169 ? 0.3041 0.3339 0.3827 -0.0019 0.0062  -0.0021 169 LEU   A O   
3759 C CB  A LEU   A 169 ? 0.3455 0.4274 0.4539 0.0115  -0.0121 -0.0420 169 LEU   A CB  
3760 C CB  B LEU   A 169 ? 0.3152 0.3357 0.3920 -0.0009 0.0030  -0.0025 169 LEU   A CB  
3761 C CG  A LEU   A 169 ? 0.3760 0.4426 0.4799 0.0083  -0.0316 -0.0610 169 LEU   A CG  
3762 C CG  B LEU   A 169 ? 0.3211 0.3410 0.4071 0.0011  -0.0003 -0.0031 169 LEU   A CG  
3763 C CD1 A LEU   A 169 ? 0.3863 0.4465 0.4924 0.0088  -0.0413 -0.0638 169 LEU   A CD1 
3764 C CD1 B LEU   A 169 ? 0.3232 0.3430 0.4129 0.0016  -0.0022 -0.0036 169 LEU   A CD1 
3765 C CD2 A LEU   A 169 ? 0.3859 0.4489 0.4855 0.0053  -0.0333 -0.0689 169 LEU   A CD2 
3766 C CD2 B LEU   A 169 ? 0.3231 0.3430 0.4113 0.0015  -0.0012 -0.0020 169 LEU   A CD2 
3767 O OXT A LEU   A 169 ? 0.3036 0.4098 0.4700 0.0074  0.0082  -0.0105 169 LEU   A OXT 
3768 O OXT B LEU   A 169 ? 0.3076 0.3356 0.3816 -0.0008 0.0092  -0.0017 169 LEU   A OXT 
3791 N N   A SER   B 1   ? 0.3678 0.3615 0.4097 -0.1274 -0.0889 0.0395  1   SER   B N   
3792 N N   B SER   B 1   ? 0.3699 0.3648 0.3694 -0.0293 -0.0243 0.0114  1   SER   B N   
3793 C CA  A SER   B 1   ? 0.3484 0.3631 0.3973 -0.1374 -0.0971 0.0347  1   SER   B CA  
3794 C CA  B SER   B 1   ? 0.3666 0.3644 0.3700 -0.0300 -0.0233 0.0109  1   SER   B CA  
3795 C C   A SER   B 1   ? 0.3203 0.3631 0.3673 -0.1313 -0.1027 0.0612  1   SER   B C   
3796 C C   B SER   B 1   ? 0.3592 0.3627 0.3681 -0.0291 -0.0249 0.0170  1   SER   B C   
3797 O O   A SER   B 1   ? 0.3255 0.3613 0.3364 -0.1226 -0.0994 0.0608  1   SER   B O   
3798 O O   B SER   B 1   ? 0.3606 0.3627 0.3621 -0.0278 -0.0256 0.0157  1   SER   B O   
3799 C CB  A SER   B 1   ? 0.3601 0.3659 0.4115 -0.1409 -0.0818 0.0059  1   SER   B CB  
3800 C CB  B SER   B 1   ? 0.3692 0.3645 0.3683 -0.0305 -0.0191 0.0041  1   SER   B CB  
3801 O OG  A SER   B 1   ? 0.3769 0.3802 0.4656 -0.1366 -0.0647 -0.0030 1   SER   B OG  
3802 O OG  B SER   B 1   ? 0.3719 0.3655 0.3766 -0.0311 -0.0168 0.0003  1   SER   B OG  
3817 N N   A MET   B 2   ? 0.2985 0.3629 0.3718 -0.1268 -0.0943 0.1101  2   MET   B N   
3818 N N   B MET   B 2   ? 0.3508 0.3606 0.3697 -0.0289 -0.0251 0.0271  2   MET   B N   
3819 C CA  A MET   B 2   ? 0.2850 0.3683 0.3905 -0.1020 -0.0931 0.1318  2   MET   B CA  
3820 C CA  B MET   B 2   ? 0.3413 0.3571 0.3715 -0.0273 -0.0253 0.0355  2   MET   B CA  
3821 C C   A MET   B 2   ? 0.2549 0.3526 0.3662 -0.0807 -0.0966 0.1506  2   MET   B C   
3822 C C   B MET   B 2   ? 0.3209 0.3395 0.3406 -0.0304 -0.0257 0.0434  2   MET   B C   
3823 O O   A MET   B 2   ? 0.2464 0.3681 0.3753 -0.0635 -0.1081 0.1503  2   MET   B O   
3824 O O   B MET   B 2   ? 0.3234 0.3442 0.3424 -0.0280 -0.0227 0.0429  2   MET   B O   
3825 C CB  A MET   B 2   ? 0.3120 0.4036 0.4735 -0.0754 -0.0793 0.1054  2   MET   B CB  
3826 C CB  B MET   B 2   ? 0.3516 0.3711 0.4069 -0.0211 -0.0252 0.0346  2   MET   B CB  
3827 C CG  A MET   B 2   ? 0.3378 0.4342 0.5550 -0.0508 -0.0600 0.0921  2   MET   B CG  
3828 C CG  B MET   B 2   ? 0.3605 0.3836 0.4399 -0.0156 -0.0249 0.0364  2   MET   B CG  
3829 S SD  A MET   B 2   ? 0.3671 0.4677 0.6383 -0.0280 -0.0407 0.0770  2   MET   B SD  
3830 S SD  B MET   B 2   ? 0.3681 0.3954 0.4681 -0.0105 -0.0257 0.0388  2   MET   B SD  
3831 C CE  A MET   B 2   ? 0.3671 0.4706 0.6298 -0.0261 -0.0325 0.0776  2   MET   B CE  
3832 C CE  B MET   B 2   ? 0.3695 0.3977 0.4743 -0.0107 -0.0235 0.0363  2   MET   B CE  
3851 N N   A VAL   B 3   ? 0.2273 0.3081 0.3367 -0.0949 -0.0866 0.1616  3   VAL   B N   
3852 N N   B VAL   B 3   ? 0.2961 0.3149 0.3077 -0.0374 -0.0301 0.0519  3   VAL   B N   
3853 C CA  A VAL   B 3   ? 0.2254 0.2746 0.3341 -0.0828 -0.0757 0.1390  3   VAL   B CA  
3854 C CA  B VAL   B 3   ? 0.2717 0.2898 0.2807 -0.0424 -0.0351 0.0594  3   VAL   B CA  
3855 C C   A VAL   B 3   ? 0.2157 0.2595 0.2855 -0.0677 -0.0663 0.1203  3   VAL   B C   
3856 C C   B VAL   B 3   ? 0.2439 0.2640 0.2534 -0.0499 -0.0463 0.0733  3   VAL   B C   
3857 O O   A VAL   B 3   ? 0.2117 0.2732 0.3021 -0.0650 -0.0667 0.1259  3   VAL   B O   
3858 O O   B VAL   B 3   ? 0.2432 0.2679 0.2466 -0.0457 -0.0464 0.0758  3   VAL   B O   
3859 C CB  A VAL   B 3   ? 0.2479 0.2689 0.3891 -0.0781 -0.0701 0.1212  3   VAL   B CB  
3860 C CB  B VAL   B 3   ? 0.2760 0.2905 0.2856 -0.0409 -0.0288 0.0533  3   VAL   B CB  
3861 C CG1 A VAL   B 3   ? 0.2600 0.2595 0.4103 -0.0807 -0.0725 0.1125  3   VAL   B CG1 
3862 C CG1 B VAL   B 3   ? 0.2781 0.2899 0.2881 -0.0409 -0.0275 0.0499  3   VAL   B CG1 
3863 C CG2 A VAL   B 3   ? 0.2536 0.2700 0.4057 -0.0738 -0.0611 0.1328  3   VAL   B CG2 
3864 C CG2 B VAL   B 3   ? 0.2775 0.2912 0.2865 -0.0397 -0.0268 0.0537  3   VAL   B CG2 
3883 N N   . ASN   B 4   ? 0.2173 0.2330 0.2394 -0.0629 -0.0597 0.0856  4   ASN   B N   
3884 C CA  . ASN   B 4   ? 0.2147 0.2224 0.2006 -0.0640 -0.0550 0.0456  4   ASN   B CA  
3885 C C   . ASN   B 4   ? 0.2260 0.2374 0.1913 -0.0632 -0.0396 0.0284  4   ASN   B C   
3886 O O   . ASN   B 4   ? 0.2278 0.2446 0.2164 -0.0579 -0.0384 0.0105  4   ASN   B O   
3887 C CB  . ASN   B 4   ? 0.2147 0.2137 0.1927 -0.0528 -0.0592 0.0460  4   ASN   B CB  
3888 C CG  . ASN   B 4   ? 0.2049 0.2014 0.1775 -0.0493 -0.0592 0.0325  4   ASN   B CG  
3889 O OD1 . ASN   B 4   ? 0.2022 0.1904 0.1830 -0.0477 -0.0542 0.0292  4   ASN   B OD1 
3890 N ND2 . ASN   B 4   ? 0.2260 0.2077 0.1972 -0.0267 -0.0358 0.0333  4   ASN   B ND2 
3898 N N   . SER   B 5   ? 0.2374 0.2553 0.2071 -0.0637 -0.0191 0.0301  5   SER   B N   
3899 C CA  . SER   B 5   ? 0.2639 0.2871 0.2436 -0.0525 -0.0000 0.0357  5   SER   B CA  
3900 C C   . SER   B 5   ? 0.2802 0.2922 0.2803 -0.0712 0.0363  0.0307  5   SER   B C   
3901 O O   . SER   B 5   ? 0.2981 0.2920 0.3581 -0.0647 0.0735  0.0312  5   SER   B O   
3902 C CB  . SER   B 5   ? 0.2776 0.3092 0.2749 -0.0392 -0.0056 0.0478  5   SER   B CB  
3903 O OG  . SER   B 5   ? 0.3054 0.3342 0.3303 -0.0275 0.0009  0.0539  5   SER   B OG  
3909 N N   . PHE   B 6   ? 0.2968 0.3111 0.2517 -0.0756 0.0475  0.0329  6   PHE   B N   
3910 C CA  . PHE   B 6   ? 0.3071 0.3168 0.2113 -0.0944 0.0455  0.0186  6   PHE   B CA  
3911 C C   . PHE   B 6   ? 0.3611 0.3522 0.2554 -0.1019 0.0640  -0.0104 6   PHE   B C   
3912 O O   . PHE   B 6   ? 0.3751 0.3885 0.2890 -0.0945 0.0383  -0.0338 6   PHE   B O   
3913 C CB  . PHE   B 6   ? 0.2733 0.2940 0.1782 -0.0831 0.0194  0.0163  6   PHE   B CB  
3914 C CG  . PHE   B 6   ? 0.2375 0.2647 0.1786 -0.0769 0.0015  0.0076  6   PHE   B CG  
3915 C CD1 . PHE   B 6   ? 0.2342 0.2375 0.1711 -0.0706 -0.0149 0.0058  6   PHE   B CD1 
3916 C CD2 . PHE   B 6   ? 0.2181 0.2627 0.1708 -0.0599 0.0017  0.0346  6   PHE   B CD2 
3917 C CE1 . PHE   B 6   ? 0.2308 0.2154 0.1716 -0.0568 -0.0157 0.0037  6   PHE   B CE1 
3918 C CE2 . PHE   B 6   ? 0.2156 0.2510 0.2041 -0.0480 0.0007  0.0279  6   PHE   B CE2 
3919 C CZ  . PHE   B 6   ? 0.2249 0.2248 0.1816 -0.0507 -0.0010 0.0115  6   PHE   B CZ  
3929 N N   . SER   B 7   ? 0.3977 0.3350 0.2573 -0.1241 0.1032  -0.0314 7   SER   B N   
3930 C CA  . SER   B 7   ? 0.4337 0.3531 0.3148 -0.1211 0.1212  -0.0411 7   SER   B CA  
3931 C C   . SER   B 7   ? 0.4284 0.3348 0.3034 -0.1222 0.1367  -0.0541 7   SER   B C   
3932 O O   . SER   B 7   ? 0.4323 0.3384 0.3353 -0.1231 0.1327  -0.0515 7   SER   B O   
3933 C CB  . SER   B 7   ? 0.4609 0.3776 0.3874 -0.1148 0.1303  -0.0373 7   SER   B CB  
3934 O OG  . SER   B 7   ? 0.4775 0.3884 0.4497 -0.1100 0.1280  -0.0255 7   SER   B OG  
3940 N N   . GLY   B 8   ? 0.4244 0.3228 0.3124 -0.1068 0.1459  -0.0601 8   GLY   B N   
3941 C CA  . GLY   B 8   ? 0.4100 0.3042 0.3168 -0.0983 0.1488  -0.0691 8   GLY   B CA  
3942 C C   . GLY   B 8   ? 0.3862 0.2755 0.3130 -0.0972 0.1514  -0.0608 8   GLY   B C   
3943 O O   . GLY   B 8   ? 0.3967 0.2855 0.3549 -0.0833 0.1529  -0.0721 8   GLY   B O   
3947 N N   . TYR   B 9   ? 0.3593 0.2510 0.2750 -0.0890 0.1257  -0.0721 9   TYR   B N   
3948 C CA  . TYR   B 9   ? 0.3327 0.2241 0.2465 -0.0734 0.0925  -0.0561 9   TYR   B CA  
3949 C C   . TYR   B 9   ? 0.3280 0.2296 0.2306 -0.0671 0.0526  -0.0444 9   TYR   B C   
3950 O O   . TYR   B 9   ? 0.3462 0.2515 0.2748 -0.0665 0.0596  -0.0290 9   TYR   B O   
3951 C CB  . TYR   B 9   ? 0.3216 0.2034 0.2595 -0.0651 0.0809  -0.0502 9   TYR   B CB  
3952 C CG  . TYR   B 9   ? 0.3100 0.1876 0.2520 -0.0716 0.0749  -0.0591 9   TYR   B CG  
3953 C CD1 . TYR   B 9   ? 0.3090 0.1940 0.2714 -0.0843 0.0796  -0.0491 9   TYR   B CD1 
3954 C CD2 . TYR   B 9   ? 0.2968 0.1870 0.2439 -0.0647 0.0720  -0.0616 9   TYR   B CD2 
3955 C CE1 . TYR   B 9   ? 0.3001 0.2077 0.2733 -0.0953 0.0850  -0.0510 9   TYR   B CE1 
3956 C CE2 . TYR   B 9   ? 0.2966 0.1849 0.2612 -0.0699 0.0673  -0.0551 9   TYR   B CE2 
3957 C CZ  . TYR   B 9   ? 0.2979 0.2075 0.2763 -0.0838 0.0716  -0.0707 9   TYR   B CZ  
3958 O OH  . TYR   B 9   ? 0.2974 0.2193 0.2958 -0.0937 0.0722  -0.0844 9   TYR   B OH  
3968 N N   . LEU   B 10  ? 0.3035 0.2113 0.1925 -0.0685 0.0268  -0.0437 10  LEU   B N   
3969 C CA  . LEU   B 10  ? 0.3019 0.2069 0.1924 -0.0779 -0.0052 -0.0316 10  LEU   B CA  
3970 C C   . LEU   B 10  ? 0.2840 0.2122 0.1942 -0.0745 -0.0233 -0.0232 10  LEU   B C   
3971 O O   . LEU   B 10  ? 0.2698 0.2197 0.1980 -0.0568 -0.0116 -0.0235 10  LEU   B O   
3972 C CB  . LEU   B 10  ? 0.3212 0.2092 0.2150 -0.0794 -0.0221 -0.0144 10  LEU   B CB  
3973 C CG  . LEU   B 10  ? 0.3452 0.2170 0.2510 -0.0726 -0.0652 -0.0046 10  LEU   B CG  
3974 C CD1 . LEU   B 10  ? 0.3597 0.2258 0.2797 -0.0692 -0.0675 -0.0095 10  LEU   B CD1 
3975 C CD2 . LEU   B 10  ? 0.3554 0.2237 0.2858 -0.0747 -0.0569 0.0144  10  LEU   B CD2 
3987 N N   . LYS   B 11  ? 0.2984 0.2378 0.2022 -0.0672 -0.0362 -0.0201 11  LYS   B N   
3988 C CA  . LYS   B 11  ? 0.3123 0.2646 0.2370 -0.0535 -0.0458 -0.0257 11  LYS   B CA  
3989 C C   . LYS   B 11  ? 0.2959 0.2382 0.2468 -0.0774 -0.0352 -0.0431 11  LYS   B C   
3990 O O   . LYS   B 11  ? 0.3143 0.2618 0.2803 -0.0896 -0.0251 -0.0772 11  LYS   B O   
3991 C CB  . LYS   B 11  ? 0.3414 0.3191 0.3030 -0.0171 -0.0486 -0.0191 11  LYS   B CB  
3992 C CG  . LYS   B 11  ? 0.3701 0.3569 0.3758 0.0031  -0.0508 -0.0138 11  LYS   B CG  
3993 C CD  . LYS   B 11  ? 0.3928 0.3817 0.4476 0.0121  -0.0484 -0.0165 11  LYS   B CD  
3994 C CE  . LYS   B 11  ? 0.4098 0.3970 0.5011 0.0132  -0.0463 -0.0128 11  LYS   B CE  
3995 N NZ  . LYS   B 11  ? 0.4196 0.4061 0.5269 0.0131  -0.0458 -0.0090 11  LYS   B NZ  
4009 N N   . LEU   B 12  ? 0.2637 0.2099 0.2419 -0.0636 -0.0306 -0.0408 12  LEU   B N   
4010 C CA  . LEU   B 12  ? 0.2474 0.1910 0.2648 -0.0557 -0.0305 -0.0352 12  LEU   B CA  
4011 C C   . LEU   B 12  ? 0.2356 0.1898 0.2702 -0.0602 -0.0447 -0.0352 12  LEU   B C   
4012 O O   . LEU   B 12  ? 0.2361 0.1944 0.2878 -0.0654 -0.0476 -0.0233 12  LEU   B O   
4013 C CB  . LEU   B 12  ? 0.2417 0.1724 0.2658 -0.0460 -0.0185 -0.0378 12  LEU   B CB  
4014 C CG  . LEU   B 12  ? 0.2389 0.1752 0.2660 -0.0430 -0.0113 -0.0330 12  LEU   B CG  
4015 C CD1 . LEU   B 12  ? 0.2466 0.1843 0.2530 -0.0268 -0.0097 -0.0192 12  LEU   B CD1 
4016 C CD2 . LEU   B 12  ? 0.2438 0.1833 0.2849 -0.0422 0.0014  -0.0403 12  LEU   B CD2 
4028 N N   . THR   B 13  ? 0.2237 0.1914 0.2705 -0.0531 -0.0416 -0.0412 13  THR   B N   
4029 C CA  . THR   B 13  ? 0.2269 0.2063 0.2572 -0.0633 -0.0538 -0.0310 13  THR   B CA  
4030 C C   . THR   B 13  ? 0.2696 0.2268 0.2791 -0.0687 -0.0615 -0.0252 13  THR   B C   
4031 O O   . THR   B 13  ? 0.2918 0.2262 0.2885 -0.0699 -0.0267 -0.0182 13  THR   B O   
4032 C CB  . THR   B 13  ? 0.2141 0.2076 0.2620 -0.0550 -0.0488 -0.0154 13  THR   B CB  
4033 O OG1 . THR   B 13  ? 0.2068 0.2020 0.2632 -0.0499 -0.0377 -0.0163 13  THR   B OG1 
4034 C CG2 . THR   B 13  ? 0.2259 0.2143 0.2697 -0.0455 -0.0307 -0.0030 13  THR   B CG2 
4042 N N   A ASP   B 14  ? 0.2839 0.2433 0.2955 -0.0759 -0.0958 -0.0111 14  ASP   B N   
4043 N N   B ASP   B 14  ? 0.2738 0.2341 0.2923 -0.0663 -0.0637 -0.0161 14  ASP   B N   
4044 C CA  A ASP   B 14  ? 0.2990 0.2695 0.3208 -0.0769 -0.1026 0.0165  14  ASP   B CA  
4045 C CA  B ASP   B 14  ? 0.2781 0.2427 0.3077 -0.0634 -0.0623 -0.0053 14  ASP   B CA  
4046 C C   A ASP   B 14  ? 0.2882 0.2483 0.2831 -0.0824 -0.0836 0.0219  14  ASP   B C   
4047 C C   B ASP   B 14  ? 0.2662 0.2293 0.2774 -0.0644 -0.0683 0.0043  14  ASP   B C   
4048 O O   A ASP   B 14  ? 0.3211 0.2708 0.2891 -0.0893 -0.0819 0.0394  14  ASP   B O   
4049 O O   B ASP   B 14  ? 0.2723 0.2314 0.2768 -0.0636 -0.0690 0.0061  14  ASP   B O   
4050 C CB  A ASP   B 14  ? 0.3237 0.3166 0.3999 -0.0668 -0.1179 0.0202  14  ASP   B CB  
4051 C CB  B ASP   B 14  ? 0.2937 0.2638 0.3544 -0.0585 -0.0547 -0.0070 14  ASP   B CB  
4052 C CG  A ASP   B 14  ? 0.3550 0.3595 0.4832 -0.0482 -0.1120 0.0066  14  ASP   B CG  
4053 C CG  B ASP   B 14  ? 0.3089 0.2815 0.3952 -0.0526 -0.0471 -0.0122 14  ASP   B CG  
4054 O OD1 A ASP   B 14  ? 0.3739 0.3778 0.4989 -0.0465 -0.1100 -0.0136 14  ASP   B OD1 
4055 O OD1 B ASP   B 14  ? 0.3153 0.2898 0.4062 -0.0514 -0.0448 -0.0166 14  ASP   B OD1 
4056 O OD2 A ASP   B 14  ? 0.3599 0.3780 0.5256 -0.0414 -0.1121 0.0117  14  ASP   B OD2 
4057 O OD2 B ASP   B 14  ? 0.3132 0.2869 0.4097 -0.0515 -0.0465 -0.0131 14  ASP   B OD2 
4066 N N   . ASN   B 15  ? 0.2487 0.2127 0.2522 -0.0623 -0.0769 0.0150  15  ASN   B N   
4067 C CA  . ASN   B 15  ? 0.2008 0.1821 0.2368 -0.0405 -0.0496 0.0062  15  ASN   B CA  
4068 C C   . ASN   B 15  ? 0.1803 0.1627 0.2197 -0.0249 -0.0400 0.0002  15  ASN   B C   
4069 O O   . ASN   B 15  ? 0.1812 0.1597 0.2457 -0.0245 -0.0499 -0.0145 15  ASN   B O   
4070 C CB  . ASN   B 15  ? 0.1900 0.1828 0.2656 -0.0182 -0.0497 0.0135  15  ASN   B CB  
4071 C CG  . ASN   B 15  ? 0.1764 0.1739 0.2551 -0.0263 -0.0294 0.0112  15  ASN   B CG  
4072 O OD1 . ASN   B 15  ? 0.1895 0.2051 0.2895 -0.0464 -0.0304 0.0118  15  ASN   B OD1 
4073 N ND2 . ASN   B 15  ? 0.1789 0.1616 0.2449 -0.0163 0.0029  -0.0123 15  ASN   B ND2 
4081 N N   . VAL   B 16  ? 0.1818 0.1621 0.2218 -0.0363 -0.0498 -0.0054 16  VAL   B N   
4082 C CA  . VAL   B 16  ? 0.1784 0.1617 0.2127 -0.0309 -0.0303 -0.0213 16  VAL   B CA  
4083 C C   . VAL   B 16  ? 0.1792 0.1773 0.2117 -0.0386 -0.0361 -0.0109 16  VAL   B C   
4084 O O   . VAL   B 16  ? 0.1814 0.1882 0.2463 -0.0320 -0.0283 -0.0299 16  VAL   B O   
4085 C CB  . VAL   B 16  ? 0.1860 0.1560 0.2144 -0.0162 -0.0187 -0.0190 16  VAL   B CB  
4086 C CG1 . VAL   B 16  ? 0.1952 0.1485 0.2105 -0.0003 -0.0141 -0.0149 16  VAL   B CG1 
4087 C CG2 . VAL   B 16  ? 0.1923 0.1632 0.2409 -0.0040 -0.0090 -0.0179 16  VAL   B CG2 
4097 N N   . TYR   B 17  ? 0.1848 0.1843 0.2026 -0.0356 -0.0197 -0.0183 17  TYR   B N   
4098 C CA  . TYR   B 17  ? 0.1935 0.1936 0.1927 -0.0381 -0.0242 -0.0102 17  TYR   B CA  
4099 C C   . TYR   B 17  ? 0.1856 0.1666 0.1960 -0.0410 -0.0136 -0.0191 17  TYR   B C   
4100 O O   . TYR   B 17  ? 0.1880 0.1741 0.2088 -0.0378 -0.0280 -0.0364 17  TYR   B O   
4101 C CB  . TYR   B 17  ? 0.2255 0.2403 0.2205 -0.0299 -0.0175 0.0306  17  TYR   B CB  
4102 C CG  . TYR   B 17  ? 0.2578 0.2914 0.2579 -0.0194 -0.0298 0.0339  17  TYR   B CG  
4103 C CD1 . TYR   B 17  ? 0.2775 0.3104 0.2848 -0.0126 -0.0460 0.0421  17  TYR   B CD1 
4104 C CD2 . TYR   B 17  ? 0.2827 0.3225 0.2711 -0.0066 -0.0417 0.0286  17  TYR   B CD2 
4105 C CE1 . TYR   B 17  ? 0.2999 0.3371 0.2965 -0.0013 -0.0547 0.0350  17  TYR   B CE1 
4106 C CE2 . TYR   B 17  ? 0.3025 0.3467 0.2926 0.0081  -0.0610 0.0336  17  TYR   B CE2 
4107 C CZ  . TYR   B 17  ? 0.3125 0.3538 0.2995 0.0106  -0.0668 0.0337  17  TYR   B CZ  
4108 O OH  . TYR   B 17  ? 0.3275 0.3700 0.3168 0.0199  -0.0729 0.0381  17  TYR   B OH  
4118 N N   . ILE   B 18  ? 0.2030 0.1715 0.1800 -0.0352 -0.0045 -0.0204 18  ILE   B N   
4119 C CA  . ILE   B 18  ? 0.2041 0.1677 0.1785 -0.0383 -0.0037 -0.0229 18  ILE   B CA  
4120 C C   . ILE   B 18  ? 0.2190 0.1687 0.1781 -0.0478 -0.0012 -0.0358 18  ILE   B C   
4121 O O   . ILE   B 18  ? 0.2378 0.1779 0.1927 -0.0430 0.0134  -0.0433 18  ILE   B O   
4122 C CB  . ILE   B 18  ? 0.2068 0.1703 0.1962 -0.0447 -0.0080 -0.0186 18  ILE   B CB  
4123 C CG1 . ILE   B 18  ? 0.2153 0.1803 0.2081 -0.0428 -0.0136 0.0009  18  ILE   B CG1 
4124 C CG2 . ILE   B 18  ? 0.2147 0.1708 0.2050 -0.0515 -0.0141 -0.0120 18  ILE   B CG2 
4125 C CD1 . ILE   B 18  ? 0.2210 0.2037 0.2344 -0.0466 -0.0264 0.0230  18  ILE   B CD1 
4137 N N   . LYS   B 19  ? 0.2151 0.1691 0.2022 -0.0277 0.0309  -0.0357 19  LYS   B N   
4138 C CA  . LYS   B 19  ? 0.2230 0.1747 0.2205 -0.0336 0.0342  -0.0355 19  LYS   B CA  
4139 C C   . LYS   B 19  ? 0.2084 0.1744 0.2295 -0.0303 0.0376  -0.0517 19  LYS   B C   
4140 O O   . LYS   B 19  ? 0.2067 0.1826 0.2136 -0.0199 0.0237  -0.0471 19  LYS   B O   
4141 C CB  . LYS   B 19  ? 0.2519 0.1964 0.2303 -0.0406 0.0397  -0.0276 19  LYS   B CB  
4142 C CG  . LYS   B 19  ? 0.2817 0.2134 0.2593 -0.0468 0.0472  -0.0311 19  LYS   B CG  
4143 C CD  . LYS   B 19  ? 0.3108 0.2470 0.2787 -0.0479 0.0621  -0.0228 19  LYS   B CD  
4144 C CE  . LYS   B 19  ? 0.3394 0.2763 0.3037 -0.0522 0.0614  -0.0242 19  LYS   B CE  
4145 N NZ  . LYS   B 19  ? 0.3606 0.2961 0.3135 -0.0563 0.0650  -0.0183 19  LYS   B NZ  
4159 N N   . ASN   B 20  ? 0.2197 0.1858 0.2636 -0.0189 0.0444  -0.0626 20  ASN   B N   
4160 C CA  . ASN   B 20  ? 0.2208 0.1891 0.2949 -0.0126 0.0517  -0.0838 20  ASN   B CA  
4161 C C   . ASN   B 20  ? 0.2156 0.2162 0.2998 -0.0263 0.0578  -0.0936 20  ASN   B C   
4162 O O   . ASN   B 20  ? 0.2357 0.2612 0.3144 -0.0399 0.0678  -0.0928 20  ASN   B O   
4163 C CB  . ASN   B 20  ? 0.2506 0.1945 0.3292 0.0134  0.0378  -0.0838 20  ASN   B CB  
4164 C CG  . ASN   B 20  ? 0.2756 0.2124 0.3407 0.0460  0.0412  -0.0906 20  ASN   B CG  
4165 O OD1 . ASN   B 20  ? 0.3062 0.2491 0.3685 0.0632  0.0266  -0.0954 20  ASN   B OD1 
4166 N ND2 . ASN   B 20  ? 0.2674 0.2145 0.3300 0.0475  0.0355  -0.0798 20  ASN   B ND2 
4173 N N   . ALA   B 21  ? 0.2135 0.1950 0.2977 -0.0393 0.0548  -0.0751 21  ALA   B N   
4174 C CA  . ALA   B 21  ? 0.2254 0.2033 0.3088 -0.0344 0.0420  -0.0652 21  ALA   B CA  
4175 C C   . ALA   B 21  ? 0.2181 0.1831 0.2993 -0.0311 0.0432  -0.0568 21  ALA   B C   
4176 O O   . ALA   B 21  ? 0.2224 0.1835 0.2884 -0.0368 0.0495  -0.0521 21  ALA   B O   
4177 C CB  . ALA   B 21  ? 0.2415 0.2317 0.3092 -0.0486 0.0423  -0.0485 21  ALA   B CB  
4183 N N   . ASP   B 22  ? 0.2045 0.1652 0.3098 -0.0273 0.0313  -0.0382 22  ASP   B N   
4184 C CA  . ASP   B 22  ? 0.1948 0.1547 0.2999 -0.0154 0.0246  -0.0252 22  ASP   B CA  
4185 C C   . ASP   B 22  ? 0.1972 0.1460 0.2465 -0.0161 0.0206  -0.0120 22  ASP   B C   
4186 O O   . ASP   B 22  ? 0.2056 0.1610 0.2400 -0.0124 0.0137  -0.0088 22  ASP   B O   
4187 C CB  . ASP   B 22  ? 0.2086 0.1748 0.3321 -0.0060 0.0305  -0.0121 22  ASP   B CB  
4188 C CG  . ASP   B 22  ? 0.2167 0.2015 0.3646 0.0058  0.0018  -0.0079 22  ASP   B CG  
4189 O OD1 . ASP   B 22  ? 0.2287 0.1994 0.3663 0.0123  -0.0193 -0.0005 22  ASP   B OD1 
4190 O OD2 . ASP   B 22  ? 0.2266 0.2303 0.4022 0.0179  -0.0206 -0.0230 22  ASP   B OD2 
4195 N N   . ILE   B 23  ? 0.1952 0.1553 0.2168 -0.0117 0.0080  0.0105  23  ILE   B N   
4196 C CA  . ILE   B 23  ? 0.1861 0.1611 0.1879 -0.0051 -0.0049 0.0077  23  ILE   B CA  
4197 C C   . ILE   B 23  ? 0.1771 0.1659 0.1759 -0.0018 -0.0129 0.0060  23  ILE   B C   
4198 O O   . ILE   B 23  ? 0.1689 0.1681 0.1761 -0.0044 -0.0067 0.0104  23  ILE   B O   
4199 C CB  . ILE   B 23  ? 0.1769 0.1700 0.2012 -0.0135 0.0007  0.0118  23  ILE   B CB  
4200 C CG1 . ILE   B 23  ? 0.1767 0.1780 0.2219 -0.0007 0.0107  0.0189  23  ILE   B CG1 
4201 C CG2 . ILE   B 23  ? 0.1934 0.1852 0.2147 -0.0191 0.0007  0.0094  23  ILE   B CG2 
4202 C CD1 . ILE   B 23  ? 0.1876 0.1849 0.2259 0.0012  0.0041  0.0159  23  ILE   B CD1 
4214 N N   . VAL   B 24  ? 0.1788 0.1673 0.1889 -0.0047 -0.0123 -0.0010 24  VAL   B N   
4215 C CA  . VAL   B 24  ? 0.1740 0.1700 0.2148 -0.0066 -0.0120 0.0026  24  VAL   B CA  
4216 C C   . VAL   B 24  ? 0.1704 0.1763 0.2264 -0.0104 0.0009  0.0081  24  VAL   B C   
4217 O O   . VAL   B 24  ? 0.1688 0.1912 0.2312 -0.0211 -0.0007 0.0204  24  VAL   B O   
4218 C CB  . VAL   B 24  ? 0.1848 0.1852 0.2214 0.0022  -0.0247 0.0107  24  VAL   B CB  
4219 C CG1 . VAL   B 24  ? 0.1871 0.1875 0.2502 0.0003  -0.0209 0.0100  24  VAL   B CG1 
4220 C CG2 . VAL   B 24  ? 0.1947 0.2128 0.2207 0.0037  -0.0236 -0.0003 24  VAL   B CG2 
4230 N N   . GLU   B 25  ? 0.1914 0.1873 0.2377 -0.0081 0.0063  0.0004  25  GLU   B N   
4231 C CA  . GLU   B 25  ? 0.2185 0.2078 0.2567 0.0052  0.0171  -0.0068 25  GLU   B CA  
4232 C C   . GLU   B 25  ? 0.2106 0.1926 0.2168 -0.0135 0.0228  0.0020  25  GLU   B C   
4233 O O   . GLU   B 25  ? 0.2115 0.2131 0.2380 -0.0108 0.0246  0.0043  25  GLU   B O   
4234 C CB  . GLU   B 25  ? 0.2593 0.2567 0.3225 0.0377  0.0247  -0.0122 25  GLU   B CB  
4235 C CG  . GLU   B 25  ? 0.3054 0.3228 0.4348 0.0474  0.0239  -0.0167 25  GLU   B CG  
4236 C CD  . GLU   B 25  ? 0.3593 0.3851 0.5320 0.0432  0.0202  -0.0197 25  GLU   B CD  
4237 O OE1 . GLU   B 25  ? 0.3810 0.4102 0.5632 0.0477  0.0254  -0.0179 25  GLU   B OE1 
4238 O OE2 . GLU   B 25  ? 0.3795 0.4032 0.5666 0.0416  0.0147  -0.0287 25  GLU   B OE2 
4245 N N   A GLU   B 26  ? 0.2120 0.1903 0.1943 -0.0305 0.0221  -0.0035 26  GLU   B N   
4246 N N   B GLU   B 26  ? 0.2049 0.1910 0.2079 -0.0225 0.0185  0.0043  26  GLU   B N   
4247 C CA  A GLU   B 26  ? 0.2098 0.1982 0.2003 -0.0381 0.0042  0.0042  26  GLU   B CA  
4248 C CA  B GLU   B 26  ? 0.1981 0.1900 0.2066 -0.0307 0.0149  0.0106  26  GLU   B CA  
4249 C C   A GLU   B 26  ? 0.1848 0.1950 0.1907 -0.0284 0.0099  0.0162  26  GLU   B C   
4250 C C   B GLU   B 26  ? 0.1835 0.1882 0.1976 -0.0274 0.0130  0.0152  26  GLU   B C   
4251 O O   A GLU   B 26  ? 0.1993 0.2191 0.2016 -0.0251 0.0003  0.0222  26  GLU   B O   
4252 O O   B GLU   B 26  ? 0.1880 0.1940 0.1987 -0.0245 0.0103  0.0156  26  GLU   B O   
4253 C CB  A GLU   B 26  ? 0.2426 0.2215 0.2419 -0.0539 0.0112  0.0129  26  GLU   B CB  
4254 C CB  B GLU   B 26  ? 0.2063 0.1919 0.2200 -0.0425 0.0205  0.0160  26  GLU   B CB  
4255 C CG  A GLU   B 26  ? 0.2772 0.2609 0.3079 -0.0553 0.0114  -0.0135 26  GLU   B CG  
4256 C CG  B GLU   B 26  ? 0.2136 0.1966 0.2375 -0.0520 0.0289  0.0182  26  GLU   B CG  
4257 C CD  A GLU   B 26  ? 0.2933 0.2836 0.3235 -0.0711 0.0266  -0.0453 26  GLU   B CD  
4258 C CD  B GLU   B 26  ? 0.2151 0.1993 0.2399 -0.0661 0.0503  0.0253  26  GLU   B CD  
4259 O OE1 A GLU   B 26  ? 0.2992 0.2809 0.3288 -0.0846 0.0651  -0.0471 26  GLU   B OE1 
4260 O OE1 B GLU   B 26  ? 0.2168 0.1972 0.2331 -0.0685 0.0686  0.0398  26  GLU   B OE1 
4261 O OE2 A GLU   B 26  ? 0.2954 0.3115 0.3704 -0.0645 0.0206  -0.0447 26  GLU   B OE2 
4262 O OE2 B GLU   B 26  ? 0.2109 0.2004 0.2499 -0.0757 0.0582  0.0346  26  GLU   B OE2 
4275 N N   . ALA   B 27  ? 0.1669 0.1811 0.1963 -0.0278 0.0130  0.0204  27  ALA   B N   
4276 C CA  . ALA   B 27  ? 0.1794 0.1736 0.2103 -0.0184 -0.0047 0.0311  27  ALA   B CA  
4277 C C   . ALA   B 27  ? 0.1843 0.1818 0.2284 -0.0099 0.0138  0.0417  27  ALA   B C   
4278 O O   . ALA   B 27  ? 0.1837 0.1952 0.2418 -0.0006 0.0198  0.0495  27  ALA   B O   
4279 C CB  . ALA   B 27  ? 0.1964 0.1637 0.2177 -0.0140 0.0052  0.0314  27  ALA   B CB  
4286 N N   . LYS   B 28  ? 0.1851 0.1914 0.2766 -0.0181 0.0212  0.0627  28  LYS   B N   
4287 C CA  . LYS   B 28  ? 0.2033 0.2312 0.2968 -0.0064 0.0555  0.0843  28  LYS   B CA  
4288 C C   . LYS   B 28  ? 0.2330 0.2632 0.2821 0.0072  0.0695  0.0815  28  LYS   B C   
4289 O O   . LYS   B 28  ? 0.2506 0.2707 0.2973 0.0062  0.0746  0.0752  28  LYS   B O   
4290 C CB  . LYS   B 28  ? 0.2204 0.2625 0.3579 0.0076  0.0701  0.0998  28  LYS   B CB  
4291 C CG  . LYS   B 28  ? 0.2388 0.3126 0.3987 0.0195  0.0703  0.1022  28  LYS   B CG  
4292 C CD  . LYS   B 28  ? 0.2823 0.3741 0.4529 0.0280  0.0816  0.0989  28  LYS   B CD  
4293 C CE  . LYS   B 28  ? 0.3120 0.4152 0.4960 0.0403  0.0854  0.1030  28  LYS   B CE  
4294 N NZ  . LYS   B 28  ? 0.3172 0.4287 0.5140 0.0553  0.0837  0.1096  28  LYS   B NZ  
4308 N N   A LYS   B 29  ? 0.2481 0.2786 0.2886 0.0301  0.0714  0.0662  29  LYS   B N   
4309 N N   B LYS   B 29  ? 0.2523 0.2850 0.2948 0.0103  0.0589  0.0710  29  LYS   B N   
4310 C CA  A LYS   B 29  ? 0.2880 0.3103 0.3160 0.0287  0.0663  0.0595  29  LYS   B CA  
4311 C CA  B LYS   B 29  ? 0.2741 0.3080 0.3142 0.0102  0.0477  0.0617  29  LYS   B CA  
4312 C C   A LYS   B 29  ? 0.2801 0.3132 0.2881 0.0274  0.0491  0.0671  29  LYS   B C   
4313 C C   B LYS   B 29  ? 0.2677 0.3067 0.2878 0.0113  0.0422  0.0637  29  LYS   B C   
4314 O O   A LYS   B 29  ? 0.2909 0.3355 0.2994 0.0345  0.0515  0.0673  29  LYS   B O   
4315 O O   B LYS   B 29  ? 0.2712 0.3126 0.2868 0.0131  0.0425  0.0646  29  LYS   B O   
4316 C CB  A LYS   B 29  ? 0.3388 0.3453 0.3854 0.0225  0.0601  0.0416  29  LYS   B CB  
4317 C CB  B LYS   B 29  ? 0.3022 0.3323 0.3651 0.0089  0.0383  0.0491  29  LYS   B CB  
4318 C CG  A LYS   B 29  ? 0.3789 0.3727 0.4682 0.0157  0.0539  0.0337  29  LYS   B CG  
4319 C CG  B LYS   B 29  ? 0.3253 0.3518 0.4178 0.0079  0.0300  0.0387  29  LYS   B CG  
4320 C CD  A LYS   B 29  ? 0.4130 0.3899 0.5297 0.0069  0.0587  0.0279  29  LYS   B CD  
4321 C CD  B LYS   B 29  ? 0.3437 0.3664 0.4600 0.0064  0.0254  0.0301  29  LYS   B CD  
4322 C CE  A LYS   B 29  ? 0.4374 0.3997 0.5712 0.0004  0.0667  0.0236  29  LYS   B CE  
4323 C CE  B LYS   B 29  ? 0.3566 0.3765 0.4887 0.0051  0.0236  0.0237  29  LYS   B CE  
4324 N NZ  A LYS   B 29  ? 0.4458 0.4055 0.6010 -0.0019 0.0691  0.0214  29  LYS   B NZ  
4325 N NZ  B LYS   B 29  ? 0.3624 0.3814 0.5077 0.0048  0.0227  0.0206  29  LYS   B NZ  
4352 N N   . VAL   B 30  ? 0.2558 0.2995 0.2703 0.0094  0.0379  0.0629  30  VAL   B N   
4353 C CA  . VAL   B 30  ? 0.2363 0.2825 0.2876 -0.0069 0.0064  0.0732  30  VAL   B CA  
4354 C C   . VAL   B 30  ? 0.2114 0.2757 0.2713 -0.0083 0.0115  0.0883  30  VAL   B C   
4355 O O   . VAL   B 30  ? 0.2222 0.2954 0.2710 -0.0044 0.0080  0.1037  30  VAL   B O   
4356 C CB  . VAL   B 30  ? 0.2443 0.2785 0.3364 -0.0232 -0.0338 0.0687  30  VAL   B CB  
4357 C CG1 . VAL   B 30  ? 0.2490 0.2910 0.3408 -0.0237 -0.0309 0.0539  30  VAL   B CG1 
4358 C CG2 . VAL   B 30  ? 0.2566 0.2768 0.3624 -0.0293 -0.0556 0.0542  30  VAL   B CG2 
4369 N N   . LYS   B 31  ? 0.2015 0.2345 0.3020 -0.0235 0.0088  0.0917  31  LYS   B N   
4370 C CA  . LYS   B 31  ? 0.1881 0.2340 0.3331 -0.0364 -0.0074 0.0951  31  LYS   B CA  
4371 C C   . LYS   B 31  ? 0.1726 0.2014 0.2979 -0.0348 -0.0269 0.0809  31  LYS   B C   
4372 O O   . LYS   B 31  ? 0.1783 0.2225 0.3128 -0.0257 -0.0162 0.1034  31  LYS   B O   
4373 C CB  . LYS   B 31  ? 0.2092 0.2888 0.3841 -0.0270 0.0179  0.1114  31  LYS   B CB  
4374 C CG  . LYS   B 31  ? 0.2425 0.3413 0.4267 -0.0251 0.0292  0.1129  31  LYS   B CG  
4375 C CD  . LYS   B 31  ? 0.2794 0.3938 0.4678 -0.0202 0.0213  0.1009  31  LYS   B CD  
4376 C CE  . LYS   B 31  ? 0.3105 0.4278 0.5071 -0.0149 0.0100  0.0904  31  LYS   B CE  
4377 N NZ  . LYS   B 31  ? 0.3190 0.4482 0.5178 -0.0062 -0.0038 0.0798  31  LYS   B NZ  
4391 N N   . PRO   B 32  ? 0.1787 0.1727 0.2295 -0.0293 -0.0429 0.0498  32  PRO   B N   
4392 C CA  . PRO   B 32  ? 0.1960 0.1721 0.1884 -0.0371 -0.0390 0.0323  32  PRO   B CA  
4393 C C   . PRO   B 32  ? 0.2067 0.1573 0.1874 -0.0453 -0.0535 0.0306  32  PRO   B C   
4394 O O   . PRO   B 32  ? 0.2195 0.1559 0.2236 -0.0468 -0.0693 0.0314  32  PRO   B O   
4395 C CB  . PRO   B 32  ? 0.2047 0.1712 0.1917 -0.0446 -0.0246 0.0112  32  PRO   B CB  
4396 C CG  . PRO   B 32  ? 0.2209 0.1572 0.2021 -0.0357 -0.0544 0.0208  32  PRO   B CG  
4397 C CD  . PRO   B 32  ? 0.2041 0.1620 0.2239 -0.0315 -0.0594 0.0249  32  PRO   B CD  
4405 N N   . THR   B 33  ? 0.2087 0.1494 0.1812 -0.0359 -0.0511 0.0191  33  THR   B N   
4406 C CA  . THR   B 33  ? 0.2118 0.1567 0.1815 -0.0349 -0.0436 0.0251  33  THR   B CA  
4407 C C   . THR   B 33  ? 0.2103 0.1470 0.1781 -0.0344 -0.0480 0.0169  33  THR   B C   
4408 O O   . THR   B 33  ? 0.2287 0.1457 0.1936 -0.0462 -0.0526 0.0176  33  THR   B O   
4409 C CB  . THR   B 33  ? 0.2202 0.1704 0.1850 -0.0219 -0.0468 0.0249  33  THR   B CB  
4410 O OG1 . THR   B 33  ? 0.2054 0.1783 0.1920 -0.0238 -0.0424 0.0320  33  THR   B OG1 
4411 C CG2 . THR   B 33  ? 0.2414 0.1821 0.1982 -0.0184 -0.0482 0.0183  33  THR   B CG2 
4419 N N   . VAL   B 34  ? 0.1893 0.1445 0.1738 -0.0395 -0.0434 0.0152  34  VAL   B N   
4420 C CA  . VAL   B 34  ? 0.1747 0.1438 0.1643 -0.0301 -0.0373 0.0130  34  VAL   B CA  
4421 C C   . VAL   B 34  ? 0.1575 0.1382 0.1475 -0.0302 -0.0226 0.0065  34  VAL   B C   
4422 O O   . VAL   B 34  ? 0.1780 0.1467 0.1562 -0.0223 -0.0354 0.0105  34  VAL   B O   
4423 C CB  . VAL   B 34  ? 0.1849 0.1546 0.1843 -0.0057 -0.0311 -0.0060 34  VAL   B CB  
4424 C CG1 . VAL   B 34  ? 0.1809 0.1733 0.2002 -0.0122 -0.0129 -0.0104 34  VAL   B CG1 
4425 C CG2 . VAL   B 34  ? 0.1938 0.1565 0.2100 -0.0028 -0.0243 -0.0064 34  VAL   B CG2 
4435 N N   . VAL   B 35  ? 0.1574 0.1287 0.1413 -0.0209 -0.0146 0.0056  35  VAL   B N   
4436 C CA  . VAL   B 35  ? 0.1576 0.1338 0.1382 -0.0182 -0.0110 0.0044  35  VAL   B CA  
4437 C C   . VAL   B 35  ? 0.1411 0.1341 0.1391 -0.0203 -0.0168 0.0052  35  VAL   B C   
4438 O O   . VAL   B 35  ? 0.1486 0.1354 0.1455 -0.0230 -0.0060 -0.0044 35  VAL   B O   
4439 C CB  . VAL   B 35  ? 0.1499 0.1513 0.1557 -0.0144 -0.0001 0.0030  35  VAL   B CB  
4440 C CG1 . VAL   B 35  ? 0.1420 0.1656 0.1809 -0.0208 0.0025  0.0023  35  VAL   B CG1 
4441 C CG2 . VAL   B 35  ? 0.1606 0.1485 0.1769 -0.0094 0.0037  -0.0005 35  VAL   B CG2 
4451 N N   . VAL   B 36  ? 0.1360 0.1336 0.1384 -0.0126 -0.0209 0.0066  36  VAL   B N   
4452 C CA  . VAL   B 36  ? 0.1448 0.1272 0.1330 -0.0108 -0.0081 0.0002  36  VAL   B CA  
4453 C C   . VAL   B 36  ? 0.1431 0.1264 0.1255 -0.0071 -0.0061 -0.0036 36  VAL   B C   
4454 O O   . VAL   B 36  ? 0.1417 0.1439 0.1579 -0.0087 -0.0035 -0.0081 36  VAL   B O   
4455 C CB  . VAL   B 36  ? 0.1454 0.1337 0.1514 -0.0154 -0.0001 0.0038  36  VAL   B CB  
4456 C CG1 . VAL   B 36  ? 0.1364 0.1422 0.1690 -0.0227 -0.0025 0.0009  36  VAL   B CG1 
4457 C CG2 . VAL   B 36  ? 0.1548 0.1403 0.1615 -0.0137 -0.0124 0.0118  36  VAL   B CG2 
4467 N N   . ASN   B 37  ? 0.1446 0.1393 0.1342 0.0003  -0.0069 0.0061  37  ASN   B N   
4468 C CA  . ASN   B 37  ? 0.1422 0.1348 0.1491 0.0013  -0.0108 0.0087  37  ASN   B CA  
4469 C C   . ASN   B 37  ? 0.1387 0.1374 0.1524 0.0089  -0.0152 0.0034  37  ASN   B C   
4470 O O   . ASN   B 37  ? 0.1506 0.1402 0.1500 0.0029  0.0016  0.0055  37  ASN   B O   
4471 C CB  . ASN   B 37  ? 0.1443 0.1418 0.1394 0.0005  -0.0155 0.0040  37  ASN   B CB  
4472 C CG  . ASN   B 37  ? 0.1480 0.1441 0.1454 -0.0055 -0.0097 -0.0031 37  ASN   B CG  
4473 O OD1 . ASN   B 37  ? 0.1541 0.1479 0.1714 0.0090  -0.0091 -0.0050 37  ASN   B OD1 
4474 N ND2 . ASN   B 37  ? 0.1576 0.1380 0.1492 -0.0025 -0.0152 0.0059  37  ASN   B ND2 
4481 N N   . ALA   B 38  ? 0.1468 0.1354 0.1585 0.0123  -0.0045 0.0001  38  ALA   B N   
4482 C CA  . ALA   B 38  ? 0.1559 0.1350 0.1594 -0.0015 0.0053  0.0132  38  ALA   B CA  
4483 C C   . ALA   B 38  ? 0.1540 0.1362 0.1658 0.0014  0.0042  0.0082  38  ALA   B C   
4484 O O   . ALA   B 38  ? 0.1675 0.1440 0.1755 0.0059  0.0045  0.0125  38  ALA   B O   
4485 C CB  . ALA   B 38  ? 0.1874 0.1532 0.1672 -0.0129 0.0212  0.0151  38  ALA   B CB  
4491 N N   . ALA   B 39  ? 0.1536 0.1460 0.1375 0.0115  -0.0018 0.0008  39  ALA   B N   
4492 C CA  . ALA   B 39  ? 0.1674 0.1449 0.1319 0.0075  -0.0063 0.0025  39  ALA   B CA  
4493 C C   . ALA   B 39  ? 0.1673 0.1468 0.1283 0.0062  -0.0035 -0.0039 39  ALA   B C   
4494 O O   . ALA   B 39  ? 0.1710 0.1593 0.1593 -0.0029 -0.0046 0.0095  39  ALA   B O   
4495 C CB  . ALA   B 39  ? 0.1641 0.1525 0.1531 -0.0011 0.0017  -0.0011 39  ALA   B CB  
4501 N N   . ASN   B 40  ? 0.1707 0.1789 0.1388 -0.0046 -0.0012 -0.0084 40  ASN   B N   
4502 C CA  . ASN   B 40  ? 0.1747 0.1849 0.1478 -0.0000 -0.0047 -0.0099 40  ASN   B CA  
4503 C C   . ASN   B 40  ? 0.1795 0.1811 0.1362 0.0070  -0.0064 -0.0090 40  ASN   B C   
4504 O O   . ASN   B 40  ? 0.1822 0.1716 0.1468 0.0050  -0.0067 -0.0017 40  ASN   B O   
4505 C CB  . ASN   B 40  ? 0.1878 0.1869 0.1726 0.0089  -0.0099 0.0035  40  ASN   B CB  
4506 C CG  . ASN   B 40  ? 0.1922 0.1885 0.1941 0.0048  -0.0238 0.0093  40  ASN   B CG  
4507 O OD1 . ASN   B 40  ? 0.1939 0.1812 0.2764 0.0025  -0.0336 0.0127  40  ASN   B OD1 
4508 N ND2 . ASN   B 40  ? 0.1979 0.1868 0.2003 0.0014  -0.0189 0.0106  40  ASN   B ND2 
4515 N N   . VAL   B 41  ? 0.1887 0.1836 0.1423 0.0131  0.0056  -0.0029 41  VAL   B N   
4516 C CA  . VAL   B 41  ? 0.2025 0.1983 0.1552 0.0134  0.0022  -0.0170 41  VAL   B CA  
4517 C C   . VAL   B 41  ? 0.1934 0.1980 0.1500 0.0264  -0.0049 -0.0156 41  VAL   B C   
4518 O O   . VAL   B 41  ? 0.1915 0.2003 0.1611 0.0172  -0.0098 -0.0218 41  VAL   B O   
4519 C CB  . VAL   B 41  ? 0.2234 0.2171 0.1770 -0.0016 0.0180  -0.0289 41  VAL   B CB  
4520 C CG1 . VAL   B 41  ? 0.2269 0.2223 0.1924 -0.0141 0.0307  -0.0312 41  VAL   B CG1 
4521 C CG2 . VAL   B 41  ? 0.2257 0.2388 0.1894 -0.0088 0.0204  -0.0239 41  VAL   B CG2 
4531 N N   . TYR   B 42  ? 0.2028 0.1922 0.1539 0.0241  -0.0173 0.0029  42  TYR   B N   
4532 C CA  . TYR   B 42  ? 0.2173 0.2034 0.1512 0.0155  -0.0294 -0.0168 42  TYR   B CA  
4533 C C   . TYR   B 42  ? 0.2007 0.1772 0.1620 0.0154  -0.0303 -0.0213 42  TYR   B C   
4534 O O   . TYR   B 42  ? 0.2024 0.1855 0.1992 0.0167  -0.0373 -0.0198 42  TYR   B O   
4535 C CB  . TYR   B 42  ? 0.2384 0.2321 0.1731 0.0142  -0.0298 0.0006  42  TYR   B CB  
4536 C CG  . TYR   B 42  ? 0.2412 0.2550 0.1770 0.0066  -0.0235 0.0157  42  TYR   B CG  
4537 C CD1 . TYR   B 42  ? 0.2360 0.2554 0.1633 0.0042  -0.0144 0.0117  42  TYR   B CD1 
4538 C CD2 . TYR   B 42  ? 0.2594 0.2692 0.2102 0.0058  -0.0044 0.0181  42  TYR   B CD2 
4539 C CE1 . TYR   B 42  ? 0.2557 0.2716 0.1740 0.0104  -0.0119 0.0147  42  TYR   B CE1 
4540 C CE2 . TYR   B 42  ? 0.2683 0.2775 0.2017 0.0095  0.0174  0.0322  42  TYR   B CE2 
4541 C CZ  . TYR   B 42  ? 0.2769 0.2870 0.2027 0.0283  0.0154  0.0184  42  TYR   B CZ  
4542 O OH  . TYR   B 42  ? 0.3136 0.3112 0.2519 0.0421  0.0267  0.0281  42  TYR   B OH  
4552 N N   . LEU   B 43  ? 0.1829 0.1628 0.1467 0.0089  -0.0202 -0.0134 43  LEU   B N   
4553 C CA  . LEU   B 43  ? 0.1771 0.1602 0.1457 0.0023  -0.0121 0.0007  43  LEU   B CA  
4554 C C   . LEU   B 43  ? 0.1857 0.1640 0.1559 -0.0003 -0.0174 0.0016  43  LEU   B C   
4555 O O   . LEU   B 43  ? 0.1840 0.1640 0.1802 0.0001  -0.0213 0.0092  43  LEU   B O   
4556 C CB  . LEU   B 43  ? 0.1677 0.1609 0.1687 -0.0024 -0.0201 -0.0088 43  LEU   B CB  
4557 C CG  . LEU   B 43  ? 0.1739 0.1556 0.1806 0.0018  -0.0233 -0.0041 43  LEU   B CG  
4558 C CD1 . LEU   B 43  ? 0.1796 0.1652 0.2246 0.0003  -0.0395 -0.0086 43  LEU   B CD1 
4559 C CD2 . LEU   B 43  ? 0.1769 0.1599 0.1804 -0.0079 -0.0278 0.0002  43  LEU   B CD2 
4571 N N   . LYS   B 44  ? 0.1835 0.1591 0.1724 0.0088  -0.0065 -0.0123 44  LYS   B N   
4572 C CA  . LYS   B 44  ? 0.1937 0.1751 0.1608 0.0099  -0.0107 0.0042  44  LYS   B CA  
4573 C C   . LYS   B 44  ? 0.1741 0.1720 0.1627 0.0107  -0.0125 0.0031  44  LYS   B C   
4574 O O   . LYS   B 44  ? 0.1995 0.1692 0.1981 0.0047  -0.0125 0.0048  44  LYS   B O   
4575 C CB  . LYS   B 44  ? 0.2242 0.1992 0.1820 0.0162  -0.0277 -0.0032 44  LYS   B CB  
4576 C CG  . LYS   B 44  ? 0.2662 0.2319 0.2209 0.0093  -0.0456 0.0021  44  LYS   B CG  
4577 C CD  . LYS   B 44  ? 0.2993 0.2525 0.2799 -0.0061 -0.0593 -0.0007 44  LYS   B CD  
4578 C CE  . LYS   B 44  ? 0.3303 0.2769 0.3314 -0.0124 -0.0614 0.0053  44  LYS   B CE  
4579 N NZ  . LYS   B 44  ? 0.3389 0.2876 0.3638 -0.0063 -0.0718 0.0196  44  LYS   B NZ  
4593 N N   . HIS   B 45  ? 0.1717 0.1733 0.1458 0.0046  -0.0128 0.0103  45  HIS   B N   
4594 C CA  . HIS   B 45  ? 0.1826 0.1717 0.1577 0.0048  -0.0114 0.0001  45  HIS   B CA  
4595 C C   . HIS   B 45  ? 0.2081 0.1979 0.1927 0.0168  -0.0157 -0.0013 45  HIS   B C   
4596 O O   . HIS   B 45  ? 0.2192 0.2207 0.2487 0.0406  0.0160  -0.0063 45  HIS   B O   
4597 C CB  . HIS   B 45  ? 0.1668 0.1716 0.1577 0.0017  -0.0127 0.0002  45  HIS   B CB  
4598 C CG  . HIS   B 45  ? 0.1631 0.1741 0.1681 -0.0063 -0.0149 0.0006  45  HIS   B CG  
4599 N ND1 . HIS   B 45  ? 0.1735 0.1715 0.1788 0.0044  -0.0238 -0.0116 45  HIS   B ND1 
4600 C CD2 . HIS   B 45  ? 0.1735 0.1759 0.1833 -0.0151 -0.0243 0.0061  45  HIS   B CD2 
4601 C CE1 . HIS   B 45  ? 0.1743 0.1575 0.1644 0.0049  -0.0276 -0.0110 45  HIS   B CE1 
4602 N NE2 . HIS   B 45  ? 0.1838 0.1632 0.1750 -0.0038 -0.0221 -0.0025 45  HIS   B NE2 
4610 N N   A GLY   B 46  ? 0.2179 0.1914 0.2171 0.0206  -0.0439 0.0091  46  GLY   B N   
4611 N N   B GLY   B 46  ? 0.2165 0.2052 0.2108 0.0150  -0.0239 0.0020  46  GLY   B N   
4612 C CA  A GLY   B 46  ? 0.2374 0.2024 0.2581 0.0218  -0.0499 0.0111  46  GLY   B CA  
4613 C CA  B GLY   B 46  ? 0.2270 0.2146 0.2318 0.0135  -0.0295 0.0045  46  GLY   B CA  
4614 C C   A GLY   B 46  ? 0.2451 0.2252 0.3068 0.0243  -0.0462 0.0084  46  GLY   B C   
4615 C C   B GLY   B 46  ? 0.2346 0.2256 0.2553 0.0133  -0.0336 0.0064  46  GLY   B C   
4616 O O   A GLY   B 46  ? 0.2571 0.2517 0.3935 0.0237  -0.0242 -0.0164 46  GLY   B O   
4617 O O   B GLY   B 46  ? 0.2369 0.2326 0.2595 0.0134  -0.0339 0.0120  46  GLY   B O   
4624 N N   . GLY   B 47  ? 0.2387 0.2303 0.2732 0.0084  -0.0315 -0.0008 47  GLY   B N   
4625 C CA  . GLY   B 47  ? 0.2180 0.1960 0.2318 0.0052  -0.0296 -0.0032 47  GLY   B CA  
4626 C C   . GLY   B 47  ? 0.1904 0.1791 0.1948 0.0021  -0.0024 -0.0031 47  GLY   B C   
4627 O O   . GLY   B 47  ? 0.1947 0.1741 0.2045 0.0056  -0.0136 0.0134  47  GLY   B O   
4632 N N   . GLY   B 48  ? 0.1782 0.1681 0.1879 -0.0013 -0.0118 0.0163  48  GLY   B N   
4633 C CA  . GLY   B 48  ? 0.1768 0.1631 0.1925 -0.0060 0.0017  0.0108  48  GLY   B CA  
4634 C C   . GLY   B 48  ? 0.1653 0.1568 0.1878 -0.0033 0.0131  0.0119  48  GLY   B C   
4635 O O   . GLY   B 48  ? 0.1613 0.1514 0.2106 0.0006  -0.0044 0.0098  48  GLY   B O   
4639 N N   . VAL   B 49  ? 0.1655 0.1676 0.1711 0.0084  0.0013  0.0093  49  VAL   B N   
4640 C CA  . VAL   B 49  ? 0.1665 0.1744 0.1485 0.0093  -0.0103 0.0021  49  VAL   B CA  
4641 C C   . VAL   B 49  ? 0.1581 0.1636 0.1420 0.0077  -0.0089 0.0107  49  VAL   B C   
4642 O O   . VAL   B 49  ? 0.1709 0.1590 0.1740 0.0055  -0.0060 0.0052  49  VAL   B O   
4643 C CB  . VAL   B 49  ? 0.1674 0.1878 0.1931 0.0009  -0.0245 0.0040  49  VAL   B CB  
4644 C CG1 . VAL   B 49  ? 0.1655 0.1879 0.1974 0.0086  -0.0409 -0.0010 49  VAL   B CG1 
4645 C CG2 . VAL   B 49  ? 0.1938 0.2085 0.2330 -0.0098 -0.0446 -0.0058 49  VAL   B CG2 
4655 N N   . ALA   B 50  ? 0.1535 0.1550 0.1577 0.0017  -0.0071 0.0096  50  ALA   B N   
4656 C CA  . ALA   B 50  ? 0.1467 0.1518 0.1657 0.0065  -0.0031 0.0076  50  ALA   B CA  
4657 C C   . ALA   B 50  ? 0.1471 0.1543 0.1620 0.0052  -0.0084 0.0071  50  ALA   B C   
4658 O O   . ALA   B 50  ? 0.1553 0.1577 0.1612 0.0028  -0.0016 0.0036  50  ALA   B O   
4659 C CB  . ALA   B 50  ? 0.1600 0.1474 0.1673 -0.0027 -0.0002 0.0104  50  ALA   B CB  
4665 N N   . GLY   B 51  ? 0.1548 0.1658 0.1757 0.0155  -0.0207 0.0135  51  GLY   B N   
4666 C CA  . GLY   B 51  ? 0.1591 0.1669 0.1934 0.0185  -0.0221 0.0176  51  GLY   B CA  
4667 C C   . GLY   B 51  ? 0.1599 0.1589 0.1918 0.0179  -0.0125 0.0125  51  GLY   B C   
4668 O O   . GLY   B 51  ? 0.1608 0.1712 0.2110 0.0075  -0.0095 0.0029  51  GLY   B O   
4672 N N   . ALA   B 52  ? 0.1532 0.1561 0.1851 0.0151  -0.0060 0.0133  52  ALA   B N   
4673 C CA  . ALA   B 52  ? 0.1601 0.1671 0.1829 0.0185  0.0061  -0.0035 52  ALA   B CA  
4674 C C   . ALA   B 52  ? 0.1599 0.1524 0.1758 0.0121  0.0017  0.0068  52  ALA   B C   
4675 O O   . ALA   B 52  ? 0.1711 0.1616 0.1938 0.0085  0.0039  0.0019  52  ALA   B O   
4676 C CB  . ALA   B 52  ? 0.1707 0.1698 0.1976 0.0112  0.0056  0.0012  52  ALA   B CB  
4682 N N   . LEU   B 53  ? 0.1521 0.1558 0.1627 0.0169  0.0029  -0.0001 53  LEU   B N   
4683 C CA  . LEU   B 53  ? 0.1545 0.1682 0.1562 0.0156  -0.0043 0.0080  53  LEU   B CA  
4684 C C   . LEU   B 53  ? 0.1584 0.1605 0.1578 0.0092  0.0051  0.0051  53  LEU   B C   
4685 O O   . LEU   B 53  ? 0.1587 0.1648 0.1804 -0.0008 0.0015  0.0187  53  LEU   B O   
4686 C CB  . LEU   B 53  ? 0.1577 0.1724 0.1759 0.0132  0.0003  0.0103  53  LEU   B CB  
4687 C CG  . LEU   B 53  ? 0.1590 0.1863 0.1857 0.0066  -0.0038 0.0253  53  LEU   B CG  
4688 C CD1 . LEU   B 53  ? 0.1661 0.2044 0.2097 0.0190  -0.0011 0.0099  53  LEU   B CD1 
4689 C CD2 . LEU   B 53  ? 0.1673 0.2119 0.2135 -0.0082 -0.0167 -0.0111 53  LEU   B CD2 
4701 N N   . ASN   B 54  ? 0.1596 0.1533 0.1533 0.0047  0.0038  0.0109  54  ASN   B N   
4702 C CA  . ASN   B 54  ? 0.1653 0.1682 0.1657 0.0095  -0.0077 -0.0076 54  ASN   B CA  
4703 C C   . ASN   B 54  ? 0.1531 0.1712 0.1933 0.0071  -0.0009 -0.0002 54  ASN   B C   
4704 O O   . ASN   B 54  ? 0.1588 0.1772 0.1994 -0.0047 -0.0012 0.0028  54  ASN   B O   
4705 C CB  . ASN   B 54  ? 0.1623 0.1775 0.1905 0.0067  -0.0025 -0.0033 54  ASN   B CB  
4706 C CG  . ASN   B 54  ? 0.1625 0.1851 0.1691 -0.0006 -0.0043 0.0051  54  ASN   B CG  
4707 O OD1 . ASN   B 54  ? 0.1629 0.1871 0.1836 -0.0025 -0.0073 -0.0083 54  ASN   B OD1 
4708 N ND2 . ASN   B 54  ? 0.1841 0.1941 0.2002 0.0010  -0.0303 0.0109  54  ASN   B ND2 
4715 N N   . LYS   B 55  ? 0.1531 0.1748 0.2125 0.0203  0.0054  -0.0011 55  LYS   B N   
4716 C CA  . LYS   B 55  ? 0.1748 0.1826 0.2274 0.0254  0.0023  0.0015  55  LYS   B CA  
4717 C C   . LYS   B 55  ? 0.1633 0.1883 0.2211 0.0143  0.0062  0.0004  55  LYS   B C   
4718 O O   . LYS   B 55  ? 0.1597 0.1993 0.2323 0.0136  0.0047  -0.0029 55  LYS   B O   
4719 C CB  . LYS   B 55  ? 0.1869 0.1926 0.2542 0.0363  0.0132  0.0057  55  LYS   B CB  
4720 C CG  . LYS   B 55  ? 0.2336 0.2286 0.3317 0.0377  0.0240  0.0270  55  LYS   B CG  
4721 C CD  . LYS   B 55  ? 0.2657 0.2588 0.3970 0.0441  0.0494  0.0384  55  LYS   B CD  
4722 C CE  . LYS   B 55  ? 0.2900 0.2792 0.4530 0.0459  0.0675  0.0364  55  LYS   B CE  
4723 N NZ  . LYS   B 55  ? 0.3011 0.2969 0.4883 0.0443  0.0576  0.0354  55  LYS   B NZ  
4737 N N   . ALA   B 56  ? 0.1577 0.1913 0.2060 0.0173  -0.0013 -0.0093 56  ALA   B N   
4738 C CA  . ALA   B 56  ? 0.1741 0.2116 0.2074 -0.0017 -0.0021 -0.0070 56  ALA   B CA  
4739 C C   . ALA   B 56  ? 0.1718 0.2009 0.1951 -0.0017 0.0150  0.0029  56  ALA   B C   
4740 O O   . ALA   B 56  ? 0.1823 0.2115 0.2110 0.0070  0.0316  0.0095  56  ALA   B O   
4741 C CB  . ALA   B 56  ? 0.1900 0.2321 0.2106 -0.0159 -0.0019 -0.0171 56  ALA   B CB  
4747 N N   . THR   B 57  ? 0.1685 0.1920 0.2009 0.0021  0.0174  0.0092  57  THR   B N   
4748 C CA  . THR   B 57  ? 0.1779 0.1890 0.2001 -0.0036 0.0195  0.0095  57  THR   B CA  
4749 C C   . THR   B 57  ? 0.1727 0.1970 0.2189 -0.0077 0.0136  0.0044  57  THR   B C   
4750 O O   . THR   B 57  ? 0.1780 0.1993 0.2337 -0.0207 0.0088  0.0080  57  THR   B O   
4751 C CB  . THR   B 57  ? 0.1822 0.1760 0.1782 -0.0010 0.0175  0.0154  57  THR   B CB  
4752 O OG1 . THR   B 57  ? 0.1797 0.1694 0.2007 0.0005  0.0184  0.0081  57  THR   B OG1 
4753 C CG2 . THR   B 57  ? 0.1726 0.1767 0.1874 -0.0074 0.0204  0.0081  57  THR   B CG2 
4761 N N   . ASN   B 58  ? 0.1578 0.2204 0.2392 -0.0169 -0.0065 -0.0114 58  ASN   B N   
4762 C CA  . ASN   B 58  ? 0.1882 0.2681 0.2813 -0.0323 0.0306  -0.0003 58  ASN   B CA  
4763 C C   . ASN   B 58  ? 0.1615 0.2309 0.2464 -0.0208 -0.0018 -0.0050 58  ASN   B C   
4764 O O   . ASN   B 58  ? 0.1657 0.2450 0.2556 -0.0173 0.0009  -0.0198 58  ASN   B O   
4765 C CB  . ASN   B 58  ? 0.3028 0.3657 0.4150 -0.0444 0.0652  0.0083  58  ASN   B CB  
4766 C CG  . ASN   B 58  ? 0.4342 0.4621 0.5778 -0.0467 0.0871  0.0275  58  ASN   B CG  
4767 O OD1 . ASN   B 58  ? 0.4631 0.4856 0.6364 -0.0482 0.0935  0.0340  58  ASN   B OD1 
4768 N ND2 . ASN   B 58  ? 0.5464 0.5464 0.6354 -0.0486 0.0951  0.0310  58  ASN   B ND2 
4775 N N   . ASN   B 59  ? 0.1591 0.2127 0.2275 -0.0146 -0.0037 0.0067  59  ASN   B N   
4776 C CA  . ASN   B 59  ? 0.1603 0.2170 0.2160 -0.0171 -0.0126 0.0109  59  ASN   B CA  
4777 C C   . ASN   B 59  ? 0.1577 0.2084 0.2101 -0.0146 -0.0173 -0.0047 59  ASN   B C   
4778 O O   . ASN   B 59  ? 0.1624 0.2071 0.2068 -0.0129 -0.0117 -0.0004 59  ASN   B O   
4779 C CB  . ASN   B 59  ? 0.1711 0.2322 0.2314 -0.0115 -0.0189 0.0160  59  ASN   B CB  
4780 C CG  . ASN   B 59  ? 0.1876 0.2480 0.2509 -0.0037 -0.0367 0.0146  59  ASN   B CG  
4781 O OD1 . ASN   B 59  ? 0.1942 0.2492 0.2386 0.0004  -0.0252 0.0232  59  ASN   B OD1 
4782 N ND2 . ASN   B 59  ? 0.1942 0.2560 0.2740 -0.0171 -0.0374 0.0094  59  ASN   B ND2 
4789 N N   . ALA   B 60  ? 0.1601 0.1984 0.2098 -0.0049 -0.0035 -0.0000 60  ALA   B N   
4790 C CA  . ALA   B 60  ? 0.1750 0.1905 0.1975 -0.0178 -0.0069 0.0026  60  ALA   B CA  
4791 C C   . ALA   B 60  ? 0.1619 0.1830 0.1865 -0.0111 -0.0047 0.0072  60  ALA   B C   
4792 O O   . ALA   B 60  ? 0.1689 0.1889 0.2043 -0.0144 0.0026  -0.0050 60  ALA   B O   
4793 C CB  . ALA   B 60  ? 0.1882 0.1959 0.2266 -0.0223 0.0068  0.0041  60  ALA   B CB  
4799 N N   . MET   B 61  ? 0.1551 0.1688 0.1823 -0.0077 -0.0006 0.0119  61  MET   B N   
4800 C CA  . MET   B 61  ? 0.1557 0.1679 0.1792 -0.0059 -0.0037 0.0059  61  MET   B CA  
4801 C C   . MET   B 61  ? 0.1647 0.1582 0.1773 -0.0094 -0.0087 0.0084  61  MET   B C   
4802 O O   . MET   B 61  ? 0.1666 0.1585 0.1780 -0.0025 -0.0044 -0.0118 61  MET   B O   
4803 C CB  . MET   B 61  ? 0.1530 0.1672 0.1793 -0.0012 -0.0070 -0.0014 61  MET   B CB  
4804 C CG  . MET   B 61  ? 0.1472 0.1628 0.1762 -0.0026 -0.0020 0.0029  61  MET   B CG  
4805 S SD  . MET   B 61  ? 0.1572 0.1677 0.1898 -0.0023 -0.0058 -0.0072 61  MET   B SD  
4806 C CE  . MET   B 61  ? 0.1579 0.1813 0.2266 0.0002  -0.0071 -0.0160 61  MET   B CE  
4816 N N   . GLN   B 62  ? 0.1657 0.1610 0.1644 -0.0024 -0.0165 0.0044  62  GLN   B N   
4817 C CA  . GLN   B 62  ? 0.1647 0.1715 0.1786 -0.0007 -0.0208 -0.0017 62  GLN   B CA  
4818 C C   . GLN   B 62  ? 0.1713 0.1733 0.1867 -0.0017 -0.0363 -0.0067 62  GLN   B C   
4819 O O   . GLN   B 62  ? 0.1867 0.1752 0.1899 -0.0045 -0.0324 -0.0177 62  GLN   B O   
4820 C CB  . GLN   B 62  ? 0.1641 0.1823 0.1780 -0.0004 -0.0186 0.0083  62  GLN   B CB  
4821 C CG  . GLN   B 62  ? 0.1742 0.1876 0.1848 -0.0012 -0.0272 -0.0066 62  GLN   B CG  
4822 C CD  . GLN   B 62  ? 0.1726 0.1781 0.1798 0.0028  -0.0245 0.0070  62  GLN   B CD  
4823 O OE1 . GLN   B 62  ? 0.1793 0.1757 0.1956 0.0044  -0.0310 -0.0091 62  GLN   B OE1 
4824 N NE2 . GLN   B 62  ? 0.1773 0.1836 0.1949 -0.0031 -0.0241 -0.0083 62  GLN   B NE2 
4833 N N   . VAL   B 63  ? 0.1684 0.1775 0.2020 -0.0155 -0.0286 -0.0098 63  VAL   B N   
4834 C CA  . VAL   B 63  ? 0.1793 0.1847 0.2189 -0.0211 -0.0273 0.0009  63  VAL   B CA  
4835 C C   . VAL   B 63  ? 0.1764 0.1739 0.2054 -0.0195 -0.0284 -0.0146 63  VAL   B C   
4836 O O   . VAL   B 63  ? 0.1906 0.1751 0.2156 -0.0147 -0.0449 -0.0133 63  VAL   B O   
4837 C CB  . VAL   B 63  ? 0.1830 0.2017 0.2595 -0.0228 -0.0215 -0.0052 63  VAL   B CB  
4838 C CG1 . VAL   B 63  ? 0.1913 0.2045 0.2737 -0.0370 -0.0147 -0.0042 63  VAL   B CG1 
4839 C CG2 . VAL   B 63  ? 0.1776 0.2215 0.2759 -0.0164 -0.0266 -0.0092 63  VAL   B CG2 
4849 N N   . GLU   B 64  ? 0.1789 0.1668 0.2059 -0.0058 -0.0261 -0.0165 64  GLU   B N   
4850 C CA  . GLU   B 64  ? 0.1747 0.1607 0.1949 -0.0134 -0.0357 -0.0036 64  GLU   B CA  
4851 C C   . GLU   B 64  ? 0.1665 0.1606 0.1875 -0.0071 -0.0284 -0.0056 64  GLU   B C   
4852 O O   . GLU   B 64  ? 0.1758 0.1721 0.1938 -0.0130 -0.0301 -0.0114 64  GLU   B O   
4853 C CB  . GLU   B 64  ? 0.1715 0.1742 0.2009 -0.0210 -0.0264 -0.0001 64  GLU   B CB  
4854 C CG  . GLU   B 64  ? 0.1837 0.1690 0.2031 -0.0253 -0.0260 -0.0134 64  GLU   B CG  
4855 C CD  . GLU   B 64  ? 0.1848 0.1925 0.2198 -0.0308 -0.0285 -0.0182 64  GLU   B CD  
4856 O OE1 . GLU   B 64  ? 0.1879 0.2129 0.2319 -0.0430 -0.0191 -0.0392 64  GLU   B OE1 
4857 O OE2 . GLU   B 64  ? 0.2008 0.1989 0.2201 -0.0315 -0.0380 -0.0238 64  GLU   B OE2 
4864 N N   . SER   B 65  ? 0.1720 0.1582 0.1754 -0.0161 -0.0106 -0.0038 65  SER   B N   
4865 C CA  . SER   B 65  ? 0.1741 0.1523 0.1801 -0.0040 -0.0191 -0.0105 65  SER   B CA  
4866 C C   . SER   B 65  ? 0.1752 0.1577 0.1809 0.0071  -0.0267 -0.0170 65  SER   B C   
4867 O O   . SER   B 65  ? 0.1810 0.1627 0.1941 -0.0004 -0.0267 -0.0271 65  SER   B O   
4868 C CB  . SER   B 65  ? 0.1759 0.1558 0.1856 -0.0083 -0.0127 -0.0090 65  SER   B CB  
4869 O OG  . SER   B 65  ? 0.1843 0.1623 0.1847 -0.0074 -0.0120 -0.0181 65  SER   B OG  
4875 N N   . ASP   B 66  ? 0.1799 0.1663 0.1800 0.0062  -0.0262 -0.0147 66  ASP   B N   
4876 C CA  . ASP   B 66  ? 0.1943 0.1783 0.1710 0.0069  -0.0292 -0.0136 66  ASP   B CA  
4877 C C   . ASP   B 66  ? 0.1962 0.1870 0.1776 -0.0055 -0.0206 -0.0246 66  ASP   B C   
4878 O O   . ASP   B 66  ? 0.1896 0.1861 0.1935 0.0045  -0.0250 -0.0282 66  ASP   B O   
4879 C CB  . ASP   B 66  ? 0.2061 0.1966 0.1992 0.0168  -0.0452 -0.0124 66  ASP   B CB  
4880 C CG  . ASP   B 66  ? 0.2309 0.2093 0.2260 0.0232  -0.0519 0.0026  66  ASP   B CG  
4881 O OD1 . ASP   B 66  ? 0.2552 0.2076 0.2294 0.0153  -0.0507 0.0053  66  ASP   B OD1 
4882 O OD2 . ASP   B 66  ? 0.2552 0.2352 0.2900 0.0470  -0.0501 0.0045  66  ASP   B OD2 
4887 N N   . ASP   B 67  ? 0.1854 0.1769 0.1779 -0.0107 -0.0182 -0.0227 67  ASP   B N   
4888 C CA  . ASP   B 67  ? 0.2002 0.1731 0.1966 -0.0072 -0.0173 -0.0112 67  ASP   B CA  
4889 C C   . ASP   B 67  ? 0.1960 0.1675 0.2103 0.0073  -0.0189 -0.0169 67  ASP   B C   
4890 O O   . ASP   B 67  ? 0.1969 0.1755 0.2147 -0.0035 -0.0136 -0.0257 67  ASP   B O   
4891 C CB  . ASP   B 67  ? 0.2264 0.1779 0.2091 -0.0130 -0.0378 -0.0122 67  ASP   B CB  
4892 C CG  . ASP   B 67  ? 0.2649 0.1881 0.2187 -0.0099 -0.0634 -0.0133 67  ASP   B CG  
4893 O OD1 . ASP   B 67  ? 0.2903 0.2002 0.2265 -0.0086 -0.0657 -0.0110 67  ASP   B OD1 
4894 O OD2 . ASP   B 67  ? 0.2813 0.1973 0.2405 0.0063  -0.0700 -0.0095 67  ASP   B OD2 
4899 N N   . TYR   B 68  ? 0.1934 0.1658 0.1925 0.0025  -0.0336 -0.0324 68  TYR   B N   
4900 C CA  . TYR   B 68  ? 0.1846 0.1858 0.2087 0.0067  -0.0423 -0.0437 68  TYR   B CA  
4901 C C   . TYR   B 68  ? 0.1765 0.1805 0.2067 0.0046  -0.0370 -0.0445 68  TYR   B C   
4902 O O   . TYR   B 68  ? 0.1851 0.1908 0.2124 0.0103  -0.0359 -0.0620 68  TYR   B O   
4903 C CB  . TYR   B 68  ? 0.1903 0.2112 0.2175 0.0139  -0.0477 -0.0504 68  TYR   B CB  
4904 C CG  . TYR   B 68  ? 0.1951 0.2290 0.2328 0.0179  -0.0366 -0.0717 68  TYR   B CG  
4905 C CD1 . TYR   B 68  ? 0.2007 0.2336 0.2604 -0.0010 -0.0375 -0.0802 68  TYR   B CD1 
4906 C CD2 . TYR   B 68  ? 0.1994 0.2464 0.2536 0.0255  -0.0512 -0.0677 68  TYR   B CD2 
4907 C CE1 . TYR   B 68  ? 0.2080 0.2490 0.2825 0.0021  -0.0371 -0.0810 68  TYR   B CE1 
4908 C CE2 . TYR   B 68  ? 0.2012 0.2559 0.2631 0.0216  -0.0437 -0.0865 68  TYR   B CE2 
4909 C CZ  . TYR   B 68  ? 0.2019 0.2527 0.2843 0.0060  -0.0433 -0.0837 68  TYR   B CZ  
4910 O OH  . TYR   B 68  ? 0.2025 0.2689 0.3105 -0.0009 -0.0310 -0.0712 68  TYR   B OH  
4920 N N   . ILE   B 69  ? 0.1794 0.1684 0.1988 0.0023  -0.0327 -0.0351 69  ILE   B N   
4921 C CA  . ILE   B 69  ? 0.1887 0.1803 0.2140 -0.0068 -0.0248 -0.0351 69  ILE   B CA  
4922 C C   . ILE   B 69  ? 0.1909 0.1767 0.1967 0.0023  -0.0367 -0.0273 69  ILE   B C   
4923 O O   . ILE   B 69  ? 0.1971 0.1879 0.1873 -0.0017 -0.0229 -0.0272 69  ILE   B O   
4924 C CB  . ILE   B 69  ? 0.1941 0.1858 0.2404 -0.0064 -0.0027 -0.0313 69  ILE   B CB  
4925 C CG1 . ILE   B 69  ? 0.1996 0.1877 0.2495 -0.0099 0.0102  -0.0449 69  ILE   B CG1 
4926 C CG2 . ILE   B 69  ? 0.2137 0.1933 0.2639 -0.0049 -0.0078 -0.0186 69  ILE   B CG2 
4927 C CD1 . ILE   B 69  ? 0.1904 0.1794 0.2699 -0.0208 0.0123  -0.0457 69  ILE   B CD1 
4939 N N   . ALA   B 70  ? 0.1860 0.1736 0.2032 0.0049  -0.0437 -0.0321 70  ALA   B N   
4940 C CA  . ALA   B 70  ? 0.1864 0.1860 0.1823 -0.0025 -0.0455 -0.0292 70  ALA   B CA  
4941 C C   . ALA   B 70  ? 0.1934 0.1874 0.1992 -0.0024 -0.0434 -0.0349 70  ALA   B C   
4942 O O   . ALA   B 70  ? 0.2076 0.1810 0.2027 0.0074  -0.0455 -0.0373 70  ALA   B O   
4943 C CB  . ALA   B 70  ? 0.1919 0.1987 0.1919 -0.0042 -0.0443 -0.0289 70  ALA   B CB  
4949 N N   . THR   B 71  ? 0.1991 0.1884 0.2046 0.0024  -0.0590 -0.0336 71  THR   B N   
4950 C CA  . THR   B 71  ? 0.2128 0.1891 0.2230 0.0080  -0.0669 -0.0347 71  THR   B CA  
4951 C C   . THR   B 71  ? 0.2041 0.1923 0.2573 0.0285  -0.0604 -0.0500 71  THR   B C   
4952 O O   . THR   B 71  ? 0.2204 0.1944 0.2934 0.0300  -0.0584 -0.0590 71  THR   B O   
4953 C CB  . THR   B 71  ? 0.2413 0.2122 0.2393 -0.0016 -0.0767 -0.0155 71  THR   B CB  
4954 O OG1 . THR   B 71  ? 0.2583 0.2350 0.2785 -0.0208 -0.0685 0.0102  71  THR   B OG1 
4955 C CG2 . THR   B 71  ? 0.2601 0.2206 0.2667 0.0038  -0.0692 0.0047  71  THR   B CG2 
4963 N N   . ASN   B 72  ? 0.1940 0.2018 0.2488 0.0116  -0.0672 -0.0727 72  ASN   B N   
4964 C CA  . ASN   B 72  ? 0.1969 0.2056 0.2432 0.0189  -0.0529 -0.0737 72  ASN   B CA  
4965 C C   . ASN   B 72  ? 0.2029 0.2154 0.2637 0.0030  -0.0270 -0.0684 72  ASN   B C   
4966 O O   . ASN   B 72  ? 0.2022 0.2302 0.2791 0.0106  -0.0146 -0.0680 72  ASN   B O   
4967 C CB  . ASN   B 72  ? 0.2083 0.2165 0.2523 0.0210  -0.0590 -0.0651 72  ASN   B CB  
4968 C CG  . ASN   B 72  ? 0.2318 0.2293 0.2608 0.0391  -0.0645 -0.0447 72  ASN   B CG  
4969 O OD1 . ASN   B 72  ? 0.2619 0.2479 0.2679 0.0221  -0.0477 -0.0493 72  ASN   B OD1 
4970 N ND2 . ASN   B 72  ? 0.2462 0.2406 0.3029 0.0522  -0.0525 -0.0105 72  ASN   B ND2 
4977 N N   . GLY   B 73  ? 0.2078 0.2137 0.2316 -0.0054 -0.0315 -0.0715 73  GLY   B N   
4978 C CA  . GLY   B 73  ? 0.2034 0.2202 0.2070 -0.0061 -0.0331 -0.0580 73  GLY   B CA  
4979 C C   . GLY   B 73  ? 0.1974 0.2183 0.1746 0.0009  -0.0256 -0.0460 73  GLY   B C   
4980 O O   . GLY   B 73  ? 0.1905 0.2063 0.1878 0.0051  -0.0254 -0.0351 73  GLY   B O   
4984 N N   . PRO   B 74  ? 0.1980 0.2302 0.1509 0.0015  -0.0268 -0.0372 74  PRO   B N   
4985 C CA  . PRO   B 74  ? 0.1919 0.2311 0.1455 0.0076  -0.0265 -0.0230 74  PRO   B CA  
4986 C C   . PRO   B 74  ? 0.1757 0.2130 0.1552 0.0053  -0.0218 -0.0204 74  PRO   B C   
4987 O O   . PRO   B 74  ? 0.1801 0.2174 0.2031 0.0038  -0.0135 -0.0337 74  PRO   B O   
4988 C CB  . PRO   B 74  ? 0.2106 0.2547 0.1603 0.0044  -0.0301 -0.0202 74  PRO   B CB  
4989 C CG  . PRO   B 74  ? 0.2305 0.2624 0.1900 0.0021  -0.0226 -0.0144 74  PRO   B CG  
4990 C CD  . PRO   B 74  ? 0.2249 0.2501 0.1739 0.0058  -0.0148 -0.0319 74  PRO   B CD  
4998 N N   . LEU   B 75  ? 0.1753 0.1975 0.1433 0.0048  -0.0248 -0.0270 75  LEU   B N   
4999 C CA  . LEU   B 75  ? 0.1773 0.1977 0.1426 0.0001  -0.0204 -0.0099 75  LEU   B CA  
5000 C C   . LEU   B 75  ? 0.1830 0.2103 0.1353 0.0060  -0.0141 -0.0060 75  LEU   B C   
5001 O O   . LEU   B 75  ? 0.1887 0.2240 0.1559 -0.0027 -0.0093 -0.0037 75  LEU   B O   
5002 C CB  . LEU   B 75  ? 0.1819 0.1975 0.1417 -0.0091 -0.0227 -0.0002 75  LEU   B CB  
5003 C CG  . LEU   B 75  ? 0.2116 0.2176 0.1696 -0.0380 -0.0114 0.0009  75  LEU   B CG  
5004 C CD1 . LEU   B 75  ? 0.2484 0.2353 0.1567 -0.0531 0.0065  -0.0029 75  LEU   B CD1 
5005 C CD2 . LEU   B 75  ? 0.2473 0.2402 0.2486 -0.0232 0.0045  0.0035  75  LEU   B CD2 
5017 N N   . LYS   B 76  ? 0.1855 0.2269 0.1719 0.0039  -0.0039 -0.0025 76  LYS   B N   
5018 C CA  . LYS   B 76  ? 0.1991 0.2327 0.2050 -0.0020 0.0233  -0.0083 76  LYS   B CA  
5019 C C   . LYS   B 76  ? 0.1925 0.2181 0.1663 0.0030  0.0089  0.0130  76  LYS   B C   
5020 O O   . LYS   B 76  ? 0.1893 0.2047 0.1744 -0.0011 0.0001  0.0073  76  LYS   B O   
5021 C CB  . LYS   B 76  ? 0.2146 0.2341 0.2690 -0.0065 0.0486  -0.0368 76  LYS   B CB  
5022 C CG  . LYS   B 76  ? 0.2275 0.2553 0.3306 0.0018  0.0339  -0.0402 76  LYS   B CG  
5023 C CD  . LYS   B 76  ? 0.2322 0.2674 0.3803 0.0092  0.0195  -0.0498 76  LYS   B CD  
5024 C CE  . LYS   B 76  ? 0.2418 0.2873 0.4391 0.0135  0.0097  -0.0557 76  LYS   B CE  
5025 N NZ  . LYS   B 76  ? 0.2422 0.2926 0.4627 0.0111  -0.0123 -0.0761 76  LYS   B NZ  
5039 N N   . VAL   B 77  ? 0.1950 0.2324 0.1639 0.0080  0.0113  0.0137  77  VAL   B N   
5040 C CA  . VAL   B 77  ? 0.2013 0.2229 0.1709 0.0161  0.0120  0.0433  77  VAL   B CA  
5041 C C   . VAL   B 77  ? 0.1803 0.1962 0.1679 0.0167  0.0219  0.0340  77  VAL   B C   
5042 O O   . VAL   B 77  ? 0.1813 0.1881 0.1849 0.0290  0.0311  0.0241  77  VAL   B O   
5043 C CB  . VAL   B 77  ? 0.2120 0.2376 0.2079 0.0188  0.0269  0.0527  77  VAL   B CB  
5044 C CG1 . VAL   B 77  ? 0.2187 0.2238 0.2464 0.0083  0.0341  0.0784  77  VAL   B CG1 
5045 C CG2 . VAL   B 77  ? 0.2347 0.2599 0.2311 0.0141  0.0031  0.0586  77  VAL   B CG2 
5055 N N   . GLY   B 78  ? 0.1818 0.1892 0.1598 0.0108  0.0144  0.0266  78  GLY   B N   
5056 C CA  . GLY   B 78  ? 0.1814 0.1841 0.1516 0.0113  0.0207  0.0138  78  GLY   B CA  
5057 C C   . GLY   B 78  ? 0.1711 0.1780 0.1535 0.0131  0.0257  0.0225  78  GLY   B C   
5058 O O   . GLY   B 78  ? 0.1779 0.1710 0.1759 0.0209  0.0259  0.0256  78  GLY   B O   
5062 N N   . GLY   B 79  ? 0.1630 0.1792 0.1693 0.0093  0.0179  0.0135  79  GLY   B N   
5063 C CA  . GLY   B 79  ? 0.1550 0.1708 0.1755 0.0104  0.0119  0.0077  79  GLY   B CA  
5064 C C   . GLY   B 79  ? 0.1451 0.1630 0.1708 0.0114  0.0145  0.0048  79  GLY   B C   
5065 O O   . GLY   B 79  ? 0.1581 0.1628 0.1816 0.0117  0.0213  0.0196  79  GLY   B O   
5069 N N   . SER   B 80  ? 0.1573 0.1592 0.1693 0.0029  0.0201  0.0010  80  SER   B N   
5070 C CA  . SER   B 80  ? 0.1479 0.1620 0.1739 -0.0003 0.0044  0.0019  80  SER   B CA  
5071 C C   . SER   B 80  ? 0.1441 0.1584 0.1771 0.0071  0.0011  -0.0054 80  SER   B C   
5072 O O   . SER   B 80  ? 0.1652 0.1614 0.2027 0.0146  0.0044  -0.0068 80  SER   B O   
5073 C CB  . SER   B 80  ? 0.1506 0.1698 0.1798 -0.0013 0.0035  0.0103  80  SER   B CB  
5074 O OG  . SER   B 80  ? 0.1655 0.1778 0.1999 -0.0008 -0.0201 0.0095  80  SER   B OG  
5080 N N   . CYS   B 81  ? 0.1486 0.1451 0.1819 -0.0005 -0.0040 -0.0094 81  CYS   B N   
5081 C CA  . CYS   B 81  ? 0.1551 0.1465 0.1705 -0.0036 -0.0145 -0.0062 81  CYS   B CA  
5082 C C   . CYS   B 81  ? 0.1540 0.1497 0.1451 0.0063  -0.0097 0.0071  81  CYS   B C   
5083 O O   . CYS   B 81  ? 0.1746 0.1465 0.1726 0.0094  -0.0018 -0.0123 81  CYS   B O   
5084 C CB  . CYS   B 81  ? 0.1791 0.1539 0.1902 -0.0119 -0.0100 -0.0044 81  CYS   B CB  
5085 S SG  . CYS   B 81  ? 0.1759 0.1752 0.1665 -0.0064 -0.0222 -0.0116 81  CYS   B SG  
5091 N N   . VAL   B 82  ? 0.1602 0.1521 0.1461 0.0056  -0.0153 0.0004  82  VAL   B N   
5092 C CA  . VAL   B 82  ? 0.1753 0.1424 0.1483 -0.0075 -0.0111 -0.0027 82  VAL   B CA  
5093 C C   . VAL   B 82  ? 0.1820 0.1313 0.1667 -0.0036 -0.0110 -0.0080 82  VAL   B C   
5094 O O   . VAL   B 82  ? 0.1764 0.1429 0.2039 -0.0087 -0.0086 -0.0225 82  VAL   B O   
5095 C CB  . VAL   B 82  ? 0.1775 0.1591 0.1683 -0.0033 -0.0140 0.0059  82  VAL   B CB  
5096 C CG1 . VAL   B 82  ? 0.2016 0.1818 0.1821 0.0034  -0.0171 0.0172  82  VAL   B CG1 
5097 C CG2 . VAL   B 82  ? 0.1861 0.1664 0.1954 -0.0056 -0.0244 0.0085  82  VAL   B CG2 
5107 N N   . LEU   B 83  ? 0.1727 0.1312 0.1673 -0.0180 -0.0216 -0.0117 83  LEU   B N   
5108 C CA  . LEU   B 83  ? 0.1695 0.1353 0.1583 -0.0124 -0.0223 -0.0038 83  LEU   B CA  
5109 C C   . LEU   B 83  ? 0.1590 0.1376 0.1619 -0.0176 -0.0236 -0.0055 83  LEU   B C   
5110 O O   . LEU   B 83  ? 0.1647 0.1494 0.1513 -0.0181 -0.0174 0.0022  83  LEU   B O   
5111 C CB  . LEU   B 83  ? 0.1669 0.1508 0.1751 -0.0132 -0.0162 -0.0173 83  LEU   B CB  
5112 C CG  . LEU   B 83  ? 0.1854 0.1731 0.1912 -0.0184 -0.0127 -0.0166 83  LEU   B CG  
5113 C CD1 . LEU   B 83  ? 0.1986 0.1829 0.1942 -0.0176 -0.0183 -0.0095 83  LEU   B CD1 
5114 C CD2 . LEU   B 83  ? 0.2010 0.1837 0.2066 -0.0085 -0.0157 -0.0279 83  LEU   B CD2 
5126 N N   . SER   B 84  ? 0.1678 0.1528 0.1792 -0.0206 -0.0238 -0.0052 84  SER   B N   
5127 C CA  . SER   B 84  ? 0.1750 0.1733 0.1666 -0.0268 -0.0144 0.0122  84  SER   B CA  
5128 C C   . SER   B 84  ? 0.1670 0.1836 0.1337 -0.0211 -0.0171 0.0189  84  SER   B C   
5129 O O   . SER   B 84  ? 0.1778 0.1647 0.1370 -0.0182 -0.0130 0.0008  84  SER   B O   
5130 C CB  . SER   B 84  ? 0.1847 0.1797 0.2256 -0.0263 0.0056  0.0076  84  SER   B CB  
5131 O OG  . SER   B 84  ? 0.1828 0.1992 0.2822 -0.0328 0.0122  0.0226  84  SER   B OG  
5137 N N   . GLY   B 85  ? 0.1679 0.2048 0.1515 -0.0184 -0.0059 0.0219  85  GLY   B N   
5138 C CA  . GLY   B 85  ? 0.1675 0.2099 0.1700 -0.0281 0.0118  -0.0044 85  GLY   B CA  
5139 C C   . GLY   B 85  ? 0.1666 0.1933 0.1520 -0.0344 0.0058  0.0024  85  GLY   B C   
5140 O O   . GLY   B 85  ? 0.1776 0.1947 0.1630 -0.0535 0.0182  -0.0181 85  GLY   B O   
5144 N N   . HIS   B 86  ? 0.1675 0.1798 0.1684 -0.0270 -0.0150 0.0067  86  HIS   B N   
5145 C CA  . HIS   B 86  ? 0.1661 0.1787 0.1622 -0.0306 -0.0248 0.0136  86  HIS   B CA  
5146 C C   . HIS   B 86  ? 0.1620 0.1906 0.1621 -0.0390 -0.0087 0.0377  86  HIS   B C   
5147 O O   . HIS   B 86  ? 0.1882 0.1986 0.1640 -0.0312 0.0028  0.0320  86  HIS   B O   
5148 C CB  . HIS   B 86  ? 0.1719 0.1821 0.1717 -0.0173 -0.0269 0.0058  86  HIS   B CB  
5149 C CG  . HIS   B 86  ? 0.1759 0.1927 0.1666 -0.0127 -0.0251 0.0092  86  HIS   B CG  
5150 N ND1 . HIS   B 86  ? 0.1926 0.2162 0.2037 -0.0207 -0.0284 -0.0042 86  HIS   B ND1 
5151 C CD2 . HIS   B 86  ? 0.1776 0.1968 0.1878 -0.0085 -0.0255 0.0082  86  HIS   B CD2 
5152 C CE1 . HIS   B 86  ? 0.1949 0.2076 0.1918 -0.0113 -0.0133 -0.0204 86  HIS   B CE1 
5153 N NE2 . HIS   B 86  ? 0.1902 0.1992 0.1860 0.0025  -0.0226 0.0010  86  HIS   B NE2 
5161 N N   . ASN   B 87  ? 0.1677 0.1886 0.1716 -0.0275 -0.0004 0.0336  87  ASN   B N   
5162 C CA  . ASN   B 87  ? 0.1850 0.2059 0.1779 -0.0278 0.0247  0.0192  87  ASN   B CA  
5163 C C   . ASN   B 87  ? 0.1993 0.1875 0.1693 -0.0298 0.0355  0.0171  87  ASN   B C   
5164 O O   . ASN   B 87  ? 0.2237 0.1975 0.2062 -0.0207 0.0588  0.0122  87  ASN   B O   
5165 C CB  . ASN   B 87  ? 0.1867 0.2392 0.2233 -0.0204 0.0208  0.0047  87  ASN   B CB  
5166 C CG  . ASN   B 87  ? 0.1869 0.2615 0.2364 0.0185  0.0277  0.0230  87  ASN   B CG  
5167 O OD1 . ASN   B 87  ? 0.1806 0.2423 0.2134 0.0220  0.0405  0.0433  87  ASN   B OD1 
5168 N ND2 . ASN   B 87  ? 0.2105 0.2802 0.2755 0.0179  0.0384  0.0176  87  ASN   B ND2 
5175 N N   . LEU   B 88  ? 0.1808 0.1800 0.1618 -0.0340 0.0229  0.0172  88  LEU   B N   
5176 C CA  . LEU   B 88  ? 0.1941 0.1771 0.1665 -0.0317 0.0028  0.0016  88  LEU   B CA  
5177 C C   . LEU   B 88  ? 0.1928 0.1701 0.1681 -0.0375 -0.0055 -0.0025 88  LEU   B C   
5178 O O   . LEU   B 88  ? 0.2134 0.1819 0.1958 -0.0169 -0.0255 -0.0120 88  LEU   B O   
5179 C CB  . LEU   B 88  ? 0.2014 0.1793 0.1834 -0.0453 -0.0010 0.0189  88  LEU   B CB  
5180 C CG  . LEU   B 88  ? 0.2409 0.2166 0.1985 -0.0353 -0.0263 0.0409  88  LEU   B CG  
5181 C CD1 . LEU   B 88  ? 0.2537 0.2523 0.2199 -0.0482 -0.0208 0.0495  88  LEU   B CD1 
5182 C CD2 . LEU   B 88  ? 0.2761 0.2476 0.2571 0.0059  -0.0585 0.0251  88  LEU   B CD2 
5194 N N   . ALA   B 89  ? 0.1846 0.1694 0.1580 -0.0375 0.0180  0.0041  89  ALA   B N   
5195 C CA  . ALA   B 89  ? 0.1808 0.1549 0.1360 -0.0345 0.0016  0.0150  89  ALA   B CA  
5196 C C   . ALA   B 89  ? 0.1774 0.1522 0.1533 -0.0459 0.0121  0.0041  89  ALA   B C   
5197 O O   . ALA   B 89  ? 0.1601 0.1718 0.1957 -0.0393 0.0152  -0.0271 89  ALA   B O   
5198 C CB  . ALA   B 89  ? 0.1690 0.1457 0.1716 -0.0377 0.0092  0.0139  89  ALA   B CB  
5204 N N   . LYS   B 90  ? 0.2016 0.1552 0.1636 -0.0459 -0.0117 0.0077  90  LYS   B N   
5205 C CA  . LYS   B 90  ? 0.2176 0.1579 0.1538 -0.0451 -0.0102 0.0061  90  LYS   B CA  
5206 C C   . LYS   B 90  ? 0.2077 0.1507 0.1669 -0.0444 -0.0080 -0.0076 90  LYS   B C   
5207 O O   . LYS   B 90  ? 0.2173 0.1688 0.1817 -0.0601 -0.0034 0.0023  90  LYS   B O   
5208 C CB  . LYS   B 90  ? 0.2402 0.1713 0.1928 -0.0401 0.0051  0.0105  90  LYS   B CB  
5209 C CG  . LYS   B 90  ? 0.2459 0.1810 0.1902 -0.0299 0.0274  0.0081  90  LYS   B CG  
5210 C CD  . LYS   B 90  ? 0.2757 0.2119 0.2498 -0.0192 0.0441  -0.0082 90  LYS   B CD  
5211 C CE  . LYS   B 90  ? 0.2853 0.2307 0.3025 -0.0217 0.0575  -0.0154 90  LYS   B CE  
5212 N NZ  . LYS   B 90  ? 0.2880 0.2268 0.2953 -0.0320 0.0815  -0.0170 90  LYS   B NZ  
5226 N N   . HIS   B 91  ? 0.1774 0.1413 0.1430 -0.0369 -0.0116 0.0111  91  HIS   B N   
5227 C CA  . HIS   B 91  ? 0.1728 0.1438 0.1565 -0.0230 -0.0124 0.0028  91  HIS   B CA  
5228 C C   . HIS   B 91  ? 0.1592 0.1504 0.1275 -0.0299 -0.0086 0.0088  91  HIS   B C   
5229 O O   . HIS   B 91  ? 0.1743 0.1526 0.1424 -0.0285 -0.0292 0.0010  91  HIS   B O   
5230 C CB  . HIS   B 91  ? 0.1910 0.1448 0.1893 -0.0063 -0.0155 0.0128  91  HIS   B CB  
5231 C CG  . HIS   B 91  ? 0.2345 0.1658 0.2546 -0.0011 0.0181  0.0240  91  HIS   B CG  
5232 N ND1 . HIS   B 91  ? 0.2691 0.1736 0.3168 -0.0019 0.0310  0.0167  91  HIS   B ND1 
5233 C CD2 . HIS   B 91  ? 0.2514 0.1894 0.3028 0.0102  0.0065  0.0500  91  HIS   B CD2 
5234 C CE1 . HIS   B 91  ? 0.2766 0.1829 0.3339 0.0200  0.0339  0.0134  91  HIS   B CE1 
5235 N NE2 . HIS   B 91  ? 0.2663 0.1989 0.3424 0.0286  0.0294  0.0520  91  HIS   B NE2 
5243 N N   . CYS   B 92  ? 0.1541 0.1514 0.1401 -0.0282 -0.0098 0.0002  92  CYS   B N   
5244 C CA  . CYS   B 92  ? 0.1659 0.1391 0.1345 -0.0246 -0.0055 -0.0042 92  CYS   B CA  
5245 C C   . CYS   B 92  ? 0.1585 0.1310 0.1274 -0.0142 -0.0009 -0.0070 92  CYS   B C   
5246 O O   . CYS   B 92  ? 0.1624 0.1447 0.1484 -0.0147 -0.0040 -0.0007 92  CYS   B O   
5247 C CB  . CYS   B 92  ? 0.1658 0.1430 0.1400 -0.0159 -0.0074 0.0051  92  CYS   B CB  
5248 S SG  . CYS   B 92  ? 0.1562 0.1532 0.1518 -0.0110 -0.0096 0.0072  92  CYS   B SG  
5254 N N   . LEU   B 93  ? 0.1520 0.1375 0.1291 -0.0168 0.0008  -0.0061 93  LEU   B N   
5255 C CA  . LEU   B 93  ? 0.1602 0.1365 0.1223 -0.0065 -0.0114 -0.0012 93  LEU   B CA  
5256 C C   . LEU   B 93  ? 0.1402 0.1364 0.1265 0.0014  -0.0085 0.0011  93  LEU   B C   
5257 O O   . LEU   B 93  ? 0.1428 0.1399 0.1529 -0.0043 -0.0036 -0.0045 93  LEU   B O   
5258 C CB  . LEU   B 93  ? 0.1565 0.1415 0.1529 -0.0003 -0.0130 0.0009  93  LEU   B CB  
5259 C CG  . LEU   B 93  ? 0.1456 0.1508 0.1760 -0.0004 0.0009  0.0105  93  LEU   B CG  
5260 C CD1 . LEU   B 93  ? 0.1432 0.1654 0.1859 0.0091  0.0086  -0.0047 93  LEU   B CD1 
5261 C CD2 . LEU   B 93  ? 0.1417 0.1509 0.1759 -0.0014 -0.0081 -0.0047 93  LEU   B CD2 
5273 N N   . HIS   B 94  ? 0.1476 0.1221 0.1368 -0.0073 -0.0123 0.0043  94  HIS   B N   
5274 C CA  . HIS   B 94  ? 0.1513 0.1293 0.1310 -0.0071 0.0025  0.0039  94  HIS   B CA  
5275 C C   . HIS   B 94  ? 0.1414 0.1331 0.1523 -0.0077 0.0016  0.0107  94  HIS   B C   
5276 O O   . HIS   B 94  ? 0.1432 0.1472 0.1929 -0.0031 0.0182  -0.0076 94  HIS   B O   
5277 C CB  . HIS   B 94  ? 0.1485 0.1442 0.1404 0.0005  -0.0011 0.0028  94  HIS   B CB  
5278 C CG  . HIS   B 94  ? 0.1463 0.1409 0.1476 -0.0097 -0.0204 0.0010  94  HIS   B CG  
5279 N ND1 . HIS   B 94  ? 0.1606 0.1430 0.1459 -0.0112 -0.0183 0.0012  94  HIS   B ND1 
5280 C CD2 . HIS   B 94  ? 0.1506 0.1443 0.1499 0.0014  -0.0036 -0.0002 94  HIS   B CD2 
5281 C CE1 . HIS   B 94  ? 0.1605 0.1443 0.1541 -0.0118 -0.0152 0.0039  94  HIS   B CE1 
5282 N NE2 . HIS   B 94  ? 0.1522 0.1462 0.1607 -0.0104 -0.0112 0.0073  94  HIS   B NE2 
5290 N N   . VAL   B 95  ? 0.1354 0.1334 0.1587 -0.0043 0.0014  0.0086  95  VAL   B N   
5291 C CA  . VAL   B 95  ? 0.1448 0.1421 0.1497 -0.0011 0.0065  0.0165  95  VAL   B CA  
5292 C C   . VAL   B 95  ? 0.1462 0.1489 0.1403 0.0013  0.0105  0.0037  95  VAL   B C   
5293 O O   . VAL   B 95  ? 0.1490 0.1494 0.1646 0.0089  0.0100  0.0174  95  VAL   B O   
5294 C CB  . VAL   B 95  ? 0.1558 0.1314 0.1542 -0.0071 -0.0026 -0.0012 95  VAL   B CB  
5295 C CG1 . VAL   B 95  ? 0.1660 0.1528 0.1722 -0.0133 -0.0010 0.0077  95  VAL   B CG1 
5296 C CG2 . VAL   B 95  ? 0.1648 0.1337 0.1548 0.0063  -0.0143 0.0059  95  VAL   B CG2 
5306 N N   . VAL   B 96  ? 0.1586 0.1543 0.1482 0.0111  0.0104  0.0124  96  VAL   B N   
5307 C CA  . VAL   B 96  ? 0.1656 0.1613 0.1326 0.0064  0.0097  0.0205  96  VAL   B CA  
5308 C C   . VAL   B 96  ? 0.1701 0.1610 0.1595 0.0141  0.0149  0.0103  96  VAL   B C   
5309 O O   . VAL   B 96  ? 0.1704 0.1589 0.1745 0.0042  0.0198  -0.0041 96  VAL   B O   
5310 C CB  . VAL   B 96  ? 0.1693 0.1786 0.1366 0.0084  0.0072  0.0097  96  VAL   B CB  
5311 C CG1 . VAL   B 96  ? 0.1765 0.1984 0.1448 0.0172  0.0096  -0.0002 96  VAL   B CG1 
5312 C CG2 . VAL   B 96  ? 0.1852 0.1782 0.1564 0.0012  0.0125  0.0016  96  VAL   B CG2 
5322 N N   . GLY   B 97  ? 0.1747 0.1589 0.1576 0.0059  0.0077  0.0217  97  GLY   B N   
5323 C CA  . GLY   B 97  ? 0.1912 0.1662 0.1537 -0.0015 0.0126  0.0267  97  GLY   B CA  
5324 C C   . GLY   B 97  ? 0.2110 0.1728 0.1752 0.0002  0.0021  0.0150  97  GLY   B C   
5325 O O   . GLY   B 97  ? 0.2139 0.1804 0.1752 0.0022  0.0037  0.0108  97  GLY   B O   
5329 N N   . PRO   B 98  ? 0.2188 0.1762 0.1753 0.0021  0.0302  0.0303  98  PRO   B N   
5330 C CA  . PRO   B 98  ? 0.2283 0.1896 0.1824 0.0092  0.0386  0.0227  98  PRO   B CA  
5331 C C   . PRO   B 98  ? 0.2379 0.1912 0.1548 0.0233  0.0372  0.0351  98  PRO   B C   
5332 O O   . PRO   B 98  ? 0.2309 0.1876 0.1693 0.0260  0.0317  0.0366  98  PRO   B O   
5333 C CB  . PRO   B 98  ? 0.2170 0.1947 0.1871 0.0085  0.0558  0.0275  98  PRO   B CB  
5334 C CG  . PRO   B 98  ? 0.2090 0.1935 0.1958 0.0071  0.0480  0.0360  98  PRO   B CG  
5335 C CD  . PRO   B 98  ? 0.1985 0.1804 0.1961 0.0091  0.0378  0.0365  98  PRO   B CD  
5343 N N   . ASN   B 99  ? 0.2482 0.2089 0.1812 0.0395  0.0364  0.0152  99  ASN   B N   
5344 C CA  . ASN   B 99  ? 0.2629 0.2147 0.1759 0.0457  0.0256  0.0396  99  ASN   B CA  
5345 C C   . ASN   B 99  ? 0.2889 0.2494 0.2008 0.0413  0.0422  0.0631  99  ASN   B C   
5346 O O   . ASN   B 99  ? 0.3040 0.2544 0.2077 0.0418  0.0312  0.0614  99  ASN   B O   
5347 C CB  . ASN   B 99  ? 0.2690 0.2120 0.1891 0.0441  0.0110  0.0369  99  ASN   B CB  
5348 C CG  . ASN   B 99  ? 0.2736 0.2213 0.2219 0.0359  0.0015  0.0278  99  ASN   B CG  
5349 O OD1 . ASN   B 99  ? 0.2752 0.2241 0.2473 0.0407  -0.0012 0.0365  99  ASN   B OD1 
5350 N ND2 . ASN   B 99  ? 0.2733 0.2202 0.2218 0.0414  -0.0165 0.0242  99  ASN   B ND2 
5357 N N   A VAL   B 100 ? 0.3027 0.2628 0.2392 0.0302  0.0469  0.0802  100 VAL   B N   
5358 N N   B VAL   B 100 ? 0.3092 0.2654 0.2420 0.0365  0.0342  0.0734  100 VAL   B N   
5359 C CA  A VAL   B 100 ? 0.3301 0.2833 0.3004 0.0215  0.0476  0.0868  100 VAL   B CA  
5360 C CA  B VAL   B 100 ? 0.3316 0.2810 0.2837 0.0319  0.0252  0.0797  100 VAL   B CA  
5361 C C   A VAL   B 100 ? 0.3495 0.2873 0.2876 0.0283  0.0489  0.1043  100 VAL   B C   
5362 C C   B VAL   B 100 ? 0.3485 0.2879 0.2882 0.0353  0.0242  0.0982  100 VAL   B C   
5363 O O   A VAL   B 100 ? 0.3581 0.2967 0.3012 0.0191  0.0685  0.0970  100 VAL   B O   
5364 O O   B VAL   B 100 ? 0.3510 0.2918 0.2914 0.0329  0.0255  0.0978  100 VAL   B O   
5365 C CB  A VAL   B 100 ? 0.3413 0.3026 0.3728 -0.0023 0.0478  0.0918  100 VAL   B CB  
5366 C CB  B VAL   B 100 ? 0.3373 0.2894 0.3160 0.0234  0.0190  0.0702  100 VAL   B CB  
5367 C CG1 A VAL   B 100 ? 0.3482 0.3089 0.3989 -0.0035 0.0526  0.0933  100 VAL   B CG1 
5368 C CG1 B VAL   B 100 ? 0.3397 0.2920 0.3280 0.0219  0.0175  0.0675  100 VAL   B CG1 
5369 C CG2 A VAL   B 100 ? 0.3421 0.3091 0.3948 -0.0105 0.0510  0.0983  100 VAL   B CG2 
5370 C CG2 B VAL   B 100 ? 0.3388 0.2924 0.3273 0.0203  0.0175  0.0676  100 VAL   B CG2 
5389 N N   . ASN   B 101 ? 0.3626 0.2917 0.2869 0.0414  0.0241  0.1142  101 ASN   B N   
5390 C CA  . ASN   B 101 ? 0.4043 0.3146 0.3157 0.0495  0.0034  0.1214  101 ASN   B CA  
5391 C C   . ASN   B 101 ? 0.4543 0.3592 0.3282 0.0493  -0.0075 0.1206  101 ASN   B C   
5392 O O   . ASN   B 101 ? 0.4633 0.3696 0.3504 0.0566  -0.0010 0.0967  101 ASN   B O   
5393 C CB  . ASN   B 101 ? 0.3981 0.3034 0.3351 0.0476  0.0079  0.1095  101 ASN   B CB  
5394 C CG  . ASN   B 101 ? 0.3917 0.2958 0.3390 0.0447  0.0151  0.1082  101 ASN   B CG  
5395 O OD1 . ASN   B 101 ? 0.3957 0.2981 0.3674 0.0365  0.0327  0.1028  101 ASN   B OD1 
5396 N ND2 . ASN   B 101 ? 0.3831 0.2923 0.3269 0.0468  0.0087  0.0958  101 ASN   B ND2 
5404 N N   A LYS   B 102 ? 0.4782 0.3768 0.3338 0.0409  -0.0056 0.1152  102 LYS   B N   
5405 N N   B LYS   B 102 ? 0.4705 0.3823 0.3542 0.0406  -0.0051 0.1083  102 LYS   B N   
5406 C CA  A LYS   B 102 ? 0.5018 0.4047 0.3528 0.0271  0.0016  0.0949  102 LYS   B CA  
5407 C CA  B LYS   B 102 ? 0.4848 0.4045 0.3799 0.0315  0.0007  0.0928  102 LYS   B CA  
5408 C C   A LYS   B 102 ? 0.5013 0.4066 0.3316 0.0292  0.0084  0.0951  102 LYS   B C   
5409 C C   B LYS   B 102 ? 0.4875 0.4059 0.3614 0.0289  0.0105  0.0949  102 LYS   B C   
5410 O O   A LYS   B 102 ? 0.5125 0.4126 0.3324 0.0297  -0.0012 0.0874  102 LYS   B O   
5411 O O   B LYS   B 102 ? 0.4906 0.4092 0.3682 0.0271  0.0066  0.0946  102 LYS   B O   
5412 C CB  A LYS   B 102 ? 0.5218 0.4296 0.4118 0.0129  0.0138  0.0604  102 LYS   B CB  
5413 C CB  B LYS   B 102 ? 0.4943 0.4226 0.4232 0.0261  0.0006  0.0722  102 LYS   B CB  
5414 C CG  A LYS   B 102 ? 0.5380 0.4529 0.4723 0.0030  0.0261  0.0274  102 LYS   B CG  
5415 C CG  B LYS   B 102 ? 0.5023 0.4378 0.4601 0.0223  0.0018  0.0524  102 LYS   B CG  
5416 C CD  A LYS   B 102 ? 0.5536 0.4724 0.5349 -0.0043 0.0369  0.0036  102 LYS   B CD  
5417 C CD  B LYS   B 102 ? 0.5092 0.4495 0.4940 0.0196  0.0034  0.0363  102 LYS   B CD  
5418 C CE  A LYS   B 102 ? 0.5661 0.4866 0.5831 -0.0097 0.0435  -0.0142 102 LYS   B CE  
5419 C CE  B LYS   B 102 ? 0.5144 0.4576 0.5182 0.0179  0.0046  0.0240  102 LYS   B CE  
5420 N NZ  A LYS   B 102 ? 0.5731 0.4960 0.6120 -0.0126 0.0447  -0.0245 102 LYS   B NZ  
5421 N NZ  B LYS   B 102 ? 0.5175 0.4621 0.5313 0.0171  0.0048  0.0171  102 LYS   B NZ  
5448 N N   . GLY   B 103 ? 0.4844 0.4008 0.3377 0.0292  0.0265  0.0930  103 GLY   B N   
5449 C CA  . GLY   B 103 ? 0.4651 0.3917 0.3437 0.0298  0.0559  0.0707  103 GLY   B CA  
5450 C C   . GLY   B 103 ? 0.4409 0.3778 0.3337 0.0260  0.0777  0.0541  103 GLY   B C   
5451 O O   . GLY   B 103 ? 0.4516 0.3912 0.3458 0.0255  0.0807  0.0552  103 GLY   B O   
5456 N N   A GLU   B 104 ? 0.4177 0.3500 0.3077 0.0252  0.1059  0.0394  104 GLU   B N   
5457 N N   B GLU   B 104 ? 0.4272 0.3750 0.3395 0.0205  0.0602  0.0418  104 GLU   B N   
5458 C CA  A GLU   B 104 ? 0.3947 0.3260 0.2760 0.0235  0.1195  0.0331  104 GLU   B CA  
5459 C CA  B GLU   B 104 ? 0.4128 0.3715 0.3395 0.0146  0.0436  0.0296  104 GLU   B CA  
5460 C C   A GLU   B 104 ? 0.4066 0.3316 0.3006 0.0085  0.1476  0.0300  104 GLU   B C   
5461 C C   B GLU   B 104 ? 0.4071 0.3721 0.3519 0.0086  0.0410  0.0234  104 GLU   B C   
5462 O O   A GLU   B 104 ? 0.4112 0.3349 0.3249 0.0030  0.1408  0.0247  104 GLU   B O   
5463 O O   B GLU   B 104 ? 0.4075 0.3732 0.3549 0.0073  0.0403  0.0225  104 GLU   B O   
5464 C CB  A GLU   B 104 ? 0.3684 0.2968 0.2561 0.0324  0.0837  0.0188  104 GLU   B CB  
5465 C CB  B GLU   B 104 ? 0.4051 0.3670 0.3279 0.0142  0.0309  0.0221  104 GLU   B CB  
5466 C CG  A GLU   B 104 ? 0.3511 0.2800 0.2319 0.0374  0.0425  -0.0070 104 GLU   B CG  
5467 C CG  B GLU   B 104 ? 0.3995 0.3639 0.3178 0.0139  0.0196  0.0132  104 GLU   B CG  
5468 C CD  A GLU   B 104 ? 0.3377 0.2655 0.2164 0.0372  0.0119  -0.0148 104 GLU   B CD  
5469 C CD  B GLU   B 104 ? 0.3958 0.3618 0.3097 0.0136  0.0111  0.0064  104 GLU   B CD  
5470 O OE1 A GLU   B 104 ? 0.3155 0.2520 0.1936 0.0370  0.0216  -0.0084 104 GLU   B OE1 
5471 O OE1 B GLU   B 104 ? 0.3938 0.3605 0.3037 0.0132  0.0109  0.0057  104 GLU   B OE1 
5472 O OE2 A GLU   B 104 ? 0.3447 0.2799 0.2407 0.0322  -0.0272 -0.0277 104 GLU   B OE2 
5473 O OE2 B GLU   B 104 ? 0.3954 0.3628 0.3116 0.0136  0.0048  0.0017  104 GLU   B OE2 
5486 N N   A ASP   B 105 ? 0.4093 0.3394 0.3068 -0.0051 0.1754  0.0390  105 ASP   B N   
5487 N N   B ASP   B 105 ? 0.4005 0.3716 0.3591 0.0038  0.0389  0.0185  105 ASP   B N   
5488 C CA  A ASP   B 105 ? 0.4189 0.3482 0.3375 -0.0173 0.1987  0.0269  105 ASP   B CA  
5489 C CA  B ASP   B 105 ? 0.3951 0.3709 0.3704 -0.0007 0.0368  0.0116  105 ASP   B CA  
5490 C C   A ASP   B 105 ? 0.4044 0.3129 0.3217 -0.0293 0.1970  0.0134  105 ASP   B C   
5491 C C   B ASP   B 105 ? 0.3870 0.3644 0.3565 -0.0024 0.0356  0.0054  105 ASP   B C   
5492 O O   A ASP   B 105 ? 0.3929 0.2993 0.3195 -0.0317 0.2039  0.0076  105 ASP   B O   
5493 O O   B ASP   B 105 ? 0.3872 0.3639 0.3514 -0.0028 0.0357  0.0053  105 ASP   B O   
5494 C CB  A ASP   B 105 ? 0.4385 0.3838 0.4059 -0.0113 0.2098  0.0133  105 ASP   B CB  
5495 C CB  B ASP   B 105 ? 0.3967 0.3754 0.3923 -0.0019 0.0363  0.0102  105 ASP   B CB  
5496 C CG  A ASP   B 105 ? 0.4562 0.4114 0.4776 -0.0078 0.2189  0.0019  105 ASP   B CG  
5497 C CG  B ASP   B 105 ? 0.3983 0.3784 0.4144 -0.0036 0.0361  0.0100  105 ASP   B CG  
5498 O OD1 A ASP   B 105 ? 0.4567 0.4174 0.4730 -0.0205 0.2389  0.0164  105 ASP   B OD1 
5499 O OD1 B ASP   B 105 ? 0.3984 0.3799 0.4201 -0.0061 0.0359  0.0112  105 ASP   B OD1 
5500 O OD2 A ASP   B 105 ? 0.4661 0.4275 0.5286 0.0030  0.2005  -0.0178 105 ASP   B OD2 
5501 O OD2 B ASP   B 105 ? 0.3982 0.3793 0.4215 -0.0040 0.0365  0.0101  105 ASP   B OD2 
5510 N N   A ILE   B 106 ? 0.3959 0.2887 0.3301 -0.0313 0.1771  0.0154  106 ILE   B N   
5511 N N   B ILE   B 106 ? 0.3778 0.3575 0.3450 -0.0023 0.0334  0.0011  106 ILE   B N   
5512 C CA  A ILE   B 106 ? 0.3737 0.2610 0.3404 -0.0408 0.1715  0.0129  106 ILE   B CA  
5513 C CA  B ILE   B 106 ? 0.3669 0.3504 0.3385 -0.0023 0.0335  -0.0031 106 ILE   B CA  
5514 C C   A ILE   B 106 ? 0.3319 0.2581 0.3279 -0.0389 0.1682  -0.0098 106 ILE   B C   
5515 C C   B ILE   B 106 ? 0.3527 0.3435 0.3330 -0.0017 0.0369  -0.0078 106 ILE   B C   
5516 O O   A ILE   B 106 ? 0.3202 0.2410 0.3280 -0.0460 0.1534  -0.0173 106 ILE   B O   
5517 O O   B ILE   B 106 ? 0.3519 0.3426 0.3298 -0.0021 0.0339  -0.0091 106 ILE   B O   
5518 C CB  A ILE   B 106 ? 0.3977 0.2496 0.3637 -0.0469 0.1627  0.0275  106 ILE   B CB  
5519 C CB  B ILE   B 106 ? 0.3698 0.3503 0.3396 -0.0031 0.0308  -0.0028 106 ILE   B CB  
5520 C CG1 A ILE   B 106 ? 0.4111 0.2524 0.3815 -0.0314 0.1465  0.0231  106 ILE   B CG1 
5521 C CG1 B ILE   B 106 ? 0.3703 0.3493 0.3409 -0.0018 0.0280  -0.0018 106 ILE   B CG1 
5522 C CG2 A ILE   B 106 ? 0.4049 0.2553 0.3908 -0.0571 0.1611  0.0294  106 ILE   B CG2 
5523 C CG2 B ILE   B 106 ? 0.3714 0.3520 0.3425 -0.0041 0.0304  -0.0036 106 ILE   B CG2 
5524 C CD1 A ILE   B 106 ? 0.4174 0.2607 0.3822 -0.0183 0.1412  0.0257  106 ILE   B CD1 
5525 C CD1 B ILE   B 106 ? 0.3703 0.3489 0.3415 -0.0002 0.0265  -0.0011 106 ILE   B CD1 
5548 N N   A GLN   B 107 ? 0.3179 0.2815 0.3476 -0.0379 0.1550  -0.0159 107 GLN   B N   
5549 N N   B GLN   B 107 ? 0.3400 0.3376 0.3360 -0.0017 0.0426  -0.0107 107 GLN   B N   
5550 C CA  A GLN   B 107 ? 0.3011 0.3016 0.3547 -0.0412 0.1408  -0.0079 107 GLN   B CA  
5551 C CA  B GLN   B 107 ? 0.3263 0.3301 0.3391 -0.0016 0.0484  -0.0109 107 GLN   B CA  
5552 C C   A GLN   B 107 ? 0.2765 0.2860 0.3227 -0.0194 0.0980  -0.0153 107 GLN   B C   
5553 C C   B GLN   B 107 ? 0.2958 0.3040 0.3030 0.0010  0.0621  -0.0138 107 GLN   B C   
5554 O O   A GLN   B 107 ? 0.2656 0.2915 0.3754 -0.0066 0.0643  -0.0347 107 GLN   B O   
5555 O O   B GLN   B 107 ? 0.2963 0.3063 0.3088 0.0017  0.0566  -0.0184 107 GLN   B O   
5556 C CB  A GLN   B 107 ? 0.3331 0.3454 0.4198 -0.0467 0.1314  -0.0019 107 GLN   B CB  
5557 C CB  B GLN   B 107 ? 0.3433 0.3476 0.3841 -0.0025 0.0389  -0.0087 107 GLN   B CB  
5558 C CG  A GLN   B 107 ? 0.3691 0.3897 0.4898 -0.0411 0.0981  0.0004  107 GLN   B CG  
5559 C CG  B GLN   B 107 ? 0.3574 0.3625 0.4261 -0.0022 0.0288  -0.0057 107 GLN   B CG  
5560 C CD  A GLN   B 107 ? 0.3904 0.4215 0.5442 -0.0412 0.0743  0.0067  107 GLN   B CD  
5561 C CD  B GLN   B 107 ? 0.3672 0.3735 0.4605 -0.0026 0.0213  -0.0022 107 GLN   B CD  
5562 O OE1 A GLN   B 107 ? 0.3985 0.4347 0.5634 -0.0399 0.0773  0.0046  107 GLN   B OE1 
5563 O OE1 B GLN   B 107 ? 0.3707 0.3776 0.4722 -0.0029 0.0210  -0.0017 107 GLN   B OE1 
5564 N NE2 A GLN   B 107 ? 0.3995 0.4307 0.5640 -0.0362 0.0579  0.0147  107 GLN   B NE2 
5565 N NE2 B GLN   B 107 ? 0.3708 0.3772 0.4729 -0.0018 0.0177  0.0004  107 GLN   B NE2 
5582 N N   . LEU   B 108 ? 0.2633 0.2745 0.2710 0.0043  0.0798  -0.0131 108 LEU   B N   
5583 C CA  . LEU   B 108 ? 0.2430 0.2502 0.2344 0.0244  0.0602  0.0029  108 LEU   B CA  
5584 C C   . LEU   B 108 ? 0.2081 0.2103 0.2145 0.0235  0.0359  0.0162  108 LEU   B C   
5585 O O   . LEU   B 108 ? 0.2122 0.2051 0.2109 0.0234  0.0270  0.0169  108 LEU   B O   
5586 C CB  . LEU   B 108 ? 0.2600 0.2722 0.2243 0.0245  0.0716  0.0047  108 LEU   B CB  
5587 C CG  . LEU   B 108 ? 0.2788 0.3008 0.2406 0.0294  0.0613  -0.0149 108 LEU   B CG  
5588 C CD1 . LEU   B 108 ? 0.2880 0.3147 0.2236 0.0167  0.0614  -0.0143 108 LEU   B CD1 
5589 C CD2 . LEU   B 108 ? 0.2940 0.3095 0.2506 0.0382  0.0518  -0.0260 108 LEU   B CD2 
5602 N N   . LEU   B 109 ? 0.1943 0.1894 0.2082 0.0173  0.0324  0.0089  109 LEU   B N   
5603 C CA  . LEU   B 109 ? 0.1788 0.1605 0.2234 0.0062  0.0313  0.0252  109 LEU   B CA  
5604 C C   . LEU   B 109 ? 0.1601 0.1485 0.2294 0.0016  0.0321  0.0243  109 LEU   B C   
5605 O O   . LEU   B 109 ? 0.1618 0.1477 0.2247 0.0088  0.0244  0.0241  109 LEU   B O   
5606 C CB  . LEU   B 109 ? 0.1930 0.1495 0.2386 0.0046  0.0192  0.0298  109 LEU   B CB  
5607 C CG  . LEU   B 109 ? 0.1834 0.1468 0.2292 0.0065  0.0185  0.0153  109 LEU   B CG  
5608 C CD1 . LEU   B 109 ? 0.1805 0.1588 0.2249 0.0079  0.0172  0.0167  109 LEU   B CD1 
5609 C CD2 . LEU   B 109 ? 0.2024 0.1573 0.2456 0.0011  0.0175  0.0153  109 LEU   B CD2 
5621 N N   . LYS   B 110 ? 0.1575 0.1513 0.2230 -0.0035 0.0255  0.0217  110 LYS   B N   
5622 C CA  . LYS   B 110 ? 0.1505 0.1498 0.2199 -0.0028 0.0244  0.0157  110 LYS   B CA  
5623 C C   . LYS   B 110 ? 0.1525 0.1479 0.2138 -0.0058 0.0363  0.0097  110 LYS   B C   
5624 O O   . LYS   B 110 ? 0.1534 0.1467 0.2180 -0.0073 0.0233  -0.0015 110 LYS   B O   
5625 C CB  . LYS   B 110 ? 0.1589 0.1476 0.2444 -0.0003 0.0270  0.0092  110 LYS   B CB  
5626 C CG  . LYS   B 110 ? 0.1593 0.1514 0.2582 -0.0105 0.0105  0.0160  110 LYS   B CG  
5627 C CD  . LYS   B 110 ? 0.1679 0.1544 0.2681 -0.0084 0.0090  0.0112  110 LYS   B CD  
5628 C CE  . LYS   B 110 ? 0.1685 0.1736 0.2857 -0.0049 0.0168  0.0020  110 LYS   B CE  
5629 N NZ  . LYS   B 110 ? 0.1639 0.1858 0.2806 0.0015  0.0094  -0.0010 110 LYS   B NZ  
5643 N N   . SER   B 111 ? 0.1617 0.1516 0.2337 -0.0116 0.0364  0.0153  111 SER   B N   
5644 C CA  . SER   B 111 ? 0.1692 0.1543 0.2204 -0.0078 0.0260  0.0144  111 SER   B CA  
5645 C C   . SER   B 111 ? 0.1581 0.1501 0.2164 -0.0097 0.0160  0.0030  111 SER   B C   
5646 O O   . SER   B 111 ? 0.1528 0.1499 0.2221 -0.0048 0.0151  0.0053  111 SER   B O   
5647 C CB  . SER   B 111 ? 0.1855 0.1731 0.2292 0.0008  0.0354  0.0225  111 SER   B CB  
5648 O OG  . SER   B 111 ? 0.2049 0.2106 0.2301 0.0084  0.0491  0.0194  111 SER   B OG  
5654 N N   . ALA   B 112 ? 0.1555 0.1469 0.2126 0.0075  0.0244  0.0138  112 ALA   B N   
5655 C CA  . ALA   B 112 ? 0.1444 0.1618 0.1902 0.0001  0.0182  0.0043  112 ALA   B CA  
5656 C C   . ALA   B 112 ? 0.1334 0.1530 0.1946 -0.0009 0.0142  0.0095  112 ALA   B C   
5657 O O   . ALA   B 112 ? 0.1413 0.1531 0.2021 -0.0056 0.0071  0.0008  112 ALA   B O   
5658 C CB  . ALA   B 112 ? 0.1527 0.1700 0.2020 0.0045  0.0045  0.0152  112 ALA   B CB  
5664 N N   . TYR   B 113 ? 0.1351 0.1370 0.2044 -0.0018 0.0104  0.0070  113 TYR   B N   
5665 C CA  . TYR   B 113 ? 0.1328 0.1437 0.1923 -0.0069 0.0080  -0.0016 113 TYR   B CA  
5666 C C   . TYR   B 113 ? 0.1286 0.1251 0.2003 -0.0036 0.0114  0.0045  113 TYR   B C   
5667 O O   . TYR   B 113 ? 0.1392 0.1348 0.1967 -0.0017 0.0047  -0.0020 113 TYR   B O   
5668 C CB  . TYR   B 113 ? 0.1379 0.1407 0.1872 -0.0010 0.0178  0.0083  113 TYR   B CB  
5669 C CG  . TYR   B 113 ? 0.1463 0.1507 0.1999 -0.0075 0.0128  0.0167  113 TYR   B CG  
5670 C CD1 . TYR   B 113 ? 0.1527 0.1493 0.2167 -0.0054 0.0184  0.0232  113 TYR   B CD1 
5671 C CD2 . TYR   B 113 ? 0.1528 0.1526 0.2020 0.0012  0.0097  0.0130  113 TYR   B CD2 
5672 C CE1 . TYR   B 113 ? 0.1467 0.1561 0.2067 -0.0078 0.0230  0.0144  113 TYR   B CE1 
5673 C CE2 . TYR   B 113 ? 0.1585 0.1484 0.2122 0.0033  0.0034  0.0119  113 TYR   B CE2 
5674 C CZ  . TYR   B 113 ? 0.1441 0.1515 0.2166 0.0035  0.0116  0.0074  113 TYR   B CZ  
5675 O OH  . TYR   B 113 ? 0.1613 0.1479 0.2377 0.0155  0.0174  0.0062  113 TYR   B OH  
5685 N N   . GLU   B 114 ? 0.1283 0.1352 0.2065 0.0009  0.0137  0.0033  114 GLU   B N   
5686 C CA  . GLU   B 114 ? 0.1394 0.1341 0.1909 0.0069  0.0030  -0.0035 114 GLU   B CA  
5687 C C   . GLU   B 114 ? 0.1394 0.1373 0.1781 0.0125  0.0024  -0.0040 114 GLU   B C   
5688 O O   . GLU   B 114 ? 0.1348 0.1390 0.2017 0.0117  -0.0068 0.0038  114 GLU   B O   
5689 C CB  . GLU   B 114 ? 0.1431 0.1381 0.2056 0.0076  0.0072  0.0038  114 GLU   B CB  
5690 C CG  . GLU   B 114 ? 0.1508 0.1380 0.2042 -0.0035 0.0116  0.0034  114 GLU   B CG  
5691 C CD  . GLU   B 114 ? 0.1491 0.1436 0.2125 -0.0105 0.0080  0.0029  114 GLU   B CD  
5692 O OE1 . GLU   B 114 ? 0.1451 0.1557 0.2154 -0.0068 0.0165  0.0066  114 GLU   B OE1 
5693 O OE2 . GLU   B 114 ? 0.1498 0.1565 0.2337 -0.0230 0.0090  -0.0005 114 GLU   B OE2 
5700 N N   . ASN   B 115 ? 0.1443 0.1296 0.1742 0.0012  -0.0059 0.0031  115 ASN   B N   
5701 C CA  . ASN   B 115 ? 0.1447 0.1403 0.1702 -0.0078 0.0001  0.0028  115 ASN   B CA  
5702 C C   . ASN   B 115 ? 0.1302 0.1442 0.1788 -0.0151 -0.0007 -0.0094 115 ASN   B C   
5703 O O   . ASN   B 115 ? 0.1457 0.1433 0.1897 -0.0173 0.0060  -0.0032 115 ASN   B O   
5704 C CB  . ASN   B 115 ? 0.1627 0.1478 0.1799 -0.0023 0.0033  0.0075  115 ASN   B CB  
5705 C CG  . ASN   B 115 ? 0.1605 0.1624 0.1837 0.0054  0.0043  -0.0002 115 ASN   B CG  
5706 O OD1 . ASN   B 115 ? 0.2111 0.1746 0.2041 0.0065  0.0134  -0.0124 115 ASN   B OD1 
5707 N ND2 . ASN   B 115 ? 0.1466 0.1753 0.1807 -0.0043 0.0102  0.0089  115 ASN   B ND2 
5714 N N   . PHE   B 116 ? 0.1380 0.1404 0.1706 -0.0021 -0.0015 -0.0117 116 PHE   B N   
5715 C CA  . PHE   B 116 ? 0.1397 0.1351 0.1754 -0.0085 -0.0068 -0.0145 116 PHE   B CA  
5716 C C   . PHE   B 116 ? 0.1413 0.1254 0.1728 -0.0087 -0.0030 0.0017  116 PHE   B C   
5717 O O   . PHE   B 116 ? 0.1475 0.1363 0.1834 -0.0047 -0.0077 0.0056  116 PHE   B O   
5718 C CB  . PHE   B 116 ? 0.1410 0.1272 0.1641 -0.0023 -0.0051 0.0043  116 PHE   B CB  
5719 C CG  . PHE   B 116 ? 0.1282 0.1387 0.1682 -0.0022 0.0032  0.0007  116 PHE   B CG  
5720 C CD1 . PHE   B 116 ? 0.1356 0.1384 0.1841 0.0004  0.0070  0.0006  116 PHE   B CD1 
5721 C CD2 . PHE   B 116 ? 0.1356 0.1480 0.1663 0.0000  -0.0003 -0.0028 116 PHE   B CD2 
5722 C CE1 . PHE   B 116 ? 0.1450 0.1445 0.1914 0.0024  -0.0073 0.0013  116 PHE   B CE1 
5723 C CE2 . PHE   B 116 ? 0.1376 0.1479 0.1763 0.0001  0.0018  0.0065  116 PHE   B CE2 
5724 C CZ  . PHE   B 116 ? 0.1286 0.1492 0.1833 -0.0001 -0.0114 0.0046  116 PHE   B CZ  
5734 N N   . ASN   B 117 ? 0.1439 0.1315 0.1886 -0.0011 -0.0115 0.0011  117 ASN   B N   
5735 C CA  . ASN   B 117 ? 0.1541 0.1325 0.1856 -0.0053 -0.0010 -0.0016 117 ASN   B CA  
5736 C C   . ASN   B 117 ? 0.1542 0.1242 0.1879 -0.0087 -0.0040 -0.0005 117 ASN   B C   
5737 O O   . ASN   B 117 ? 0.1557 0.1413 0.2146 -0.0066 -0.0281 0.0034  117 ASN   B O   
5738 C CB  . ASN   B 117 ? 0.1504 0.1357 0.2035 -0.0002 0.0064  0.0076  117 ASN   B CB  
5739 C CG  . ASN   B 117 ? 0.1385 0.1300 0.2122 -0.0013 0.0004  0.0021  117 ASN   B CG  
5740 O OD1 . ASN   B 117 ? 0.1638 0.1418 0.2260 -0.0090 0.0048  -0.0102 117 ASN   B OD1 
5741 N ND2 . ASN   B 117 ? 0.1478 0.1386 0.2027 -0.0068 0.0022  0.0022  117 ASN   B ND2 
5748 N N   . GLN   B 118 ? 0.1507 0.1240 0.1992 -0.0113 -0.0172 -0.0014 118 GLN   B N   
5749 C CA  . GLN   B 118 ? 0.1526 0.1330 0.2018 0.0003  -0.0149 -0.0007 118 GLN   B CA  
5750 C C   . GLN   B 118 ? 0.1520 0.1368 0.2096 -0.0055 -0.0038 -0.0006 118 GLN   B C   
5751 O O   . GLN   B 118 ? 0.1707 0.1362 0.2458 -0.0102 0.0078  0.0107  118 GLN   B O   
5752 C CB  . GLN   B 118 ? 0.1653 0.1411 0.2100 0.0011  -0.0166 -0.0019 118 GLN   B CB  
5753 C CG  . GLN   B 118 ? 0.1723 0.1514 0.2102 0.0089  -0.0091 -0.0160 118 GLN   B CG  
5754 C CD  . GLN   B 118 ? 0.1793 0.1420 0.2083 -0.0000 -0.0084 -0.0188 118 GLN   B CD  
5755 O OE1 . GLN   B 118 ? 0.1856 0.1426 0.2241 -0.0006 0.0114  0.0017  118 GLN   B OE1 
5756 N NE2 . GLN   B 118 ? 0.1932 0.1376 0.2233 0.0011  -0.0184 0.0004  118 GLN   B NE2 
5765 N N   . HIS   B 119 ? 0.1597 0.1421 0.1800 -0.0068 -0.0069 -0.0027 119 HIS   B N   
5766 C CA  . HIS   B 119 ? 0.1708 0.1503 0.1671 -0.0060 -0.0140 0.0034  119 HIS   B CA  
5767 C C   . HIS   B 119 ? 0.1606 0.1472 0.1701 -0.0111 -0.0255 0.0100  119 HIS   B C   
5768 O O   . HIS   B 119 ? 0.1773 0.1476 0.1896 -0.0299 -0.0144 0.0046  119 HIS   B O   
5769 C CB  . HIS   B 119 ? 0.1728 0.1537 0.1893 -0.0026 -0.0223 0.0059  119 HIS   B CB  
5770 C CG  . HIS   B 119 ? 0.1775 0.1731 0.2049 0.0067  -0.0453 -0.0113 119 HIS   B CG  
5771 N ND1 . HIS   B 119 ? 0.1991 0.1847 0.2411 0.0013  -0.0538 -0.0330 119 HIS   B ND1 
5772 C CD2 . HIS   B 119 ? 0.1942 0.2004 0.2108 0.0362  -0.0608 -0.0191 119 HIS   B CD2 
5773 C CE1 . HIS   B 119 ? 0.2202 0.2031 0.2476 0.0170  -0.0616 -0.0406 119 HIS   B CE1 
5774 N NE2 . HIS   B 119 ? 0.2194 0.2240 0.2274 0.0306  -0.0565 -0.0303 119 HIS   B NE2 
5782 N N   . GLU   B 120 ? 0.1849 0.1488 0.1744 -0.0144 -0.0318 0.0136  120 GLU   B N   
5783 C CA  . GLU   B 120 ? 0.2158 0.1677 0.1770 -0.0021 -0.0447 0.0202  120 GLU   B CA  
5784 C C   . GLU   B 120 ? 0.1927 0.1546 0.1773 -0.0068 -0.0385 0.0223  120 GLU   B C   
5785 O O   . GLU   B 120 ? 0.1799 0.1708 0.1752 -0.0145 -0.0316 0.0060  120 GLU   B O   
5786 C CB  . GLU   B 120 ? 0.2841 0.2087 0.2379 0.0279  -0.0759 0.0362  120 GLU   B CB  
5787 C CG  . GLU   B 120 ? 0.3515 0.2912 0.3442 0.0384  -0.0944 0.0625  120 GLU   B CG  
5788 C CD  . GLU   B 120 ? 0.4053 0.3661 0.4565 0.0412  -0.0949 0.0798  120 GLU   B CD  
5789 O OE1 . GLU   B 120 ? 0.4307 0.3899 0.4928 0.0325  -0.0910 0.0953  120 GLU   B OE1 
5790 O OE2 . GLU   B 120 ? 0.4283 0.3977 0.5112 0.0431  -0.0906 0.0734  120 GLU   B OE2 
5797 N N   . VAL   B 121 ? 0.1782 0.1532 0.1752 -0.0183 -0.0218 0.0152  121 VAL   B N   
5798 C CA  . VAL   B 121 ? 0.1730 0.1686 0.1610 -0.0125 -0.0160 0.0161  121 VAL   B CA  
5799 C C   . VAL   B 121 ? 0.1674 0.1611 0.1586 -0.0212 -0.0178 0.0221  121 VAL   B C   
5800 O O   . VAL   B 121 ? 0.1779 0.1598 0.1796 -0.0369 -0.0214 0.0031  121 VAL   B O   
5801 C CB  . VAL   B 121 ? 0.1968 0.2048 0.1743 0.0037  -0.0253 0.0186  121 VAL   B CB  
5802 C CG1 . VAL   B 121 ? 0.2005 0.2141 0.2169 -0.0087 -0.0096 0.0170  121 VAL   B CG1 
5803 C CG2 . VAL   B 121 ? 0.2247 0.2324 0.1798 0.0118  -0.0223 0.0026  121 VAL   B CG2 
5813 N N   . LEU   B 122 ? 0.1604 0.1544 0.1561 -0.0105 -0.0200 0.0128  122 LEU   B N   
5814 C CA  . LEU   B 122 ? 0.1459 0.1586 0.1357 -0.0123 -0.0169 0.0164  122 LEU   B CA  
5815 C C   . LEU   B 122 ? 0.1473 0.1446 0.1472 -0.0244 -0.0193 0.0141  122 LEU   B C   
5816 O O   . LEU   B 122 ? 0.1593 0.1496 0.1822 -0.0326 -0.0180 -0.0026 122 LEU   B O   
5817 C CB  . LEU   B 122 ? 0.1743 0.1755 0.1717 0.0020  -0.0268 0.0056  122 LEU   B CB  
5818 C CG  . LEU   B 122 ? 0.1650 0.1827 0.1907 -0.0139 -0.0116 -0.0012 122 LEU   B CG  
5819 C CD1 . LEU   B 122 ? 0.1737 0.2032 0.1994 -0.0184 -0.0185 0.0141  122 LEU   B CD1 
5820 C CD2 . LEU   B 122 ? 0.1757 0.1799 0.1600 -0.0094 0.0009  -0.0084 122 LEU   B CD2 
5832 N N   . LEU   B 123 ? 0.1518 0.1321 0.1504 -0.0212 -0.0091 0.0146  123 LEU   B N   
5833 C CA  . LEU   B 123 ? 0.1613 0.1426 0.1535 -0.0245 -0.0223 -0.0005 123 LEU   B CA  
5834 C C   . LEU   B 123 ? 0.1517 0.1330 0.1479 -0.0287 -0.0229 0.0012  123 LEU   B C   
5835 O O   . LEU   B 123 ? 0.1641 0.1381 0.1493 -0.0317 -0.0143 0.0005  123 LEU   B O   
5836 C CB  . LEU   B 123 ? 0.1635 0.1504 0.1576 -0.0266 -0.0080 -0.0045 123 LEU   B CB  
5837 C CG  . LEU   B 123 ? 0.1639 0.1522 0.1745 -0.0207 -0.0065 0.0037  123 LEU   B CG  
5838 C CD1 . LEU   B 123 ? 0.1691 0.1626 0.1773 -0.0203 -0.0030 -0.0103 123 LEU   B CD1 
5839 C CD2 . LEU   B 123 ? 0.1730 0.1505 0.1958 -0.0179 0.0042  0.0073  123 LEU   B CD2 
5851 N N   . ALA   B 124 ? 0.1524 0.1378 0.1505 -0.0238 -0.0081 -0.0028 124 ALA   B N   
5852 C CA  . ALA   B 124 ? 0.1460 0.1396 0.1632 -0.0127 -0.0027 -0.0092 124 ALA   B CA  
5853 C C   . ALA   B 124 ? 0.1478 0.1268 0.1547 -0.0144 -0.0111 -0.0026 124 ALA   B C   
5854 O O   . ALA   B 124 ? 0.1578 0.1371 0.1683 -0.0156 -0.0103 -0.0010 124 ALA   B O   
5855 C CB  . ALA   B 124 ? 0.1465 0.1463 0.1771 -0.0019 0.0035  -0.0098 124 ALA   B CB  
5861 N N   . PRO   B 125 ? 0.1553 0.1398 0.1456 -0.0225 -0.0135 0.0088  125 PRO   B N   
5862 C CA  . PRO   B 125 ? 0.1698 0.1425 0.1673 -0.0203 -0.0080 0.0202  125 PRO   B CA  
5863 C C   . PRO   B 125 ? 0.1550 0.1352 0.1889 -0.0207 -0.0059 0.0148  125 PRO   B C   
5864 O O   . PRO   B 125 ? 0.1533 0.1410 0.2088 -0.0111 0.0004  0.0141  125 PRO   B O   
5865 C CB  . PRO   B 125 ? 0.1720 0.1702 0.1766 -0.0269 -0.0211 0.0243  125 PRO   B CB  
5866 C CG  . PRO   B 125 ? 0.1748 0.1748 0.1731 -0.0304 -0.0225 0.0180  125 PRO   B CG  
5867 C CD  . PRO   B 125 ? 0.1674 0.1571 0.1466 -0.0369 -0.0124 0.0036  125 PRO   B CD  
5875 N N   . LEU   B 126 ? 0.1643 0.1391 0.2018 -0.0250 0.0098  0.0123  126 LEU   B N   
5876 C CA  . LEU   B 126 ? 0.1801 0.1377 0.2026 -0.0198 0.0192  0.0173  126 LEU   B CA  
5877 C C   . LEU   B 126 ? 0.1689 0.1457 0.2057 0.0021  0.0227  0.0229  126 LEU   B C   
5878 O O   . LEU   B 126 ? 0.1782 0.1735 0.2409 0.0241  -0.0041 -0.0068 126 LEU   B O   
5879 C CB  . LEU   B 126 ? 0.1926 0.1415 0.2437 -0.0188 0.0259  0.0102  126 LEU   B CB  
5880 C CG  . LEU   B 126 ? 0.2120 0.1479 0.2524 -0.0230 0.0220  -0.0069 126 LEU   B CG  
5881 C CD1 . LEU   B 126 ? 0.2231 0.1578 0.3034 -0.0257 0.0181  -0.0211 126 LEU   B CD1 
5882 C CD2 . LEU   B 126 ? 0.2126 0.1644 0.2545 -0.0301 0.0142  -0.0094 126 LEU   B CD2 
5894 N N   . LEU   B 127 ? 0.1671 0.1361 0.2044 0.0017  0.0258  0.0139  127 LEU   B N   
5895 C CA  . LEU   B 127 ? 0.1613 0.1514 0.2017 -0.0040 0.0261  0.0255  127 LEU   B CA  
5896 C C   . LEU   B 127 ? 0.1490 0.1489 0.2094 0.0035  0.0182  0.0196  127 LEU   B C   
5897 O O   . LEU   B 127 ? 0.1556 0.1441 0.2223 -0.0162 0.0128  0.0154  127 LEU   B O   
5898 C CB  . LEU   B 127 ? 0.1719 0.1548 0.2068 -0.0086 0.0227  0.0225  127 LEU   B CB  
5899 C CG  . LEU   B 127 ? 0.1877 0.1499 0.2221 -0.0045 0.0203  0.0180  127 LEU   B CG  
5900 C CD1 . LEU   B 127 ? 0.1960 0.1502 0.2311 -0.0006 0.0091  0.0058  127 LEU   B CD1 
5901 C CD2 . LEU   B 127 ? 0.1917 0.1604 0.2292 -0.0130 0.0213  0.0302  127 LEU   B CD2 
5913 N N   . SER   B 128 ? 0.1582 0.1580 0.2037 0.0093  0.0028  0.0139  128 SER   B N   
5914 C CA  . SER   B 128 ? 0.1688 0.1636 0.1974 0.0170  -0.0002 0.0147  128 SER   B CA  
5915 C C   . SER   B 128 ? 0.1837 0.1635 0.2231 0.0131  -0.0198 0.0184  128 SER   B C   
5916 O O   . SER   B 128 ? 0.2006 0.1625 0.2613 0.0081  -0.0163 0.0318  128 SER   B O   
5917 C CB  . SER   B 128 ? 0.1719 0.1690 0.2094 0.0123  0.0045  0.0235  128 SER   B CB  
5918 O OG  . SER   B 128 ? 0.1760 0.1781 0.2177 0.0139  0.0180  0.0346  128 SER   B OG  
5924 N N   . ALA   B 129 ? 0.1911 0.1673 0.2529 0.0357  -0.0142 0.0008  129 ALA   B N   
5925 C CA  . ALA   B 129 ? 0.2138 0.1794 0.2761 0.0400  -0.0168 -0.0157 129 ALA   B CA  
5926 C C   . ALA   B 129 ? 0.1961 0.1717 0.2571 0.0299  -0.0041 -0.0082 129 ALA   B C   
5927 O O   . ALA   B 129 ? 0.1887 0.1729 0.2514 0.0235  -0.0082 0.0065  129 ALA   B O   
5928 C CB  . ALA   B 129 ? 0.2431 0.2043 0.3088 0.0368  -0.0082 -0.0264 129 ALA   B CB  
5934 N N   . GLY   B 130 ? 0.1979 0.1691 0.2550 0.0358  0.0041  -0.0130 130 GLY   B N   
5935 C CA  . GLY   B 130 ? 0.2004 0.1799 0.2657 0.0289  0.0250  -0.0065 130 GLY   B CA  
5936 C C   . GLY   B 130 ? 0.2005 0.1765 0.2598 0.0169  0.0180  0.0045  130 GLY   B C   
5937 O O   . GLY   B 130 ? 0.2112 0.1837 0.2643 0.0143  0.0058  0.0117  130 GLY   B O   
5941 N N   . ILE   B 131 ? 0.1922 0.1866 0.2708 0.0361  0.0224  -0.0010 131 ILE   B N   
5942 C CA  . ILE   B 131 ? 0.2237 0.1953 0.2657 0.0346  0.0047  0.0071  131 ILE   B CA  
5943 C C   . ILE   B 131 ? 0.2373 0.1802 0.2374 0.0220  -0.0015 0.0111  131 ILE   B C   
5944 O O   . ILE   B 131 ? 0.2680 0.1968 0.2498 0.0254  -0.0173 0.0223  131 ILE   B O   
5945 C CB  . ILE   B 131 ? 0.2287 0.2268 0.3065 0.0337  -0.0025 0.0152  131 ILE   B CB  
5946 C CG1 . ILE   B 131 ? 0.2316 0.2433 0.3149 0.0068  0.0074  0.0216  131 ILE   B CG1 
5947 C CG2 . ILE   B 131 ? 0.2312 0.2465 0.3316 0.0401  -0.0047 0.0115  131 ILE   B CG2 
5948 C CD1 . ILE   B 131 ? 0.2413 0.2599 0.3223 -0.0138 -0.0002 0.0338  131 ILE   B CD1 
5960 N N   . PHE   B 132 ? 0.2133 0.1681 0.2279 0.0197  0.0169  0.0149  132 PHE   B N   
5961 C CA  . PHE   B 132 ? 0.2206 0.1803 0.2266 0.0084  0.0278  0.0077  132 PHE   B CA  
5962 C C   . PHE   B 132 ? 0.2417 0.1931 0.2486 0.0054  0.0382  0.0054  132 PHE   B C   
5963 O O   . PHE   B 132 ? 0.2605 0.2151 0.2776 0.0005  0.0514  0.0156  132 PHE   B O   
5964 C CB  . PHE   B 132 ? 0.1984 0.1830 0.2111 0.0109  0.0335  0.0178  132 PHE   B CB  
5965 C CG  . PHE   B 132 ? 0.2010 0.1923 0.2115 0.0136  0.0289  0.0144  132 PHE   B CG  
5966 C CD1 . PHE   B 132 ? 0.2127 0.1953 0.2531 0.0022  0.0282  0.0248  132 PHE   B CD1 
5967 C CD2 . PHE   B 132 ? 0.2006 0.1877 0.1841 0.0201  0.0294  0.0217  132 PHE   B CD2 
5968 C CE1 . PHE   B 132 ? 0.2183 0.1993 0.2559 0.0014  0.0290  0.0284  132 PHE   B CE1 
5969 C CE2 . PHE   B 132 ? 0.2103 0.1951 0.1991 0.0165  0.0220  0.0154  132 PHE   B CE2 
5970 C CZ  . PHE   B 132 ? 0.2189 0.1972 0.2298 0.0098  0.0067  0.0340  132 PHE   B CZ  
5980 N N   . GLY   B 133 ? 0.2336 0.1849 0.2459 0.0042  0.0183  0.0269  133 GLY   B N   
5981 C CA  . GLY   B 133 ? 0.2443 0.1968 0.2504 -0.0238 0.0174  0.0431  133 GLY   B CA  
5982 C C   . GLY   B 133 ? 0.2499 0.2076 0.2435 -0.0359 0.0286  0.0513  133 GLY   B C   
5983 O O   . GLY   B 133 ? 0.2696 0.2233 0.2962 -0.0461 0.0297  0.0553  133 GLY   B O   
5987 N N   . ALA   B 134 ? 0.2338 0.2090 0.2314 -0.0350 0.0306  0.0281  134 ALA   B N   
5988 C CA  . ALA   B 134 ? 0.2313 0.2037 0.2516 -0.0260 0.0450  0.0130  134 ALA   B CA  
5989 C C   . ALA   B 134 ? 0.2399 0.1919 0.2450 -0.0212 0.0458  0.0313  134 ALA   B C   
5990 O O   . ALA   B 134 ? 0.2448 0.2144 0.2650 -0.0027 0.0335  0.0211  134 ALA   B O   
5991 C CB  . ALA   B 134 ? 0.2212 0.1998 0.2827 -0.0129 0.0339  0.0003  134 ALA   B CB  
5997 N N   . ASP   B 135 ? 0.2584 0.1828 0.2449 -0.0209 0.0275  0.0271  135 ASP   B N   
5998 C CA  . ASP   B 135 ? 0.2731 0.1724 0.2652 -0.0164 0.0048  0.0299  135 ASP   B CA  
5999 C C   . ASP   B 135 ? 0.2516 0.1730 0.2499 -0.0010 0.0057  0.0200  135 ASP   B C   
6000 O O   . ASP   B 135 ? 0.2354 0.1678 0.2719 -0.0117 0.0062  0.0230  135 ASP   B O   
6001 C CB  . ASP   B 135 ? 0.3055 0.1852 0.2900 -0.0408 0.0076  0.0331  135 ASP   B CB  
6002 C CG  . ASP   B 135 ? 0.3357 0.1928 0.3367 -0.0637 0.0064  0.0255  135 ASP   B CG  
6003 O OD1 . ASP   B 135 ? 0.3484 0.1809 0.3319 -0.0403 0.0022  0.0253  135 ASP   B OD1 
6004 O OD2 . ASP   B 135 ? 0.3625 0.2336 0.3986 -0.0791 -0.0003 0.0076  135 ASP   B OD2 
6009 N N   . PRO   B 136 ? 0.2433 0.1786 0.2607 0.0231  -0.0138 0.0169  136 PRO   B N   
6010 C CA  . PRO   B 136 ? 0.2258 0.1653 0.2598 0.0205  -0.0131 0.0077  136 PRO   B CA  
6011 C C   . PRO   B 136 ? 0.2016 0.1546 0.2642 0.0139  -0.0081 -0.0003 136 PRO   B C   
6012 O O   . PRO   B 136 ? 0.1800 0.1520 0.2541 0.0166  -0.0044 0.0058  136 PRO   B O   
6013 C CB  . PRO   B 136 ? 0.2253 0.1857 0.2761 0.0326  -0.0153 -0.0075 136 PRO   B CB  
6014 C CG  . PRO   B 136 ? 0.2458 0.1926 0.3002 0.0305  -0.0085 -0.0119 136 PRO   B CG  
6015 C CD  . PRO   B 136 ? 0.2449 0.1861 0.2784 0.0457  -0.0061 0.0042  136 PRO   B CD  
6023 N N   . ILE   B 137 ? 0.2069 0.1517 0.2717 0.0090  -0.0100 -0.0032 137 ILE   B N   
6024 C CA  . ILE   B 137 ? 0.2159 0.1527 0.2779 -0.0094 -0.0036 0.0017  137 ILE   B CA  
6025 C C   . ILE   B 137 ? 0.2008 0.1489 0.2748 -0.0139 0.0025  0.0084  137 ILE   B C   
6026 O O   . ILE   B 137 ? 0.1896 0.1583 0.2703 -0.0154 -0.0032 0.0101  137 ILE   B O   
6027 C CB  . ILE   B 137 ? 0.2450 0.1557 0.3227 -0.0105 -0.0059 -0.0074 137 ILE   B CB  
6028 C CG1 . ILE   B 137 ? 0.2689 0.1866 0.3692 -0.0003 0.0012  -0.0224 137 ILE   B CG1 
6029 C CG2 . ILE   B 137 ? 0.2515 0.1616 0.3398 -0.0333 -0.0068 0.0018  137 ILE   B CG2 
6030 C CD1 . ILE   B 137 ? 0.2942 0.2076 0.4128 0.0102  -0.0072 -0.0166 137 ILE   B CD1 
6042 N N   . HIS   B 138 ? 0.2086 0.1524 0.2770 -0.0085 0.0191  0.0151  138 HIS   B N   
6043 C CA  . HIS   B 138 ? 0.2147 0.1640 0.2756 -0.0080 0.0330  0.0148  138 HIS   B CA  
6044 C C   . HIS   B 138 ? 0.1946 0.1516 0.2723 -0.0155 0.0281  0.0210  138 HIS   B C   
6045 O O   . HIS   B 138 ? 0.1900 0.1648 0.2916 -0.0010 0.0320  0.0356  138 HIS   B O   
6046 C CB  . HIS   B 138 ? 0.2400 0.1745 0.2943 -0.0102 0.0538  0.0114  138 HIS   B CB  
6047 C CG  . HIS   B 138 ? 0.2596 0.1839 0.2954 -0.0132 0.0698  0.0311  138 HIS   B CG  
6048 N ND1 . HIS   B 138 ? 0.2719 0.2066 0.3296 -0.0068 0.0801  0.0244  138 HIS   B ND1 
6049 C CD2 . HIS   B 138 ? 0.2760 0.1937 0.2918 -0.0153 0.0779  0.0211  138 HIS   B CD2 
6050 C CE1 . HIS   B 138 ? 0.2747 0.2015 0.3213 -0.0065 0.0877  0.0300  138 HIS   B CE1 
6051 N NE2 . HIS   B 138 ? 0.2860 0.1937 0.3019 -0.0017 0.0871  0.0210  138 HIS   B NE2 
6059 N N   . SER   B 139 ? 0.1916 0.1371 0.2595 -0.0066 0.0234  0.0056  139 SER   B N   
6060 C CA  . SER   B 139 ? 0.1858 0.1366 0.2460 -0.0055 0.0231  0.0021  139 SER   B CA  
6061 C C   . SER   B 139 ? 0.1610 0.1403 0.2392 0.0065  0.0191  0.0018  139 SER   B C   
6062 O O   . SER   B 139 ? 0.1712 0.1357 0.2446 0.0029  0.0044  0.0067  139 SER   B O   
6063 C CB  . SER   B 139 ? 0.1901 0.1409 0.2635 0.0008  0.0088  0.0074  139 SER   B CB  
6064 O OG  . SER   B 139 ? 0.1915 0.1434 0.2599 -0.0038 -0.0080 0.0155  139 SER   B OG  
6070 N N   . LEU   B 140 ? 0.1655 0.1302 0.2409 0.0016  0.0188  -0.0068 140 LEU   B N   
6071 C CA  . LEU   B 140 ? 0.1602 0.1307 0.2548 -0.0002 0.0112  -0.0021 140 LEU   B CA  
6072 C C   . LEU   B 140 ? 0.1514 0.1317 0.2621 -0.0016 0.0013  -0.0039 140 LEU   B C   
6073 O O   . LEU   B 140 ? 0.1539 0.1409 0.2580 -0.0001 0.0013  -0.0043 140 LEU   B O   
6074 C CB  . LEU   B 140 ? 0.1612 0.1377 0.2566 -0.0108 0.0178  -0.0060 140 LEU   B CB  
6075 C CG  . LEU   B 140 ? 0.1662 0.1482 0.2484 -0.0109 0.0114  0.0043  140 LEU   B CG  
6076 C CD1 . LEU   B 140 ? 0.1799 0.1560 0.2697 -0.0206 0.0216  0.0106  140 LEU   B CD1 
6077 C CD2 . LEU   B 140 ? 0.1891 0.1610 0.2454 -0.0052 0.0134  -0.0081 140 LEU   B CD2 
6089 N N   . ARG   B 141 ? 0.1488 0.1301 0.2731 -0.0097 0.0081  -0.0069 141 ARG   B N   
6090 C CA  . ARG   B 141 ? 0.1573 0.1309 0.3027 -0.0188 0.0263  -0.0032 141 ARG   B CA  
6091 C C   . ARG   B 141 ? 0.1500 0.1268 0.2832 -0.0108 0.0122  -0.0058 141 ARG   B C   
6092 O O   . ARG   B 141 ? 0.1601 0.1432 0.2737 -0.0136 0.0015  -0.0162 141 ARG   B O   
6093 C CB  . ARG   B 141 ? 0.1769 0.1501 0.3390 -0.0231 0.0292  -0.0048 141 ARG   B CB  
6094 C CG  . ARG   B 141 ? 0.2156 0.1757 0.3654 -0.0258 0.0327  0.0048  141 ARG   B CG  
6095 C CD  . ARG   B 141 ? 0.2554 0.1971 0.3658 -0.0159 0.0197  -0.0001 141 ARG   B CD  
6096 N NE  . ARG   B 141 ? 0.2783 0.2065 0.3619 -0.0357 0.0299  -0.0017 141 ARG   B NE  
6097 C CZ  . ARG   B 141 ? 0.2912 0.1858 0.3406 -0.0291 0.0330  -0.0226 141 ARG   B CZ  
6098 N NH1 . ARG   B 141 ? 0.3035 0.1734 0.3286 -0.0267 0.0259  -0.0247 141 ARG   B NH1 
6099 N NH2 . ARG   B 141 ? 0.2988 0.1929 0.3493 -0.0208 0.0193  -0.0119 141 ARG   B NH2 
6113 N N   . VAL   B 142 ? 0.1565 0.1335 0.2715 -0.0099 0.0192  -0.0139 142 VAL   B N   
6114 C CA  . VAL   B 142 ? 0.1542 0.1397 0.2586 -0.0047 0.0268  -0.0074 142 VAL   B CA  
6115 C C   . VAL   B 142 ? 0.1505 0.1435 0.2564 -0.0006 0.0130  -0.0120 142 VAL   B C   
6116 O O   . VAL   B 142 ? 0.1584 0.1305 0.2738 0.0025  0.0169  -0.0046 142 VAL   B O   
6117 C CB  . VAL   B 142 ? 0.1599 0.1526 0.2689 0.0003  0.0303  0.0057  142 VAL   B CB  
6118 C CG1 . VAL   B 142 ? 0.1589 0.1503 0.2724 0.0115  0.0280  0.0029  142 VAL   B CG1 
6119 C CG2 . VAL   B 142 ? 0.1872 0.1523 0.2675 -0.0012 0.0195  0.0100  142 VAL   B CG2 
6129 N N   . CYS   B 143 ? 0.1490 0.1384 0.2415 -0.0040 0.0098  0.0036  143 CYS   B N   
6130 C CA  . CYS   B 143 ? 0.1472 0.1438 0.2313 -0.0062 0.0026  0.0001  143 CYS   B CA  
6131 C C   . CYS   B 143 ? 0.1370 0.1529 0.2371 -0.0042 0.0003  -0.0021 143 CYS   B C   
6132 O O   . CYS   B 143 ? 0.1452 0.1541 0.2429 -0.0043 -0.0040 0.0012  143 CYS   B O   
6133 C CB  . CYS   B 143 ? 0.1555 0.1523 0.2394 -0.0041 -0.0056 -0.0073 143 CYS   B CB  
6134 S SG  . CYS   B 143 ? 0.1581 0.1614 0.2301 -0.0040 0.0075  0.0019  143 CYS   B SG  
6140 N N   . VAL   B 144 ? 0.1466 0.1502 0.2488 -0.0107 -0.0002 -0.0176 144 VAL   B N   
6141 C CA  . VAL   B 144 ? 0.1544 0.1505 0.2724 -0.0171 -0.0140 -0.0199 144 VAL   B CA  
6142 C C   . VAL   B 144 ? 0.1530 0.1535 0.2792 -0.0071 -0.0138 -0.0046 144 VAL   B C   
6143 O O   . VAL   B 144 ? 0.1585 0.1703 0.2948 0.0005  -0.0113 0.0146  144 VAL   B O   
6144 C CB  . VAL   B 144 ? 0.1795 0.1692 0.3395 -0.0092 -0.0301 -0.0300 144 VAL   B CB  
6145 C CG1 . VAL   B 144 ? 0.2117 0.2156 0.3839 -0.0063 -0.0343 -0.0240 144 VAL   B CG1 
6146 C CG2 . VAL   B 144 ? 0.1937 0.1608 0.3376 0.0050  -0.0358 -0.0430 144 VAL   B CG2 
6156 N N   . ASP   B 145 ? 0.1570 0.1436 0.2901 -0.0036 -0.0027 -0.0258 145 ASP   B N   
6157 C CA  . ASP   B 145 ? 0.1657 0.1470 0.3064 -0.0080 0.0069  -0.0125 145 ASP   B CA  
6158 C C   . ASP   B 145 ? 0.1657 0.1398 0.2895 -0.0064 0.0137  -0.0137 145 ASP   B C   
6159 O O   . ASP   B 145 ? 0.1669 0.1568 0.3427 -0.0055 0.0078  -0.0217 145 ASP   B O   
6160 C CB  . ASP   B 145 ? 0.1750 0.1623 0.3422 -0.0165 0.0170  -0.0059 145 ASP   B CB  
6161 C CG  . ASP   B 145 ? 0.1908 0.1689 0.3835 -0.0246 0.0340  -0.0046 145 ASP   B CG  
6162 O OD1 . ASP   B 145 ? 0.1919 0.1653 0.3939 -0.0264 -0.0059 -0.0196 145 ASP   B OD1 
6163 O OD2 . ASP   B 145 ? 0.2232 0.1786 0.4323 -0.0345 0.0523  0.0048  145 ASP   B OD2 
6168 N N   . THR   B 146 ? 0.1512 0.1408 0.2451 -0.0160 0.0013  -0.0033 146 THR   B N   
6169 C CA  . THR   B 146 ? 0.1511 0.1481 0.2391 -0.0144 0.0042  -0.0081 146 THR   B CA  
6170 C C   . THR   B 146 ? 0.1516 0.1403 0.2363 0.0045  -0.0016 -0.0084 146 THR   B C   
6171 O O   . THR   B 146 ? 0.1553 0.1477 0.2395 0.0049  -0.0012 -0.0060 146 THR   B O   
6172 C CB  . THR   B 146 ? 0.1505 0.1493 0.2537 -0.0067 0.0165  -0.0019 146 THR   B CB  
6173 O OG1 . THR   B 146 ? 0.1499 0.1495 0.2543 -0.0061 0.0184  0.0026  146 THR   B OG1 
6174 C CG2 . THR   B 146 ? 0.1660 0.1483 0.2432 -0.0069 0.0137  -0.0130 146 THR   B CG2 
6182 N N   . VAL   B 147 ? 0.1548 0.1395 0.2198 0.0073  0.0101  -0.0019 147 VAL   B N   
6183 C CA  . VAL   B 147 ? 0.1552 0.1389 0.2048 -0.0091 0.0001  0.0008  147 VAL   B CA  
6184 C C   . VAL   B 147 ? 0.1448 0.1478 0.2224 -0.0219 -0.0086 -0.0066 147 VAL   B C   
6185 O O   . VAL   B 147 ? 0.1586 0.1631 0.2223 -0.0244 -0.0258 -0.0096 147 VAL   B O   
6186 C CB  . VAL   B 147 ? 0.1562 0.1495 0.1991 -0.0015 -0.0102 0.0025  147 VAL   B CB  
6187 C CG1 . VAL   B 147 ? 0.1565 0.1605 0.1914 -0.0132 -0.0120 0.0060  147 VAL   B CG1 
6188 C CG2 . VAL   B 147 ? 0.1640 0.1480 0.2044 -0.0041 0.0006  0.0045  147 VAL   B CG2 
6198 N N   . ARG   B 148 ? 0.1445 0.1477 0.2200 -0.0083 -0.0201 -0.0044 148 ARG   B N   
6199 C CA  . ARG   B 148 ? 0.1597 0.1432 0.2225 -0.0069 -0.0274 -0.0092 148 ARG   B CA  
6200 C C   . ARG   B 148 ? 0.1664 0.1567 0.1980 -0.0096 -0.0303 -0.0010 148 ARG   B C   
6201 O O   . ARG   B 148 ? 0.1778 0.1914 0.2005 -0.0271 -0.0347 0.0013  148 ARG   B O   
6202 C CB  . ARG   B 148 ? 0.1630 0.1560 0.2274 -0.0028 -0.0351 -0.0159 148 ARG   B CB  
6203 C CG  . ARG   B 148 ? 0.1642 0.1753 0.2313 -0.0131 -0.0277 -0.0346 148 ARG   B CG  
6204 C CD  . ARG   B 148 ? 0.1696 0.1957 0.2298 0.0080  -0.0226 -0.0425 148 ARG   B CD  
6205 N NE  . ARG   B 148 ? 0.1704 0.1904 0.2186 0.0189  -0.0299 -0.0350 148 ARG   B NE  
6206 C CZ  . ARG   B 148 ? 0.1671 0.1866 0.2038 0.0068  -0.0192 -0.0175 148 ARG   B CZ  
6207 N NH1 . ARG   B 148 ? 0.1632 0.1903 0.2179 -0.0054 0.0028  -0.0159 148 ARG   B NH1 
6208 N NH2 . ARG   B 148 ? 0.1830 0.1661 0.2186 0.0121  -0.0140 -0.0104 148 ARG   B NH2 
6222 N N   . THR   B 149 ? 0.1654 0.1484 0.2083 -0.0147 -0.0277 -0.0017 149 THR   B N   
6223 C CA  . THR   B 149 ? 0.1682 0.1583 0.1976 -0.0185 -0.0249 0.0063  149 THR   B CA  
6224 C C   . THR   B 149 ? 0.1661 0.1572 0.1893 -0.0221 -0.0242 0.0037  149 THR   B C   
6225 O O   . THR   B 149 ? 0.1711 0.1595 0.2091 -0.0188 -0.0114 0.0024  149 THR   B O   
6226 C CB  . THR   B 149 ? 0.1679 0.1553 0.2001 -0.0162 -0.0302 0.0002  149 THR   B CB  
6227 O OG1 . THR   B 149 ? 0.1741 0.1580 0.1879 -0.0245 -0.0321 -0.0002 149 THR   B OG1 
6228 C CG2 . THR   B 149 ? 0.1648 0.1658 0.2039 -0.0044 -0.0188 0.0100  149 THR   B CG2 
6236 N N   . ASN   B 150 ? 0.1698 0.1508 0.1946 -0.0132 -0.0279 0.0031  150 ASN   B N   
6237 C CA  . ASN   B 150 ? 0.1776 0.1658 0.1855 -0.0209 -0.0215 -0.0034 150 ASN   B CA  
6238 C C   . ASN   B 150 ? 0.1743 0.1537 0.1889 -0.0128 -0.0229 -0.0013 150 ASN   B C   
6239 O O   . ASN   B 150 ? 0.1841 0.1523 0.2093 -0.0304 -0.0376 -0.0028 150 ASN   B O   
6240 C CB  . ASN   B 150 ? 0.2075 0.2034 0.1947 -0.0257 -0.0382 0.0159  150 ASN   B CB  
6241 C CG  . ASN   B 150 ? 0.2353 0.2432 0.2325 -0.0235 -0.0342 0.0347  150 ASN   B CG  
6242 O OD1 . ASN   B 150 ? 0.2448 0.2634 0.2456 -0.0328 -0.0468 0.0262  150 ASN   B OD1 
6243 N ND2 . ASN   B 150 ? 0.2479 0.2658 0.2704 -0.0146 -0.0415 0.0710  150 ASN   B ND2 
6250 N N   . VAL   B 151 ? 0.1665 0.1538 0.1773 -0.0187 -0.0222 -0.0023 151 VAL   B N   
6251 C CA  . VAL   B 151 ? 0.1622 0.1576 0.1810 -0.0225 -0.0229 0.0026  151 VAL   B CA  
6252 C C   . VAL   B 151 ? 0.1598 0.1581 0.1722 -0.0345 -0.0234 -0.0086 151 VAL   B C   
6253 O O   . VAL   B 151 ? 0.1715 0.1658 0.1887 -0.0243 -0.0108 -0.0104 151 VAL   B O   
6254 C CB  . VAL   B 151 ? 0.1860 0.1676 0.1936 -0.0083 -0.0239 -0.0051 151 VAL   B CB  
6255 C CG1 . VAL   B 151 ? 0.1939 0.1725 0.2267 -0.0195 -0.0110 -0.0149 151 VAL   B CG1 
6256 C CG2 . VAL   B 151 ? 0.2047 0.1892 0.1776 0.0071  -0.0154 0.0046  151 VAL   B CG2 
6266 N N   . TYR   B 152 ? 0.1563 0.1483 0.1794 -0.0247 -0.0156 -0.0055 152 TYR   B N   
6267 C CA  . TYR   B 152 ? 0.1593 0.1642 0.1618 -0.0289 -0.0139 -0.0110 152 TYR   B CA  
6268 C C   . TYR   B 152 ? 0.1587 0.1395 0.1566 -0.0269 -0.0086 -0.0162 152 TYR   B C   
6269 O O   . TYR   B 152 ? 0.1719 0.1463 0.1781 -0.0277 -0.0017 -0.0121 152 TYR   B O   
6270 C CB  . TYR   B 152 ? 0.1740 0.1747 0.1736 -0.0298 -0.0164 0.0056  152 TYR   B CB  
6271 C CG  . TYR   B 152 ? 0.1884 0.1791 0.1822 -0.0422 -0.0146 0.0067  152 TYR   B CG  
6272 C CD1 . TYR   B 152 ? 0.2006 0.1911 0.1717 -0.0305 -0.0235 0.0111  152 TYR   B CD1 
6273 C CD2 . TYR   B 152 ? 0.2093 0.1964 0.1834 -0.0372 -0.0065 -0.0014 152 TYR   B CD2 
6274 C CE1 . TYR   B 152 ? 0.2176 0.2065 0.1874 -0.0267 -0.0249 0.0243  152 TYR   B CE1 
6275 C CE2 . TYR   B 152 ? 0.2223 0.2224 0.1882 -0.0349 -0.0114 -0.0060 152 TYR   B CE2 
6276 C CZ  . TYR   B 152 ? 0.2255 0.2365 0.1720 -0.0323 -0.0398 0.0193  152 TYR   B CZ  
6277 O OH  . TYR   B 152 ? 0.2521 0.2767 0.2120 -0.0184 -0.0393 0.0196  152 TYR   B OH  
6287 N N   . LEU   B 153 ? 0.1614 0.1408 0.1725 -0.0301 -0.0133 -0.0112 153 LEU   B N   
6288 C CA  . LEU   B 153 ? 0.1697 0.1312 0.1602 -0.0216 -0.0054 -0.0130 153 LEU   B CA  
6289 C C   . LEU   B 153 ? 0.1762 0.1409 0.1622 -0.0244 -0.0089 -0.0163 153 LEU   B C   
6290 O O   . LEU   B 153 ? 0.1821 0.1625 0.1763 -0.0159 -0.0091 -0.0314 153 LEU   B O   
6291 C CB  . LEU   B 153 ? 0.1774 0.1322 0.1726 -0.0220 -0.0021 -0.0122 153 LEU   B CB  
6292 C CG  . LEU   B 153 ? 0.1697 0.1456 0.2043 -0.0276 -0.0009 -0.0045 153 LEU   B CG  
6293 C CD1 . LEU   B 153 ? 0.1803 0.1619 0.2125 -0.0315 0.0056  -0.0005 153 LEU   B CD1 
6294 C CD2 . LEU   B 153 ? 0.1650 0.1587 0.2017 -0.0329 0.0072  0.0018  153 LEU   B CD2 
6306 N N   . ALA   B 154 ? 0.1690 0.1444 0.1711 -0.0093 -0.0121 -0.0103 154 ALA   B N   
6307 C CA  . ALA   B 154 ? 0.1801 0.1505 0.1926 -0.0072 -0.0176 -0.0225 154 ALA   B CA  
6308 C C   . ALA   B 154 ? 0.1901 0.1608 0.2014 0.0026  -0.0305 -0.0331 154 ALA   B C   
6309 O O   . ALA   B 154 ? 0.2250 0.1539 0.2337 0.0083  -0.0165 -0.0178 154 ALA   B O   
6310 C CB  . ALA   B 154 ? 0.1835 0.1636 0.2167 -0.0103 -0.0129 -0.0303 154 ALA   B CB  
6316 N N   . VAL   B 155 ? 0.1601 0.1520 0.2125 -0.0053 -0.0030 -0.0165 155 VAL   B N   
6317 C CA  . VAL   B 155 ? 0.1589 0.1495 0.2156 -0.0015 -0.0136 -0.0080 155 VAL   B CA  
6318 C C   . VAL   B 155 ? 0.1622 0.1520 0.2124 0.0055  -0.0086 -0.0112 155 VAL   B C   
6319 O O   . VAL   B 155 ? 0.1749 0.1725 0.2528 0.0082  -0.0062 -0.0343 155 VAL   B O   
6320 C CB  . VAL   B 155 ? 0.1685 0.1656 0.2542 -0.0040 -0.0133 0.0086  155 VAL   B CB  
6321 C CG1 . VAL   B 155 ? 0.1681 0.1613 0.2670 -0.0133 -0.0127 0.0115  155 VAL   B CG1 
6322 C CG2 . VAL   B 155 ? 0.1645 0.1747 0.2895 -0.0038 -0.0141 0.0310  155 VAL   B CG2 
6332 N N   . PHE   B 156 ? 0.1568 0.1586 0.2341 0.0099  -0.0027 -0.0192 156 PHE   B N   
6333 C CA  . PHE   B 156 ? 0.1545 0.1642 0.2748 0.0137  -0.0017 -0.0199 156 PHE   B CA  
6334 C C   . PHE   B 156 ? 0.1434 0.1720 0.3059 0.0119  -0.0098 -0.0420 156 PHE   B C   
6335 O O   . PHE   B 156 ? 0.1786 0.1912 0.3318 0.0243  -0.0014 -0.0447 156 PHE   B O   
6336 C CB  . PHE   B 156 ? 0.1655 0.1606 0.2712 0.0077  -0.0148 -0.0156 156 PHE   B CB  
6337 C CG  . PHE   B 156 ? 0.1627 0.1722 0.2890 0.0082  -0.0180 0.0030  156 PHE   B CG  
6338 C CD1 . PHE   B 156 ? 0.1669 0.1862 0.3253 0.0074  0.0012  0.0335  156 PHE   B CD1 
6339 C CD2 . PHE   B 156 ? 0.1718 0.1820 0.2843 0.0131  -0.0344 -0.0032 156 PHE   B CD2 
6340 C CE1 . PHE   B 156 ? 0.1702 0.2087 0.3378 0.0113  -0.0031 0.0391  156 PHE   B CE1 
6341 C CE2 . PHE   B 156 ? 0.1770 0.2024 0.3096 0.0169  -0.0264 0.0070  156 PHE   B CE2 
6342 C CZ  . PHE   B 156 ? 0.1650 0.2103 0.3385 0.0181  -0.0192 0.0233  156 PHE   B CZ  
6352 N N   . ASP   B 157 ? 0.1604 0.1610 0.3303 0.0165  -0.0178 -0.0216 157 ASP   B N   
6353 C CA  . ASP   B 157 ? 0.1814 0.1648 0.3548 0.0069  -0.0155 -0.0342 157 ASP   B CA  
6354 C C   . ASP   B 157 ? 0.1689 0.1646 0.3569 0.0095  -0.0194 -0.0555 157 ASP   B C   
6355 O O   . ASP   B 157 ? 0.1585 0.1721 0.3435 0.0072  -0.0191 -0.0400 157 ASP   B O   
6356 C CB  . ASP   B 157 ? 0.2039 0.1836 0.3739 0.0030  -0.0281 -0.0228 157 ASP   B CB  
6357 C CG  . ASP   B 157 ? 0.2414 0.2077 0.4068 0.0002  -0.0130 -0.0180 157 ASP   B CG  
6358 O OD1 . ASP   B 157 ? 0.2402 0.2003 0.4268 0.0095  -0.0085 -0.0134 157 ASP   B OD1 
6359 O OD2 . ASP   B 157 ? 0.2758 0.2255 0.4388 -0.0054 0.0022  -0.0140 157 ASP   B OD2 
6364 N N   . LYS   B 158 ? 0.1653 0.1897 0.3694 0.0059  -0.0032 -0.0723 158 LYS   B N   
6365 C CA  . LYS   B 158 ? 0.1883 0.2099 0.3769 0.0082  -0.0003 -0.0863 158 LYS   B CA  
6366 C C   . LYS   B 158 ? 0.1902 0.1960 0.3842 0.0075  -0.0112 -0.0784 158 LYS   B C   
6367 O O   . LYS   B 158 ? 0.1940 0.1916 0.4058 -0.0041 -0.0043 -0.0948 158 LYS   B O   
6368 C CB  . LYS   B 158 ? 0.2157 0.2593 0.3835 0.0122  0.0082  -0.1107 158 LYS   B CB  
6369 C CG  . LYS   B 158 ? 0.2551 0.3045 0.3891 0.0206  0.0252  -0.1249 158 LYS   B CG  
6370 C CD  . LYS   B 158 ? 0.2837 0.3551 0.4110 0.0181  0.0319  -0.1211 158 LYS   B CD  
6371 C CE  . LYS   B 158 ? 0.3061 0.3925 0.4311 0.0194  0.0323  -0.1164 158 LYS   B CE  
6372 N NZ  . LYS   B 158 ? 0.3045 0.4112 0.4334 0.0170  0.0339  -0.1130 158 LYS   B NZ  
6386 N N   A ASN   B 159 ? 0.1874 0.1771 0.4053 0.0098  -0.0224 -0.0696 159 ASN   B N   
6387 N N   B ASN   B 159 ? 0.1919 0.1943 0.3617 0.0077  -0.0183 -0.0638 159 ASN   B N   
6388 C CA  A ASN   B 159 ? 0.2062 0.1754 0.4209 0.0231  -0.0350 -0.0568 159 ASN   B CA  
6389 C CA  B ASN   B 159 ? 0.1965 0.1936 0.3457 0.0102  -0.0262 -0.0502 159 ASN   B CA  
6390 C C   A ASN   B 159 ? 0.1913 0.1619 0.4080 0.0132  -0.0526 -0.0501 159 ASN   B C   
6391 C C   B ASN   B 159 ? 0.1894 0.1814 0.3574 0.0087  -0.0367 -0.0453 159 ASN   B C   
6392 O O   A ASN   B 159 ? 0.1996 0.1495 0.4299 -0.0065 -0.0572 -0.0436 159 ASN   B O   
6393 O O   B ASN   B 159 ? 0.1924 0.1802 0.3506 0.0062  -0.0370 -0.0443 159 ASN   B O   
6394 C CB  A ASN   B 159 ? 0.2330 0.1976 0.4440 0.0349  -0.0376 -0.0481 159 ASN   B CB  
6395 C CB  B ASN   B 159 ? 0.2061 0.2044 0.3272 0.0130  -0.0251 -0.0421 159 ASN   B CB  
6396 C CG  A ASN   B 159 ? 0.2629 0.2281 0.4690 0.0391  -0.0533 -0.0564 159 ASN   B CG  
6397 C CG  B ASN   B 159 ? 0.2160 0.2165 0.3201 0.0154  -0.0266 -0.0394 159 ASN   B CG  
6398 O OD1 A ASN   B 159 ? 0.2771 0.2340 0.4730 0.0486  -0.0530 -0.0693 159 ASN   B OD1 
6399 O OD1 B ASN   B 159 ? 0.2199 0.2202 0.3166 0.0173  -0.0256 -0.0404 159 ASN   B OD1 
6400 N ND2 A ASN   B 159 ? 0.2685 0.2440 0.4829 0.0357  -0.0654 -0.0532 159 ASN   B ND2 
6401 N ND2 B ASN   B 159 ? 0.2194 0.2224 0.3197 0.0160  -0.0283 -0.0376 159 ASN   B ND2 
6414 N N   . LEU   B 160 ? 0.1801 0.1710 0.3863 0.0069  -0.0414 -0.0407 160 LEU   B N   
6415 C CA  . LEU   B 160 ? 0.1751 0.1641 0.3562 0.0096  -0.0347 -0.0243 160 LEU   B CA  
6416 C C   . LEU   B 160 ? 0.1716 0.1501 0.3477 -0.0020 -0.0262 -0.0269 160 LEU   B C   
6417 O O   . LEU   B 160 ? 0.1605 0.1555 0.3384 -0.0016 -0.0244 -0.0198 160 LEU   B O   
6418 C CB  . LEU   B 160 ? 0.1736 0.1709 0.3297 0.0059  -0.0358 -0.0151 160 LEU   B CB  
6419 C CG  . LEU   B 160 ? 0.1735 0.1827 0.3028 0.0067  -0.0275 -0.0039 160 LEU   B CG  
6420 C CD1 . LEU   B 160 ? 0.1946 0.2015 0.3068 -0.0005 -0.0144 -0.0108 160 LEU   B CD1 
6421 C CD2 . LEU   B 160 ? 0.1747 0.1889 0.3031 0.0216  -0.0267 -0.0074 160 LEU   B CD2 
6434 N N   . TYR   B 161 ? 0.1669 0.1602 0.3427 -0.0060 -0.0075 -0.0403 161 TYR   B N   
6435 C CA  . TYR   B 161 ? 0.1688 0.1622 0.3204 -0.0192 0.0148  -0.0479 161 TYR   B CA  
6436 C C   . TYR   B 161 ? 0.1790 0.1627 0.3091 -0.0028 0.0164  -0.0407 161 TYR   B C   
6437 O O   . TYR   B 161 ? 0.1851 0.1596 0.3038 -0.0089 0.0051  -0.0360 161 TYR   B O   
6438 C CB  . TYR   B 161 ? 0.1869 0.1786 0.3224 -0.0282 0.0366  -0.0541 161 TYR   B CB  
6439 C CG  . TYR   B 161 ? 0.2126 0.1919 0.3176 -0.0330 0.0465  -0.0577 161 TYR   B CG  
6440 C CD1 . TYR   B 161 ? 0.2152 0.1874 0.3141 -0.0442 0.0433  -0.0582 161 TYR   B CD1 
6441 C CD2 . TYR   B 161 ? 0.2395 0.2037 0.2999 -0.0282 0.0365  -0.0592 161 TYR   B CD2 
6442 C CE1 . TYR   B 161 ? 0.2374 0.2039 0.3214 -0.0449 0.0423  -0.0541 161 TYR   B CE1 
6443 C CE2 . TYR   B 161 ? 0.2567 0.2150 0.3108 -0.0375 0.0396  -0.0506 161 TYR   B CE2 
6444 C CZ  . TYR   B 161 ? 0.2555 0.2138 0.3127 -0.0509 0.0303  -0.0437 161 TYR   B CZ  
6445 O OH  . TYR   B 161 ? 0.2893 0.2379 0.3278 -0.0572 0.0279  -0.0420 161 TYR   B OH  
6455 N N   . ASP   B 162 ? 0.1752 0.1679 0.3219 -0.0024 -0.0006 -0.0524 162 ASP   B N   
6456 C CA  . ASP   B 162 ? 0.1882 0.1845 0.3156 -0.0096 -0.0033 -0.0580 162 ASP   B CA  
6457 C C   . ASP   B 162 ? 0.1889 0.1652 0.3086 -0.0172 -0.0095 -0.0458 162 ASP   B C   
6458 O O   . ASP   B 162 ? 0.1984 0.1598 0.3230 -0.0214 -0.0273 -0.0352 162 ASP   B O   
6459 C CB  . ASP   B 162 ? 0.2102 0.2016 0.3400 0.0062  0.0008  -0.0757 162 ASP   B CB  
6460 C CG  . ASP   B 162 ? 0.2209 0.2245 0.3731 0.0097  0.0025  -0.0870 162 ASP   B CG  
6461 O OD1 . ASP   B 162 ? 0.2166 0.2460 0.3647 0.0033  0.0099  -0.0827 162 ASP   B OD1 
6462 O OD2 . ASP   B 162 ? 0.2433 0.2350 0.4042 0.0228  0.0105  -0.0835 162 ASP   B OD2 
6467 N N   A LYS   B 163 ? 0.1806 0.1518 0.3118 -0.0095 -0.0340 -0.0282 163 LYS   B N   
6468 N N   B LYS   B 163 ? 0.1996 0.1851 0.3087 -0.0147 -0.0134 -0.0310 163 LYS   B N   
6469 C CA  A LYS   B 163 ? 0.1901 0.1546 0.3163 -0.0233 -0.0270 -0.0031 163 LYS   B CA  
6470 C CA  B LYS   B 163 ? 0.2114 0.2065 0.3155 -0.0150 -0.0111 -0.0164 163 LYS   B CA  
6471 C C   A LYS   B 163 ? 0.1617 0.1556 0.3052 -0.0300 -0.0250 0.0008  163 LYS   B C   
6472 C C   B LYS   B 163 ? 0.1803 0.1850 0.2927 -0.0165 -0.0133 -0.0066 163 LYS   B C   
6473 O O   A LYS   B 163 ? 0.1716 0.1529 0.3396 -0.0323 -0.0218 0.0016  163 LYS   B O   
6474 O O   B LYS   B 163 ? 0.1817 0.1855 0.2926 -0.0158 -0.0112 -0.0078 163 LYS   B O   
6475 C CB  A LYS   B 163 ? 0.2310 0.1748 0.3525 -0.0145 -0.0286 0.0152  163 LYS   B CB  
6476 C CB  B LYS   B 163 ? 0.2511 0.2479 0.3535 -0.0135 -0.0094 -0.0127 163 LYS   B CB  
6477 C CG  A LYS   B 163 ? 0.3058 0.2485 0.4045 -0.0150 -0.0168 0.0164  163 LYS   B CG  
6478 C CG  B LYS   B 163 ? 0.2918 0.2899 0.3968 -0.0117 -0.0072 -0.0090 163 LYS   B CG  
6479 C CD  A LYS   B 163 ? 0.3701 0.3101 0.4629 -0.0239 -0.0162 0.0094  163 LYS   B CD  
6480 C CD  B LYS   B 163 ? 0.3330 0.3318 0.4382 -0.0114 -0.0068 -0.0070 163 LYS   B CD  
6481 C CE  A LYS   B 163 ? 0.4194 0.3592 0.4966 -0.0317 -0.0106 0.0081  163 LYS   B CE  
6482 C CE  B LYS   B 163 ? 0.3630 0.3621 0.4688 -0.0118 -0.0055 -0.0053 163 LYS   B CE  
6483 N NZ  A LYS   B 163 ? 0.4485 0.3809 0.5275 -0.0358 -0.0079 0.0029  163 LYS   B NZ  
6484 N NZ  B LYS   B 163 ? 0.3718 0.3689 0.4893 -0.0120 -0.0048 -0.0053 163 LYS   B NZ  
6511 N N   . LEU   B 164 ? 0.1502 0.1626 0.2792 -0.0183 -0.0162 0.0054  164 LEU   B N   
6512 C CA  . LEU   B 164 ? 0.1572 0.1592 0.2620 -0.0091 -0.0199 -0.0004 164 LEU   B CA  
6513 C C   . LEU   B 164 ? 0.1590 0.1560 0.2590 -0.0118 -0.0225 0.0009  164 LEU   B C   
6514 O O   . LEU   B 164 ? 0.1633 0.1775 0.2765 -0.0165 -0.0216 -0.0008 164 LEU   B O   
6515 C CB  . LEU   B 164 ? 0.1528 0.1534 0.2489 -0.0139 -0.0173 -0.0053 164 LEU   B CB  
6516 C CG  . LEU   B 164 ? 0.1725 0.1638 0.2638 -0.0080 -0.0074 -0.0003 164 LEU   B CG  
6517 C CD1 . LEU   B 164 ? 0.1748 0.1627 0.2682 -0.0187 -0.0274 -0.0066 164 LEU   B CD1 
6518 C CD2 . LEU   B 164 ? 0.1916 0.1986 0.2802 -0.0008 0.0050  -0.0243 164 LEU   B CD2 
6531 N N   . VAL   B 165 ? 0.1897 0.1610 0.2872 -0.0268 -0.0233 -0.0122 165 VAL   B N   
6532 C CA  . VAL   B 165 ? 0.2307 0.1772 0.2797 -0.0376 -0.0420 -0.0051 165 VAL   B CA  
6533 C C   . VAL   B 165 ? 0.2601 0.1897 0.3122 -0.0424 -0.0768 -0.0033 165 VAL   B C   
6534 O O   . VAL   B 165 ? 0.2791 0.1945 0.3259 -0.0458 -0.0795 0.0026  165 VAL   B O   
6535 C CB  . VAL   B 165 ? 0.2564 0.1979 0.2797 -0.0255 -0.0174 -0.0234 165 VAL   B CB  
6536 C CG1 . VAL   B 165 ? 0.2772 0.2029 0.3133 -0.0303 -0.0059 -0.0260 165 VAL   B CG1 
6537 C CG2 . VAL   B 165 ? 0.2469 0.2030 0.2811 -0.0270 -0.0040 -0.0201 165 VAL   B CG2 
6547 N N   . SER   B 166 ? 0.2677 0.1838 0.3446 -0.0400 -0.0904 -0.0216 166 SER   B N   
6548 C CA  . SER   B 166 ? 0.2607 0.1880 0.3950 -0.0425 -0.0731 -0.0422 166 SER   B CA  
6549 C C   . SER   B 166 ? 0.2436 0.1933 0.4120 -0.0476 -0.0681 -0.0110 166 SER   B C   
6550 O O   . SER   B 166 ? 0.2457 0.2115 0.4527 -0.0574 -0.0814 -0.0379 166 SER   B O   
6551 C CB  . SER   B 166 ? 0.2606 0.1982 0.4218 -0.0293 -0.0607 -0.0519 166 SER   B CB  
6552 O OG  . SER   B 166 ? 0.2504 0.1883 0.4329 -0.0236 -0.0599 -0.0361 166 SER   B OG  
6558 N N   . SER   B 167 ? 0.2268 0.1919 0.3800 -0.0510 -0.0789 0.0339  167 SER   B N   
6559 C CA  . SER   B 167 ? 0.2185 0.2024 0.3813 -0.0429 -0.0529 0.0376  167 SER   B CA  
6560 C C   . SER   B 167 ? 0.2030 0.2115 0.3667 -0.0544 -0.0463 0.0599  167 SER   B C   
6561 O O   . SER   B 167 ? 0.2063 0.2181 0.3568 -0.0610 -0.0474 0.0466  167 SER   B O   
6562 C CB  . SER   B 167 ? 0.2037 0.1995 0.3826 -0.0360 -0.0199 0.0301  167 SER   B CB  
6563 O OG  . SER   B 167 ? 0.2035 0.1931 0.3787 -0.0244 -0.0047 0.0286  167 SER   B OG  
6569 N N   . PHE   B 168 ? 0.2016 0.2030 0.3559 -0.0508 -0.0292 0.0639  168 PHE   B N   
6570 C CA  . PHE   B 168 ? 0.2144 0.1973 0.3272 -0.0506 -0.0336 0.0397  168 PHE   B CA  
6571 C C   . PHE   B 168 ? 0.1937 0.1763 0.2802 -0.0286 -0.0142 0.0177  168 PHE   B C   
6572 O O   . PHE   B 168 ? 0.2226 0.1675 0.2804 -0.0043 -0.0084 -0.0039 168 PHE   B O   
6573 C CB  . PHE   B 168 ? 0.2340 0.1990 0.3277 -0.0614 -0.0529 0.0586  168 PHE   B CB  
6574 C CG  . PHE   B 168 ? 0.2608 0.1846 0.3116 -0.0613 -0.0526 0.0418  168 PHE   B CG  
6575 C CD1 . PHE   B 168 ? 0.2938 0.1988 0.3172 -0.0555 -0.0640 0.0275  168 PHE   B CD1 
6576 C CD2 . PHE   B 168 ? 0.2484 0.1774 0.3108 -0.0576 -0.0616 0.0406  168 PHE   B CD2 
6577 C CE1 . PHE   B 168 ? 0.3054 0.2084 0.3154 -0.0416 -0.0564 0.0339  168 PHE   B CE1 
6578 C CE2 . PHE   B 168 ? 0.2762 0.1876 0.3151 -0.0397 -0.0617 0.0332  168 PHE   B CE2 
6579 C CZ  . PHE   B 168 ? 0.2926 0.1903 0.3139 -0.0318 -0.0639 0.0453  168 PHE   B CZ  
6589 N N   . LEU   B 169 ? 0.2089 0.1998 0.2764 -0.0074 -0.0071 0.0035  169 LEU   B N   
6590 C CA  . LEU   B 169 ? 0.2420 0.2253 0.3161 -0.0153 -0.0074 -0.0367 169 LEU   B CA  
6591 C C   . LEU   B 169 ? 0.2660 0.2498 0.3879 -0.0018 -0.0060 -0.0652 169 LEU   B C   
6592 O O   . LEU   B 169 ? 0.2889 0.2654 0.4442 -0.0014 0.0034  -0.0832 169 LEU   B O   
6593 C CB  . LEU   B 169 ? 0.2678 0.2669 0.3229 -0.0205 -0.0135 -0.0050 169 LEU   B CB  
6594 C CG  . LEU   B 169 ? 0.3108 0.3054 0.3700 -0.0103 -0.0060 0.0064  169 LEU   B CG  
6595 C CD1 . LEU   B 169 ? 0.3262 0.3260 0.3797 -0.0113 -0.0093 0.0225  169 LEU   B CD1 
6596 C CD2 . LEU   B 169 ? 0.3105 0.3118 0.3772 0.0015  0.0096  -0.0020 169 LEU   B CD2 
6597 O OXT . LEU   B 169 ? 0.2729 0.2693 0.3942 0.0309  0.0039  -0.0643 169 LEU   B OXT 
6609 N N2  B A1BBU C .   ? 0.1956 0.2270 0.2099 -0.0085 0.0152  -0.0201 201 A1BBU A N2  
6610 C C3  B A1BBU C .   ? 0.2311 0.2546 0.2554 -0.0293 0.0188  -0.0166 201 A1BBU A C3  
6611 C C6  B A1BBU C .   ? 0.2336 0.2439 0.2454 -0.0215 0.0006  -0.0112 201 A1BBU A C6  
6612 C C9  B A1BBU C .   ? 0.1983 0.2270 0.2061 -0.0086 0.0135  -0.0139 201 A1BBU A C9  
6613 C C12 B A1BBU C .   ? 0.1790 0.2154 0.1882 -0.0078 0.0208  -0.0114 201 A1BBU A C12 
6614 C C14 B A1BBU C .   ? 0.1518 0.1992 0.1646 -0.0162 0.0239  -0.0048 201 A1BBU A C14 
6615 C C1  B A1BBU C .   ? 0.2309 0.2558 0.2472 -0.0243 0.0179  -0.0143 201 A1BBU A C1  
6616 C C10 B A1BBU C .   ? 0.1883 0.2247 0.2023 -0.0079 0.0176  -0.0136 201 A1BBU A C10 
6617 C C11 B A1BBU C .   ? 0.1730 0.2121 0.1851 -0.0085 0.0165  -0.0074 201 A1BBU A C11 
6618 C C13 B A1BBU C .   ? 0.1695 0.2090 0.1782 -0.0118 0.0286  -0.0078 201 A1BBU A C13 
6619 C C2  B A1BBU C .   ? 0.2312 0.2535 0.2510 -0.0265 0.0165  -0.0134 201 A1BBU A C2  
6620 C C4  B A1BBU C .   ? 0.2315 0.2568 0.2509 -0.0263 0.0231  -0.0093 201 A1BBU A C4  
6621 C C5  B A1BBU C .   ? 0.2298 0.2463 0.2429 -0.0217 0.0065  -0.0118 201 A1BBU A C5  
6622 C C7  B A1BBU C .   ? 0.2352 0.2418 0.2449 -0.0205 -0.0049 -0.0118 201 A1BBU A C7  
6623 C C8  B A1BBU C .   ? 0.2307 0.2396 0.2385 -0.0176 -0.0020 -0.0126 201 A1BBU A C8  
6624 N N1  B A1BBU C .   ? 0.2205 0.2388 0.2280 -0.0143 0.0059  -0.0136 201 A1BBU A N1  
6625 N N3  B A1BBU C .   ? 0.1815 0.2189 0.1951 -0.0122 0.0184  -0.0050 201 A1BBU A N3  
6626 N N4  B A1BBU C .   ? 0.1632 0.2038 0.1771 -0.0062 0.0136  -0.0035 201 A1BBU A N4  
6647 O O   . HOH   D .   ? 0.3266 0.1972 0.2232 0.0226  0.0354  0.0085  301 HOH   A O   
6648 O O   . HOH   D .   ? 0.3782 0.2814 0.3656 -0.0553 -0.0494 0.0410  302 HOH   A O   
6649 O O   . HOH   D .   ? 0.4263 0.7061 0.5001 -0.1158 0.0785  0.0632  303 HOH   A O   
6650 O O   . HOH   D .   ? 0.5845 0.6271 0.5538 -0.0603 0.0779  -0.0157 304 HOH   A O   
6651 O O   . HOH   D .   ? 0.2878 0.7023 0.5600 -0.0019 -0.0460 0.1659  305 HOH   A O   
6652 O O   . HOH   D .   ? 0.2291 0.2015 0.2489 0.0284  -0.0356 0.0046  306 HOH   A O   
6653 O O   . HOH   D .   ? 0.4290 0.3424 0.5668 0.0005  0.1545  -0.0314 307 HOH   A O   
6654 O O   . HOH   D .   ? 0.2717 0.5109 0.6370 -0.0131 0.1017  0.2533  308 HOH   A O   
6655 O O   . HOH   D .   ? 0.4659 0.3424 0.5228 -0.0269 0.1187  0.1083  309 HOH   A O   
6656 O O   . HOH   D .   ? 0.7588 0.4582 0.4395 -0.1207 0.1486  0.1506  310 HOH   A O   
6657 O O   . HOH   D .   ? 0.6841 0.4962 0.3697 0.1929  -0.1330 0.0553  311 HOH   A O   
6658 O O   . HOH   D .   ? 0.3253 0.3623 0.1810 -0.0264 0.0609  0.0428  312 HOH   A O   
6659 O O   . HOH   D .   ? 0.2521 0.2579 0.3405 -0.0186 0.0556  0.0914  313 HOH   A O   
6660 O O   A HOH   D .   ? 0.4593 0.5612 0.2879 -0.1038 0.1155  0.1032  314 HOH   A O   
6661 O O   . HOH   D .   ? 0.2303 0.3731 0.4490 -0.0447 0.0263  -0.1195 315 HOH   A O   
6662 O O   . HOH   D .   ? 0.4773 0.4452 0.4286 -0.2088 -0.0730 0.1982  316 HOH   A O   
6663 O O   . HOH   D .   ? 0.2263 0.2073 0.3677 -0.0466 -0.0077 -0.0303 317 HOH   A O   
6664 O O   . HOH   D .   ? 0.3357 0.3040 0.3114 -0.0967 0.0279  0.0596  318 HOH   A O   
6665 O O   . HOH   D .   ? 0.7044 0.5979 0.3851 -0.0077 -0.0590 0.1144  319 HOH   A O   
6666 O O   . HOH   D .   ? 0.1969 0.4279 0.3018 0.0707  -0.0143 0.0174  320 HOH   A O   
6667 O O   . HOH   D .   ? 0.3434 0.3858 0.4076 -0.0425 0.1301  0.0185  321 HOH   A O   
6668 O O   . HOH   D .   ? 0.2728 0.5552 0.4605 0.0099  -0.0468 0.1292  322 HOH   A O   
6669 O O   . HOH   D .   ? 0.1821 0.3689 0.2986 -0.0058 0.0283  0.0856  323 HOH   A O   
6670 O O   . HOH   D .   ? 0.2792 0.2727 0.4518 -0.0246 -0.1021 0.1036  324 HOH   A O   
6671 O O   . HOH   D .   ? 0.2175 0.1900 0.1826 -0.0079 0.0210  0.0178  325 HOH   A O   
6672 O O   . HOH   D .   ? 0.2444 0.4229 0.4393 -0.0410 -0.1022 0.1764  326 HOH   A O   
6673 O O   . HOH   D .   ? 0.3550 0.4536 0.2858 -0.0168 0.0658  0.0332  327 HOH   A O   
6674 O O   . HOH   D .   ? 0.2420 0.2269 0.3167 0.0341  0.0341  0.0331  328 HOH   A O   
6675 O O   . HOH   D .   ? 0.1767 0.1653 0.2391 -0.0268 0.0074  0.0013  329 HOH   A O   
6676 O O   . HOH   D .   ? 0.5461 0.6341 0.4564 0.0405  -0.1170 -0.1070 330 HOH   A O   
6677 O O   . HOH   D .   ? 0.5579 0.2349 0.5314 0.0965  -0.0308 -0.0121 331 HOH   A O   
6678 O O   . HOH   D .   ? 0.4516 0.4025 0.3496 -0.1025 -0.1037 -0.0118 332 HOH   A O   
6679 O O   . HOH   D .   ? 0.5581 0.5668 0.4749 -0.1681 -0.1129 -0.0610 333 HOH   A O   
6680 O O   . HOH   D .   ? 0.5327 0.3980 0.3203 0.0347  0.0596  0.1186  334 HOH   A O   
6681 O O   . HOH   D .   ? 0.3598 0.4579 0.3938 -0.1221 -0.0931 -0.0604 335 HOH   A O   
6682 O O   . HOH   D .   ? 0.7714 0.4713 0.6261 -0.0766 -0.1349 0.0521  336 HOH   A O   
6683 O O   . HOH   D .   ? 0.6186 0.4929 0.4921 0.0873  0.1669  -0.1131 337 HOH   A O   
6684 O O   . HOH   D .   ? 0.2288 0.2340 0.3210 0.0220  -0.0436 0.0316  338 HOH   A O   
6685 O O   . HOH   D .   ? 0.4391 0.2638 0.4664 0.0276  -0.1136 0.1094  339 HOH   A O   
6686 O O   . HOH   D .   ? 0.1599 0.1961 0.2861 0.0062  -0.0342 -0.0482 340 HOH   A O   
6687 O O   . HOH   D .   ? 0.1671 0.2306 0.2400 0.0009  -0.0081 0.0478  341 HOH   A O   
6688 O O   . HOH   D .   ? 0.1623 0.1940 0.2114 0.0064  -0.0212 -0.0345 342 HOH   A O   
6689 O O   . HOH   D .   ? 0.1421 0.1500 0.1690 -0.0044 0.0160  0.0135  343 HOH   A O   
6690 O O   . HOH   D .   ? 0.2767 0.4640 0.3599 -0.0586 0.0459  0.0128  344 HOH   A O   
6691 O O   . HOH   D .   ? 0.5081 0.3372 0.3436 -0.1330 0.0186  0.0906  345 HOH   A O   
6692 O O   . HOH   D .   ? 0.3587 0.4413 0.4832 0.1539  0.0831  0.0529  346 HOH   A O   
6693 O O   . HOH   D .   ? 0.5066 0.5001 0.5413 0.1850  0.1469  -0.0110 347 HOH   A O   
6694 O O   . HOH   D .   ? 0.3149 0.3821 0.2726 -0.0850 -0.0187 -0.0791 348 HOH   A O   
6695 O O   . HOH   D .   ? 0.1664 0.2053 0.2593 0.0114  -0.0047 -0.0005 349 HOH   A O   
6696 O O   . HOH   D .   ? 0.1772 0.1512 0.2465 -0.0118 0.0217  -0.0122 350 HOH   A O   
6697 O O   . HOH   D .   ? 0.2872 0.4073 0.3767 0.1127  -0.0889 -0.0135 351 HOH   A O   
6698 O O   . HOH   D .   ? 0.6188 0.4604 0.5567 -0.1639 0.0281  0.0790  352 HOH   A O   
6699 O O   A HOH   D .   ? 0.2421 0.2826 0.2812 0.0350  0.0303  0.0280  353 HOH   A O   
6700 O O   . HOH   D .   ? 0.2063 0.2207 0.3875 0.0220  0.0957  -0.0056 354 HOH   A O   
6701 O O   . HOH   D .   ? 0.6443 0.4288 0.6068 0.0221  -0.0916 0.0522  355 HOH   A O   
6702 O O   . HOH   D .   ? 0.3803 0.4718 0.4671 0.1892  0.0691  0.0138  356 HOH   A O   
6703 O O   . HOH   D .   ? 0.2940 0.2222 0.2639 -0.0392 0.0214  -0.0174 357 HOH   A O   
6704 O O   . HOH   D .   ? 0.2052 0.2233 0.2508 -0.0396 0.0082  0.0369  358 HOH   A O   
6705 O O   . HOH   D .   ? 0.2145 0.2606 0.3925 0.0255  0.0868  -0.0583 359 HOH   A O   
6706 O O   . HOH   D .   ? 0.3978 0.2324 0.2497 0.1155  0.0386  0.0099  360 HOH   A O   
6707 O O   . HOH   D .   ? 0.5390 0.2703 0.4272 -0.1626 0.1760  -0.0696 361 HOH   A O   
6708 O O   A HOH   D .   ? 0.2752 0.5152 0.5789 0.0921  0.0333  0.0432  362 HOH   A O   
6709 O O   A HOH   D .   ? 0.1788 0.2580 0.2529 0.0528  0.0525  0.0761  363 HOH   A O   
6710 O O   . HOH   D .   ? 0.1672 0.1730 0.1635 -0.0034 -0.0109 -0.0045 364 HOH   A O   
6711 O O   . HOH   D .   ? 0.3989 0.3445 0.3938 -0.1223 -0.0245 -0.0006 365 HOH   A O   
6712 O O   . HOH   D .   ? 0.2995 0.3668 0.5114 -0.0724 -0.0865 -0.0830 366 HOH   A O   
6713 O O   . HOH   D .   ? 0.1928 0.1989 0.2333 0.0109  -0.0211 0.0294  367 HOH   A O   
6714 O O   . HOH   D .   ? 0.4094 0.2635 0.4833 -0.1224 0.0952  0.0311  368 HOH   A O   
6715 O O   . HOH   D .   ? 0.4068 0.7018 0.4993 -0.0536 -0.1600 0.0659  369 HOH   A O   
6716 O O   . HOH   D .   ? 0.2259 0.2408 0.2233 -0.0298 -0.0363 0.0352  370 HOH   A O   
6717 O O   . HOH   D .   ? 0.2338 0.2134 0.2905 -0.0035 -0.0646 -0.0211 371 HOH   A O   
6718 O O   . HOH   D .   ? 0.1868 0.1828 0.2548 -0.0201 0.0121  0.0332  372 HOH   A O   
6719 O O   . HOH   D .   ? 0.2357 0.2191 0.2101 0.0007  0.0198  0.0068  373 HOH   A O   
6720 O O   . HOH   D .   ? 0.2830 0.2972 0.4308 -0.0755 0.1094  -0.0029 374 HOH   A O   
6721 O O   . HOH   D .   ? 0.3567 0.2271 0.5525 -0.0561 0.0153  -0.0021 375 HOH   A O   
6722 O O   . HOH   D .   ? 0.2497 0.3412 0.3297 -0.0117 -0.0071 -0.0497 376 HOH   A O   
6723 O O   . HOH   D .   ? 0.3472 0.2851 0.3782 -0.0129 -0.0578 0.1102  377 HOH   A O   
6724 O O   . HOH   D .   ? 0.3033 0.4370 0.3537 0.0639  0.0956  0.1900  378 HOH   A O   
6725 O O   B HOH   D .   ? 0.2439 0.1712 0.1741 0.0541  0.0065  0.0427  379 HOH   A O   
6726 O O   . HOH   D .   ? 0.1966 0.2600 0.3592 -0.0074 0.0716  0.0627  380 HOH   A O   
6727 O O   . HOH   D .   ? 0.3305 0.3143 0.2170 0.0444  0.0699  -0.0046 381 HOH   A O   
6728 O O   . HOH   D .   ? 0.3775 0.4371 0.3566 -0.0099 -0.0378 0.0957  382 HOH   A O   
6729 O O   . HOH   D .   ? 0.1935 0.2460 0.2173 -0.0183 0.0014  0.0685  383 HOH   A O   
6730 O O   . HOH   D .   ? 0.4464 0.4571 0.5278 0.1628  0.0878  -0.1040 384 HOH   A O   
6731 O O   . HOH   D .   ? 0.2030 0.2741 0.2756 0.0417  0.0371  0.0870  385 HOH   A O   
6732 O O   A HOH   D .   ? 0.2423 0.2283 0.2727 0.0150  0.0057  0.0583  386 HOH   A O   
6733 O O   . HOH   D .   ? 0.1743 0.1760 0.2168 0.0004  -0.0250 0.0051  387 HOH   A O   
6734 O O   . HOH   D .   ? 0.6248 0.3499 0.4655 0.1456  0.0000  -0.0241 388 HOH   A O   
6735 O O   . HOH   D .   ? 0.2839 0.2016 0.2149 -0.0581 0.0393  0.0201  389 HOH   A O   
6736 O O   . HOH   D .   ? 0.5219 0.5212 0.6009 -0.1010 0.0005  0.1082  390 HOH   A O   
6737 O O   . HOH   D .   ? 0.4172 0.6319 0.4102 0.1430  0.1192  -0.0946 391 HOH   A O   
6738 O O   . HOH   D .   ? 0.6350 0.6509 0.4345 0.2272  -0.0606 -0.0526 392 HOH   A O   
6739 O O   . HOH   D .   ? 0.3354 0.2900 0.2296 -0.0696 -0.0728 0.0195  393 HOH   A O   
6740 O O   . HOH   D .   ? 0.2340 0.2580 0.4455 0.0131  -0.0608 -0.0347 394 HOH   A O   
6741 O O   . HOH   D .   ? 0.4299 0.6742 0.4308 -0.1158 -0.0153 0.1338  395 HOH   A O   
6742 O O   . HOH   D .   ? 0.2384 0.1800 0.3228 -0.0010 -0.0445 0.0228  396 HOH   A O   
6743 O O   . HOH   D .   ? 0.1463 0.1572 0.2153 0.0021  -0.0122 0.0053  397 HOH   A O   
6744 O O   . HOH   D .   ? 0.1998 0.1915 0.2589 0.0213  -0.0366 0.0288  398 HOH   A O   
6745 O O   . HOH   D .   ? 0.2974 0.4024 0.3665 -0.0213 0.1007  -0.0609 399 HOH   A O   
6746 O O   . HOH   D .   ? 0.4571 0.5905 0.5355 0.1043  0.0740  0.0528  400 HOH   A O   
6747 O O   . HOH   D .   ? 0.1862 0.1503 0.1919 -0.0227 0.0198  0.0042  401 HOH   A O   
6748 O O   A HOH   D .   ? 0.2891 0.2327 0.4114 -0.0049 0.1040  -0.0194 402 HOH   A O   
6749 O O   . HOH   D .   ? 0.5121 0.4338 0.2213 -0.0271 0.0867  0.0562  403 HOH   A O   
6750 O O   . HOH   D .   ? 0.2171 0.2245 0.2897 -0.0140 -0.0194 0.0763  404 HOH   A O   
6751 O O   . HOH   D .   ? 0.1934 0.2118 0.3669 0.0338  0.0963  0.0840  405 HOH   A O   
6752 O O   . HOH   D .   ? 0.9340 0.9048 0.7274 -0.0589 0.0167  -0.0942 406 HOH   A O   
6753 O O   . HOH   D .   ? 0.5788 0.3510 0.7175 0.0791  -0.0336 -0.1008 407 HOH   A O   
6754 O O   . HOH   D .   ? 0.2196 0.2750 0.4088 -0.0216 -0.0228 0.0188  408 HOH   A O   
6755 O O   . HOH   D .   ? 0.4660 0.6106 0.3684 -0.0928 -0.0164 0.1265  409 HOH   A O   
6756 O O   . HOH   D .   ? 0.4173 0.2451 0.5537 -0.0747 -0.2406 0.0946  410 HOH   A O   
6757 O O   . HOH   D .   ? 0.7104 0.3928 0.5124 0.1949  -0.0685 0.1398  411 HOH   A O   
6758 O O   . HOH   D .   ? 0.2600 0.2066 0.2787 -0.0026 0.0139  0.0245  412 HOH   A O   
6759 O O   . HOH   D .   ? 0.2987 0.3438 0.3505 -0.0197 0.1033  -0.0085 413 HOH   A O   
6760 O O   . HOH   D .   ? 0.5861 0.4930 0.3932 0.0060  -0.1472 0.0184  414 HOH   A O   
6761 O O   . HOH   D .   ? 0.3668 0.4455 0.3739 0.1174  -0.0393 -0.1407 415 HOH   A O   
6762 O O   . HOH   D .   ? 0.2818 0.3972 0.7262 -0.0016 0.1237  -0.0590 416 HOH   A O   
6763 O O   . HOH   D .   ? 0.2675 0.2226 0.2875 -0.0565 -0.0015 0.0474  417 HOH   A O   
6764 O O   . HOH   D .   ? 0.4046 0.3900 0.2779 -0.0332 -0.1319 0.0531  418 HOH   A O   
6765 O O   . HOH   D .   ? 0.6681 0.5990 0.5318 -0.0511 0.1259  0.0593  419 HOH   A O   
6766 O O   . HOH   D .   ? 0.3085 0.3783 0.5291 -0.0438 0.1312  -0.0209 420 HOH   A O   
6767 O O   . HOH   D .   ? 0.1741 0.1852 0.3260 0.0052  -0.0050 0.0188  421 HOH   A O   
6768 O O   . HOH   D .   ? 0.3398 0.1510 0.2288 0.0033  -0.0520 0.0154  422 HOH   A O   
6769 O O   . HOH   D .   ? 0.6469 0.7212 0.5872 0.0489  0.0019  0.0191  423 HOH   A O   
6770 O O   . HOH   D .   ? 0.2457 0.4480 0.2770 0.1530  -0.0176 0.0288  424 HOH   A O   
6771 O O   A HOH   D .   ? 0.6252 0.4701 0.3912 -0.0763 0.0712  0.1200  425 HOH   A O   
6772 O O   . HOH   D .   ? 0.4067 0.3064 0.5890 0.1026  0.1259  0.0698  426 HOH   A O   
6773 O O   . HOH   D .   ? 0.1888 0.2348 0.3179 -0.0265 -0.0092 0.0560  427 HOH   A O   
6774 O O   . HOH   D .   ? 0.2831 0.6614 0.1827 -0.0492 0.0411  0.0062  428 HOH   A O   
6775 O O   . HOH   D .   ? 0.2443 0.2798 0.2797 0.0019  -0.0639 0.0289  429 HOH   A O   
6776 O O   . HOH   D .   ? 0.4999 0.6831 0.3791 0.0878  0.1939  -0.0720 430 HOH   A O   
6777 O O   . HOH   D .   ? 0.5960 0.5809 0.6242 -0.1326 -0.0093 -0.1190 431 HOH   A O   
6778 O O   A HOH   D .   ? 0.3047 0.2238 0.3728 0.0315  0.0740  0.0821  432 HOH   A O   
6779 O O   . HOH   D .   ? 0.4495 0.3218 0.2551 -0.0397 -0.0273 0.0353  433 HOH   A O   
6780 O O   . HOH   D .   ? 0.6122 0.6040 0.5855 0.0523  -0.1019 0.0328  434 HOH   A O   
6781 O O   . HOH   D .   ? 0.4457 0.5988 0.6938 -0.1785 0.0507  -0.0987 435 HOH   A O   
6782 O O   . HOH   D .   ? 0.4588 0.4589 0.4968 -0.1262 -0.0878 -0.1103 436 HOH   A O   
6783 O O   . HOH   D .   ? 0.2286 0.1689 0.1789 -0.0091 -0.0062 -0.0125 437 HOH   A O   
6784 O O   A HOH   D .   ? 0.2300 0.1732 0.2517 0.0257  -0.0713 -0.0390 438 HOH   A O   
6785 O O   . HOH   D .   ? 0.7939 0.7227 0.4855 0.2605  -0.1012 0.1771  439 HOH   A O   
6786 O O   . HOH   D .   ? 0.2744 0.1891 0.2853 0.0033  0.0083  0.0027  440 HOH   A O   
6787 O O   . HOH   D .   ? 0.2167 0.2167 0.5343 -0.0233 -0.0953 0.0670  441 HOH   A O   
6788 O O   . HOH   D .   ? 0.3845 0.2697 0.1967 -0.0712 0.0154  0.0246  442 HOH   A O   
6789 O O   . HOH   D .   ? 0.3278 0.3145 0.5672 -0.0062 0.1507  -0.0795 443 HOH   A O   
6790 O O   . HOH   D .   ? 0.4637 0.3986 0.3285 0.2543  -0.0268 -0.0423 444 HOH   A O   
6791 O O   . HOH   D .   ? 0.6445 0.4941 0.4638 -0.0667 0.1143  0.1448  445 HOH   A O   
6792 O O   . HOH   D .   ? 0.2419 0.2943 0.2832 -0.0007 -0.0245 -0.0459 446 HOH   A O   
6793 O O   . HOH   D .   ? 0.2655 0.2211 0.2774 0.0146  0.0368  0.0278  447 HOH   A O   
6794 O O   . HOH   D .   ? 0.5367 0.5485 0.7794 0.0336  -0.1348 0.1696  448 HOH   A O   
6795 O O   A HOH   D .   ? 0.2289 0.1886 0.3842 -0.0128 0.0688  0.0625  449 HOH   A O   
6796 O O   . HOH   D .   ? 0.2975 0.3147 0.4006 0.0655  -0.0429 0.0540  450 HOH   A O   
6797 O O   . HOH   D .   ? 0.5791 0.3942 0.4468 0.0389  0.0446  0.0718  451 HOH   A O   
6798 O O   . HOH   D .   ? 0.5012 0.4840 0.4212 0.0316  -0.0122 0.1081  452 HOH   A O   
6799 O O   . HOH   D .   ? 0.5153 0.3492 0.4815 0.0485  0.0633  0.0611  453 HOH   A O   
6800 O O   . HOH   D .   ? 0.3259 0.3150 0.3581 -0.0751 0.0141  -0.0661 454 HOH   A O   
6801 O O   . HOH   D .   ? 0.7000 0.8251 0.5090 -0.0240 -0.0484 -0.0286 455 HOH   A O   
6802 O O   . HOH   D .   ? 0.3603 0.5310 0.5082 0.0762  -0.0792 0.1562  456 HOH   A O   
6803 O O   . HOH   D .   ? 0.3196 0.5732 0.5518 -0.1541 0.1076  -0.1479 457 HOH   A O   
6804 O O   . HOH   D .   ? 0.4147 0.5778 0.3795 0.0206  -0.0317 -0.0474 458 HOH   A O   
6805 O O   . HOH   D .   ? 0.6014 0.5094 0.5101 0.0260  0.1159  0.0563  459 HOH   A O   
6806 O O   . HOH   D .   ? 0.3279 0.4318 0.4168 -0.0137 -0.0330 0.0091  460 HOH   A O   
6807 O O   . HOH   D .   ? 0.5673 0.6674 0.4632 0.1459  -0.1308 0.0431  461 HOH   A O   
6808 O O   . HOH   D .   ? 0.2902 0.2865 0.3481 -0.0887 0.0429  -0.0320 462 HOH   A O   
6809 O O   . HOH   D .   ? 0.3008 0.2147 0.2613 0.0437  -0.0820 -0.0336 463 HOH   A O   
6810 O O   . HOH   D .   ? 0.3028 0.3972 0.6358 0.0440  0.0290  -0.1979 464 HOH   A O   
6811 O O   . HOH   D .   ? 0.5533 0.5967 0.4696 0.1391  -0.0936 -0.1119 465 HOH   A O   
6812 O O   . HOH   D .   ? 0.3935 0.5927 0.4129 -0.0711 -0.0871 0.1782  466 HOH   A O   
6813 O O   . HOH   D .   ? 0.7061 0.5014 0.5611 0.1235  0.2120  0.1960  467 HOH   A O   
6814 O O   A HOH   D .   ? 0.2994 0.2867 0.5082 0.0743  -0.1416 -0.0536 468 HOH   A O   
6815 O O   . HOH   D .   ? 0.3197 0.3001 0.3873 0.0055  0.0658  -0.0095 469 HOH   A O   
6816 O O   . HOH   D .   ? 0.5607 0.3501 0.7804 0.0592  0.0700  0.2298  470 HOH   A O   
6817 O O   . HOH   D .   ? 0.6600 0.4224 0.4870 -0.0745 0.1549  -0.0150 471 HOH   A O   
6818 O O   . HOH   D .   ? 0.4679 0.4894 0.5259 -0.2055 -0.0274 0.0113  472 HOH   A O   
6819 O O   . HOH   D .   ? 0.5402 0.6118 0.6200 -0.1814 -0.1185 0.0101  473 HOH   A O   
6820 O O   . HOH   D .   ? 0.4736 0.4766 0.3565 -0.0728 -0.0323 0.0052  474 HOH   A O   
6821 O O   . HOH   D .   ? 0.4215 0.3956 0.2993 -0.0990 0.1171  -0.0615 475 HOH   A O   
6822 O O   . HOH   D .   ? 0.8089 0.4283 0.3461 -0.0354 -0.1189 -0.0186 476 HOH   A O   
6823 O O   . HOH   D .   ? 0.2720 0.2684 0.2725 0.0239  0.0091  0.0052  477 HOH   A O   
6824 O O   . HOH   D .   ? 0.6359 0.5427 0.4700 -0.0654 -0.0701 -0.0741 478 HOH   A O   
6825 O O   . HOH   D .   ? 0.5930 0.5353 0.6460 -0.1694 0.0200  -0.0876 479 HOH   A O   
6826 O O   . HOH   D .   ? 0.4519 0.5512 0.2890 -0.0151 0.0084  0.0284  480 HOH   A O   
6827 O O   . HOH   D .   ? 0.6010 0.4341 0.4559 0.0394  0.0147  -0.1368 481 HOH   A O   
6828 O O   . HOH   D .   ? 0.4667 0.2689 0.3811 -0.0736 -0.1337 0.0635  482 HOH   A O   
6829 O O   . HOH   D .   ? 0.5372 0.5656 0.6541 0.0555  0.1232  -0.1187 483 HOH   A O   
6830 O O   . HOH   D .   ? 0.2837 0.5822 0.4039 0.1187  0.1114  0.2599  484 HOH   A O   
6831 O O   . HOH   D .   ? 0.5730 0.6926 0.4766 -0.0697 0.1374  0.1038  485 HOH   A O   
6832 O O   . HOH   D .   ? 0.2837 0.4805 0.4988 0.0135  0.1093  0.1020  486 HOH   A O   
6833 O O   . HOH   D .   ? 0.2631 0.2973 0.6805 -0.0270 -0.1327 0.0348  487 HOH   A O   
6834 O O   . HOH   D .   ? 0.6157 0.7029 0.6300 0.0459  -0.1273 0.0444  488 HOH   A O   
6835 O O   . HOH   D .   ? 0.6508 0.2883 0.4753 -0.0838 0.0806  0.0977  489 HOH   A O   
6836 O O   . HOH   D .   ? 0.4483 0.3506 0.4766 -0.0231 0.2332  0.0150  490 HOH   A O   
6837 O O   . HOH   D .   ? 0.3089 0.2542 0.5322 0.0238  0.0386  0.0834  491 HOH   A O   
6838 O O   . HOH   D .   ? 0.4138 0.3090 0.4623 -0.1087 0.0245  0.0742  492 HOH   A O   
6839 O O   . HOH   D .   ? 0.2704 0.3480 0.5089 -0.0177 0.0971  -0.0707 493 HOH   A O   
6840 O O   . HOH   D .   ? 0.3947 0.8222 0.5880 -0.1133 -0.0314 0.2275  494 HOH   A O   
6841 O O   . HOH   D .   ? 0.2571 0.3564 0.3750 0.0439  -0.0492 0.0633  495 HOH   A O   
6842 O O   . HOH   D .   ? 0.4852 0.2858 0.4983 -0.1433 0.0241  0.0581  496 HOH   A O   
6843 O O   . HOH   D .   ? 0.3357 0.4778 0.3729 -0.0055 -0.0431 -0.1001 497 HOH   A O   
6844 O O   . HOH   D .   ? 0.2860 0.3944 0.4513 0.0325  -0.0221 0.0420  498 HOH   A O   
6845 O O   . HOH   D .   ? 0.4907 0.6943 0.5264 0.0636  -0.0741 0.1007  499 HOH   A O   
6846 O O   . HOH   D .   ? 0.7273 0.4407 0.5312 0.0491  0.0409  0.0334  500 HOH   A O   
6847 O O   . HOH   D .   ? 0.3706 0.8266 0.3343 0.0352  0.1048  -0.0100 501 HOH   A O   
6848 O O   . HOH   D .   ? 0.5140 0.7008 0.4969 0.2405  -0.0137 0.1380  502 HOH   A O   
6849 O O   . HOH   D .   ? 0.3196 0.2626 0.4957 0.0300  0.0534  0.0683  503 HOH   A O   
6850 O O   . HOH   D .   ? 0.4578 0.6259 0.4811 0.0669  -0.0545 -0.1076 504 HOH   A O   
6851 O O   . HOH   D .   ? 0.2988 0.6817 0.4353 0.0667  0.0434  -0.0007 505 HOH   A O   
6852 O O   . HOH   D .   ? 0.4633 0.4897 0.4154 0.1277  -0.0622 0.0726  506 HOH   A O   
6853 O O   . HOH   D .   ? 0.4962 0.6745 0.5387 -0.0464 -0.0789 -0.0262 507 HOH   A O   
6854 O O   . HOH   D .   ? 0.3005 0.4216 0.6496 -0.0286 -0.0703 0.2629  508 HOH   A O   
6855 O O   . HOH   E .   ? 0.2790 0.2256 0.3457 0.0245  0.0928  0.0340  201 HOH   B O   
6856 O O   . HOH   E .   ? 0.3982 0.7201 0.3959 0.0854  0.0111  0.2404  202 HOH   B O   
6857 O O   . HOH   E .   ? 0.5928 0.6649 0.6229 0.1731  0.0453  -0.0099 203 HOH   B O   
6858 O O   . HOH   E .   ? 0.4971 0.4947 0.2504 0.0387  -0.0546 -0.1268 204 HOH   B O   
6859 O O   . HOH   E .   ? 0.7600 0.4224 0.5604 0.0790  0.1831  0.0428  205 HOH   B O   
6860 O O   . HOH   E .   ? 0.4984 0.2768 0.4304 -0.0568 -0.0037 -0.1034 206 HOH   B O   
6861 O O   . HOH   E .   ? 0.4056 0.3179 0.6510 -0.0217 0.0473  -0.0313 207 HOH   B O   
6862 O O   . HOH   E .   ? 0.2114 0.2431 0.3228 -0.0038 0.0154  -0.0185 208 HOH   B O   
6863 O O   . HOH   E .   ? 0.4236 0.4633 0.4347 0.2038  -0.0451 0.0191  209 HOH   B O   
6864 O O   . HOH   E .   ? 0.5527 0.4547 0.3501 -0.0713 -0.1132 0.0606  210 HOH   B O   
6865 O O   . HOH   E .   ? 0.4689 0.5733 0.4476 0.2795  -0.1304 -0.0410 211 HOH   B O   
6866 O O   . HOH   E .   ? 0.2927 0.3158 0.6669 0.0571  -0.1190 0.0578  212 HOH   B O   
6867 O O   . HOH   E .   ? 0.2706 0.5987 0.5318 -0.0059 0.1292  -0.2063 213 HOH   B O   
6868 O O   . HOH   E .   ? 0.1647 0.2122 0.2971 -0.0207 -0.0062 0.0105  214 HOH   B O   
6869 O O   . HOH   E .   ? 0.5448 0.4044 0.6691 0.0587  -0.0883 0.2673  215 HOH   B O   
6870 O O   . HOH   E .   ? 0.4176 0.5688 0.5270 0.2402  0.0448  -0.0571 216 HOH   B O   
6871 O O   . HOH   E .   ? 0.3224 0.2089 0.5397 0.0174  0.1801  0.0736  217 HOH   B O   
6872 O O   . HOH   E .   ? 0.4278 0.4142 0.5277 -0.1812 0.0221  0.1036  218 HOH   B O   
6873 O O   . HOH   E .   ? 0.4236 0.4584 0.5558 -0.1195 -0.0104 -0.1549 219 HOH   B O   
6874 O O   . HOH   E .   ? 0.1924 0.2231 0.3178 -0.0089 0.0143  -0.0188 220 HOH   B O   
6875 O O   . HOH   E .   ? 0.3286 0.3615 0.5366 0.0401  -0.0734 -0.0186 221 HOH   B O   
6876 O O   . HOH   E .   ? 0.5267 0.2369 0.3801 -0.0106 -0.1201 0.0013  222 HOH   B O   
6877 O O   . HOH   E .   ? 0.6042 0.4925 0.4803 0.1217  0.0104  -0.1209 223 HOH   B O   
6878 O O   . HOH   E .   ? 0.4261 0.5052 0.4306 0.0506  0.0587  -0.1633 224 HOH   B O   
6879 O O   . HOH   E .   ? 0.3317 0.2567 0.4442 -0.0042 0.1484  -0.0013 225 HOH   B O   
6880 O O   . HOH   E .   ? 0.4347 0.3621 0.6657 -0.0209 -0.1886 -0.0879 226 HOH   B O   
6881 O O   . HOH   E .   ? 0.2675 0.2021 0.3032 -0.0347 0.1000  0.0030  227 HOH   B O   
6882 O O   . HOH   E .   ? 0.2857 0.3891 0.3966 -0.0821 0.0164  0.0148  228 HOH   B O   
6883 O O   . HOH   E .   ? 0.5282 0.6512 0.3748 0.1088  0.0221  0.0678  229 HOH   B O   
6884 O O   . HOH   E .   ? 0.5243 0.3263 0.4092 -0.1554 0.0274  -0.0059 230 HOH   B O   
6885 O O   . HOH   E .   ? 0.5257 0.3580 0.4747 -0.2513 0.0121  0.0008  231 HOH   B O   
6886 O O   . HOH   E .   ? 0.3462 0.2023 0.6104 -0.0230 -0.1279 -0.0087 232 HOH   B O   
6887 O O   . HOH   E .   ? 0.1697 0.1590 0.1816 -0.0101 -0.0014 0.0034  233 HOH   B O   
6888 O O   . HOH   E .   ? 0.2505 0.2462 0.4059 -0.0305 -0.0095 -0.0570 234 HOH   B O   
6889 O O   . HOH   E .   ? 0.2798 0.2960 0.3396 0.0395  0.0226  -0.0954 235 HOH   B O   
6890 O O   . HOH   E .   ? 0.3971 0.3626 0.2275 0.0436  0.0787  0.0613  236 HOH   B O   
6891 O O   . HOH   E .   ? 0.3536 0.3288 0.6400 0.0113  0.0927  0.0130  237 HOH   B O   
6892 O O   . HOH   E .   ? 0.2129 0.1530 0.3661 0.0074  -0.0463 -0.0204 238 HOH   B O   
6893 O O   . HOH   E .   ? 0.3772 0.2608 0.4622 0.0713  -0.0643 -0.0985 239 HOH   B O   
6894 O O   . HOH   E .   ? 0.2389 0.2652 0.3220 -0.0525 -0.0031 -0.0206 240 HOH   B O   
6895 O O   . HOH   E .   ? 0.3815 0.2413 0.4294 0.0272  -0.0427 -0.0883 241 HOH   B O   
6896 O O   . HOH   E .   ? 0.2801 0.2464 0.3087 0.0830  0.0558  0.0018  242 HOH   B O   
6897 O O   . HOH   E .   ? 0.2300 0.3971 0.3470 -0.0341 -0.0521 -0.0638 243 HOH   B O   
6898 O O   . HOH   E .   ? 0.2412 0.3942 0.2607 -0.0480 -0.0215 0.0683  244 HOH   B O   
6899 O O   . HOH   E .   ? 0.1726 0.1690 0.2733 -0.0096 0.0080  -0.0185 245 HOH   B O   
6900 O O   . HOH   E .   ? 0.1614 0.1445 0.1819 -0.0018 -0.0097 0.0075  246 HOH   B O   
6901 O O   . HOH   E .   ? 0.3717 0.2131 0.2273 0.0203  -0.0674 -0.0206 247 HOH   B O   
6902 O O   . HOH   E .   ? 0.5037 0.7618 0.4043 0.3056  0.0376  -0.0180 248 HOH   B O   
6903 O O   . HOH   E .   ? 0.2950 0.3768 0.5341 0.1100  -0.0665 -0.0852 249 HOH   B O   
6904 O O   . HOH   E .   ? 0.2473 0.2259 0.2325 -0.0389 -0.0481 0.0151  250 HOH   B O   
6905 O O   . HOH   E .   ? 0.2361 0.1641 0.2236 -0.0348 -0.0416 0.0285  251 HOH   B O   
6906 O O   . HOH   E .   ? 0.1586 0.1808 0.2157 -0.0093 0.0035  0.0116  252 HOH   B O   
6907 O O   . HOH   E .   ? 0.3681 0.3565 0.2437 0.0465  0.0686  0.0338  253 HOH   B O   
6908 O O   . HOH   E .   ? 0.3520 0.2557 0.3385 -0.0447 0.0388  -0.0646 254 HOH   B O   
6909 O O   . HOH   E .   ? 0.1772 0.1831 0.3069 -0.0152 -0.0171 0.0042  255 HOH   B O   
6910 O O   . HOH   E .   ? 0.4745 0.3716 0.4019 -0.0948 0.0612  -0.0768 256 HOH   B O   
6911 O O   . HOH   E .   ? 0.4231 0.3562 0.5368 -0.0365 -0.1048 -0.1081 257 HOH   B O   
6912 O O   . HOH   E .   ? 0.2765 0.2342 0.2041 0.0166  -0.0045 0.0039  258 HOH   B O   
6913 O O   . HOH   E .   ? 0.5519 0.3285 0.2959 0.0039  0.1090  -0.0393 259 HOH   B O   
6914 O O   . HOH   E .   ? 0.2616 0.3453 0.2320 -0.0434 0.0300  0.0560  260 HOH   B O   
6915 O O   . HOH   E .   ? 0.2732 0.4111 0.3752 -0.0666 0.0749  -0.1636 261 HOH   B O   
6916 O O   . HOH   E .   ? 0.2420 0.2357 0.2250 0.0106  0.0081  -0.0090 262 HOH   B O   
6917 O O   . HOH   E .   ? 0.2286 0.2144 0.4343 -0.0102 -0.0457 -0.0386 263 HOH   B O   
6918 O O   . HOH   E .   ? 0.2137 0.1730 0.2465 -0.0238 -0.0160 0.0054  264 HOH   B O   
6919 O O   . HOH   E .   ? 0.2288 0.4659 0.5242 -0.0465 -0.0172 -0.1752 265 HOH   B O   
6920 O O   . HOH   E .   ? 0.2902 0.4799 0.3890 -0.1090 -0.0199 -0.0903 266 HOH   B O   
6921 O O   . HOH   E .   ? 0.2007 0.1914 0.1847 -0.0460 -0.0444 0.0138  267 HOH   B O   
6922 O O   . HOH   E .   ? 0.2490 0.2291 0.2842 0.0776  -0.0784 -0.0634 268 HOH   B O   
6923 O O   . HOH   E .   ? 0.2940 0.4416 0.5909 0.0383  0.0513  -0.1045 269 HOH   B O   
6924 O O   . HOH   E .   ? 0.4613 0.4885 0.5177 -0.0033 -0.1067 -0.0237 270 HOH   B O   
6925 O O   . HOH   E .   ? 0.2732 0.3067 0.2714 -0.0384 -0.0907 0.0058  271 HOH   B O   
6926 O O   . HOH   E .   ? 0.2804 0.2679 0.2653 -0.0605 -0.0675 -0.0320 272 HOH   B O   
6927 O O   . HOH   E .   ? 0.2686 0.3016 0.2483 0.0962  -0.0114 0.0148  273 HOH   B O   
6928 O O   . HOH   E .   ? 0.3244 0.5413 0.3839 -0.0631 -0.1034 0.1457  274 HOH   B O   
6929 O O   . HOH   E .   ? 0.1884 0.1629 0.5043 -0.0116 -0.0184 -0.0230 275 HOH   B O   
6930 O O   . HOH   E .   ? 0.2727 0.2136 0.2989 -0.0612 0.0181  -0.0070 276 HOH   B O   
6931 O O   . HOH   E .   ? 0.1788 0.1700 0.1994 -0.0027 0.0075  0.0010  277 HOH   B O   
6932 O O   . HOH   E .   ? 0.2737 0.2710 0.2945 0.0163  -0.0625 0.0342  278 HOH   B O   
6933 O O   . HOH   E .   ? 0.2953 0.2444 0.4843 0.0213  0.0441  0.0393  279 HOH   B O   
6934 O O   . HOH   E .   ? 0.2572 0.4144 0.4011 0.0128  0.0992  0.0039  280 HOH   B O   
6935 O O   . HOH   E .   ? 0.3851 0.2523 0.4488 -0.0992 -0.2077 0.1063  281 HOH   B O   
6936 O O   . HOH   E .   ? 0.2999 0.5753 0.7907 0.1032  -0.0745 -0.1220 282 HOH   B O   
6937 O O   . HOH   E .   ? 0.5238 0.6180 0.2842 -0.0605 -0.0821 0.1152  283 HOH   B O   
6938 O O   . HOH   E .   ? 0.3557 0.3652 0.4727 0.1119  -0.0695 -0.0989 284 HOH   B O   
6939 O O   . HOH   E .   ? 0.1904 0.1755 0.3425 -0.0201 0.0099  -0.0018 285 HOH   B O   
6940 O O   . HOH   E .   ? 0.3163 0.3179 0.5211 -0.0527 0.0140  -0.0864 286 HOH   B O   
6941 O O   . HOH   E .   ? 0.1802 0.2141 0.1774 -0.0171 -0.0167 0.0012  287 HOH   B O   
6942 O O   . HOH   E .   ? 0.3693 0.7436 0.3125 0.0964  -0.0767 0.0446  288 HOH   B O   
6943 O O   . HOH   E .   ? 0.3306 0.4821 0.5260 -0.0990 -0.1182 0.1142  289 HOH   B O   
6944 O O   . HOH   E .   ? 0.5006 0.3635 0.5090 -0.0873 0.0087  0.1449  290 HOH   B O   
6945 O O   . HOH   E .   ? 0.1869 0.3398 0.5109 0.0243  -0.0069 -0.1595 291 HOH   B O   
6946 O O   . HOH   E .   ? 0.1906 0.2168 0.3050 0.0206  -0.0161 -0.0063 292 HOH   B O   
6947 O O   . HOH   E .   ? 0.3447 0.2988 0.4869 -0.0231 -0.0571 0.1037  293 HOH   B O   
6948 O O   . HOH   E .   ? 0.3279 0.3231 0.2923 -0.0124 0.0133  -0.1388 294 HOH   B O   
6949 O O   . HOH   E .   ? 0.2511 0.3913 0.4504 -0.0310 -0.1131 0.0983  295 HOH   B O   
6950 O O   . HOH   E .   ? 0.6166 0.4496 0.3660 0.2968  0.1389  0.0906  296 HOH   B O   
6951 O O   . HOH   E .   ? 0.3276 0.3393 0.4420 -0.1108 0.1306  -0.0492 297 HOH   B O   
6952 O O   . HOH   E .   ? 0.2035 0.1763 0.2549 0.0130  0.0194  0.0149  298 HOH   B O   
6953 O O   . HOH   E .   ? 0.2346 0.2871 0.5942 0.0461  -0.0490 -0.1036 299 HOH   B O   
6954 O O   . HOH   E .   ? 0.4247 0.4527 0.3210 0.0914  0.0073  -0.1270 300 HOH   B O   
6955 O O   . HOH   E .   ? 0.3563 0.3098 0.2409 0.0330  -0.0706 -0.0174 301 HOH   B O   
6956 O O   . HOH   E .   ? 0.2341 0.1809 0.2737 -0.0316 -0.0317 -0.0016 302 HOH   B O   
6957 O O   . HOH   E .   ? 0.2815 0.7076 0.2933 0.1027  -0.0410 -0.0590 303 HOH   B O   
6958 O O   . HOH   E .   ? 0.3527 0.2116 0.3795 0.0783  0.1270  0.0808  304 HOH   B O   
6959 O O   . HOH   E .   ? 0.6316 0.5573 0.5576 -0.1010 -0.0312 0.1082  305 HOH   B O   
6960 O O   . HOH   E .   ? 0.4592 0.3981 0.2955 0.1335  -0.0929 0.0397  306 HOH   B O   
6961 O O   . HOH   E .   ? 0.2179 0.1865 0.3584 0.0362  -0.1068 -0.0093 307 HOH   B O   
6962 O O   . HOH   E .   ? 0.4502 0.4833 0.2385 -0.0031 0.0707  0.0503  308 HOH   B O   
6963 O O   . HOH   E .   ? 0.1758 0.2047 0.3038 -0.0292 -0.0099 0.0110  309 HOH   B O   
6964 O O   . HOH   E .   ? 0.2914 0.3094 0.3733 -0.0367 0.1086  -0.0860 310 HOH   B O   
6965 O O   . HOH   E .   ? 0.2528 0.1686 0.2792 -0.0159 -0.0151 0.0259  311 HOH   B O   
6966 O O   . HOH   E .   ? 0.5394 0.3049 0.2815 -0.1924 0.0832  -0.0309 312 HOH   B O   
6967 O O   . HOH   E .   ? 0.1717 0.1777 0.3369 0.0068  0.0021  -0.0009 313 HOH   B O   
6968 O O   . HOH   E .   ? 0.5328 0.2556 0.3660 0.0391  0.0565  0.0931  314 HOH   B O   
6969 O O   . HOH   E .   ? 0.3710 0.3819 0.7959 -0.0119 -0.0912 0.1793  315 HOH   B O   
6970 O O   . HOH   E .   ? 0.2294 0.2081 0.2064 -0.0057 0.0198  0.0114  316 HOH   B O   
6971 O O   . HOH   E .   ? 0.5006 0.3997 0.2705 0.1248  -0.0347 -0.0167 317 HOH   B O   
6972 O O   . HOH   E .   ? 0.3015 0.2336 0.2649 0.0238  -0.0159 0.0307  318 HOH   B O   
6973 O O   . HOH   E .   ? 0.4843 0.4757 0.2843 0.0347  -0.0344 -0.0748 319 HOH   B O   
6974 O O   . HOH   E .   ? 0.2478 0.3330 0.4663 -0.0172 -0.0238 -0.0084 320 HOH   B O   
6975 O O   . HOH   E .   ? 0.1872 0.2974 0.2684 -0.0117 -0.0236 0.0690  321 HOH   B O   
6976 O O   . HOH   E .   ? 0.1838 0.1747 0.3060 -0.0141 -0.0074 -0.0176 322 HOH   B O   
6977 O O   . HOH   E .   ? 0.7171 0.4735 0.5741 0.1451  0.1082  0.0546  323 HOH   B O   
6978 O O   . HOH   E .   ? 0.4798 0.3523 0.5661 0.1490  0.2411  0.1944  324 HOH   B O   
6979 O O   . HOH   E .   ? 0.4516 0.2745 0.3149 0.1793  0.1101  0.0334  325 HOH   B O   
6980 O O   . HOH   E .   ? 0.4758 0.4347 0.6468 0.0606  -0.0469 0.1008  326 HOH   B O   
6981 O O   . HOH   E .   ? 0.6464 0.5256 0.5360 0.2250  0.0368  0.0413  327 HOH   B O   
6982 O O   . HOH   E .   ? 0.2209 0.2148 0.3118 0.0388  0.0431  0.0275  328 HOH   B O   
6983 O O   . HOH   E .   ? 0.5958 0.5192 0.6102 0.0973  -0.0989 0.2226  329 HOH   B O   
6984 O O   . HOH   E .   ? 0.2762 0.2194 0.5255 0.0053  -0.0060 0.0382  330 HOH   B O   
6985 O O   . HOH   E .   ? 0.7358 0.3536 0.3831 -0.0095 0.1534  0.1074  331 HOH   B O   
6986 O O   . HOH   E .   ? 0.8399 0.2243 0.3290 0.0048  -0.0749 0.0097  332 HOH   B O   
6987 O O   . HOH   E .   ? 0.2183 0.5805 0.6097 -0.0446 -0.0191 0.0529  333 HOH   B O   
6988 O O   . HOH   E .   ? 0.1974 0.2966 0.3473 0.0480  -0.0109 -0.0653 334 HOH   B O   
6989 O O   . HOH   E .   ? 0.4124 0.6374 0.4109 -0.0699 -0.0959 -0.0468 335 HOH   B O   
6990 O O   . HOH   E .   ? 0.1875 0.1680 0.2535 0.0053  -0.0292 0.0099  336 HOH   B O   
6991 O O   . HOH   E .   ? 0.5801 0.4634 0.6116 -0.0674 -0.0592 -0.1056 337 HOH   B O   
6992 O O   . HOH   E .   ? 0.5259 0.5608 0.3589 0.0169  -0.1026 0.0482  338 HOH   B O   
6993 O O   . HOH   E .   ? 0.2422 0.2483 0.6027 -0.0538 0.0270  0.1305  339 HOH   B O   
6994 O O   . HOH   E .   ? 0.5490 0.3798 0.3999 0.0181  0.0648  -0.1505 340 HOH   B O   
6995 O O   . HOH   E .   ? 0.5273 0.3393 0.3303 0.0395  -0.1233 -0.0698 341 HOH   B O   
6996 O O   . HOH   E .   ? 0.6417 0.6921 0.3279 -0.0405 -0.0477 0.1331  342 HOH   B O   
6997 O O   . HOH   E .   ? 0.2992 0.5741 0.6477 -0.0477 -0.0996 0.0321  343 HOH   B O   
6998 O O   . HOH   E .   ? 0.5120 0.6579 0.3299 -0.0070 0.0047  0.1518  344 HOH   B O   
6999 O O   . HOH   E .   ? 0.4378 0.5597 0.5541 0.0281  -0.0991 -0.0212 345 HOH   B O   
7000 O O   . HOH   E .   ? 0.2400 0.2095 0.3290 -0.0141 0.0722  -0.0045 346 HOH   B O   
7001 O O   . HOH   E .   ? 0.3049 0.2382 0.5054 -0.0291 -0.0903 -0.0525 347 HOH   B O   
7002 O O   . HOH   E .   ? 0.5959 0.4937 0.5334 -0.1283 0.0679  0.0663  348 HOH   B O   
7003 O O   . HOH   E .   ? 0.2501 0.4097 0.5641 -0.0024 0.0273  0.0560  349 HOH   B O   
7004 O O   . HOH   E .   ? 0.2314 0.6372 0.3729 0.1402  -0.0408 -0.1551 350 HOH   B O   
7005 O O   . HOH   E .   ? 0.3620 0.2417 0.3536 -0.0422 -0.0241 -0.0649 351 HOH   B O   
7006 O O   . HOH   E .   ? 0.4821 0.2575 0.6179 -0.0720 0.1495  0.0394  352 HOH   B O   
7007 O O   . HOH   E .   ? 0.3123 0.2119 0.4339 0.0569  -0.1305 -0.0545 353 HOH   B O   
7008 O O   . HOH   E .   ? 0.5062 0.6258 0.6009 0.0638  0.0220  -0.0441 354 HOH   B O   
7009 O O   . HOH   E .   ? 0.3844 0.3090 0.4562 -0.0891 -0.0235 -0.0685 355 HOH   B O   
7010 O O   . HOH   E .   ? 0.5584 0.3983 0.4656 0.0739  0.1326  -0.0500 356 HOH   B O   
7011 O O   . HOH   E .   ? 0.3775 0.5047 0.5175 -0.1898 -0.0215 0.0424  357 HOH   B O   
7012 O O   . HOH   E .   ? 0.5245 0.5455 0.5351 0.2077  -0.1195 0.1302  358 HOH   B O   
7013 O O   . HOH   E .   ? 0.5169 0.3478 0.4676 0.0208  -0.1724 -0.0081 359 HOH   B O   
7014 O O   . HOH   E .   ? 0.4743 0.5447 0.5132 -0.0510 -0.0758 0.0310  360 HOH   B O   
7015 O O   . HOH   E .   ? 0.5680 0.3940 0.6190 0.0072  0.0373  0.0824  361 HOH   B O   
7016 O O   . HOH   E .   ? 0.4387 0.6717 0.3249 0.2379  -0.0143 0.0356  362 HOH   B O   
7017 O O   . HOH   E .   ? 0.2397 0.3715 0.6888 -0.0721 -0.0730 -0.0435 363 HOH   B O   
7018 O O   . HOH   E .   ? 0.4936 0.3478 0.5927 -0.1362 -0.0688 0.0373  364 HOH   B O   
7019 O O   . HOH   E .   ? 0.6344 0.4690 0.4801 0.0953  0.0972  0.0678  365 HOH   B O   
7020 O O   . HOH   E .   ? 0.6796 0.2546 0.4277 0.0051  0.0235  0.0913  366 HOH   B O   
7021 O O   . HOH   E .   ? 0.5467 0.3598 0.5631 0.0915  -0.1421 0.0351  367 HOH   B O   
7022 O O   . HOH   E .   ? 0.7393 0.4379 0.3430 -0.1351 -0.1199 -0.0951 368 HOH   B O   
7023 O O   . HOH   E .   ? 0.4690 0.5597 0.6048 0.2261  0.1142  0.0928  369 HOH   B O   
7024 O O   . HOH   E .   ? 0.7866 0.8868 0.6147 0.2672  -0.1415 0.1529  370 HOH   B O   
7025 O O   . HOH   E .   ? 0.5290 0.5622 0.4426 -0.0559 -0.0758 -0.1147 371 HOH   B O   
7026 O O   . HOH   E .   ? 0.5736 0.6057 0.3593 0.1329  -0.1573 0.0454  372 HOH   B O   
7027 O O   . HOH   E .   ? 0.6883 0.3709 0.5046 -0.0658 0.0209  -0.0037 373 HOH   B O   
7028 O O   . HOH   E .   ? 0.3387 0.4229 0.2719 0.0863  0.0187  0.0192  374 HOH   B O   
7029 O O   . HOH   E .   ? 0.3998 0.3921 0.4233 0.0499  -0.1447 -0.0245 375 HOH   B O   
7030 O O   . HOH   E .   ? 0.4735 0.4958 0.4786 -0.0750 -0.0632 0.0160  376 HOH   B O   
7031 O O   . HOH   E .   ? 0.2536 0.4278 0.5175 0.0393  -0.0955 -0.0405 377 HOH   B O   
7032 O O   . HOH   E .   ? 0.5308 0.7948 0.6159 0.1479  0.0374  0.3194  378 HOH   B O   
7033 O O   . HOH   E .   ? 0.3619 0.4890 0.5555 0.0897  -0.0327 0.0457  379 HOH   B O   
7034 O O   . HOH   E .   ? 0.5121 0.6844 0.4477 -0.0985 0.0445  -0.1513 380 HOH   B O   
7035 O O   . HOH   E .   ? 0.5596 0.7307 0.6325 0.0636  0.2193  0.1667  381 HOH   B O   
7036 O O   . HOH   E .   ? 0.3106 0.2604 0.3541 0.0062  0.0298  0.0184  382 HOH   B O   
7037 O O   . HOH   E .   ? 0.3980 0.8132 0.6062 0.1441  0.1642  0.0896  383 HOH   B O   
7038 O O   . HOH   E .   ? 0.6120 0.4280 0.5841 -0.0231 0.0708  0.0255  384 HOH   B O   
7039 O O   . HOH   E .   ? 0.6144 0.3870 0.5336 0.0926  0.1310  -0.0736 385 HOH   B O   
7040 O O   . HOH   E .   ? 0.7785 0.6737 0.4845 0.2071  -0.0079 0.0908  386 HOH   B O   
7041 O O   . HOH   E .   ? 0.5312 0.5194 0.4519 -0.0711 -0.0656 -0.0452 387 HOH   B O   
7042 O O   . HOH   E .   ? 0.2500 0.4948 0.3780 -0.0861 -0.0683 -0.0383 388 HOH   B O   
7043 O O   . HOH   E .   ? 0.4818 0.3844 0.3403 -0.0306 0.0511  -0.0286 389 HOH   B O   
7044 O O   . HOH   E .   ? 0.4402 0.2494 0.3504 0.1023  -0.0228 0.0241  390 HOH   B O   
7045 O O   . HOH   E .   ? 0.4961 0.4631 0.4339 -0.0334 0.0557  0.0471  391 HOH   B O   
7046 O O   . HOH   E .   ? 0.5034 0.2506 0.4928 -0.0822 0.0580  0.0358  392 HOH   B O   
7047 O O   . HOH   E .   ? 0.2574 0.5528 0.6554 -0.1305 -0.0801 -0.0093 393 HOH   B O   
7048 O O   . HOH   E .   ? 0.3453 0.3893 0.3654 0.0555  0.0127  -0.0690 394 HOH   B O   
7049 O O   . HOH   E .   ? 0.5227 0.5963 0.3912 0.1610  -0.0197 -0.0821 395 HOH   B O   
7050 O O   . HOH   E .   ? 0.4117 0.4154 0.4593 -0.0133 0.0749  0.1024  396 HOH   B O   
7051 O O   . HOH   E .   ? 0.2278 0.3510 0.5896 -0.0575 -0.0511 -0.0047 397 HOH   B O   
7052 O O   . HOH   E .   ? 0.6083 0.6385 0.7500 0.1588  -0.0918 0.2047  398 HOH   B O   
7053 O O   . HOH   E .   ? 0.5857 0.4600 0.3349 -0.2131 -0.0259 0.1348  399 HOH   B O   
7054 O O   . HOH   E .   ? 0.6322 0.5858 0.4098 0.1690  0.0033  0.0144  400 HOH   B O   
# 
